PTN1_HUMAN
ID PTN1_HUMAN Reviewed; 435 AA.
AC P18031; Q5TGD8; Q9BQV9; Q9NQQ4;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 251.
DE RecName: Full=Tyrosine-protein phosphatase non-receptor type 1;
DE EC=3.1.3.48;
DE AltName: Full=Protein-tyrosine phosphatase 1B;
DE Short=PTP-1B;
GN Name=PTPN1; Synonyms=PTP1B;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Placenta;
RX PubMed=2157211; DOI=10.1073/pnas.87.7.2735;
RA Chernoff J., Schievella A.R., Jost C.A., Erikson R.L., Neel B.G.;
RT "Cloning of a cDNA for a major human protein-tyrosine-phosphatase.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:2735-2739(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC TISSUE=Placenta;
RX PubMed=2164224; DOI=10.1073/pnas.87.13.5148;
RA Brown-Shimer S., Johnson K.A., Lawrence J.B., Johnson C., Bruskin A.,
RA Green N.R., Hill D.E.;
RT "Molecular cloning and chromosome mapping of the human gene encoding
RT protein phosphotyrosyl phosphatase 1B.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:5148-5152(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye, and Lymph;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PROTEIN SEQUENCE OF 1-321, AND ACETYLATION AT MET-1.
RC TISSUE=Placenta;
RX PubMed=2546149; DOI=10.1073/pnas.86.14.5252;
RA Charbonneau H., Tonks N.K., Kumar S., Diltz C.D., Harrylock M., Cool D.E.,
RA Krebs E.G., Fischer E.H., Walsh K.A.;
RT "Human placenta protein-tyrosine-phosphatase: amino acid sequence and
RT relationship to a family of receptor-like proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:5252-5256(1989).
RN [7]
RP PHOSPHORYLATION AT SER-352; SER-378 AND SER-386.
RX PubMed=8491187; DOI=10.1002/j.1460-2075.1993.tb05843.x;
RA Flint A.J., Gebbink M.F.G.B., Franza B.R. Jr., Hill D.E., Tonks N.K.;
RT "Multi-site phosphorylation of the protein tyrosine phosphatase, PTP1B:
RT identification of cell cycle regulated and phorbol ester stimulated sites
RT of phosphorylation.";
RL EMBO J. 12:1937-1946(1993).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=1739967; DOI=10.1016/0092-8674(92)90190-n;
RA Frangioni J.V., Beahm P.H., Shifrin V., Jost C.A., Neel B.G.;
RT "The nontransmembrane tyrosine phosphatase PTP-1B localizes to the
RT endoplasmic reticulum via its 35 amino acid C-terminal sequence.";
RL Cell 68:545-560(1992).
RN [9]
RP PHOSPHORYLATION AT TYR-66.
RX PubMed=9355745; DOI=10.1042/bj3270139;
RA Liu F., Chernoff J.;
RT "Protein tyrosine phosphatase 1B interacts with and is tyrosine
RT phosphorylated by the epidermal growth factor receptor.";
RL Biochem. J. 327:139-145(1997).
RN [10]
RP PHOSPHORYLATION AT SER-50; SER-242 AND SER-243, AND MUTAGENESIS OF SER-50.
RX PubMed=10480872; DOI=10.1074/jbc.274.38.26697;
RA Moeslein F.M., Myers M.P., Landreth G.E.;
RT "The CLK family kinases, CLK1 and CLK2, phosphorylate and activate the
RT tyrosine phosphatase, PTP-1B.";
RL J. Biol. Chem. 274:26697-26704(1999).
RN [11]
RP PHOSPHORYLATION AT SER-50, AND MUTAGENESIS OF SER-50.
RX PubMed=11579209; DOI=10.1210/mend.15.10.0711;
RA Ravichandran L.V., Chen H., Li Y., Quon M.J.;
RT "Phosphorylation of PTP1B at Ser(50) by Akt impairs its ability to
RT dephosphorylate the insulin receptor.";
RL Mol. Endocrinol. 15:1768-1780(2001).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-20, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [13]
RP FUNCTION IN DEPHOSPHORYLATION OF MET, AND INTERACTION WITH MET.
RX PubMed=18819921; DOI=10.1074/jbc.m805916200;
RA Sangwan V., Paliouras G.N., Abella J.V., Dube N., Monast A., Tremblay M.L.,
RA Park M.;
RT "Regulation of the Met receptor-tyrosine kinase by the protein-tyrosine
RT phosphatase 1B and T-cell phosphatase.";
RL J. Biol. Chem. 283:34374-34383(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-352, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [15]
RP INTERACTION WITH EPHA3, FUNCTION IN EPHA3 DEPHOSPHORYLATION, AND
RP SUBCELLULAR LOCATION.
RX PubMed=21135139; DOI=10.1083/jcb.201005035;
RA Nievergall E., Janes P.W., Stegmayer C., Vail M.E., Haj F.G., Teng S.W.,
RA Neel B.G., Bastiaens P.I., Lackmann M.;
RT "PTP1B regulates Eph receptor function and trafficking.";
RL J. Cell Biol. 191:1189-1203(2010).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-352, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [18]
RP FUNCTION, SULFHYDRATION AT CYS-215, S-NITROSYLATION AT CYS-215, MUTAGENESIS
RP OF CYS-215, AND MUTAGENESIS OF ASP-181 AND CYS-215.
