LOCUS hBDP1\(NP_ 460 aa 17-MAY-2003 DEFINITION protein tyrosine phosphatase, non-receptor type 18; brain-derived phosphatase [Homo sapiens]. ACCESSION NP_055184 DBSOURCE REFSEQ: accession NM_014369.2 SOURCE Homo sapiens (human). ORGANISM Homo sapiens Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. REFERENCE 1 (residues 1 to 460) AUTHORS Kim,Y.W., Wang,H., Sures,I., Lammers,R., Martell,K.J. and Ullrich,A. TITLE Characterization of the PEST family protein tyrosine phosphatase BDP1 JOURNAL Oncogene 13 (10), 2275-2279 (1996) MEDLINE 97108674 COMMENT REVIEWED REFSEQ: This record has been curated by NCBI staff. The reference sequence was derived from X79568.1 and BI261717.1. On Jan 25, 2002 this sequence version replaced gi:7657484. 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 a PEST motif, which often serves as a protein-protein interaction domain, and may be related to protein intracellular half-live. This gene was found to be expressed in brain, colon tissues, and several different tumor-derived cell lines. The bilogical function of this PTP has not yet been determined. COMMENT This file is created by Vector NTI suite COMMENT ORIGDB|GenPept COMMENT VNTDATE|304502400| COMMENT VNTNAME|hBDP1 (NP_055184) PTPN18| 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..460 /organism="Homo sapiens" /db_xref="taxon:9606" /chromosome="2" /map="2q21.2" /vntifkey="269" Protein 1..460 /product="protein tyrosine phosphatase, non-receptor type 18" /EC_number="3.1.3.48" /vntifkey="270" /note="brain-derived phosphatase" Region 26..292 /region_name="Protein tyrosine phosphatase, catalytic domain" /db_xref="CDD:smart00194" /vntifkey="266" /label=Region_1 /note="PTPc" ORIGIN 1 msrsldsars flerleargg regavlagef sdiqacsaaw kadgvcstva gsrpenvrkn 61 rykdvlpydq trvilsllqe eghsdyingn firgvdgsla yiatqgplph tlldfwrlvw 121 efgvkvilma creiengrkr cerywaqeqe plqtglfcit likekwlned imlrtlkvtf 181 qkesrsvyql qymswpdrgv psspdhmlam veearrlqgs gpeplcvhcs agcgrtgvlc 241 tvdyvrqlll tqmippdfsl fdvvlkmrkq rpaavqteeq yrflyhtvaq mfcstlqnas 301 phyqnikenc aplyddalfl rtpqallaip rppggvlrsi svpgspgham adtyavvqkr 361 gapagagsgt qtgtgtgtga rsaeeaplys kvtpraqrpg ahaedargtl pgrvpadqsp 421 agsgayedva ggaqtgglgf nlrigrpkgp rdppaewtrv // LOCUS hCD45\(NP_ 1304 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|304502400| COMMENT VNTNAME|hCD45 (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..1304 /organism="Homo sapiens" /db_xref="taxon:9606" /chromosome="1" /map="1q31-q32" /vntifkey="269" Protein 1..1304 /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..23 /vntifkey="200" /label=Signal_1 Region 21..135 /region_name="COG5243, HRD1, HRD ubiquitin ligase complex, ER membrane component [Posttranslational modification, protein turnover, chaperones]" /db_xref="CDD:COG5243" /vntifkey="266" /label=Region_1 /note="HRD1" Region 24..1304 /product="protein tyrosine phosphatase, receptor type, C" /vntifkey="203" /label=Chain_1 Region 390..460 /region_name="Fibronectin type 3 domain" /db_xref="CDD:smart00060" /vntifkey="1000" /label=Dom_Misc_1 /note="FN3" Region 486..563 /region_name="Fibronectin type III domain" /db_xref="CDD:pfam00041" /vntifkey="1000" /label=Dom_Misc_2 /note="fn3" Region 650..910 /region_name="Protein tyrosine phosphatase, catalytic domain" /db_xref="CDD:smart00194" /vntifkey="266" /label=Region_2 /note="PTPc" Region 942..1227 /region_name="Protein tyrosine phosphatase, catalytic domain" /db_xref="CDD:smart00194" /vntifkey="266" /label=Region_3 /note="PTPc" ORIGIN 1 mylwlkllaf gfafldtevf vtgqsptpsp tglttakmps vplssdplpt httafspast 61 ferendfset ttslspdnts tqvspdsldn asafnttgvs svqtphlpth adsqtpsagt 121 dtqtfsgsaa naklnptpgs naisdvpger stastfptdp vspltttlsl ahhssaalpa 181 rtsnttitan tsdaylnase tttlspsgsa vistttiatt pskptcdeky anitvdylyn 241 ketklftakl nvnenvecgn ntctnnevhn ltecknasvs ishnsctapd ktlildvppg 301 vekfqlhdct qvekadttic lkwknietft cdtqnityrf qcgnmifdnk eiklenlepe 361 heykcdseil ynnhkftnas kiiktdfgsp gepqiifcrs eaahqgvitw nppqrsfhnf 421 tlcyiketek dclnldknli kydlqnlkpy tkyvlslhay iiakvqrngs aamchfttks 481 appsqvwnmt vsmtsdnsmh vkcrpprdrn gpheryhlev eagntlvrne shkncdfrvk 541 dlqystdytf kayfhngdyp gepfilhhst synskaliaf lafliivtsi allvvlykiy 601 dlhkkrscnl deqqelverd dekqlmnvep ihadillety krkiadegrl flaefqsipr 661 vfskfpikea rkpfnqnknr yvdilpydyn rvelseingd agsnyinasy idgfkeprky 721 iaaqgprdet vddfwrmiwe qkatvivmvt rceegnrnkc aeywpsmeeg trafgdvvvk 781 inqhkrcpdy iiqklnivnk kekatgrevt hiqftswpdh gvpedphlll klrrrvnafs 841 nffsgpivvh csagvgrtgt yigidamleg leaenkvdvy gyvvklrrqr clmvqveaqy 901 ilihqalvey nqfgetevnl selhpylhnm kkrdppseps pleaefqrlp syrswrtqhi 961 gnqeenkskn rnsnvipydy nrvplkhele mskesehdsd essdddsdse epskyinasf 1021 imsywkpevm iaaqgplket igdfwqmifq rkvkvivmlt elkhgdqeic aqywgegkqt 1081 ygdievdlkd tdksstytlr vfelrhskrk dsrtvyqyqy tnwsveqlpa epkelismiq 1141 vvkqklpqkn ssegnkhhks tpllihcrdg sqqtgifcal lnllesaete evvdifqvvk 1201 alrkarpgmv stfeqyqfly dviastypaq ngqvkknnhq edkiefdnev dkvkqdancv 1261 nplgapeklp eakeqaegse ptsgtegpeh svngpaspal nqgs // LOCUS hDEP1\(NP_ 1337 aa 17-MAY-2003 DEFINITION protein tyrosine phosphatase, receptor type, J precursor; protein tyrosine phosphatase, receptor type, J polypeptide; human density enhanced phosphatase-1; CD148 antigen [Homo sapiens]. ACCESSION NP_002834 DBSOURCE REFSEQ: accession NM_002843.2 SOURCE Homo sapiens (human). ORGANISM Homo sapiens Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. REFERENCE 1 (residues 1 to 1337) AUTHORS Ruivenkamp,C.A., van Wezel,T., Zanon,C., Stassen,A.P., Vlcek,C., Csikos,T., Klous,A.M., Tripodis,N., Perrakis,A., Boerrigter,L., Groot,P.C., Lindeman,J., Mooi,W.J., Meijjer,G.A., Scholten,G., Dauwerse,H., Paces,V., van Zandwijk,N., van Ommen,G.J. and Demant,P. TITLE Ptprj is a candidate for the mouse colon-cancer susceptibility locus Scc1 and is frequently deleted in human cancers JOURNAL Nat. Genet. 31 (3), 295-300 (2002) MEDLINE 22084388 REMARK GeneRIF: This protein is frequently deleted in human breast cancers. REFERENCE 2 (residues 1 to 1337) AUTHORS Baker,J.E., Majeti,R., Tangye,S.G. and Weiss,A. TITLE Protein tyrosine phosphatase CD148-mediated inhibition of T-cell receptor signal transduction is associated with reduced LAT and phospholipase Cgamma1 phosphorylation JOURNAL Mol. Cell. Biol. 21 (7), 2393-2403 (2001) MEDLINE 21160271 REFERENCE 3 (residues 1 to 1337) AUTHORS Kovalenko,M., Denner,K., Sandstrom,J., Persson,C., Gross,S., Jandt,E., Vilella,R., Bohmer,F. and Ostman,A. TITLE Site-selective dephosphorylation of the platelet-derived growth factor beta-receptor by the receptor-like protein-tyrosine phosphatase DEP-1 JOURNAL J. Biol. Chem. 275 (21), 16219-16226 (2000) MEDLINE 20283660 REFERENCE 4 (residues 1 to 1337) AUTHORS Gross,S., Knebel,A., Tenev,T., Neininger,A., Gaestel,M., Herrlich,P. and Bohmer,F.D. TITLE Inactivation of protein-tyrosine phosphatases as mechanism of UV-induced signal transduction JOURNAL J. Biol. Chem. 274 (37), 26378-26386 (1999) MEDLINE 99403084 REFERENCE 5 (residues 1 to 1337) AUTHORS Tangye,S.G., Phillips,J.H., Lanier,L.L., de Vries,J.E. and Aversa,G. TITLE CD148: a receptor-type protein tyrosine phosphatase involved in the regulation of human T cell activation JOURNAL J. Immunol. 161 (7), 3249-3255 (1998) MEDLINE 98430639 REFERENCE 6 (residues 1 to 1337) AUTHORS de la Fuente-Garcia,M.A., Nicolas,J.M., Freed,J.H., Palou,E., Thomas,A.P., Vilella,R., Vives,J. and Gaya,A. TITLE CD148 is a membrane protein tyrosine phosphatase present in all hematopoietic lineages and is involved in signal transduction on lymphocytes JOURNAL Blood 91 (8), 2800-2809 (1998) MEDLINE 98200586 REFERENCE 7 (residues 1 to 1337) AUTHORS Honda,H., Inazawa,J., Nishida,J., Yazaki,Y. and Hirai,H. TITLE Molecular cloning, characterization, and chromosomal localization of a novel protein-tyrosine phosphatase, HPTP eta JOURNAL Blood 84 (12), 4186-4194 (1994) MEDLINE 95086212 REFERENCE 8 (residues 1 to 1337) AUTHORS Ostman,A., Yang,Q. and Tonks,N.K. TITLE Expression of DEP-1, a receptor-like protein-tyrosine-phosphatase, is enhanced with increasing cell density JOURNAL Proc. Natl. Acad. Sci. U.S.A. 91 (21), 9680-9684 (1994) MEDLINE 95024024 COMMENT REVIEWED REFSEQ: This record has been curated by NCBI staff. The reference sequence was derived from U10886.1. On Feb 22, 2002 this sequence version replaced gi:4506315. 