LOCUS hCD45_D2\( 308 aa 17-MAY-2003 DEFINITION protein tyrosine phosphatase, receptor type, C isoform 1 precursor; protein tyrosine phosphatase, receptor type, c polypeptide; leukocyte-common antigen; T200 glycoprotein; human homolog of severe combined immunodeficiency due to PTPRC deficiency; SCID due to PTPRC deficiency; CD45 antigen [Homo sapiens]. ACCESSION NP_002829 DBSOURCE REFSEQ: accession NM_002838.2 SOURCE Homo sapiens (human). ORGANISM Homo sapiens Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. REFERENCE 1 (residues 1 to 1304) AUTHORS Baldwin,T.A. and Ostergaard,H.L. TITLE The protein-tyrosine phosphatase CD45 reaches the cell surface via golgi-dependent and -independent pathways JOURNAL J. Biol. Chem. 277 (52), 50333-50340 (2002) MEDLINE 22384317 REMARK GeneRIF: reaches the cell surface via Golgi-dependent and -independent pathways REFERENCE 2 (residues 1 to 1304) AUTHORS Harashima,A., Suzuki,M., Okochi,A., Yamamoto,M., Matsuo,Y., Motoda,R., Yoshioka,T. and Orita,K. TITLE CD45 tyrosine phosphatase inhibits erythroid differentiation of umbilical cord blood CD34+ cells associated with selective inactivation of Lyn JOURNAL Blood 100 (13), 4440-4445 (2002) MEDLINE 22340750 REMARK GeneRIF: CD45 may play a pivotal role in erythropoiesis. CD45 tyrosine phosphatase inhibits erythroid differentiation of umbilical cord blood CD34+ cells associated with selective inactivation of Lyn. REFERENCE 3 (residues 1 to 1304) AUTHORS Blanchetot,C., Tertoolen,L.G., Overvoorde,J. and den Hertog,J. TITLE Intra- and intermolecular interactions between intracellular domains of receptor protein-tyrosine phosphatases JOURNAL J. Biol. Chem. 277 (49), 47263-47269 (2002) MEDLINE 22344739 REMARK GeneRIF: interactions between RPTP-domain1s and RPTP-domain 2s are a common but specific mechanism that is likely to be regulated- domain2s and the wedge structures are crucial determinants of binding specificity, thus regulating cross-talk between RPTPs REFERENCE 4 (residues 1 to 1304) AUTHORS Pradhan,D. and Morrow,J. TITLE The spectrin-ankyrin skeleton controls CD45 surface display and interleukin-2 production JOURNAL Immunity 17 (3), 303-315 (2002) MEDLINE 22241694 REMARK GeneRIF: The spectrin-ankyrin skeleton controls CD45 surface display and interleukin-2 production. REFERENCE 5 (residues 1 to 1304) AUTHORS Ballerini,C., Rosati,E., Salvetti,M., Ristori,G., Cannoni,S., Biagioli,T., Massacesi,L., Sorbi,S. and Vergelli,M. TITLE Protein tyrosine phosphatase receptor-type C exon 4 gene mutation distribution in an Italian multiple sclerosis population JOURNAL Neurosci. Lett. 328 (3), 325-327 (2002) MEDLINE 22142931 REMARK GeneRIF: Role of the C-->G mutation in position 77 of exon 4 of the protein tyrosine phosphatase receptor-type C (PTPRC) gene, coding for the CD45 molecule, for the development of multiple sclerosis (MS) in Italy. REFERENCE 6 (residues 1 to 1304) AUTHORS Yamada,T., Zhu,D., Saxon,A. and Zhang,K. TITLE CD45 controls interleukin-4-mediated IgE class switch recombination in human B cells through its function as a Janus kinase phosphatase JOURNAL J. Biol. Chem. 277 (32), 28830-28835 (2002) MEDLINE 22151051 REMARK GeneRIF: CD45 controls interleukin-4-mediated IgE class switch recombination in human B cells REFERENCE 7 (residues 1 to 1304) AUTHORS Yu,C., Yu,H.S., Sun,K.H., Hsieh,S.C. and Tsai,C.Y. TITLE Anti-CD45 isoform antibodies enhance phagocytosis and gene expression of IL-8 and TNF-alpha in human neutrophils by differential suppression on protein tyrosine phosphorylation and p56lck tyrosine kinase JOURNAL Clin. Exp. Immunol. 129 (1), 78-85 (2002) MEDLINE 22095000 REMARK GeneRIF: Biological functions of membrane expressed CD45 isoforms on PMNs were studied. Cross-linking of CD45 isoforms by specific MAbs stimulated different PMN activities by differential suppression on protein tyrosine phosphorylation and p56lck. REFERENCE 8 (residues 1 to 1304) AUTHORS Jacobsen,M., Hoffmann,S., Cepok,S., Stei,S., Ziegler,A., Sommer,N. and Hemmer,B. TITLE A novel mutation in PTPRC interferes with splicing and alters the structure of the human CD45 molecule JOURNAL Immunogenetics 54 (3), 158-163 (2002) MEDLINE 22067726 REMARK GeneRIF: a mutation in PTPRC interferes with splicing and alters the structure of the CD45 molecule REFERENCE 9 (residues 1 to 1304) AUTHORS Tchilian,E.Z. and Beverley,P.C. TITLE CD45 in memory and disease JOURNAL Arch. Immunol. Ther. Exp. (Warsz.) 50 (2), 85-93 (2002) MEDLINE 22017393 REMARK GeneRIF: Role of high and low molecular weight isoforms of CD45 in the function of na##ve and memory T lymphocytes. Review. REFERENCE 10 (residues 1 to 1304) AUTHORS Fajka-Boja,R., Szemes,M., Ion,G., Legradi,A., Caron,M. and Monostori,E. TITLE Receptor tyrosine phosphatase, CD45 binds galectin-1 but does not mediate its apoptotic signal in T cell lines JOURNAL Immunol. Lett. 82 (1-2), 149-154 (2002) MEDLINE 22003829 REMARK GeneRIF: Receptor tyrosine phosphatase, CD45 binds galectin-1 but does not mediate its apoptotic signal in Jurkat cells REFERENCE 11 (residues 1 to 1304) AUTHORS Fukuhara,K., Okumura,M., Shiono,H., Inoue,M., Kadota,Y., Miyoshi,S. and Matsuda,H. TITLE A study on CD45 isoform expression during T-cell development and selection events in the human thymus JOURNAL Hum. Immunol. 63 (5), 394-404 (2002) MEDLINE 21972715 REMARK GeneRIF: analysis of CD45 isoform expression during T-cell development and selection in the human thymus REFERENCE 12 (residues 1 to 1304) AUTHORS Wu,L., Fu,J. and Shen,S.H. TITLE SKAP55 coupled with CD45 positively regulates T-cell receptor-mediated gene transcription JOURNAL Mol. Cell. Biol. 22 (8), 2673-2686 (2002) MEDLINE 21907230 REMARK GeneRIF: SKAP55 coupled with CD45 positively regulates T-cell receptor-mediated gene transcription. REFERENCE 13 (residues 1 to 1304) AUTHORS Ishikawa,H., Tsuyama,N., Abroun,S., Liu,S., Li,F.J., Taniguchi,O. and Kawano,M.M. TITLE Requirements of src family kinase activity associated with CD45 for myeloma cell proliferation by interleukin-6 JOURNAL Blood 99 (6), 2172-2178 (2002) MEDLINE 21866149 REMARK GeneRIF: Requirements of src family kinase activity associated with CD45 for myeloma cell proliferation by interleukin-6 REFERENCE 14 (residues 1 to 1304) AUTHORS Tchilian,E.Z., Dawes,R., Ramaley,P.A., Whitworth,J.A., Yuldasheva,N., Wells,R.S., Watera,C., French,N., Gilks,C.F., Kunachiwa,W., Ruzibakiev,R., Leetrakool,N., Carrington,C.V., Ramdath,D.D., Gotch,F., Stephens,H.A., Hill,A.V. and Beverley,P.C. TITLE A CD45 polymorphism associated with abnormal splicing is absent in African populations JOURNAL Immunogenetics 53 (10-11), 980-983 (2002) MEDLINE 21850514 REMARK GeneRIF: we examined the frequency of the C77G allele in African and Asian populations from countries with high or low prevalence of HIV infection; Here we report that the variant CD45 C77G allele is absent in African populations REFERENCE 15 (residues 1 to 1304) AUTHORS Wood,J.P., Bieda,K., Segni,M., Herwig,J., Krause,M., Usadel,K.H. and Badenhoop,K. TITLE CD45 exon 4 point mutation does not confer susceptibility to type 1 diabetes mellitus or Graves' disease JOURNAL Eur. J. Immunogenet. 29 (1), 73-74 (2002) MEDLINE 21830605 REMARK GeneRIF: CD45 variant (C77G, exon 4) does not confer susceptibility to either IDDM or Graves' disease REFERENCE 16 (residues 1 to 1304) AUTHORS Moro,H., Iwai,K., Mori,N., Watanabe,M., Fukushi,M., Oie,M., Arai,M., Tanaka,Y., Miyawaki,T., Gejyo,F., Arakawa,M. and Fujii,M. TITLE Interleukin-2-dependent but not independent T-cell lines infected with human T-cell leukemia virus type 1 selectively express CD45RO, a marker for persistent infection in vivo JOURNAL Virus Genes 23 (3), 263-271 (2001) MEDLINE 21636965 REMARK GeneRIF: role of CD45RO in the persistent HTLV-1 infection in vivo REFERENCE 17 (residues 1 to 1304) AUTHORS Irie-Sasaki,J., Sasaki,T., Matsumoto,W., Opavsky,A., Cheng,M., Welstead,G., Griffiths,E., Krawczyk,C., Richardson,C.D., Aitken,K., Iscove,N., Koretzky,G., Johnson,P., Liu,P., Rothstein,D.M. and Penninger,J.M. TITLE CD45 is a JAK phosphatase and negatively regulates cytokine receptor signalling JOURNAL Nature 409 (6818), 349-354 (2001) MEDLINE 21069057 REFERENCE 18 (residues 1 to 1304) AUTHORS Goff,L.K., van Soest,S., Timon,M., Tchilian,E. and Beverley,P.C. TITLE Protein tyrosine phosphatase receptor type C polypeptide (PTPRC) on human chromosome band 1q31-->q32 localizes with marker D1S413(1) on a 610-kb yeast artificial chromosome JOURNAL Cytogenet. Cell Genet. 