HUMAN PROTEINS HAVING SECRETORY SIGNAL SEQUENCES AND DNAs ENCODING THESE PROTEINS

Abstract: [Problems to be solved] To provide human proteins having secretory signal sequences and cDNAs encoding said proteins. [Means to solve the problems] Proteins containing any of the amino acid sequences represented by Sequence No. 1 to Sequence No. 9 and DNAs encoding said proteins exemplified by cDNAs containing any of the base sequences represented by Sequence No. 10 to Sequence No. 18. Said proteins can be provided by expressing cDNAs encoding human proteins having secretory signal sequences with verified secretory functions and recombinants of these human cDNAs.

Description: DESCRIPTION Human Proteins Having Secretory Signal Sequences and DNAs Encoding These Proteins TECHNICAL FIELD The present invention relates to human proteins having secretory signal sequences and DNAs encoding these proteins . The proteins of the present invention can be used as pharmaceuticals or as antigens for preparing antibodies against said proteins . The cDNAs of the present invention can be used as probes for the gene diagnosis and gene sources for the gene therapy. Furthermore, the cDNAs can be used as gene sources for large-scale production of the proteins encoded by said cDNAs . BACKGROUND ART Cells secrete many proteins outside the cells. These secretory proteins play important roles for the proliferation control, the differentiation induction, the material transportation, the biological protection, etc. in the cells. Different from intracellular proteins, the secretory proteins exert their actions outside the cells, whereby they can be administered in the intracorporeal manner such as the injection or the drip to anticipate the potentialities as medicines. In fact, a number of human secretory proteins such as interleukins , interferons, erythropoietin, thrombolytic agents, etc. have been currently utilized as medicines. In addition, secretory proteins other than those described above have been undergoing clinical trials to develop as pharmaceuticals. Since it has been conceived that the human cells still produce many unknown secretory proteins, availability of these secretory proteins as well as genes encoding them is expected to lead to the development of novel pharmaceuticals using these proteins. Heretofore, such a secretory protein has been obtained by a method comprising the isolation and purification of the target protein from a large amount of the blood or a cell culture supernatant by using the biological activity as an indicator, determination of its primary structure followed by cloning of the corresponding cDNA on the basis of the information on the thus-obtained amino acid sequence, and production of the reco binant protein using said cDNA. However, the contents of the secretory proteins are generally so low that the isolation and purification are difficult in many cases. On the other hand, secretory proteins and type-I membrane proteins possess hydrophobic sequences, defined as the secretory signal sequences, consisting of about 20 amino acid residues at the amino acid termini (the N-termini). Therefore, the cloning of genes encoding the secretory proteins or type-I membrane proteins is expected to be performed by using the presence or the absence of these secretory signal sequences as indicators. DISCLOSURE OF INVENTION The object of the present invention is to provide novel human proteins having secretory signal sequences and DNAs encoding said proteins . As the result of intensive studies, the present inventors were successful in cloning of cDNAs having secretory signal sequences from a human full-length cDNA bank, thereby completing the present invention. That is to say, the present invention provides proteins containing any of the amino acid sequences represented by Sequence No. 1 to Sequence No. 9 that are human proteins having secretory signal sequences. The present invention, also, provides DNAs encoding said proteins exemplified as cDNAs containing any of the base sequences represented by Sequence No. 10 to sequence No. 18. 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 preparation of the peptide by the chemical synthesis on the basis of the amino acid sequence of the present invention, or a method for production with the recombinant DNA technology using the DNA encoding the human secretory protein of the present invention, wherein the method for obtainment by the recombinant DNA technology is employed preferably. For example, an in vitro expression can be achieved by preparation of an RNA by the in vitro transcription from a vector having a cDNA of the present invention, followed by the in vitro translation using this RNA as a template. Also, the recombination of the translation domain to a suitable expression vector by the method known in the art leads to the expression of a large amount of the encoded protein by using Escherichia coll , Bacillus subtilis, yeasts, animal cells, and so on. In the case in which a protein of the present invention is expressed by a microorganism such as Escherichia coli , the translation region of a cDNA of the present invention is constructed in an expression vector having an origin, a promoter, ribosome-binding site(s), cDNA-cloning site(s), a terminator, etc. that can be replicated in the microorganism and, after transformation of the host cells with said expression vector, the thus-obtained transformant is incubated, whereby the protein encoded by said cDNA can be produced on a large scale in the microorganism. In that case, a maturation protein can be obtained by performing the expression with inserting an initiation codon in the translation region where the secretary signal sequence is removed. Alternatively, a fusion protein with another protein can be expressed. Only a protein portion encoding said cDNA can be obtained by cleavage of said fusion protein with an appropriate protease. In the case in which a protein of the present invention is secretory-expressed in animal cells, the protein of the present invention can be secretory-produced as a maturation protein outside the cells, when the translation region of said cDNA is subjected to recombination to an expression vector for animal cells that has a promoter for the animal cells, a splicing domain, a poly(A) addition site, etc., followed by transfection into the animal cells. The proteins of the present invention include peptide fragments (more than 5 amino acid residues) containing any partial amino acid sequence of the amino acid sequences represented by Sequence No. 1 to Sequence No. 9. These fragments can be used as antigens for preparation of the antibodies. Also, the proteins of the present invention are secreted in the form of maturation proteins outside the cells, after the signal sequences are removed. Therefore, these maturation proteins shall come within the scope of the present invention. The N-terminal amino acid sequences of the maturation proteins can be easily identified by using the method for the cleavage-site determination in a signal sequence [Japanese Patent Kokai Publication No. 1996-187100]. Furthermore, many secretory proteins are subjected to the processing after the secretion to be converted to the active forms . These activated proteins or peptides shall come within the scope of the present invention. When glycosylation sites are present in the amino acid sequences, expression in appropriate animal cells affords glycosylated proteins. Therefore, these glycosylated proteins or peptides also shall come within the scope of the present invention. The DNAs of the present invention include all DNAs encoding the above-mentioned proteins . Said DNAs can be obtained using the method by chemical synthesis, the method by cDNA cloning, and so on. 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 as a template a poly(A) RNA extracted from human cells. The human cells may be cells delivered from the human body, for example, by the operation or may be the culture cells. The cDNA can be synthesized by 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 so on, but it is preferred to use the capping method [Kato, S. et al . , Gene 150: 243-250 (1994)] as illustrated in Examples in order to obtain a full- length clone in an effective manner. The primary selection of a cDNA encoding a human protein having a secretory signal sequence is performed by the sequencing of a partial base sequence of the cDNA clone selected at random from the cDNA library, sequencing of the amino acid sequence encoded by the base sequence, and recognition of the presence or absence of hydrophobic site(s) in the resulting N-terminal amino acid sequence region. Next, the secondary selection is carried out by determination of the whole base sequence by the sequencing and the protein expression by the in vitro translation. The ascertainment of the cDNA of the present invention for encoding the protein having the secretory signal sequence is performed by using the signal sequence detection method fYokoya a-Kobayashi , M. et al., Gene 163: 193-196 (1995)]. In other words, the ascertainment 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 protease domain of urokinase and then expressing the resulting cDNA in COS7 cells to detect the urokinase activity in the cell culture medium. The cDNAs of the present invention are characterized by containing any of the base sequences represented by Sequence No. 10 to Sequence No. 18 or any of the base sequences represented by Sequence No. 19 to Sequence No. 27. Table 1 summarizes the clone number (HP number), the cells affording the cDNA, the total base number of the cDNA, and the number of the amino acid residues of the encoded protein, for each of the cDNAs . Table 1 Hereupon, the same clone as any of the cDNAs of the present invention can be easily obtained by screening of the cDNA library constructed from the cell line or the human tissue employed in the present invention, by the use of an oligonucleotide probe synthesized on the basis of the corresponding cDNA base sequence depicted in Sequence No. 19 to Sequence No. 27. In general, the polymorphism due to the individual difference is frequently observed in human genes. Therefore, any cDNA that is subjected to insertion or deletion of one or plural nucleotides and/or substitution with other nucleotides in Sequence No. 10 to Sequence No. 27 shall come within the scope of the present invention. In a similar manner, any protein that is produced by these modifications comprising insertion or deletion of one or plural nucleotides and/or substitution with other nucleotides shall come within the scope of the present invention, as far as said protein possesses the activity of the corresponding protein having the amino acid sequence represented by Sequence No. 1 to Sequence No. 9. The cDNAs of the present invention include cDNA fragments (more than 10 bp) containing any partial base sequence of the base sequence represented by Sequence No. 10 to No. 18 or of the base sequence represented by Sequence No. 19 to No. 27. For example, as illustrated in Examples, the portion encoding the secretory signal sequence can be employed as means to secrete an optionally selected protein outside the cells by fusing with a cDNA encoding another protein. Also, DNA fragments consisting of a sense chain and an anti-sense chain shall come within this scope. These DNA fragments can be used as the probes for the gene diagnosis. BRIEF DESCRIPTION OF DRAWINGS Figure 1: A figure depicting the structure of the secretory signal sequence detection vector pSSD3. Figure 2: A figure depicting the construction of the secretory signal sequence - the urokinase fusion gene. Figure 3: A figure depicting the hydrophobicity/hydrophilicity profile of the protein encoded by clone HP00685. Figure 4: A figure depicting the hydrophobicity/hydrophilicity profile of the protein encoded by clone HP00714. Figure 5: A figure depicting the hydrophobicity/hydrophilicity profile of the protein encoded by clone HP00876. Figure 6: A figure depicting the hydrophobicity/hydrophilicity profile of the protein encoded by clone HP01134. Figure 7: A figure depicting the hydrophobicity/hydrophilicity profile of the protein encoded by clone HP10029. Figure 8: A figure depicting the hydrophobicity/hydrophilicity profile of the protein encoded by clone HP10189. Figure 9: A figure depicting the hydrophobicity/hydrophilicity profile of the protein encoded by clone HP10269. Figure 10: A figure depicting the hydrophobicity/hydrophilicity profile of the protein encoded by clone HP10298. Figure 11: A figure depicting the hydrophobicity/hydrophilicity profile of the protein encoded by clone HP10368. BEST MODE FOR CARRING OUT INVENTION EXAMPLE The present invention is embodied in more detail by the following examples, but this embodiment is not intended to restrict the present invention. The basic operations and the enzyme reactions with regard to the DNA recombination are carried out according to the literature ["Molecular Cloning. A Laboratory Manual", Cold Spring Harbor Laboratory, 1989]. Unless otherwise stated, restrictive enzymes and a variety of modification enzymes to be used were those available from Takara Shuzo Co., Ltd. The manufacturer's instructions were used for the buffer 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 fibrosarcoma cell line HT-1080 (ATCC CCL 121), the epidermoid carcinoma cell line KB (ATCC CRL 17), the histiocyte ly phoma cell line U937 (ATCC CRL 1593) stimulated by phorbol esters, tissues of stomach cancer delivered by the operation, and liver were used for human cells to extract mRNAs. Each of the cell lines was cultured by a conventional procedure . After about 1 g of human tissues was homogenized in 20 ml of a 5.5 M guanidinium thiocyanate solution, total mRNAs were prepared in accordance with 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 solution (pH 7.6), 0.5 M NaCl , and 1 mM EDTA to obtain a poly(A) RNA in accordance with the above-mentioned literature . (2) Construction of cDNA Library To a solution of 10 μg of the above-mentioned poly(A) RNA in 100 mM Tris-hydrochloric acid buffer solution (pH 8) was added one unit of an RNase-free, bacterium-origin alkaline phosphatase and the resulting solution was allowed to react at 37 °C for one hour. After the reaction solution underwent the phenol extraction followed by the ethanol precipitation, the obtained pellets 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. Thereto was added one unit of a tobacco-origin pyrophosphatase (Epicenter Technologies) and the resulting solution at a total volume of 100 μl was allowed to react at 37 °C for one hour. After the reaction solution underwent the phenol extraction followed by the ethanol precipitation, the thus-obtained pellets were dissolved in water to obtain a decapped poly(A) RNA solution. To a solution of the decapped poly(A) RNA and 3 nmol of a DNA-RNA chimeric oligonucleotide ( 5 ' -dG-dG-dG-dG-dA-dA-dT- dT-dC-dG-dA-G-G-A-3' ) in a mixed aqueous solution of 50 mM Tris-hydrochloric acid buffer solution (pH 7.5), 0.5 mM ATP, 5 mM MgCl , 10 mM 2-mercaptoethanol, and 25% polyethylene glycol were added 50 units of T4 RNA ligase and the resulting solution at a total volume of 30 μl was allowed to react at 20°C for 12 hours. After the reaction solution underwent the phenol extraction followed by the ethanol precipitation, the thus-obtained pellets were dissolved in water to obtain a chimeric oligo-capped poly(A) RNA. After the vector pKAl developed by the present inventors (Japanese Patent Kokai Publication No. 1992-117292) was digested with Kpnl, an about 60-dT tail was inserted by a terminal transferase. This product was digested with EcoRV to remove the dT tail at one side and the resulting molecule was used as a vectorial primer. After 6 μg of the previously-prepared chimeric oligo- capped poly(A) RNA was annealed with 1.2 μg of the vectorial primer, the product was dissolved in a mixed solution of 50 mM Tris-hydrochloric acid buffer solution (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 at a total volume of 20 μl was allowed to react at 42°C for one hour. After the reaction solution underwent the phenol extraction followed by the ethanol precipitation, the thus- obtained pellets were dissolved in a mixed solution of 50 mM Tris-hydrochloric acid buffer solution (pH 7.5), 100 mM NaCl, 10 mM MgCl 2 , and 1 mM dithiothreitol. Thereto were added 100 units of EcoRI and the resulting solution at a total volume of 20 μl was allowed to react at 37 °C for one hour. After the reaction solution underwent the phenol extraction followed by the ethanol precipitation, the obtained pellets were dissolved in a mixed solution of 20 mM Tris-hydrochloric acid buffer solution (pH 7.5), 100 mM KCl, 4 mM MgCl 2 , 10 mM (NH^) 2 S0^, and 50 μg/ l bovine serum albumin. Thereto were 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 unit of Escherichia coli DNase H and the resulting solution was allowed to react at 12°C for one hour and then at 22°C for one hour. Next, the cDNA-synthesis reaction solution was used to transform Escherichia coli DH12S (GIBCO-BRL) . The transformation was carried out by the electroporation method. A portion of the transformant was inoculated on a 2xYT agar culture medium containing 100 μg/ l ampicillin, which was incubated at 37 °C overnight. A colony grown on the culture medium was randomly picked up and inoculated on 2 ml of the 2xYT culture medium containing 100 μg/ml 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 double-digested with EcoRI and Notl, the product was subjected to 0.8% agarose gel electrophoresis to determine the size of the cDNA insert. In addition, by the use of the obtained plasmid as a template, the sequence reaction using Ml3 universal primer labeled with a fluorescent dye and Taq polymerase (a kit of Applied Biosystems Inc.) was carried out and the product was analyzed by a fluorescent DNA-sequencer (Applied Biosystems Inc.) to determine