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 containing five fibronectin type III repeats, a single transmembrane region, and a single intracytoplasmic catalytic domain, and thus represents a receptor-type PTP. This PTP is present in all hematopoietic lineages, and was shown to negatively regulate T cell receptor signaling possibly through interfering with the phosphorylation of Phospholipase C Gamma 1 (PLCG1) and Linker for Activation of T Cells (LAT). This PTP was also found to dephosphorylate PDGF beta receptor, and may be involved in UV-induced signal transduction. COMMENT This file is created by Vector NTI suite COMMENT ORIGDB|GenPept COMMENT VNTDATE|304502400| COMMENT VNTNAME|hDEP1 (NP_002834) PTPRJ| 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..1337 /organism="Homo sapiens" /db_xref="taxon:9606" /chromosome="11" /map="11p11.2" /vntifkey="269" Protein 1..1337 /product="protein tyrosine phosphatase, receptor type, J precursor" /EC_number="3.1.3.48" /vntifkey="270" /note="protein tyrosine phosphatase, receptor type, J polypeptide; human density enhanced phosphatase-1; CD148 antigen" Region 1..36 /vntifkey="200" /label=Signal_1 Region 37..1337 /product="protein tyrosine phosphatase, receptor type, J" /vntifkey="203" /label=Chain_1 Region 119..187 /region_name="Fibronectin type 3 domain" /db_xref="CDD:smart00060" /vntifkey="1000" /label=Dom_Misc_1 /note="FN3" Region 369..445 /region_name="Fibronectin type III domain" /db_xref="CDD:pfam00041" /vntifkey="1000" /label=Dom_Misc_2 /note="fn3" Region 540..615 /region_name="Fibronectin type 3 domain" /db_xref="CDD:smart00060" /vntifkey="1000" /label=Dom_Misc_3 /note="FN3" Region 626..705 /region_name="Fibronectin type 3 domain" /db_xref="CDD:smart00060" /vntifkey="1000" /label=Dom_Misc_4 /note="FN3" Region 1040..1300 /region_name="Protein tyrosine phosphatase, catalytic domain" /db_xref="CDD:smart00194" /vntifkey="266" /label=Region_1 /note="PTPc" ORIGIN 1 mkpaarearl pprspglrwa lpllllllrl gqilcaggtp spipdpsvat vatgengitq 61 isstaesfhk qngtgtpqve tntsedgess gandslrtpe qgsngtdgas qktpsstgps 121 pvfdikavsi sptnviltwk sndtaaseyk yvvkhkmene ktitvvhqpw cnitglrpat 181 syvfsitpgi gnetwgdprv ikvitepipv sdlrvaltgv rkaalswsng ngtascrvll 241 esigsheelt qdsrlqvnis glkpgvqyni npyllqsnkt kgdplgtegg ldasntersr 301 agsptapvhd eslvgpvdps sgqqsrdtev llvglepgtr ynatvysqaa ngtegqpqai 361 efrtnaiqvf dvtavnisat sltliwkvsd nesssnytyk ihvagetdss nlnvseprav 421 ipglrsstfy nitvcpvlgd iegtpgflqv htppvpvsdf rvtvvsttei glawsshdae 481 sfqmhitqeg agnsrveitt nqsiiigglf pgtkycfeiv pkgpngtega srtvcnrtvp 541 savfdihvvy vtttemwldw kspdgaseyv yhlvieskhg snhtstydka itlqglipgt 601 lynitispev dhvwgdpnst aqytrpsnvs nidvstntta atlswqnfdd asptysycll 661 iekagnssna tqvvtdigit datvtelipg ssytveifaq vgdgikslep grksfctdpa 721 smasfdcevv pkepalvlkw tcppganagf elevssgawn nathlescss engteyrtev 781 tylnfstsyn isittvscgk maaptrntct tgitdppppd gspnitsvsh nsvkvkfsgf 841 eashgpikay avilttgeag hpsadvlkyt yddfkkgasd tyvtylirte ekgrsqslse 901 vlkyeidvgn esttlgyyng kleplgsyra cvagftnitf hpqnkglidg aesyvsfsry 961 sdavslpqdp gvicgavfgc ifgalvivtv ggfifwrkkr kdaknnevsf sqikpkkskl 1021 irvenfeayf kkqqadsncg faeeyedlkl vgisqpkyaa elaenrgknr ynnvlpydis 1081 rvklsvqths tddyinanym pgyhskkdfi atqgplpntl kdfwrmvwek nvyaiimltk 1141 cveqgrtkce eywpskqaqd ygditvamts eivlpewtir dftvkniqts eshplrqfhf 1201 tswpdhgvpd ttdllinfry lvrdymkqsp pespilvhcs agvgrtgtfi aidrliyqie 1261 nentvdvygi vydlrmhrpl mvqtedqyvf lnqcvldivr sqkdskvdli yqnttamtiy 1321 enlapvttfg ktngyia // LOCUS hGLEPP1\(N 1216 aa 17-MAY-2003 DEFINITION receptor-type protein tyrosine phosphatase O isoform a precursor; glomerular epithelial protein-1; protein tyrosine phosphatase PTP-U2; phosphotyrosine phosphatase U2; PTPase U2; PTPROt [Homo sapiens]. ACCESSION NP_109592 DBSOURCE REFSEQ: accession NM_030667.1 SOURCE Homo sapiens (human). ORGANISM Homo sapiens Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. REFERENCE 1 (residues 1 to 1216) AUTHORS Aguiar,R.C., Yakushijin,Y., Kharbanda,S., Tiwari,S., Freeman,G.J. and Shipp,M.A. TITLE PTPROt: an alternatively spliced and developmentally regulated B-lymphoid phosphatase that promotes G0/G1 arrest JOURNAL Blood 94 (7), 2403-2413 (1999) MEDLINE 99428326 REFERENCE 2 (residues 1 to 1216) AUTHORS Seimiya,H., Sawabe,T., Inazawa,J. and Tsuruo,T. TITLE Cloning, expression and chromosomal localization of a novel gene for protein tyrosine phosphatase (PTP-U2) induced by various differentiation-inducing agents JOURNAL Oncogene 10 (9), 1731-1738 (1995) MEDLINE 95273089 REFERENCE 3 (residues 1 to 1216) AUTHORS Wiggins,R.C., Wiggins,J.E., Goyal,M., Wharram,B.L. and Thomas,P.E. TITLE Molecular cloning of cDNAs encoding human GLEPP1, a membrane protein tyrosine phosphatase: characterization of the GLEPP1 protein distribution in human kidney and assignment of the GLEPP1 gene to human chromosome 12p12-p13 JOURNAL Genomics 27 (1), 174-181 (1995) MEDLINE 95394455 COMMENT REVIEWED REFSEQ: This record has been curated by NCBI staff. The reference sequence was derived from Z48541.1 and U20489.1. Summary: This gene encodes a receptor-type protein tyrosine phosphatase containing a single intracellular catalytic domain with a characteristic signature motif. The gene product, which has a transmembrane domain, is an integral membrane protein. Several alternatively spliced transcript variants, some of which encode different isoforms of the protein, have been described. These variants exhibit tissue-specific expression. Transcript Variant: This variant (1) encodes the longest isoform (a) known to date. The encoded protein has a large extracellular domain containing 8 repeats of a fibronectin type III-like motif. This variant is expressed in the glomerulus of kidney and in brain. In kidney, it may play a role in regulating glomerular epithelial cell (podocyte) structure and/or function. COMMENT This file is created by Vector NTI suite COMMENT ORIGDB|GenPept COMMENT VNTDATE|304502400| COMMENT VNTNAME|hGLEPP1 (NP_109592) PTPRO| 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..1216 /organism="Homo sapiens" /db_xref="taxon:9606" /chromosome="12" /map="12p13.3-p13.2" /vntifkey="269" Protein 1..1216 /product="receptor-type protein tyrosine phosphatase O isoform a precursor" /EC_number="3.1.3.48" /vntifkey="270" /note="glomerular epithelial protein-1; protein tyrosine phosphatase PTP-U2; phosphotyrosine phosphatase U2; PTPase U2; PTPROt" Region 1..29 /vntifkey="200" /label=Signal_1 Region 30..1216 /product="receptor-type protein tyrosine phosphatase O, isoform a" /vntifkey="203" /label=Chain_1 Region 50..813 /region_name="fibronectin type III-like motifs region" /vntifkey="266" /label=Region_1 Region 436..521 /region_name="Fibronectin type III domain" /db_xref="CDD:pfam00041" /vntifkey="1000" /label=Dom_Misc_1 /note="fn3" Region 726..805 /region_name="Fibronectin type III domain" /db_xref="CDD:pfam00041" /vntifkey="1000" /label=Dom_Misc_2 /note="fn3" Region 820..844 /region_name="transmembrane domain" /vntifkey="210" /label=Transmem_1 Region 937..1192 /region_name="Protein tyrosine phosphatase, catalytic domain" /db_xref="CDD:smart00194" /vntifkey="266" /label=Region_2 /note="PTPc" Region 1134..1144 /region_name="catalytic domain signature motif" /vntifkey="1000" /label=Dom_Misc_3 ORIGIN 1 mghlptgihg arrllpllwl fvlfknataf hvtvqddnni vvsleasdvi spasvyvvki 61 tgesknyffe feefnstlpp pvifkasyhg lyyiitlvvv ngnvvtkpsr sitvltkplp 121 vtsvsiydyk pspetgvlfe ihypekynvf trvnisyweg kdfrtmlykd ffkgktvfnh 181 wlpgmcysni tfqlvseatf nkstlveysg vshepkqhrt apyppqnisv rivnlnknnw 241 eeqsgnfpee sfmrsqdtig keklfhftee tpeipsgnis sgwpdfnssd yettsqpyww 301 dsasaapese defvsvlpme yennstlset ekstsgsfsf fpvqmiltwl ppkpptafdg 361 fhihiereen fteylmvdee ahefvaelke pgkyklsvtt fsssgscetr ksqsakslsf 421 yispsgewie eltekpqhvs vhvlssttal mswtssqeny nstivsvvsl tcqkqkesqr 481 lekqyctqvn sskpiienlv pgaqyqvviy lrkgpligpp sdpvtfaivp tgikdlmlyp 541 lgptavvlsw trpylgvfrk yvvemfyfnp atmtsewtty yeiaatvslt asvrianllp 601 awyynfrvtm vtwgdpelsc cdsstisfit apvapeitsv eyfnsllyis wtygddttdl 661 shsrmlhwmv vaegkkkikk svtrnvmtai lslppgdiyn lsvtacterg sntsmlrlvk 721 lepappkslf avnktqtsvt llwveegvad ffevfcqqvg ssqktklqep vavsshvvti 781 ssllpatayn csvtsfshds psvptfiavs tmvtemnpnv vvisvlails tlliglllvt 841 liilrkkhlq marecgagtf vnfaslerdg klpynwrrsi fafltllpsc lwtdyllafy 901 inpwsknglk krkltnpvql ddfdayikdm akdsdykfsl qfeelkligl diphfaadlp 961 lnrcknrytn ilpydfsrvr lvsmneeega dyinanyipg ynspqeyiat qgplpetrnd 1021 fwkmvlqqks qiivmltqcn ekrrvkcdhy wpfteepiay gditvemise eeqddwacrh 1081 frinyademq dvmhfnytaw pdhgvptana aesilqfvhm vrqqatkskg pmiihcsagv 1141 grtgtfiald rllqhirdhe fvdilglvse mrsyrmsmvq teeqyifihq cvqlmwmkkk 1201 qqfcisdviy envsks // LOCUS hHDPTP\(NP 1636 aa 17-MAY-2003 DEFINITION protein tyrosine phosphatase, non-receptor type 23; His-domain protein tyrosine phosphatase [Homo sapiens]. ACCESSION NP_056281 DBSOURCE REFSEQ: accession NM_015466.1 SOURCE Homo sapiens (human). ORGANISM Homo sapiens Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. REFERENCE 1 (residues 1 to 1636) AUTHORS Qu,X., Zhai,Y., Wei,H., Zhang,C., Xing,G., Lu,C., Wang,M. and He,F. TITLE Cloning, chromosomal assignment and tissue expression of a novel human protein tyrosine phosphatase (PTP-TD14) gene JOURNAL I Chuan 23 (6), 1-9 (2001) REFERENCE 2 (residues 1 to 1636) AUTHORS Toyooka,S., Ouchida,M., Jitsumori,Y., Tsukuda,K., Sakai,A., Nakamura,A., Shimizu,N. and Shimizu,K. TITLE HD-PTP: A novel protein tyrosine phosphatase gene on human chromosome 3p21.3 JOURNAL Biochem. Biophys. Res. Commun. 