87 (3-4), 223-224 (1999) MEDLINE 20169194 REFERENCE 19 (residues 1 to 1304) AUTHORS Petricoin,E.F. III, Ito,S., Williams,B.L., Audet,S., Stancato,L.F., Gamero,A., Clouse,K., Grimley,P., Weiss,A., Beeler,J., Finbloom,D.S., Shores,E.W., Abraham,R. and Larner,A.C. TITLE Antiproliferative action of interferon-alpha requires components of T-cell-receptor signalling JOURNAL Nature 390 (6660), 629-632 (1997) MEDLINE 98065953 REFERENCE 20 (residues 1 to 1304) AUTHORS Kaplan,R., Morse,B., Huebner,K., Croce,C., Howk,R., Ravera,M., Ricca,G., Jaye,M. and Schlessinger,J. TITLE Cloning of three human tyrosine phosphatases reveals a multigene family of receptor-linked protein-tyrosine-phosphatases expressed in brain JOURNAL Proc. Natl. Acad. Sci. U.S.A. 87 (18), 7000-7004 (1990) MEDLINE 90384936 REFERENCE 21 (residues 1 to 1304) AUTHORS Schraven,B., Samstag,Y., Altevogt,P. and Meuer,S.C. TITLE Association of CD2 and CD45 on human T lymphocytes JOURNAL Nature 345 (6270), 71-74 (1990) MEDLINE 90231464 REFERENCE 22 (residues 1 to 1304) AUTHORS Pingel,J.T. and Thomas,M.L. TITLE Evidence that the leukocyte-common antigen is required for antigen-induced T lymphocyte proliferation JOURNAL Cell 58 (6), 1055-1065 (1989) MEDLINE 89376557 REFERENCE 23 (residues 1 to 1304) AUTHORS Charbonneau,H., Tonks,N.K., Walsh,K.A. and Fischer,E.H. TITLE The leukocyte common antigen (CD45): a putative receptor-linked protein tyrosine phosphatase JOURNAL Proc. Natl. Acad. Sci. U.S.A. 85 (19), 7182-7186 (1988) MEDLINE 89017162 REFERENCE 24 (residues 1 to 1304) AUTHORS Streuli,M., Hall,L.R., Saga,Y., Schlossman,S.F. and Saito,H. TITLE Differential usage of three exons generates at least five different mRNAs encoding human leukocyte common antigens JOURNAL J. Exp. Med. 166 (5), 1548-1566 (1987) MEDLINE 88061067 REFERENCE 25 (residues 1 to 1304) AUTHORS Ralph,S.J., Thomas,M.L., Morton,C.C. and Trowbridge,I.S. TITLE Structural variants of human T200 glycoprotein (leukocyte-common antigen) JOURNAL EMBO J. 6 (5), 1251-1257 (1987) MEDLINE 87275816 COMMENT REVIEWED REFSEQ: This record has been curated by NCBI staff. The reference sequence was derived from Y00638.1 and Y00062.1. On Feb 8, 2002 this sequence version replaced gi:4506307. Summary: The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. This PTP contains an extracellular domain, a single transmembrane segment and two tandem intracytoplasmic catalytic domains, and thus belongs to receptor type PTP. This gene is specifically expressed in hematopoietic cells. This PTP has been shown to be an essential regulator of T- and B-cell antigen receptor signaling. It functions through either direct interaction with components of the antigen receptor complexes, or by activating various Src family kinases required for the antigen receptor signaling. This PTP also suppresses JAK kinases, and thus functions as a regulator of cytokine receptor signaling. Four alternatively spliced transcripts variants of this gene, which encode distinct isoforms, have been reported. Transcript Variant: This variant (1) encodes the longest isoform (1). COMMENT This file is created by Vector NTI suite COMMENT ORIGDB|GenPept COMMENT VNTDATE|302014800| COMMENT VNTNAME|hCD45_D2 (NP_002829) PTPRC| COMMENT VNTAUTHORNAME|Jannik N Andersen| COMMENT VNTAUTHOREML|jannik@noergaardandersen.com| COMMENT VNTAUTHORWWW|http://ptp.cshl.edu & http://science.novonordisk.com/ptp| COMMENT VNTOAUTHORNAME|NCBI Entrez| COMMENT VNTOAUTHORTEL|(301)496-2475| COMMENT VNTOAUTHORFAX|(301)480-9241| COMMENT VNTOAUTHOREML|info@ncbi.nlm.nih.gov| COMMENT VNTOAUTHORWWW|http://www3.ncbi.nlm.nih.gov/Entrez/| COMMENT VNTOAUTHORAD1|National Center for Biotechnology Information| COMMENT VNTOAUTHORAD2|National Library of Medicine| COMMENT VNTOAUTHORAD3|Building 38A, Room 8N805| COMMENT VNTOAUTHORAD4|Bethesda, MD 20894, U.S.A.| FEATURES Location/Qualifiers source 1..308 /organism="Homo sapiens" /db_xref="taxon:9606" /chromosome="1" /map="1q31-q32" /vntifkey="269" Protein 1..308 /product="protein tyrosine phosphatase, receptor type, C isoform 1 precursor" /EC_number="3.1.3.48" /vntifkey="270" /note="protein tyrosine phosphatase, receptor type, c polypeptide; leukocyte-common antigen; T200 glycoprotein; human homolog of severe combined immunodeficiency due to PTPRC deficiency; SCID due to PTPRC deficiency; CD45 antigen" Region 1..308 /product="protein tyrosine phosphatase, receptor type, C" /vntifkey="203" /label=Chain_1 Region 22..307 /region_name="Protein tyrosine phosphatase, catalytic domain" /db_xref="CDD:smart00194" /vntifkey="266" /label=Region_3 /note="PTPc" ORIGIN 1 selhpylhnm kkrdppseps pleaefqrlp syrswrtqhi gnqeenkskn rnsnvipydy 61 nrvplkhele mskesehdsd essdddsdse epskyinasf imsywkpevm iaaqgplket 121 igdfwqmifq rkvkvivmlt elkhgdqeic aqywgegkqt ygdievdlkd tdksstytlr 181 vfelrhskrk dsrtvyqyqy tnwsveqlpa epkelismiq vvkqklpqkn ssegnkhhks 241 tpllihcrdg sqqtgifcal lnllesaete evvdifqvvk alrkarpgmv stfeqyqfly 301 dviastyp // LOCUS hLAR_D2\(N 283 aa 17-MAY-2003 DEFINITION protein tyrosine phosphatase, receptor type, F isoform 1 precursor; protein tyrosine phosphatase, receptor type, F polypeptide; receptor-linked protein-tyrosine phosphatase LAR; leukocyte antigen-related tyrosine phosphatase; LCA-homolog [Homo sapiens]. ACCESSION NP_002831 DBSOURCE REFSEQ: accession NM_002840.2 SOURCE Homo sapiens (human). ORGANISM Homo sapiens Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. REFERENCE 1 (residues 1 to 1897) AUTHORS Blanchetot,C., Tertoolen,L.G., Overvoorde,J. and den Hertog,J. TITLE Intra- and intermolecular interactions between intracellular domains of receptor protein-tyrosine phosphatases JOURNAL J. Biol. Chem. 277 (49), 47263-47269 (2002) MEDLINE 22344739 REMARK GeneRIF: interactions between RPTP-domain1s and RPTP-domain 2s are a common but specific mechanism that is likely to be regulated- domain2s and the wedge structures are crucial determinants of binding specificity, thus regulating cross-talk between RPTPs REFERENCE 2 (residues 1 to 1897) AUTHORS Symons,J.R., LeVea,C.M. and Mooney,R.A. TITLE Expression of the leucocyte common antigen-related (LAR) tyrosine phosphatase is regulated by cell density through functional E-cadherin complexes JOURNAL Biochem. J. 365 (Pt 2), 513-519 (2002) MEDLINE 22090243 REMARK GeneRIF: regulation of expression by cell density through functional E-cadherin complexes REFERENCE 3 (residues 1 to 1897) AUTHORS Zabolotny,J.M., Kim,Y.B., Peroni,O.D., Kim,J.K., Pani,M.A., Boss,O., Klaman,L.D., Kamatkar,S., Shulman,G.I., Kahn,B.B. and Neel,B.G. TITLE Overexpression of the LAR (leukocyte antigen-related) protein-tyrosine phosphatase in muscle causes insulin resistance JOURNAL Proc. Natl. Acad. Sci. U.S.A. 98 (9), 5187-5192 (2001) MEDLINE 21221100 REFERENCE 4 (residues 1 to 1897) AUTHORS Muller,T., Choidas,A., Reichmann,E. and Ullrich,A. TITLE Phosphorylation and free pool of beta-catenin are regulated by tyrosine kinases and tyrosine phosphatases during epithelial cell migration JOURNAL J. Biol. Chem. 274 (15), 10173-10183 (1999) MEDLINE 99214576 REFERENCE 5 (residues 1 to 1897) AUTHORS Ahmad,F. and Goldstein,B.J. TITLE Functional association between the insulin receptor and the transmembrane protein-tyrosine phosphatase LAR in intact cells JOURNAL J. Biol. Chem. 272 (1), 448-457 (1997) MEDLINE 97150746 REFERENCE 6 (residues 1 to 1897) AUTHORS Harder,K.W., Saw,J., Miki,N. and Jirik,F. TITLE Coexisting amplifications of the chromosome 1p32 genes (PTPRF and MYCL1) encoding protein tyrosine phosphatase LAR and L-myc in a small cell lung cancer line JOURNAL Genomics 27 (3), 552-553 (1995) MEDLINE 96047346 REFERENCE 7 (residues 1 to 1897) AUTHORS Schaapveld,R.Q., van den Maagdenberg,A.M., Schepens,J.T., Weghuis,D.O., Geurts van Kessel,A., Wieringa,B. and Hendriks,W.J. TITLE The mouse gene Ptprf encoding the leukocyte common antigen-related molecule LAR: cloning, characterization, and chromosomal localization JOURNAL Genomics 27 (1), 124-130 (1995) MEDLINE 95394448 REFERENCE 8 (residues 1 to 1897) AUTHORS O'Grady,P., Krueger,N.X., Streuli,M. and Saito,H. TITLE Genomic organization of the human LAR protein tyrosine phosphatase gene and alternative splicing in the extracellular fibronectin type-III domains JOURNAL J. Biol. Chem. 269 (40), 25193-25199 (1994) MEDLINE 95014301 REFERENCE 9 (residues 1 to 1897) AUTHORS Streuli,M., Krueger,N.X., Hall,L.R., Schlossman,S.F. and Saito,H. TITLE A new member of the immunoglobulin superfamily that has a cytoplasmic region homologous to the leukocyte common antigen JOURNAL J. Exp. Med. 168 (5), 1523-1530 (1988) MEDLINE 89035978 COMMENT REVIEWED REFSEQ: This record has been curated by NCBI staff. The reference sequence was derived from Y00815.1 and BI711143.1. Summary: The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. This PTP possesses an extracellular region, a single transmembrane region, and two tandem intracytoplasmic catalytic domains, and thus represents a receptor-type PTP. The extracellular region contains three Ig-like domains, and nine non-Ig like domains similar to that of neural-cell adhesion molecule. This PTP was shown to function in the regulation of epithelial cell-cell contacts at adherents junctions, as well as in the control of beta-catenin signaling. An increased expression level of this protein was found in the insulin-responsive tissue of obese, insulin-resistant individuals, and may contribute to the pathogenesis of insulin resistance. Two alternatively spliced transcript variants of this gene, which encode distinct proteins, have been reported. Transcript Variant: This variant (1) contains an extra internal fragment within the coding region when compared to variant 2. It thus encodes a protein that has a 9 aa internal fragment absent in isoform 2. COMMENT This file is created by Vector NTI suite COMMENT ORIGDB|GenPept COMMENT VNTDATE|302014800| COMMENT VNTNAME|hLAR_D2 (NP_002831) PTPRF| COMMENT VNTAUTHORNAME|Jannik N Andersen| COMMENT VNTAUTHOREML|jannik@noergaardandersen.com| COMMENT VNTAUTHORWWW|http://ptp.cshl.edu & http://science.novonordisk.com/ptp| COMMENT VNTOAUTHORNAME|NCBI Entrez| COMMENT VNTOAUTHORTEL|(301)496-2475| COMMENT VNTOAUTHORFAX|(301)480-9241| COMMENT VNTOAUTHOREML|info@ncbi.nlm.nih.gov| COMMENT VNTOAUTHORWWW|http://www3.ncbi.nlm.nih.gov/Entrez/| COMMENT VNTOAUTHORAD1|National Center for Biotechnology Information| COMMENT VNTOAUTHORAD2|National Library of Medicine| COMMENT VNTOAUTHORAD3|Building 38A, Room 8N805| COMMENT VNTOAUTHORAD4|Bethesda, MD 20894, U.S.A.