the base sequence of the cDNA 5 '-terminal of about 400 bp. The sequence data were filed as a homo-protein cDNA bank data base. ( 3 ) Selection of cDNAs Encoding Proteins Having Secretory Signal Sequence The base sequence registered in the homo-protein cDNA bank was converted to three frames of amino acid sequences and the presence or absence of an open reading frame (ORF) beginning from the initiation codon. Then, the selection was made for the presence of a signal sequence that is characteristic to a secretory protein at the N-terminal of the portion encoded by ORF . These clones were sequenced from the both 5 ' and 3 ' directions by using the deletion method to determine the whole base sequence. The hydrophobicity/hydrophilicity profiles were obtained for proteins encoded by ORF by the Kyte-Doolittle method [Kyte, J. & Doolittle, R. F., J. Mol . Bio. 157: 105-132 (1982)] to examine the presence or absence of a hydrophobic region. In the case in which there is not 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 that did not possess a secretory protein or transmembrane domain ( s ) . (4) Construction of Secretory Signal Detection Vector pSSD3 One microgram of pSSDl carrying the SV40 promoter and a cDNA encoding the protease domain of urokinase [Yokoyama- Kobayashi, M. et al . , Gene 163: 193-196 (1995)] was digested with 5 units of Bglll and 5 units of EcoRV. Then, after dephosphorylation at the 5' terminal by the CIP treatment, a DNA fragment of about 4.2 kbp was purified by cutting off from the gel of agarose gel electrophoresis. Two oligo DNA linkers, LI ( 5 ' -GATCCCGGGTCACGTGGGAT-3 ' ) and L2 (5'-ATCCCACGTGACCCGG-3' ) , were synthesized and phosphorylated by T4 polynucleotide kinase . After annealing of the both linkers, followed by ligation with the previously-prepared pSSDl fragment by T4 DNA ligase, Escherichia coli JM109 was transformed. A plasmid pSSD3 was prepared from the transformant and the objective recombinant was confirmed by the determination of the base sequence of the linker-inserted fragment. Figure 1 illustrates the structure of the thus-obtained plasmid. The present plasmid vector carries three types of blunt-end formation restriction enzyme sites, Smal, P aCI, and EcoRV. Since these cleavage sites are positioned in succession at an interval of 7 bp, selection of an appropriate site in combination of three types of frames for the inserting cDNA allows to construct a vector expressing a fusion protein. (5) Functional Verification of Secretory Signal Sequence Whether the N-terminal hydrophobic region in the secretory protein clone candidate obtained in the above- mentioned steps functions 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 cleaved at an appropriate restriction enzyme site that existed at the downstream from the portion expected for encoding the secretory signal sequence. In the case in which this restriction enzyme site was a protruding 5 '-terminus, the site was blunt-ended by the Klenow treatment. Digestion with Hindlll was further carried out and a DNA fragment containing the SV40 promoter and a cDNA encoding the secretory sequence at the downstream from the promoter was separated by agarose gel electrophoresis . This fragment was inserted between the pSSD3 Hindlll site and a restriction enzyme site selected so as to match with the urokinase-coding frame, thereby constructing a vector expressing a fusion protein of the secretory signal portion of the target cDNA and the urokinase protease domain (refer to Figure 2). After Escherichia coli (host: JM109) bearing 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 ampicillin, the helper phage M13K07 (50 μl ) was added and the incubation was continued at 37°C overnight. A supernatant separated by centrifugation underwent 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, there was used as a control a suspension of single-stranded particles prepared in the same manner from the vector pKAl-UPA containing pSSD3 and a full-length cDNA of urokinase [Yokoyama-Kobayashi, M. et al., Gene 163: 193-196 (1995)]. The simian-kidney-origin culture cells, C0S7, were incubated at 37 °C in the presence of 5% C0 2 in the Dulbecco's modified Eagle's culture medium (DMEM) containing 10% fetal calf albumin. Into a 6-well plate (Nunc Inc., 3 cm in the well diameter) were inoculated 1 x 10 COS7 cells and incubation was carried out at 37 °C for 22 hours in the presence of 5% C0 2 • After the culture medium was removed, the cell surface was washed with a phosphate buffer solution and then washed again with DMEM containing 50 mM Tris- hydrochloric acid (pH 7.5) (TDMEM) . To the cells were added 1 μl of the single-stranded phage suspension, 0.6 ml of the TM 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% C0 2 . After the sample solution was removed, the cell surface was washed with TDMEM, 2 ml per well of DMEM containing 10% fetal calf albumin was added, and the incubation was carried out at 37 °C for 2 days in the presence of 5% C0 2 • To 10 ml of 50 mM phosphate buffer solution (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 plate of 9 cm in diameter to prepare a fibrin plate. Ten icroliters of the culture supernatant of the transfected COS7 cells were spotted on the fibrin plate, which was incubated at 37 °C for 15 hours. The diameter of the thus-obtained clear circle was taken as an index for the urokinase activity. Table 2 shows the restriction enzyme site used for cutting off the cDNA fragment from each clone, the restriction enzyme site used for cleavage of pSSD3, and the presence or absence of a clear circle. Except for pSSD3 used as the control, each of the samples formed a clear circle to identify that urokinase was secreted in the culture medium. That is to say, it is indicated that each of the cDNA fragments codes for the amino acid sequence that functions as the secretory signal sequence . Table 2 followed by the Klenow treatment. (6) Protein Synthesis by In Vitro Translation The plasmid vector carrying the cDNA of the present invention was utilized for the in vitro transcription/translation by the T N T rabbit reticulocyte lysate kit (Promega Biotec). In this case, [ 35S]methionine was added and the expression product was labeled with the radioisotope. All reactions were carried out by following the protocols attached to the kit. Two micrograms of the plasmid was allowed to react at 30°C for 90 minutes in total 25 ml of a reaction solution containing 12.5 μl of the T N T rabbit reticulocyte lysate, 0.5 μl of the buffer solution (attached to the kit), 2 μl of an amino acid mixture (methionine-free) , 2 μl (0.37 MBq/μl) of [ 35S]methionine (Amersha Corporation), 0.5 μl of T7 RNA polymerase, and 20 U of RNasin. Also, the experiment in the presence of the membrane system was carried out by adding 2.5 μl of the dog pancreatic microsome fraction (Promega Biotec) into this reaction system. To 3 μl of the reaction solution was added 2 μl of an SDS sampling buffer (125 mM Tris-hydrochloric acid buffer solution, 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. Table 3 shows the molecular weight of the in vitro translation product obtained from each of the clones in the presence/absence of the membrane microsome together with the calculated value of the molecular weight of the protein encoded by ORF of the cDNA. Table 3 * - means "Not examined" . ( 7 ) Clone Examples <HP00658> (Sequence Number 1, 10, 19) Determination of the whole base sequence for the cDNA insert of clone HP00658 obtained from the human fibrosarcoma cell line HT-1080 cDNA libraries revealed the structure consisting of a 5 '-non-translation region of 55 bp, an ORF of 465 bp, and a 3 ' -non-translation region of 776 bp. The ORF codes for a protein consisting of 154 amino acid residues with a hydrophobic region of a putative secretory signal sequence at the N-terminal. Figure 3 depicts the hydrophobicity/hydrophilicity profile of the present protein obtained by the Kyte-Doolittle method. Search of the protein data base using the amino acid sequence encoded by the ORF revealed that the N-terminal 63 amino acid residues thereof were completely identical with those in the RANTES protein (EMBL Accession No. 21121) except for one amino acid residue at position 7 (arginine in RANTES and alanine in the present protein), but the sequences in both proteins were completely different after position 64. Hereupon, RANTES consisted of 91 amino acid residues, whereas the present protein consisted of longer 154 amino acid residues. The in vitro translation resulted in the formation of a translation product of 18 kDa that was almost consistent with the molecular weight of 17,037 predicted from the ORF. In this case, the addition of the microsome resulted in the formation of a 16-kDa product in which the secretory signal sequence portion was putatively removed by cleavage. This result together with the result on pSSD3 verifies that the present protein possesses the secretory signal sequence. Application of the (-3,-1) rule, a method for predicting the signal sequence cleavage site [von Heijne, G., Nucl . Acid Res. 14: 4683-4690 (1986)], allows to expect that the maturation protein starts from serine at position 24. Comparison of the base sequences for the both proteins revealed that the base sequence from position 2 to position 325 in the present cDNA was deficient in the RANTES cDNA. It is considered that this deficiency resulted in induction of a frame shift to form an ORF of a different size. Some mutations were observed in other regions , wherein the homology was 97.7% up to position 241 and was 98.0% after position 325. RANTES has been obtained as a T cell-specific protein [Schall, T. J. et al . , J. Immunol. 141: 1018-1025 (1988)], whereas the present cDNA was obtained from the fibrosarcoma cells. Accordingly, the present protein is considered to possess a different function from that of RANTES. Furthermore, the search of GenBank using the base sequence of the present cDNA revealed that any EST possessing the homology of 90% or more was not found. <HP00714> (Sequence Number 2, 11, 20) Determination of the whole base sequence for the cDNA insert of clone HP00714 obtained from the human epidermoid carcinoma cell line KB cDNA libraries revealed the structure consisting of a 5 ' -non-translation region of 56 bp, an ORF of 948 bp, and a 3 ' -non-translation region of 2310 bp. The ORF codes for a protein consisting of 315 amino acid residues with a hydrophobic region of a putative secretory signal sequence at the N-terminal . Figure 4 depicts 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 47 kDa that was somewhat larger than the molecular weight of 37,106 predicted from the ORF. Since the molecular weight of the human reticulocalbin analogous to the present protein is also larger by about 10 kDa than the molecular weight expected from the translation-product band on SDS-PAGE [Ozawa, M., J. Biochem. 117: 1113-1119 (1995)], the molecular weight difference in the present protein is considered to be arisen from its physicochemical properties. Application of the (-3,-1) rule, a method for predicting the signal sequence cleavage site, allows to expect that the maturation protein starts from lysine at position 20. There is a possibility that the present protein exists in the endoplasmic reticulum because this protein possesses the C-terminal sequence HDEF analogous to KDEL, the signal motif sequence localized in the endoplasmic reticulum. The search of the protein data base using the amino acid sequence of the present protein revealed that the protein was analogous to the human reticulocalbin (GenBank Accession No. D42073). Table 4 indicates the comparison of the amino acid sequences between the human protein of the present invention (HP) and the human reticulocalbin (RC) . - represents a gap, * 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. The both proteins possessed a homology of 60.5%. Table 4 HP " MDLRQFLMCLSLCTAPALSKPTBKKDR-VHHEPQLSDKVHNDAQSFDYDH RC MARGGRGRRLGLALGLLLALVLAPRVLRAKPTVRKBRVRPDSBLGERPPEONQSFQYDH HP DAFLGAEBAKTFDQLTPEESKERLGKIVSKIDGDDGFVTVDELKDWIKFAQKRWIYEDV RC BAFLGKEDSKTFDQLTPDBSKERLGKIVDRIDNDGDGFVTTEE TWIKRVQKRYIFDNV HP ERQWKGHDLNEDGLVSWBBYNATYGYVLDDP DPDDGFNYKQMMVRDBRRFKMADK RC AKVWKDYDRDDDKISWEBYKQATYGYYLGNPAEFHDSSDHHTFKKMLPRDERRFKAADL HP DGDLIATKEEFTAFLHPEEYDYMKDIVVαETMEDIDKNADGFIDLEEYIGDMYSHDGNTD RC NGDLTATREEFTAFLHPEBFEHMKBI VETLEDIDKNGOGFVDQDEYIADMFSHEENGP HP EPEWVKTERBQRVEFRDKNRDGKMDKEBTKDWILPSDYDHABAEARHLVYESDQNKDGK RC EPDWVLSBRBQFNEFRDLNKDGKLDKDEIRHWILPQDYDHAQABARHLVYESDKNKDEKL HP TKEBIVDKYDLFVGSQATDFGEALVR-HDEF RC TKEBILENWNMFVGSQATNYGEDLTKNHDBL Furthermore, the search of GenBank using the base sequence of the present cDNA revealed that there existed some ESTs possessing the homology of 90% or more and containing the initiation codon (for example, Accession No. F3872), but any of the sequences thereof did not allow to predict the present protein. Reticulocalbin is a protein localized on the membrane surface of the endoplasmic reticulum and has been considered to participate in the protein folding. Accordingly, the protein of the present invention is considered to be applicable to the folding process of recombinant proteins. <HP00876> (Sequence Number 3, 12, 21) Determination of the whole base sequence for the cDNA insert of clone HP0876 obtained from the human stomach cancer cDNA libraries revealed the structure consisting of a 5 '-non- translation region of 146 bp, an ORF of 477 bp, and a 3 ' -non- translation region of 529 bp. The ORF codes for a protein consisting of 158 amino acid residues with a hydrophobic region of a putative secretory signal sequence at the N- terminal. Figure 5 depicts 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 18 kDa that was almost consistent with the molecular weight of 18,230 predicted from the ORF. In this case, the addition of the microsome resulted in the formation of a 16-kDa product in which the secretory signal sequence portion was putatively removed by cleavage. This result together with the result on pSSD3 verifies that the present protein possesses the secretory signal. Application of the (-3,-1) rule, a method for predicting the signal sequence cleavage site, allows to expect that the maturation protein starts from glycine at position 18 or aspartic acid at position 23. The search of the protein data base using the amino acid sequence of the present protein revealed that the protein was analogous to several type-C lectins . As an example, Table 5 indicates the comparison of the amino acid sequences between the human protein of the present invention (HP) and the rattlesnake lectin (CL) (Swiss-PROT Accession No. P21963). - represents a gap, * 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. The both proteins possessed a homology of 35.3%. Table 5 HP MASRSMRLLLLLSCLAKTGVLGDI I RPSCAPGWFYHKSNCYGYFRKLRNWSDAELBCQS CL NNCPLDWLPMNG CYKI FNQLKTWEDAEMFCRK HP YGNGAHLASI LSLKBASTIAEYISGYQRSα-PIWI GLHDPQKRQQWαWI DGA YLYRSWS CL YKPGCHLASFHRYGBSLEIABYI SDYHKGQBNVWI GLRDK KDFSWEWTDRSCTDYLTWD HP GKSMGG— NKH-CABMSSNNNFLTWSSNBCN RQHFLCKYRP **. *. #, * . . . *. . . *. . . . ***. CL KN Q PDHY Q NKEFCVELVSLTGYRLWNDQVCESKDAFLCαCKF Furthermore, the search of GenBank using the base sequence of the present cDNA revealed that any EST possessing the homology of 90% or more was not found . After 1 μg of the plasmid pHP00876 was digested with 20 units of PvuII , the product was subjected to 1% agarose gel electrophoresis and an about 700-bp DNA fragment was cut off from the gel . Next , 1 μg of pET-21a (Novagen ) was digested with 20 units of Nhel , the product was subjected to the Klenow treatment followed by 1% agarose gel electrophoresis and an about 5.4-kbp DNA fragment was cut off from the gel . After ligation of the vector fragment and the cDNA fragment using a ligation kit , Escherichia coli BL21 ( DE3 ) ( Novagen ) was transformed . A plasmid pET876 was prepared from the transfor ant and the objective recombinant was confirmed from the restriction enzyme cleavage map . The present expression vector expresses a protein in which methionine-alanine was inserted before a protein starting from serine at position 29 in the protein encoded by the clone HP00876. A suspension of pET876/BL21 (DE3) in 5 ml of the LB culture medium containing 100 μg/ml ampicillin was incubated in a shaker at 37 °C and isopropylthiogalactoside was added to make 1 mM when A 600 reached to about 0.5. After the incubation was continued at 37 °C for 6 hours, cells were collected by centrifugation and suspended in 25 ml of a column buffer solution for the amylose column (10 mM Tris- hydrochloric acid, pH 7.4, 200 mM NaCl, and 1 mM EDTA). The resulting suspension was sonicated and then the insoluble fraction was subjected to SDS-polyacrylamide electrophoresis to identify a band originating from the expression of the present vector at a position of about 14 kDa. Since lectins recognize and then bind to sugar chains, lectins are useful as sugar-chain detection reagents and as affinity carriers for purification of glycoproteins . In addition, extracellular secretory lectins play important roles also in intercellular signal transduction and thereby are useful as medicines. <HP01134> (Sequence Number 4, 13, 22) Determination of the whole base sequence for the cDNA insert of clone HP01134 obtained from the human liver cDNA libraries revealed the structure consisting of a 5 ' -non- translation region of 116 bp, an ORF of 1131 bp, and a 3'- non-translation region of 502 bp. The ORF codes for a protein consisting of 376 amino acid residues with a hydrophobic region of a putative secretory signal sequence at the N- terminal. Figure 6 depicts 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 42 kDa that was almost consistent with the molecular weight of 42,947 predicted from the ORF. In this case, the addition of the microsome resulted in the formation of a 49-kDa product in which a sugar chain was putatively added by N-glycosylation after the