RX PubMed=22169477; DOI=10.1126/scisignal.2002329;
RA Krishnan N., Fu C., Pappin D.J., Tonks N.K.;
RT "H2s-induced sulfhydration of the phosphatase PTP1B and its role in the
RT endoplasmic reticulum stress response.";
RL Sci. Signal. 4:RA86-RA86(2011).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-378, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50; SER-352; SER-363;
RP SER-365; THR-368; SER-378 AND SER-386, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [21]
RP TISSUE SPECIFICITY.
RX PubMed=29043977; DOI=10.7554/elife.27356;
RA Mishra A., Oules B., Pisco A.O., Ly T., Liakath-Ali K., Walko G.,
RA Viswanathan P., Tihy M., Nijjher J., Dunn S.J., Lamond A.I., Watt F.M.;
RT "A protein phosphatase network controls the temporal and spatial dynamics
RT of differentiation commitment in human epidermis.";
RL Elife 6:0-0(2017).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-321.
RX PubMed=8128219; DOI=10.1126/science.8128219;
RA Barford D., Flint A.J., Tonks N.K.;
RT "Crystal structure of human protein tyrosine phosphatase 1B.";
RL Science 263:1397-1404(1994).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-298 OF MUTANT SER-215.
RX PubMed=9391040; DOI=10.1073/pnas.94.25.13420;
RA Puius Y.A., Zhao Y., Sullivan M., Lawrence D.S., Almo S.C., Zhang Z.Y.;
RT "Identification of a second aryl phosphate-binding site in protein-tyrosine
RT phosphatase 1B: a paradigm for inhibitor design.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:13420-13425(1997).
RN [24]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-285.
RX PubMed=9553104; DOI=10.1074/jbc.273.17.10454;
RA Pannifer A.D., Flint A.J., Tonks N.K., Barford D.;
RT "Visualization of the cysteinyl-phosphate intermediate of a protein-
RT tyrosine phosphatase by X-ray crystallography.";
RL J. Biol. Chem. 273:10454-10462(1998).
RN [25]
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 1-298.
RX PubMed=9922143; DOI=10.1021/bi9816958;
RA Groves M.R., Yao Z.-J., Roller P.P., Burke T.R. Jr., Barford D.;
RT "Structural basis for inhibition of the protein tyrosine phosphatase 1B by
RT phosphotyrosine peptide mimetics.";
RL Biochemistry 37:17773-17783(1998).
RN [26]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1-321, OXIDATION AT CYS-215, AND
RP CROSS-LINK 215-CYS-SER-216.
RX PubMed=12802338; DOI=10.1038/nature01680;
RA Salmeen A., Andersen J.N., Myers M.P., Meng T.-C., Hinks J.A., Tonks N.K.,
RA Barford D.;
RT "Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-
RT amide intermediate.";
RL Nature 423:769-773(2003).
RN [27]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-321, OXIDATION AT CYS-215, AND
RP CROSS-LINK 215-CYS-SER-216.
RX PubMed=12802339; DOI=10.1038/nature01681;
RA Van Montfort R.L.M., Congreve M., Tisi D., Carr R., Jhoti H.;
RT "Oxidation state of the active-site cysteine in protein tyrosine
RT phosphatase 1B.";
RL Nature 423:773-777(2003).
RN [28]
RP ASSOCIATION OF VARIANT LEU-387 WITH LOW GLUCOSE TOLERANCE.
RX PubMed=15919835; DOI=10.1038/oby.2005.95;
RA Ukkola O., Rankinen T., Lakka T., Leon A.S., Skinner J.S., Wilmore J.H.,
RA Rao D.C., Kesaeniemi Y.A., Bouchard C.;
RT "Protein tyrosine phosphatase 1B variant associated with fat distribution
RT and insulin metabolism.";
RL Obes. Res. 13:829-834(2005).
CC -!- FUNCTION: Tyrosine-protein phosphatase which acts as a regulator of
CC endoplasmic reticulum unfolded protein response. Mediates
CC dephosphorylation of EIF2AK3/PERK; inactivating the protein kinase
CC activity of EIF2AK3/PERK. May play an important role in CKII- and p60c-
CC src-induced signal transduction cascades. May regulate the EFNA5-EPHA3
CC signaling pathway which modulates cell reorganization and cell-cell
CC repulsion. May also regulate the hepatocyte growth factor receptor
CC signaling pathway through dephosphorylation of MET.
CC {ECO:0000269|PubMed:18819921, ECO:0000269|PubMed:21135139,
CC ECO:0000269|PubMed:22169477}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10044};
CC -!- SUBUNIT: Interacts with EPHA3 (phosphorylated); dephosphorylates EPHA3
CC and may regulate its trafficking and function. Interacts with MET.
CC {ECO:0000269|PubMed:18819921, ECO:0000269|PubMed:21135139}.