| FEATURES Location/Qualifiers source 1..283 /organism="Homo sapiens" /db_xref="taxon:9606" /chromosome="1" /map="1p34" /vntifkey="269" Protein 1..283 /product="protein tyrosine phosphatase, receptor type, F isoform 1 precursor" /EC_number="3.1.3.48" /vntifkey="270" /note="protein tyrosine phosphatase, receptor type, F polypeptide; receptor-linked protein-tyrosine phosphatase LAR; leukocyte antigen-related tyrosine phosphatase; LCA-homolog" Region 1..283 /product="protein tyrosine phosphatase, receptor type, F, isoform 1" /vntifkey="203" /label=Chain_1 Region 25..282 /region_name="Protein tyrosine phosphatase, catalytic domain" /db_xref="CDD:smart00194" /vntifkey="266" /label=Region_5 /note="PTPc" ORIGIN 1 rnlyahiqkl gqvppgesvt amelefklla sskahtsrfi sanlpcnkfk nrlvnimpye 61 ltrvclqpir gvegsdyina sfldgyrqqk ayiatqgpla estedfwrml wehnstiivm 121 ltklremgre kchqywpaer saryqyfvvd pmaeynmpqy ilrefkvtda rdgqsrtirq 181 fqftdwpeqg vpktgegfid figqvhktke qfgqdgpitv hcsagvgrtg vfitlsivle 241 rmryegvvdm fqtvktlrtq rpamvqtedq yqlcyraale ylg // LOCUS hPTPalpha_ 282 aa 17-MAY-2003 DEFINITION protein tyrosine phosphatase, receptor type, A isoform 1 precursor; protein tyrosine phosphatase, receptor type, alpha polypeptide; PTPase-alpha; Leukocyte common antigen-related peptide (protein tyrosine phosphate); tyrosine phosphatase alpha; PTPLCA-related phosphatase [Homo sapiens]. ACCESSION NP_002827 DBSOURCE REFSEQ: accession NM_002836.2 SOURCE Homo sapiens (human). ORGANISM Homo sapiens Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. REFERENCE 1 (residues 1 to 802) AUTHORS Blanchetot,C., Tertoolen,L.G., Overvoorde,J. and den Hertog,J. TITLE Intra- and intermolecular interactions between intracellular domains of receptor protein-tyrosine phosphatases JOURNAL J. Biol. Chem. 277 (49), 47263-47269 (2002) MEDLINE 22344739 REMARK GeneRIF: interactions between RPTP-domain1s and RPTP-domain 2s are a common but specific mechanism that is likely to be regulated- domain2s and the wedge structures are crucial determinants of binding specificity, thus regulating cross-talk between RPTPs REFERENCE 2 (residues 1 to 802) AUTHORS Mustelin,T. and Hunter,T. TITLE Meeting at mitosis: cell cycle-specific regulation of c-Src by RPTPalpha JOURNAL Sci STKE 2002 (115), PE3 (2002) MEDLINE 21655780 REMARK GeneRIF: In entering mitosis the cell cycle-specific regulation of c-Src by RPTPalpha can occur by dephosphorylation of phospho-Tyr527 that activates c-Src in a reaction catalyzed by the transmembrane receptor-like protein tyrosine phosphatase RPTPalpha. REFERENCE 3 (residues 1 to 802) AUTHORS Ardini,E., Agresti,R., Tagliabue,E., Greco,M., Aiello,P., Yang,L.T., Menard,S. and Sap,J. TITLE Expression of protein tyrosine phosphatase alpha (RPTPalpha) in human breast cancer correlates with low tumor grade, and inhibits tumor cell growth in vitro and in vivo JOURNAL Oncogene 19 (43), 4979-4987 (2000) MEDLINE 20499263 REFERENCE 4 (residues 1 to 802) AUTHORS Peters,G.H., Iversen,L.F., Branner,S., Andersen,H.S., Mortensen,S.B., Olsen,O.H., Moller,K.B. and Moller,N.P. TITLE Residue 259 is a key determinant of substrate specificity of protein-tyrosine phosphatases 1B and alpha JOURNAL J. Biol. Chem. 275 (24), 18201-18209 (2000) MEDLINE 20309769 REFERENCE 5 (residues 1 to 802) AUTHORS Harder,K.W., Moller,N.P., Peacock,J.W. and Jirik,F.R. TITLE Protein-tyrosine phosphatase alpha regulates Src family kinases and alters cell-substratum adhesion JOURNAL J. Biol. Chem. 273 (48), 31890-31900 (1998) MEDLINE 99041953 REFERENCE 6 (residues 1 to 802) AUTHORS Zheng,X.M., Wang,Y. and Pallen,C.J. TITLE Cell transformation and activation of pp60c-src by overexpression of a protein tyrosine phosphatase JOURNAL Nature 359 (6393), 336-339 (1992) MEDLINE 93024881 REFERENCE 7 (residues 1 to 802) AUTHORS Rao,V.V., Loffler,C., Sap,J., Schlessinger,J. and Hansmann,I. TITLE The gene for receptor-linked protein-tyrosine-phosphatase (PTPA) is assigned to human chromosome 20p12-pter by in situ hybridization (ISH and FISH) JOURNAL Genomics 13 (3), 906-907 (1992) MEDLINE 92347910 REFERENCE 8 (residues 1 to 802) AUTHORS Ohagi,S., Nishi,M. and Steiner,D.F. TITLE Sequence of a cDNA encoding human LRP (leukocyte common antigen-related peptide) JOURNAL Nucleic Acids Res. 18 (23), 7159 (1990) MEDLINE 91088320 REFERENCE 9 (residues 1 to 802) AUTHORS Jirik,F.R., Janzen,N.M., Melhado,I.G. and Harder,K.W. TITLE Cloning and chromosomal assignment of a widely expressed human receptor-like protein-tyrosine phosphatase JOURNAL FEBS Lett. 273 (1-2), 239-242 (1990) MEDLINE 91032191 REFERENCE 10 (residues 1 to 802) AUTHORS Krueger,N.X., Streuli,M. and Saito,H. TITLE Structural diversity and evolution of human receptor-like protein tyrosine phosphatases JOURNAL EMBO J. 9 (10), 3241-3252 (1990) MEDLINE 91006018 REFERENCE 11 (residues 1 to 802) AUTHORS Kaplan,R., Morse,B., Huebner,K., Croce,C., Howk,R., Ravera,M., Ricca,G., Jaye,M. and Schlessinger,J. TITLE Cloning of three human tyrosine phosphatases reveals a multigene family of receptor-linked protein-tyrosine-phosphatases expressed in brain JOURNAL Proc. Natl. Acad. Sci. U.S.A. 87 (18), 7000-7004 (1990) MEDLINE 90384936 REFERENCE 12 (residues 1 to 802) AUTHORS Sap,J., D'Eustachio,P., Givol,D. and Schlessinger,J. TITLE Cloning and expression of a widely expressed receptor tyrosine phosphatase JOURNAL Proc. Natl. Acad. Sci. U.S.A. 87 (16), 6112-6116 (1990) MEDLINE 90349565 COMMENT REVIEWED REFSEQ: This record has been curated by NCBI staff. The reference sequence was derived from M34668.1 and AI284972.1. Summary: The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. This PTP contains an extracellular domain, a single transmembrane segment and two tandem intracytoplasmic catalytic domains, and thus represents a receptor-type PTP. This PTP has been shown to dephosphorylate and activate Src family tyrosine kinases, and is implicated in the regulation of integrin signaling, cell adhesion and proliferation. Three alternatively spliced variants of this gene, which encode two distinct isoforms, have been reported. Transcript Variant: This variant (1) contains a unique 5' UTR region when compared to other variants. The genomic exons forming the 5' end region of this transcript are also used to form an internal coding region in the transcripts of VPS16, a distinct gene located at the locus immediately upstream of this gene on chromosome 20. This variant encodes the longest isoform (1). COMMENT This file is created by Vector NTI suite COMMENT ORIGDB|GenPept COMMENT VNTDATE|302014800| COMMENT VNTNAME|hPTPalpha_D2 (NP_002827) PTPRA| COMMENT VNTAUTHORNAME|Jannik N Andersen| COMMENT VNTAUTHOREML|jannik@noergaardandersen.com| COMMENT VNTAUTHORWWW|http://ptp.cshl.edu & http://science.novonordisk.com/ptp| COMMENT VNTOAUTHORNAME|NCBI Entrez| COMMENT VNTOAUTHORTEL|(301)496-2475| COMMENT VNTOAUTHORFAX|(301)480-9241| COMMENT VNTOAUTHOREML|info@ncbi.nlm.nih.gov| COMMENT VNTOAUTHORWWW|http://www3.ncbi.nlm.nih.gov/Entrez/| COMMENT VNTOAUTHORAD1|National Center for Biotechnology Information| COMMENT VNTOAUTHORAD2|National Library of Medicine| COMMENT VNTOAUTHORAD3|Building 38A, Room 8N805| COMMENT VNTOAUTHORAD4|Bethesda, MD 20894, U.S.A.| FEATURES Location/Qualifiers source 1..282 /organism="Homo sapiens" /db_xref="taxon:9606" /chromosome="20" /map="20p13" /vntifkey="269" Protein 1..282 /product="protein tyrosine phosphatase, receptor type, A isoform 1 precursor" /EC_number="3.1.3.48" /vntifkey="270" /note="protein tyrosine phosphatase, receptor type, alpha polypeptide; PTPase-alpha; Leukocyte common antigen-related peptide (protein tyrosine phosphate); tyrosine phosphatase alpha; PTPLCA-related phosphatase" Region 1..282 /product="protein tyrosine phosphatase, receptor type, A, isoform 1" /vntifkey="203" /label=Chain_1 Region 21..281 /region_name="Protein tyrosine phosphatase, catalytic domain" /db_xref="CDD:smart00194" /vntifkey="266" /label=Region_2 /note="PTPc" ORIGIN 1 tslethlqki ynkipgtsnn gleeefkklt sikiqndkmr tgnlpanmkk nrvlqiipye 61 fnrviipvkr geentdyvna sfidgyrqkd syiasqgpll htiedfwrmi wewkscsivm 121 lteleergqe kcaqywpsdg lvsygditve lkkeeecesy tvrdllvtnt renksrqirq 181 fhfhgwpevg ipsdgkgmis iiaavqkqqq qsgnhpitvh csagagrtgt fcalstvler 241 vkaegildvf qtvkslrlqr phmvqtleqy efcykvvqey id // LOCUS hPTPdelta_ 283 aa 17-MAY-2003 DEFINITION protein tyrosine phosphatase, receptor type, D isoform 1 precursor; protein tyrosine phosphatase, receptor type, delta polypeptide; protein tyrosine phosphatase delta [Homo sapiens]. ACCESSION NP_002830 DBSOURCE REFSEQ: accession NM_002839.1 SOURCE Homo sapiens (human). ORGANISM Homo sapiens Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. REFERENCE 1 (residues 1 to 1912) AUTHORS Blanchetot,C., Tertoolen,L.G., Overvoorde,J. and den Hertog,J. TITLE Intra- and intermolecular interactions between intracellular