secretion. Hereupon, there exist in the amino acid sequence of this protein four possible N-glycosylation sites (Asn-Gly-Thr at position 91, Asn-Glu-Thr at position 167, Asn-Thr-Ser at position 263, and Asn-Lys-Thr at position 272). The above result together with the result on pSSD3 verifies that the present protein possesses the secretory signal. Application of the (-3,-1) rule, a method for predicting the signal sequence cleavage site, allows to expect that the maturation protein starts from alanine at position 17 or valine at position 18. The search of the protein data base using the amino acid sequence of the present protein revealed that the protein was analogous to several cysteine proteinases . As an example, Table 6 indicates the comparison of the amino acid sequences between the human protein of the present invention (HP) and the tangerine cysteine proteinase (CP) (GenBank Accession No. Z47793). - represents a gap, * 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. The both proteins possessed a homology of 49% among the N-terminal region of 286 amino acid residues. Table 6 HP MVWVAVFLSVALGIGAVPIDDPEDGGKH CP MTRLASGVLITLLVALAGIADGSRDIAGDILKLPSEAYRFFHNGGGGAKVNDDDDSVGTR HP WVIVAGSNGWYNYRHQADACHAYαilHRNGIPDEQIVVMMYDDIAYSEDNPTPGIVINR ^ ^^ Φ Φ^r> π* ^N *p^* ^S^S CP WAVLLAGSNGFWNYRH ADICHAYαLLRKGGL DENI I VF YDDIAFNEENPRPGVI I NH HP PNGTDVYQGVPKDYTGEDVTPQNFLAVLRGDAEAVKGI GSGKVLKS ' GP Q DHVFI YFTDHG CP PHGDDVYKGVPKDYTGEDVTVEKFFAVVLGNKTALTG-GSGKVVDSGPNDHIFIFYSDHG HP STGILVFPNED-LHVDLNETIHYMYKHKYRKMVFYIEACESGSMMN-HLPDNINVYAT CP GPGVLGPTSRYIYADELIDVLKKKHASGNYKSLVFYLEACESGSIFEGLLLEGLNIYAT HP TAANPRESSYACY —-DEKRST —LGDWYSVNWMEDSDVEDLTKETLHKQYHLVKS ^N^ ^s ^^'^π * ^ * Φ ^S ^^ ^ ^^ ^^ <^^^^ CP TASNAEESSWGTYCPGEIPGPPPEYSTCLGDLYSIAWMEDSDI HNLRTBTLHQQYBLVKT HP HT NTSHVMQYGN TISTMKVMQFQGM RKASSPVPLPPVTHLDLTPSPDVPLTI CP RTASYNSYGSHVMQYGDIGLSKNNLFTYLGTNPANDNYTFVDENSLRPASKAVNQRDADL Furthermore , the search of GenBank using the base sequence of the present cDNA revealed that there existed some ESTs possessing the homology of 90% or more ( for example , Accession No . F01300 ) , but they were shorter than the present cDNA and any molecule containing the initiation codon was not identified . Extracellular secretory proteases possess a variety of physiological functions and thereby are useful as medicines. In addition, the proteases have been utilized as research reagents for the structure analysis of proteins by restricted degradation and so on. <HP10029> (Sequence Number 5, 14, 23) Determination of the whole base sequence for the cDNA insert of clone HP10029 obtained from the human epidermoid carcinoma cell line KB cDNA libraries revealed the structure consisting of a 5' -non-translation region of 8 bp, an ORF of 522 bp, and a 3 ' -non-translation region of 458 bp. The ORF codes for a protein consisting of 173 amino acid residues with a hydrophobic region of a putative secretory signal sequence at the N-terminal. Figure 7 depicts 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 21 kDa that was almost consistent with the molecular weight of 18,894 predicted from the ORF. In this case, the addition of the microsome resulted in the formation of a 18-kDa product in which the secretory signal sequence portion was putatively removed by cleavage. This result together with the result on pSSD3 verifies that the present protein possesses the secretory signal sequence. Application of the (-3,-1) rule, a method for predicting the signal sequence cleavage site, allows to expect that the maturation protein starts from valine at position 32. There is a possibility that the present protein exists in the endoplasmic reticulum because this protein possesses the C- terminal sequence RTEL analogous to KDEL, the signal motif sequence localized in the endoplasmic reticulum. The search of the protein data base using the amino acid sequence of the present protein revealed that the protein was not homologous with any of known proteins. Hereupon, the search of GenBank using the base sequence revealed that there existed some ESTs possessing the homology of 90% or more (for example, Accession No. H87021), but they were shorter than the present cDNA and any molecule containing the initiation codon was not identified. <HP10189> (Sequence Number 6, 15, 24) Determination of the whole base sequence for the cDNA insert of clone HP10189 obtained from the human epidermoid carcinoma cell line KB cDNA libraries revealed the structure consisting of a 5 ' -non-translation region of 101 bp, an ORF of 222 bp, and a 3 ' -non-translation region of 67 bp . The ORF codes for a protein consisting of 73 amino acid residues with a hydrophobic region of a putative secretory signal sequence at the N-terminal. Figure 8 depicts 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 10 kDa that was almost consistent with the molecular weight of 9,113 predicted from the ORF. Application of the (-3,-1) rule, a method for predicting the signal sequence cleavage site, allows to expect that the maturation protein starts from alanine at position 27. The search of the protein data base using the amino acid sequence of the present protein revealed that the protein was not homologous with any of known proteins. Hereupon, the search of GenBank using the base sequence revealed that there existed some ESTs possessing the homology of 90% or more and containing the initiation codon (for example, Accession No. N56270), but a frame shift had occurred and the same ORF as that in the present cDNA was not identified. <HP10269> (Sequence Number 7, 16, 25) Determination of the whole base sequence for the cDNA insert of clone HP10269 obtained from the human lymphoma cell line U937 cDNA libraries revealed the structure consisting of a 5 ' -non-translation region of 753 bp, an ORF of 351 bp, and a 3 '-non-translation region of 395 bp. The ORF codes for a protein consisting of 1172 amino acid residues with a hydrophobic region of a putative secretory signal sequence at the N-terminal. Figure 9 depicts 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 130 kDa that was almost consistent with the molecular weight of 129,571 predicted from the ORF. Application of the (-3,-1) rule, a method for predicting the signal sequence cleavage site, allows to expect that the maturation protein starts from glutamine at position 18. The search of the protein data base using the amino acid sequence of the present protein revealed that the protein was analogous to the B3 chain of laminin S. Table 7 indicates the comparison of the amino acid sequences between the human protein of the present invention (HP) and the B3 chain of human laminin S (B3) (GenBank Accession No. L25541) Table 7 Amino Acid Residue Number HP B3 124 Gin Arg 269 Pro Deficient 388 Pro Ala 426 Gin Arg 427 Gly Arg 439 Arg Deficient 441 Asp Glu 603 Arg Pro 815 Gly Ala Comparison of the base sequence of the present cDNA and the base sequence described in the data base reveals that the 5 ' -terminus in the present cDNA is longer by 600 or more bp and the 81-bp 5 '-terminus in the base sequence described in the data base is not consistent at all with the base sequence of the present cDNA. Accordingly, the both proteins originate from different mRNAs. As an extracellular matrix, laminin deeply participates in the proliferation and differentiation of cells. Accordingly, laminin has been employed as an additive for the cell culture and so on. <HP10298> (Sequence Number 8, 17, 26) Determination of the whole base sequence for the cDNA insert of clone HP10298 obtained from the human stomach cancer cDNA libraries revealed the structure consisting of a 5 '-non-translation region of 137 bp, an ORF of 369 bp, and a 3 ' -non-translation region of 580 bp. The ORF codes for a protein consisting of 122 amino acid residues with a hydrophobic region of a putative secretory signal sequence at the N-terminal. Figure 10 depicts 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 16 kDa that was almost consistent with the molecular weight of 13,161 predicted from the ORF. Application of the (-3,-1) rule, a method for predicting the signal sequence cleavage site, allows to expect that the maturation protein starts from leucine at position 18. There is also a possibility that the present protein possessing the hydrophobic C-terminal sequence of about 20 amino acid residues binds to the membrane via this portion. The search of the protein data base using the amino acid sequence of the present protein revealed that the protein was not homologous with any of known proteins. Hereupon, the search of GenBank using the base sequence revealed that there existed some ESTs possessing the homology of 90% or more and containing the initiation codon (for example, Accession No. D78655), but many sequences were not distinct and the same ORF as that in the present cDNA was not identified. <HP10368> (Sequence Number 9, 18, 27) Determination of the whole base sequence for the cDNA insert of clone HP10368 obtained from the human stomach cancer cDNA libraries revealed the structure consisting of a 5 '-non-translation region of 72 bp, an ORF of 528 bp, and a 3 '-non-translation region of 266 bp. The ORF codes for a protein consisting of 175 amino acid residues with a hydrophobic region of a putative secretory signal sequence at the N-terminal. Figure 11 depicts 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 19,979 predicted from the ORF. In this case, the addition of the microsome resulted in the formation of a 19-kDa product in which the secretory signal sequence portion was putatively removed by cleavage. This result together with the result on pSSD3 verifies that the present protein possesses the secretory signal. Application of the (- 3,-1) rule, a method for predicting the signal sequence cleavage site, allows to expect that the maturation protein starts from leucine at position 19 or arginine at position 21. There is a possibility that the present protein exists in the endoplasmic reticulum because this protein possesses the C-terminal sequence KTEL analogous to KDEL, the signal motif sequence localized in the endoplasmic reticulum. The search of the protein data base using the amino acid sequence of the present protein revealed that the protein was not homologous with any of known proteins. Hereupon, the search of GenBank using the base sequence revealed that there existed some ESTs possessing the homology of 90% or more and containing the initiation codon (for example. Accession No. T86663), but many sequences were not distinct and the same ORF as that in the present cDNA was not identified. INDUSTRIAL APPLICATION The present invention provides human proteins having secretory signal sequences and cDNAs encoding said proteins. All of the proteins of the present invention are putative proteins controlling the proliferation and differentiation of the cells, because said proteins are secreted outside the cells and exist in the extracellular liquid or on the cell membrane surface. Therefore, the proteins of the present invention can be used as pharmaceuticals or as antigens for preparing antibodies against said proteins. Furthermore, said DNAs can be used for the expression of large amounts of said proteins . In addition to the activities and uses described above, the polynucleotides and proteins of the present invention may exhibit one or more of the uses or biological activities (including those associated with assays cited herein) identified below. Uses or activities described for proteins of the present invention may be provided by administration or use of such proteins or by administration or use of polynucleotides encoding such proteins (such as, for example, in gene therapies or vectors suitable for introduction of DNA) . Research Uses 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 preferentially expressed (either constitutively or at a particular stage of tissue differentiation or development or in disease states); as molecular weight markers on Southern gels; as chromosome markers or tags (when labeled) to identify chromosomes or to map related gene positions; to compare with endogenous DNA sequences in patients to identify potential genetic disorders; as probes to hybridize and thus discover novel, related DNA sequences; as a source of information to derive PCR primers for genetic fingerprinting; as a probe to "subtract-out" known sequences in the process of discovering other novel polynucleotides; for selecting and making oligomers for attachment to a "gene chip" or other support, including for examination of expression patterns; to raise anti-protein antibodiesusing DNA immunization techniques; and as an antigen to raise anti-DNA antibodies or elicit another immune response. Where the polynucleotide encodes a protein which 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 Gyuris et al . , Cell 75:791-803 (1993)) to identify polynucleotides encoding the other protein with which binding occurs or to identify inhibitors of the binding interaction. The proteins provided by the present invention can similarly be used in assay to determine biological activity, including in a panel of multiple proteins for high-throughput screening; to raise antibodies or to elicit another immune response; as a reagent (including the labeled 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 disease 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 binding occurs or to identify inhibitors of the binding interaction. Proteins involved in these binding interactions can also be used to screen for peptide or small molecule inhibitors or agonists of the binding interaction. Any or all of these research utilities are capable of being developed into reagent grade or kit format for commercialization as research products. Methods for performing the uses listed above are well known to those skilled in the art. References disclosing such methods include without limitation "Molecular Cloning: A Laboratory Manual", 2d 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. and A.R. Kimmel eds., 1987. Nutritional Uses Polynucleotides and proteins of the present invention can also be used as nutritional sources or supplements . Such uses include without limitation use as a protein or amino acid supplement, use as a carbon source, use as a nitrogen source and use as a source of carbohydrate. In such cases the protein or polynucleotide of the invention can be added to the feed of a particular organism or can be administered as a separate solid or liquid preparation, such as in the form of 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 Cell Proliferation/DifferentiationActivity A protein of the present invention may exhibit cytokine, cell proliferation (either inducing or inhibiting) or cell differentiation (either inducing or inhibiting) activity or may 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 any one of a number of routine factor dependent cell proliferation assays for cell lines including, without limitation, 32D, DA2, DA1G, T10, B9 , B9/11, BaF3, MC9/G, M+ (preB M+), 2E8, RB5 , DAI, 123, T1165, HT2, CTLL2, TF-1, Mo7e and CMK. The activity of a protein of the invention may, among other means, be measured by the following methods: Assays for T-cell or thymocyte proliferation include without limitation those described in: Current Protocols in Immunology, Ed 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; 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 cytokine production and/or proliferation of spleen cells, lymph node cells or thymocytes include, without limitation, those described in: Po lyclonal T cell stimulation, Kruisbeek, A.M. and Shevach, E.M. 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 Measurement of mouse and human Interferon γ, 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. Assays for 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, L.S. 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 . Natl. 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. Natl. 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 for T-cell clone responses to antigens (which will identify, among others, proteins that affect APC-T cell interactions as well as direct T-cell effects by measuring proliferation and cytokine production) include, without limitation, those described in: Current Protocols in Immunology, Ed 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; Chapter 6, Cytokines and their cellular receptors; Chapter 7, Immunologic studies in Humans); Weinberger et al., Proc. Natl. Acad. Sci. USA 77:6091-6095, 1980; Weinberger et al., Eur. J. Immun. 11:405-411, 1981; Takai et al . , J. Immunol. 137:3494-3500, 1986; Takai et al., J. Immunol. 