CC -!- INTERACTION:
CC P18031; Q13520: AQP6; NbExp=3; IntAct=EBI-968788, EBI-13059134;
CC P18031; P56945: BCAR1; NbExp=5; IntAct=EBI-968788, EBI-702093;
CC P18031; P11274-1: BCR; NbExp=3; IntAct=EBI-968788, EBI-8658094;
CC P18031; P07384: CAPN1; NbExp=4; IntAct=EBI-968788, EBI-1542113;
CC P18031; Q03135: CAV1; NbExp=5; IntAct=EBI-968788, EBI-603614;
CC P18031; Q14247: CTTN; NbExp=2; IntAct=EBI-968788, EBI-351886;
CC P18031; P00533: EGFR; NbExp=8; IntAct=EBI-968788, EBI-297353;
CC P18031; Q9GZR5: ELOVL4; NbExp=3; IntAct=EBI-968788, EBI-18535450;
CC P18031; P19235: EPOR; NbExp=3; IntAct=EBI-968788, EBI-617321;
CC P18031; P10912: GHR; NbExp=5; IntAct=EBI-968788, EBI-286316;
CC P18031; P62993: GRB2; NbExp=4; IntAct=EBI-968788, EBI-401755;
CC P18031; P08069: IGF1R; NbExp=3; IntAct=EBI-968788, EBI-475981;
CC P18031; P06213: INSR; NbExp=32; IntAct=EBI-968788, EBI-475899;
CC P18031; P06213-1: INSR; NbExp=2; IntAct=EBI-968788, EBI-15558981;
CC P18031; P05556: ITGB1; NbExp=2; IntAct=EBI-968788, EBI-703066;
CC P18031; P05106: ITGB3; NbExp=4; IntAct=EBI-968788, EBI-702847;
CC P18031; O60674: JAK2; NbExp=5; IntAct=EBI-968788, EBI-518647;
CC P18031; O43561: LAT; NbExp=3; IntAct=EBI-968788, EBI-1222766;
CC P18031; P08581: MET; NbExp=3; IntAct=EBI-968788, EBI-1039152;
CC P18031; P04629: NTRK1; NbExp=2; IntAct=EBI-968788, EBI-1028226;
CC P18031; P09619: PDGFRB; NbExp=3; IntAct=EBI-968788, EBI-641237;
CC P18031; P57054: PIGP; NbExp=3; IntAct=EBI-968788, EBI-17630288;
CC P18031; P08922: ROS1; NbExp=3; IntAct=EBI-968788, EBI-7371065;
CC P18031; P12931: SRC; NbExp=14; IntAct=EBI-968788, EBI-621482;
CC P18031; P40763: STAT3; NbExp=2; IntAct=EBI-968788, EBI-518675;
CC P18031; P42229: STAT5A; NbExp=2; IntAct=EBI-968788, EBI-749537;
CC P18031; Q9NPL8: TIMMDC1; NbExp=3; IntAct=EBI-968788, EBI-6268651;
CC P18031; Q96HV5: TMEM41A; NbExp=3; IntAct=EBI-968788, EBI-10288884;
CC P18031; Q8N661: TMEM86B; NbExp=3; IntAct=EBI-968788, EBI-2548832;
CC P18031; Q9H1D0: TRPV6; NbExp=6; IntAct=EBI-968788, EBI-7198335;
CC P18031; P10599: TXN; NbExp=2; IntAct=EBI-968788, EBI-594644;
CC P18031; Q61140: Bcar1; Xeno; NbExp=5; IntAct=EBI-968788, EBI-77088;
CC P18031; Q63767: Bcar1; Xeno; NbExp=5; IntAct=EBI-968788, EBI-1176801;
CC P18031; P15116: Cdh2; Xeno; NbExp=3; IntAct=EBI-968788, EBI-397974;
CC P18031; Q63768: Crk; Xeno; NbExp=2; IntAct=EBI-968788, EBI-8423843;
CC P18031; P62994: Grb2; Xeno; NbExp=3; IntAct=EBI-968788, EBI-401775;
CC P18031; P35570: Irs1; Xeno; NbExp=3; IntAct=EBI-968788, EBI-520230;
CC P18031; P05622: Pdgfrb; Xeno; NbExp=3; IntAct=EBI-968788, EBI-1554855;
CC P18031; P10686: Plcg1; Xeno; NbExp=4; IntAct=EBI-968788, EBI-520788;
CC P18031; P34152: Ptk2; Xeno; NbExp=2; IntAct=EBI-968788, EBI-77070;
CC P18031; Q8VI36: Pxn; Xeno; NbExp=2; IntAct=EBI-968788, EBI-983394;
CC P18031; Q9WUD9: Src; Xeno; NbExp=2; IntAct=EBI-968788, EBI-7784541;
CC P18031; P63166: Sumo1; Xeno; NbExp=2; IntAct=EBI-968788, EBI-80152;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:1739967, ECO:0000269|PubMed:21135139}; Peripheral
CC membrane protein {ECO:0000269|PubMed:1739967,
CC ECO:0000269|PubMed:21135139}; Cytoplasmic side
CC {ECO:0000269|PubMed:1739967, ECO:0000269|PubMed:21135139}.
CC Note=Interacts with EPHA3 at the cell membrane.
CC -!- TISSUE SPECIFICITY: Expressed in keratinocytes (at protein level).
CC {ECO:0000269|PubMed:29043977}.
CC -!- PTM: Oxidized on Cys-215; the Cys-SOH formed in response to redox
CC signaling reacts with the alpha-amido of the following residue to form
CC a sulfenamide cross-link, triggering a conformational change that
CC inhibits substrate binding and activity. The active site can be
CC restored by reduction. {ECO:0000269|PubMed:12802338,
CC ECO:0000269|PubMed:12802339}.
CC -!- PTM: Ser-50 is the major site of phosphorylation as compared to Ser-242
CC and Ser-243. Activated by phosphorylation at Ser-50.
CC {ECO:0000269|PubMed:10480872, ECO:0000269|PubMed:11579209,
CC ECO:0000269|PubMed:8491187, ECO:0000269|PubMed:9355745}.
CC -!- PTM: S-nitrosylation of Cys-215 inactivates the enzyme activity.
CC {ECO:0000269|PubMed:22169477}.
CC -!- PTM: Sulfhydration at Cys-215 following endoplasmic reticulum stress
CC inactivates the enzyme activity, promoting EIF2AK3/PERK activity.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class 1 subfamily. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/PTPN1ID41909ch20q13.html";
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DR EMBL; M31724; AAA60223.1; -; mRNA.
DR EMBL; M33689; AAA60157.1; -; mRNA.
