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Tyrosine-protein phosphatase non-receptor type 2 (EC 3.1.3.48) (T-cell protein-tyrosine phosphatase) (TCPTP)

 PTN2_HUMAN              Reviewed;         415 AA.
P17706; A8K955; A8MXU3; K7ENG3; Q96AU5; Q96HR2;
01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
05-MAY-2009, sequence version 2.
25-OCT-2017, entry version 190.
RecName: Full=Tyrosine-protein phosphatase non-receptor type 2;
EC=3.1.3.48;
AltName: Full=T-cell protein-tyrosine phosphatase;
Short=TCPTP;
Name=PTPN2; Synonyms=PTPT;
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), AND TISSUE SPECIFICITY.
TISSUE=T-cell;
PubMed=2546150; DOI=10.1073/pnas.86.14.5257;
Cool D., Tonks N.K., Charbonneau H., Walsh K.A., Fischer E.H.,
Krebs E.G.;
"cDNA isolated from a human T-cell library encodes a member of the
protein-tyrosine-phosphatase family.";
Proc. Natl. Acad. Sci. U.S.A. 86:5257-5261(1989).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Testis;
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).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NHLBI resequencing and genotyping service (RS&G);
Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16177791; DOI=10.1038/nature03983;
Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D.,
Taylor T.D., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K.,
FitzGerald M.G., Yang X., Abouelleil A., Allen N.R., Anderson S.,
Bloom T., Bugalter B., Butler J., Cook A., DeCaprio D., Engels R.,
Garber M., Gnirke A., Hafez N., Hall J.L., Norman C.H., Itoh T.,
Jaffe D.B., Kuroki Y., Lehoczky J., Lui A., Macdonald P., Mauceli E.,
Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C., Noguchi H.,
O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
"DNA sequence and analysis of human chromosome 18.";
Nature 437:551-555(2005).
[5]
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.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
TISSUE=Brain, and Eye;
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).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 350-415 (ISOFORM 2), AND TISSUE
SPECIFICITY.
PubMed=1731319; DOI=10.1073/pnas.89.2.499;
Mosinger B. Jr., Tillmann U., Westphal H., Tremblay M.L.;
"Cloning and characterization of a mouse cDNA encoding a cytoplasmic
protein-tyrosine-phosphatase.";
Proc. Natl. Acad. Sci. U.S.A. 89:499-503(1992).
[8]
SUBCELLULAR LOCATION (ISOFORMS 1 AND 2), AND MUTAGENESIS OF
350-ARG--ARG-352 AND LYS-380.
PubMed=7593185; DOI=10.1083/jcb.131.3.631;
Lorenzen J.A., Dadabay C.Y., Fischer E.H.;
"COOH-terminal sequence motifs target the T cell protein tyrosine
phosphatase to the ER and nucleus.";
J. Cell Biol. 131:631-643(1995).
[9]
ENZYME REGULATION.
PubMed=9361013; DOI=10.1074/jbc.272.46.29322;
Hao L., Tiganis T., Tonks N.K., Charbonneau H.;
"The noncatalytic C-terminal segment of the T cell protein tyrosine
phosphatase regulates activity via an intramolecular mechanism.";
J. Biol. Chem. 272:29322-29329(1997).
[10]
FUNCTION IN DEPHOSPHORYLATION OF EGFR AND SHC1, MUTAGENESIS OF
ASP-182, AND SUBCELLULAR LOCATION (ISOFORM 2).
PubMed=9488479; DOI=10.1128/MCB.18.3.1622;
Tiganis T., Bennett A.M., Ravichandran K.S., Tonks N.K.;
"Epidermal growth factor receptor and the adaptor protein p52Shc are
specific substrates of T-cell protein tyrosine phosphatase.";
Mol. Cell. Biol. 18:1622-1634(1998).
[11]
FUNCTION IN DEPHOSPHORYLATION OF INSR.
PubMed=10734133; DOI=10.1074/jbc.275.13.9792;
Waelchli S., Curchod M.L., Gobert R.P., Arkinstall S.,
Hooft van Huijsduijnen R.;
"Identification of tyrosine phosphatases that dephosphorylate the
insulin receptor. A brute force approach based on 'substrate-trapping'
mutants.";
J. Biol. Chem. 275:9792-9796(2000).
[12]
FUNCTION IN DEPHOSPHORYLATION OF STAT3(ISOFORM 2).