278 (3), 671-678 (2000) MEDLINE 20549011 COMMENT PREDICTED REFSEQ: The mRNA record is supported by experimental evidence; however, the coding sequence is predicted. The reference sequence was derived from AF290614.1. COMMENT This file is created by Vector NTI suite COMMENT ORIGDB|GenPept COMMENT VNTDATE|304502400| COMMENT VNTNAME|hHDPTP (NP_056281) PTPN23| 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..1636 /organism="Homo sapiens" /db_xref="taxon:9606" /chromosome="3" /map="3p21.3" /clone="F2896" /tissue_type="liver" /dev_stage="fetus" /vntifkey="269" Protein 1..1636 /product="protein tyrosine phosphatase, non-receptor type 23" /vntifkey="270" /note="His-domain protein tyrosine phosphatase" Region 8..161 /region_name="BRO1-like domain. This functionally uncharacterised domain is found in a number of signal transduction proteins, including Rhophilin and BRO1" /db_xref="CDD:pfam03097" /vntifkey="1000" /label=Dom_Misc_1 /note="BRO1" Region 550..711 /region_name="Chromosome segregation ATPases [Cell division and chromosome partitioning]" /db_xref="CDD:COG1196" /vntifkey="266" /label=Region_1 /note="Smc" Region 1191..1454 /region_name="Protein tyrosine phosphatase, catalytic domain" /db_xref="CDD:smart00194" /vntifkey="266" /label=Region_2 /note="PTPc" ORIGIN 1 meavprmpmi wldlkeagdf hfqpavkkfv lknygenpea yneelkklel lrqnavrvpr 61 dfegcsvlrk ylgqlhylqs rvpmgsgqea avpvtwteif sgksvahedi kyeqacilyn 121 lgalhsmlga mdkrvseegm kvscthfqca agafaylreh fpqaysvdms rqiltlnvnl 181 mlgqaqecll eksmldnrks flvarisaqv vdyykeacra lenpdtasll griqkdwkkl 241 vqmkiyyfaa vahlhmgkqa eeqqkfgerv ayfqsaldkl neaiklakgq pdtvqdalrf 301 tmdviggkyn sakkdndfiy heavpaldtl qpvkgaplvk plpvnptdpa vtgpdifakl 361 vpmaaheass lyseekakll remmakiedk nevldqfmds mqldpetvdn ldayshippq 421 lmekcaalsv rpdtvrnlvq smqvlsgvft dveaslkdir dlleedelle qkfqeavgqa 481 gaisitskae laevrrewak ymevhekasf tnselhramn lhvgnlrlls gpldqvraal 541 ptpalspedk avlqnlkril akvqemrdqr vsleqqlrel iqkdditasl vttdhsemkk 601 lfeeqlkkyd qlkvyleqnl aaqdrvlcal teanvqyaav rrvlsdldqk wnstlqtlva 661 syeayedlmk ksqegrdfya dleskvaall ertqstcqar eaarqqlldr elkkkppprp 721 tapkpllprr eeseaveagd ppeelrslpp dmvagprlpd tflgsatplh fppspfpsst 781 gpgphylsgp lppgtysgpt qliqprapgp hampvapgpa lypapaytpe lglvprsspq 841 hgvvsspyvg vgpappvagl psapppqfsg pelamavrpa tttvdsiqap ipshtaprpn 901 ptpappppcf pvpppqplpt pytypagakq pipaqhhfss gipagfpapr igpqpqphpq 961 phpsqafgpq ppqqplplqh phlfppqapg llppqspypy apqpgvlgqp ppplhtqlyp 1021 gpaqdplpah sgalpfpspg ppqpphppla ygpapstrpm gpqaapltir gpssagqstp 1081 sphlvpspap spgpgpvppr ppaaepppcl rrgaaaadll ssspesqhgg tqspgggqpl 1141 lqptkvdaae grrpqalrli erdpyehper lrqlqqelea frgqlgdvga ldtvwrelqd 1201 aqehdargrs iaiarcyslk nrhqdvmpyd snrvvlrsgk ddyinascve glspycpplv 1261 atqaplpgta adfwlmvheq kvsvivmlvs eaemekqkva ryfptergqp mvhgalslal 1321 ssvrstethv ervlslqfrd qslkrslvhl hfptwpelgl pdspsnllrf iqevhahylh 1381 qrplhtpiiv hcssgvgrtg afallyaavq eveagngipe lpqlvrrmrq qrkhmlqekl 1441 hlrfcyeavv rhveqvlqrh gvpppckpla sasisqknhl pqdsqdlvlg gdvpissiqa 1501 tiaklsirpp gglespvasl pgpaeppglp paslpestpi psssppplss plpeapqpke 1561 eppvpeapss gppssslell asltpeafsl dsslrgkqrm skhnflqahn gqglratrps 1621 ddplslldpl wtlnkt // LOCUS hHePTP\(NP 360 aa 17-MAY-2003 DEFINITION protein tyrosine phosphatase, non-receptor type 7 isoform 1; protein-tyrosine phoshatase, nonreceptor-type, stress induced; hematopoietic protein-tyrosine phosphatase [Homo sapiens]. ACCESSION NP_002823 DBSOURCE REFSEQ: accession NM_002832.2 SOURCE Homo sapiens (human). ORGANISM Homo sapiens Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. REFERENCE 1 (residues 1 to 360) AUTHORS Oh-hora,M., Ogata,M., Mori,Y., Adachi,M., Imai,K., Kosugi,A. and Hamaoka,T. TITLE Direct suppression of TCR-mediated activation of extracellular signal-regulated kinase by leukocyte protein tyrosine phosphatase, a tyrosine-specific phosphatase JOURNAL J. Immunol. 163 (3), 1282-1288 (1999) MEDLINE 99343735 REFERENCE 2 (residues 1 to 360) AUTHORS Saxena,M., Williams,S., Brockdorff,J., Gilman,J. and Mustelin,T. TITLE Inhibition of T cell signaling by mitogen-activated protein kinase-targeted hematopoietic tyrosine phosphatase (HePTP) JOURNAL J. Biol. Chem. 274 (17), 11693-11700 (1999) MEDLINE 99223488 REFERENCE 3 (residues 1 to 360) AUTHORS Saxena,M., Williams,S., Gilman,J. and Mustelin,T. TITLE Negative regulation of T cell antigen receptor signal transduction by hematopoietic tyrosine phosphatase (HePTP) JOURNAL J. Biol. Chem. 273 (25), 15340-15344 (1998) MEDLINE 98288260 REFERENCE 4 (residues 1 to 360) AUTHORS Swieter,M., Berenstein,E.H., Swaim,W.D. and Siraganian,R.P. TITLE Aggregation of IgE receptors in rat basophilic leukemia 2H3 cells induces tyrosine phosphorylation of the cytosolic protein-tyrosine phosphatase HePTP JOURNAL J. Biol. Chem. 270 (37), 21902-21906 (1995) MEDLINE 95394959 REFERENCE 5 (residues 1 to 360) AUTHORS Adachi,M., Sekiya,M., Isobe,M., Kumura,Y., Ogita,Z., Hinoda,Y., Imai,K. and Yachi,A. TITLE Molecular cloning and chromosomal mapping of a human protein-tyrosine phosphatase LC-PTP JOURNAL Biochem. Biophys. Res. Commun. 186 (3), 1607-1615 (1992) MEDLINE 92378634 REFERENCE 6 (residues 1 to 360) 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 REFERENCE 7 (sites) AUTHORS Zanke,B., Suzuki,H., Kishihara,K., Mizzen,L., Minden,M., Pawson,A. and Mak,T.W. TITLE Cloning and expression of an inducible lymphoid-specific, protein tyrosine phosphatase (HePTPase) JOURNAL Eur. J. Immunol. 22 (1), 235-239 (1992) MEDLINE 92111631 COMMENT REVIEWED REFSEQ: This record has been curated by NCBI staff. The reference sequence was derived from BC001746.1, BG340453.1, D11327.1 and M64322.1. On Jan 25, 2002 this sequence version replaced gi:4506299. 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 gene is preferentially expressed in a variety of hematopoietic cells, and is an early response gene in lymphokine stimulated cells. The noncatalytic N-terminus of this PTP can interact with MAP kinases and suppress the MAP kinase activities. This PTP was shown to be involved in the regulation of T cell antigen receptor (TCR) signaling, which was thought to function through dephosphorylating the molecules related to MAP kinase pathway. Three alternatively spliced transcript variants of this gene, which encode two distinct isoforms, are reported. Transcript Variant: This variant (1) contains a different 5' region, which includes a part of the coding sequence when compared to variant 2. It thus encodes a protein that has a shorter N-terminus, as compared to isoform 2. COMMENT This file is created by Vector NTI suite COMMENT ORIGDB|GenPept COMMENT VNTDATE|304502400| COMMENT VNTNAME|hHePTP (NP_002823) PTPN7| 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..360 /organism="Homo sapiens" /db_xref="taxon:9606" /chromosome="1" /map="1q32.1" /vntifkey="269" Protein 1..360 /product="protein tyrosine phosphatase, non-receptor type 7 isoform 1" /vntifkey="270" /note="protein-tyrosine phoshatase, nonreceptor-type, stress induced; hematopoietic protein-tyrosine phosphatase" Region 96..350 /region_name="Protein tyrosine phosphatase, catalytic domain" /db_xref="CDD:smart00194" /vntifkey="266" /label=Region_1 /note="PTPc" ORIGIN 1 mvqahggrsr aqpltlslga amtqpppekt pakkhvrlqe rrgsnvalml dvrslgavep 61 icsvntprev tlhflrtagh pltrwalqrq ppspkqleee flkipsnfvs pedldipgha 121 skdryktilp npqsrvclgr aqsqedgdyi nanyirgydg kekvyiatqg pmpntvsdfw 181 emvwqeevsl ivmltqlreg kekcvhywpt eeetygpfqi riqdmkecpe ytvrqltiqy 241 qeerrsvkhi lfsawpdhqt pesagpllrl vaeveespet aahpgpivvh csagigrtgc 301 fiatrigcqq lkargevdil givcqlrldr ggmiqtaeqy qflhhtlaly agqlpeepsp // LOCUS hIA2\(NP_0 979 aa 17-MAY-2003 DEFINITION protein tyrosine phosphatase, receptor type, N precursor; islet cell antigen 2; islet cell antigen 512; islet cell autoantigen 3; protein tyrosine phosphatase-like N precursor [Homo sapiens]. ACCESSION NP_002837 DBSOURCE REFSEQ: accession NM_002846.2 SOURCE Homo sapiens (human). ORGANISM Homo sapiens Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. REFERENCE 1 (residues 1 to 979) AUTHORS Sanjeevi,C.B., Das,A.K. and Shtauvere-Brameus,A. TITLE BCG vaccination and GAD65 and IA-2 autoantibodies in autoimmune diabetes in southern India JOURNAL Ann. N. Y. Acad. Sci. 958, 293-296 (2002) MEDLINE 22015049 REMARK GeneRIF: BCG vaccination and GAD65 and IA-2 autoantibodies in autoimmune diabetes in southern India. REFERENCE 2 (residues 1 to 979) AUTHORS Kawasaki,E., Yamaguchi,H., Hattori,H., Egashira,T. and Eguchi,K. TITLE Autoantibodies to IA-2 in type 1 diabetes: measurements with a new enzyme-linked immunosorbent assay JOURNAL Ann. N. Y. Acad. Sci. 958, 241-246 (2002) MEDLINE 22015037 REMARK GeneRIF: Autoantibodies to IA-2 in type 1 diabetes: measurements with a new enzyme-linked immunosorbent assay. REFERENCE 3 (residues 1 to 979) AUTHORS Miao,D., Yu,L., Tiberti,C., Cuthbertson,D.D., Rewers,M., di Mario,U., Eisenbarth,G.S. and Dotta,F. TITLE ICA512(IA-2) epitope specific assays distinguish transient from diabetes associated autoantibodies JOURNAL J. Autoimmun. 