140:508-512, 1988. Immune Stimulating or Suppressing Activity A protein of the present invention may also exhibit immune stimulating or immune suppressing activity, including without limitation the activities for which assays are described herein. A protein may be useful in the treatment of various immune deficiencies and disorders (including severe combined immunodeficiency (SCID)), e.g., in regulating (up or down) growth and proliferation of T and/or B lymphocytes, as well as effecting the cytolytic activity of NK cells and other cell populations. These immune deficiencies may be genetic or be caused by viral (e.g., HIV) as well as bacterial orfungal infections, or may result from autoimmune disorders. More specifically, infectious diseases causes by viral, bacterial, fungal or other infection may be treatable using a protein of the present invention, including infections by HIV, hepatitis viruses, herpesviruses , mycobacteria, Leishmania 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 a boost to the immune system generally may be desirable, i.e., in the treatment of cancer. Autoimmune disorders which may be treated using a protein of the present invention include, for example, connective tissue disease, multiple sclerosis, systemic lupus erythematosus, rheumatoid arthritis, autoimmune pulmonary inflammation, Guillain-Barre syndrome, autoimmune thyroiditis, insulin dependent diabetes mellitis, myasthenia gravis, graft-versus-host disease and autoimmune inflammatory eye disease. Such a protein of the present invention may also to be useful in the treatment of allergic reactions and conditions, such as asthma (particularly allergic asthma) or other respiratory problems. Other conditions, in which immune suppression is desired (including, for example, organ transplantation), may also be treatable using a protein of the present invention . Using the proteins of the invention it may also be possible to immune responses, in a number of ways. Down regulation may be in the form of inhibiting or blocking an immune response already in progress or may involve preventing the induction of an immune response. The functions of activated T cells may be inhibited by suppressing T cell responses or by inducing specific tolerance in T cells, or both. Immunosuppression of T cell responses is generally an active, non-antigen-specific, process which requires continuous exposure of the T cells to the suppressive agent. Tolerance, which involves inducing non-responsiveness or anergy in T cells, is distinguishable from immunosuppression in that it is generally antigen-specific and persists after exposure to the tolerizing agent has ceased. Operationally, tolerance can be demonstrated by the lack of a T cell response upon reexposure to specific antigen in the absence of the tolerizing agent. Down regulating or preventing one or more antigen functions (including without limitation B lymphocyte antigen functions (such as , for example, B7 ) ) , e.g., preventing high level lymphokine synthesis by activated T cells, will be useful in situations of tissue, skin and organ transplantation and in graft-versus-host disease (GVHD). For example, blockage of T cell function should result in reduced tissue destruction in tissue transplantation. Typically, in tissue transplants, rejection of the transplant is initiated through its recognition as foreign by T cells, followed by an immune reaction that destroys the transplant . The administration of a molecule which inhibits or blocks interaction of a B7 lymphocyte antigen with its natural ligand(s) on 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), prior to transplantation can lead to the binding of the molecule to the natural ligand(s) on the immune cells without transmitting the corresponding costimulatory signal. Blocking B lymphocyte antigen function in this matter prevents cytokine synthesis 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. Induction of long-term tolerance by B lymphocyte antigen-blocking reagents may avoid the necessity of 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 efficacy of particular blocking reagents in preventing organ transplant rejection or GVHD can be assessed using animal models that are predictive of efficacy in humans. Examples of appropriate systems which can be used include allogeneic cardiac grafts in rats and xenogeneic pancreatic islet cell 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., Science 257:789-792 (1992) and Turka et al., Proc. Natl. Acad. Sci USA, 89:11102-11105 (1992). In addition, murine models of GVHD (see Paul ed., Fundamental Immunology, Raven Press, New York, 1989, pp. 846-847) can be used to determine the effect of blocking B lymphocyte antigen function in vivo on the development of that disease. Blocking antigen function may also be therapeutically useful for treating autoimmune diseases . Many autoimmune disorders are the result of inappropriate activation of T cells that are reactive against self tissue and which promote the production of cytokines and autoantibodies involved in the pathology of the diseases . Preventing the activation of autoreactive T cells may reduce or eliminate disease symptoms. Administration of reagents which block costimulation of T cells by disrupting receptor : ligand interactions of B lymphocyte antigens can be used to inhibit T cell activation and prevent production of autoantibodies or T cell-derived cytokines which may be involved in the disease process. Additionally, blocking reagents may induce antigen-specific tolerance of autoreactive T cells which could lead to long-term relief from the disease. The efficacy of blocking reagents in preventing or alleviating autoimmune disorders can be determined using a number of well-characterized animal models of human autoimmune diseases. Examples include murine experimental autoimmune encephalitis, systemic lupus erythmatosis 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 ed., Fundamental Immunology, Raven Press, New York, 1989, pp. 840-856). Upregulation of an antigen function (preferably a B lymphocyte antigen function), as a means of up regulating immune responses, may also be useful in therapy. Upregulation of immune responses may be in the form of enhancing an existing immune response or eliciting an initial immune response. For example, enhancing an immune response through stimulating B lymphocyte antigen function may be useful in cases of viral infection. In addition, systemic viral diseases such as influenza, the commoncold, and encephalitis might be alleviated by the administration of stimulatory forms of B lymphocyte antigens systemically. Alternatively, anti-viral immune responses may be enhanced in an infected patient by removing T cells from the patient, costimulating the T cells in vitro with viral antigen-pulsed APCs either expressing a peptide of the present invention or together with a stimulatory form of a soluble peptide of the present invention and reintroducing the in vitro activated T cells into the patient. Another method of enhancing anti-viral immune responses would be to isolate infected cells from a patient, transfect them with a nucleic acid encoding a protein of the present invention as described herein such that the cells express all or a portion of the protein on their surface, and reintroduce the transfected cells into the patient. The infected cells would now be capable of delivering a costimulatory signal to, and thereby activate, T cells in vivo. In another application, up regulation or enhancement of antigen function (preferably B lymphocyte antigen function) may 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 tumor-specific tolerance in the subject. If desired, the tumor cell 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 directing the expression of a peptide having B7-2-like activity alone, or in conjunction with a peptide having B7-l-like activity and/or B7-3-like activity. The transfected tumor cells are returned to the patient to result in expression of the peptides on the surface of the transfected cell. 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 having the activity of a B lymphocyte antigen(s) on the surface of the tumor cell provides the necessary costimulation signal to T cells to induce a T cell mediated immune response against the transfected tumor cells. In addition, tumor cells which lack MHC class I or MHC class II molecules, or which fail to 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 cytoplasmic-domain truncated portion) of an MHC class I chain protein and β 2 microglobulin protein or an MHC class Il chain protein and an MHC class Ilβ chain protein to thereby express MHC class I or MHC class II proteins on the cell surface. Expression of the appropriate class I or class II MHC in conjunction with a peptide having the activity of a B lymphocyte antigen (e.g., B7-1, B7-2, B7-3) induces a T cell mediated immune response against the transfected tumor cell. Optionally, a gene encoding an antisense construct which blocks expression of an MHC class II associated protein, such as the invariant chain, can also be cotransfected with a DNA encoding a peptide having the activity of a B lymphocyte antigen to promote presentation of tumor associated antigens and induce tumor specific immunity. Thus, the induction of a T cell mediated immune response in a human subject may be sufficient to overcome tumor-specific tolerance in the subject. The activity of a protein of the invention may, among other means, be measured by the following methods: Suitable assays for thymocyte or splenocyte cytotoxicity include, without limitation, those described in: Current Protocols in Immunology, Ed 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. Natl. 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; Herrmann et al., Proc. Natl. 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; Bowmanet 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 for 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) assays (which will identify, among others, proteins that generate predominantly Thl and CTL responses) include, without limitation, those described in: Current Protocols in Immunology, Ed 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 naive 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. Assays for lymphocyte survival/apoptosis (which will identify, among others, proteins that prevent apoptosis after superantigen induction and proteins that regulate 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. Assays for proteins that influence early steps of T-cell commitment and development 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 Regulating Activity A protein of the present invention may be useful in regulation of hematopoiesis and, consequently, in the treatment of myeloid or lymphoid cell deficiencies. Even marginal biological activity in support of colony forming cells or of factor-dependent cell lines indicates involvement in regulating hematopoiesis, e.g. in supporting the growth and proliferation of erythroid progenitor cells alone or in combination with other cytokines, thereby indicating utility, for example, in treating various anemias or for use 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 onocytes/macrophages (i.e., traditional CSF activity) useful, for example, in conjunction with chemotherapy to prevent or treat consequent myelo-suppression; in supporting the growth and proliferation of megakaryocytes and consequently of platelets thereby allowing prevention or treatment of various platelet disorders such as thrombocytopenia, and generally for use in place of or complimentary to platelet transfusions; and/or in supporting the growth and proliferation of hematopoietic stem cells which are capable of maturing to any and all of the above-mentioned hematopoietic cells and therefore find therapeutic utility in various stem cell disorders (such as those usually treated with transplantation, including, without limitation, aplastic anemia and paroxysmal nocturnal hemoglobinuria) , as well as in repopulating the stem cell compartment post irradiation/chemotherapy, either in-vivo or ex-vivo (i.e., in conjunction with bone marrow transplantation or with peripheral progenitor cell transplantation (homologous or heterologous ) ) as normal cells or genetically manipulated for gene therapy. The activity of a protein of the invention may, among other means, be measured by the following methods: Suitable assays for proliferation and differentiation of various hematopoietic lines are cited above. Assays for embryonic stem cell differentiation (which will identify, among others, proteins that influence embryonic differentiation hematopoiesis) 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. Assays for stem cell survival and differentiation (which will identify, among others, proteins that regulate lympho-hematopoiesis ) include, without limitation, those described in: Methylcellulose colony forming assays, Freshney, M.G. In Culture of Hematopoietic Cells. R.I. Freshney, et al . eds. Vol pp. 265-268, Wiley-Liss, Inc., New York, NY. 1994; Hiraya a et al., Proc. Natl. 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 marrow cultures in the presence of stromal cells, Spooncer, E., Dexter, M. and Allen, 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 Hematopoietic 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 also may have utility in compositions used for bone, cartilage, tendon, ligament and/or nerve tissue growth or regeneration, as well as for wound healing and tissue repair and replacement, and in the treatment of burns, incisions and ulcers. A protein of the present invention, which induces cartilage and/or bone growth in circumstances where bone is not normally formed, has application in the healing of bone fractures and cartilage damage or defects in humans and other animals . Such a preparation employing a protein of the invention may have prophylactic use in closed as well as open fracture reduction and also in the improved fixation of artificial joints. De novo bone formation induced by an osteogenic agent contributes to the repair of congenital, trauma induced, or oncologic resection induced craniofacial defects, and also is useful in cosmetic plastic surgery. A protein of this invention may also be used in the treatment of periodontal disease, and in other tooth repair processes. Such agents may provide an environment to attract bone-forming cells, stimulate growth of bone-forming cells or induce 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 stimulation of bone and/or cartilage repair or by blocking inflammation or processes of tissue destruction (collagenase activity, osteoclast 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 tendon/ligament-like tissue or other tissue formation in circumstances where such tissue is not normally formed, has application in the healing of tendon or ligament tears, deformities and other tendon or ligament defects in humans and other animals. Such a preparation employing a tendon/ligament-like tissue inducing protein may have prophylactic use in preventing damage to tendon or ligament tissue, as well as use in the improved fixation of tendon or ligament to bone or other tissues, and in repairing defects to tendon or ligament tissue. De novo tendon/ligament-like tissue formation induced by a composition of the present invention contributes to the repair of congenital, trauma induced, or other tendon or ligament defects of other origin, and is also useful in cosmetic plastic surgery for attachment or repair of tendons or ligaments. The compositions of the present invention may provide an environment to attract tendon- or ligament-forming cells, stimulate growth of tendon- or ligament-forming cells, induce differentiation of progenitors of tendon- or ligament-forming cells, or induce growth of tendon/ligament cells or progenitors ex vivo for return in vivo to effect tissue repair. The compositions of the invention may also be useful in the treatment of tendinitis, carpal tunnel syndrome and other tendon or ligament defects. The compositions may also include an appropriate matrix and/or sequestering agent as a carrier as is well known in the art. The protein of the present invention may also be useful for proliferation of neural cells and for regeneration of nerve and brain tissue, i.e. for the treatment of central and peripheral nervous system diseases and neuropathies, as well as mechanical and traumatic disorders, which involve degeneration, death or trauma to neural cells or nerve tissue. More specifically, a protein may be used in the treatment of diseases of the peripheral nervous system, such as peripheral nerve injuries, peripheral neuropathy and localized neuropathies, and central nervous system diseases, such as Alzheimer's, Parkinson's disease, Huntington's disease, amyotrophic lateral sclerosis, and Shy-Drager syndrome. Further conditions which may be treated in accordance with the present invention include mechanical and traumatic disorders, such as spinal cord disorders, head trauma and cerebrovascular diseases such as stroke. Peripheral neuropathies resulting from chemotherapy or other medical therapies may also be treatable using a protein of the invention. Proteins of the invention may also be useful to promote better or faster closure of non-healing wounds, including without limitation pressure ulcers, ulcers associated with vascular insufficiency, surgical and traumatic wounds, and the like. It is expected that a protein of the present invention may also exhibit activity for generation or regeneration of other tissues, such as organs (including, for example, pancreas, liver, intestine, kidney, skin, endothelium) , muscle (smooth, skeletal or cardiac) and vascular (including vascular endothelium) tissue, or for promoting the growth of cells comprising such tissues. Part of the desired effects may be by inhibition or modulation of fibrotic scarring to allow normal tissue to regenerate. A protein of the invention may also exhibit angiogenic activity. A protein of the present invention may also be useful for gut protection or regeneration and 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 differentiation of tissues described above from precursor tissues or cells; or for inhibiting the growth of tissues described above. The activity of a protein of the invention may, among other means, be measured by the following methods: Assays for 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, neuronal); International Patent Publication No. WO91/07491 (skin, endothelium ). Assays for wound healing activity include, without limitation, those described in: Winter, Epidermal Wound Healing, pps . 71-112 (Maibach, HI and Rovee, DT, eds.), Year Book Medical Publishers, Inc., Chicago, as modified by Eaglstein and Mertz, J. Invest. Dermatol 71:382-84 (1978). Activin/Inhibin Activity A protein of the present invention may also exhibit activin- or inhibin-related activities. Inhibins are characterized by their ability to inhibit the release of follicle stimulating hormone (FSH), while activins and are characterized by their ability to stimulate the release of follicle stimulating hormone (FSH). Thus, a protein of the present invention, alone or in heterodimers with a member of the inhibin family, may be useful as a contraceptive based on the ability of inhibins to decrease fertility in female mammals and decrease spermatogenesis in male mammals. 