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Tyrosine-protein phosphatase non-receptor type 6 (EC 3.1.3.48) (Hematopoietic cell protein-tyrosine phosphatase) (Protein-tyrosine phosphatase 1C) (PTP-1C) (Protein-tyrosine phosphatase SHP-1) (SH-PTP1)

 PTN6_HUMAN              Reviewed;         595 AA.
P29350; A8K306; G3V0F8; Q969V8; Q9UK67;
01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
01-DEC-1992, sequence version 1.
18-JUL-2018, entry version 215.
RecName: Full=Tyrosine-protein phosphatase non-receptor type 6;
EC=3.1.3.48;
AltName: Full=Hematopoietic cell protein-tyrosine phosphatase;
AltName: Full=Protein-tyrosine phosphatase 1C;
Short=PTP-1C;
AltName: Full=Protein-tyrosine phosphatase SHP-1;
AltName: Full=SH-PTP1;
Name=PTPN6; Synonyms=HCP, PTP1C;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=1732748; DOI=10.1128/MCB.12.2.836;
Yi T., Cleveland J.L., Ihle J.N.;
"Protein tyrosine phosphatase containing SH2 domains:
characterization, preferential expression in hematopoietic cells, and
localization to human chromosome 12p12-p13.";
Mol. Cell. Biol. 12:836-846(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
TISSUE=Mammary gland;
PubMed=1652101; DOI=10.1038/352736a0;
Shen S.H., Bastien L., Posner B.I., Chretien P.;
"A protein-tyrosine phosphatase with sequence similarity to the SH2
domain of the protein-tyrosine kinases.";
Nature 352:736-739(1991).
[3]
ERRATUM, AND SEQUENCE REVISION.
Shen S.H., Bastien L., Posner B.I., Chretien P.;
Nature 353:868-868(1991).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=1736296; DOI=10.1073/pnas.89.3.1123;
Plutzky J., Neel B.G., Rosenberg R.D.;
"Isolation of a src homology 2-containing tyrosine phosphatase.";
Proc. Natl. Acad. Sci. U.S.A. 89:1123-1127(1992).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1; 2 AND 3).
PubMed=7665165; DOI=10.1006/geno.1995.1020;
Banville D., Stocco R., Shen S.H.;
"Human protein tyrosine phosphatase 1C (PTPN6) gene structure:
alternate promoter usage and exon skipping generate multiple
transcripts.";
Genomics 27:165-173(1995).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9074930; DOI=10.1101/gr.7.3.268;
Ansari-Lari M.A., Shen Y., Muzny D.M., Lee W., Gibbs R.A.;
"Large-scale sequencing in human chromosome 12p13: experimental and
computational gene structure determination.";
Genome Res. 7:268-280(1997).
[7]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
PubMed=10497187; DOI=10.1074/jbc.274.40.28301;
Jin Y.J., Yu C.L., Burakoff S.J.;
"Human 70-kDa SHP-1L differs from 68-kDa SHP-1 in its C-terminal
structure and catalytic activity.";
J. Biol. Chem. 274:28301-28307(1999).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2).
Oka T., Ouchida M.;
"Gene silencing of SHP-1 gene in leukemias/lymphomas by aberrant
methylation.";
Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Umbilical cord blood;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[13]
PHOSPHORYLATION.
PubMed=7781604;
Li R.Y., Gaits F., Ragab A., Ragab-Thomas J.M.F., Chap H.;
"Tyrosine phosphorylation of an SH2-containing protein tyrosine
phosphatase is coupled to platelet thrombin receptor via a pertussis
toxin-sensitive heterotrimeric G-protein.";
EMBO J. 14:2519-2526(1995).
[14]
INTERACTION WITH LILRB1.
PubMed=9285411; DOI=10.1016/S1074-7613(00)80529-4;
Cosman D., Fanger N., Borges L., Kubin M., Chin W., Peterson L.,
Hsu M.-L.;
"A novel immunoglobulin superfamily receptor for cellular and viral
MHC class I molecules.";
Immunity 7:273-282(1997).
[15]
INTERACTION WITH LILRB2.
PubMed=9842885;
DOI=10.1002/(SICI)1521-4141(199811)28:11<3423::AID-IMMU3423>3.0.CO;2-2;
Fanger N.A., Cosman D., Peterson L., Braddy S.C., Maliszewski C.R.,
Borges L.;
"The MHC class I binding proteins LIR-1 and LIR-2 inhibit Fc receptor-
mediated signaling in monocytes.";
Eur. J. Immunol. 28:3423-3434(1998).
[16]
INTERACTION WITH SIRPA.
PubMed=9712903; DOI=10.1074/jbc.273.35.22719;
Veillette A., Thibaudeau E., Latour S.;
"High expression of inhibitory receptor SHPS-1 and its association
with protein tyrosine phosphatase SHP-1 in macrophages.";
J. Biol. Chem. 273:22719-22728(1998).
[17]
INTERACTION WITH LYN, AND PHOSPHORYLATION AT TYR-564.
PubMed=10574931; DOI=10.1074/jbc.274.49.34663;
Yoshida K., Kharbanda S., Kufe D.;
"Functional interaction between SHPTP1 and the Lyn tyrosine kinase in
the apoptotic response to DNA damage.";
J. Biol. Chem. 274:34663-34668(1999).
[18]
INTERACTION WITH FCRL2 AND FCRL3.