DR EMBL; M33684; AAA60158.1; -; Genomic_DNA.
DR EMBL; M33688; AAA60158.1; JOINED; Genomic_DNA.
DR EMBL; M33687; AAA60158.1; JOINED; Genomic_DNA.
DR EMBL; M33686; AAA60158.1; JOINED; Genomic_DNA.
DR EMBL; M33685; AAA60158.1; JOINED; Genomic_DNA.
DR EMBL; BT006752; AAP35398.1; -; mRNA.
DR EMBL; AL133230; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL034429; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC015660; AAH15660.1; -; mRNA.
DR EMBL; BC018164; AAH18164.1; -; mRNA.
DR CCDS; CCDS13430.1; -.
DR PIR; A35992; TPHUN1.
DR RefSeq; NP_001265547.1; NM_001278618.1.
DR RefSeq; NP_002818.1; NM_002827.3.
DR PDB; 1A5Y; X-ray; 2.50 A; A=1-330.
DR PDB; 1AAX; X-ray; 1.90 A; A=1-321.
DR PDB; 1BZC; X-ray; 2.35 A; A=1-321.
DR PDB; 1BZH; X-ray; 2.10 A; A=1-298.
DR PDB; 1BZJ; X-ray; 2.25 A; A=2-298.
DR PDB; 1C83; X-ray; 1.80 A; A=1-298.
DR PDB; 1C84; X-ray; 2.35 A; A=1-298.
DR PDB; 1C85; X-ray; 2.72 A; A=1-298.
DR PDB; 1C86; X-ray; 2.30 A; A=1-298.
DR PDB; 1C87; X-ray; 2.10 A; A=1-298.
DR PDB; 1C88; X-ray; 1.80 A; A=1-298.
DR PDB; 1ECV; X-ray; 1.95 A; A=1-298.
DR PDB; 1EEN; X-ray; 1.90 A; A=1-321.
DR PDB; 1EEO; X-ray; 1.80 A; A=1-321.
DR PDB; 1G1F; X-ray; 2.00 A; A=1-298.
DR PDB; 1G1G; X-ray; 2.20 A; A=1-298.
DR PDB; 1G1H; X-ray; 2.40 A; A=1-298.
DR PDB; 1G7F; X-ray; 1.80 A; A=1-298.
DR PDB; 1G7G; X-ray; 2.20 A; A=1-298.
DR PDB; 1GFY; X-ray; 2.13 A; A=1-298.
DR PDB; 1I57; X-ray; 2.10 A; A=1-298.
DR PDB; 1JF7; X-ray; 2.20 A; A/B=1-298.
DR PDB; 1KAK; X-ray; 2.50 A; A=1-298.
DR PDB; 1KAV; X-ray; 2.35 A; A=1-298.
DR PDB; 1L8G; X-ray; 2.50 A; A=1-321.
DR PDB; 1LQF; X-ray; 2.50 A; A/B/C/D=1-283.
DR PDB; 1NL9; X-ray; 2.40 A; A=1-321.
DR PDB; 1NNY; X-ray; 2.40 A; A=1-321.
DR PDB; 1NO6; X-ray; 2.40 A; A=1-321.
DR PDB; 1NWE; X-ray; 3.10 A; A=1-298.
DR PDB; 1NWL; X-ray; 2.40 A; A=1-298.
DR PDB; 1NZ7; X-ray; 2.40 A; A=1-321.
DR PDB; 1OEM; X-ray; 1.80 A; X=1-321.
DR PDB; 1OEO; X-ray; 2.15 A; X=1-321.
DR PDB; 1OES; X-ray; 2.20 A; A=1-321.
DR PDB; 1OET; X-ray; 2.30 A; A=1-321.
DR PDB; 1OEU; X-ray; 2.50 A; A=1-321.
DR PDB; 1OEV; X-ray; 2.20 A; A=1-321.
DR PDB; 1ONY; X-ray; 2.15 A; A=1-321.
DR PDB; 1ONZ; X-ray; 2.40 A; A=1-321.
DR PDB; 1PA1; X-ray; 1.60 A; A=1-298.
DR PDB; 1PH0; X-ray; 2.20 A; A=1-321.
DR PDB; 1PTT; X-ray; 2.90 A; A=1-321.
DR PDB; 1PTU; X-ray; 2.60 A; A=1-321.
DR PDB; 1PTV; X-ray; 2.30 A; A=1-321.
DR PDB; 1PTY; X-ray; 1.85 A; A=1-321.
DR PDB; 1PXH; X-ray; 2.15 A; A=1-321.
DR PDB; 1PYN; X-ray; 2.20 A; A=1-321.
DR PDB; 1Q1M; X-ray; 2.60 A; A=1-321.
DR PDB; 1Q6J; X-ray; 2.20 A; A=1-298.
DR PDB; 1Q6M; X-ray; 2.20 A; A=1-298.
DR PDB; 1Q6N; X-ray; 2.10 A; A/B=1-298.
DR PDB; 1Q6P; X-ray; 2.30 A; A/B=1-298.
DR PDB; 1Q6S; X-ray; 2.20 A; A/B=1-298.
DR PDB; 1Q6T; X-ray; 2.30 A; A/B=1-298.
DR PDB; 1QXK; X-ray; 2.30 A; A=1-321.
DR PDB; 1SUG; X-ray; 1.95 A; A=1-321.
DR PDB; 1T48; X-ray; 2.20 A; A=1-298.
DR PDB; 1T49; X-ray; 1.90 A; A=1-298.
DR PDB; 1T4J; X-ray; 2.70 A; A=1-298.
DR PDB; 1WAX; X-ray; 2.20 A; A=1-321.