domains of receptor protein-tyrosine phosphatases JOURNAL J. Biol. Chem. 277 (49), 47263-47269 (2002) MEDLINE 22344739 REMARK GeneRIF: interactions between RPTP-domain1s and RPTP-domain 2s are a common but specific mechanism that is likely to be regulated- domain2s and the wedge structures are crucial determinants of binding specificity, thus regulating cross-talk between RPTPs REFERENCE 2 (residues 1 to 1912) AUTHORS Pulido,R., Serra-Pages,C., Tang,M. and Streuli,M. TITLE The LAR/PTP delta/PTP sigma subfamily of transmembrane protein-tyrosine-phosphatases: multiple human LAR, PTP delta, and PTP sigma isoforms are expressed in a tissue-specific manner and associate with the LAR-interacting protein LIP.1 JOURNAL Proc. Natl. Acad. Sci. U.S.A. 92 (25), 11686-11690 (1995) MEDLINE 96102179 REFERENCE 3 (residues 1 to 1912) AUTHORS Pulido,R., Krueger,N.X., Serra-Pages,C., Saito,H. and Streuli,M. TITLE Molecular characterization of the human transmembrane protein-tyrosine phosphatase delta. Evidence for tissue-specific expression of alternative human transmembrane protein-tyrosine phosphatase delta isoforms JOURNAL J. Biol. Chem. 270 (12), 6722-6728 (1995) MEDLINE 95204468 REFERENCE 4 (residues 1 to 1912) AUTHORS Krueger,N.X., Streuli,M. and Saito,H. TITLE Structural diversity and evolution of human receptor-like protein tyrosine phosphatases JOURNAL EMBO J. 9 (10), 3241-3252 (1990) MEDLINE 91006018 COMMENT REVIEWED REFSEQ: This record has been curated by NCBI staff. The reference sequence was derived from L38929.1. Summary: The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. This PTP contains an extracellular region, a single transmembrane segment and two tandem intracytoplasmic catalytic domains, thus represents a receptor-type PTP. The extracellular region of this protein is composed of three Ig-like and eight fibronectin type III-like domains. Studies of the similar genes in chick and fly suggest the role of this PTP is in promoting neurite growth, and regulating neurons axon guidance. Multiple tissue specific alternatively spliced transcript variants of this gene have been reported. Transcript Variant: This variant (1) encodes the longest isoform (1). COMMENT This file is created by Vector NTI suite COMMENT ORIGDB|GenPept COMMENT VNTDATE|302014800| COMMENT VNTNAME|hPTPdelta_D2 (NP_002830) PTPRD| COMMENT VNTAUTHORNAME|Jannik N Andersen| COMMENT VNTAUTHOREML|jannik@noergaardandersen.com| COMMENT VNTAUTHORWWW|http://ptp.cshl.edu & http://science.novonordisk.com/ptp| COMMENT VNTOAUTHORNAME|NCBI Entrez| COMMENT VNTOAUTHORTEL|(301)496-2475| COMMENT VNTOAUTHORFAX|(301)480-9241| COMMENT VNTOAUTHOREML|info@ncbi.nlm.nih.gov| COMMENT VNTOAUTHORWWW|http://www3.ncbi.nlm.nih.gov/Entrez/| COMMENT VNTOAUTHORAD1|National Center for Biotechnology Information| COMMENT VNTOAUTHORAD2|National Library of Medicine| COMMENT VNTOAUTHORAD3|Building 38A, Room 8N805| COMMENT VNTOAUTHORAD4|Bethesda, MD 20894, U.S.A.| FEATURES Location/Qualifiers source 1..283 /organism="Homo sapiens" /db_xref="taxon:9606" /chromosome="9" /map="9p23-p24.3" /vntifkey="269" Protein 1..283 /product="protein tyrosine phosphatase, receptor type, D isoform 1 precursor" /EC_number="3.1.3.48" /vntifkey="270" /note="protein tyrosine phosphatase, receptor type, delta polypeptide; protein tyrosine phosphatase delta" Region 1..283 /product="protein tyrosine phosphatase, receptor type, D, isoform 1" /vntifkey="203" /label=Chain_1 Region 21..282 /region_name="Protein tyrosine phosphatase, catalytic domain" /db_xref="CDD:smart00194" /vntifkey="266" /label=Region_5 /note="PTPc" ORIGIN 1 rnlyayiqkl tqietgenvt gmelefkrla sskahtsrfi sanlpcnkfk nrlvnimpye 61 strvclqpir gvegsdyina sfidgyrqqk ayiatqgpla ettedfwrml wehnstivvm 121 ltklremgre kchqywpaer saryqyfvvd pmaeynmpqy ilrefkvtda rdgqsrtvrq 181 fqftdwpeqg vpksgegfid figqvhktke qfgqdgpisv hcsagvgrtg vfitlsivle 241 rmryegvvdi fqtvkmlrtq rpamvqtedq yqfsyraale ylg // LOCUS hPTPepsilo 287 aa 17-MAY-2003 DEFINITION protein tyrosine phosphatase, receptor type, E isoform 1 precursor; protein tyrosine phosphatase, receptor type, epsilon; protein tyrosine phosphatase, receptor type, epsilon polypeptide; protein tyrosine phosphatase epsilon [Homo sapiens]. ACCESSION NP_006495 DBSOURCE REFSEQ: accession NM_006504.2 SOURCE Homo sapiens (human). ORGANISM Homo sapiens Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. REFERENCE 1 (residues 1 to 700) AUTHORS Blanchetot,C., Tertoolen,L.G., Overvoorde,J. and den Hertog,J. TITLE Intra- and intermolecular interactions between intracellular domains of receptor protein-tyrosine phosphatases JOURNAL J. Biol. Chem. 277 (49), 47263-47269 (2002) MEDLINE 22344739 REMARK GeneRIF: interactions between RPTP-domain1s and RPTP-domain 2s are a common but specific mechanism that is likely to be regulated- domain2s and the wedge structures are crucial determinants of binding specificity, thus regulating cross-talk between RPTPs REFERENCE 2 (residues 1 to 700) AUTHORS Wabakken,T., Hauge,H., Funderud,S. and Aasheim,H.C. TITLE Characterization, expression and functional aspects of a novel protein tyrosine phosphatase epsilon isoform JOURNAL Scand. J. Immunol. 56 (3), 276-285 (2002) MEDLINE 22181756 REMARK GeneRIF: Characterization, expression and functional aspects of an alternative spliced isoform of protein tyrosine phosphatase epsilon REFERENCE 3 (residues 1 to 700) AUTHORS Wabakken,T., Hauge,H., Finne,E.F., Wiedlocha,A. and Aasheim,H. TITLE Expression of human protein tyrosine phosphatase epsilon in leucocytes: a potential ERK pathway-regulating phosphatase JOURNAL Scand. J. Immunol. 56 (2), 195-203 (2002) MEDLINE 22118122 REMARK GeneRIF: Transfection of cells with different PTPepsilon constructs and activator protein-1 reporter gene indicates that the catalytic activity of PTPepsilon is involved in the regulation of the mitogen-activated protein kinase cascade. REFERENCE 4 (residues 1 to 700) AUTHORS Tanuma,N., Nakamura,K., Shima,H. and Kikuchi,K. TITLE Protein-tyrosine phosphatase PTPepsilon C inhibits Jak-STAT signaling and differentiation induced by interleukin-6 and leukemia inhibitory factor in M1 leukemia cells JOURNAL J. Biol. Chem. 275 (36), 28216-28221 (2000) MEDLINE 20428741 REMARK functional study of the mouse homolog REFERENCE 5 (residues 1 to 700) AUTHORS Peretz,A., Gil-Henn,H., Sobko,A., Shinder,V., Attali,B. and Elson,A. TITLE Hypomyelination and increased activity of voltage-gated K(+) channels in mice lacking protein tyrosine phosphatase epsilon JOURNAL EMBO J. 19 (15), 4036-4045 (2000) MEDLINE 20380937 REMARK functional study of the mouse homolog REFERENCE 6 (residues 1 to 700) AUTHORS Toledano-Katchalski,H. and Elson,A. TITLE The transmembranal and cytoplasmic forms of protein tyrosine phosphatase epsilon physically associate with the adaptor molecule Grb2 JOURNAL Oncogene 18 (36), 5024-5031 (1999) MEDLINE 99422037 REMARK functional study of the mouse homolog REFERENCE 7 (residues 1 to 700) AUTHORS Elson,A. and Leder,P. TITLE Identification of a cytoplasmic, phorbol ester-inducible isoform of protein tyrosine phosphatase epsilon JOURNAL Proc. Natl. Acad. Sci. U.S.A. 92 (26), 12235-12239 (1995) MEDLINE 96109240 REFERENCE 8 (residues 1 to 700) AUTHORS van den Maagdenberg,A.M., van den Hurk,H.H., Weghuis,D., Wieringa,B., Geurts van Kessel,A. and Hendriks,W.J. TITLE Assignment of the human protein tyrosine phosphatase epsilon (PTPRE) gene to chromosome 10q26 by fluorescence in situ hybridization JOURNAL Genomics 30 (1), 128-129 (1995) MEDLINE 96129319 REFERENCE 9 (residues 1 to 700) AUTHORS Krueger,N.X., Streuli,M. and Saito,H. TITLE Structural diversity and evolution of human receptor-like protein tyrosine phosphatases JOURNAL EMBO J. 9 (10), 3241-3252 (1990) MEDLINE 91006018 COMMENT REVIEWED REFSEQ: This record has been curated by NCBI staff. The reference sequence was derived from X54134.1, AJ315969.1 and BI559814.1. Summary: The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. Two alternatively spliced transcript variants of this gene have been reported, one of which encodes a receptor-type PTP that possesses a short extracellular domain, a single transmembrane region, and two tandem intracytoplasmic catalytic domains; Another one encodes a PTP that contains a distinct hydrophilic N-terminus, and thus represents a nonreceptor-type isoform of this PTP. Studies of the similar gene in mice suggested the regulatory roles of this PTP in RAS related signal transduction pathways, cytokines induced SATA signaling, as well as the activation of voltage-gated K+ channels. Transcript Variant: This variant (1) contains a different 5' end region that includes a part of the coding region, when compared to variant 2. It thus encodes a protein that has a distinct N-terminus, as compared to isoform 2. The encoded protein is a receptor type isoform of this PTP. COMMENT This file is created by Vector NTI suite COMMENT ORIGDB|GenPept COMMENT VNTDATE|302014800| COMMENT VNTNAME|hPTPepsilon_D2 (NP_006495) PTPRE| COMMENT VNTAUTHORNAME|Jannik N Andersen| COMMENT VNTAUTHOREML|jannik@noergaardandersen.com| COMMENT VNTAUTHORWWW|http://ptp.cshl.edu & http://science.novonordisk.com/ptp| COMMENT VNTOAUTHORNAME|NCBI Entrez| COMMENT VNTOAUTHORTEL|(301)496-2475| COMMENT VNTOAUTHORFAX|(301)480-9241| COMMENT VNTOAUTHOREML|info@ncbi.nlm.nih.gov| COMMENT VNTOAUTHORWWW|http://www3.ncbi.nlm.nih.gov/Entrez/| COMMENT VNTOAUTHORAD1|National Center for Biotechnology Information| COMMENT VNTOAUTHORAD2|National Library of Medicine| COMMENT VNTOAUTHORAD3|Building 38A, Room 8N805| COMMENT VNTOAUTHORAD4|Bethesda, MD 20894, U.S.A.