PubMed=11162587; DOI=10.1006/bbrc.2000.4213;
Xu M.-J., Zhao R., Zhao Z.J.;
"Molecular cloning and characterization of SPAP1, an inhibitory
receptor.";
Biochem. Biophys. Res. Commun. 280:768-775(2001).
[19]
INTERACTION WITH CD84.
PubMed=11414741; DOI=10.1006/clim.2001.5035;
Lewis J., Eiben L.J., Nelson D.L., Cohen J.I., Nichols K.E.,
Ochs H.D., Notarangelo L.D., Duckett C.S.;
"Distinct interactions of the X-linked lymphoproliferative syndrome
gene product SAP with cytoplasmic domains of members of the CD2
receptor family.";
Clin. Immunol. 100:15-23(2001).
[20]
FUNCTION IN ROS1 DEPHOSPHORYLATION, AND INTERACTION WITH ROS1.
PubMed=11266449; DOI=10.1083/jcb.152.2.325;
Keilhack H., Mueller M., Boehmer S.A., Frank C., Weidner K.M.,
Birchmeier W., Ligensa T., Berndt A., Kosmehl H., Guenther B.,
Mueller T., Birchmeier C., Boehmer F.D.;
"Negative regulation of Ros receptor tyrosine kinase signaling. An
epithelial function of the SH2 domain protein tyrosine phosphatase
SHP-1.";
J. Cell Biol. 152:325-334(2001).
[21]
INTERACTION WITH FCRL4.
PubMed=14597715; DOI=10.1073/pnas.1935944100;
Ehrhardt G.R.A., Davis R.S., Hsu J.T., Leu C.-M., Ehrhardt A.,
Cooper M.D.;
"The inhibitory potential of Fc receptor homolog 4 on memory B
cells.";
Proc. Natl. Acad. Sci. U.S.A. 100:13489-13494(2003).
[22]
INTERACTION WITH CD300LF.
PubMed=15184070; DOI=10.1016/j.bbrc.2004.05.065;
Sui L., Li N., Liu Q., Zhang W., Wan T., Wang B., Luo K., Sun H.,
Cao X.;
"IgSF13, a novel human inhibitory receptor of the immunoglobulin
superfamily, is preferentially expressed in dendritic cells and
monocytes.";
Biochem. Biophys. Res. Commun. 319:920-928(2004).
[23]
REVIEW ON ROLE IN KIT SIGNALING.
PubMed=15526160; DOI=10.1007/s00018-004-4189-6;
Ronnstrand L.;
"Signal transduction via the stem cell factor receptor/c-Kit.";
Cell. Mol. Life Sci. 61:2535-2548(2004).
[24]
REVIEW ON ROLE IN KIT SIGNALING.
PubMed=16129412; DOI=10.1016/j.bbrc.2005.08.055;
Roskoski R. Jr.;
"Signaling by Kit protein-tyrosine kinase--the stem cell factor
receptor.";
Biochem. Biophys. Res. Commun. 337:1-13(2005).
[25]
INTERACTION WITH KIR2DL1.
PubMed=18604210; DOI=10.1038/ni.1635;
Yu M.-C., Su L.-L., Zou L., Liu Y., Wu N., Kong L., Zhuang Z.-H.,
Sun L., Liu H.P., Hu J.-H., Li D., Strominger J.L., Zang J.-W.,
Pei G., Ge B.-X.;
"An essential function for beta-arrestin 2 in the inhibitory signaling
of natural killer cells.";
Nat. Immunol. 9:898-907(2008).
[26]
SUBCELLULAR LOCATION, AND INTERACTION WITH PDPK1.
PubMed=19591923; DOI=10.1016/j.cellsig.2009.06.010;
Sephton C.F., Zhang D., Lehmann T.M., Pennington P.R., Scheid M.P.,
Mousseau D.D.;
"The nuclear localization of 3'-phosphoinositide-dependent kinase-1 is
dependent on its association with the protein tyrosine phosphatase
SHP-1.";
Cell. Signal. 21:1634-1644(2009).
[27]
INTERACTION WITH FCRL3.
PubMed=19843936; DOI=10.4049/jimmunol.0901982;
Kochi Y., Myouzen K., Yamada R., Suzuki A., Kurosaki T., Nakamura Y.,
Yamamoto K.;
"FCRL3, an autoimmune susceptibility gene, has inhibitory potential on
B-cell receptor-mediated signaling.";
J. Immunol. 183:5502-5510(2009).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-64, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[29]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[30]
SUBCELLULAR LOCATION, AND INTERACTION WITH CDK2.
PubMed=21262353; DOI=10.1016/j.cellsig.2011.01.019;
Fiset A., Xu E., Bergeron S., Marette A., Pelletier G.,
Siminovitch K.A., Olivier M., Beauchemin N., Faure R.L.;
"Compartmentalized CDK2 is connected with SHP-1 and beta-catenin and
regulates insulin internalization.";
Cell. Signal. 23:911-919(2011).
[31]
INTERACTION WITH FCRL6.