PubMed=12359225; DOI=10.1016/S0006-291X(02)02291-X;
Yamamoto T., Sekine Y., Kashima K., Kubota A., Sato N., Aoki N.,
Matsuda T.;
"The nuclear isoform of protein-tyrosine phosphatase TC-PTP regulates
interleukin-6-mediated signaling pathway through STAT3
dephosphorylation.";
Biochem. Biophys. Res. Commun. 297:811-817(2002).
[13]
FUNCTION IN DEPHOSPHORYLATION OF JAK1 AND JAK3, AND INTERACTION WITH
JAK1 AND JAK3.
PubMed=11909529; DOI=10.1016/S0960-9822(02)00697-8;
Simoncic P.D., Lee-Loy A., Barber D.L., Tremblay M.L., McGlade C.J.;
"The T cell protein tyrosine phosphatase is a negative regulator of
janus family kinases 1 and 3.";
Curr. Biol. 12:446-453(2002).
[14]
FUNCTION IN DEPHOSPHORYLATION OF STAT1.
PubMed=12138178; DOI=10.1128/MCB.22.16.5662-5668.2002;
ten Hoeve J., de Jesus Ibarra-Sanchez M., Fu Y., Zhu W., Tremblay M.,
David M., Shuai K.;
"Identification of a nuclear Stat1 protein tyrosine phosphatase.";
Mol. Cell. Biol. 22:5662-5668(2002).
[15]
FUNCTION IN DEPHOSPHORYLATION OF INSR, MUTAGENESIS OF ASP-182, AND
SUBCELLULAR LOCATION (ISOFORM 2).
PubMed=12612081; DOI=10.1128/MCB.23.6.2096-2108.2003;
Galic S., Klingler-Hoffmann M., Fodero-Tavoletti M.T., Puryer M.A.,
Meng T.C., Tonks N.K., Tiganis T.;
"Regulation of insulin receptor signaling by the protein tyrosine
phosphatase TCPTP.";
Mol. Cell. Biol. 23:2096-2108(2003).
[16]
PHOSPHORYLATION AT SER-304 BY CDK1 AND CDK2 (ISOFORM 2), AND
MUTAGENESIS OF SER-304.
PubMed=15030318; DOI=10.1042/BJ20031780;
Bukczynska P., Klingler-Hoffmann M., Mitchelhill K.I., Lam M.H.,
Ciccomancini M., Tonks N.K., Sarcevic B., Kemp B.E., Tiganis T.;
"The T-cell protein tyrosine phosphatase is phosphorylated on Ser-304
by cyclin-dependent protein kinases in mitosis.";
Biochem. J. 380:939-949(2004).
[17]
FUNCTION IN DEPHOSPHORYLATION OF PDGFRB.
PubMed=14966296; DOI=10.1128/MCB.24.5.2190-2201.2004;
Persson C., Saevenhed C., Bourdeau A., Tremblay M.L., Markova B.,
Boehmer F.D., Haj F.G., Neel B.G., Elson A., Heldin C.H.,
Roennstrand L., Ostman A., Hellberg C.;
"Site-selective regulation of platelet-derived growth factor beta
receptor tyrosine phosphorylation by T-cell protein tyrosine
phosphatase.";
Mol. Cell. Biol. 24:2190-2201(2004).
[18]
INTERACTION WITH RMDN3.
PubMed=15609043; DOI=10.1007/s00418-004-0732-7;
Stenzinger A., Kajosch T., Tag C., Porsche A., Welte I., Hofer H.W.,
Steger K., Wimmer M.;
"The novel protein PTPIP51 exhibits tissue- and cell-specific
expression.";
Histochem. Cell Biol. 123:19-28(2005).
[19]
FUNCTION IN DEPHOSPHORYLATION OF EGFR, INTERACTION WITH ITGA1, AND
SUBCELLULAR LOCATION.
PubMed=15592458; DOI=10.1038/ncb1209;
Mattila E., Pellinen T., Nevo J., Vuoriluoto K., Arjonen A.,
Ivaska J.;
"Negative regulation of EGFR signalling through integrin-alpha1beta1-
mediated activation of protein tyrosine phosphatase TCPTP.";
Nat. Cell Biol. 7:78-85(2005).