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-β group, may be useful as a fertility inducing therapeutic, based upon the ability of activin molecules in stimulating FSH release from cells of the anterior pituitary. See, for example. United States Patent 4,798,885. A protein of the invention may also be useful for advancement of the onset of fertility in sexually immature mammals, so as to increase the lifetime reproductive performance of domestic animals such as cows, sheep and pigs . The activity of a protein of the invention may, among other means, be measured by the following methods: Assays for 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. Natl. Acad. Sci. USA 83:3091-3095, 1986. Chemotactic/Chemokinetic Activity A protein of the present invention may have chemotactic or chemokinetic activity (e.g., act as a chemokine) for mammalian cells, including, for example, monocytes, fibroblasts, neutrophils, T-cells, mast cells, eosinophils, epithelial and/or endothelial cells. Chemotactic and chemokinetic proteins can be used to mobilize or attract a desired cell population to a desired site of action. Chemotactic or chemokinetic proteins provide particular advantages in treatment of wounds and other trauma to tissues, as well as in treatment of localized infections. For example, attraction of lymphocytes, monocytes or neutrophils to tumors or sites of infection may result in improved immune responses against the tumor or infecting agent. A protein or peptide has chemotactic activity for a particular cell population if it can stimulate, directly or indirectly, the directed orientation or movement of such cell population. Preferably, the protein or peptide has the ability to directly stimulate directed movement of cells. Whether a particular protein has chemotactic activity for a population of cells can be readily determined by employing such protein or peptide in any known assay for cell che otaxis . The activity of a protein of the invention may, among other means, be measured by the following methods: Assays for 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 across a membrane as well as the ability of a protein to induce the adhesion of one cell population to another cell population. Suitable assays for movement and adhesion include, without limitation, those described in: Current Protocols in Immunology, Ed by J.E. Coligan, A.M. Kruisbeek, D.H. Margulies, E.M. Shevach, W. Strober, Pub. 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; Johnston et al . J. of Immunol. 153: 1762-1768, 1994. Hemostatic and Thrombolytic Activity A protein of the invention may also exhibit hemostatic or thrombolytic activity. As a result, such a protein is expected to be useful in treatment of various coagulation disorders (includinghereditary disorders, such as hemophilias) or to enhance coagulation and other hemostatic events in treating wounds resulting from trauma, surgery or other causes. A protein of the invention may also be useful for dissolving or inhibiting formation of thromboses and for treatment and prevention of conditions resulting therefrom (such as, for example, infarction of cardiac and central nervous system vessels (e.g., stroke). The activity of a protein of the invention may, among other means, be measured by the following methods: Assay for hemostatic 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 may also demonstrate activity as receptors, receptor ligands or inhibitors or agonists of receptor/ligand interactions. Examples of such receptors and ligands include, without limitation, cytokine receptors and their ligands, receptor kinases and their ligands, receptor phosphatases and their ligands, receptors involved in cell-cell interactions and their ligands (including without limitation, cellular 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). Receptors and ligands are also useful for 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 themselves be useful as inhibitors of receptor/ligand interactions. The activity of a protein of the invention may, among other means, be measured by the following methods: Suitable assays for receptor-ligand activity include without limitation those described in: Current Protocols in Immunology, Ed 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, Measurement of Cellular Adhesion under static conditions 7.28.1-7.28.22), Takai et al . , Proc. Natl. 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 Proteins of the present invention may also exhibit anti-inflammatory activity. The anti-inflammatory activity may be achieved by providing a stimulus to cells involved in the inflammatory response, by inhibiting or promoting cell-cell interactions (such as, for example, cell adhesion), by inhibiting or promoting chemotaxis of cells involved in the inflammatory process, inhibiting or promoting cell extravasation, or by stimulating or suppressing production of other factors which more 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 infection (such as septic shock, sepsis or systemic inflammatory response syndrome (SIRS)), ischemia-reperfusion injury, endotoxin lethality, arthritis, complement-mediated hyperacute rejection, nephritis, cytokine or chemokine-induced lung injury, inflammatory bowel disease, Crohn's disease or resulting from over production of ytokines such as TNF or IL-1. Proteins of the invention may also be useful to treat anaphylaxis and hypersensitivity to an antigenic substance or material. Tumor Inhibition Activity In addition to the activities described above for immunological treatment or prevention of tumors, a protein of the invention may exhibit other anti-tumor activities. A protein may inhibit tumor growth 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, by inhibiting formation of tissues necessary to support tumor growth (such as, for example, by inhibiting angiogenesis ) , by causing production of other factors, agents or cell types which inhibit tumor growth, or by suppressing, eliminating or inhibiting factors, agents or cell types which promote tumor growth Other Activities A protein of the invention may also exhibit one or more of the following additional activities or effects: inhibiting the growth, infection or function of, or killing, infectious agents, including, without limitation, bacteria, viruses, fungi and other parasites; effecting (suppressing or enhancing) bodily characteristics, including, without limitation, height, weight, hair color, eye color, skin, fat to lean ratio or other tissue pigmentation, or organ or body part size or shape (such as, for example, breast augmentation or diminution, change in bone form or shape); effecting biorhythms or caricadic cycles or rhythms; effecting the fertility of male or female subjects; effecting the metabolism, catabolism, anabolis , processing, utilization, storage or elimination of dietary fat, lipid, protein, carbohydrate, vitamins, minerals, cofactors or other nutritional factors or component ( s ) ; effecting behavioral characteristics, including, without limitation, appetite, libido, stress, cognition (including cognitive disorders), depression (including depressive disorders) and violent behaviors; providing analgesic effects or other pain reducing effects; promoting differentiation and growth of embryonic stem cells in lineages other than hematopoietic lineages; hormonal or endocrine activity; in the case of enzymes, correcting deficiencies of the enzyme and treating deficiency-related diseases; treatment of hyperproliferative disorders (such as, for example, psoriasis); immunoglobulin-like activity (such as, for example, the ability to bind antigens or complement); and the ability to act as an antigen in a vaccine composition to raise an immune response against such protein or another material or entity which is cross-reactive with such protein. SEQUENCE LISTING Sequence No. : 1 Sequence length: 154 Sequence type: Amino acid Topology: Linear Sequence kind: Protein Hypothetical : No Original source: Organism species: Homo sapiens Cell kind: Fibrosarcoma Cell line: HT-1080 Clone name: HP00658 Sequence description Met Lys Val Ser Ala Ala Ala Leu Ala Val He Leu He Ala Thr Ala 1 5 10 15 Leu Cys Ala Pro Ala Ser Ala Ser Pro Tyr Ser Ser Asp Thr Thr Pro 20 25 30 Cys Cys Phe Ala Tyr He Ala Arg Pro Leu Pro Arg Ala His He Lys 35 40 45 Glu Tyr Phe Tyr Thr Ser Gly Lys Cys Ser Asn Pro Ala Val Val His 50 55 60 Arg Ser Arg Met Pro Lys Arg Glu Gly Gin Gin Val Trp Gin Asp Phe 65 70 75 80 Leu Tyr Asp Ser Arg Leu Asn Lys Gly Lys Leu Cys His Pro Lys Glu 85 90 95 Pro Pro Ser Val Cys Gin Pro Arg Glu Glu Met Gly Ser Gly Val His 100 105 110 Gin Leu Phe Gly Asp Glu Leu Gly Trp Arg Val Leu Glu Pro Glu Leu 115 120 125 Thr Gin He Cys Leu Phe Leu Leu Ala Leu Val Leu Ala Trp Glu Ala 130 135 140 Ser Pro His Tyr Pro Thr Pro Pro Ala Pro 145 150 Sequence No. : 2 Sequence length: 315 Sequence type: Amino acid Topology: Linear Sequence kind: Protein Hypothetical : No Original source: Organism species: Homo sapiens Cell kind: Epidermoid carcinoma Cell line: KB Clone name: HP00714 Sequence description Met Asp Leu Arg Gin Phe Leu Met Cys Leu Ser Leu Cys Thr Ala Phe 1 5 10 15 Ala Leu Ser Lys Pro Thr Glu Lys Lys Asp Arg Val His His Glu Pro 20 25 30 Gin Leu Ser Asp Lys Val His Asn Asp Ala Gin Ser Phe Asp Tyr Asp 35 40 45 His Asp Ala Phe Leu Gly Ala Glu Glu Ala Lys Thr Phe Asp Gin Leu 50 55 60 Thr Pro Glu Glu Ser Lys Glu Arg Leu Gly Lys He Val Ser Lys He 65 70 75 80 sp Gly Asp Lys Asp Gly Phe Val Thr Val Asp Glu Leu Lys Asp Trp 85 90 95 He Lys Phe Ala Gin Lys Arg Trp He Tyr Glu Asp Val Glu Arg Gin 100 105 110 Trp Lys Gly His Asp Leu Asn Glu Asp Gly Leu Val Ser Trp Glu Glu 115 120 125 Tyr Lys Asn Ala Thr Tyr Gly Tyr Val Leu Asp Asp Pro Asp Pro Asp 130 135 140 Asp Gly Phe Asn Tyr Lys Gin Met Met Val Arg Asp Glu Arg Arg Phe 145 150 155 160 Lys Met Ala Asp Lys Asp Gly Asp Leu He Ala Thr Lys Glu Glu Phe 165 170 175 Thr Ala Phe Leu His Pro Glu Glu Tyr Asp Tyr Met Lys Asp He Val 180 185 190 Val Gin Glu Thr Met Glu Asp He Asp Lys Asn Ala Asp Gly Phe He 195 200 205 Asp Leu Glu Glu Tyr He Gly Asp Met Tyr Ser His Asp Gly Asn Thr 210 215 220 Asp Glu Pro Glu Trp Val Lys Thr Glu Arg Glu Gin Phe Val Glu Phe 225 230 235 240 Arg Asp Lys Asn Arg Asp Gly Lys Met Asp Lys Glu Glu Thr Lys Asp 245 250 255 Trp He Leu Pro Ser Asp Tyr Asp His Ala Glu Ala Glu Ala Arg His 260 265 270 Leu Val Tyr Glu Ser Asp Gin Asn Lys Asp Gly Lys Leu Thr Lys Glu 275 280 285 Glu He Val Asp Lys Tyr Asp Leu Phe Val Gly Ser Gin Ala Thr Asp 290 295 300 Phe Gly Glu Ala Leu Val Arg His Asp Glu Phe 305 310 315 Sequence No. : 3 Sequence length: 158 Sequence type : Amino acid Topology: Linear Sequence kind : Protein Hypothetical : No Original source : Organism species : Homo sapiens Cell kind: Stomach cancer Clone name: HP00876 Sequence description Met Ala Ser Arg Ser Met Arg Leu Leu Leu Leu Leu Ser Cys Leu Ala 1 5 10 15 Lys Thr Gly Val Leu Gly Asp He He Met Arg Pro Ser Cys Ala Pro 20 25 30 Gly Trp Phe Tyr His Lys Ser Asn Cys Tyr Gly Tyr Phe Arg Lys Leu 35 40 45 Arg Asn Trp Ser Asp Ala Glu Leu Glu Cys Gin Ser Tyr Gly Asn Gly 50 55 60 Ala His Leu Ala Ser He Leu Ser Leu Lys Glu Ala Ser Thr He Ala 65 70 75 80 Glu Tyr He Ser Gly Tyr Gin Arg Ser Gin Pro He Trp He Gly Leu 85 90 95 His Asp Pro Gin Lys Arg Gin Gin Trp Gin Trp He Asp Gly Ala Met 100 105 110 Tyr Leu Tyr Arg Ser Trp Ser Gly Lys Ser Met Gly Gly Asn Lys His 115 120 125 Cys Ala Glu Met Ser Ser Asn Asn Asn Phe Leu Thr Trp Ser Ser Asn 130 135 140 Glu Cys Asn Lys Arg Gin His Phe Leu Cys Lys Tyr Arg Pro 145 150 155 Sequence No. : 4 Sequence length: 376 Sequence type: Amino acid Topology: Linear Sequence kind: Protein Hypothetical : No Original source: Organism species: Homo sapiens Cell kind: Liver Clone name: HP01134 Sequence description Met Val Trp Lys Val Ala Val Phe Leu Ser Val Ala Leu Gly He Gly 1 5 10 15 Ala Val Pro He Asp Asp Pro Glu Asp Gly Gly Lys His Trp Val Val 20 25 30 He Val Ala Gly Ser Asn Gly Trp Tyr Asn Tyr Arg His Gin Ala Asp 35 40 45 Ala Cys His Ala Tyr Gin He He His Arg Asn Gly He Pro Asp Glu 50 55 60 Gin He Val Val Met Met Tyr Asp Asp He Ala Tyr Ser Glu Asp Asn 65 70 75 80 Pro Thr Pro Gly He Val He Asn Arg Pro Asn Gly Thr Asp Val Tyr 85 90 95 Gin Gly Val Pro Lys Asp Tyr Thr Gly Glu Asp Val Thr Pro Gin Asn 100 105 110 Phe Leu Ala Val Leu Arg Gly Asp Ala Glu Ala Val Lys Gly He Gly 115 120 125 Ser Gly Lys Val Leu Lys Ser Gly Pro Gin Asp His Val Phe He Tyr 130 135 140 Phe Thr Asp His Gly Ser Thr Gly He Leu Val Phe Pro Asn Glu Asp 145 150 155 160 Leu His Val Lys Asp Leu Asn Glu Thr He His Tyr Met Tyr Lys His 165 170 175 Lys Met Tyr Arg Lys Met Val Phe Tyr He Glu Ala Cys Glu Ser Gly 180 185 190 Ser Met Met Asn His Leu Pro Asp Asn He Asn Val Tyr Ala Thr Thr 195 200 205 Ala Ala Asn Pro Arg Glu Ser Ser Tyr Ala Cys Tyr Tyr Asp Glu Lys 210 215 220 Arg Ser Thr Tyr Leu Gly Asp Trp Tyr Ser Val Asn Trp Met Glu Asp 225 230 235 240 Ser Asp Val Glu Asp Leu Thr Lys Glu Thr Leu His Lys Gin Tyr His 245 250 255 Leu Val Lys Ser His Thr Asn Thr Ser His Val Met Gin Tyr Gly Asn 260 265 270 Lys Thr He Ser Thr Met Lys Val Met Gin Phe Gin Gly Met Lys Arg 275 280 285 Lys Ala Ser Ser Pro Val Pro Leu Pro Pro Val Thr His Leu Asp Leu 290 295 300 Thr Pro Ser Pro Asp Val Pro Leu Thr He Met Lys Arg Lys Leu Met 305 310 315 320 Asn Thr Asn Asp Leu Glu Glu Ser Arg Gin Leu Thr Glu Glu He Gin 325 330 335 Arg His Leu Asp Tyr Glu Tyr Ala Leu Arg His Leu Tyr Val Leu Val 340 345 350 Asn Leu Cys Glu Lys Pro Tyr Pro Leu His Arg He Lys Leu Ser Met 355 360 365 Asp His Val Cys Leu Gly His Tyr 370 375 Sequence No . : 5 Sequence length: 173 Sequence type: Amino acid Topology : Linear Sequence kind: Protein Hypothetical : No Original source: Organism species: Homo sapiens Cell kind: Epidermoid carcinoma Cell line: KB Clone name: HP10029 Sequence description Met Ala Ala Pro Ser Gly Gly Trp Asn Gly Val Arg Ala Ser Leu Trp 1 5 10 15 Ala Ala Leu Leu Leu Gly Ala Val Ala Leu Arg Pro Ala Glu Ala Val 20 25 30 Ser Glu Pro Thr Thr Val Ala Phe Asp Val Arg Pro Gly Gly Val Val 35 40 45 His Ser Phe Ser His Asn Val Gly Pro Gly Asp Lys Tyr Thr Cys Met 50 55 60 Phe Thr Tyr Ala Ser Gin Gly Gly Thr Asn Glu Gin Trp Gin Met Ser 65 70 75 80 Leu Gly Thr Ser Glu Asp His Gin His Phe Thr Cys Thr He Trp Arg 85 90 95 Pro Gin Gly Lys Ser Tyr Leu Tyr Phe Thr Gin Phe Lys Ala Glu Val 100 105 110 Arg Gly Ala Glu He Glu Tyr Ala Met Ala Tyr Ser Lys Ala Ala Phe 115 120 125 Glu Arg Glu Ser Asp Val Pro Leu Lys Thr Glu Glu Phe Glu Val Thr 130 135 140 Lys Thr Ala Val Ala His Arg Pro Gly Ala Phe Lys Ala Glu Leu Ser 145 150 155 160 Lys Leu Val He Val Ala Lys Ala Ser Arg Thr Glu Leu 165 170 Sequence No. : 6 Sequence length: 73 Sequence type : Amino acid Topology : Linear Sequence kind: Protein Hypothetical: No Original source : Organism species: Homo sapiens Cell kind: Epidermoid carcinoma Cell line: KB Clone name: HP10189 Sequence description Met Gly Val Lys Leu Glu He Phe Arg Met He He Tyr Leu Thr Phe 1 5 10 15 Pro Val Ala Met Phe Trp Val Ser Asn Gin Ala Glu Trp Phe Glu Asp 20 25 30 Asp Val He Gin Arg Lys Arg Glu Leu Trp Pro Pro Glu Lys Leu Gin 35 40 45 Glu He Glu Glu Phe Lys Glu Arg Leu Arg Lys Arg Arg Glu Glu Lys 50 55 60 Leu Leu Arg Asp Ala Gin Gin Asn Ser 65 70 Sequence No. : 7 Sequence length: 1172 Sequence type: Amino acid Topology: Linear Sequence kind: Protein Hypothetical : No Original source : Organism species: Homo sapiens Cell kind: Histiocyte lymphoma Cell line: U937 Clone name: HP10269 Sequence description Met Arg Pro Phe Phe Leu Leu Cys Phe Ala Leu Pro Gly Leu Leu His 1 5 10 15 Ala Gin Gin Ala Cys Ser Arg Gly Ala Cys Tyr Pro Pro Val Gly Asp 20 25 30 Leu Leu Val Gly Arg Thr Arg Phe Leu Arg Ala Ser Ser Thr Cys Gly 35 40 45 Leu Thr Lys Pro Glu Thr Tyr Cys Thr Gin Tyr Gly Glu Trp Gin Met 50 55 60 Lys Cys Cys Lys Cys Asp Ser Arg Gin Pro His Asn Tyr Tyr Ser His 65 70 75 80 Arg Val Glu Asn Val Ala Ser Ser Ser Gly Pro Met Arg Trp Trp Gin 85 90 95 Ser Gin Asn Asp Val Asn Pro Val Ser Leu Gin Leu Asp Leu Asp Arg 100 105 110 Arg Phe Gin Leu Gin Glu Val Met Met Glu Phe Gin Gly Pro Met Pro 115 120 125 Ala Gly Met Leu He Glu Arg Ser Ser Asp Phe Gly Lys Thr Trp Arg 130 135 140 Val Tyr Gin Tyr Leu Ala Ala Asp Cys Thr Ser Thr Phe Pro Arg Val 145 150 155 160 Arg Gin Gly Arg Pro Gin Ser Trp Gin Asp Val Arg Cys Gin Ser Leu 165 170 175 Pro Gin Arg Pro Asn Ala Arg Leu Asn Gly Gly Lys Val Gin Leu Asn 180 185 190 Leu Met Asp Leu Val Ser Gly He Pro Ala Thr Gin Ser Gin Lys He 195 200 205 Gin Glu Val Gly Glu He Thr Asn Leu Arg Val Asn Phe Thr Arg Leu 210 215 220 Ala Pro Val Pro Gin Arg Gly Tyr His Pro Pro Ser Ala Tyr Tyr Ala 225 230 235 240 Val Ser Gin Leu Arg Leu Gin Gly Ser Cys Phe Cys His Gly His Ala 245 250 255 Asp Arg Cys Ala Pro Lys Pro Gly Ala Ser Ala Gly Pro Ser Thr Ala 260 265 270 Val Gin Val His Asp Val Cys Val Cys Gin His Asn Thr Ala Gly Pro 275 280 285 Asn Cys Glu Arg Cys Ala Pro Phe Tyr Asn Asn Arg Pro Trp Arg Pro 290 295 300 Ala Glu Gly Gin Asp Ala His Glu Cys Gin Arg Cys Asp Cys Asn Gly 305 310 315 320 His Ser Glu Thr Cys His Phe Asp Pro Ala Val Phe Ala Ala Ser Gin 325 330 335 Gly Ala Tyr Gly Gly Val Cys Asp Asn Cys Arg Asp His Thr Glu Gly 340 345 350 Lys Asn Cys Glu Arg Cys Gin Leu His Tyr Phe Arg Asn Arg Arg Pro 355 360 365 Gly Ala Ser He Gin Glu Thr Cys He Ser Cys Glu Cys Asp Pro Asp 370 375 380 Gly Ala Val Pro Gly Ala Pro Cys Asp Pro Val Thr Gly Gin Cys Val 385 390 395 400 Cys Lys Glu His Val Gin Gly Glu Arg Cys Asp Leu Cys Lys Pro Gly 405 410 415 Phe Thr Gly Leu Thr Tyr Ala Asn Pro Gin Gly Cys His Arg Cys Asp 420 425 430 Cys Asn He Leu Gly Ser Arg Arg Asp Met Pro Cys Asp Glu Glu Ser 435 440 445 Gly Arg Cys Leu Cys Leu Pro Asn Val Val Gly Pro Lys Cys Asp Gin 450 455 460 Cys Ala Pro Tyr His Trp Lys Leu Ala Ser Gly Gin Gly Cys Glu Pro 465 470 475 480 Cys Ala Cys Asp Pro His Asn Ser Leu Ser Pro Gin Cys Asn Gin Phe 485 490 495 Thr Gly Gin Cys Pro Cys Arg Glu Gly Phe Gly Gly Leu Met Cys Ser 500 505 510 Ala Ala Ala He Arg