PubMed=20933011; DOI=10.1016/j.imlet.2010.09.023;
Kulemzin S.V., Zamoshnikova A.Y., Yurchenko M.Y., Vitak N.Y.,
Najakshin A.M., Fayngerts S.A., Chikaev N.A., Reshetnikova E.S.,
Kashirina N.M., Peclo M.M., Rutkevich P.N., Shevelev A.Y.,
Yanushevskaya E.V., Baranov K.O., Mamonkin M., Vlasik T.N.,
Sidorenko S.P., Taranin A.V., Mechetina L.V.;
"FCRL6 receptor: expression and associated proteins.";
Immunol. Lett. 134:174-182(2011).
[32]
INTERACTION WITH EGFR.
PubMed=21258366; DOI=10.1038/ncb2158;
Hsu J.M., Chen C.T., Chou C.K., Kuo H.P., Li L.Y., Lin C.Y., Lee H.J.,
Wang Y.N., Liu M., Liao H.W., Shi B., Lai C.C., Bedford M.T.,
Tsai C.H., Hung M.C.;
"Crosstalk between Arg 1175 methylation and Tyr 1173 phosphorylation
negatively modulates EGFR-mediated ERK activation.";
Nat. Cell Biol. 13:174-181(2011).
[33]
INTERACTION WITH MPIG6B.
PubMed=23112346; DOI=10.1126/scisignal.2002936;
Mazharian A., Wang Y.J., Mori J., Bem D., Finney B., Heising S.,
Gissen P., White J.G., Berndt M.C., Gardiner E.E., Nieswandt B.,
Douglas M.R., Campbell R.D., Watson S.P., Senis Y.A.;
"Mice lacking the ITIM-containing receptor G6b-B exhibit
macrothrombocytopenia and aberrant platelet function.";
Sci. Signal. 5:RA78-RA78(2012).
[34]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[35]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[36]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 248-399.
PubMed=9774441; DOI=10.1074/jbc.273.43.28199;
Yang J., Liang X., Niu T., Meng W., Zhao Z., Zhou G.W.;
"Crystal structure of the catalytic domain of protein-tyrosine
phosphatase SHP-1.";
J. Biol. Chem. 273:28199-28207(1998).
[37]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-532, AND DOMAIN SH2.
PubMed=12482860; DOI=10.1074/jbc.M210430200;
Yang J., Liu L., He D., Song X., Liang X., Zhao Z.J., Zhou G.W.;
"Crystal structure of human protein-tyrosine phosphatase SHP-1.";
J. Biol. Chem. 278:6516-6520(2003).
[38]
STRUCTURE BY NMR OF 110-214.
RIKEN structural genomics initiative (RSGI);
"Solution structures of the SH2 domain of human protein-tyrosine
phosphatase SHP-1.";
Submitted (NOV-2005) to the PDB data bank.
[39]
X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS), AND DOMAIN SH2.
PubMed=21465528; DOI=10.1002/jcb.23125;
Wang W., Liu L., Song X., Mo Y., Komma C., Bellamy H.D., Zhao Z.J.,
Zhou G.W.;
"Crystal structure of human protein tyrosine phosphatase SHP-1 in the
open conformation.";
J. Cell. Biochem. 112:2062-2071(2011).
-!- FUNCTION: Modulates signaling by tyrosine phosphorylated cell
surface receptors such as KIT and the EGF receptor/EGFR. The SH2
regions may interact with other cellular components to modulate
its own phosphatase activity against interacting substrates.
Together with MTUS1, induces UBE2V2 expression upon angiotensin II
stimulation. Plays a key role in hematopoiesis.
{ECO:0000269|PubMed:11266449}.
-!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
tyrosine + phosphate. {ECO:0000255|PROSITE-ProRule:PRU10044}.
-!- SUBUNIT: Monomer. Interacts with MTUS1 (By similarity). Interacts
with MILR1 (tyrosine-phosphorylated) (By similarity). Interacts
with KIT (By similarity). Interacts with SIRPA/PTPNS1
(PubMed:9712903). Interacts with LILRB1 and LILRB2
(PubMed:9285411, PubMed:9842885). Interacts with FCRL2 and FCRL4
(PubMed:11162587, PubMed:14597715). Interacts with FCRL3 and FCRL6
(tyrosine phosphorylated form) (PubMed:20933011, PubMed:11162587,
PubMed:19843936). Interacts with CD84 (PubMed:11414741). Interacts
with CD300LF (PubMed:15184070). Interacts with CDK2
(PubMed:21262353). Interacts with KIR2DL1; the interaction is
enhanced by ARRB2 (PubMed:18604210). Interacts (via SH2 1 domain)
with ROS1; the interaction is direct and promotes ROS1
dephosphorylation (PubMed:11266449). Interacts with EGFR; inhibits
EGFR-dependent activation of MAPK/ERK (PubMed:21258366). Interacts
with LYN (PubMed:10574931). Interacts with the tyrosine
phosphorylated form of PDPK1 (PubMed:19591923). Interacts with
CEACAM1 (via cytoplasmic domain); this interaction depends on the
monomer/dimer equilibrium and is phosphorylation-dependent (By
similarity). Interacts with MPIG6B (via ITIM motif)
(PubMed:23112346). {ECO:0000250|UniProtKB:P29351,
ECO:0000250|UniProtKB:P81718, ECO:0000269|PubMed:10574931,
ECO:0000269|PubMed:11162587, ECO:0000269|PubMed:11266449,
ECO:0000269|PubMed:11414741, ECO:0000269|PubMed:14597715,
ECO:0000269|PubMed:15184070, ECO:0000269|PubMed:18604210,
ECO:0000269|PubMed:19591923, ECO:0000269|PubMed:19843936,
ECO:0000269|PubMed:20933011, ECO:0000269|PubMed:21258366,
ECO:0000269|PubMed:21262353, ECO:0000269|PubMed:23112346,
ECO:0000269|PubMed:9285411, ECO:0000269|PubMed:9712903,
ECO:0000269|PubMed:9842885}.