[20]
INTERACTION WITH TRAF2.
PubMed=15696169; DOI=10.1038/ni1169;
van Vliet C., Bukczynska P.E., Puryer M.A., Sadek C.M., Shields B.J.,
Tremblay M.L., Tiganis T.;
"Selective regulation of tumor necrosis factor-induced Erk signaling
by Src family kinases and the T cell protein tyrosine phosphatase.";
Nat. Immunol. 6:253-260(2005).
[21]
PHOSPHORYLATION BY PKR.
PubMed=16431927; DOI=10.1074/jbc.M504977200;
Wang S., Raven J.F., Baltzis D., Kazemi S., Brunet D.V., Hatzoglou M.,
Tremblay M.L., Koromilas A.E.;
"The catalytic activity of the eukaryotic initiation factor-2alpha
kinase PKR is required to negatively regulate Stat1 and Stat3 via
activation of the T-cell protein-tyrosine phosphatase.";
J. Biol. Chem. 281:9439-9449(2006).
[22]
INTERACTION WITH TMED9.
PubMed=16595549; DOI=10.1242/jcs.02885;
Gupta V., Swarup G.;
"Evidence for a role of transmembrane protein p25 in localization of
protein tyrosine phosphatase TC48 to the ER.";
J. Cell Sci. 119:1703-1714(2006).
[23]
FUNCTION IN DEPHOSPHORYLATION OF STAT6 (ISOFORM 2), AND INDUCTION BY
IL4.
PubMed=17210636; DOI=10.1128/MCB.01234-06;
Lu X., Chen J., Sasmono R.T., Hsi E.D., Sarosiek K.A., Tiganis T.,
Lossos I.S.;
"T-cell protein tyrosine phosphatase, distinctively expressed in
activated-B-cell-like diffuse large B-cell lymphomas, is the nuclear
phosphatase of STAT6.";
Mol. Cell. Biol. 27:2166-2179(2007).
[24]
FUNCTION IN DEPHOSPHORYLATION OF MET, AND INTERACTION WITH MET.
PubMed=18819921; DOI=10.1074/jbc.M805916200;
Sangwan V., Paliouras G.N., Abella J.V., Dube N., Monast A.,
Tremblay M.L., Park M.;
"Regulation of the Met receptor-tyrosine kinase by the protein-
tyrosine phosphatase 1B and T-cell phosphatase.";
J. Biol. Chem. 283:34374-34383(2008).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-298 AND SER-304, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[27]
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).
[28]
FUNCTION IN DEPHOSPHORYLATION OF LCK AND FYN.
PubMed=22080863; DOI=10.1172/JCI59492;
Wiede F., Shields B.J., Chew S.H., Kyparissoudis K., van Vliet C.,
Galic S., Tremblay M.L., Russell S.M., Godfrey D.I., Tiganis T.;
"T cell protein tyrosine phosphatase attenuates T cell signaling to
maintain tolerance in mice.";
J. Clin. Invest. 121:4758-4774(2011).
[29]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[30]
INTERACTION WITH STX17, AND SUBCELLULAR LOCATION.
PubMed=23006999; DOI=10.1016/j.bbamcr.2012.09.003;
Muppirala M., Gupta V., Swarup G.;
"Tyrosine phosphorylation of a SNARE protein, Syntaxin 17:
Implications for membrane trafficking in the early secretory
pathway.";
Biochim. Biophys. Acta 1823:2109-2119(2012).
[31]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-293; SER-298 AND
SER-304, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
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).