18 (2), 191-196 (2002) MEDLINE 21906940 REMARK GeneRIF: ICA512(IA-2) epitope specific assays distinguish transient from diabetes associated autoantibodies. REFERENCE 4 (residues 1 to 979) AUTHORS Mikulecky,M. and Michalkova,D. TITLE Secular and seasonal cycling of IA2-ab autoantibody in Slovak diabetic children JOURNAL Biomed. Pharmacother. 55 Suppl 1, 106S-109S (2001) MEDLINE 21630621 REFERENCE 5 (residues 1 to 979) AUTHORS Cui,L., Yu,W.P., DeAizpurua,H.J., Schmidli,R.S. and Pallen,C.J. TITLE Cloning and characterization of islet cell antigen-related protein-tyrosine phosphatase (PTP), a novel receptor-like PTP and autoantigen in insulin-dependent diabetes JOURNAL J. Biol. Chem. 271 (40), 24817-24823 (1996) MEDLINE 96394649 REFERENCE 6 (residues 1 to 979) AUTHORS van den Maagdenberg,A.M., Olde Weghuis,D., Rijss,J., van de Wetering,R.A., Wieringa,B., Geurts van Kessel,A. and Hendriks,W.J. TITLE Assignment of the human gene for receptor-type protein tyrosine phosphatase IA-2 (PTPRN) to chromosome region 2q35 --> q36.1 and identification of an intragenic genetic marker JOURNAL Cytogenet. Cell Genet. 73 (1-2), 145-148 (1996) MEDLINE 96244610 REFERENCE 7 (residues 1 to 979) AUTHORS Lan,M.S., Lu,J., Goto,Y. and Notkins,A.L. TITLE Molecular cloning and identification of a receptor-type protein tyrosine phosphatase, IA-2, from human insulinoma JOURNAL DNA Cell Biol. 13 (5), 505-514 (1994) MEDLINE 94296553 REFERENCE 8 (residues 1 to 979) AUTHORS Rabin,D.U., Pleasic,S.M., Shapiro,J.A., Yoo-Warren,H., Oles,J., Hicks,J.M., Goldstein,D.E. and Rae,P.M. TITLE Islet cell antigen 512 is a diabetes-specific islet autoantigen related to protein tyrosine phosphatases JOURNAL J. Immunol. 152 (6), 3183-3188 (1994) MEDLINE 94194080 COMMENT REVIEWED REFSEQ: This record has been curated by NCBI staff. The reference sequence was derived from L18983.1, AF042285.4 and BC007713.1. 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 a single catalytic domain, and thus represents a receptor-type PTP. This PTP was found to be an autoantigen that is reactive with insulin-dependent diabetes mellitus (IDDM) patient sera, and thus may be a potential target of autoimmunity in diabetes mellitus. COMMENT This file is created by Vector NTI suite COMMENT ORIGDB|GenPept COMMENT VNTDATE|304502400| COMMENT VNTNAME|hIA2 (NP_002837) PTPRN| 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..979 /organism="Homo sapiens" /db_xref="taxon:9606" /chromosome="2" /map="2q35-q36.1" /vntifkey="269" Protein 1..979 /product="protein tyrosine phosphatase, receptor type, N precursor" /EC_number="3.1.3.48" /vntifkey="270" /note="islet cell antigen 2; islet cell antigen 512; islet cell autoantigen 3; protein tyrosine phosphatase-like N precursor" Region 1..25 /vntifkey="200" /label=Signal_1 Region 26..979 /product="protein tyrosine phosphatase, receptor type, N" /vntifkey="203" /label=Chain_1 Region 709..970 /region_name="Protein tyrosine phosphatase, catalytic domain" /db_xref="CDD:smart00194" /vntifkey="266" /label=Region_1 /note="PTPc" ORIGIN 1 mrrprrpggl ggsgglrlll cllllssrpg gcsavsahgc lfdrrlcshl evciqdglfg 61 qcqvgvgqar pllqvtspvl qrlqgvlrql msqglswhdd ltqyvisqem eriprlrppe 121 prprdrsgla pkrpgpagel llqdiptgsa paaqhrlpqp pvgkggagas sslsplqael 181 lppllehlll ppqpphpsls yepallqpyl fhqfgsrdgs rvsegspgmv svgplpkaea 241 palfsrtask gifgdhpghs ygdlpgpspa qlfqdsglly laqelpapsr arvprlpeqg 301 sssraedspe gyekeglgdr gekpaspavq pdaalqrlaa vlagygvelr qltpeqlstl 361 ltllqllpkg agrnpggvvn vgadikktme gpvegrdtae lpartspmpg hptasptsse 421 vqqvpspvss eppkaarppv tpvllekksp lgqsqptvag qpsarpaaee ygyivtdqkp 481 lslaagvkll eilaehvhms sgsfinisvv gpaltfrirh neqnlsladv tqqaglvkse 541 leaqtglqil qtgvgqreea aavlpqtahs tspmrsvllt lvalagvagl lvalavalcv 601 rqharqqdke rlaalgpega hgdttfeyqd lcrqhmatks lfnraegppe psrvssvssq 661 fsdaaqasps shsstpswce epaqanmdis tghmilayme dhlrnrdrla kewqalcayq 721 aepntcataq gegnikknrh pdflpydhar iklkvessps rsdyinaspi iehdprmpay 781 iatqgplsht iadfwqmvwe sgctvivmlt plvedgvkqc drywpdegas lyhvyevnlv 841 sehiwcedfl vrsfylknvq tqetrtltqf hflswpaegt pastrplldf rrkvnkcyrg 901 rscpiivhcs dgagrtgtyi lidmvlnrma kgvkeidiaa tlehvrdqrp glvrskdqfe 961 faltavaeev nailkalpq // LOCUS hIA2beta\( 1015 aa 17-MAY-2003 DEFINITION protein tyrosine phosphatase, receptor type, N polypeptide 2 isoform 1 precursor; protein tyrosine phosphatase receptor pi; phogrin; tyrosine phosphatase IA-2 beta; IAR/receptor-like protein-tyrosine phosphatase [Homo sapiens]. ACCESSION NP_002838 DBSOURCE REFSEQ: accession NM_002847.2 SOURCE Homo sapiens (human). ORGANISM Homo sapiens Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. REFERENCE 1 (residues 1 to 1015) AUTHORS van den Maagdenberg,A.M., Schepens,J.T., Schepens,M.T., Pepers,B., Wieringa,B., van Kessel,A.G. and Hendriks,W.J. TITLE Assignment of Ptprn2, the gene encoding receptor-type protein tyrosine phosphatase IA-2beta, a major autoantigen in insulin-dependent diabetes mellitus, to mouse chromosome region 12F JOURNAL Cytogenet. Cell Genet. 82 (3-4), 153-155 (1998) MEDLINE 99077744 REFERENCE 2 (residues 1 to 1015) AUTHORS Schmidli,R.S., Colman,P.G., Cui,L., Yu,W.P., Kewming,K., Jankulovski,C., Harrison,L.C., Pallen,C.J. and DeAizpurua,H.J. TITLE Antibodies to the protein tyrosine phosphatases IAR and IA-2 are associated with progression to insulin-dependent diabetes (IDDM) in first-degree relatives at-risk for IDDM JOURNAL Autoimmunity 28 (1), 15-23 (1998) MEDLINE 98425805 REFERENCE 3 (residues 1 to 1015) AUTHORS Li,Q., Borovitskaya,A.E., DeSilva,M.G., Wasserfall,C., Maclaren,N.K., Notkins,A.L. and Lan,M.S. TITLE Autoantigens in insulin-dependent diabetes mellitus: molecular cloning and characterization of human IA-2 beta JOURNAL Proc. Assoc. Am. Physicians 109 (4), 429-439 (1997) MEDLINE 97364262 REFERENCE 4 (residues 1 to 1015) AUTHORS Smith,P.D., Barker,K.T., Wang,J., Lu,Y.J., Shipley,J. and Crompton,M.R. TITLE ICAAR, a novel member of a new family of transmembrane, tyrosine phosphatase-like proteins JOURNAL Biochem. Biophys. Res. Commun. 229 (2), 402-411 (1996) MEDLINE 97127415 REFERENCE 5 (residues 1 to 1015) AUTHORS Kawasaki,E., Hutton,J.C. and Eisenbarth,G.S. TITLE Molecular cloning and characterization of the human transmembrane protein tyrosine phosphatase homologue, phogrin, an autoantigen of type 1 diabetes JOURNAL Biochem. Biophys. Res. Commun. 227 (2), 440-447 (1996) MEDLINE 97032784 REFERENCE 6 (residues 1 to 1015) AUTHORS Cui,L., Yu,W.P., DeAizpurua,H.J., Schmidli,R.S. and Pallen,C.J. TITLE Cloning and characterization of islet cell antigen-related protein-tyrosine phosphatase (PTP), a novel receptor-like PTP and autoantigen in insulin-dependent diabetes JOURNAL J. Biol. Chem. 271 (40), 24817-24823 (1996) MEDLINE 96394649 COMMENT REVIEWED REFSEQ: This record has been curated by NCBI staff. The reference sequence was derived from U66702.1 and AF007555.1. 