-!- INTERACTION:
Q14790:CASP8; NbExp=3; IntAct=EBI-78260, EBI-78060;
P20273:CD22; NbExp=4; IntAct=EBI-78260, EBI-78277;
Q9BZW8:CD244; NbExp=2; IntAct=EBI-78260, EBI-1580565;
P20138:CD33; NbExp=8; IntAct=EBI-78260, EBI-3906571;
P11049:CD37; NbExp=4; IntAct=EBI-78260, EBI-6139068;
P19235:EPOR; NbExp=11; IntAct=EBI-78260, EBI-617321;
P31994:FCGR2B; NbExp=3; IntAct=EBI-78260, EBI-724784;
Q13643:FHL3; NbExp=3; IntAct=EBI-78260, EBI-741101;
P62993:GRB2; NbExp=3; IntAct=EBI-78260, EBI-401755;
P43626:KIR2DL1; NbExp=4; IntAct=EBI-78260, EBI-8684277;
P43628:KIR2DL3; NbExp=13; IntAct=EBI-78260, EBI-8632435;
Q6GTX8:LAIR1; NbExp=5; IntAct=EBI-78260, EBI-965864;
P06239:LCK; NbExp=5; IntAct=EBI-78260, EBI-1348;
Q8NHL6:LILRB1; NbExp=4; IntAct=EBI-78260, EBI-2805262;
Q8N423:LILRB2; NbExp=3; IntAct=EBI-78260, EBI-2816428;
O75022:LILRB3; NbExp=4; IntAct=EBI-78260, EBI-2830524;
Q8NHJ6:LILRB4; NbExp=4; IntAct=EBI-78260, EBI-2805248;
O94916-1:NFAT5; NbExp=4; IntAct=EBI-78260, EBI-15828651;
P16284:PECAM1; NbExp=4; IntAct=EBI-78260, EBI-716404;
Q9UKJ1:PILRA; NbExp=5; IntAct=EBI-78260, EBI-965833;
Q05397:PTK2; NbExp=3; IntAct=EBI-7399369, EBI-702142;
P08922:ROS1; NbExp=4; IntAct=EBI-78260, EBI-7371065;
Q92734:TFG; NbExp=2; IntAct=EBI-7399369, EBI-357061;
Q8N1K5:THEMIS; NbExp=4; IntAct=EBI-78260, EBI-2873538;
B7UM99:tir (xeno); NbExp=4; IntAct=EBI-78260, EBI-2504426;
Q7DB77:tir (xeno); NbExp=2; IntAct=EBI-78260, EBI-6480811;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=In neurons,
translocates into the nucleus after treatment with angiotensin II
(By similarity). Shuttles between the cytoplasm and nucleus via
its association with PDPK1. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1; Synonyms=Long;
IsoId=P29350-1; Sequence=Displayed;
Name=2;
IsoId=P29350-3; Sequence=VSP_007775;
Name=3; Synonyms=Short;
IsoId=P29350-2; Sequence=VSP_005129, VSP_005130;
Name=4; Synonyms=70-kDa, SHP-1L;
IsoId=P29350-4; Sequence=VSP_044447;
-!- TISSUE SPECIFICITY: Isoform 1 is expressed in hematopoietic cells.
Isoform 2 is expressed in non-hematopoietic cells.
-!- DOMAIN: The N-terminal SH2 domain functions as an auto-inhibitory
domain, blocking the catalytic domain in the ligand-free close
conformation. {ECO:0000269|PubMed:12482860,
ECO:0000269|PubMed:21465528}.
-!- PTM: Phosphorylated on tyrosine residues. Binding of KITLG/SCF to
KIT increases tyrosine phosphorylation (By similarity).
Phosphorylation at Tyr-564 enhances phosphatase activity.
{ECO:0000250, ECO:0000269|PubMed:10574931,
ECO:0000269|PubMed:7781604}.
-!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
Non-receptor class 2 subfamily. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/PTPN6ID41920ch12p13.html";
-----------------------------------------------------------------------
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EMBL; M74903; AAA35963.1; -; mRNA.
EMBL; X62055; CAA43982.1; -; mRNA.
EMBL; M77273; AAA36610.1; -; mRNA.
EMBL; U15528; AAA82880.1; -; Genomic_DNA.
EMBL; U15536; AAA82880.1; JOINED; Genomic_DNA.
EMBL; U15535; AAA82880.1; JOINED; Genomic_DNA.
EMBL; U15534; AAA82880.1; JOINED; Genomic_DNA.
EMBL; U15533; AAA82880.1; JOINED; Genomic_DNA.