[32]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-298 AND SER-304, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[33]
X-RAY CRYSTALLOGRAPHY (2.56 ANGSTROMS) OF 1-314, AND
BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=11907034; DOI=10.1074/jbc.M200567200;
Iversen L.F., Moller K.B., Pedersen A.K., Peters G.H., Petersen A.S.,
Andersen H.S., Branner S., Mortensen S.B., Moller N.P.;
"Structure determination of T cell protein-tyrosine phosphatase.";
J. Biol. Chem. 277:19982-19990(2002).
-!- FUNCTION: Non-receptor type tyrosine-specific phosphatase that
dephosphorylates receptor protein tyrosine kinases including INSR,
EGFR, CSF1R, PDGFR. Also dephosphorylates non-receptor protein
tyrosine kinases like JAK1, JAK2, JAK3, Src family kinases, STAT1,
STAT3 and STAT6 either in the nucleus or the cytoplasm. Negatively
regulates numerous signaling pathways and biological processes
like hematopoiesis, inflammatory response, cell proliferation and
differentiation, and glucose homeostasis. Plays a multifaceted and
important role in the development of the immune system. Functions
in T-cell receptor signaling through dephosphorylation of FYN and
LCK to control T-cells differentiation and activation.
Dephosphorylates CSF1R, negatively regulating its downstream
signaling and macrophage differentiation. Negatively regulates
cytokine (IL2/interleukin-2 and interferon)-mediated signaling
through dephosphorylation of the cytoplasmic kinases JAK1, JAK3
and their substrate STAT1, that propagate signaling downstream of
the cytokine receptors. Also regulates the IL6/interleukin-6 and
IL4/interleukin-4 cytokine signaling through dephosphorylation of
STAT3 and STAT6 respectively. In addition to the immune system, it
is involved in anchorage-dependent, negative regulation of EGF-
stimulated cell growth. Activated by the integrin ITGA1/ITGB1, it
dephosphorylates EGFR and negatively regulates EGF signaling.
Dephosphorylates PDGFRB and negatively regulates platelet-derived
growth factor receptor-beta signaling pathway and therefore cell
proliferation. Negatively regulates tumor necrosis factor-mediated
signaling downstream via MAPK through SRC dephosphorylation. May
also regulate the hepatocyte growth factor receptor signaling
pathway through dephosphorylation of the hepatocyte growth factor
receptor MET. Plays also an important role in glucose homeostasis.
For instance, negatively regulates the insulin receptor signaling
pathway through the dephosphorylation of INSR and control
gluconeogenesis and liver glucose production through negative
regulation of the IL6 signaling pathways. May also bind DNA.
{ECO:0000269|PubMed:10734133, ECO:0000269|PubMed:11909529,
ECO:0000269|PubMed:12138178, ECO:0000269|PubMed:12612081,
ECO:0000269|PubMed:14966296, ECO:0000269|PubMed:15592458,
ECO:0000269|PubMed:18819921, ECO:0000269|PubMed:22080863,
ECO:0000269|PubMed:9488479}.
-!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
tyrosine + phosphate. {ECO:0000255|PROSITE-ProRule:PRU10044}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.48 mM for p-nitrophenyl phosphate (at pH 6.5 and 25 degrees
Celsius) {ECO:0000269|PubMed:11907034};
-!- SUBUNIT: Interacts with RMDN3. Isoform 1 interacts with TMED9.
Isoform 1 interacts with STX17; dephosphorylates STX17. Interacts
with ITGA1 (via cytoplasmic domain); activates the phosphatase
activity towards EGFR. Interacts with TRAF2; probably involved in
tumor necrosis factor-mediated signaling. Interacts with MET.
{ECO:0000269|PubMed:11909529, ECO:0000269|PubMed:15592458,
ECO:0000269|PubMed:15609043, ECO:0000269|PubMed:15696169,
ECO:0000269|PubMed:16595549, ECO:0000269|PubMed:18819921,
ECO:0000269|PubMed:23006999}.
-!- INTERACTION:
P10912:GHR; NbExp=8; IntAct=EBI-984930, EBI-286316;
P49755:TMED10; NbExp=5; IntAct=EBI-4409481, EBI-998422;
Q9BVK6:TMED9; NbExp=5; IntAct=EBI-4409481, EBI-1056827;
-!- SUBCELLULAR LOCATION: Isoform 1: Endoplasmic reticulum
{ECO:0000269|PubMed:7593185}. Endoplasmic reticulum-Golgi
intermediate compartment {ECO:0000269|PubMed:7593185}.
Note=Targeted to the endoplasmic reticulum by its C-terminal
hydrophobic region. {ECO:0000269|PubMed:7593185}.