DR PDB; 1XBO; X-ray; 2.50 A; A=1-321.
DR PDB; 2AZR; X-ray; 2.00 A; A=1-299.
DR PDB; 2B07; X-ray; 2.10 A; A=1-299.
DR PDB; 2B4S; X-ray; 2.30 A; A/C=1-298.
DR PDB; 2BGD; X-ray; 2.40 A; A=1-321.
DR PDB; 2BGE; X-ray; 1.80 A; A=1-321.
DR PDB; 2CM2; X-ray; 1.50 A; A=2-298.
DR PDB; 2CM3; X-ray; 2.10 A; A/B=1-298.
DR PDB; 2CM7; X-ray; 2.10 A; A=1-321.
DR PDB; 2CM8; X-ray; 2.10 A; A=1-321.
DR PDB; 2CMA; X-ray; 2.30 A; A=1-321.
DR PDB; 2CMB; X-ray; 1.70 A; A=1-298.
DR PDB; 2CMC; X-ray; 2.20 A; A=1-298.
DR PDB; 2CNE; X-ray; 1.80 A; A=1-298.
DR PDB; 2CNF; X-ray; 2.20 A; A=1-321.
DR PDB; 2CNG; X-ray; 1.90 A; A=1-321.
DR PDB; 2CNH; X-ray; 1.80 A; A=1-321.
DR PDB; 2CNI; X-ray; 2.00 A; A=1-321.
DR PDB; 2F6F; X-ray; 2.00 A; A=1-298.
DR PDB; 2F6T; X-ray; 1.70 A; A=1-298.
DR PDB; 2F6V; X-ray; 1.70 A; A=1-298.
DR PDB; 2F6W; X-ray; 2.20 A; A=1-298.
DR PDB; 2F6Y; X-ray; 2.15 A; A=1-298.
DR PDB; 2F6Z; X-ray; 1.70 A; A=1-298.
DR PDB; 2F70; X-ray; 2.12 A; A=1-298.
DR PDB; 2F71; X-ray; 1.55 A; A=1-298.
DR PDB; 2FJM; X-ray; 2.10 A; A/B=1-298.
DR PDB; 2FJN; X-ray; 2.20 A; A/B=1-298.
DR PDB; 2H4G; X-ray; 2.50 A; A=1-299.
DR PDB; 2H4K; X-ray; 2.30 A; A=1-299.
DR PDB; 2HB1; X-ray; 2.00 A; A=1-299.
DR PDB; 2HNP; X-ray; 2.85 A; A=1-321.
DR PDB; 2HNQ; X-ray; 2.85 A; A=1-321.
DR PDB; 2NT7; X-ray; 2.10 A; A=1-299.
DR PDB; 2NTA; X-ray; 2.10 A; A=1-299.
DR PDB; 2QBP; X-ray; 2.50 A; A=1-299.
DR PDB; 2QBQ; X-ray; 2.10 A; A=1-299.
DR PDB; 2QBR; X-ray; 2.30 A; A=1-299.
DR PDB; 2QBS; X-ray; 2.10 A; A=1-299.
DR PDB; 2VEU; X-ray; 2.40 A; A=1-321.
DR PDB; 2VEV; X-ray; 1.80 A; A=1-321.
DR PDB; 2VEW; X-ray; 2.00 A; A=1-321.
DR PDB; 2VEX; X-ray; 2.20 A; A=1-321.
DR PDB; 2VEY; X-ray; 2.20 A; A=1-321.
DR PDB; 2ZMM; X-ray; 2.10 A; A=1-299.
DR PDB; 2ZN7; X-ray; 2.10 A; A=1-299.
DR PDB; 3A5J; X-ray; 1.70 A; A=2-321.
DR PDB; 3A5K; X-ray; 1.85 A; A=2-298.
DR PDB; 3CWE; X-ray; 1.60 A; A=1-283.
DR PDB; 3D9C; X-ray; 2.30 A; A=1-321.
DR PDB; 3EAX; X-ray; 1.90 A; A=1-321.
DR PDB; 3EB1; X-ray; 2.40 A; A=1-321.
DR PDB; 3EU0; X-ray; 2.70 A; A=1-282.
DR PDB; 3I7Z; X-ray; 2.30 A; A=1-321.
DR PDB; 3I80; X-ray; 2.25 A; A=1-321.
DR PDB; 3QKP; X-ray; 2.05 A; A=1-321.
DR PDB; 3QKQ; X-ray; 2.20 A; A=1-321.
DR PDB; 3SME; X-ray; 1.70 A; A=1-298.
DR PDB; 3ZMP; X-ray; 2.62 A; A/B=1-321.
DR PDB; 3ZMQ; X-ray; 3.30 A; A=1-321.
DR PDB; 3ZV2; X-ray; 2.80 A; A=1-320.
DR PDB; 4BJO; X-ray; 2.06 A; A/B=2-321.
DR PDB; 4I8N; X-ray; 2.50 A; A=1-320.
DR PDB; 4QAH; X-ray; 2.40 A; A=1-299.
DR PDB; 4QAP; X-ray; 1.90 A; A=1-299.
DR PDB; 4QBE; X-ray; 2.29 A; A=1-298.
DR PDB; 4QBW; X-ray; 1.91 A; A=1-299.
DR PDB; 4Y14; X-ray; 1.90 A; A/B=2-301.
DR PDB; 4ZRT; X-ray; 1.74 A; A=1-298.
DR PDB; 5K9V; X-ray; 1.90 A; A=1-301.
DR PDB; 5K9W; X-ray; 2.01 A; A=1-301.
DR PDB; 5KA0; X-ray; 1.99 A; A=1-284.