EMBL; U15532; AAA82880.1; JOINED; Genomic_DNA.
EMBL; U15531; AAA82880.1; JOINED; Genomic_DNA.
EMBL; U15530; AAA82880.1; JOINED; Genomic_DNA.
EMBL; U15529; AAA82880.1; JOINED; Genomic_DNA.
EMBL; U15528; AAA82879.1; -; Genomic_DNA.
EMBL; U15537; AAA82879.1; JOINED; Genomic_DNA.
EMBL; U15535; AAA82879.1; JOINED; Genomic_DNA.
EMBL; U15534; AAA82879.1; JOINED; Genomic_DNA.
EMBL; U15533; AAA82879.1; JOINED; Genomic_DNA.
EMBL; U15532; AAA82879.1; JOINED; Genomic_DNA.
EMBL; U15531; AAA82879.1; JOINED; Genomic_DNA.
EMBL; U15530; AAA82879.1; JOINED; Genomic_DNA.
EMBL; U15529; AAA82879.1; JOINED; Genomic_DNA.
EMBL; U47924; AAB51322.1; -; Genomic_DNA.
EMBL; U47924; AAB51323.1; -; Genomic_DNA.
EMBL; AF178946; AAD53317.1; -; mRNA.
EMBL; AB079851; BAC81774.1; -; Genomic_DNA.
EMBL; AB079851; BAC81775.1; -; Genomic_DNA.
EMBL; AK290421; BAF83110.1; -; mRNA.
EMBL; CH471116; EAW88703.1; -; Genomic_DNA.
EMBL; CH471116; EAW88704.1; -; Genomic_DNA.
EMBL; BC002523; AAH02523.1; -; mRNA.
EMBL; BC007667; AAH07667.1; -; mRNA.
CCDS; CCDS41744.1; -. [P29350-3]
CCDS; CCDS44820.1; -. [P29350-1]
CCDS; CCDS44821.1; -. [P29350-4]
PIR; B42031; S20825.
RefSeq; NP_002822.2; NM_002831.5. [P29350-1]
RefSeq; NP_536858.1; NM_080548.4. [P29350-3]
RefSeq; NP_536859.1; NM_080549.3. [P29350-4]
RefSeq; XP_011519290.1; XM_011520988.1. [P29350-3]
UniGene; Hs.63489; -.
PDB; 1FPR; X-ray; 2.50 A; A=243-526.
PDB; 1GWZ; X-ray; 2.50 A; A=243-541.
PDB; 1X6C; NMR; -; A=110-214.
PDB; 2B3O; X-ray; 2.80 A; A=1-532.
PDB; 2RMX; NMR; -; A=110-214.
PDB; 2YU7; NMR; -; A=110-214.
PDB; 3PS5; X-ray; 3.10 A; A=1-595.
PDB; 4GRY; X-ray; 1.70 A; A=243-528.
PDB; 4GRZ; X-ray; 1.37 A; A=243-528.
PDB; 4GS0; X-ray; 1.80 A; A/B=243-528.
PDB; 4HJP; X-ray; 1.40 A; A=243-528.
PDB; 4HJQ; X-ray; 1.80 A; A/B=243-528.
PDBsum; 1FPR; -.
PDBsum; 1GWZ; -.
PDBsum; 1X6C; -.
PDBsum; 2B3O; -.
PDBsum; 2RMX; -.
PDBsum; 2YU7; -.
PDBsum; 3PS5; -.
PDBsum; 4GRY; -.
PDBsum; 4GRZ; -.
PDBsum; 4GS0; -.
PDBsum; 4HJP; -.
PDBsum; 4HJQ; -.
ProteinModelPortal; P29350; -.
SMR; P29350; -.
BioGrid; 111742; 115.
DIP; DIP-31002N; -.
IntAct; P29350; 71.
MINT; P29350; -.
STRING; 9606.ENSP00000391592; -.
BindingDB; P29350; -.
ChEMBL; CHEMBL3166; -.
MoonDB; P29350; Predicted.
DEPOD; P29350; -.
iPTMnet; P29350; -.
PhosphoSitePlus; P29350; -.
BioMuta; PTPN6; -.
DMDM; 131469; -.
OGP; P29350; -.
EPD; P29350; -.
MaxQB; P29350; -.
PaxDb; P29350; -.
PeptideAtlas; P29350; -.
PRIDE; P29350; -.
ProteomicsDB; 54543; -.
ProteomicsDB; 54544; -. [P29350-2]
ProteomicsDB; 54545; -. [P29350-3]
DNASU; 5777; -.
Ensembl; ENST00000318974; ENSP00000326010; ENSG00000111679. [P29350-1]
Ensembl; ENST00000399448; ENSP00000382376; ENSG00000111679. [P29350-3]
Ensembl; ENST00000456013; ENSP00000391592; ENSG00000111679. [P29350-4]
GeneID; 5777; -.
KEGG; hsa:5777; -.
UCSC; uc001qsb.3; human. [P29350-1]
CTD; 5777; -.
DisGeNET; 5777; -.
EuPathDB; HostDB:ENSG00000111679.16; -.
GeneCards; PTPN6; -.
HGNC; HGNC:9658; PTPN6.
HPA; CAB004572; -.