Gin Cys Pro Asp Arg Thr Tyr Gly Asp Val Ala 515 520 525 Thr Gly Cys Arg Ala Cys Asp Cys Asp Phe Arg Gly Thr Glu Gly Pro 530 535 540 Gly Cys Asp Lys Ala Ser Gly Arg Cys Leu Cys Arg Pro Gly Leu Thr 545 550 555 560 Gly Pro Arg Cys Asp Gin Cys Gin Arg Gly Tyr Cys Asn Arg Tyr Pro 565 570 575 Val Cys Val Ala Cys His Pro Cys Phe Gin Thr Tyr Asp Ala Asp Leu 580 585 590 Arg Glu Gin Ala Leu Arg Phe Gly Arg Leu Arg Asn Ala Thr Ala Ser 595 600 605 Leu Trp Ser Gly Pro Gly Leu Glu Asp Arg Gly Leu Ala Ser Arg He 610 615 620 Leu Asp Ala Lys Ser Lys He Glu Gin He Arg Ala Val Leu Ser Ser 625 630 635 640 Pro Ala Val Thr Glu Gin Glu Val Ala Gin Val Ala Ser Ala He Leu 645 650 655 Ser Leu Arg Arg Thr Leu Gin Gly Leu Gin Leu Asp Leu Pro Leu Glu 660 665 670 Glu Glu Thr Leu Ser Leu Pro Arg Asp Leu Glu Ser Leu Asp Arg Ser 675 680 685 Phe Asn Gly Leu Leu Thr Met Tyr Gin Arg Lys Arg Glu Gin Phe Glu 690 695 700 Lys He Ser Ser Ala Asp Pro Ser Gly Ala Phe Arg Met Leu Ser Thr 705 710 715 720 Ala Tyr Glu Gin Ser Ala Gin Ala Ala Gin Gin Val Ser Asp Ser Ser 725 730 735 Arg Leu Leu Asp Gin Leu Arg Asp Ser Arg Arg Glu Ala Glu Arg Leu 740 745 750 Val Arg Gin Ala Gly Gly Gly Gly Gly Thr Gly Ser Pro Lys Leu Val 755 760 765 Ala Leu Arg Leu Glu Met Ser Ser Leu Pro Asp Leu Thr Pro Thr Phe 770 775 780 Asn Lys Leu Cys Gly Asn Ser Arg Gin Met Ala Cys Thr Pro He Ser 785 790 795 800 Cys Pro Gly Glu Leu Cys Pro Gin Asp Asn Gly Thr Ala Cys Gly Ser 805 810 815 Arg Cys Arg Gly Val Leu Pro Arg Ala Gly Gly Ala Phe Leu Met Ala 820 825 830 Gly Gin Val Ala Glu Gin Leu Arg Gly Phe Asn Ala Gin Leu Gin Arg 835 840 845 Thr Arg Gin Met He Arg Ala Ala Glu Glu Ser Ala Ser Gin He Gin 850 855 860 Ser Ser Ala Gin Arg Leu Glu Thr Gin Val Ser Ala Ser Arg Ser Gin 865 870 875 880 Met Glu Glu Asp Val Arg Arg Thr Arg Leu Leu He Gin Gin Val Arg 885 890 895 Asp Phe Leu Thr Asp Pro Asp Thr Asp Ala Ala Thr He Gin Glu Val 900 905 910 Ser Glu Ala Val Leu Ala Leu Trp Leu Pro Thr Asp Ser Ala Thr Val 915 920 925 Leu Gin Lys Met Asn Glu He Gin Ala He Ala Ala Arg Leu Pro Asn 930 935 940 Val Asp Leu Val Leu Ser Gin Thr Lys Gin Asp He Ala Arg Ala Arg 945 950 955 960 Arg Leu Gin Ala Glu Ala Glu Glu Ala Arg Ser Arg Ala His Ala Val 965 970 975 Glu Gly Gin Val Glu Asp Val Val Gly Asn Leu Arg Gin Gly Thr Val 980 985 990 Ala Leu Gin Glu Ala Gin Asp Thr Met Gin Gly Thr Ser Arg Ser Leu 995 1000 1005 Arg Leu He Gin Asp Arg Val Ala Glu Val Gin Gin Val Leu Arg Pro 1010 1015 1020 Ala Glu Lys Leu Val Thr Ser Met Thr Lys Gin Leu Gly Asp Phe Trp 1025 1030 1035 1040 Thr Arg Met Glu Glu Leu Arg His Gin Ala Arg Gin Gin Gly Ala Glu 1045 1050 1055 Ala Val Gin Ala Gin Gin Leu Ala Glu Gly Ala Ser Glu Gin Ala Leu 1060 1065 1070 Ser Ala Gin Glu Gly Phe Glu Arg He Lys Gin Lys Tyr Ala Glu Leu 1075 1080 1085 Lys Asp Arg Leu Gly Gin Ser Ser Met Leu Gly Glu Gin Gly Ala Arg 1090 1095 1100 He Gin Ser Val Lys Thr Glu Ala Glu Glu Leu Phe Gly Glu Thr Met 1105 1110 1115 1120 Glu Met Met Asp Arg Met Lys Asp Met Glu Leu Glu Leu Leu Arg Gly 1125 1130 1135 Ser Gin Ala He Met Leu Arg Ser Ala Asp Leu Thr Gly Leu Glu Lys 1140 1145 1150 Arg Val Glu Gin He Arg Asp His He Asn Gly Arg Val Leu Tyr Tyr 1155 1160 1165 Ala Thr Cys Lys 1170 Sequence No. : 8 Sequence length: 122 Sequence type: Amino acid Topo1ogy: Linear Sequence kind: Protein Hypothetical : No Original source: Organism species: Homo sapiens Cell kind: Stomach cancer Clone name: HP10298 Sequence description Met Gly Leu Leu Leu Leu Val Pro Leu Leu Leu Leu Pro Gly Ser Tyr 1 5 10 15 Gly Leu Pro Phe Tyr Asn Gly Phe Tyr Tyr Ser Asn Ser Ala Asn Asp 20 25 30 Gin Asn Leu Gly Asn Gly His Gly Lys Asp Leu Leu Asn Gly Val Lys 35 40 45 Leu Val Val Glu Thr Pro Glu Glu Thr Leu Phe Thr Arg He Leu Thr 50 55 60 Val Gly Pro Gin Ser Leu Gly Ser Glu Ala Leu Ala Ser Pro Thr Arg 65 70 75 80 Arg Ala Ala Cys Thr Val Phe Thr Ala Thr Ala Ser Thr Arg Thr Trp 85 90 95 Gly Pro Pro Leu Pro His Ser Leu Thr Gly Cys Val Phe He Glu Trp 100 105 110 Phe Val Phe Pro Cys Gly Leu Glu Pro Phe 115 120 Sequence No. : 9 Sequence length: 175 Sequence type: Amino acid Topology : Linear Sequence kind: Protein Hypothetical : No Original source: Organism species: Homo sapiens Cell kind: Stomach cancer Clone name: HP10368 Sequence description Met Glu Lys He Pro Val Ser Ala Phe Leu Leu Leu Val Ala Leu Ser 1 5 10 15 Tyr Thr Leu Ala Arg Asp Thr Thr Val Lys Pro Gly Ala Lys Lys Asp 20 25 30 Thr Lys Asp Ser Arg Pro Lys Leu Pro Gin Thr Leu Ser Arg Gly Trp 35 40 45 Gly Asp Gin Leu He Trp Thr Gin Thr Tyr Glu Glu Ala Leu Tyr Lys 50 55 60 Ser Lys Thr Ser Asn Lys Pro Leu Met He He His His Leu Asp Glu 65 70 75 80 Cys Pro His Ser Gin Ala Leu Lys Lys Val Phe Ala Glu Asn Lys Glu 85 90 95 He Gin Lys Leu Ala Glu Gin Phe Val Leu Leu Asn Leu Val Tyr Glu 100 105 110 Thr Thr Asp Lys His Leu Ser Pro Asp Gly Gin Tyr Val Pro Arg He 115 120 125 Met Phe Val Asp Pro Ser Leu Thr Val Arg Ala Asp He Thr Gly Arg 130 135 140 Tyr Ser Asn Arg Leu Tyr Ala Tyr Glu Pro Ala Asp Thr Ala Leu Leu 145 150 155 160 Leu Asp Asn Met Lys Lys Ala Leu Lys Leu Leu Lys Thr Glu Leu 165 170 175 Sequence No.: 10 Sequence length: 462 Sequence type: Nucleic acid Strandedness: Double Topolog : Linear Sequence kind: cDNA to mRNA Original source: Organism species: Homo sapiens Cell kind: Fibrosarcoma Cell line: HT-1080 Clone name: HP00658 Sequence description ATGAAGGTCT CCGCGGCAGC CCTCGCTGTC ATCCTCATTG CTACTGCCCT CTGCGCTCCT 60 GCATCTGCCT CCCCATATTC CTCGGACACC ACACCCTGCT GCTTTGCCTA CATTGCCCGC 120 CCACTGCCCC GTGCCCACAT CAAGGAGTAT TTCTACACCA GTGGCAAGTG CTCCAACCCA 180 GCAGTCGTCC ACAGGTCAAG GATGCCAAAG AGAGAGGGAC AGCAAGTCTG GCAGGATTTC 240 CTGTATGACT CCCGGCTGAA CAAGGGCAAG CTTTGTCACC CGAAAGAACC GCCAAGTGTG 300 TGCCAACCCA GAGAAGAAAT GGGTTCGGGA GTACATCAAC TCTTTGGAGA TGAGCTAGGA 360 TGGAGAGTCC TTGAACCTGA ACTTACACAA ATTTGCCTGT TTCTGCTTGC TCTTGTCCTA 420 GCTTGGGAGG CTTCCCCTCA CTATCCTACC CCACCCGCTC CT 462 Sequence No. : 11 Sequence length: 945 Sequence type: Nucleic acid Strandedness : Double Topology: Linear Sequence kind: cDNA to mRNA Original source: Organism species: Homo sapiens Cell kind: Epidermoid carcinoma Cell line: KB Clone name: HP00714 Sequence description ATGGACCTGC GACAGTTTCT TATGTGCCTG TCCCTGTGCA CAGCCTTTGC CTTGAGCAAA 60 CCCACAGAAA AGAAGGACCG TGTACATCAT GAGCCTCAGC TCAGTGACAA GGTTCACAAT 120 GATGCTCAGA GTTTTGATTA TGACCATGAT GCCTTCTTGG GTGCTGAAGA AGCAAAGACC 180 TTTGATCAGC TGACACCAGA AGAGAGCAAG GAAAGGCTTG GAAAGATTGT AAGTAAAATA 240 GATGGCGACA AGGACGGGTT TGTCACTGTG GATGAGCTCA AAGACTGGAT TAAATTTGCA 300 CAAAAGCGCT GGATTTACGA GGATGTAGAG CGACAGTGGA AGGGGCATGA CCTCAATGAG 360 GACGGCCTCG TTTCCTGGGA GGAGTATAAA AATGCCACCT ACGGCTACGT TTTAGATGAT 420 CCAGATCCTG ATGATGGATT TAACTATAAA CAGATGATGG TTAGAGATGA GCGGAGGTTT 480 AAAATGGCAG ACAAGGATGG AGACCTCATT GCCACCAAGG AGGAGTTCAC AGCTTTCCTG 540 CACCCTGAGG AGTATGACTA CATGAAAGAT ATAGTAGTAC AGGAAACAAT GGAAGATATA 600 GATAAGAATG CTGATGGTTT CATTGATCTA GAAGAGTATA TTGGTGACAT GTACAGCCAT 660 GATGGGAATA CTGATGAGCC AGAATGGGTA AAGACAGAGC GAGAGCAGTT TGTTGAGTTT 720 CGGGATAAGA ACCGTGATGG GAAGATGGAC AAGGAAGAGA CCAAAGACTG GATCCTTCCC 780 TCAGACTATG ATCATGCAGA GGCAGAAGCC AGGCACCTGG TCTATGAATC AGACCAAAAC 840 AAGGATGGCA AGCTTACCAA GGAGGAGATC GTTGACAAGT ATGACTTATT TGTTGGCAGC 900 CAGGCCACAG ATTTTGGGGA GGCCTTAGTA CGGCATGATG AGTTC 945 Sequence No. : 12 Sequence length: 474 Sequence type: Nucleic acid Strandedness : Double Topology: Linear Sequence kind: cDNA to mRNA Original source: Organism species: Homo sapiens Cell kind: Stomach cancer Clone name: HP00876 Sequence description ATGGCTTCCA GAAGCATGCG GCTGCTCCTA TTGCTGAGCT GCCTGGCCAA AACAGGAGTC 60 CTGGGTGATA TCATCATGAG ACCCAGCTGT GCTCCTGGAT GGTTTTACCA CAAGTCCAAT 120 TGCTATGGTT ACTTCAGGAA GCTGAGGAAC TGGTCTGATG CCGAGCTCGA GTGTCAGTCT 180 TACGGAAACG GAGCCCACCT GGCATCTATC CTGAGTTTAA AGGAAGCCAG CACCATAGCA 240 GAGTACATAA GTGGCTATCA GAGAAGCCAG CCGATATGGA TTGGCCTGCA CGACCCACAG 300 AAGAGGCAGC AGTGGCAGTG GATTGATGGG GCCATGTATC TGTACAGATC CTGGTCTGGC 360 AAGTCCATGG GTGGGAACAA GCACTGTGCT GAGATGAGCT CCAATAACAA CTTTTTAACT 420 TGGAGCAGCA ACGAATGCAA CAAGCGCCAA CACTTCCTGT GCAAGTACCG ACCA 474 Sequence No.: 13 Sequence length: 1128 Sequence type: Nucleic acid Strandedness: Double Topology: Linear Sequence kind: cDNA to mRNA Original source: Organism species: Homo sapiens Cell kind: Liver Clone name: HP01134 Sequence description ATGGTTTGGA AAGTAGCTGT ATTCCTCAGT GTGGCCCTGG GCATTGGTGC CGTTCCTATA 60 GATGATCCTG AAGATGGAGG CAAGCACTGG GTGGTGATCG TGGCAGGTTC AAATGGCTGG 120 TATAATTΔTA GGCACCAGGC AGACGCGTGC CATGCCTACC AGATCATTCA CCGCAATGGG 180 ATTCCTGACG AACAGATCGT TGTGATGATG TACGATGACA TTGCTTACTC TGAAGACAAT 240 CCCACTCCAG GAATTGTGAT CAACAGGCCC AATGGCACAG ATGTCTATCA GGGAGTCCCG 300 AAGGACTACA CTGGAGAGGA TGTTACCCCA CAAAATTTCC TTGCTGTGTT GAGAGGCGAT 360 GCAGAAGCAG TGAAGGGCAT AGGATCCGGC AAAGTCCTGA AGAGTGGCCC CCAGGATCAC 420 GTGTTCATTT ACTTCACTGA CCATGGATCT ACTGGAATAC TGGTTTTTCC CAATGAAGAT 480 CTTCATGTAA AGGACCTGAA TGAGACCATC CATTACATGT ACAAACACAA AATGTACCGA 540 AAGATGGTGT TCTACATTGA AGCCTGTGAG TCTGGGTCCA TGATGAACCA CCTGCCGGAT 600 AACATCAATG TTTATGCAAC TACTGCTGCC AACCCCAGAG AGTCGTCCTA CGCCTGTTAC 660 TATGATGAGA AGAGGTCCAC GTACCTGGGG GACTGGTACA GCGTCAACTG GATGGAAGAC 720 TCGGACGTGG AAGATCTGAC TAAAGAGACC CTGCACAAGC AGTACCACCT GGTAAAATCG 780 CACACCAACA CCAGCCACGT CATGCAGTAT GGAAACAAAA CAATCTCCAC CATGAAAGTG 840 ATGCAGTTTC AGGGTATGAA ACGCAAAGCC AGTTCTCCCG TCCCCCTACC TCCAGTCACA 900 CACCTTGACC TCACCCCCAG CCCTGATGTG CCTCTCACCA TCATGAAAAG GAAACTGATG 960 AACACCAATG ATCTGGAGGA GTCCAGGCAG CTCACGGAGG AGATCCAGCG GCATCTGGAT 1020 TACGAGTATG CGTTGAGACA TTTGTACGTG CTGGTCAACC TTTGTGAGAA GCCGTATCCG 1080 CTTCACAGGA TAAAATTGTC CATGGACCAC GTGTGCCTTG GTCACTAC 1128 Sequence No . : 14 Sequence length: 519 Sequence type: Nucleic acid Strandedness: Double Topology: Linear Sequence kind: cDNA to mRNA Original source : Organism species: Homo sapiens Cell kind: Epidermoid carcinoma Cell line: KB Clone name: HP10029 Sequence description ATGGCGGCGC CCAGCGGAGG GTGGAACGGC GTCCGCGCGA GCTTGTGGGC CGCGCTGCTC 60 CTAGGGGCCG TGGCGCTGAG GCCGGCGGAG GCGGTGTCCG AGCCCACGAC CGTGGCGTTT 120 GACGTGCGGC CCGGCGGCGT CGTGCATTCC TTCTCCCATA ACGTGGGCCC GGGGGACAAA 180 TATACGTGTA TGTTCACTTA CGCCTCTCAA GGAGGGACCA ATGAGCAATG GCAGATGAGT 240 CTGGGGACCA GCGAAGACCA CCAGCACTTC ACCTGCACCA TCTGGAGGCC CCAGGGGAAG 300 TCCTATCTGT ACTTCACACA GTTCAAGGCA GAGGTGCGGG GCGCTGAGAT TGAGTACGCC 360 ATGGCCTACT CTAAAGCCGC ATTTGAAAGG GAAAGTGATG TCCCTCTGAA AACTGAGGAA 420 TTTGAAGTGA CCAAAACAGC AGTGGCTCAC AGGCCCGGGG CATTCAAAGC TGAGCTGTCC 480 AAGCTGGTGA TTGTGGCCAA GGCATCGCGC ACTGAGCTG 519 Sequence No. : 15 Sequence length: 219 Sequence type: Nucleic acid Strandedness: Double Topology: Linear Sequence kind: cDNA to mRNA Original source: Organism species: Homo sapiens Cell kind: Epidermoid carcinoma Cell line: KB Clone name: HP10189 Sequence description ATGGGGGTGA AGCTGGAGAT ATTTCGGATG ATAATCTACC TCACTTTCCC TGTGGCTATG 60 TTCTGGGTTT CCAATCAGGC CGAGTGGTTT GAGGACGATG TCATACAGCG CAAGAGGGAG 120 CTGTGGCCAC CTGAGAAGCT TCAAGAGATA GAGGAATTCA AAGAGAGGTT ACGGAAGCGG 180 CGGGAGGAGA AGCTCCTTCG CGACGCCCAG CAGAACTCC 219 Sequence No.: 16 Sequence length: 3516 Sequence type: Nucleic acid Strandedness: Double Topology: Linear Sequence kind: cDNA to mRNA Original source: Organism species: Homo sapiens Cell kind: Lymphoma Cell line: U937 Clone name: HP10269 Sequence description ATGAGACCAT TCTTCCTCTT GTGTTTTGCC CTGCCTGGCC TCCTGCATGC CCAACAAGCC 60 TGCTCCCGTG GGGCCTGCTA TCCACCTGTT GGGGACCTGC TTGTTGGGAG GACCCGGTTT 120 CTCCGAGCTT CATCTACCTG TGGACTGACC AAGCCTGAGA CCTACTGCAC CCAGTATGGC 180 GAGTGGCAGA TGAAATGCTG CAAGTGTGAC TCCAGGCAGC CTCACAACTA CTACAGTCAC 240 CGAGTAGAGA ATGTGGCTTC ATCCTCCGGC CCCATGCGCT GGTGGCAGTC CCAGAATGAT 300 GTGAACCCTG TCTCTCTGCA GCTGGACCTG GACAGGAGAT TCCAGCTTCA AGAAGTCATG 360 ATGGAGTTCC AGGGGCCCAT GCCTGCCGGC ATGCTGATTG AGCGCTCCTC AGACTTCGGT 420 AAGACCTGGC GAGTGTACCA GTACCTGGCT GCCGACTGCA CCTCCACCTT CCCTCGGGTC 480 CGCCAGGGTC GGCCTCAGAG CTGGCAGGAT GTTCGGTGCC AGTCCCTGCC TCAGAGGCCT 540 AATGCACGCC TAAATGGGGG GAAGGTCCAA CTTAACCTTA TGGATTTAGT GTCTGGGATT 600 CCAGCAACTC AAAGTCAAAA AATTCAAGAG GTGGGGGAGA TCACAAACTT GAGAGTCAAT 660 TTCACCAGGC TGGCCCCTGT GCCCCAAAGG GGCTACCACC CTCCCAGCGC CTACTATGCT 720 GTGTCCCAGC TCCGTCTGCA GGGGAGCTGC TTCTGTCACG GCCATGCTGA TCGCTGCGCA 780 CCCAAGCCTG GGGCCTCTGC AGGCCCCTCC ACCGCTGTGC AGGTCCACGA TGTCTGTGTC 840 TGCCAGCACA ACACTGCCGG CCCAAATTGT GAGCGCTGTG CACCCTTCTA CAACAACCGG 900 CCCTGGAGAC CGGCGGAGGG CCAGGACGCC CATGAATGCC AAAGGTGCGA CTGCAATGGG 960 CACTCAGAGA CATGTCACTT TGACCCCGCT GTGTTTGCCG CCAGCCAGGG GGCATATGGA 1020 GGTGTGTGTG ACAATTGCCG GGACCACACC GAAGGCAAGA ACTGTGAGCG GTGTCAGCTG 1080 CACTATTTCC GGAACCGGCG CCCGGGAGCT TCCATTCAGG AGACCTGCAT CTCCTGCGAG 1140 TGTGATCCGG ATGGGGCAGT GCCAGGGGCT CCCTGTGACC CAGTGACCGG GCAGTGTGTG 1200 TGCAAGGAGC ATGTGCAGGG AGAGCGCTGT GACCTATGCA AGCCGGGCTT CACTGGACTC 1260 ACCTACGCCA ACCCGCAGGG CTGCCACCGC TGTGACTGCA ACATCCTGGG GTCCCGGAGG 1320 GACATGCCGT GTGACGAGGA GAGTGGGCGC TGCCTTTGTC TGCCCAACGT GGTGGGTCCC 1380 AAATGTGACC AGTGTGCTCC CTACCACTGG AAGCTGGCCA GTGGCCAGGG CTGTGAACCG 1440 TGTGCCTGCG ACCCGCACAA CTCCCTCAGC CCACAGTGCA ACCAGTTCAC AGGGCAGTGC 1500 CCCTGTCGGG AAGGCTTTGG TGGCCTGATG TGCAGCGCTG CAGCCATCCG CCAGTGTCCA 1560 GACCGGACCT ATGGAGACGT GGCCACAGGA TGCCGAGCCT GTGACTGTGA TTTCCGGGGA 1620 ACAGAGGGCC CGGGCTGCGA CAAGGCATCA GGCCGCTGCC TCTGCCGCCC TGGCTTGACC 1680 GGGCCCCGCT GTGACCAGTG CCAGCGAGGC TACTGCAATC GCTACCCGGT GTGCGTGGCC 1740 TGCCACCCTT GCTTCCAGAC CTATGATGCG GACCTCCGGG AGCAGGCCCT GCGCTTTGGT 1800 AGACTCCGCA ATGCCACCGC CAGCCTGTGG TCAGGGCCTG GGCTGGAGGA CCGTGGCCTG 1860 GCCTCCCGGA TCCTAGATGC AAAGAGTAAG ATTGAGCAGA TCCGAGCAGT TCTCAGCAGC 1920 CCCGCAGTCA CAGAGCAGGA GGTGGCTCAG GTGGCCAGTG CCATCCTCTC CCTCAGGCGA 1980 ACTCTCCAGG GCCTGCAGCT GGATCTGCCC CTGGAGGAGG AGACGTTGTC CCTTCCGAGA 2040 GACCTGGAGA GTCTTGACAG AAGCTTCAAT GGTCTCCTTA CTATGTATCA GAGGAAGAGG 2100 GAGCAGTTTG AAAAAATAAG CAGTGCTGAT CCTTCAGGAG CCTTCCGGAT GCTGAGCACA 2160 GCCTACGAGC AGTCAGCCCA GGCTGCTCAG CAGGTCTCCG ACAGCTCGCG CCTTTTGGAC 2220 CAGCTCAGGG ACAGCCGGAG AGAGGCAGAG AGGCTGGTGC GGCAGGCGGG AGGAGGAGGA 2280 GGCACCGGCA GCCCCAAGCT TGTGGCCCTG AGGCTGGAGA TGTCTTCGTT GCCTGACCTG 2340 ACACCCACCT TCAACAAGCT CTGTGGCAAC TCCAGGCAGA TGGCTTGCAC CCCAATATCA 2400 TGCCCTGGTG AGCTATGTCC CCAAGACAAT GGCACAGCCT GTGGCTCCCG CTGCAGGGGT 2460 GTCCTTCCCA GGGCCGGTGG GGCCTTCTTG ATGGCGGGGC AGGTGGCTGA GCAGCTGCGG 2520 GGCTTCAATG CCCAGCTCCA GCGGACCAGG CAGATGATTA GGGCAGCCGA GGAATCTGCC 2580 TCACAGATTC AATCCAGTGC CCAGCGCTTG GAGACCCAGG TGAGCGCCAG CCGCTCCCAG 2640 ATGGAGGAAG ATGTCAGACG CACACGGCTC CTAATCCAGC AGGTCCGGGA CTTCCTAACA 2700 GACCCCGACA CTGATGCAGC CACTATCCAG GAGGTCAGCG AGGCCGTGCT GGCCCTGTGG 2760 CTGCCCACAG ACTCAGCTAC TGTTCTGCAG AAGATGAATG AGATCCAGGC CATTGCAGCC 2820 AGGCTCCCCA ACGTGGACTT GGTGCTGTCC CAGACCAAGC AGGACATTGC GCGTGCCCGC 2880 CGGTTGCAGG CTGAGGCTGA GGAAGCCAGG AGCCGAGCCC ATGCAGTGGA GGGCCAGGTG 2940 GAAGATGTGG TTGGGAACCT GCGGCAGGGG ACAGTGGCAC TGCAGGAAGC TCAGGACACC 3000 ATGCAAGGCA CCAGCCGCTC CCTTCGGCTT ATCCAGGACA GGGTTGCTGA GGTTCAGCAG 3060 GTACTGCGGC CAGCAGAAAA GCTGGTGACA AGCATGACCA AGCAGCTGGG TGACTTCTGG 3120 ACACGGATGG AGGAGCTCCG CCACCAAGCC CGGCAGCAGG GGGCAGAGGC AGTCCAGGCC 3180 CAGCAGCTTG CGGAAGGTGC CAGCGAGCAG GCATTGAGTG CCCAAGAGGG ATTTGAGAGA 3240 ATAAAACAAA AGTATGCTGA GTTGAAGGAC CGGTTGGGTC AGAGTTCCAT GCTGGGTGAG 3300 CAGGGTGCCC GGATCCAGAG TGTGAAGACA GAGGCAGAGG AGCTGTTTGG GGAGACCATG 3360 GAGATGATGG ACAGGATGAA AGACATGGAG TTGGAGCTGC TGCGGGGCAG CCAGGCCATC 3420 ATGCTGCGCT CAGCGGACCT GACAGGACTG GAGAAGCGTG TGGAGCAGAT CCGTGACCAC 3480 ATCAATGGGC GCGTGCTCTA CTATGCCACC TGCAAG 3516 Sequence No . : 17 Sequence length: 366 Sequence type: Nucleic acid Strandedness: Double Topology: Linear Sequence kind: cDNA to mRNA Original source: Organism species: Homo sapiens Cell kind: Stomach cancer Clone name: HP10298 Sequence description ATGGGCCTGT TGCTCCTGGT CCCATTGCTC CTGCTGCCCG GCTCCTACGG ACTGCCCTTC 60 TACAACGGCT TCTACTACTC CAACAGCGCC AACGACCAGA ACCTAGGCAA CGGTCATGGC 120 AAAGACCTCC TTAATGGAGT GAAGCTGGTG GTGGAGACAC CCGAGGAGAC CCTGTTCACC 180 CGCATCCTAA CTGTGGGCCC CCAGAGCCTG GGGTCCGAAG CTTTGGCTTC CCCGACCCGC 240 AGAGCCGCTT GTACGGTGTT TACTGCTACC GCCAGCACTA GGACCTGGGG CCCTCCCCTG 300 CCGCATTCCC TCACTGGCTG TGTATTTATT GAGTGGTTCG TTTTCCCTTG TGGGTTGGAG 360 CCATTT 366 Sequence No. : 18 Sequence length: 525 Sequence type: Nucleic acid Strandedness: Double Topology: Linear Sequence kind: cDNA to mRNA Original source: Organism species: Homo sapiens Cell kind: Stomach cancer Clone name: HP10368 Sequence description ATGGAGAAAA TTCCAGTGTC AGCATTCTTG CTCCTTGTGG CCCTCTCCTA CACTCTGGCC 60 AGAGATACCA CAGTCAAACC TGGAGCCAAA AAGGACACAA AGGACTCTCG ACCCAAACTG 120 CCCCAGACCC TCTCCAGAGG TTGGGGTGAC CAACTCATCT GGACTCAGAC ATATGAAGAA 180 GCTCTATATA AATCCAAGAC AAGCAACAAA CCCTTGATGA TTATTCATCA CTTGGATGAG 240 TGCCCACACA GTCAAGCTTT AAAGAAAGTG TTTGCTGAAA ATAAAGAAAT CCAGAAATTG 300 GCAGAGCAGT TTGTCCTCCT CAATCTGGTT TATGAAACAA CTGACAAACA CCTTTCTCCT 360 GATGGCCAGT ATGTCCCCAG GATTATGTTT GTTGACCCAT CTCTGACAGT TAGAGCCGAT 420 ATCACTGGAA GATATTCAAA CCGTCTCTAT GCTTACGAAC CTGCAGATAC AGCTCTGTTG 480 CTTGACAACA TGAAGAAAGC TCTCAAGTTG CTGAAGACTG AATTG 525 Sequence No.: 19 Sequence length: 1296 Sequence type : Nucleic acid Strandedness: Double Topology: Linear Sequence kind: cDNA to mRNA Original source: Organism species : Homo sapiens Cell kind: Fibrosarcoma Cell line: HT-1080 Clone name: HP00658 Sequence characteristics: Code representing characteristics: CDS Existence site: 56.. 