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 a single intracellular catalytic domain, and thus represents a receptor-type PTP. The catalytic domain of this PTP is most closely related to PTPRN/IA-2beta. This PTP and PTPRN are both found to be major autoantigens associated with insulin-dependent diabetes mellitus. Three alternatively spliced transcript variants of this gene, 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|304502400| COMMENT VNTNAME|hIA2beta (NP_002838) PTPRN2| 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..1015 /organism="Homo sapiens" /db_xref="taxon:9606" /chromosome="7" /map="7q36" /vntifkey="269" Protein 1..1015 /product="protein tyrosine phosphatase, receptor type, N polypeptide 2 isoform 1 precursor" /vntifkey="270" /note="protein tyrosine phosphatase receptor pi; phogrin; tyrosine phosphatase IA-2 beta; IAR/receptor-like protein-tyrosine phosphatase" Region 1..21 /vntifkey="200" /label=Signal_1 Region 22..1015 /product="protein tyrosine phosphatase, receptor type, N polypeptide 2, isoform 1" /vntifkey="203" /label=Chain_1 Region 745..1006 /region_name="Protein tyrosine phosphatase, catalytic domain" /db_xref="CDD:smart00194" /vntifkey="266" /label=Region_1 /note="PTPc" ORIGIN 1 mgpplpllll lllllpprvl paapssvprg rqlpgrlgcl leeglcgase acvndgvfgr 61 cqkvpamdfy ryevspvalq rlrvalqkls gtgftwqddy tqyvmdqela dlpktylrrp 121 eassparpsk hsvgserrys reggaalana lrrhlpflea lsqapasdvl arthtaqdrp 181 paegddrfse siltyvahts altyppgprt qlredllprt lgqlqpdels pkvdsgvdrh 241 hlmaalsaya aqrppappge gslepqyllr apsrmprpll apaapqkwps plgdsedpss 301 tgdgarihtl lkdlqrqpae vrglsgleld gmaelmaglm qgvdhgvarg spgraalges 361 geqadgpkat lrgdsfpddg vqddddrlyq evhrlsatlg gllqdhgsrl lpgalpfarp 421 ldmerkkseh pesslsseee tagvenvksq tyskdllgqq phsepgaaaf gelqnqmpgp 481 skeeqslpag aqealsdglq levqpseeea rgyivtdrdp lrpeegrrlv edvarllqvp 541 ssafadvevl gpavtfkvsa nvqnvttedv ekatvdnkdk leetsglkil qtgvgskskl 601 kflppqaeqe dstkfialtl vslacilgvl lasgliyclr hssqhrlkek lsglggdpga 661 dataayqelc rqrmatrppd rpegphtsri ssvssqfsdg pipspsarss asswseepvq 721 snmdistghm ilsymedhlk nknrlekewe alcayqaepn ssfvaqreen vpknrslavl 781 tydhsrvllk aenshshsdy inaspimdhd prnpayiatq gplpatvadf wqmvwesgcv 841 vivmltplae ngvrqcyhyw pdegsnlyhi yevnlvsehi wcedflvrsf ylknlqtnet 901 rtvtqfhfls wydrgvpsss rslldfrrkv nkcyrgrscp iivhcsdgag rsgtyvlidm 961 vlnkmakgak eidiaatleh lrdqrpgmvq tkeqfefalt avaeevnail kalpq // LOCUS hLAR\(NP_0 1897 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|304502400| COMMENT VNTNAME|hLAR (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..1897 /organism="Homo sapiens" /db_xref="taxon:9606" /chromosome="1" /map="1p34" /vntifkey="269" Protein 1..1897 /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..16 /vntifkey="200" /label=Signal_1 Region 17..1897 /product="protein tyrosine phosphatase, receptor type, F, isoform 1" /vntifkey="203" /label=Chain_1 Region 29..115 /region_name="Immunoglobulin" /db_xref="CDD:smart00409" /vntifkey="266" /label=Region_1 /note="IG" Region 140..204 /region_name="Immunoglobulin C-2 Type" /db_xref="CDD:smart00408" /vntifkey="266" /label=Region_2 /note="IGc2" Region 228..306 /region_name="Immunoglobulin" /db_xref="CDD:smart00409" /vntifkey="266" /label=Region_3 /note="IG" Region 333..391 /region_name="Fibronectin type III domain" /db_xref="CDD:pfam00041" /vntifkey="1000" /label=Dom_Misc_1 /note="fn3" Region 407..490 /region_name="Fibronectin type III domain" /db_xref="CDD:pfam00041" /vntifkey="1000" /label=Dom_Misc_2 /note="fn3" Region 502..581 /region_name="Fibronectin type 3 domain" /db_xref="CDD:smart00060" /vntifkey="1000" /label=Dom_Misc_3 /note="FN3" Region 600..686 /region_name="Fibronectin type III domain" /db_xref="CDD:pfam00041" /vntifkey="1000" /label=Dom_Misc_4 /note="fn3" Region 824..893 /region_name="Fibronectin type III domain" /db_xref="CDD:pfam00041" /vntifkey="1000" /label=Dom_Misc_5 /note="fn3" Region 909..990 /region_name="Fibronectin type III domain" /db_xref="CDD:pfam00041" /vntifkey="1000" /label=Dom_Misc_6 /note="fn3" Region 1341..1596 /region_name="Protein tyrosine phosphatase, catalytic domain" /db_xref="CDD:smart00194" /vntifkey="266" /label=Region_4 /note="PTPc" Region 1632..1889 /region_name="Protein tyrosine phosphatase, catalytic domain" /db_xref="CDD:smart00194" /vntifkey="266" /label=Region_5 /note="PTPc" ORIGIN 1 mvplvpalvm lglvagahgd skpvfikvpe dqtglsggva sfvcqatgep kpritwmkkg 61 kkvssqrfev iefddgagsv lriqplrvqr deaiyectat nslgeintsa klsvleeeql 121 ppgfpsidmg pqlkvvekar tatmlcaagg npdpeiswfk dflpvdpats ngrikqlrsg 181 alqiessees dqgkyecvat nsagtrysap anlyvrvrrv aprfsippss qevmpggsvn 241 ltcvavgapm pyvkwmmgae eltkedempv grnvlelsnv vrsanytcva isslgmieat 301 aqvtvkalpk ppidlvvtet tatsvtltwd sgnsepvtyy giqyraagte gpfqevdgva 361 ttrysiggls pfseyafrvl avnsigrgpp seavrartge qapsspprrv qarmlsastm 421 lvqweppeep nglvrgyrvy ytpdsrrppn awhkhntdag llttvgsllp gityslrvla 481 ftavgdgpps ptiqvktqqg vpaqpadfqa evesdtriql swllppqeri imyelvywaa 541 ededqqhkvt fdptssytle dlkpdtlyrf qlaarsdmgv gvftptiear taqstpsapp 601 qkvmcvsmgs ttvrvswvpp padsrngvit qysvaheavd gedrgrhvvd gisrehsswd 661 lvglekwtey rvwvrahtdv gpgpesspvl vrtdedvpsg pprkvevepl nstavhvywk 721 lpvpskqhgq irgyqvtyvr lengeprglp iiqdvmlaea qwrpeesedy ettisgltpe 781 ttysvtvaay ttkgdgarsk pkivtttgav pgrptmmist tamntallqw hppkelpgel 841 lgyrlqycra dearpntidf gkddqhftvt glhkgttyif rlaaknragl geefekeirt 901 pedlpsgfpq nlhvtgltts ttelawdppv laerngriis ytvvfrdins qqelqnittd 961 trftltglkp dttydikvra wtskgsgpls psiqsrtmpv eqvfaknfrv aaamktsvll 1021 swevpdsyks avpfkilyng qsvevdghsm rkliadlqpn teysfvlmnr gssagglqhl 1081 vsirtapdll phkplpasay iedgrfdlsm phvqdpslvr wfyivvvpid rvggsmltpr 1141 wstpeeleld elleaieqgg eeqrrrrrqa erlkpyvaaq ldvlpetftl gdkknyrgfy 1201 nrplspdlsy qcfvlaslke pmdqkryass pysdeivvqv tpaqqqeepe mlwvtgpvla 1261 viliilivia illfkrkrth spsskdeqsi glkdsllahs sdpvemrrln yqtpgmrdhp 1321 pipitdladn ierlkandgl kfsqeyesid pgqqftwens nlevnkpknr yanviaydhs 1381 rviltsidgv pgsdyinany idgyrkqnay iatqgplpet mgdfwrmvwe qrtatvvmmt 1441 rleeksrvkc dqywpargte tcgliqvtll dtvelatytv rtfalhksgs sekrelrqfq 1501 fmawpdhgvp eyptpilafl rrvkacnpld agpmvvhcsa gvgrtgcfiv idamlermkh 1561 ektvdiyghv tcmrsqrnym vqtedqyvfi healleaatc ghtevparnl yahiqklgqv 1621 ppgesvtame lefkllassk ahtsrfisan lpcnkfknrl vnimpyeltr vclqpirgve 1681 gsdyinasfl dgyrqqkayi atqgplaest edfwrmlweh nstiivmltk lremgrekch 1741 qywpaersar yqyfvvdpma eynmpqyilr efkvtdardg qsrtirqfqf tdwpeqgvpk 1801 tgegfidfig qvhktkeqfg qdgpitvhcs agvgrtgvfi tlsivlermr yegvvdmfqt 1861 vktlrtqrpa mvqtedqyql cyraaleylg sfdhyat // LOCUS hLyPTP\(NP 807 aa 17-MAY-2003 DEFINITION lymphoid-specific protein tyrosine phosphatase isoform 1; lymphoid-specific protein tyrosine phosphatase; protein tyrosine phosphatase homolog [Homo sapiens]. ACCESSION NP_057051 DBSOURCE REFSEQ: accession NM_015967.2 SOURCE Homo sapiens (human). ORGANISM Homo sapiens Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. REFERENCE 1 (residues 1 to 807) AUTHORS Hill,R.J., Zozulya,S., Lu,Y.L., Ward,K., Gishizky,M. and Jallal,B. TITLE The lymphoid protein tyrosine phosphatase Lyp interacts with the adaptor molecule Grb2 and functions as a negative regulator of T-cell activation JOURNAL Exp. Hematol. 30 (3), 237-244 (2002) MEDLINE 21876996 REMARK GeneRIF: data demonstrate a novel interaction between Lyp and the adaptor Grb2 and are consistent with a negative regulatory role for Lyp in T-cell signaling. REFERENCE 2 (residues 1 to 807) AUTHORS Cohen,S., Dadi,H., Shaoul,E., Sharfe,N. and Roifman,C.M. TITLE Cloning and characterization of a lymphoid-specific, inducible human protein tyrosine phosphatase, Lyp JOURNAL Blood 93 (6), 2013-2024 (1999) MEDLINE 99168989 COMMENT REVIEWED REFSEQ: This record has been curated by NCBI staff. The reference sequence was derived from AF077031.1 and AF001846.1. Summary: This gene encodes a protein tyrosine phosphatase which is expressed primarily in lymphoid tissues. This enzyme associates with the molecular adapter protein CBL and may be involved in regulating CBL function in the T-cell receptor signaling pathway. Alternative splicing of this gene results in two transcript variants encoding distinct isoforms. Transcript Variant: This variant (1) encodes the longer isoform (1) which is 116 aa longer than isoform 2 and has a distinct C-terminus. COMMENT This file is created by Vector NTI suite COMMENT ORIGDB|GenPept COMMENT VNTDATE|304502400| COMMENT VNTNAME|hLyPTP (NP_057051) PTPN22| 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..807 /organism="Homo sapiens" /db_xref="taxon:9606" /chromosome="1" /map="1p13.3-p13.1" /vntifkey="269" Protein 1..807 /product="lymphoid-specific protein tyrosine phosphatase isoform 1" /vntifkey="270" /note="lymphoid-specific protein tyrosine phosphatase; protein tyrosine phosphatase homolog" Region 24..291 /region_name="Protein tyrosine phosphatase, catalytic domain" /db_xref="CDD:smart00194" /vntifkey="266" /label=Region_1 /note="PTPc" ORIGIN 1 mdqreilqkf ldeaqskkit keefaneflk lkrqstkyka dktypttvae