-!- SUBCELLULAR LOCATION: Isoform 2: Nucleus. Cytoplasm. Cell
membrane. Note=Predominantly localizes to chromatin (By
similarity). Able to shuttle between the nucleus and the cytoplasm
and to dephosphorylate plasma membrane receptors (PubMed:9488479).
Recruited by activated ITGA1 at the plasma membrane. {ECO:0000250,
ECO:0000269|PubMed:9488479}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1; Synonyms=PTPB, p48TC, TC48, TC-PTPb;
IsoId=P17706-1; Sequence=Displayed;
Note=Minor isoform.;
Name=2; Synonyms=PTPA, p45TC, TC45, TC-PTPa;
IsoId=P17706-2; Sequence=VSP_005125;
Note=Major isoform. Contains a phosphoserine at position 304.
Contains a nuclear location signal at positions 377-381 (Ref.8)
and an autoinhibitory region acting through intramolecular
interactions is found at positions 353-387.
{ECO:0000269|PubMed:15030318, ECO:0000305|PubMed:7593185};
Name=3;
IsoId=P17706-3; Sequence=VSP_043383, VSP_005125;
Note=No experimental confirmation available.;
Name=4;
IsoId=P17706-4; Sequence=VSP_054821, VSP_005125;
Note=No experimental confirmation available. Gene prediction
based on cDNA data.;
-!- TISSUE SPECIFICITY: Ubiquitously expressed. Isoform 2 is probably
the major isoform. Isoform 1 is expressed in T-cells and in
placenta. {ECO:0000269|PubMed:1731319,
ECO:0000269|PubMed:2546150}.
-!- INDUCTION: Up-regulated by IL4/interleukin-4 (at protein level).
{ECO:0000269|PubMed:17210636}.
-!- PTM: Isoform 2: Specifically phosphorylated in a cell cycle-
dependent manner by cyclin-dependent kinases CDK1 and CDK2.
Probably activated through phosphorylation by PKR.
{ECO:0000269|PubMed:15030318, ECO:0000269|PubMed:16431927}.
-!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
Non-receptor class 1 subfamily. {ECO:0000305}.
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EMBL; M25393; AAA65997.1; -; mRNA.
EMBL; AK292570; BAF85259.1; -; mRNA.
EMBL; EF445017; ACA06062.1; -; Genomic_DNA.
EMBL; EF445017; ACA06064.1; -; Genomic_DNA.
EMBL; AP001077; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP002449; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP005482; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471113; EAX01532.1; -; Genomic_DNA.
EMBL; CH471113; EAX01539.1; -; Genomic_DNA.
EMBL; BC008244; AAH08244.1; -; mRNA.
EMBL; BC016727; AAH16727.1; -; mRNA.
EMBL; M81478; -; NOT_ANNOTATED_CDS; mRNA.
CCDS; CCDS11863.1; -. [P17706-2]
CCDS; CCDS11864.1; -. [P17706-3]
CCDS; CCDS11865.1; -. [P17706-1]
CCDS; CCDS59306.1; -. [P17706-4]
PIR; A33899; A33899.
RefSeq; NP_001193942.1; NM_001207013.1. [P17706-4]
RefSeq; NP_002819.2; NM_002828.3. [P17706-1]
RefSeq; NP_536347.1; NM_080422.2. [P17706-2]
RefSeq; NP_536348.1; NM_080423.2. [P17706-3]
UniGene; Hs.654527; -.
UniGene; Hs.663373; -.
PDB; 1L8K; X-ray; 2.56 A; A=1-314.
PDBsum; 1L8K; -.
ProteinModelPortal; P17706; -.
SMR; P17706; -.
BioGrid; 111737; 89.
CORUM; P17706; -.
IntAct; P17706; 26.
MINT; MINT-3975566; -.
STRING; 9606.ENSP00000311857; -.
BindingDB; P17706; -.
ChEMBL; CHEMBL3807; -.
DEPOD; P17706; -.
iPTMnet; P17706; -.
PhosphoSitePlus; P17706; -.
BioMuta; PTPN2; -.
DMDM; 229462762; -.
EPD; P17706; -.
MaxQB; P17706; -.
PaxDb; P17706; -.
PeptideAtlas; P17706; -.
PRIDE; P17706; -.
DNASU; 5771; -.