HPA; CAB072845; -.
HPA; HPA001466; -.
MIM; 176883; gene.
neXtProt; NX_P29350; -.
OpenTargets; ENSG00000111679; -.
PharmGKB; PA34002; -.
eggNOG; KOG0790; Eukaryota.
eggNOG; COG5599; LUCA.
GeneTree; ENSGT00920000148980; -.
HOGENOM; HOG000273907; -.
HOVERGEN; HBG000223; -.
InParanoid; P29350; -.
KO; K05697; -.
OMA; QAKGEPW; -.
OrthoDB; EOG091G0VZ3; -.
PhylomeDB; P29350; -.
TreeFam; TF351632; -.
BRENDA; 3.1.3.48; 2681.
Reactome; R-HSA-114604; GPVI-mediated activation cascade.
Reactome; R-HSA-1433559; Regulation of KIT signaling.
Reactome; R-HSA-210990; PECAM1 interactions.
Reactome; R-HSA-388841; Costimulation by the CD28 family.
Reactome; R-HSA-389948; PD-1 signaling.
Reactome; R-HSA-391160; Signal regulatory protein family interactions.
Reactome; R-HSA-432142; Platelet sensitization by LDL.
Reactome; R-HSA-512988; Interleukin-3, 5 and GM-CSF signaling.
Reactome; R-HSA-5690714; CD22 mediated BCR regulation.
Reactome; R-HSA-6798695; Neutrophil degranulation.
Reactome; R-HSA-877300; Interferon gamma signaling.
Reactome; R-HSA-877312; Regulation of IFNG signaling.
Reactome; R-HSA-9008059; Interleukin-37 signaling.
Reactome; R-HSA-909733; Interferon alpha/beta signaling.
Reactome; R-HSA-912526; Interleukin receptor SHC signaling.
Reactome; R-HSA-912694; Regulation of IFNA signaling.
Reactome; R-HSA-982772; Growth hormone receptor signaling.
Reactome; R-HSA-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
SignaLink; P29350; -.
SIGNOR; P29350; -.
ChiTaRS; PTPN6; human.
EvolutionaryTrace; P29350; -.
GeneWiki; PTPN6; -.
GenomeRNAi; 5777; -.
PMAP-CutDB; P29350; -.
PRO; PR:P29350; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000111679; -.
CleanEx; HS_PTPN6; -.
ExpressionAtlas; P29350; baseline and differential.
Genevisible; P29350; HS.
GO; GO:0042105; C:alpha-beta T cell receptor complex; IEA:Ensembl.
GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0016020; C:membrane; TAS:ProtInc.
GO; GO:0005730; C:nucleolus; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
GO; GO:0032991; C:protein-containing complex; IMP:UniProtKB.
GO; GO:0035580; C:specific granule lumen; TAS:Reactome.
GO; GO:1904724; C:tertiary granule lumen; TAS:Reactome.
GO; GO:0050839; F:cell adhesion molecule binding; IEA:Ensembl.
GO; GO:0140031; F:phosphorylation-dependent protein binding; IPI:UniProtKB.
GO; GO:0001784; F:phosphotyrosine residue binding; IMP:UniProtKB.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0004725; F:protein tyrosine phosphatase activity; IMP:UniProtKB.
GO; GO:0042169; F:SH2 domain binding; IEA:Ensembl.
GO; GO:0017124; F:SH3 domain binding; IEA:Ensembl.
GO; GO:0005001; F:transmembrane receptor protein tyrosine phosphatase activity; IDA:UniProtKB.
GO; GO:0033277; P:abortive mitotic cell cycle; IEA:Ensembl.
GO; GO:0006915; P:apoptotic process; TAS:ProtInc.
GO; GO:0050853; P:B cell receptor signaling pathway; IEA:Ensembl.
GO; GO:0030154; P:cell differentiation; IDA:UniProtKB.
GO; GO:0008283; P:cell proliferation; IDA:UniProtKB.
GO; GO:0071345; P:cellular response to cytokine stimulus; TAS:Reactome.
GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; TAS:ProtInc.
GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IEA:Ensembl.
GO; GO:0035556; P:intracellular signal transduction; IEA:Ensembl.
GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
GO; GO:0035855; P:megakaryocyte development; IEA:Ensembl.
GO; GO:0042267; P:natural killer cell mediated cytotoxicity; IEA:Ensembl.
GO; GO:0050859; P:negative regulation of B cell receptor signaling pathway; IEA:Ensembl.
GO; GO:0008285; P:negative regulation of cell proliferation; NAS:UniProtKB.
GO; GO:0002924; P:negative regulation of humoral immune response mediated by circulating immunoglobulin; IEA:Ensembl.
GO; GO:0043407; P:negative regulation of MAP kinase activity; IEA:Ensembl.
GO; GO:0050732; P:negative regulation of peptidyl-tyrosine phosphorylation; IMP:BHF-UCL.
GO; GO:0042130; P:negative regulation of T cell proliferation; IEA:Ensembl.
GO; GO:0050860; P:negative regulation of T cell receptor signaling pathway; IEA:Ensembl.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; IMP:UniProtKB.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:UniProtKB.
GO; GO:0030168; P:platelet activation; TAS:Reactome.
GO; GO:0070527; P:platelet aggregation; IEA:Ensembl.