kpknikknry 61 kdilpydysr velslitsde dssyinanfi kgvygpkayi atqgplsttl ldfwrmiwey 121 svliigmacm eyemgkkkce rywaepvemq lefgpfsvsc eaekrksdyi irtlkvkfns 181 etrtiyqfhy knwpdhdvps sidpileliw dvrcyqedds vpicihcsag cgrtgvicai 241 dytwmllkdg iipenfsvfs liremrtqrp slvqtqeqye lvynavlelf krqmdvirdk 301 hsgtesqakh cipeknhtlq adsyspnlpk sttkaakmmn qqrtkmeike sssfdfrtse 361 isakeelvlh paksstsfdf lelnysfdkn adttmkwqtk afpivgeplq khqsldlgsp 421 lfegcsnskp vnaagryfns kvpitrtkst pfeliqqret kevdskenfs ylesqphdsc 481 fvemqaqkvm hvssaelnys lpydskhqir nasnvkhhds salgvysyip lvenpyfssw 541 ppsgtsskms ldlpekqdgt vfpssllpts stslfsyyns hdslslnspt nissllnqes 601 avlataprid deippplpvw tpesfivvee agefspnvpk slssavkvki gtslewggts 661 epkkfddsvi lrpsksvklr spkselhqdr sspppplper tlesfflade dcmqaqsiet 721 ystsypdtme nstsskqtlk tsgksftrsk slkilrnmkk sicnscppnk paesvqsnns 781 ssflnfgfan rfskpkgprn ppptwni // LOCUS hMEG1\(NP_ 926 aa 17-MAY-2003 DEFINITION protein tyrosine phosphatase, non-receptor type 4; megakaryocyte phosphatase; PTPase-MEG1; protein tyrosine phosphatase MEG1; megakaryocyte protein-tyrosine phosphatase [Homo sapiens]. ACCESSION NP_002821 DBSOURCE REFSEQ: accession NM_002830.2 SOURCE Homo sapiens (human). ORGANISM Homo sapiens Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. REFERENCE 1 (residues 1 to 926) AUTHORS Hironaka,K., Umemori,H., Tezuka,T., Mishina,M. and Yamamoto,T. TITLE The protein-tyrosine phosphatase PTPMEG interacts with glutamate receptor delta 2 and epsilon subunits JOURNAL J. Biol. Chem. 275 (21), 16167-16173 (2000) MEDLINE 20283654 REFERENCE 2 (residues 1 to 926) AUTHORS Gu,M., Meng,K. and Majerus,P.W. TITLE The effect of overexpression of the protein tyrosine phosphatase PTPMEG on cell growth and on colony formation in soft agar in COS-7 cells JOURNAL Proc. Natl. Acad. Sci. U.S.A. 93 (23), 12980-12985 (1996) MEDLINE 97075104 REFERENCE 3 (residues 1 to 926) AUTHORS Gu,M. and Majerus,P.W. TITLE The properties of the protein tyrosine phosphatase PTPMEG JOURNAL J. Biol. Chem. 271 (44), 27751-27759 (1996) MEDLINE 97066967 REFERENCE 4 (residues 1 to 926) AUTHORS Gu,M.X., York,J.D., Warshawsky,I. and Majerus,P.W. TITLE Identification, cloning, and expression of a cytosolic megakaryocyte protein-tyrosine-phosphatase with sequence homology to cytoskeletal protein 4.1 JOURNAL Proc. Natl. Acad. Sci. U.S.A. 88 (13), 5867-5871 (1991) MEDLINE 91288564 COMMENT REVIEWED REFSEQ: This record has been curated by NCBI staff. The reference sequence was derived from M68941.1 and BC010674.1. 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 protein contains a C-terminal PTP domain and an N-terminal domain homologous to the band 4.1 superfamily of cytoskeletal-associated proteins. This PTP has been shown to interact with glutamate receptor delta 2 and epsilon subunits, and is thought to play a role in signalling downstream of the glutamate receptors through tyrosine dephosphorylation. COMMENT This file is created by Vector NTI suite COMMENT ORIGDB|GenPept COMMENT VNTDATE|304502400| COMMENT VNTNAME|hMEG1 (NP_002821) PTPN4| 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..926 /organism="Homo sapiens" /db_xref="taxon:9606" /chromosome="2" /map="2q14.1" /vntifkey="269" Protein 1..926 /product="protein tyrosine phosphatase, non-receptor type 4" /EC_number="3.1.3.48" /vntifkey="270" /note="megakaryocyte phosphatase; PTPase-MEG1; protein tyrosine phosphatase MEG1; megakaryocyte protein-tyrosine phosphatase" Region 31..222 /region_name="FERM domain (Band 4.1 family). This domain has been renamed the FERM domain, which stands for F for 4.1, E for Ezrin, R for radixin and M for moesin" /db_xref="CDD:pfam00373" /vntifkey="1000" /label=Dom_Misc_1 /note="Band_41" Region 517..604 /region_name="PDZ domain (Also known as DHR or GLGF). PDZ domains are found in diverse signaling proteins" /db_xref="CDD:pfam00595" /vntifkey="1000" /label=Dom_Misc_2 /note="PDZ" Region 655..913 /region_name="Protein tyrosine phosphatase, catalytic domain" /db_xref="CDD:smart00194" /vntifkey="266" /label=Region_1 /note="PTPc" ORIGIN 1 mtsrfrlpag rtynvrasel ardrqhtevv cnillldntv qafkvnkhdq gqvlldvvfk 61 hldlteqdyf glqladdstd nprwldpnkp irkqlkrgsp yslnfrvkff vsdpnklqee 121 ytryqyflqi kqdiltgrlp cpsntaalla sfavqselgd ydqsenlsgy lsdysfipnq 181 pqdfekeiak lhqqhiglsp aeaefnylnt artlelygve fhyardqsnn eimigvmsgg 241 iliyknrvrm ntfpwlkivk isfkckqffi qlrkelhesr etllgfnmvn yracknlwka 301 cvehhtffrl drplppqknf fahyftlgsk frycgrtevq svqygkekan kdrvfarsps 361 kplarklmdw evvsrnsisd drletqslps rsppgtpnhr nstftqegtr lrpssvghlv 421 dhmvhtspse vfvnqrspss tqansivles spsqetpgdg kppalppkqs kknswnqihy 481 shsqqdlesh inetfdipss pekptpnggi phdnlvlirm kpdengrfgf nvkggydqkm 541 pvivsrvapg tpadlcvprl negdqvvlin grdiaehthd qvvlfikasc erhsgelmll 601 vrpnavydvv eeklenepdf qyipekapld svhqddhslr esmiqlaegl itgtvltqfd 661 qlyrkkpgmt mscaklpqni sknryrdisp ydatrvilkg nedyinanyi nmeipsssii 721 nqyiacqgpl phtctdfwqm tweqgssmvv mlttqvergr vkchqywpep tgsssygcyq 781 vtchseegnt ayifrkmtlf nqeknesrpl tqiqyiawpd hgvpddssdf ldfvchvrnk 841 ragkeepvvv hcsagigrtg vlitmetamc liecnqpvyp ldivrtmrdq rammiqtpsq 901 yrfvceailk vyeegfvkpl ttstnk // LOCUS hMEG2\(NP_ 593 aa 17-MAY-2003 DEFINITION protein tyrosine phosphatase, non-receptor type 9; protein-tyrosine phosphatase MEG2; PTPase-MEG2 [Homo sapiens]. ACCESSION NP_002824 DBSOURCE REFSEQ: accession NM_002833.2 SOURCE Homo sapiens (human). ORGANISM Homo sapiens Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. REFERENCE 1 (residues 1 to 593) AUTHORS Qi,Y., Zhao,R., Cao,H., Sui,X., Krantz,S.B. and Zhao,Z.J. TITLE Purification and characterization of protein tyrosine phosphatase PTP-MEG2 JOURNAL J. Cell. Biochem. 86 (1), 79-89 (2002) MEDLINE 22106294 REMARK GeneRIF: Purification and characterization of protein tyrosine phosphatase PTP-MEG2 REFERENCE 2 (residues 1 to 593) AUTHORS Kruger,J.M., Fukushima,T., Cherepanov,V., Borregaard,N., Loeve,C., Shek,C., Sharma,K., Tanswell,A.K., Chow,C.W. and Downey,G.P. TITLE Protein-tyrosine phosphatase MEG2 is expressed by human neutrophils. Localization to the phagosome and activation by polyphosphoinositides JOURNAL J. Biol. Chem. 277 (4), 2620-2628 (2002) MEDLINE 21659736 REFERENCE 3 (residues 1 to 593) AUTHORS Gu,M., Warshawsky,I. and Majerus,P.W. TITLE Cloning and expression of a cytosolic megakaryocyte protein-tyrosine-phosphatase with sequence homology to retinaldehyde-binding protein and yeast SEC14p JOURNAL Proc. Natl. Acad. Sci. U.S.A. 89 (7), 2980-2984 (1992) MEDLINE 92212952 COMMENT REVIEWED REFSEQ: This record has been curated by NCBI staff. The reference sequence was derived from M83738.1. 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 N-terminal domain that shares a significant similarity with yeast SEC14, which is a protein that has phosphatidylinositol transfer activity and is required for protein secretion through the Golgi complex in yeast. This PTP was found to be activated by polyphosphoinositide, and is thought to be involved in signaling events regulating phagocytosis. COMMENT This file is created by Vector NTI suite COMMENT ORIGDB|GenPept COMMENT VNTDATE|304502400| COMMENT VNTNAME|hMEG2 (NP_002824) PTPN9| 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..593 /organism="Homo sapiens" /db_xref="taxon:9606" /chromosome="15" /map="15q23" /vntifkey="269" Protein 1..593 /product="protein tyrosine phosphatase, non-receptor type 9" /EC_number="3.1.3.48" /vntifkey="270" /note="protein-tyrosine phosphatase MEG2; PTPase-MEG2" Region 10..80 /region_name="CRAL/TRIO, N-terminus. This all-alpha domain is found to the N-terminus of pfam00650" /db_xref="CDD:pfam03765" /vntifkey="1000" /label=Dom_Misc_1 /note="CRAL_TRIO_N" Region 84..266 /region_name="CRAL/TRIO domain. The original profile has been extended to include the carboxyl domain from the known structure of Sec14" /db_xref="CDD:pfam00650" /vntifkey="1000" /label=Dom_Misc_2 /note="CRAL_TRIO" Region 302..576 /region_name="Protein tyrosine phosphatase, catalytic domain" /db_xref="CDD:smart00194" /vntifkey="266" /label=Region_1 /note="PTPc" ORIGIN 1 mepataprpd mapeltpeee qatkqfleei nkwtvqynvs plswnvavkf lmarkfdvlr 61 aielfhsyre trrkegivkl kpheeplrse ilsgkftiln vrdptgasia lftarlhhph 121 ksvqhvvlqa lfylldravd sfetqrnglv fiydmcgsny anfeldlgkk vlnllkgafp 181 arlkkvlivg apiwfrvpys iislllkdkv reriqilkts evtqhlprec lpenlggyvk 241 idlatwnfqf lpqvnghpdp fdeiilfslp paldwdsvhv pgphamtiqe lvdyvnarqk 301 qgiyeeyedi rrenpvgtfh csmspgnlek nrygdvpcld qtrvkltkrs ghtqtdyina 361 sfmdgykqkn ayigtqgple ntyrdfwlmv weqkvlvivm ttrfeeggrr kcgqywplek 421 dsrirfgflt vtnlgvenmn