| FEATURES Location/Qualifiers source 1..287 /organism="Homo sapiens" /db_xref="taxon:9606" /chromosome="10" /map="10q26" /vntifkey="269" Protein 1..287 /product="protein tyrosine phosphatase, receptor type, E isoform 1 precursor" /EC_number="3.1.3.48" /vntifkey="270" /note="protein tyrosine phosphatase, receptor type, epsilon; protein tyrosine phosphatase, receptor type, epsilon polypeptide; protein tyrosine phosphatase epsilon" Region 1..287 /product="protein tyrosine phosphatase, receptor type, E, isoform 1" /EC_number="3.1.3.48" /vntifkey="203" /label=Chain_1 Region 21..286 /region_name="Protein tyrosine phosphatase, catalytic domain" /db_xref="CDD:smart00194" /vntifkey="266" /label=Region_2 /note="PTPc" ORIGIN 1 sslekhlqtm hgttthfdki gleeefrklt nvrimkenmr tgnlpanmkk arviqiipyd 61 fnrvilsmkr gqeytdyina sfidgyrqkd yfiatqgpla htvedfwrmi wewkshtivm 121 ltevqereqd kcyqywpteg svthgeitie ikndtlseai sirdflvtln qpqarqeeqv 181 rvvrqfhfhg wpeigipaeg kgmidliaav qkqqqqtgnh pitvhcsaga grtgtfials 241 nilervkaeg lldvfqavks lrlqrphmvq tleqyefcyk vvqdfid // LOCUS hPTPgamma_ 283 aa 17-MAY-2003 DEFINITION protein tyrosine phosphatase, receptor type, G precursor; protein tyrosine phosphatase, receptor type, gamma polypeptide; protein tyrosine phosphatase gamma; receptor-type protein phosphatase gamma; receptor tyrosine phosphatase gamma [Homo sapiens]. ACCESSION NP_002832 DBSOURCE REFSEQ: accession NM_002841.2 SOURCE Homo sapiens (human). ORGANISM Homo sapiens Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. REFERENCE 1 (residues 1 to 1445) AUTHORS Liu,S., Sugimoto,Y., Kulp,S.K., Jiang,J., Chang,H.L., Park,K.Y., Kashida,Y. and Lin,Y.C. TITLE Estrogenic down-regulation of protein tyrosine phosphatase gamma (PTP gamma) in human breast is associated with estrogen receptor alpha JOURNAL Anticancer Res. 22 (6C), 3917-3923 (2002) MEDLINE 22441179 REMARK GeneRIF: Estrogenic down-regulation of protein tyrosine phosphatase gamma (PTP gamma) in human breast is associated with estrogen receptor alpha. REFERENCE 2 (residues 1 to 1445) AUTHORS Liu,S., Kulp,S.K., Sugimoto,Y., Jiang,J., Chang,H.L. and Lin,Y.C. TITLE Involvement of breast epithelial-stromal interactions in the regulation of protein tyrosine phosphatase-gamma (PTPgamma) mRNA expression by estrogenically active agents JOURNAL Breast Cancer Res. Treat. 71 (1), 21-35 (2002) MEDLINE 21848634 REMARK GeneRIF: both estradiol-17beta and zeranol regulate PTPgamma expression in human breast; epithelial-stromal cell interaction is important in regulation of PTPgamma expression by estrogenically active agents REFERENCE 3 (residues 1 to 1445) AUTHORS Kastury,K., Ohta,M., Lasota,J., Moir,D., Dorman,T., LaForgia,S., Druck,T. and Huebner,K. TITLE Structure of the human receptor tyrosine phosphatase gamma gene (PTPRG) and relation to the familial RCC t(3;8) chromosome translocation JOURNAL Genomics 32 (2), 225-235 (1996) MEDLINE 96429999 REFERENCE 4 (residues 1 to 1445) AUTHORS Barnea,G., Silvennoinen,O., Shaanan,B., Honegger,A.M., Canoll,P.D., D'Eustachio,P., Morse,B., Levy,J.B., Laforgia,S., Huebner,K. et al. TITLE Identification of a carbonic anhydrase-like domain in the extracellular region of RPTP gamma defines a new subfamily of receptor tyrosine phosphatases JOURNAL Mol. Cell. Biol. 13 (3), 1497-1506 (1993) MEDLINE 93180796 REFERENCE 5 (residues 1 to 1445) AUTHORS LaForgia,S., Morse,B., Levy,J., Barnea,G., Cannizzaro,L.A., Li,F., Nowell,P.C., Boghosian-Sell,L., Glick,J., Weston,A. et al. TITLE Receptor protein-tyrosine phosphatase gamma is a candidate tumor suppressor gene at human chromosome region 3p21 JOURNAL Proc. Natl. Acad. Sci. U.S.A. 88 (11), 5036-5040 (1991) MEDLINE 91271326 REFERENCE 6 (residues 1 to 1445) AUTHORS Krueger,N.X., Streuli,M. and Saito,H. TITLE Structural diversity and evolution of human receptor-like protein tyrosine phosphatases JOURNAL EMBO J. 9 (10), 3241-3252 (1990) MEDLINE 91006018 COMMENT REVIEWED REFSEQ: This record has been curated by NCBI staff. The reference sequence was derived from L09247.1, AI872451.1 and U46089.1. On Feb 22, 2002 this sequence version replaced gi:11386169. Summary: The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. This PTP possesses an extracellular region, a single transmembrane region, and two tandem intracytoplasmic catalytic domains, and thus represents a receptor-type PTP. The extracellular region of this PTP contains a carbonic anhydrase-like (CAH) domain, which is also found in the extracellular region of PTPRBETA/ZETA. This gene is located in a chromosomal region that is frequently deleted in renal cell carcinoma and lung carcinoma, thus is thought to be a candidate tumor suppressor gene. COMMENT This file is created by Vector NTI suite COMMENT ORIGDB|GenPept COMMENT VNTDATE|302014800| COMMENT VNTNAME|hPTPgamma_D2 (NP_002832) PTPRG| COMMENT VNTAUTHORNAME|Jannik N Andersen| COMMENT VNTAUTHOREML|jannik@noergaardandersen.com| COMMENT VNTAUTHORWWW|http://ptp.cshl.edu & http://science.novonordisk.com/ptp| COMMENT VNTOAUTHORNAME|NCBI Entrez| COMMENT VNTOAUTHORTEL|(301)496-2475| COMMENT VNTOAUTHORFAX|(301)480-9241| COMMENT VNTOAUTHOREML|info@ncbi.nlm.nih.gov| COMMENT VNTOAUTHORWWW|http://www3.ncbi.nlm.nih.gov/Entrez/| COMMENT VNTOAUTHORAD1|National Center for Biotechnology Information| COMMENT VNTOAUTHORAD2|National Library of Medicine| COMMENT VNTOAUTHORAD3|Building 38A, Room 8N805| COMMENT VNTOAUTHORAD4|Bethesda, MD 20894, U.S.A.| FEATURES Location/Qualifiers source 1..283 /organism="Homo sapiens" /db_xref="taxon:9606" /chromosome="3" /map="3p21-p14" /vntifkey="269" Protein 1..283 /product="protein tyrosine phosphatase, receptor type, G precursor" /EC_number="3.1.3.48" /vntifkey="270" /note="protein tyrosine phosphatase, receptor type, gamma polypeptide; protein tyrosine phosphatase gamma; receptor-type protein phosphatase gamma; receptor tyrosine phosphatase gamma" Region 1..283 /product="protein tyrosine phosphatase, receptor type, G" /vntifkey="203" /label=Chain_1 Region 21..283 /region_name="Protein tyrosine phosphatase, catalytic domain" /db_xref="CDD:smart00194" /vntifkey="266" /label=Region_3 /note="PTPc" ORIGIN 1 nqlhsyvnsi lipgvggktr lekqfklvtq cnakyvecfs aqkecnkekn rnssvvpser 61 arvglaplpg mkgtdyinas yimgyyrsne fiitqhplph ttkdfwrmiw dhnaqiivml 121 pdnqslaede fvywpsrees mnceaftvtl iskdrlclsn eeqiiihdfi leatqddyvl 181 evrhfqcpkw pnpdapisst felinvikee altrdgptiv hdeygavsag mlcalttlsq 241 qlenenavdv fqvakminlm rpgvftdieq yqfiykarls lvs // LOCUS hPTPkappa_ 283 aa 17-MAY-2003 DEFINITION protein tyrosine phosphatase, receptor type, K precursor; protein-tyrosine phosphatase, receptor type, kappa; protein-tyrosine phosphatase kappa; protein-tyrosine phosphatase kappa precursor [Homo sapiens]. ACCESSION NP_002835 DBSOURCE REFSEQ: accession NM_002844.2 SOURCE Homo sapiens (human). ORGANISM Homo sapiens Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. REFERENCE 1 (residues 1 to 1440) AUTHORS Yang,Y., Gil,M.C., Choi,E.Y., Park,S.H., Pyun,K.H. and Ha,H. TITLE Molecular cloning and chromosomal localization of a human gene homologous to the murine R-PTP-kappa, a receptor-type protein tyrosine phosphatase JOURNAL Gene 186 (1), 77-82 (1997) MEDLINE 97199372 REFERENCE 2 (residues 1 to 1440) AUTHORS Yang,Y., Gil,M., Byun,S.M., Choi,I., Pyun,K.H. and Ha,H. TITLE Transforming growth factor-beta1 inhibits human keratinocyte proliferation by upregulation of a receptor-type tyrosine phosphatase R-PTP-kappa gene expression JOURNAL Biochem. Biophys. Res. Commun. 228 (3), 807-812 (1996) MEDLINE 97096334 REFERENCE 3 (residues 1 to 1440) AUTHORS Fuchs,M., Muller,T., Lerch,M.M. and Ullrich,A. TITLE Association of human protein-tyrosine phosphatase kappa with members of the armadillo family JOURNAL J. Biol. Chem. 271 (28), 16712-16719 (1996) MEDLINE 96279245 REFERENCE 4 (residues 1 to 1440) AUTHORS Zondag,G.C., Koningstein,G.M., Jiang,Y.P., Sap,J., Moolenaar,W.H. and Gebbink,M.F. TITLE Homophilic interactions mediated by receptor tyrosine phosphatases mu and kappa. A critical role for the novel extracellular MAM domain JOURNAL J. Biol. Chem. 270 (24), 14247-14250 (1995) MEDLINE 95301498 REFERENCE 5 (residues 1 to 1440) AUTHORS Sap,J., Jiang,Y.P., Friedlander,D., Grumet,M. and Schlessinger,J. TITLE Receptor tyrosine phosphatase R-PTP-kappa mediates homophilic binding JOURNAL Mol. Cell. Biol. 14 (1), 1-9 (1994) MEDLINE 94088505 COMMENT REVIEWED REFSEQ: This record has been curated by NCBI staff. The reference sequence was derived from L77886.1 and BI755683.1. On Feb 22, 2002 this sequence version replaced gi:4506317. Summary: The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. This PTP possesses an extracellular region, a single transmembrane region, and two tandem catalytic domains, and thus represents a receptor-type PTP. The extracellular region contains a meprin-A5 antigen-PTP mu (MAM) domain, an Ig-like domain and four fibronectin type III-like repeats. This PTP was shown to mediate homophilic intercellular interaction, possibly through the interaction with beta- and gamma-catenin at adherens junctions. Expression of this gene was found to be stimulated by TGF-beta 1, which may be important for the inhibition of keratinocyte proliferation. COMMENT This file is created by Vector NTI suite COMMENT ORIGDB|GenPept COMMENT VNTDATE|302014800| COMMENT VNTNAME|hPTPkappa_D2 (NP_002835) PTPRK| COMMENT VNTAUTHORNAME|Jannik N Andersen| COMMENT VNTAUTHOREML|jannik@noergaardandersen.com| COMMENT VNTAUTHORWWW|http://ptp.cshl.edu & http://science.novonordisk.com/ptp| COMMENT VNTOAUTHORNAME|NCBI Entrez| COMMENT VNTOAUTHORTEL|(301)496-2475| COMMENT VNTOAUTHORFAX|(301)480-9241| COMMENT VNTOAUTHOREML|info@ncbi.nlm.nih.gov| COMMENT VNTOAUTHORWWW|http://www3.ncbi.nlm.nih.gov/Entrez/| COMMENT VNTOAUTHORAD1|National Center for Biotechnology Information| COMMENT VNTOAUTHORAD2|National Library of Medicine| COMMENT VNTOAUTHORAD3|Building 38A, Room 8N805| COMMENT VNTOAUTHORAD4|Bethesda, MD 20894, U.S.A.