GO; GO:0030220; P:platelet formation; IEA:Ensembl.
GO; GO:0033630; P:positive regulation of cell adhesion mediated by integrin; IEA:Ensembl.
GO; GO:0008284; P:positive regulation of cell proliferation; IMP:BHF-UCL.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IMP:BHF-UCL.
GO; GO:0006470; P:protein dephosphorylation; IDA:UniProtKB.
GO; GO:0045577; P:regulation of B cell differentiation; IEA:Ensembl.
GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; IDA:UniProtKB.
GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; IMP:BHF-UCL.
GO; GO:0051279; P:regulation of release of sequestered calcium ion into cytosol; IEA:Ensembl.
GO; GO:0060338; P:regulation of type I interferon-mediated signaling pathway; TAS:Reactome.
GO; GO:0031295; P:T cell costimulation; TAS:Reactome.
Gene3D; 3.30.505.10; -; 2.
Gene3D; 3.90.190.10; -; 1.
InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
InterPro; IPR000242; PTPase_domain.
InterPro; IPR000980; SH2.
InterPro; IPR036860; SH2_dom_sf.
InterPro; IPR016130; Tyr_Pase_AS.
InterPro; IPR003595; Tyr_Pase_cat.
InterPro; IPR012152; Tyr_Pase_non-rcpt_typ-6/11.
InterPro; IPR000387; TYR_PHOSPHATASE_dom.
Pfam; PF00017; SH2; 2.
Pfam; PF00102; Y_phosphatase; 1.
PIRSF; PIRSF000929; Tyr-Ptase_nr_6; 1.
PRINTS; PR00700; PRTYPHPHTASE.
PRINTS; PR00401; SH2DOMAIN.
SMART; SM00194; PTPc; 1.
SMART; SM00404; PTPc_motif; 1.
SMART; SM00252; SH2; 2.
SUPFAM; SSF52799; SSF52799; 1.
SUPFAM; SSF55550; SSF55550; 2.
PROSITE; PS50001; SH2; 2.
PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
Hydrolase; Nucleus; Phosphoprotein; Protein phosphatase;
Reference proteome; Repeat; SH2 domain.
CHAIN 1 595 Tyrosine-protein phosphatase non-receptor
type 6.
/FTId=PRO_0000094758.
DOMAIN 4 100 SH2 1. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
DOMAIN 110 213 SH2 2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
DOMAIN 244 515 Tyrosine-protein phosphatase.
{ECO:0000255|PROSITE-ProRule:PRU00160}.
REGION 453 459 Substrate binding. {ECO:0000250}.
ACT_SITE 453 453 Phosphocysteine intermediate.
BINDING 419 419 Substrate. {ECO:0000250}.
BINDING 500 500 Substrate. {ECO:0000250}.
MOD_RES 10 10 Phosphoserine.
{ECO:0000250|UniProtKB:P81718}.
MOD_RES 57 57 Phosphoserine.
{ECO:0000250|UniProtKB:P29351}.
MOD_RES 64 64 Phosphotyrosine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 377 377 Phosphotyrosine.
{ECO:0000250|UniProtKB:P29351}.
MOD_RES 536 536 Phosphotyrosine.
{ECO:0000250|UniProtKB:P29351}.
MOD_RES 564 564 Phosphotyrosine; by LYN.
{ECO:0000269|PubMed:10574931}.
VAR_SEQ 1 39 Missing (in isoform 3).
{ECO:0000303|PubMed:1652101}.
/FTId=VSP_005129.
VAR_SEQ 1 3 MVR -> MLSRG (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_007775.
VAR_SEQ 40 44 SLSVR -> MLSRG (in isoform 3).
{ECO:0000303|PubMed:1652101}.
/FTId=VSP_005130.
VAR_SEQ 559 595 HKEDVYENLHTKNKREEKVKKQRSADKEKSKGSLKRK ->
SLESSAGTVAASPVRRGGQRGLPVPGPPVLSPDLHQLPVLA
PLHPAADTRRMCMRTCTLRTRGRRK (in isoform 4).
{ECO:0000303|PubMed:10497187}.
/FTId=VSP_044447.
CONFLICT 6 6 H -> L (in Ref. 5; AAA82880).
{ECO:0000305}.
CONFLICT 86 86 L -> V (in Ref. 4; AAA36610 and 7;
AAD53317). {ECO:0000305}.
CONFLICT 146 146 V -> E (in Ref. 5; AAA82880/AAA82879).
{ECO:0000305}.
HELIX 11 21 {ECO:0000244|PDB:2B3O}.
STRAND 26 31 {ECO:0000244|PDB:2B3O}.
STRAND 33 45 {ECO:0000244|PDB:2B3O}.
STRAND 48 55 {ECO:0000244|PDB:2B3O}.
STRAND 57 59 {ECO:0000244|PDB:2B3O}.
STRAND 61 63 {ECO:0000244|PDB:2B3O}.
STRAND 68 70 {ECO:0000244|PDB:2B3O}.
HELIX 72 80 {ECO:0000244|PDB:2B3O}.
STRAND 89 91 {ECO:0000244|PDB:2B3O}.
HELIX 105 107 {ECO:0000244|PDB:2B3O}.