hykkttleih nteerqkrqv thfqflswpd ygvpssaasl 481 idflrvvrnq qslavsnmga rskgqcpepp ivvhcsagig rtgtfcsldi claqleelgt 541 lnvfqtvsrm rtqrafsiqt peqyyfcyka ilefaekegm vssgqnllav esq // LOCUS hPCPTP1\(N 657 aa 17-MAY-2003 DEFINITION protein tyrosine phosphatase, receptor type, R isoform 1 precursor; protein tyrosine phosphatase, receptor type, Q; protein-tyrosine phosphatase NC-PTPCOM1; protein tyrosine phosphatase Cr1PTPase precursor; Ch-1 PTPase [Homo sapiens]. ACCESSION NP_002840 DBSOURCE REFSEQ: accession NM_002849.2 SOURCE Homo sapiens (human). ORGANISM Homo sapiens Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. REFERENCE 1 (residues 1 to 657) AUTHORS Blanco-Aparicio,C., Torres,J. and Pulido,R. TITLE A novel regulatory mechanism of MAP kinases activation and nuclear translocation mediated by PKA and the PTP-SL tyrosine phosphatase JOURNAL J. Cell Biol. 147 (6), 1129-1136 (1999) MEDLINE 20069779 REFERENCE 2 (residues 1 to 657) AUTHORS Shiozuka,K., Watanabe,Y., Ikeda,T., Hashimoto,S. and Kawashima,H. TITLE Cloning and expression of PCPTP1 encoding protein tyrosine phosphatase JOURNAL Gene 162 (2), 279-284 (1995) MEDLINE 96032358 REMARK founctional study of the rat homolog REFERENCE 3 (residues 1 to 657) AUTHORS Ogata,M., Sawada,M., Fujino,Y. and Hamaoka,T. TITLE cDNA cloning and characterization of a novel receptor-type protein tyrosine phosphatase expressed predominantly in the brain JOURNAL J. Biol. Chem. 270 (5), 2337-2343 (1995) MEDLINE 95138207 REMARK functional study of the mouse homolog REFERENCE 4 (residues 1 to 657) AUTHORS Sharma,E. and Lombroso,P.J. TITLE A neuronal protein tyrosine phosphatase induced by nerve growth factor JOURNAL J. Biol. Chem. 270 (1), 49-53 (1995) MEDLINE 95113874 COMMENT REVIEWED REFSEQ: This record has been curated by NCBI staff. The reference sequence was derived from D64053.1. 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 a single intracellular catalytic domains, and thus represents a receptor-type PTP. The similar gene predominately expressed in mouse brain was found to associate with, and thus regulate the activity and cellular localization of MAP kinases. The rat counterpart of this gene was reported to be regulated by the nerve growth factor, which suggested the function of this gene in neuronal growth and differentiation. Transcript Variant: This variant (1) contains a different 5' end region when compared to variant 2. It thus encodes a protein that has a longer N-terminus, as compared to isoform 2. COMMENT This file is created by Vector NTI suite COMMENT ORIGDB|GenPept COMMENT VNTDATE|304502400| COMMENT VNTNAME|hPCPTP1 (NP_002840) PTPRR| 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..657 /organism="Homo sapiens" /db_xref="taxon:9606" /chromosome="12" /map="12q15" /vntifkey="269" Protein 1..657 /product="protein tyrosine phosphatase, receptor type, R isoform 1 precursor" /vntifkey="270" /note="protein tyrosine phosphatase, receptor type, Q; protein-tyrosine phosphatase NC-PTPCOM1; protein tyrosine phosphatase Cr1PTPase precursor; Ch-1 PTPase" Region 1..23 /vntifkey="200" /label=Signal_1 Region 24..657 /product="protein tyrosine phosphatase, receptor type, R isoform 1" /vntifkey="203" /label=Chain_1 Region 392..647 /region_name="Protein tyrosine phosphatase, catalytic domain" /db_xref="CDD:smart00194" /vntifkey="266" /label=Region_1 /note="PTPc" ORIGIN 1 mrravcfpal clllnlhaag cfsgnndhfl ainqkksgkp vfiykhsqdi eksldiapqk 61 iyrhsyhsss eaqvskrhqi vnsafprpay dpslnllamd gqdlevenlp ipaanvivvt 121 lqmdvnklni tllrifrqgv aaalgllpqq vhinrligkk nsielfvspi nrktgisdal 181 pseevlrsln invlhqslsq fgitevspek nvlqgqhead kiwskegfya vviflsifvi 241 ivtclmilyr lkerfqlslr qdkeknqeih lspitlqpal seaktvhsmv qpeqapkvln 301 vvvdpqgrga peirattats vcpspfkmkp iglqerrgsn vsltldmssl gniepfvsip 361 tprekvamey lqsasriltr sqlrdvvass hllqsefmei pmnfvdpkei diprhgtknr 421 yktilpnpls rvclrpknvt dslstyinan yirgysgkek afiatqgpmi ntvddfwqmv 481 wqedspvivm itklkeknek cvlywpekrg iygkvevlvi svnecdnyti rnlvlkqgsh 541 tqhvkhywyt swpdhktpds aqpllqlmld veedrlasqg rgpvvvhcsa gigrtgcfia 601 tsigcqqlke egvvdalsiv cqlrmdrggm vqtseqyefv hhalclyesr lsaetvq // LOCUS hPEST\(NP_ 780 aa 17-MAY-2003 DEFINITION protein tyrosine phosphatase, non-receptor type 12; protein-tyrosine phosphatase G1 [Homo sapiens]. ACCESSION NP_002826 DBSOURCE REFSEQ: accession NM_002835.2 SOURCE Homo sapiens (human). ORGANISM Homo sapiens Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. REFERENCE 1 (residues 1 to 780) AUTHORS Lyons,P.D., Dunty,J.M., Schaefer,E.M. and Schaller,M.D. TITLE Inhibition of the catalytic activity of cell adhesion kinase beta by protein-tyrosine phosphatase-PEST-mediated dephosphorylation JOURNAL J. Biol. Chem. 276 (26), 24422-24431 (2001) MEDLINE 21316574 REFERENCE 2 (residues 1 to 780) AUTHORS Cong,F., Spencer,S., Cote,J.F., Wu,Y., Tremblay,M.L., Lasky,L.A. and Goff,S.P. TITLE Cytoskeletal protein PSTPIP1 directs the PEST-type protein tyrosine phosphatase to the c-Abl kinase to mediate Abl dephosphorylation JOURNAL Mol. Cell 6 (6), 1413-1423 (2000) MEDLINE 21111050 REFERENCE 3 (residues 1 to 780) AUTHORS Shen,Y., Lyons,P., Cooley,M., Davidson,D., Veillette,A., Salgia,R., Griffin,J.D. and Schaller,M.D. TITLE The noncatalytic domain of protein-tyrosine phosphatase-PEST targets paxillin for dephosphorylation in vivo JOURNAL J. Biol. Chem. 275 (2), 1405-1413 (2000) MEDLINE 20092920 REFERENCE 4 (residues 1 to 780) AUTHORS Nishiya,N., Iwabuchi,Y., Shibanuma,M., Cote,J.F., Tremblay,M.L. and Nose,K. TITLE Hic-5, a paxillin homologue, binds to the protein-tyrosine phosphatase PEST (PTP-PEST) through its LIM 3 domain JOURNAL J. Biol. Chem. 274 (14), 9847-9853 (1999) MEDLINE 99194842 REFERENCE 5 (residues 1 to 780) AUTHORS Garton,A.J. and Tonks,N.K. TITLE Regulation of fibroblast motility by the protein tyrosine phosphatase PTP-PEST JOURNAL J. Biol. Chem. 274 (6), 3811-3818 (1999) MEDLINE 99121127 REFERENCE 6 (residues 1 to 780) AUTHORS Takekawa,M., Itoh,F., Hinoda,Y., Adachi,M., Ariyama,T., Inazawa,J., Imai,K. and Yachi,A. TITLE Chromosomal localization of the protein tyrosine phosphatase G1 gene and characterization of the aberrant transcripts in human colon cancer cells JOURNAL FEBS Lett. 339 (3), 222-228 (1994) MEDLINE 94156037 REFERENCE 7 (residues 1 to 780) AUTHORS Yang,Q., Co,D., Sommercorn,J. and Tonks,N.K. TITLE Cloning and expression of PTP-PEST. A novel, human, nontransmembrane protein tyrosine phosphatase JOURNAL J. Biol. Chem. 268 (9), 6622-6628 (1993) MEDLINE 93203262 REFERENCE 8 (residues 1 to 780) AUTHORS Takekawa,M., Itoh,F., Hinoda,Y., Arimura,Y., Toyota,M., Sekiya,M., Adachi,M., Imai,K. and Yachi,A. TITLE Cloning and characterization of a human cDNA encoding a novel putative cytoplasmic protein-tyrosine-phosphatase JOURNAL Biochem. Biophys. Res. Commun. 189 (2), 1223-1230 (1992) MEDLINE 93112015 COMMENT REVIEWED REFSEQ: This record has been curated by NCBI staff. The reference sequence was derived from M93425.1. On Jan 25, 2002 this sequence version replaced gi:4506287. 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 a C-terminal PEST motif, which serves as a protein-protein interaction domain, and may be related to protein intracellular half-life. This PTP was found to bind and dephosphorylate the product of oncogene c-ABL, thus may play a role in oncogenesis. This PTP was shown to interact with, and dephosphorylate, various of cytoskeleton and cell adhesion molecules, such as p130 (Cas), CAKbeta/PTK2B, PSTPIP1, and paxillin, which suggested its regulatory roles in controlling cell shape and mobility. COMMENT This file is created by Vector NTI suite COMMENT ORIGDB|GenPept COMMENT VNTDATE|304502400| COMMENT VNTNAME|hPEST (NP_002826) PTPN12| 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..780 /organism="Homo sapiens" /db_xref="taxon:9606" /chromosome="7" /map="7q11.23" /vntifkey="269" Protein 1..780 /product="protein tyrosine phosphatase, non-receptor type 12" /EC_number="3.1.3.48" /vntifkey="270" /note="protein-tyrosine phosphatase G1" Region 28..295 /region_name="Protein tyrosine phosphatase, catalytic domain" /db_xref="CDD:smart00194" /vntifkey="266" /label=Region_1 /note="PTPc" ORIGIN 1 meqveilrkf iqrvqamksp dhngednfar dfmrlrrlst kyrtekiypt atgekeenvk 61 knrykdilpf dhsrvkltlk tpsqdsdyin anfikgvygp kayvatqgpl antvidfwrm 121 iweynvviiv macrefemgr kkcerywply gedpitfapf kiscedeqar tdyfirtlll 181 efqnesrrly qfhyvnwpdh dvpssfdsil dmislmrkyq ehedvpicih csagcgrtga 241 icaidytwnl lkagkipeef nvfnliqemr tqrhsavqtk eqyelvhrai aqlfekqlql 301 yeihgaqkia dgvneinten missiepekq dspppkpprt rsclvegdak eeilqppeph 361 pvppiltpsp psafptvttv wqdndryhpk pvlhmvsseq hsadlnrnys kstelpgkne 421 stieqidkkl ernlsfeikk vplqegpksf dgntllnrgh aikiksaspc iadkiskpqe 481 lssdlnvgdt sqnscvdcsv tqsnkvsvtp peesqnsdtp prpdrlplde kghvtwsfhg 541 penaipipdl segnssdiny qtrktvsltp spttqvetpd lvdhdntspl frtplsftnp 601 lhsddsdsde rnsdgavtqn ktnistasat vsaatstesi strkvlpmsi arhniagtth 661 sgaekdvdvs edsppplper tpesfvlase hntpvrsews elqsqerseq kkseglitse 721 nekcdhpagg ihyemciecp ptfsdkreqi senpteatdi gfgnrcgkpk gprdppsewt // LOCUS hPTP1B\(NP 435 aa 17-MAY-2003 DEFINITION protein tyrosine phosphatase, non-receptor type 1; non-receptor tyrosine phophatase 1; protein tyrosine phophatase 1B; protein tyrosine phophatase, placental [Homo sapiens]. ACCESSION NP_002818 DBSOURCE REFSEQ: accession NM_002827.2 SOURCE Homo sapiens (human). ORGANISM Homo sapiens Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. REFERENCE 1 (residues 1 to 435) AUTHORS Li,S. and Whorton,A.R. TITLE Regulation of protein tyrosine phosphatase 1B in intact cells by S-nitrosothiols JOURNAL Arch. Biochem. Biophys. 