Ensembl; ENST00000309660; ENSP00000311857; ENSG00000175354. [P17706-1]
Ensembl; ENST00000327283; ENSP00000320298; ENSG00000175354. [P17706-2]
Ensembl; ENST00000353319; ENSP00000320546; ENSG00000175354. [P17706-3]
Ensembl; ENST00000591115; ENSP00000466936; ENSG00000175354. [P17706-4]
GeneID; 5771; -.
KEGG; hsa:5771; -.
UCSC; uc002krl.4; human. [P17706-1]
CTD; 5771; -.
DisGeNET; 5771; -.
EuPathDB; HostDB:ENSG00000175354.18; -.
GeneCards; PTPN2; -.
HGNC; HGNC:9650; PTPN2.
HPA; HPA015004; -.
HPA; HPA046176; -.
MalaCards; PTPN2; -.
MIM; 176887; gene.
neXtProt; NX_P17706; -.
OpenTargets; ENSG00000175354; -.
Orphanet; 206; Crohn disease.
Orphanet; 85408; Juvenile rheumatoid factor-negative polyarthritis.
Orphanet; 85410; Oligoarticular juvenile arthritis.
Orphanet; 771; Ulcerative colitis.
PharmGKB; PA33993; -.
eggNOG; KOG0789; Eukaryota.
eggNOG; COG5599; LUCA.
GeneTree; ENSGT00900000140785; -.
HOGENOM; HOG000273908; -.
HOVERGEN; HBG008321; -.
InParanoid; P17706; -.
KO; K18026; -.
OMA; VAKYPEN; -.
OrthoDB; EOG091G082B; -.
PhylomeDB; P17706; -.
TreeFam; TF315897; -.
BRENDA; 3.1.3.48; 2681.
Reactome; R-HSA-6807004; Negative regulation of MET activity.
Reactome; R-HSA-877312; Regulation of IFNG signaling.
SignaLink; P17706; -.
SIGNOR; P17706; -.
ChiTaRS; PTPN2; human.
EvolutionaryTrace; P17706; -.
GeneWiki; PTPN2; -.
GenomeRNAi; 5771; -.
PRO; PR:P17706; -.
Proteomes; UP000005640; Chromosome 18.
Bgee; ENSG00000175354; -.
CleanEx; HS_PTPN2; -.
ExpressionAtlas; P17706; baseline and differential.
Genevisible; P17706; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005178; F:integrin binding; IPI:UniProtKB.
GO; GO:0004726; F:non-membrane spanning protein tyrosine phosphatase activity; IEA:Ensembl.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:UniProtKB.
GO; GO:0030971; F:receptor tyrosine kinase binding; IPI:UniProtKB.
GO; GO:0097677; F:STAT family protein binding; IEA:Ensembl.
GO; GO:0019905; F:syntaxin binding; IPI:UniProtKB.
GO; GO:0030183; P:B cell differentiation; ISS:UniProtKB.
GO; GO:0030218; P:erythrocyte differentiation; ISS:UniProtKB.
GO; GO:0042593; P:glucose homeostasis; ISS:UniProtKB.
GO; GO:0008286; P:insulin receptor signaling pathway; ISS:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; IMP:UniProtKB.
GO; GO:0050922; P:negative regulation of chemotaxis; ISS:UniProtKB.
GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; IMP:UniProtKB.
GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
GO; GO:0050728; P:negative regulation of inflammatory response; ISS:UniProtKB.
GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; ISS:UniProtKB.
GO; GO:0060336; P:negative regulation of interferon-gamma-mediated signaling pathway; ISS:UniProtKB.
GO; GO:1902206; P:negative regulation of interleukin-2-mediated signaling pathway; IMP:UniProtKB.
GO; GO:1902215; P:negative regulation of interleukin-4-mediated signaling pathway; IMP:UniProtKB.
GO; GO:0070104; P:negative regulation of interleukin-6-mediated signaling pathway; IMP:UniProtKB.
GO; GO:0010888; P:negative regulation of lipid storage; ISS:UniProtKB.
GO; GO:1902227; P:negative regulation of macrophage colony-stimulating factor signaling pathway; ISS:UniProtKB.
GO; GO:0045650; P:negative regulation of macrophage differentiation; ISS:UniProtKB.