STRAND 111 114 {ECO:0000244|PDB:3PS5}.
HELIX 117 127 {ECO:0000244|PDB:2B3O}.
STRAND 132 137 {ECO:0000244|PDB:2B3O}.
STRAND 139 141 {ECO:0000244|PDB:2B3O}.
STRAND 145 154 {ECO:0000244|PDB:2B3O}.
STRAND 155 157 {ECO:0000244|PDB:2RMX}.
STRAND 162 170 {ECO:0000244|PDB:2B3O}.
HELIX 172 174 {ECO:0000244|PDB:3PS5}.
STRAND 175 181 {ECO:0000244|PDB:2B3O}.
STRAND 184 186 {ECO:0000244|PDB:2B3O}.
HELIX 187 197 {ECO:0000244|PDB:2B3O}.
STRAND 199 201 {ECO:0000244|PDB:2RMX}.
STRAND 202 204 {ECO:0000244|PDB:2B3O}.
STRAND 205 207 {ECO:0000244|PDB:2RMX}.
HELIX 221 223 {ECO:0000244|PDB:2B3O}.
STRAND 236 238 {ECO:0000244|PDB:3PS5}.
HELIX 244 256 {ECO:0000244|PDB:4GRZ}.
TURN 257 259 {ECO:0000244|PDB:4HJP}.
HELIX 263 266 {ECO:0000244|PDB:4GRZ}.
HELIX 268 273 {ECO:0000244|PDB:4GRZ}.
STRAND 275 278 {ECO:0000244|PDB:1GWZ}.
TURN 283 285 {ECO:0000244|PDB:4GRZ}.
STRAND 286 288 {ECO:0000244|PDB:4GRZ}.
STRAND 290 292 {ECO:0000244|PDB:4GS0}.
STRAND 294 296 {ECO:0000244|PDB:3PS5}.
TURN 297 300 {ECO:0000244|PDB:4GRZ}.
STRAND 301 307 {ECO:0000244|PDB:4GRZ}.
STRAND 309 312 {ECO:0000244|PDB:1GWZ}.
HELIX 314 316 {ECO:0000244|PDB:1FPR}.
STRAND 321 324 {ECO:0000244|PDB:4GRZ}.
HELIX 329 331 {ECO:0000244|PDB:4GRZ}.
HELIX 332 341 {ECO:0000244|PDB:4GRZ}.
STRAND 346 349 {ECO:0000244|PDB:4GRZ}.
STRAND 353 355 {ECO:0000244|PDB:4GRZ}.
STRAND 356 358 {ECO:0000244|PDB:1FPR}.
STRAND 371 374 {ECO:0000244|PDB:4GRZ}.
STRAND 377 386 {ECO:0000244|PDB:4GRZ}.
STRAND 388 399 {ECO:0000244|PDB:4GRZ}.
HELIX 400 402 {ECO:0000244|PDB:2B3O}.
STRAND 403 405 {ECO:0000244|PDB:1FPR}.
STRAND 407 414 {ECO:0000244|PDB:4GRZ}.
STRAND 419 421 {ECO:0000244|PDB:2B3O}.
STRAND 424 426 {ECO:0000244|PDB:4GRZ}.
HELIX 427 442 {ECO:0000244|PDB:4GRZ}.
STRAND 443 445 {ECO:0000244|PDB:4HJQ}.
STRAND 449 452 {ECO:0000244|PDB:4GRZ}.
STRAND 454 457 {ECO:0000244|PDB:4GRZ}.
HELIX 458 476 {ECO:0000244|PDB:4GRZ}.
HELIX 484 492 {ECO:0000244|PDB:4GRZ}.
HELIX 502 523 {ECO:0000244|PDB:4GRZ}.
SEQUENCE 595 AA; 67561 MW; 4D7736C21D3542D2 CRC64;
MVRWFHRDLS GLDAETLLKG RGVHGSFLAR PSRKNQGDFS LSVRVGDQVT HIRIQNSGDF
YDLYGGEKFA TLTELVEYYT QQQGVLQDRD GTIIHLKYPL NCSDPTSERW YHGHMSGGQA
ETLLQAKGEP WTFLVRESLS QPGDFVLSVL SDQPKAGPGS PLRVTHIKVM CEGGRYTVGG
LETFDSLTDL VEHFKKTGIE EASGAFVYLR QPYYATRVNA ADIENRVLEL NKKQESEDTA
KAGFWEEFES LQKQEVKNLH QRLEGQRPEN KGKNRYKNIL PFDHSRVILQ GRDSNIPGSD
YINANYIKNQ LLGPDENAKT YIASQGCLEA TVNDFWQMAW QENSRVIVMT TREVEKGRNK
CVPYWPEVGM QRAYGPYSVT NCGEHDTTEY KLRTLQVSPL DNGDLIREIW HYQYLSWPDH
GVPSEPGGVL SFLDQINQRQ ESLPHAGPII VHCSAGIGRT GTIIVIDMLM ENISTKGLDC
DIDIQKTIQM VRAQRSGMVQ TEAQYKFIYV AIAQFIETTK KKLEVLQSQK GQESEYGNIT
YPPAMKNAHA KASRTSSKHK EDVYENLHTK NKREEKVKKQ RSADKEKSKG SLKRK


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