DR PDB; 5KA1; X-ray; 1.84 A; A=1-284.
DR PDB; 5KA2; X-ray; 2.07 A; A=1-301.
DR PDB; 5KA3; X-ray; 2.14 A; A=1-301.
DR PDB; 5KA4; X-ray; 2.19 A; A=1-301.
DR PDB; 5KA7; X-ray; 2.06 A; A=1-301.
DR PDB; 5KA8; X-ray; 1.97 A; A=1-301.
DR PDB; 5KA9; X-ray; 2.07 A; A=1-301.
DR PDB; 5KAA; X-ray; 1.97 A; A=1-284.
DR PDB; 5KAB; X-ray; 1.97 A; A=1-284.
DR PDB; 5KAC; X-ray; 1.90 A; A=1-301.
DR PDB; 5KAD; X-ray; 1.90 A; A/B=1-301.
DR PDB; 5QDE; X-ray; 1.76 A; A=1-321.
DR PDB; 5QDF; X-ray; 1.71 A; A=1-321.
DR PDB; 5QDG; X-ray; 1.79 A; A=1-321.
DR PDB; 5QDH; X-ray; 1.68 A; A=1-321.
DR PDB; 5QDI; X-ray; 1.62 A; A=1-321.
DR PDB; 5QDJ; X-ray; 1.76 A; A=1-321.
DR PDB; 5QDK; X-ray; 1.55 A; A=1-321.
DR PDB; 5QDL; X-ray; 1.83 A; A=1-321.
DR PDB; 5QDM; X-ray; 2.65 A; A=1-321.
DR PDB; 5QDN; X-ray; 1.82 A; A=1-321.
DR PDB; 5QDO; X-ray; 1.79 A; A=1-321.
DR PDB; 5QDP; X-ray; 1.74 A; A=1-321.
DR PDB; 5QDQ; X-ray; 1.57 A; A=1-321.
DR PDB; 5QDR; X-ray; 1.78 A; A=1-321.
DR PDB; 5QDS; X-ray; 1.75 A; A=1-321.
DR PDB; 5QDT; X-ray; 1.82 A; A=1-321.
DR PDB; 5QDU; X-ray; 1.67 A; A=1-321.
DR PDB; 5QDV; X-ray; 1.77 A; A=1-321.
DR PDB; 5QDW; X-ray; 2.21 A; A=1-321.
DR PDB; 5QDX; X-ray; 2.06 A; A=1-321.
DR PDB; 5QDY; X-ray; 1.83 A; A=1-321.
DR PDB; 5QDZ; X-ray; 2.14 A; A=1-321.
DR PDB; 5QE0; X-ray; 1.98 A; A=1-321.
DR PDB; 5QE1; X-ray; 1.69 A; A=1-321.
DR PDB; 5QE2; X-ray; 1.79 A; A=1-321.
DR PDB; 5QE3; X-ray; 1.74 A; A=1-321.
DR PDB; 5QE4; X-ray; 1.85 A; A=1-321.
DR PDB; 5QE5; X-ray; 1.77 A; A=1-321.
DR PDB; 5QE6; X-ray; 1.77 A; A=1-321.
DR PDB; 5QE7; X-ray; 1.71 A; A=1-321.
DR PDB; 5QE8; X-ray; 1.81 A; A=1-321.
DR PDB; 5QE9; X-ray; 1.69 A; A=1-321.
DR PDB; 5QEA; X-ray; 1.74 A; A=1-321.
DR PDB; 5QEB; X-ray; 1.73 A; A=1-321.
DR PDB; 5QEC; X-ray; 1.67 A; A=1-321.
DR PDB; 5QED; X-ray; 1.75 A; A=1-321.
DR PDB; 5QEE; X-ray; 1.93 A; A=1-321.
DR PDB; 5QEF; X-ray; 1.60 A; A=1-321.
DR PDB; 5QEG; X-ray; 1.97 A; A=1-321.
DR PDB; 5QEH; X-ray; 1.94 A; A=1-321.
DR PDB; 5QEI; X-ray; 1.74 A; A=1-321.
DR PDB; 5QEJ; X-ray; 1.92 A; A=1-321.
DR PDB; 5QEK; X-ray; 1.90 A; A=1-321.
DR PDB; 5QEL; X-ray; 1.65 A; A=1-321.
DR PDB; 5QEM; X-ray; 1.75 A; A=1-321.
DR PDB; 5QEN; X-ray; 1.77 A; A=1-321.
DR PDB; 5QEO; X-ray; 1.72 A; A=1-321.
DR PDB; 5QEP; X-ray; 1.77 A; A=1-321.
DR PDB; 5QEQ; X-ray; 1.97 A; A=1-321.
DR PDB; 5QER; X-ray; 1.73 A; A=1-321.
DR PDB; 5QES; X-ray; 1.75 A; A=1-321.
DR PDB; 5QET; X-ray; 1.72 A; A=1-321.
DR PDB; 5QEU; X-ray; 1.74 A; A=1-321.
DR PDB; 5QEV; X-ray; 1.72 A; A=1-321.
DR PDB; 5QEW; X-ray; 1.83 A; A=1-321.
DR PDB; 5QEX; X-ray; 1.67 A; A=1-321.
DR PDB; 5QEY; X-ray; 1.77 A; A=1-321.
DR PDB; 5QEZ; X-ray; 1.65 A; A=1-321.
DR PDB; 5QF0; X-ray; 1.71 A; A=1-321.
DR PDB; 5QF1; X-ray; 1.84 A; A=1-321.
DR PDB; 5QF2; X-ray; 1.77 A; A=1-321.