GO; GO:2000587; P:negative regulation of platelet-derived growth factor receptor-beta signaling pathway; ISS:UniProtKB.
GO; GO:1902233; P:negative regulation of positive thymic T cell selection; ISS:UniProtKB.
GO; GO:0061099; P:negative regulation of protein tyrosine kinase activity; IEA:Ensembl.
GO; GO:0050860; P:negative regulation of T cell receptor signaling pathway; ISS:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
GO; GO:0010804; P:negative regulation of tumor necrosis factor-mediated signaling pathway; ISS:UniProtKB.
GO; GO:0060339; P:negative regulation of type I interferon-mediated signaling pathway; IMP:UniProtKB.
GO; GO:0042532; P:negative regulation of tyrosine phosphorylation of STAT protein; IDA:UniProtKB.
GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; IDA:UniProtKB.
GO; GO:1902237; P:positive regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway; IEA:Ensembl.
GO; GO:0045722; P:positive regulation of gluconeogenesis; ISS:UniProtKB.
GO; GO:1903899; P:positive regulation of PERK-mediated unfolded protein response; IEA:Ensembl.
GO; GO:1902202; P:regulation of hepatocyte growth factor receptor signaling pathway; IMP:UniProtKB.
GO; GO:0060334; P:regulation of interferon-gamma-mediated signaling pathway; TAS:Reactome.
GO; GO:0030217; P:T cell differentiation; ISS:UniProtKB.
Gene3D; 3.90.190.10; -; 1.
InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
InterPro; IPR000242; PTPase_domain.
InterPro; IPR012265; Ptpn1/Ptpn2.
InterPro; IPR016130; Tyr_Pase_AS.
InterPro; IPR003595; Tyr_Pase_cat.
InterPro; IPR000387; TYR_PHOSPHATASE_dom.
Pfam; PF00102; Y_phosphatase; 1.
PIRSF; PIRSF000926; Tyr-Ptase_nr1; 1.
PRINTS; PR00700; PRTYPHPHTASE.
SMART; SM00194; PTPc; 1.
SMART; SM00404; PTPc_motif; 1.
SUPFAM; SSF52799; SSF52799; 1.
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; Cell membrane; Complete proteome;
Cytoplasm; Endoplasmic reticulum; Hydrolase; Membrane; Nucleus;
Phosphoprotein; Protein phosphatase; Reference proteome;
S-nitrosylation.
CHAIN 1 415 Tyrosine-protein phosphatase non-receptor
type 2.
/FTId=PRO_0000094752.
DOMAIN 5 275 Tyrosine-protein phosphatase.
{ECO:0000255|PROSITE-ProRule:PRU00160}.
REGION 216 222 Substrate binding. {ECO:0000250}.
REGION 346 415 Endoplasmic reticulum location.
REGION 376 415 Mediates interaction with STX17.
{ECO:0000269|PubMed:23006999}.
ACT_SITE 216 216 Phosphocysteine intermediate.
{ECO:0000255|PROSITE-ProRule:PRU00160,
ECO:0000255|PROSITE-ProRule:PRU10044}.
BINDING 182 182 Substrate. {ECO:0000250}.
BINDING 260 260 Substrate. {ECO:0000250}.
MOD_RES 22 22 Phosphotyrosine.
{ECO:0000250|UniProtKB:P18031}.
MOD_RES 52 52 Phosphoserine.
{ECO:0000250|UniProtKB:P18031}.
MOD_RES 68 68 Phosphotyrosine.
{ECO:0000250|UniProtKB:P18031}.
MOD_RES 216 216 S-nitrosocysteine.
{ECO:0000250|UniProtKB:P18031}.
MOD_RES 293 293 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 298 298 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 304 304 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
VAR_SEQ 165 165 N -> NYIENLWITLYLKLLMLDVKRSLK (in isoform
4). {ECO:0000305}.
/FTId=VSP_054821.
VAR_SEQ 347 380 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_043383.
VAR_SEQ 382 415 WLYWQPILTKMGFMSVILVGAFVGWTLFFQQNAL -> PRL
TDT (in isoform 2, isoform 3 and isoform
4). {ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:1731319}.
/FTId=VSP_005125.