| FEATURES Location/Qualifiers source 1..283 /organism="Homo sapiens" /db_xref="taxon:9606" /chromosome="6" /map="6q22.2-23.1" /vntifkey="269" Protein 1..283 /product="protein tyrosine phosphatase, receptor type, K precursor" /EC_number="3.1.3.48" /vntifkey="270" /note="protein-tyrosine phosphatase, receptor type, kappa; protein-tyrosine phosphatase kappa; protein-tyrosine phosphatase kappa precursor" Region 1..283 /product="protein tyrosine phosphatase, receptor type, K" /vntifkey="203" /label=Chain_1 Region 19..283 /region_name="Protein tyrosine phosphatase, catalytic domain" /db_xref="CDD:smart00194" /vntifkey="266" /label=Region_3 /note="PTPc" ORIGIN 1 kaayfdmiri dsqtnsshlk defqtlnsvt prlqaedcsi aclprnhdkn rfmdmlppdr 61 clpflitidg essnyinaal mdsyrqpaaf ivtqyplpnt vkdfwrlvyd ygctsivmln 121 evdlsqgcpq ywpeegmlry gpiqvecmsc smdcdvinri fricnltrpq egylmvqqfq 181 ylgwashrev pgskrsflkl ilqvekwqee ceegegrtii hclngggrsg mfcaigivve 241 mvkrqnvvdv fhavktlrns kpnmveapeq yrfcydvale yle // LOCUS hPTPlamda_ 284 aa 17-MAY-2003 DEFINITION protein tyrosine phosphatase, receptor type, U isoform 3 precursor; protein tyrosine phosphatase J; protein tyrosine phosphatase receptor omicron [Homo sapiens]. ACCESSION NP_005695 DBSOURCE REFSEQ: accession NM_005704.2 SOURCE Homo sapiens (human). ORGANISM Homo sapiens Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. REFERENCE 1 (residues 1 to 1446) AUTHORS Yan,H.X., He,Y.Q., Dong,H., Zhang,P., Zeng,J.Z., Cao,H.F., Wu,M.C. and Wang,H.Y. TITLE Physical and functional interaction between receptor-like protein tyrosine phosphatase PCP-2 and beta-catenin JOURNAL Biochemistry 41 (52), 15854-15860 (2002) MEDLINE 22389441 REMARK GeneRIF: Expressed in a cell density-dependent fashion, PCP-2 interacts directly with its substrate beta-catenin, independent of the tyrosine phosphorylation state of beta-catenin. REFERENCE 2 (residues 1 to 1446) AUTHORS Wang,B., Kishihara,K., Zhang,D., Sakamoto,T. and Nomoto,K. TITLE Transcriptional regulation of a receptor protein tyrosine phosphatase gene hPTP-J by PKC-mediated signaling pathways in Jurkat and Molt-4 T lymphoma cells JOURNAL Biochim. Biophys. Acta 1450 (3), 331-340 (1999) MEDLINE 99326162 REFERENCE 3 (residues 1 to 1446) AUTHORS Avraham,S., London,R., Tulloch,G.A., Ellis,M., Fu,Y., Jiang,S., White,R.A., Painter,C., Steinberger,A.A. and Avraham,H. TITLE Characterization and chromosomal localization of PTPRO, a novel receptor protein tyrosine phosphatase, expressed in hematopoietic stem cells JOURNAL Gene 204 (1-2), 5-16 (1997) MEDLINE 98094249 REFERENCE 4 (residues 1 to 1446) AUTHORS Wang,B., Kishihara,K., Zhang,D., Hara,H. and Nomoto,K. TITLE Molecular cloning and characterization of a novel human receptor protein tyrosine phosphatase gene, hPTP-J: down-regulation of gene expression by PMA and calcium ionophore in Jurkat T lymphoma cells JOURNAL Biochem. Biophys. Res. Commun. 231 (1), 77-81 (1997) MEDLINE 97223402 REFERENCE 5 (residues 1 to 1446) AUTHORS Crossland,S., Smith,P.D. and Crompton,M.R. TITLE Molecular cloning and characterization of PTP pi, a novel receptor-like protein-tyrosine phosphatase JOURNAL Biochem. J. 319 (Pt 1), 249-254 (1996) MEDLINE 97024447 REFERENCE 6 (residues 1 to 1446) AUTHORS Wang,H., Lian,Z., Lerch,M.M., Chen,Z., Xie,W. and Ullrich,A. TITLE Characterization of PCP-2, a novel receptor protein tyrosine phosphatase of the MAM domain family JOURNAL Oncogene 12 (12), 2555-2562 (1996) MEDLINE 96293401 COMMENT REVIEWED REFSEQ: This record has been curated by NCBI staff. The reference sequence was derived from X97198.1 and X95712.1. On Mar 26, 2002 this sequence version replaced gi:5032003. Summary: The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. This PTP possesses an extracellular region, a single transmembrane region, and two tandem intracellular catalytic domains, and thus represents a receptor-type PTP. The extracellular region contains a meprin-A5 antigen-PTP (MAM) domain, Ig-like and fibronectin type III-like repeats. This PTP was thought to play roles in cell-cell recognition and adhesion. Studies of the similar gene in mice suggested the role of this PTP in early neural development. The expression of this gene was reported to be regulated by phorbol myristate acetate (PMA) or calcium ionophore in Jurkat T lymphoma cells. Three alternatively spliced transcript variants, which encode distinct proteins, have been reported. Transcript Variant: This variant (3) encodes the longest isoform (3). COMMENT This file is created by Vector NTI suite COMMENT ORIGDB|GenPept COMMENT VNTDATE|302014800| COMMENT VNTNAME|hPTPlamda_D2 (NP_005695) PTPRU| COMMENT VNTAUTHORNAME|Jannik N Andersen| COMMENT VNTAUTHOREML|jannik@noergaardandersen.com| COMMENT VNTAUTHORWWW|http://ptp.cshl.edu & http://science.novonordisk.com/ptp| COMMENT VNTOAUTHORNAME|NCBI Entrez| COMMENT VNTOAUTHORTEL|(301)496-2475| COMMENT VNTOAUTHORFAX|(301)480-9241| COMMENT VNTOAUTHOREML|info@ncbi.nlm.nih.gov| COMMENT VNTOAUTHORWWW|http://www3.ncbi.nlm.nih.gov/Entrez/| COMMENT VNTOAUTHORAD1|National Center for Biotechnology Information| COMMENT VNTOAUTHORAD2|National Library of Medicine| COMMENT VNTOAUTHORAD3|Building 38A, Room 8N805| COMMENT VNTOAUTHORAD4|Bethesda, MD 20894, U.S.A.| FEATURES Location/Qualifiers source 1..284 /organism="Homo sapiens" /db_xref="taxon:9606" /chromosome="1" /map="1p35.3-p35.1" /vntifkey="269" Protein 1..284 /product="protein tyrosine phosphatase, receptor type, U isoform 3 precursor" /vntifkey="270" /note="protein tyrosine phosphatase J; protein tyrosine phosphatase receptor omicron" Region 1..284 /product="protein tyrosine phosphatase, receptor type, U, isoform 3" /vntifkey="203" /label=Chain_1 Region 18..284 /region_name="Protein tyrosine phosphatase, catalytic domain" /db_xref="CDD:smart00194" /vntifkey="266" /label=Region_3 /note="PTPc" ORIGIN 1 katykemiri dpqsnssqlr eefqtlnsvt ppldveecsi allprnrdkn rsmdvlppdr 61 clpflistdg dsnnyinaal tdsytrsaaf ivtlhplqst tpdfwrlvyd ygctsivmln 121 qlnqsnsawp clqywpepgr qqyglmevef msgtadedlv arvfrvqnis rlqeghllvr 181 hfqflrwsay rdtpdskkaf lhllaevdkw qaesgdgrti vhclngggrs gtfcacatvl 241 emirchnlvd vffaaktlrn ykpnmvetmd qyhfcydval eyle // LOCUS hPTPmu_D2\ 283 aa 17-MAY-2003 DEFINITION protein tyrosine phosphatase, receptor type, M precursor; protein tyrosine phosphatase, receptor type, mu polypeptide; protein tyrosine phosphatase mu precursor [Homo sapiens]. ACCESSION NP_002836 DBSOURCE REFSEQ: accession NM_002845.2 SOURCE Homo sapiens (human). ORGANISM Homo sapiens Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. REFERENCE 1 (residues 1 to 1452) AUTHORS Blanchetot,C., Tertoolen,L.G., Overvoorde,J. and den Hertog,J. TITLE Intra- and intermolecular interactions between intracellular domains of receptor protein-tyrosine phosphatases JOURNAL J. Biol. Chem. 277 (49), 47263-47269 (2002) MEDLINE 22344739 REMARK GeneRIF: interactions between RPTP-domain1s and RPTP-domain 2s are a common but specific mechanism that is likely to be regulated- domain2s and the wedge structures are crucial determinants of binding specificity, thus regulating cross-talk between RPTPs REFERENCE 2 (residues 1 to 1452) AUTHORS Mourton,T., Hellberg,C.B., Burden-Gulley,S.M., Hinman,J., Rhee,A. and Brady-Kalnay,S.M. TITLE The PTPmu protein-tyrosine phosphatase binds and recruits the scaffolding protein RACK1 to cell-cell contacts JOURNAL J. Biol. Chem. 276 (18), 14896-14901 (2001) MEDLINE 21226727 REFERENCE 3 (residues 1 to 1452) AUTHORS Feiken,E., van Etten,I., Gebbink,M.F., Moolenaar,W.H. and Zondag,G.C. TITLE Intramolecular interactions between the juxtamembrane domain and phosphatase domains of receptor protein-tyrosine phosphatase RPTPmu. Regulation of catalytic activity JOURNAL J. Biol. Chem. 275 (20), 15350-15356 (2000) MEDLINE 20270248 REFERENCE 4 (residues 1 to 1452) AUTHORS Brady-Kalnay,S.M. and Tonks,N.K. TITLE Identification of the homophilic binding site of the receptor protein tyrosine phosphatase PTP mu JOURNAL J. Biol. Chem. 269 (45), 28472-28477 (1994) MEDLINE 95050637 REFERENCE 5 (residues 1 to 1452) AUTHORS Suijkerbuijk,R.F., Gebbink,M.F., Moolenaar,W.H. and Geurts van Kessel,A. TITLE Fine mapping of the human receptor-like protein tyrosine phosphatase gene (PTPRM) to 18p11.2 by fluorescence in situ hybridization JOURNAL Cytogenet. Cell Genet. 