410 (2), 269-279 (2003) MEDLINE 22461115 REMARK GeneRIF: PTP1B inhibition by S-nitrosylation is caused by formation of a mixed disulfide REFERENCE 2 (residues 1 to 435) AUTHORS Fukada,T. and Tonks,N.K. TITLE Identification of YB-1 as a regulator of PTP1B expression: implications for regulation of insulin and cytokine signaling JOURNAL EMBO J. 22 (3), 479-493 (2003) MEDLINE 22441887 REMARK GeneRIF: Data show that Y box-binding protein-1 (YB-1) is a regulator of protein tyrosine phosphatase 1B (PTP1B) expression, and highlight PTP1B as a critical regulator of insulin- and cytokine-mediated signal transduction. REFERENCE 3 (residues 1 to 435) AUTHORS Yigzaw,Y., Poppleton,H.M., Sreejayan,N., Hassid,A. and Patel,T.B. TITLE Protein-tyrosine phosphatase-1B (PTP1B) mediates the anti-migratory actions of Sprouty JOURNAL J. Biol. Chem. 278 (1), 284-288 (2003) MEDLINE 22393490 REMARK GeneRIF: Data show that an increase in soluble protein-tyrosine phosphatase 1B activity contributes to the anti-migratory, but not anti-mitogenic, actions of human Sprouty 2. REFERENCE 4 (residues 1 to 435) AUTHORS Di Paola,R., Frittitta,L., Miscio,G., Bozzali,M., Baratta,R., Centra,M., Spampinato,D., Santagati,M.G., Ercolino,T., Cisternino,C., Soccio,T., Mastroianno,S., Tassi,V., Almgren,P., Pizzuti,A., Vigneri,R. and Trischitta,V. TITLE A variation in 3' UTR of hPTP1B increases specific gene expression and associates with insulin resistance JOURNAL Am. J. Hum. Genet. 70 (3), 806-812 (2002) MEDLINE 21832513 REMARK GeneRIF: variation in 3' UTR of hPTP1B increases specific gene expression and associates with insulin resistance REFERENCE 5 (residues 1 to 435) AUTHORS Myers,M.P., Andersen,J.N., Cheng,A., Tremblay,M.L., Horvath,C.M., Parisien,J.P., Salmeen,A., Barford,D. and Tonks,N.K. TITLE TYK2 and JAK2 are substrates of protein-tyrosine phosphatase 1B JOURNAL J. Biol. Chem. 276 (51), 47771-47774 (2001) MEDLINE 21611285 REFERENCE 6 (residues 1 to 435) AUTHORS Wang,J., Cheung,A.T., Kolls,J.K., Starks,W.W., Martinez-Hernandez,A., Dietzen,D. and Bryer-Ash,M. TITLE Effects of adenovirus-mediated liver-selective overexpression of protein tyrosine phosphatase-1b on insulin sensitivity in vivo JOURNAL Diabetes Obes Metab 3 (5), 367-380 (2001) MEDLINE 21560532 REMARK GeneRIF: Moderate overabundance of PTP-1B in liver tissue does not alter insulin action on glucose metabolism, and the site of action of PTP-1B is presumably at insulin-responsive target tissue or tissues other than the liver. REFERENCE 7 (residues 1 to 435) AUTHORS Dadke,S., Kusari,A. and Kusari,J. TITLE Phosphorylation and activation of protein tyrosine phosphatase (PTP) 1B by insulin receptor JOURNAL Mol. Cell. Biochem. 221 (1-2), 147-154 (2001) MEDLINE 21396990 REFERENCE 8 (residues 1 to 435) AUTHORS Egawa,K., Maegawa,H., Shimizu,S., Morino,K., Nishio,Y., Bryer-Ash,M., Cheung,A.T., Kolls,J.K., Kikkawa,R. and Kashiwagi,A. TITLE Protein-tyrosine phosphatase-1B negatively regulates insulin signaling in l6 myocytes and Fao hepatoma cells JOURNAL J. Biol. Chem. 276 (13), 10207-10211 (2001) MEDLINE 21167830 REFERENCE 9 (residues 1 to 435) AUTHORS Salmeen,A., Andersen,J.N., Myers,M.P., Tonks,N.K. and Barford,D. TITLE Molecular basis for the dephosphorylation of the activation segment of the insulin receptor by protein tyrosine phosphatase 1B JOURNAL Mol. Cell 6 (6), 1401-1412 (2000) MEDLINE 21111049 REFERENCE 10 (residues 1 to 435) 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 11 (residues 1 to 435) AUTHORS Ahmad,F., Li,P.M., Meyerovitch,J. and Goldstein,B.J. TITLE Osmotic loading of neutralizing antibodies demonstrates a role for protein-tyrosine phosphatase 1B in negative regulation of the insulin action pathway JOURNAL J. Biol. Chem. 270 (35), 20503-20508 (1995) MEDLINE 95386495 REFERENCE 12 (residues 1 to 435) AUTHORS Milarski,K.L., Zhu,G., Pearl,C.G., McNamara,D.J., Dobrusin,E.M., MacLean,D., Thieme-Sefler,A., Zhang,Z.Y., Sawyer,T., Decker,S.J. et al. TITLE Sequence specificity in recognition of the epidermal growth factor receptor by protein tyrosine phosphatase 1B JOURNAL J. Biol. Chem. 268 (31), 23634-23639 (1993) MEDLINE 94043167 REFERENCE 13 (residues 1 to 435) AUTHORS Brown-Shimer,S., Johnson,K.A., Lawrence,J.B., Johnson,C., Bruskin,A., Green,N.R. and Hill,D.E. TITLE Molecular cloning and chromosome mapping of the human gene encoding protein phosphotyrosyl phosphatase 1B JOURNAL Proc. Natl. Acad. Sci. U.S.A. 87 (13), 5148-5152 (1990) MEDLINE 90311360 REFERENCE 14 (residues 1 to 435) AUTHORS Chernoff,J., Schievella,A.R., Jost,C.A., Erikson,R.L. and Neel,B.G. TITLE Cloning of a cDNA for a major human protein-tyrosine-phosphatase JOURNAL Proc. Natl. Acad. Sci. U.S.A. 87 (7), 2735-2739 (1990) MEDLINE 90207272 REFERENCE 15 (residues 1 to 435) AUTHORS Charbonneau,H., Tonks,N.K., Kumar,S., Diltz,C.D., Harrylock,M., Cool,D.E., Krebs,E.G., Fischer,E.H. and Walsh,K.A. TITLE Human placenta protein-tyrosine-phosphatase: amino acid sequence and relationship to a family of receptor-like proteins JOURNAL Proc. Natl. Acad. Sci. U.S.A. 86 (14), 5252-5256 (1989) MEDLINE 89315775 COMMENT REVIEWED REFSEQ: This record has been curated by NCBI staff. The reference sequence was derived from M33689.1 and AU117677.1. Summary: The protein encoded by this gene is the founding member of the protein tyrosine phosphatase (PTP) family, which was isolated and identified based on its enzymatic activity and amino acid sequence. PTPs catalyze the hydrolysis of the phosphate monoesters specifically on tyrosine residues. Members of the PTP family share a highly conserved catalytic motif, which is essential for the catalytic activity. 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 has been shown to act as a negative regulator of insulin signaling by dephosphorylating the phosphotryosine residues of insulin receptor kinase. This PTP was also reported to dephosphorylate epidermal growth factor receptor kinase, as well as JAK2 and TYK2 kinases, which implicated the role of this PTP in cell growth control, and cell response to interferon stimulation. COMMENT This file is created by Vector NTI suite COMMENT ORIGDB|GenPept COMMENT VNTDATE|304502400| COMMENT VNTNAME|hPTP1B (NP_002818) PTPN1| 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..435 /organism="Homo sapiens" /db_xref="taxon:9606" /chromosome="20" /map="20q13.1-q13.2" /vntifkey="269" Protein 1..435 /product="protein tyrosine phosphatase, non-receptor type 1" /EC_number="3.1.3.48" /vntifkey="270" /note="non-receptor tyrosine phophatase 1; protein tyrosine phophatase 1B; protein tyrosine phophatase, placental" Region 3..279 /region_name="Protein tyrosine phosphatase, catalytic domain" /db_xref="CDD:smart00194" /vntifkey="266" /label=Region_1 /note="PTPc" ORIGIN 1 memekefeqi dksgswaaiy qdirheasdf pcrvaklpkn knrnryrdvs pfdhsriklh 61 qedndyinas likmeeaqrs yiltqgplpn tcghfwemvw eqksrgvvml nrvmekgslk 121 caqywpqkee kemifedtnl kltlisedik syytvrqlel enlttqetre ilhfhyttwp 181 dfgvpespas flnflfkvre sgslspehgp vvvhcsagig rsgtfcladt clllmdkrkd 241 pssvdikkvl lemrkfrmgl iqtadqlrfs ylaviegakf imgdssvqdq wkelshedle 301 pppehipppp rppkrileph ngkcreffpn hqwvkeetqe dkdcpikeek gsplnaapyg 361 iesmsqdtev rsrvvggslr gaqaaspakg epslpekded halsywkpfl vnmcvatvlt 421 agaylcyrfl fnsnt // LOCUS hPTPalpha\ 802 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|304502400| COMMENT VNTNAME|hPTPalpha (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..802 /organism="Homo sapiens" /db_xref="taxon:9606" /chromosome="20" /map="