520 Characterization method: E Sequence description CCTGCAGAGG ATCAAGACAG CACGTGGACC TCGCACAGCC TCTCCCACAG GTACC ATG 58 Met 1 AAG GTC TCC GCG GCA GCC CTC GCT GTC ATC CTC ATT GCT ACT GCC CTC 106 Lys Val Ser Ala Ala Ala Leu Ala Val He Leu He Ala Thr Ala Leu 5 10 15 TGC GCT CCT GCA TCT GCC TCC CCA TAT TCC TCG GAC ACC ACA CCC TGC 154 Cys Ala Pro Ala Ser Ala Ser Pro Tyr Ser Ser Asp Thr Thr Pro Cys 20 25 30 TGC TTT GCC TAC ATT GCC CGC CCA CTG CCC CGT GCC CAC ATC AAG GAG 202 Cys Phe Ala Tyr He Ala Arg Pro Leu Pro Arg Ala His He Lys Glu 35 40 45 TAT TTC TAC ACC AGT GGC AAG TGC TCC AAC CCA GCA GTC GTC CAC AGG 250 Tyr Phe Tyr Thr Ser Gly Lys Cys Ser Asn Pro Ala Val Val His Arg 50 55 60 65 TCA AGG ATG CCA AAG AGA GAG GGA CAG CAA GTC TGG CAG GAT TTC CTG 298 Ser Arg Met Pro Lys Arg Glu Gly Gin Gin Val Trp Gin Asp Phe Leu 70 75 80 TAT GAC TCC CGG CTG AAC AAG GGC AAG CTT TGT CAC CCG AAA GAA CCG 346 Tyr Asp Ser Arg Leu Asn Lys Gly Lys Leu Cys His Pro Lys Glu Pro 85 90 95 CCA AGT GTG TGC CAA CCC AGA GAA GAA ATG GGT TCG GGA GTA CAT CAA 394 Pro Ser Val Cys Gin Pro Arg Glu Glu Met Gly Ser Gly Val His Gin 100 105 110 CTC TTT GGA GAT GAG CTA GGA TGG AGA GTC CTT GAA CCT GAA CTT ACA 442 Leu Phe Gly Asp Glu Leu Gly Trp Arg Val Leu Glu Pro Glu Leu Thr 115 120 125 CAA ATT TGC CTG TTT CTG CTT GCT CTT GTC CTA GCT TGG GAG GCT TCC 490 Gin He Cys Leu Phe Leu Leu Ala Leu Val Leu Ala Trp Glu Ala Ser 130 135 140 145 CCT CAC TAT CCT ACC CCA CCC GCT CCT TGAAGGGCCC AGA 530 Pro His Tyr Pro Thr Pro Pro Ala Pro 150 TTCTACCACA CAGCAGCAGT TACAAAAACC TTCCCCAGGC TGGACGTGGT GGCTCACGCC 590 TGTAATCCCA GCACTTTGGG AGGCCAAGGT GGGTGGATCA CTTGAGGTCA GGAGTTCGAG 650 ACCAGCCTGG CCAACATGAT GAAACCCCAT CTCTACTAAA AATACAAAAA ATTAGCCGGG 710 CGTGGTAGCG GGCGCCTGTA GTCCCAGCTA CTCGGGAGGC TGAGGCAGGA GAATGGCGTG 770 AACCCGGGAG GCGGAGCTTG CAGTGAGCCG AGATCGCGCC ACTGCACTCC AGCCTGGGCG 830 ACAGAGCGAG ACTCCGTCTC AAAAAAAAAA AAAAAAAAAA AAATACAAAA ATTAGCCGGG 890 CGTGGTGGCC CACGCCTGTA ATCCCAGCTA CTCGGGAGGC TAAGGCAGGA AAATTGTTTG 950 AACCCAGGAG GTGGAGGCTG CAGTGAGCTG AGATTGTGCC ACTTCACTCC AGCCTGGGTG 1010 ACAAAGTGAG ACTCCGTCAC AACAACAACA ACAAAAAGCT TCCCCAACTA AAGCCTAGAA 1070 GAGCTTCTGA GGCGCTGCTT TGTCAAAAGG AAGTCTCTAG GTTCTGAGCT CTGGCTTTGC 1130 CTTGGCTTTG CCAGGGCTCT GTGACCAGGA AGGAAGTCAG CATGCCTCTA GAGGCAAGGA 1190 GGGGAGGAAC GCTGCACTCT TAAGCTTCCG CCGTCTCAAC CCCTCACAGG AGCTTACTGG 1250 CAAACATGAA AAATCGGCTT ACCATTAAAG TTCTCAATGC AACCAT 1296 Sequence No. : 20 Sequence length: 3311 Sequence type: Nucleic acid Strandedness: Double Topology: Linear Sequence kind: cDNA to mRNA Original source: Organism species: Homo sapiens Cell kind: Epidermoid carcinoma Cell line: KB Clone name: HP00714 Sequence characteristics: Code representing characteristics: CDS Existence site: 57.. 1004 Characterization method: E Sequence description GAGCGGCGGC CACGGCATCC TGTGCTGTGG GGGCTACGAG GAAAGATCTA ATTATC ATG 59 Met 1 GAC CTG CGA CAG TTT CTT ATG TGC CTG TCC CTG TGC ACA GCC TTT GCC 107 Asp Leu Arg Gin Phe Leu Met Cys Leu Ser Leu Cys Thr Ala Phe Ala 5 10 15 TTG AGC AAA CCC ACA GAA AAG AAG GAC CGT GTA CAT CAT GAG CCT CAG 155 Leu Ser Lys Pro Thr Glu Lys Lys Asp Arg Val His His Glu Pro Gin 20 25 30 CTC AGT GAC AAG GTT CAC AAT GAT GCT CAG AGT TTT GAT TAT GAC CAT 203 Leu Ser Asp Lys Val His Asn Asp Ala Gin Ser Phe Asp Tyr Asp His 35 40 45 GAT GCC TTC TTG GGT GCT GAA GAA GCA AAG ACC TTT GAT CAG CTG ACA 251 Asp Ala Phe Leu Gly Ala Glu Glu Ala Lys Thr Phe Asp Gin Leu Thr 50 55 60 65 CCA GAA GAG AGC AAG GAA AGG CTT GGA AAG ATT GTA AGT AAA ATA GAT 299 Pro Glu Glu Ser Lys Glu Arg Leu Gly Lys He Val Ser Lys He Asp 70 75 80 GGC GAC AAG GAC GGG TTT GTC ACT GTG GAT GAG CTC AAA GAC TGG ATT 347 Gly Asp Lys Asp Gly Phe Val Thr Val Asp Glu Leu Lys Asp Trp He 85 90 95 AAA TTT GCA CAA AAG CGC TGG ATT TAC GAG GAT GTA GAG CGA CAG TGG 395 Lys Phe Ala Gin Lys Arg Trp He Tyr Glu Asp Val Glu Arg Gin Trp 100 105 110 AAG GGG CAT GAC CTC AAT GAG GAC GGC CTC GTT TCC TGG GAG GAG TAT 443 Lys Gly His Asp Leu Asn Glu Asp Gly Leu Val Ser Trp Glu Glu Tyr 115 120 125 AAA AAT GCC ACC TAC GGC TAC GTT TTA GAT GAT CCA GAT CCT GAT GAT 491 Lys Asn Ala Thr Tyr Gly Tyr Val Leu Asp Asp Pro Asp Pro Asp Asp 130 135 140 145 GGA TTT AAC TAT AAA CAG ATG ATG GTT AGA GAT GAG CGG AGG TTT AAA 539 Gly Phe Asn Tyr Lys Gin Met Met Val Arg Asp Glu Arg Arg Phe Lys 150 155 160 ATG GCA GAC AAG GAT GGA GAC CTC ATT GCC ACC AAG GAG GAG TTC ACA 587 Met Ala Asp Lys Asp Gly Asp Leu He Ala Thr Lys Glu Glu Phe Thr 165 170 175 GCT TTC CTG CAC CCT GAG GAG TAT GAC TAC ATG AAA GAT ATA GTA GTA 635 Ala Phe Leu His Pro Glu Glu Tyr Asp Tyr Met Lys Asp He Val Val 180 185 190 CAG GAA ACA ATG GAA GAT ATA GAT AAG AAT GCT GAT GGT TTC ATT GAT 683 Gin Glu Thr Met Glu Asp He Asp Lys Asn Ala Asp Gly Phe He Asp 195 200 205 CTA GAA GAG TAT ATT GGT GAC ATG TAC AGC CAT GAT GGG AAT ACT GAT 731 Leu Glu Glu Tyr He Gly Asp Met Tyr Ser His Asp Gly Asn Thr Asp 210 215 220 225 GAG CCA GAA TGG GTA AAG ACA GAG CGA GAG CAG TTT GTT GAG TTT CGG 779 Glu Pro Glu Trp Val Lys Thr Glu Arg Glu Gin Phe Val Glu Phe Arg 230 235 240 GAT AAG AAC CGT GAT GGG AAG ATG GAC AAG GAA GAG ACC AAA GAC TGG 827 Asp Lys Asn Arg Asp Gly Lys Met Asp Lys Glu Glu Thr Lys Asp Trp 245 250 255 ATC CTT CCC TCA GAC TAT GAT CAT GCA GAG GCA GAA GCC AGG CAC CTG 875 He Leu Pro Ser Asp Tyr Asp His Ala Glu Ala Glu Ala Arg His Leu 260 265 270 GTC TAT GAA TCA GAC CAA AAC AAG GAT GGC AAG CTT ACC AAG GAG GAG 923 Val Tyr Glu Ser Asp Gin Asn Lys Asp Gly Lys Leu Thr Lys Glu Glu 275 280 285 ATC GTT GAC AAG TAT GAC TTA TTT GTT GGC AGC CAG GCC ACA GAT TTT 971 He Val Asp Lys Tyr Asp Leu Phe Val Gly Ser Gin Ala Thr Asp Phe 290 295 300 305 GGG GAG GCC TTA GTA CGG CAT GAT GAG TTC TGAGCTACGG AGGAACCCT 1020 Gly Glu Ala Leu Val Arg His Asp Glu Phe 310 315 CATTTCCTCA AAAGTAATTT ATTTTTACAG CTTCTGGTTT CACATGAAAT TGTTTGCGCT 1080 ACTGAGACTG TTACTACAAA CTTTTTAAGA CATGAAAAGG CGTAATGAAA ACCATCCCGT 1140 CCCCATTCCT CCTCCTCTCT GAGGGACTGG AGGGAAGCCG TGCTTCTGAG GAACAACTCT 1200 AATTAGTACA CTTGTGTTTG TAGATTTACA CTTTGTATTA TGTATTAACA TGGCGTGTTT 1260 ATTTTTGTAT TTTTCTCTGG TTGGGAGTAT GATATGAAGG ATCAAGATCC TCAACTCACA 1320 CATGTAGACA AACATTAGCT CTTTACTCTT TCTCAACCCC TTTTATGATT TTAATAATTC 1380 TCACTTAACT AATTTTGTAA GCCTGAGATC AATAAGAAAT GTTCAGGAGA GAGGAAAGAA 1440 AAAAAATATA TGCTCCACAA TTTATATTTA GAGAGAGAAC ACTTAGTCTT GCCTGTCAAA 1500 AAGTCCAACA TTTCATAGGT AGTAGGGGCC ACATATTACA TTCAGTTGCT ATAGGTCCAG 1560 CAACTGAACC TGCCATTACC TGGGCAAGGA AAGATCCCTT TGCTCTAGGA AAGCTTGGCC 1620 CAAATTGATT TTCTTCTTTT TCCCCCTGTA GGACTGACTG TTGGCTAATT TTGTCAAGCA 1680 CAGCTGTGGT GGGAAGAGTT AGGGCCAGTG TCTTGAAAAT CAATCAAGTA GTGAATGTGA 1740 TCTCTTTGCA GAGCTATAGA TAGAAACAGC TGGAAAACTA AAGGAAAAAT ACAAGTGTTT 1800 TCGGGGCATA CATTTTTTTT CTGGGTGTGC ATCTGTTGAA ATGCTCAAGA CTTAATTATT 1860 TGCCTTTTGA AATCACTGTA AATGCCCCCA TCCGGTTCCT CTTCTTCCCA GGTGTGCCAA 1920 GGAATTAATC TTGGTTTCAC TACAATTAAA ATTCACTCCT TTCCAATCAT GTCATTGAAA 1980 GTGCCTTTAA CGAAAGAAAT GGTCACTGAA TGGGAATTCT CTTAAGAAAC CCTGAGATTA 2040 AAAAAAGACT ATTTGGATAA CTTATAGGAA AGCCTAGAAC CTCCCAGTAG AGTGGGGATT 2100 TTTTTCTTCT TCCCTTTCTC TTTTGGACAA TAGTTAAATT AGCAGTATTA GTTATGAGTT 2160 TGGTTGCAGT GTTCTTATCT TGTGGGCTGA TTTCCAAAAA CCACATGCTG CTGAATTTAC 2220 CAGGGATCCT CATACCTCAC AATGCAAACC ACTTACTACC AGGCCTTTTT CTGTGTCCAC 2280 TGGAGAGCTT GAGCTCACAC TCAAAGATCA GAGGACCTAC AGAGAGGGCT CTTTGGTTTG 2340 AGGACCATGG CTTACCTTTC CTGCCTTTGA CCCATCACAC CCCATTTCCT CCTCTTTCCC 2400 TCTCCCCGCT GCCAAAAAAA AAAAAAAAAG GAAACGTTTA TCATGAATCA ACAGGGTTTC 2460 AGTCCTTATC AAAGAGAGAT GTGGAAAGAG CTAAAGAAAC CACCCTTTGT TCCCAACTCC 2520 ACTTTACCCA TATTTTATGC AACACAAACA CTGTCCTTTT GGGTCCCTTT CTTACAGATG 2580 GACCTCTTGA GAAGAATTAT CGTATTCCAC GTTTTTAGCC CTCAGGTTAC CAAGATAAAT 2640 ATATGTATAT ATAACCTTTA TTATTGCTAT ATCTTTGTGG ATAATACATT CAGGTGGTGC 2700 TGGGTGATTT ATTATAATCT GAACCTAGGT ATATCCTTTG GTCTTCCACA GTCATGTTGA 2760 GGTGGGCTCC CTGGTATGGT AAAAAGCCAG GTATAATGTA ACTTCACCCC AGCCTTTGTA 2820 CTAAGCTCTT GATAGTGGAT ATACTCTTTT AAGTTTAGCC CCAATATAGG GTAATGGAAA 2880 TTTCCTGCCC TCTGGGTTCC CCATTTTTAC TATTAAGAAG ACCAGTGATA ATTTAATAAT 2940 GCCACCAACT CTGGCTTAGT TAAGTGAGAG TGTGAACTGT GTGGCAAGAG AGCCTCACAC 3000 CTCACTAGGT GCAGAGAGCC CAGGCCTTAT GTTAAAATCA TGCACTTGAA AAGCAAACCT 3060 TAATCTGCAA AGACAGCAGC AAGCATTATA CGGTCATCTT GAATGATCCC TTTGAAATTT 3120 TTTTTTTGTT TGTTTGTTTA AATCAAGCCT GAGGCTGGTG AACAGTAGCT ACACACCCAT 3180 ATTGTGTGTT CTGTGAATGC TAGCTTTCTT GAATTTGGAT ATTGGTTATT TTTTATAGAG 3240 TGTAAACCAA GTTTTATATT CTGCAATGCG AACAGGTACC TATCTGTTTC TAAATAAAAC 3300 TGTTTACATT C 3311 Sequence No. : 21 Sequence length: 1152 Sequence type : Nucleic acid Strandedness: Double Topology: Linear Sequence kind: cDNA to mRNA Original source: Organism species: Homo sapiens Cell kind: Stomach cancer Clone name: HP00876 Sequence characteristics: Code representing characteristics: CDS Existence site: 147.. 623 Characterization method: E Sequence description ACTGGAGACA CTGAAGAAGG CAGGGGCCCT TAGAGTCTTG GTTGCCAAAC AGATTTGCAG 60 ATCAAGGAGA ACCCAGGAGT TTCAAAGAAG CGCTAGTAAG GTCTCTGAGA TCCTTGCACT 120 AGCTACATCC TCAGGGTAGG AGGAAG ATG GCT TCC AGA AGC ATG CGG CTG CTC 173 Met Ala Ser Arg Ser Met Arg Leu Leu 1 5 CTA TTG CTG AGC TGC CTG GCC AAA ACA GGA GTC CTG GGT GAT ATC ATC 221 Leu Leu Leu Ser Cys Leu Ala Lys Thr Gly Val Leu Gly Asp He He 10 15 20 25 ATG AGA CCC AGC TGT GCT CCT GGA TGG TTT TAC CAC AAG TCC AAT TGC 269 Met Arg Pro Ser Cys Ala Pro Gly Trp Phe Tyr His Lys Ser Asn Cys 30 35 40 TAT GGT TAC TTC AGG AAG CTG AGG AAC TGG TCT GAT GCC GAG CTC GAG 317 Tyr Gly Tyr Phe Arg Lys Leu Arg Asn Trp Ser Asp Ala Glu Leu Glu 45 50 55 TGT CAG TCT TAC GGA AAC GGA GCC CAC CTG GCA TCT ATC CTG AGT TTA 365 Cys Gin Ser Tyr Gly Asn Gly Ala His Leu Ala Ser He Leu Ser Leu 60 65 70 AAG GAA GCC AGC ACC ATA GCA GAG TAC ATA AGT GGC TAT CAG AGA AGC 413 Lys Glu Ala Ser Thr He Ala Glu Tyr He Ser Gly Tyr Gin Arg Ser 75 80 85 CAG CCG ATA TGG ATT GGC CTG CAC GAC CCA CAG AAG AGG CAG CAG TGG 461 Gin Pro He Trp He Gly Leu His Asp Pro Gin Lys Arg Gin Gin Trp 90 95 100 105 CAG TGG ATT GAT GGG GCC ATG TAT CTG TAC AGA TCC TGG TCT GGC AAG 509 Gin Trp He Asp Gly Ala Met Tyr Leu Tyr Arg Ser Trp Ser Gly Lys 110 115 120 TCC ATG GGT GGG AAC AAG CAC TGT GCT GAG ATG AGC TCC AAT AAC AAC 557 Ser Met Gly Gly Asn Lys His Cys Ala Glu Met Ser Ser Asn Asn Asn 125 130 135 TTT TTA ACT TGG AGC AGC AAC GAA TGC AAC AAG CGC CAA CAC TTC CTG 605 Phe Leu Thr Trp Ser Ser Asn Glu Cys Asn Lys Arg Gin His Phe Leu 140 145 150 TGC AAG TAC CGA CCA TAGAGCAAGA ATCAAGATTC TGCTAACTCC 650 Cys Lys Tyr Arg Pro 155 TGCACAGCCC CGTCCTCTTC CTTTCTGCTA GCCTGGCTAA ATCTGCTCAT TATTTCAGAG 710 GGGAAACCTA GCAAACTAAG AGTGATAAGG GCCCTACTAC ACTGGCTTTT TTAGGCTTAG 770 AGACAGAAAC TTTAGCATTG GCCCAGTAGT GGCTTCTAGC TCTAAATGTT TGCCCCGCCA 830 TCCCTTTCCA CAGTATCCTT CTTCCCTCCT CCCCTGTCTC TGGCTGTCTC GAGCAGTCTA 890 GAAGAGTGCA TCTCCAGCCT ATGAAACAGC TGGGTCTTTG GCCATAAGAA GTAAAGATTT 950 GAAGACAGAA GGAAGAAACT CAGGAGTAAG CTTCTAGCCC CCTTCAGCTT CTACACCCTT 1010 CTGCCCTCTC TCCATTGCCT GCACCCCACC CCAGCCACTC AACTCCTGCT TGTTTTTCCT 1070 TTGGCCATGG GAAGGTTTAC CAGTAGAATC CTTGCTAGGT TGATGTGGGC CATACATTCC 1130 TTTAATAAAC CATTGTGTAC AT 1152 Sequence No. : 22 Sequence length: 1749 Sequence type: Nucleic acid Strandedness : Double Topology: Linear Sequence kind: cDNA to mRNA Original source: Organism species: Homo sapiens Cell kind: Liver Clone name: HP01134 Sequence characteristics: Code representing characteristics: CDS Existence site: 117.. 1247 Characterization method: E Sequence description AATCACAGCA GTNCCGACGT CGTGGGTGTT TGGTGTGAGG CTGCGAGCCG CCGCCGCCAC 60 CACTGCCACC ACGGTCGCCT GCCACAGGTG TCTGCAATTG AACTCCAAGG TGCAGA ATG 119 Met 1 GTT TGG AAA GTA GCT GTA TTC CTC AGT GTG GCC CTG GGC ATT GGT GCC 167 Val Trp Lys Val Ala Val Phe Leu Ser Val Ala Leu Gly He Gly Ala 5 10 15 GTT CCT ATA GAT GAT CCT GAA GAT GGA GGC AAG CAC TGG GTG GTG ATC 215 Val Pro He Asp Asp Pro Glu Asp Gly Gly Lys His Trp Val Val He 20 25 30 GTG GCA GGT TCA AAT GGC TGG TAT AAT TAT AGG CAC CAG GCA GAC GCG 263 Val Ala Gly Ser Asn Gly Trp Tyr Asn Tyr Arg His Gin Ala Asp Ala 35 40 45 TGC CAT GCC TAC CAG ATC ATT CAC CGC AAT GGG ATT CCT GAC GAA CAG 311 Cys His Ala Tyr Gin He He His Arg Asn Gly He Pro Asp Glu Gin 50 55 60 65 ATC GTT GTG ATG ATG TAC GAT GAC ATT GCT TAC TCT GAA GAC AAT CCC 359 He Val Val Met Met Tyr Asp Asp He Ala Tyr Ser Glu Asp Asn Pro 70 75 80 ACT CCA GGA ATT GTG ATC AAC AGG CCC AAT GGC ACA GAT GTC TAT CAG 407 Thr Pro Gly He Val He Asn Arg Pro Asn Gly Thr Asp Val Tyr Gin 85 90 95 GGA GTC CCG AAG GAC TAC ACT GGA GAG GAT GTT ACC CCA CAA AAT TTC 455 Gly Val Pro Lys Asp Tyr Thr Gly Glu Asp Val Thr Pro Gin Asn Phe 100 105 110 CTT GCT GTG TTG AGA GGC GAT GCA GAA GCA GTG AAG GGC ATA GGA TCC 503 Leu Ala Val Leu Arg Gly Asp Ala Glu Ala Val Lys Gly He Gly Ser 115 120 125 GGC AAA GTC CTG AAG AGT GGC CCC CAG GAT CAC GTG TTC ATT TAC TTC 551 Gly Lys Val Leu Lys Ser Gly Pro Gin Asp His Val Phe He Tyr Phe 130 135 140 145 ACT GAC CAT GGA TCT ACT GGA ATA CTG GTT TTT CCC AAT GAA GAT CTT 599 Thr Asp His Gly Ser Thr Gly He Leu Val Phe Pro Asn Glu Asp Leu 150 155 160 CAT GTA AAG GAC CTG AAT GAG ACC ATC CAT TAC ATG TAC AAA CAC AAA 647 His Val Lys Asp Leu Asn Glu Thr He His Tyr Met Tyr Lys His Lys 165 170 175 ATG TAC CGA AAG ATG GTG TTC TAC ATT GAA GCC TGT GAG TCT GGG TCC 695 Met Tyr Arg Lys Met Val Phe Tyr He Glu Ala Cys Glu Ser Gly Ser 180 185 190 ATG ATG AAC CAC CTG CCG GAT AAC ATC AAT GTT TAT GCA ACT ACT GCT 743 Met Met Asn His Leu Pro Asp Asn He Asn Val Tyr Ala Thr Thr Ala 195 200 205 GCC AAC CCC AGA GAG TCG TCC TAC GCC TGT TAC TAT GAT GAG AAG AGG 791 Ala Asn Pro Arg Glu Ser Ser Tyr Ala Cys Tyr Tyr Asp Glu Lys Arg 210 215 220 225 TCC ACG TAC CTG GGG GAC TGG TAC AGC GTC AAC TGG ATG GAA GAC TCG 839 Ser Thr Tyr Leu Gly Asp Trp Tyr Ser Val Asn Trp Met Glu Asp Ser 230 235 240 GAC GTG GAA GAT CTG ACT AAA GAG ACC CTG CAC AAG CAG TAC CAC CTG 887 Asp Val Glu Asp Leu Thr Lys Glu Thr Leu His Lys Gin Tyr His Leu 245 250 255 GTA AAA TCG CAC ACC AAC ACC AGC CAC GTC ATG CAG TAT GGA AAC AAA 935 Val Lys Ser His Thr Asn Thr Ser His Val Met Gin Tyr Gly Asn Lys 260 265 270 ACA ATC TCC ACC ATG AAA GTG ATG CAG TTT CAG GGT ATG AAA CGC AAA 983 Thr He Ser Thr Met Lys Val Met Gin Phe Gin Gly Met Lys Arg Lys 275 280 285 GCC AGT TCT CCC GTC CCC CTA CCT CCA GTC ACA CAC CTT GAC CTC ACC 1031 Ala Ser Ser Pro Val Pro Leu Pro Pro Val Thr His Leu Asp Leu Thr 290 295 300 305 CCC AGC CCT GAT GTG CCT CTC ACC ATC ATG AAA AGG AAA CTG ATG AAC 1079 Pro Ser Pro Asp Val Pro Leu Thr He Met Lys Arg Lys Leu Met Asn 310 315 320 ACC AAT GAT CTG GAG GAG TCC AGG CAG CTC ACG GAG GAG ATC CAG CGG 1127 Thr Asn Asp Leu Glu Glu Ser Arg Gin Leu Thr Glu Glu He Gin Arg 325 330 335 CAT CTG GAT TAC GAG TAT GCG TTG AGA CAT TTG TAC GTG CTG GTC AAC 1175 His Leu Asp Tyr Glu Tyr Ala Leu Arg His Leu Tyr Val Leu Val Asn 340 345 350 CTT TGT GAG AAG CCG TAT CCG CTT CAC AGG ATA AAA TTG TCC ATG GAC 1223 Leu Cys Glu Lys Pro Tyr Pro Leu His Arg He Lys Leu Ser Met Asp 355 360 365 CAC GTG TGC CTT GGT CAC TAC TGAAGAGCTG CCTCCTGGAA GCTTTT 1270 His Val Cys Leu Gly His Tyr 370 375 CCAAGTGTGA GCGCCCCACC GACTGTGTGC TGATCAGAGA CTGGAGAGGT GGAGTGAGAA 1330 GTCTCCGCTG CTCGGGCCCT CCTGGGGAGC CCCCGCTCCA GGGCTCGCTC CAGGACCTTC 1390 TTCACAAGAT GACTTGCTCG CTGTTACCTG CTTCCCCAGT CTTTTCTGAA AAACTACAAA 1450 TTAGGGTGGG AAAAGCTCTG TATTGAGAAG GGTCATATTT GCTTTCTAGG AGGTTTGTTG 1510 TTTTGCCTGT TAGTTTTGAG GAGCAGGAAG CTCATGGGGG CTTCTGTAGC CCCTCTCAAA 1570 AGGAGTCTTT ATTCTGAGAA TTTGAAGCTG AAACCTCTTT AAATCTTCAG AATGATTTTA 1630 TTGAAGAGGG CCGCAAGCCC CAAATGGAAA ACTGTTTTTA GAAAATATGA TGATTTTTGA 1690 TTGCTTTTGT ATTTAATTCT GCAGGTGTTC AAGTCTTAAA AAATAAAGAT TTATAACAG 1749 Sequence No.: 23 Sequence length: 988 Sequence type: Nucleic acid Strandedness: Double Topology: Linear Sequence kind: cDNA to mRNA Original source: Organism species: Homo sapiens Cell kind: Epidermoid carcinoma Cell line: KB Clone name: HP10029 Sequence characteristics: Code representing characteristics: CDS Existence site: 9.. 530 Characterization method: E Sequence description AGTCCAAC ATG GCG GCG CCC AGC GGA GGG TGG AAC GGC GTC CGC GCG AGC 50 Met Ala Ala Pro Ser Gly Gly Trp Asn Gly Val Arg Ala Ser 1 5 10 TTG TGG GCC GCG CTG CTC CTA GGG GCC GTG GCG CTG AGG CCG GCG GAG 98 Leu Trp Ala Ala Leu Leu Leu Gly Ala Val Ala Leu Arg Pro Ala Glu 15 20 25 30 GCG GTG TCC GAG CCC ACG ACC GTG GCG TTT GAC GTG CGG CCC GGC GGC 146 Ala Val Ser Glu Pro Thr Thr Val Ala Phe Asp Val Arg Pro Gly Gly 35 40 45 GTC GTG CAT TCC TTC TCC CAT AAC GTG GGC CCG GGG GAC AAA TAT ACG 194 Val Val His Ser Phe Ser His Asn Val Gly Pro Gly Asp Lys Tyr Thr 50 55 60 TGT ATG TTC ACT TAC GCC TCT CAA GGA GGG ACC AAT GAG CAA TGG CAG 242 Cys Met Phe Thr Tyr Ala Ser Gin Gly Gly Thr Asn Glu Gin Trp Gin 65 70 75 ATG AGT CTG GGG ACC AGC GAA GAC CAC CAG CAC TTC ACC TGC ACC ATC 290 Met Ser Leu Gly Thr Ser Glu Asp His Gin His Phe Thr Cys Thr He 80 85 90 TGG AGG CCC CAG GGG AAG TCC TAT CTG TAC TTC ACA CAG TTC AAG GCA 338 Trp Arg Pro Gin Gly Lys Ser Tyr Leu Tyr Phe Thr Gin Phe Lys Ala 95 100 105 110 GAG GTG CGG GGC GCT GAG ATT GAG TAC GCC ATG GCC TAC TCT AAA GCC 386 Glu Val Arg Gly Ala Glu He Glu Tyr Ala Met Ala Tyr Ser Lys Ala 115 120 125 GCA TTT GAA AGG GAA AGT GAT GTC CCT CTG AAA ACT GAG GAA TTT GAA 434 Ala Phe Glu Arg Glu Ser Asp Val Pro Leu Lys Thr Glu Glu Phe Glu 130 135 140 GTG ACC AAA ACA GCA GTG GCT CAC AGG CCC GGG GCA TTC AAA GCT GAG 482 Val Thr Lys Thr Ala Val Ala His Arg Pro Gly Ala Phe Lys Ala Glu 145 150 155 CTG TCC AAG CTG GTG ATT GTG GCC AAG GCA TCG CGC ACT GAG CTG 527 Leu Ser Lys Leu Val He Val Ala Lys Ala Ser Arg Thr Glu Leu 160 165 170 TGA CCAGCAGCCC TGTTGCGGGT GGCACCTTCT CATCTCCGGT GAAGCTGAAG 580 GGGCCTGTGG CCCTGAAAGG GCCAGCACAT CACTGGTTTT CTAGGAGGGA CTCTTAAGTT 640 TTCTACCTGG GCTGACGTTG CCTTGTCCGG AGGGGCTTGC AGGGTGGCTG AAGCCCTGGG 700 GCAGAGAACA GAGGGTCCAG GGCCCTCCTG GCTCCCAACA GCTTCTCAGT TCCCACTTCC 760 TGCTGAGCTC TTCTGGACTC AGGATCGCAG ATCCGGGGCA CAAAGAGGGT GGGGAACATG 820 GGGGCTATGC TGGGGAAAGC AGCCATGCTC CCCCCGACCT CCAGCCGAGC ATCCTTCATG 880 AGCCTGCAGA ACTGCTTTCC TATGTTTACC CAGGGGACCT CCTTTCAGAT GAACTGGGAA 940 GAGATGAAAT GTTTTTTCAT ATTTAAATAA ATAAGAACAT TAAAAAGC 988 Sequence No. : 24 Sequence length: 390 Sequence type : Nucleic acid Strandedness: Double Topology: Linear Sequence kind: cDNA to mRNA Original source : Organism species : Homo sapiens Cell kind: Epidermoid carcinoma Cell line: KB Clone name: HP10189 Sequence characteristics: Code representing characteristics : CDS Existence site: 102.. 323 Characterization method: E Sequence description AATCAGCTTC AGCAATGGAG CGTGCAAAAC ACCAGTGAGC TTCTGTCTTG CTGGAGGGTC 60 GGCTTTGGGC GGAACTGGCT TTGTTGACCG GGAGAAACGA G ATG GGG GTG AAG CTG 116 Met Gly Val Lys Leu 1 5 GAG ATA TTT CGG ATG ATA ATC TAC CTC ACT TTC CCT GTG GCT ATG TTC 164 Glu He Phe Arg Met He He Tyr Leu Thr Phe Pro Val Ala Met Phe 10 15 20 TGG GTT TCC AAT CAG GCC GAG TGG TTT GAG GAC GAT GTC ATA CAG CGC 212 Trp Val Ser Asn Gin Ala Glu Trp Phe Glu Asp Asp Val He Gin Arg 25 30 35 AAG AGG GAG CTG TGG CCA CCT GAG AAG CTT CAA GAG ATA GAG GAA TTC 260 Lys Arg Glu Leu Trp Pro Pro Glu Lys Leu Gin Glu He Glu Glu Phe 40 45 50 AAA GAG AGG TTA CGG AAG CGG CGG GAG GAG AAG CTC CTT CGC GAC GCC 308 Lys Glu Arg Leu Arg Lys Arg Arg Glu Glu Lys Leu Leu Arg Asp Ala 55 60 65 CAG CAG AAC TCC TGAGGCCTCC AAGTGGGAGT CCTAGCCCCT 350 Gin Gin Asn Ser 70 CCCCTGATGA AATATACATA TACTCAGTTC CTTGTTATTC 390 Sequence No. : 25 Sequence length: 4667 Sequence type: Nucleic acid Strandedness: Double Topology: Linear Sequence kind: cDNA to mRNA Original source: Organism species: Homo sapiens Cell kind: Lymphoma Cell line: U937 Clone name: HP10269 Sequence characteristics: Code representing characteristics: CDS Existence site: 754.. 