DR PDB; 5QF3; X-ray; 1.56 A; A=1-321.
DR PDB; 5QF4; X-ray; 1.83 A; A=1-321.
DR PDB; 5QF5; X-ray; 1.73 A; A=1-321.
DR PDB; 5QF6; X-ray; 1.76 A; A=1-321.
DR PDB; 5QF7; X-ray; 1.75 A; A=1-321.
DR PDB; 5QF8; X-ray; 1.99 A; A=1-321.
DR PDB; 5QF9; X-ray; 1.94 A; A=1-321.
DR PDB; 5QFA; X-ray; 1.74 A; A=1-321.
DR PDB; 5QFB; X-ray; 1.85 A; A=1-321.
DR PDB; 5QFC; X-ray; 1.84 A; A=1-321.
DR PDB; 5QFD; X-ray; 1.69 A; A=1-321.
DR PDB; 5QFE; X-ray; 1.56 A; A=1-321.
DR PDB; 5QFF; X-ray; 1.70 A; A=1-321.
DR PDB; 5QFG; X-ray; 1.65 A; A=1-321.
DR PDB; 5QFH; X-ray; 1.59 A; A=1-321.
DR PDB; 5QFI; X-ray; 1.68 A; A=1-321.
DR PDB; 5QFJ; X-ray; 1.95 A; A=1-321.
DR PDB; 5QFK; X-ray; 1.59 A; A=1-321.
DR PDB; 5QFL; X-ray; 1.82 A; A=1-321.
DR PDB; 5QFM; X-ray; 1.83 A; A=1-321.
DR PDB; 5QFN; X-ray; 1.68 A; A=1-321.
DR PDB; 5QFO; X-ray; 1.85 A; A=1-321.
DR PDB; 5QFP; X-ray; 1.77 A; A=1-321.
DR PDB; 5QFQ; X-ray; 1.62 A; A=1-321.
DR PDB; 5QFR; X-ray; 1.62 A; A=1-321.
DR PDB; 5QFS; X-ray; 1.85 A; A=1-321.
DR PDB; 5QFT; X-ray; 1.96 A; A=1-321.
DR PDB; 5QFU; X-ray; 1.61 A; A=1-321.
DR PDB; 5QFV; X-ray; 1.64 A; A=1-321.
DR PDB; 5QFW; X-ray; 1.66 A; A=1-321.
DR PDB; 5QFX; X-ray; 1.82 A; A=1-321.
DR PDB; 5QFY; X-ray; 1.77 A; A=1-321.
DR PDB; 5QFZ; X-ray; 1.72 A; A=1-321.
DR PDB; 5QG0; X-ray; 1.75 A; A=1-321.
DR PDB; 5QG1; X-ray; 2.21 A; A=1-321.
DR PDB; 5QG2; X-ray; 2.12 A; A=1-321.
DR PDB; 5QG3; X-ray; 1.65 A; A=1-321.
DR PDB; 5QG4; X-ray; 1.79 A; A=1-321.
DR PDB; 5QG5; X-ray; 2.07 A; A=1-321.
DR PDB; 5QG6; X-ray; 1.73 A; A=1-321.
DR PDB; 5QG7; X-ray; 1.81 A; A=1-321.
DR PDB; 5QG8; X-ray; 1.63 A; A=1-321.
DR PDB; 5QG9; X-ray; 1.67 A; A=1-321.
DR PDB; 5QGA; X-ray; 1.65 A; A=1-321.
DR PDB; 5QGB; X-ray; 1.55 A; A=1-321.
DR PDB; 5QGC; X-ray; 1.59 A; A=1-321.
DR PDB; 5QGD; X-ray; 1.66 A; A=1-321.
DR PDB; 5QGE; X-ray; 1.70 A; A=1-321.
DR PDB; 5QGF; X-ray; 1.51 A; A=1-321.
DR PDB; 5T19; X-ray; 2.10 A; A=1-321.
DR PDB; 6B8E; X-ray; 1.82 A; A=1-321.
DR PDB; 6B8T; X-ray; 1.85 A; A=1-321.
DR PDB; 6B8X; X-ray; 1.74 A; A=1-321.
DR PDB; 6B8Z; X-ray; 1.80 A; A=1-321.
DR PDB; 6B90; X-ray; 1.95 A; A=1-321.
DR PDB; 6B95; X-ray; 1.95 A; A=1-321.
DR PDB; 6BAI; X-ray; 1.95 A; A=1-321.
DR PDB; 6CWU; X-ray; 2.08 A; A=1-321.
DR PDB; 6CWV; X-ray; 1.98 A; A=1-321.
DR PDB; 6NTP; X-ray; 1.89 A; A=1-298.
DR PDB; 6OL4; X-ray; 2.15 A; A=2-297.
DR PDB; 6OLQ; X-ray; 2.10 A; A=2-298.
DR PDB; 6OLV; X-ray; 2.10 A; A=2-297.
DR PDB; 6OMY; X-ray; 2.10 A; A=2-298.
DR PDB; 6PFW; X-ray; 2.34 A; A=2-298.
DR PDB; 6PG0; X-ray; 2.10 A; A=2-298.
DR PDB; 6PGT; X-ray; 2.20 A; A=2-299.
DR PDB; 6PHA; X-ray; 2.30 A; A=2-298.
DR PDB; 6PHS; X-ray; 2.13 A; A=2-298.
DR PDB; 6PM8; X-ray; 2.06 A; A=2-298.
DR PDB; 6W30; X-ray; 2.10 A; A=1-321.
DR PDB; 6XE8; X-ray; 1.95 A; A=1-321.