MUTAGEN 182 182 D->A: Substrate-trapping mutant;
catalytically inactive it forms a stable
complex with physiological substrates
including INSR and EGFR. Accumulates in
the cytoplasm upon stimulation by insulin
or EGF; isoform 2.
{ECO:0000269|PubMed:12612081,
ECO:0000269|PubMed:9488479}.
MUTAGEN 222 222 R->M: Impairs phosphatase activity.
MUTAGEN 304 304 S->A: Alters phosphorylation by cyclin-
dependent kinases of isoform 2 but has no
effect on its phosphatase activity.
{ECO:0000269|PubMed:15030318}.
MUTAGEN 350 352 RKR->QQQ: Alters location to the
endoplasmic reticulum; isoform 1.
{ECO:0000269|PubMed:7593185}.
MUTAGEN 380 380 K->Q: Prevents location to the nucleus;
isoform 2. {ECO:0000269|PubMed:7593185}.
CONFLICT 407 407 T -> R (in Ref. 1; AAA65997 and 7;
M81478). {ECO:0000305}.
HELIX 7 14 {ECO:0000244|PDB:1L8K}.
HELIX 19 28 {ECO:0000244|PDB:1L8K}.
HELIX 35 38 {ECO:0000244|PDB:1L8K}.
HELIX 40 45 {ECO:0000244|PDB:1L8K}.
TURN 55 57 {ECO:0000244|PDB:1L8K}.
STRAND 58 60 {ECO:0000244|PDB:1L8K}.
STRAND 68 76 {ECO:0000244|PDB:1L8K}.
HELIX 77 79 {ECO:0000244|PDB:1L8K}.
STRAND 81 87 {ECO:0000244|PDB:1L8K}.
TURN 91 93 {ECO:0000244|PDB:1L8K}.
HELIX 94 103 {ECO:0000244|PDB:1L8K}.
STRAND 108 111 {ECO:0000244|PDB:1L8K}.
STRAND 129 132 {ECO:0000244|PDB:1L8K}.
STRAND 134 136 {ECO:0000244|PDB:1L8K}.
TURN 137 140 {ECO:0000244|PDB:1L8K}.
STRAND 141 150 {ECO:0000244|PDB:1L8K}.
STRAND 152 163 {ECO:0000244|PDB:1L8K}.
TURN 164 166 {ECO:0000244|PDB:1L8K}.
STRAND 169 177 {ECO:0000244|PDB:1L8K}.
STRAND 182 184 {ECO:0000244|PDB:1L8K}.
HELIX 190 201 {ECO:0000244|PDB:1L8K}.
TURN 202 205 {ECO:0000244|PDB:1L8K}.
STRAND 212 221 {ECO:0000244|PDB:1L8K}.
HELIX 222 235 {ECO:0000244|PDB:1L8K}.
STRAND 236 239 {ECO:0000244|PDB:1L8K}.
HELIX 244 251 {ECO:0000244|PDB:1L8K}.
TURN 252 254 {ECO:0000244|PDB:1L8K}.
HELIX 262 275 {ECO:0000244|PDB:1L8K}.
SEQUENCE 415 AA; 48473 MW; 0207694A4F058E68 CRC64;
MPTTIEREFE ELDTQRRWQP LYLEIRNESH DYPHRVAKFP ENRNRNRYRD VSPYDHSRVK
LQNAENDYIN ASLVDIEEAQ RSYILTQGPL PNTCCHFWLM VWQQKTKAVV MLNRIVEKES
VKCAQYWPTD DQEMLFKETG FSVKLLSEDV KSYYTVHLLQ LENINSGETR TISHFHYTTW
PDFGVPESPA SFLNFLFKVR ESGSLNPDHG PAVIHCSAGI GRSGTFSLVD TCLVLMEKGD
DINIKQVLLN MRKYRMGLIQ TPDQLRFSYM AIIEGAKCIK GDSSIQKRWK ELSKEDLSPA
FDHSPNKIMT EKYNGNRIGL EEEKLTGDRC TGLSSKMQDT MEENSESALR KRIREDRKAT
TAQKVQQMKQ RLNENERKRK RWLYWQPILT KMGFMSVILV GAFVGWTLFF QQNAL


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