64 (3-4), 245-246 (1993) MEDLINE 94007972 REFERENCE 6 (residues 1 to 1452) AUTHORS Brady-Kalnay,S.M., Flint,A.J. and Tonks,N.K. TITLE Homophilic binding of PTP mu, a receptor-type protein tyrosine phosphatase, can mediate cell-cell aggregation JOURNAL J. Cell Biol. 122 (4), 961-972 (1993) MEDLINE 93352709 REFERENCE 7 (residues 1 to 1452) AUTHORS Gebbink,M.F., van Etten,I., Hateboer,G., Suijkerbuijk,R., Beijersbergen,R.L., Geurts van Kessel,A. and Moolenaar,W.H. TITLE Cloning, expression and chromosomal localization of a new putative receptor-like protein tyrosine phosphatase JOURNAL FEBS Lett. 290 (1-2), 123-130 (1991) MEDLINE 92008644 COMMENT REVIEWED REFSEQ: This record has been curated by NCBI staff. The reference sequence was derived from X58288.1 and AA281524.1. On Feb 22, 2002 this sequence version replaced gi:4506319. Summary: The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. This PTP possesses an extracellular region, a single transmembrane region, and two tandem catalytic domains, and thus represents a receptor-type PTP. The extracellular region contains a meprin-A5 antigen-PTP mu (MAM) domain, an Ig-like domain and four fibronectin type III-like repeats. This PTP has been shown to mediate cell-cell aggregation through the interaction with another molecule of this PTP on an adjacent cell. This PTP can interact with scaffolding protein RACK1/GNB2L1, which may be necessary for the downstream signaling in response to cell-cell adhesion. COMMENT This file is created by Vector NTI suite COMMENT ORIGDB|GenPept COMMENT VNTDATE|302014800| COMMENT VNTNAME|hPTPmu_D2 (NP_002836) PTPRM| COMMENT VNTAUTHORNAME|Jannik N Andersen| COMMENT VNTAUTHOREML|jannik@noergaardandersen.com| COMMENT VNTAUTHORWWW|http://ptp.cshl.edu & http://science.novonordisk.com/ptp| COMMENT VNTOAUTHORNAME|NCBI Entrez| COMMENT VNTOAUTHORTEL|(301)496-2475| COMMENT VNTOAUTHORFAX|(301)480-9241| COMMENT VNTOAUTHOREML|info@ncbi.nlm.nih.gov| COMMENT VNTOAUTHORWWW|http://www3.ncbi.nlm.nih.gov/Entrez/| COMMENT VNTOAUTHORAD1|National Center for Biotechnology Information| COMMENT VNTOAUTHORAD2|National Library of Medicine| COMMENT VNTOAUTHORAD3|Building 38A, Room 8N805| COMMENT VNTOAUTHORAD4|Bethesda, MD 20894, U.S.A.| FEATURES Location/Qualifiers source 1..283 /organism="Homo sapiens" /db_xref="taxon:9606" /chromosome="18" /map="18p11.2" /vntifkey="269" Protein 1..283 /product="protein tyrosine phosphatase, receptor type, M precursor" /EC_number="3.1.3.48" /vntifkey="270" /note="protein tyrosine phosphatase, receptor type, mu polypeptide; protein tyrosine phosphatase mu precursor" Region 1..283 /product="protein tyrosine phosphatase, receptor type, M" /vntifkey="203" /label=Chain_1 Region 18..282 /region_name="Protein tyrosine phosphatase, catalytic domain" /db_xref="CDD:smart00194" /vntifkey="266" /label=Region_3 /note="PTPc" ORIGIN 1 rslyydmnkl dpqtnssqik eefrtlnmvt ptlrvedcsi allprnhekn rcmdilppdr 61 clpflitidg essnyinaal mdsykqpsaf ivtqhplpnt vkdfwrlvld yhctsvvmln 121 dvdpaqlcpq ywpengvhrh gpiqvefvsa dleediisri friynaarpq dgyrmvqqfq 181 flgwpmyrdt pvskrsflkl irqvdkwqee ynggegptvv hclngggrsg tfcaisivce 241 mlrhqrtvdv fhavktlrnn kpnmvdlldq ykfcyevale yln // LOCUS hPTPrho_D2 283 aa 17-MAY-2003 DEFINITION protein tyrosine phosphatase, receptor type, T isoform 1 precursor; receptor protein tyrosine phosphatase [Homo sapiens]. ACCESSION NP_573400 DBSOURCE REFSEQ: accession NM_133170.1 SOURCE Homo sapiens (human). ORGANISM Homo sapiens Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. REFERENCE 1 (residues 1 to 1463) AUTHORS Besco,J.A., Frostholm,A., Popesco,M.C., Burghes,A.H. and Rotter,A. TITLE Genomic organization and alternative splicing of the human and mouse RPTPrho genes JOURNAL BMC Genomics 2 (1), 1 (2001) REFERENCE 2 (residues 1 to 1463) AUTHORS McAndrew,P.E., Frostholm,A., White,R.A., Rotter,A. and Burghes,A.H. TITLE Identification and characterization of RPTP rho, a novel RPTP mu/kappa-like receptor protein tyrosine phosphatase whose expression is restricted to the central nervous system JOURNAL Brain Res. Mol. Brain Res. 56 (1-2), 9-21 (1998) MEDLINE 98267260 REFERENCE 3 (residues 1 to 1463) AUTHORS McAndrew,P.E., Frostholm,A., Evans,J.E., Zdilar,D., Goldowitz,D., Chiu,I.M., Burghes,A.H. and Rotter,A. TITLE Novel receptor protein tyrosine phosphatase (RPTPrho) and acidic fibroblast growth factor (FGF-1) transcripts delineate a rostrocaudal boundary in the granule cell layer of the murine cerebellar cortex JOURNAL J. Comp. Neurol. 391 (4), 444-455 (1998) MEDLINE 98146229 REFERENCE 4 (residues 1 to 1463) AUTHORS Hillier,L.D., Lennon,G., Becker,M., Bonaldo,M.F., Chiapelli,B., Chissoe,S., Dietrich,N., DuBuque,T., Favello,A., Gish,W., Hawkins,M., Hultman,M., Kucaba,T., Lacy,M., Le,M., Le,N., Mardis,E., Moore,B., Morris,M., Parsons,J., Prange,C., Rifkin,L., Rohlfing,T., Schellenberg,K., Marra,M. et al. TITLE Generation and analysis of 280,000 human expressed sequence tags JOURNAL Genome Res. 6 (9), 807-828 (1996) MEDLINE 97044478 COMMENT REVIEWED REFSEQ: This record has been curated by NCBI staff. The reference sequence was derived from AF043644.4 and R50970.1. Summary: The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. This PTP possesses an extracellular region, a single transmembrane region, and two tandem intracellular catalytic domains, and thus represents a receptor-type PTP. The extracellular region contains a meprin-A5 antigen-PTP (MAM) domain, Ig-like and fibronectin type III-like repeats. The protein domain structure and the expression pattern of the mouse counterpart of this PTP suggest its roles in both signal transduction and cellular adhesion in the central nervous system. Two alternatively spliced transcript variants of this gene, which encode distinct proteins, have been reported. Transcript Variant: This variant (1) contains an additional fragment within the coding region when compared to variant 2, and thus encodes a protein that contains an extra internal segment, as compared to isoform 2. COMMENT This file is created by Vector NTI suite COMMENT ORIGDB|GenPept COMMENT VNTDATE|302014800| COMMENT VNTNAME|hPTPrho_D2 (NP_573400) PTPRT| COMMENT VNTAUTHORNAME|Jannik N Andersen| COMMENT VNTAUTHOREML|jannik@noergaardandersen.com| COMMENT VNTAUTHORWWW|http://ptp.cshl.edu & http://science.novonordisk.com/ptp| COMMENT VNTOAUTHORNAME|NCBI Entrez| COMMENT VNTOAUTHORTEL|(301)496-2475| COMMENT VNTOAUTHORFAX|(301)480-9241| COMMENT VNTOAUTHOREML|info@ncbi.nlm.nih.gov| COMMENT VNTOAUTHORWWW|http://www3.ncbi.nlm.nih.gov/Entrez/| COMMENT VNTOAUTHORAD1|National Center for Biotechnology Information| COMMENT VNTOAUTHORAD2|National Library of Medicine| COMMENT VNTOAUTHORAD3|Building 38A, Room 8N805| COMMENT VNTOAUTHORAD4|Bethesda, MD 20894, U.S.A.| FEATURES Location/Qualifiers source 1..283 /organism="Homo sapiens" /db_xref="taxon:9606" /chromosome="20" /map="20q12-q13" /vntifkey="269" Protein 1..283 /product="protein tyrosine phosphatase, receptor type, T isoform 1 precursor" /vntifkey="270" /note="receptor protein tyrosine phosphatase" Region 1..283 /product="protein tyrosine phosphatase, receptor type, T, isoform 1" /vntifkey="203" /label=Chain_1 Region 18..283 /region_name="Protein tyrosine phosphatase, catalytic domain" /db_xref="CDD:smart00194" /vntifkey="266" /label=Region_2 /note="PTPc" ORIGIN 1 rslyynisrl dpqtnssqik defqtlnivt prvrpedcsi gllprnhdkn rsmdvlpldr 61 clpflisvdg essnyinaal mdshkqpaaf vvtqhplpnt vadfwrlvfd yncssvvmln 121 emdtaqfcmq ywpektsgcy gpiqvefvsa didediihri fricnmarpq dgyrivqhlq 181 yigwpayrdt ppskrsllkv vrrlekwqeq ydgregrtvv hclngggrsg tfcaicsvce 241 miqqqniidv fhivktlrnn ksnmvetleq ykfvyevale yls // LOCUS hPTPsigma_ 283 aa 17-MAY-2003 DEFINITION protein tyrosine phosphatase, receptor type, sigma isoform 1 precursor; protein tyrosine phosphatase PTPsigma [Homo sapiens]. ACCESSION NP_002841 DBSOURCE REFSEQ: accession NM_002850.2 SOURCE Homo sapiens (human). ORGANISM Homo sapiens Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. REFERENCE 1 (residues 1 to 1948) AUTHORS Blanchetot,C., Tertoolen,L.G., Overvoorde,J. and den Hertog,J. TITLE Intra- and intermolecular interactions between intracellular domains of receptor protein-tyrosine phosphatases JOURNAL J. Biol. Chem. 277 (49), 47263-47269 (2002) MEDLINE 22344739 REMARK GeneRIF: interactions between RPTP-domain1s and RPTP-domain 2s are a common but specific mechanism that is likely to be regulated- domain2s and the wedge structures are crucial determinants of binding specificity, thus regulating cross-talk between RPTPs REFERENCE 2 (residues 1 to 1948) AUTHORS Wallace,M.J., Batt,J., Fladd,C.A., Henderson,J.T., Skarnes,W. and Rotin,D. TITLE Neuronal defects and posterior pituitary hypoplasia in mice lacking the receptor tyrosine phosphatase PTPsigma JOURNAL Nat. Genet. 21 (3), 334-338 (1999) MEDLINE 99178277 REMARK functional study of the mouse homolog REFERENCE 3 (residues 1 to 1948) AUTHORS Elchebly,M., Wagner,J., Kennedy,T.E., Lanctot,C., Michaliszyn,E., Itie,A., Drouin,J. and Tremblay,M.L. TITLE Neuroendocrine dysplasia in mice lacking protein tyrosine phosphatase sigma JOURNAL Nat. Genet. 21 (3), 330-333 (1999) MEDLINE 99178276 REMARK functional study of the mouse homolog REFERENCE 4 (residues 1 to 1948) AUTHORS Haworth,K., Shu,K.K., Stokes,A., Morris,R. and Stoker,A. TITLE The expression of receptor tyrosine phosphatases is responsive to sciatic nerve crush JOURNAL Mol. Cell. Neurosci. 