4272 Characterization method: E Sequence description CATTTAGTTA CTCTGCTCAT TTCTCTTAAG CTTTCCTTGG ATGAGTTGAG CTTTGAATCC 60 TTCCTGATGA ACCTTGCCTT TTAAGGATCC TCCAAATGCC CCAAGAAGCT GGGATTTTTC 120 ATTTTTTTTT TCACTGGGGA GGGGAATGGT GCTTTCCAGG GTCCTGGATG TTTGAGTCTT 180 CTCACCTTCC AGCCCGGTGA TATGTCTGGA GCTTTAACTC TCTATATAAG CCCTAATCTT 240 TGTGTTCTCT GCCTGATCTT CTGTCTGGGG TGGTCCAGGT CACAAGAAGA AGCTGACCCC 300 TGCTGGCTTT GGGAAAATGC TGAGTTCATT GCCTGGCACA AATGCAAGGG CCCTTCCCCA 360 CCCTGTGAAT TCTGGTCTCT GATGATCACT TACATGTGCC TTGTGCTTTC TGTTTGAGGG 420 GCCCCTTGCA GCCCCCACAG GCAGGTGGGC ATTGTGGAGC TCACTACAAG AACTCTGGGA 480 CCGACCGACC AACCCACTTG CCCAGTCCCG TCCTGGGAGG TGGGGGTGCA GTGACGACAG 540 ATGGGTGTGA CGGCTGCCAG ATTCCTGAGA CCCGCCCTGC GGTGGGGCTA CACCCAGCCA 600 GGGAGTCTCC AGAGGTGAGG CTGTTGTTTA AAAACCTGGA GCCGGGAGGG GAGACCCCCA 660 CATTCAAGAG GAGCTTTCAG GCGATCTGGA GAAAGAACGG CAGAACACAC AGCAAGGAAA 720 GGTCCTTTCT GGGGATCACC CCATTGGCTG AAG ATG AGA CCA TTC TTC CTC TTG 774 Met Arg Pro Phe Phe Leu Leu 1 5 TGT TTT GCC CTG CCT GGC CTC CTG CAT GCC CAA CAA GCC TGC TCC CGT 822 Cys Phe Ala Leu Pro Gly Leu Leu His Ala Gin Gin Ala Cys Ser Arg 10 15 20 GGG GCC TGC TAT CCA CCT GTT GGG GAC CTG CTT GTT GGG AGG ACC CGG 870 Gly Ala Cys Tyr Pro Pro Val Gly Asp Leu Leu Val Gly Arg Thr Arg 25 30 35 TTT CTC CGA GCT TCA TCT ACC TGT GGA CTG ACC AAG CCT GAG ACC TAC 918 Phe Leu Arg Ala Ser Ser Thr Cys Gly Leu Thr Lys Pro Glu Thr Tyr 40 45 50 55 TGC ACC CAG TAT GGC GAG TGG CAG ATG AAA TGC TGC AAG TGT GAC TCC 966 Cys Thr Gin Tyr Gly Glu Trp Gin Met Lys Cys Cys Lys Cys Asp Ser 60 65 70 AGG CAG CCT CAC AAC TAC TAC AGT CAC CGA GTA GAG AAT GTG GCT TCA 1014 Arg Gin Pro His Asn Tyr Tyr Ser His Arg Val Glu Asn Val Ala Ser 75 80 85 TCC TCC GGC CCC ATG CGC TGG TGG CAG TCC CAG AAT GAT GTG AAC CCT 1062 Ser Ser Gly Pro Met Arg Trp Trp Gin Ser Gin Asn Asp Val Asn Pro 90 95 100 GTC TCT CTG CAG CTG GAC CTG GAC AGG AGA TTC CAG CTT CAA GAA GTC 1110 Val Ser Leu Gin Leu Asp Leu Asp Arg Arg Phe Gin Leu Gin Glu Val 105 110 115 ATG ATG GAG TTC CAG GGG CCC ATG CCT GCC GGC ATG CTG ATT GAG CGC 1158 Met Met Glu Phe Gin Gly Pro Met Pro Ala Gly Met Leu He Glu Arg 120 125 130 135 TCC TCA GAC TTC GGT AAG ACC TGG CGA GTG TAC CAG TAC CTG GCT GCC 1206 Ser Ser Asp Phe Gly Lys Thr Trp Arg Val Tyr Gin Tyr Leu Ala Ala 140 145 150 GAC TGC ACC TCC ACC TTC CCT CGG GTC CGC CAG GGT CGG CCT CAG AGC 1254 Asp Cys Thr Ser Thr Phe Pro Arg Val Arg Gin Gly Arg Pro Gin Ser 155 160 165 TGG CAG GAT GTT CGG TGC CAG TCC CTG CCT CAG AGG CCT AAT GCA CGC 1302 Trp Gin Asp Val Arg Cys Gin Ser Leu Pro Gin Arg Pro Asn Ala Arg 170 175 180 CTA AAT GGG GGG AAG GTC CAA CTT AAC CTT ATG GAT TTA GTG TCT GGG 1350 Leu Asn Gly Gly Lys Val Gin Leu Asn Leu Met Asp Leu Val Ser Gly 185 190 195 ATT CCA GCA ACT CAA AGT CAA AAA ATT CAA GAG GTG GGG GAG ATC ACA 1398 He Pro Ala Thr Gin Ser Gin Lys He Gin Glu Val Gly Glu He Thr 200 205 210 215 AAC TTG AGA GTC AAT TTC ACC AGG CTG GCC CCT GTG CCC CAA AGG GGC 1446 Asn Leu Arg Val Asn Phe Thr Arg Leu Ala Pro Val Pro Gin Arg Gly 220 225 230 TAC CAC CCT CCC AGC GCC TAC TAT GCT GTG TCC CAG CTC CGT CTG CAG 1494 Tyr His Pro Pro Ser Ala Tyr Tyr Ala Val Ser Gin Leu Arg Leu Gin 235 240 245 GGG AGC TGC TTC TGT CAC GGC CAT GCT GAT CGC TGC GCA CCC AAG CCT 1542 Gly Ser Cys Phe Cys His Gly His Ala Asp Arg Cys Ala Pro Lys Pro 250 255 260 GGG GCC TCT GCA GGC CCC TCC ACC GCT GTG CAG GTC CAC GAT GTC TGT 1590 Gly Ala Ser Ala Gly Pro Ser Thr Ala Val Gin Val His Asp Val Cys 265 270 275 GTC TGC CAG CAC AAC ACT GCC GGC CCA AAT TGT GAG CGC TGT GCA CCC 1638 Val Cys Gin His Asn Thr Ala Gly Pro Asn Cys Glu Arg Cys Ala Pro 280 285 290 295 TTC TAC AAC AAC CGG CCC TGG AGA CCG GCG GAG GGC CAG GAC GCC CAT 1686 Phe Tyr Asn Asn Arg Pro Trp Arg Pro Ala Glu Gly Gin Asp Ala His 300 305 310 GAA TGC CAA AGG TGC GAC TGC AAT GGG CAC TCA GAG ACA TGT CAC TTT 1734 Glu Cys Gin Arg Cys Asp Cys Asn Gly His Ser Glu Thr Cys His Phe 315 320 325 GAC CCC GCT GTG TTT GCC GCC AGC CAG GGG GCA TAT GGA GGT GTG TGT 1782 Asp Pro Ala Val Phe Ala Ala Ser Gin Gly Ala Tyr Gly Gly Val Cys 330 335 340 GAC AAT TGC CGG GAC CAC ACC GAA GGC AAG AAC TGT GAG CGG TGT CAG 1830 Asp Asn Cys Arg Asp His Thr Glu Gly Lys Asn Cys Glu Arg Cys Gin 345 350 355 CTG CAC TAT TTC CGG AAC CGG CGC CCG GGA GCT TCC ATT CAG GAG ACC 1878 Leu His Tyr Phe Arg Asn Arg Arg Pro Gly Ala Ser He Gin Glu Thr 360 365 370 375 TGC ATC TCC TGC GAG TGT GAT CCG GAT GGG GCA GTG CCA GGG GCT CCC 1926 Cys He Ser Cys Glu Cys Asp Pro Asp Gly Ala Val Pro Gly Ala Pro 380 385 390 TGT GAC CCA GTG ACC GGG CAG TGT GTG TGC AAG GAG CAT GTG CAG GGA 1974 Cys Asp Pro Val Thr Gly Gin Cys Val Cys Lys Glu His Val Gin Gly 395 400 405 GAG CGC TGT GAC CTA TGC AAG CCG GGC TTC ACT GGA CTC ACC TAC GCC 2022 Glu Arg Cys Asp Leu Cys Lys Pro Gly Phe Thr Gly Leu Thr Tyr Ala 410 415 420 AAC CCG CAG GGC TGC CAC CGC TGT GAC TGC AAC ATC CTG GGG TCC CGG 2070 Asn Pro Gin Gly Cys His Arg Cys Asp Cys Asn He Leu Gly Ser Arg 425 430 435 AGG GAC ATG CCG TGT GAC GAG GAG AGT GGG CGC TGC CTT TGT CTG CCC 2118 Arg Asp Met Pro Cys Asp Glu Glu Ser Gly Arg Cys Leu Cys Leu Pro 440 445 450 455 AAC GTG GTG GGT CCC AAA TGT GAC CAG TGT GCT CCC TAC CAC TGG AAG 2166 Asn Val Val Gly Pro Lys Cys Asp Gin Cys Ala Pro Tyr His Trp Lys 460 465 470 CTG GCC AGT GGC CAG GGC TGT GAA CCG TGT GCC TGC GAC CCG CAC AAC 2214 Leu Ala Ser Gly Gin Gly Cys Glu Pro Cys Ala Cys Asp Pro His Asn 475 480 485 TCC CTC AGC CCA CAG TGC AAC CAG TTC ACA GGG CAG TGC CCC TGT CGG 2262 Ser Leu Ser Pro Gin Cys Asn Gin Phe Thr Gly Gin Cys Pro Cys Arg 490 495 500 GAA GGC TTT GGT GGC CTG ATG TGC AGC GCT GCA GCC ATC CGC CAG TGT 2310 Glu Gly Phe Gly Gly Leu Met Cys Ser Ala Ala Ala He Arg Gin Cys 505 510 515 CCA GAC CGG ACC TAT GGA GAC GTG GCC ACA GGA TGC CGA GCC TGT GAC 2358 Pro Asp Arg Thr Tyr Gly Asp Val Ala Thr Gly Cys Arg Ala Cys Asp 520 525 530 535 TGT GAT TTC CGG GGA ACA GAG GGC CCG GGC TGC GAC AAG GCA TCA GGC 2406 Cys Asp Phe Arg Gly Thr Glu Gly Pro Gly Cys Asp Lys Ala Ser Gly 540 545 550 CGC TGC CTC TGC CGC CCT GGC TTG ACC GGG CCC CGC TGT GAC CAG TGC 2454 Arg Cys Leu Cys Arg Pro Gly Leu Thr Gly Pro Arg Cys Asp Gin Cys 555 560 565 CAG CGA GGC TAC TGC AAT CGC TAC CCG GTG TGC GTG GCC TGC CAC CCT 2502 Gin Arg Gly Tyr Cys Asn Arg Tyr Pro Val Cys Val Ala Cys His Pro 570 575 580 TGC TTC CAG ACC TAT GAT GCG GAC CTC CGG GAG CAG GCC CTG CGC TTT 2550 Cys Phe Gin Thr Tyr Asp Ala Asp Leu Arg Glu Gin Ala Leu Arg Phe 585 590 595 GGT AGA CTC CGC AAT GCC ACC GCC AGC CTG TGG TCA GGG CCT GGG CTG 2598 Gly Arg Leu Arg Asn Ala Thr Ala Ser Leu Trp Ser Gly Pro Gly Leu 600 605 610 615 GAG GAC CGT GGC CTG GCC TCC CGG ATC CTA GAT GCA AAG AGT AAG ATT 2646 Glu Asp Arg Gly Leu Ala Ser Arg He Leu Asp Ala Lys Ser Lys He 620 625 630 GAG CAG ATC CGA GCA GTT CTC AGC AGC CCC GCA GTC ACA GAG CAG GAG 2694 Glu Gin He Arg Ala Val Leu Ser Ser Pro Ala Val Thr Glu Gin Glu 635 640 645 GTG GCT CAG GTG GCC AGT GCC ATC CTC TCC CTC AGG CGA ACT CTC CAG 2742 Val Ala Gin Val Ala Ser Ala He Leu Ser Leu Arg Arg Thr Leu Gin 650 655 660 GGC CTG CAG CTG GAT CTG CCC CTG GAG GAG GAG ACG TTG TCC CTT CCG 2790 Gly Leu Gin Leu Asp Leu Pro Leu Glu Glu Glu Thr Leu Ser Leu Pro 665 670 675 AGA GAC CTG GAG AGT CTT GAC AGA AGC TTC AAT GGT CTC CTT ACT ATG 2838 Arg Asp Leu Glu Ser Leu Asp Arg Ser Phe Asn Gly Leu Leu Thr Met 680 685 690 695 TAT CAG AGG AAG AGG GAG CAG TTT GAA AAA ATA AGC AGT GCT GAT CCT 2886 Tyr Gin Arg Lys Arg Glu Gin Phe Glu Lys He Ser Ser Ala Asp Pro 700 705 710 TCA GGA GCC TTC CGG ATG CTG AGC ACA GCC TAC GAG CAG TCA GCC CAG 2934 Ser Gly Ala Phe Arg Met Leu Ser Thr Ala Tyr Glu Gin Ser Ala Gin 715 720 725 GCT GCT CAG CAG GTC TCC GAC AGC TCG CGC CTT TTG GAC CAG CTC AGG 2982 Ala Ala Gin Gin Val Ser Asp Ser Ser Arg Leu Leu Asp Gin Leu Arg 730 735 740 GAC AGC CGG AGA GAG GCA GAG AGG CTG GTG CGG CAG GCG GGA GGA GGA 3030 Asp Ser Arg Arg Glu Ala Glu Arg Leu Val Arg Gin Ala Gly Gly Gly 745 750 755 GGA GGC ACC GGC AGC CCC AAG CTT GTG GCC CTG AGG CTG GAG ATG TCT 3078 Gly Gly Thr Gly Ser Pro Lys Leu Val Ala Leu Arg Leu Glu Met Ser 760 765 770 775 TCG TTG CCT GAC CTG ACA CCC ACC TTC AAC AAG CTC TGT GGC AAC TCC 3126 Ser Leu Pro Asp Leu Thr Pro Thr Phe Asn Lys Leu Cys Gly Asn Ser 780 785 790 AGG CAG ATG GCT TGC ACC CCA ATA TCA TGC CCT GGT GAG CTA TGT CCC 3174 Arg Gin Met Ala Cys Thr Pro He Ser Cys Pro Gly Glu Leu Cys Pro 795 800 805 CAA GAC AAT GGC ACA GCC TGT GGC TCC CGC TGC AGG GGT GTC CTT CCC 3222 Gin Asp Asn Gly Thr Ala Cys Gly Ser Arg Cys Arg Gly Val Leu Pro 810 815 820 AGG GCC GGT GGG GCC TTC TTG ATG GCG GGG CAG GTG GCT GAG CAG CTG 3270 Arg Ala Gly Gly Ala Phe Leu Met Ala Gly Gin Val Ala Glu Gin Leu 825 830 835 CGG GGC TTC AAT GCC CAG CTC CAG CGG ACC AGG CAG ATG ATT AGG GCA 3318 Arg Gly Phe Asn Ala Gin Leu Gin Arg Thr Arg Gin Met He Arg Ala 840 845 850 855 GCC GAG GAA TCT GCC TCA CAG ATT CAA TCC AGT GCC CAG CGC TTG GAG 3366 Ala Glu Glu Ser Ala Ser Gin He Gin Ser Ser Ala Gin Arg Leu Glu 860 865 870 ACC CAG GTG AGC GCC AGC CGC TCC CAG ATG GAG GAA GAT GTC AGA CGC 3414 Thr Gin Val Ser Ala Ser Arg Ser Gin Met Glu Glu Asp Val Arg Arg 875 880 885 ACA CGG CTC CTA ATC CAG CAG GTC CGG GAC TTC CTA ACA GAC CCC GAC 3462 Thr Arg Leu Leu He Gin Gin Val Arg Asp Phe Leu Thr Asp Pro Asp 890 895 900 ACT GAT GCA GCC ACT ATC CAG GAG GTC AGC GAG GCC GTG CTG GCC CTG 3510 Thr Asp Ala Ala Thr He Gin Glu Val Ser Glu Ala Val Leu Ala Leu 905 910 915 TGG CTG CCC ACA GAC TCA GCT ACT GTT CTG CAG AAG ATG AAT GAG ATC 3558 Trp Leu Pro Thr Asp Ser Ala Thr Val Leu Gin Lys Met Asn Glu He 920 925 930 935 CAG GCC ATT GCA GCC AGG CTC CCC AAC GTG GAC TTG GTG CTG TCC CAG 3606 Gin Ala He Ala Ala Arg Leu Pro Asn Val Asp Leu Val Leu Ser Gin 940 945 950 ACC AAG CAG GAC ATT GCG CGT GCC CGC CGG TTG CAG GCT GAG GCT GAG 3654 Thr Lys Gin Asp He Ala Arg Ala Arg Arg Leu Gin Ala Glu Ala Glu 955 960 965 GAA GCC AGG AGC CGA GCC CAT GCA GTG GAG GGC CAG GTG GAA GAT GTG 3702 Glu Ala Arg Ser Arg Ala His Ala Val Glu Gly Gin Val Glu Asp Val 970 975 980 GTT GGG AAC CTG CGG CAG GGG ACA GTG GCA CTG CAG GAA GCT CAG GAC 3750 Val Gly Asn Leu Arg Gin Gly Thr Val Ala Leu Gin Glu Ala Gin Asp 985 990 995 ACC ATG CAA GGC ACC AGC CGC TCC CTT CGG CTT ATC CAG GAC AGG GTT 3798 Thr Met Gin Gly Thr Ser Arg Ser Leu Arg Leu He Gin Asp Arg Val 1000 1005 1010 1015 GCT GAG GTT CAG CAG GTA CTG CGG CCA GCA GAA AAG CTG GTG ACA AGC 3846 Ala Glu Val Gin Gin Val Leu Arg Pro Ala Glu Lys Leu Val Thr Ser 1020 1025 1030 ATG ACC AAG CAG CTG GGT GAC TTC TGG ACA CGG ATG GAG GAG CTC CGC 3894 Met Thr Lys Gin Leu Gly Asp Phe Trp Thr Arg Met Glu Glu Leu Arg 1035 1040 1045 CAC CAA GCC CGG CAG CAG GGG GCA GAG GCA GTC CAG GCC CAG CAG CTT 3942 His Gin Ala Arg Gin Gin Gly Ala Glu Ala Val Gin Ala Gin Gin Leu 1050 1055 1060 GCG GAA GGT GCC AGC GAG CAG GCA TTG AGT GCC CAA GAG GGA TTT GAG 3990 Ala Glu Gly Ala Ser Glu Gin Ala Leu Ser Ala Gin Glu Gly Phe Glu 1065 1070 1075 AGA ATA AAA CAA AAG TAT GCT GAG TTG AAG GAC CGG TTG GGT CAG AGT 4038 Arg He Lys Gin Lys Tyr Ala Glu Leu Lys Asp Arg Leu Gly Gin Ser 1080 1085 1090 1095 TCC ATG CTG GGT GAG CAG GGT GCC CGG ATC CAG AGT GTG AAG ACA GAG 4086 Ser Met Leu Gly Glu Gin Gly Ala Arg He Gin Ser Val Lys Thr Glu 1100 1105 1110 GCA GAG GAG CTG TTT GGG GAG ACC ATG GAG ATG ATG GAC AGG ATG AAA 4134 Ala Glu Glu Leu Phe Gly Glu Thr Met Glu Met Met Asp Arg Met Lys 1115 1120 1125 GAC ATG GAG TTG GAG CTG CTG CGG GGC AGC CAG GCC ATC ATG CTG CGC 4182 Asp Met Glu Leu Glu Leu Leu Arg Gly Ser Gin Ala He Met Leu Arg 1130 1135 1140 TCA GCG GAC CTG ACA GGA CTG GAG AAG CGT GTG GAG CAG ATC CGT GAC 4230 Ser Ala Asp Leu Thr Gly Leu Glu Lys Arg Val Glu Gin He Arg Asp 1145 1150 1155 CAC ATC AAT GGG CGC GTG CTC TAC TAT GCC ACC TGC AAG T 4270 His He Asn Gly Arg Val Leu Tyr Tyr Ala Thr Cys Lys 1160 1165 1170 GATGCTACAG CTTCCAGCCC GTTGCCCCAC TCATCTGCCG CCTTTGCTTT TGGTTGGGGG 4330 CAGATTGGGT TGGAATGCTT TCCATCTCCA GGAGACTTTC ATGCAGCCTA AAGTACAGCC 4390 TGGACCACCC CTGGTGTGTA GCTAGTAAGA TTACCCTGAG CTGCAGCTGA GCCTGAGCCA 4450 ATGGGACAGT TACACTTGAC AGACAAAGAT GGTGGAGATT GGCATGCCAT TGAAACTAAG 4510 AGCTCTCAAG TCAAGGAAGC TGGGCTGGGC AGTATCCCCC GCCTTTAGTT CTCCACTGGG 4570 GAGGAATCCT GGACCAAGCA CAAAAACTTA ACAAAAGTGA TGTAAAAATG AAAAGCCAAA 4630 TAAAAATCTT TGGAAAAGAG CCTGGAGGTT CAACGAG 4667 Sequence No.: 26 Sequence length: 1086 Sequence type: Nucleic acid Strandedness: Double Topology: Linear Sequence kind: cDNA to mRNA Original source: Organism species: Homo sapiens Cell kind: Stomach cancer Clone name: HP10298 Sequence characteristics: Code representing characteristics: CDS Existence site: 138.. 506 Characterization method: E Sequence description TTTAATTTCC CCGAAATCAG ACTGCTGCCT TGGACCGGGA CAGCTCGCGG CCCCCGAGAG 60 CTCTAGCCGT CGAGGAGCTG CCTGGGGACG TTTGCCCTGG GGCCCCAGCC TGGCCCGGGT 120 CACCCTGGCA TGAGGAG ATG GGC CTG TTG CTC CTG GTC CCA TTG CTC CTG 170 Met Gly Leu Leu Leu Leu Val Pro Leu Leu Leu 1 5 10 CTG CCC GGC TCC TAC GGA CTG CCC TTC TAC AAC GGC TTC TAC TAC TCC 218 Leu Pro Gly Ser Tyr Gly Leu Pro Phe Tyr Asn Gly Phe Tyr Tyr Ser 15 20 25 AAC AGC GCC AAC GAC CAG AAC CTA GGC AAC GGT CAT GGC AAA GAC CTC 266 Asn Ser Ala Asn Asp Gin Asn Leu Gly Asn Gly His Gly Lys Asp Leu 30 35 40 CTT AAT GGA GTG AAG CTG GTG GTG GAG ACA CCC GAG GAG ACC CTG TTC 314 Leu Asn Gly Val Lys Leu Val Val Glu Thr Pro Glu Glu Thr Leu Phe 45 50 55 ACC CGC ATC CTA ACT GTG GGC CCC CAG AGC CTG GGG TCC GAA GCT TTG 362 Thr Arg He Leu Thr Val Gly Pro Gin Ser Leu Gly Ser Glu Ala Leu 60 65 70 75 GCT TCC CCG ACC CGC AGA GCC GCT TGT ACG GTG TTT ACT GCT ACC GCC 410 Ala Ser Pro Thr Arg Arg Ala Ala Cys Thr Val Phe Thr Ala Thr Ala 80 85 90 AGC ACT AGG ACC TGG GGC CCT CCC CTG CCG CAT TCC CTC ACT GGC TGT 458 Ser Thr Arg Thr Trp Gly Pro Pro Leu Pro His Ser Leu Thr Gly Cys 95 100 105 GTA TTT ATT GAG TGG TTC GTT TTC CCT TGT GGG TTG GAG CCA TTT 503 Val Phe He Glu Trp Phe Val Phe Pro Cys Gly Leu Glu Pro Phe 110 115 120 TAACTGT TTTTATACTT CTCAATTTAA ATTTTCTTTA AACATTTTTT TACTATTTTT 560 TGTAAAGCAA ACAGAACCCA ATGCCTCCCT TTGCTCCTGG ATGCCCCACT CCAGGAATCA 620 TGCTTGCTCC CCTGGGCCAT TTGCGGTTTT GTGGGCTTCT GGAGGGTTCC CCGCCATCCA 680 GGCTGGTCTC CCTCCCTTAA GGAGGTTGGT GCCCAGAGTG GGCGGTGGCC TGTCTAGAAT 740 GCCGCCGGGA GTCCGGGCAT GGTGGGCACA GTTCTCCCTG CCCCTCAGCC TGGGGGAAGA 800 AGAGGGCCTC GGGGGCCTCC GGAGCTGGGC TTTGGGCCTC TCCTGCCCAC CTCTACTTCT 860 CTGTGAAGCC GCTGACCCCA GTCTGCCCAC TGAGGGGCTA GGGCTGGAAG CCAGTTCTAG 920 GCTTCCAGGC GAAAGCTGAG GGAAGGAAGA AACTCCCCTC CCCGTTCCCC TTCCCCTCTC 980 GGTTCCAAAG AATCTGTTTT GTTGTCATTT GTTTCTCCTG TTTCCCTGTG TGGGGAGGGG 1040 CCCTCAGGTG TGTGTACTTT GGACAATAAA TGGTGCTATG ACTGCC 1086 Sequence No. : 27 Sequence length: 866 Sequence type : Nucleic acid Strandedness: Double Topology: Linear Sequence kind: cDNA to mRNA Original source: Organism species: Homo sapiens Cell kind: Stomach cancer Clone name: HP10368 Sequence characteristics: Code representing characteristics: CDS Existence site: 73.. 600 Characterization method: E Sequence description ACTCAGAAGC TTGGACCGCA TCCTAGCCGC CGACTCACAC AAGGCAGGTG GGTGAGGAAA 60 TCCAGAGTTG CC ATG GAG AAA ATT CCA GTG TCA GCA TTC TTG CTC CTT GTG 111 Met Glu Lys He Pro Val Ser Ala Phe Leu Leu Leu Val 1 5 10 GCC CTC TCC TAC ACT CTG GCC AGA GAT ACC ACA GTC AAA CCT GGA GCC 159 Ala Leu Ser Tyr Thr Leu Ala Arg Asp Thr Thr Val Lys Pro Gly Ala 15 20 25 AAA AAG GAC ACA AAG GAC TCT CGA CCC AAA CTG CCC CAG ACC CTC TCC 207 Lys Lys Asp Thr Lys Asp Ser Arg Pro Lys Leu Pro Gin Thr Leu Ser 30 35 40 45 AGA GGT TGG GGT GAC CAA CTC ATC TGG ACT CAG ACA TAT GAA GAA GCT 255 Arg Gly Trp Gly Asp Gin Leu He Trp Thr Gin Thr Tyr Glu Glu Ala 50 55 60 CTA TAT AAA TCC AAG ACA AGC AAC AAA CCC TTG ATG ATT ATT CAT CAC 303 Leu Tyr Lys Ser Lys Thr Ser Asn Lys Pro Leu Met He He His His 65 70 75 TTG GAT GAG TGC CCA CAC AGT CAA GCT TTA AAG AAA GTG TTT GCT GAA 351 Leu Asp Glu Cys Pro His Ser Gin Ala Leu Lys Lys Val Phe Ala Glu 80 85 90 AAT AAA GAA ATC CAG AAA TTG GCA GAG CAG TTT GTC CTC CTC AAT CTG 399 Asn Lys Glu He Gin Lys Leu Ala Glu Gin Phe Val Leu Leu Asn Leu 95 100 105 GTT TAT GAA ACA ACT GAC AAA CAC CTT TCT CCT GAT GGC CAG TAT GTC 447 Val Tyr Glu Thr Thr Asp Lys His Leu Ser Pro Asp Gly Gin Tyr Val 110 115 120 125 CCC AGG ATT ATG TTT GTT GAC CCA TCT CTG ACA GTT AGA GCC GAT ATC 495 Pro Arg He Met Phe Val Asp Pro Ser Leu Thr Val Arg Ala Asp He 130 135 140 ACT GGA AGA TAT TCA AAC CGT CTC TAT GCT TAC GAA CCT GCA GAT ACA 543 Thr Gly Arg Tyr Ser Asn Arg Leu Tyr Ala Tyr Glu Pro Ala Asp Thr 145 150 155 GCT CTG TTG CTT GAC AAC ATG AAG AAA GCT CTC AAG TTG CTG AAG ACT 591 Ala Leu Leu Leu Asp Asn Met Lys Lys Ala Leu Lys Leu Leu Lys Thr 160 165 170 GAA TTG TAAAGAAAAA AAATCTCCAA GCCCTTCTGT CTGTCAGGCC TTG 640 Glu Leu 175 AGACTTGAAA CCAGAAGAAG TGTGAGAAGA CTGGCTAGTG TGGAAGCATA GTGAACACAC 700 TGATTAGGTT ATGGTTTAAT GTTACAACAA CTATTTTTTA AGAAAAACAA GTTTTAGAAA 760 TTTGGTTTCA AGTGTACATG TGTGAAAACA ATATTGTATA CTACCATAGT GAGCCATGAT 820 TTTCTAAAAA AAAAAATAAA TGTTTTGGGG GTGTTCTGTT TTCTCC 866

Claims: Claims 1. Proteins containing any of the amino acid sequences represented by Sequence No . 1 to Sequence No . 9. 2. DNAs encoding any of the proteins as described in Claim 1. 3. cDNAs containing any of the base sequences represented by Sequence No. 10 to Sequence No. 18. 4. cDNAs described in Claim 3 which comprise any of the base sequences represented by Sequence No. 19 to Sequence No. 27.

Inventors: KATO SEISHI, KOBAYASHI MIDORI, SEKINE SHINGO, YAMAGUCHI TOMOKO, KATO, SEISHI, KOBAYASHI, MIDORI, SEKINE, SHINGO, YAMAGUCHI, TOMOKO
Applicants: KATO SEISHI, KOBAYASHI MIDORI, PROTEGENE INC, SAGAMI CHEM RES, SEKINE SHINGO, YAMAGUCHI TOMOKO, KATO, SEISHI, KOBAYASHI, MIDORI, PROTEGENE INC., SAGAMI CHEMICAL RESEARCH CENTER, SEKINE, SHINGO, YAMAGUCHI, TOMOKO
Application year: 1997
Main classification: C12N15
IPC codes: C07K14, C12N15