12 (3), 93-104 (1998) MEDLINE 99009170 REMARK functional study of the rat homolog REFERENCE 5 (residues 1 to 1948) AUTHORS Wagner,J., Gordon,L.A., Heng,H.H., Tremblay,M.L. and Olsen,A.S. TITLE Physical mapping of receptor type protein tyrosine phosphatase sigma (PTPRS) to human chromosome 19p13.3 JOURNAL Genomics 38 (1), 76-78 (1996) MEDLINE 97124849 REFERENCE 6 (residues 1 to 1948) AUTHORS Endo,N., Rutledge,S.J., Opas,E.E., Vogel,R., Rodan,G.A. and Schmidt,A. TITLE Human protein tyrosine phosphatase-sigma: alternative splicing and inhibition by bisphosphonates JOURNAL J. Bone Miner. Res. 11 (4), 535-543 (1996) MEDLINE 96255038 REFERENCE 7 (residues 1 to 1948) AUTHORS Pulido,R., Serra-Pages,C., Tang,M. and Streuli,M. TITLE The LAR/PTP delta/PTP sigma subfamily of transmembrane protein-tyrosine-phosphatases: multiple human LAR, PTP delta, and PTP sigma isoforms are expressed in a tissue-specific manner and associate with the LAR-interacting protein LIP.1 JOURNAL Proc. Natl. Acad. Sci. U.S.A. 92 (25), 11686-11690 (1995) MEDLINE 96102179 REFERENCE 8 (residues 1 to 1948) AUTHORS Adachi,M., Sekiya,M., Arimura,Y., Takekawa,M., Itoh,F., Hinoda,Y., Imai,K. and Yachi,A. TITLE Protein-tyrosine phosphatase expression in pre-B cell NALM-6 JOURNAL Cancer Res. 52 (3), 737-740 (1992) MEDLINE 92119637 COMMENT REVIEWED REFSEQ: This record has been curated by NCBI staff. The reference sequence was derived from U35234.1 and BI461316.1. On Mar 26, 2002 this sequence version replaced gi:4506327. Summary: The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. This PTP contains an extracellular region, a single transmembrane segment and two tandem intracytoplasmic catalytic domains, and thus represents a receptor-type PTP. The extracellular region of this protein is composed of multiple Ig-like and fibronectin type III-like domains. Studies of the similar gene in mice suggested that this PTP may be involved in cell-cell interaction, primary axonogenesis, and axon guidance during embryogenesis. This PTP has been also implicated in the molecular control of adult nerve repair. Four alternatively spliced transcript variants, which encode distinct proteins, have been reported. Transcript Variant: This variant (1) encodes the longest isoform (1). COMMENT This file is created by Vector NTI suite COMMENT ORIGDB|GenPept COMMENT VNTDATE|302014800| COMMENT VNTNAME|hPTPsigma_D2 (NP_002841) PTPRS| COMMENT VNTAUTHORNAME|Jannik N Andersen| COMMENT VNTAUTHOREML|jannik@noergaardandersen.com| COMMENT VNTAUTHORWWW|http://ptp.cshl.edu & http://science.novonordisk.com/ptp| COMMENT VNTOAUTHORNAME|NCBI Entrez| COMMENT VNTOAUTHORTEL|(301)496-2475| COMMENT VNTOAUTHORFAX|(301)480-9241| COMMENT VNTOAUTHOREML|info@ncbi.nlm.nih.gov| COMMENT VNTOAUTHORWWW|http://www3.ncbi.nlm.nih.gov/Entrez/| COMMENT VNTOAUTHORAD1|National Center for Biotechnology Information| COMMENT VNTOAUTHORAD2|National Library of Medicine| COMMENT VNTOAUTHORAD3|Building 38A, Room 8N805| COMMENT VNTOAUTHORAD4|Bethesda, MD 20894, U.S.A.| FEATURES Location/Qualifiers source 1..283 /organism="Homo sapiens" /db_xref="taxon:9606" /chromosome="19" /map="19p13.3" /vntifkey="269" Protein 1..283 /product="protein tyrosine phosphatase, receptor type, sigma isoform 1 precursor" /vntifkey="270" /note="protein tyrosine phosphatase PTPsigma" Region 1..283 /product="protein tyrosine phosphatase, receptor type, sigma, isoform 1" /vntifkey="203" /label=Chain_1 Region 21..282 /region_name="Protein tyrosine phosphatase, catalytic domain" /db_xref="CDD:smart00194" /vntifkey="266" /label=Region_5 /note="PTPc" ORIGIN 1 rslyayiqkl aqvepgehvt gmelefkrla nskahtsrfi sanlpcnkfk nrlvnimpye 61 strvclqpir gvegsdyina sfidgyrqqk ayiatqgpla ettedfwrml wennstivvm 121 ltklremgre kchqywpaer saryqyfvvd pmaeynmpqy ilrefkvtda rdgqsrtvrq 181 fqftdwpeqg vpksgegfid figqvhktke qfgqdgpisv hcsagvgrtg vfitlsivle 241 rmryegvvdi fqtvkmlrtq rpamvqtede yqfcyqaale ylg // LOCUS hPTPzeta_D 282 aa 17-MAY-2003 DEFINITION protein tyrosine phosphatase, receptor-type, Z polypeptide 1; protein tyrosine phosphatase, receptor-type, zeta polypeptide 1; receptor-type tyrosine phosphatase beta/zeta [Homo sapiens]. ACCESSION NP_002842 DBSOURCE REFSEQ: accession NM_002851.1 SOURCE Homo sapiens (human). ORGANISM Homo sapiens Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. REFERENCE 1 (residues 1 to 2314) AUTHORS Harroch,S., Furtado,G.C., Brueck,W., Rosenbluth,J., Lafaille,J., Chao,M., Buxbaum,J.D. and Schlessinger,J. TITLE A critical role for the protein tyrosine phosphatase receptor type Z in functional recovery from demyelinating lesions JOURNAL Nat. Genet. 32 (3), 411-414 (2002) MEDLINE 22297719 REMARK GeneRIF: PTPRZ1 has a role in oligodendrocyte survival and in recovery from demyelinating disease REFERENCE 2 (residues 1 to 2314) AUTHORS Thomaidou,D., Coquillat,D., Meintanis,S., Noda,M., Rougon,G. and Matsas,R. TITLE Soluble forms of NCAM and F3 neuronal cell adhesion molecules promote Schwann cell migration: identification of protein tyrosine phosphatases zeta/beta as the putative F3 receptors on Schwann cells JOURNAL J. Neurochem. 78 (4), 767-778 (2001) MEDLINE 21412137 REFERENCE 3 (residues 1 to 2314) AUTHORS Kawachi,H., Fujikawa,A., Maeda,N. and Noda,M. TITLE Identification of GIT1/Cat-1 as a substrate molecule of protein tyrosine phosphatase zeta /beta by the yeast substrate-trapping system JOURNAL Proc. Natl. Acad. Sci. U.S.A. 98 (12), 6593-6598 (2001) MEDLINE 21287250 REFERENCE 4 (residues 1 to 2314) AUTHORS Meng,K., Rodriguez-Pena,A., Dimitrov,T., Chen,W., Yamin,M., Noda,M. and Deuel,T.F. TITLE Pleiotrophin signals increased tyrosine phosphorylation of beta beta-catenin through inactivation of the intrinsic catalytic activity of the receptor-type protein tyrosine phosphatase beta/zeta JOURNAL Proc. Natl. Acad. Sci. U.S.A. 97 (6), 2603-2608 (2000) MEDLINE 20183934 REFERENCE 5 (residues 1 to 2314) AUTHORS Kawachi,H., Tamura,H., Watakabe,I., Shintani,T., Maeda,N. and Noda,M. TITLE Protein tyrosine phosphatase zeta/RPTPbeta interacts with PSD-95/SAP90 family JOURNAL Brain Res. Mol. Brain Res. 72 (1), 47-54 (1999) MEDLINE 99453345 REFERENCE 6 (residues 1 to 2314) AUTHORS Onyango,P., Lubyova,B., Gardellin,P., Kurzbauer,R. and Weith,A. TITLE Molecular cloning and expression analysis of five novel genes in chromosome 1p36 JOURNAL Genomics 50 (2), 187-198 (1998) MEDLINE 98317532 REFERENCE 7 (residues 1 to 2314) AUTHORS Ariyama,T., Hasegawa,K., Inazawa,J., Mizuno,K., Ogimoto,M., Katagiri,T. and Yakura,H. TITLE Assignment of the human protein tyrosine phosphatase, receptor-type, zeta (PTPRZ) gene to chromosome band 7q31.3 JOURNAL Cytogenet. Cell Genet. 70 (1-2), 52-54 (1995) MEDLINE 95254878 REFERENCE 8 (residues 1 to 2314) AUTHORS Levy,J.B., Canoll,P.D., Silvennoinen,O., Barnea,G., Morse,B., Honegger,A.M., Huang,J.T., Cannizzaro,L.A., Park,S.H., Druck,T. et al. TITLE The cloning of a receptor-type protein tyrosine phosphatase expressed in the central nervous system JOURNAL J. Biol. Chem. 268 (14), 10573-10581 (1993) MEDLINE 93252948 REFERENCE 9 (residues 1 to 2314) AUTHORS Krueger,N.X. and Saito,H. TITLE A human transmembrane protein-tyrosine-phosphatase, PTP zeta, is expressed in brain and has an N-terminal receptor domain homologous to carbonic anhydrases JOURNAL Proc. Natl. Acad. Sci. U.S.A. 89 (16), 7417-7421 (1992) MEDLINE 92366472 COMMENT PROVISIONAL REFSEQ: This record has not yet been subject to final NCBI review. The reference sequence was derived from M93426.1. COMMENT This file is created by Vector NTI suite COMMENT ORIGDB|GenPept COMMENT VNTDATE|302014800| COMMENT VNTNAME|hPTPzeta_D2 (NP_002842) PTPRZ1| COMMENT VNTAUTHORNAME|Jannik N Andersen| COMMENT VNTAUTHOREML|jannik@noergaardandersen.com| COMMENT VNTAUTHORWWW|http://ptp.cshl.edu & http://science.novonordisk.com/ptp| COMMENT VNTOAUTHORNAME|NCBI Entrez| COMMENT VNTOAUTHORTEL|(301)496-2475| COMMENT VNTOAUTHORFAX|(301)480-9241| COMMENT VNTOAUTHOREML|info@ncbi.nlm.nih.gov| COMMENT VNTOAUTHORWWW|http://www3.ncbi.nlm.nih.gov/Entrez/| COMMENT VNTOAUTHORAD1|National Center for Biotechnology Information| COMMENT VNTOAUTHORAD2|National Library of Medicine| COMMENT VNTOAUTHORAD3|Building 38A, Room 8N805| COMMENT VNTOAUTHORAD4|Bethesda, MD 20894, U.S.A.| FEATURES Location/Qualifiers source 1..282 /organism="Homo sapiens" /db_xref="taxon:9606" /chromosome="7" /map="7q31.3" /tissue_type="brain" /dev_stage="fetus" /tissue_lib="lambda gt10 and gt11" /vntifkey="269" Protein 1..282 /product="protein tyrosine phosphatase, receptor-type, Z polypeptide 1" /vntifkey="270" /note="protein tyrosine phosphatase, receptor-type, zeta polypeptide 1; receptor-type tyrosine phosphatase beta/zeta" Region 20..282 /region_name="Protein tyrosine phosphatase, catalytic domain" /db_xref="CDD:smart00194" /vntifkey="266" /label=Region_3 /note="PTPc" ORIGIN 1 shihayvnal lipgpagktk lekqfqllsq sniqqsdysa alkqcnrekn rtssiipver 61 srvgisslsg egtdyinasy imgyyqsnef iitqhpllht ikdfwrmiwd hnaqlvvmip 121 dgqnmaedef vywpnkdepi ncesfkvtlm aeehkclsne ekliiqdfil eatqddyvle 181 vrhfqcpkwp npdspisktf elisvikeea anrdgpmivh dehggvtagt fcalttlmhq 241 lekensvdvy qvakminlmr pgvfadieqy qflykvilsl vs //