DR PDB; 6XEA; X-ray; 1.55 A; A=1-321.
DR PDB; 6XED; X-ray; 1.79 A; A=1-321.
DR PDB; 6XEE; X-ray; 2.50 A; A=1-321.
DR PDB; 6XEF; X-ray; 2.05 A; A=1-321.
DR PDB; 6XEG; X-ray; 2.55 A; A=1-321.
DR PDB; 7KEN; X-ray; 1.80 A; A=2-323.
DR PDB; 7KEY; X-ray; 1.77 A; A=2-283.
DR PDB; 7KLX; X-ray; 1.84 A; A=2-283.
DR PDB; 7L0C; X-ray; 1.80 A; A=1-321.
DR PDB; 7L0H; X-ray; 2.10 A; A=1-321.
DR PDB; 7LFO; X-ray; 1.94 A; A=1-321.
DR PDB; 7MM1; X-ray; 1.85 A; A=1-321.
DR PDB; 7RIN; X-ray; 1.85 A; A=1-321.
DR PDBsum; 1A5Y; -.
DR PDBsum; 1AAX; -.
DR PDBsum; 1BZC; -.
DR PDBsum; 1BZH; -.
DR PDBsum; 1BZJ; -.
DR PDBsum; 1C83; -.
DR PDBsum; 1C84; -.
DR PDBsum; 1C85; -.
DR PDBsum; 1C86; -.
DR PDBsum; 1C87; -.
DR PDBsum; 1C88; -.
DR PDBsum; 1ECV; -.
DR PDBsum; 1EEN; -.
DR PDBsum; 1EEO; -.
DR PDBsum; 1G1F; -.
DR PDBsum; 1G1G; -.
DR PDBsum; 1G1H; -.
DR PDBsum; 1G7F; -.
DR PDBsum; 1G7G; -.
DR PDBsum; 1GFY; -.
DR PDBsum; 1I57; -.
DR PDBsum; 1JF7; -.
DR PDBsum; 1KAK; -.
DR PDBsum; 1KAV; -.
DR PDBsum; 1L8G; -.
DR PDBsum; 1LQF; -.
DR PDBsum; 1NL9; -.
DR PDBsum; 1NNY; -.
DR PDBsum; 1NO6; -.
DR PDBsum; 1NWE; -.
DR PDBsum; 1NWL; -.
DR PDBsum; 1NZ7; -.
DR PDBsum; 1OEM; -.
DR PDBsum; 1OEO; -.
DR PDBsum; 1OES; -.
DR PDBsum; 1OET; -.
DR PDBsum; 1OEU; -.
DR PDBsum; 1OEV; -.
DR PDBsum; 1ONY; -.
DR PDBsum; 1ONZ; -.
DR PDBsum; 1PA1; -.
DR PDBsum; 1PH0; -.
DR PDBsum; 1PTT; -.
DR PDBsum; 1PTU; -.
DR PDBsum; 1PTV; -.
DR PDBsum; 1PTY; -.
DR PDBsum; 1PXH; -.
DR PDBsum; 1PYN; -.
DR PDBsum; 1Q1M; -.
DR PDBsum; 1Q6J; -.
DR PDBsum; 1Q6M; -.
DR PDBsum; 1Q6N; -.
DR PDBsum; 1Q6P; -.
DR PDBsum; 1Q6S; -.
DR PDBsum; 1Q6T; -.
DR PDBsum; 1QXK; -.
DR PDBsum; 1SUG; -.
DR PDBsum; 1T48; -.
DR PDBsum; 1T49; -.
DR PDBsum; 1T4J; -.
DR PDBsum; 1WAX; -.
DR PDBsum; 1XBO; -.
DR PDBsum; 2AZR; -.
DR PDBsum; 2B07; -.
DR PDBsum; 2B4S; -.
DR PDBsum; 2BGD; -.
DR PDBsum; 2BGE; -.
DR PDBsum; 2CM2; -.
DR PDBsum; 2CM3; -.
DR PDBsum; 2CM7; -.
DR PDBsum; 2CM8; -.
DR PDBsum; 2CMA; -.
DR PDBsum; 2CMB; -.
DR PDBsum; 2CMC; -.
DR PDBsum; 2CNE; -.
DR PDBsum; 2CNF; -.
DR PDBsum; 2CNG; -.
DR PDBsum; 2CNH; -.
DR PDBsum; 2CNI; -.
DR PDBsum; 2F6F; -.
DR PDBsum; 2F6T; -.
DR PDBsum; 2F6V; -.
DR PDBsum; 2F6W; -.
DR PDBsum; 2F6Y; -.
DR PDBsum; 2F6Z; -.
DR PDBsum; 2F70; -.
DR PDBsum; 2F71; -.
DR PDBsum; 2FJM; -.
DR PDBsum; 2FJN; -.
DR PDBsum; 2H4G; -.
DR PDBsum; 2H4K; -.
DR PDBsum; 2HB1; -.
DR PDBsum; 2HNP; -.
DR PDBsum; 2HNQ; -.
DR PDBsum; 2NT7; -.
DR PDBsum; 2NTA; -.
DR PDBsum; 2QBP; -.
DR PDBsum; 2QBQ; -.
DR PDBsum; 2QBR; -.
DR PDBsum; 2QBS; -.
DR PDBsum; 2VEU; -.
DR PDBsum; 2VEV; -.
DR PDBsum; 2VEW; -.
DR PDBsum; 2VEX; -.
DR PDBsum; 2VEY; -.
DR PDBsum; 2ZMM; -.
DR PDBsum; 2ZN7; -.
DR PDBsum; 3A5J; -.
DR PDBsum; 3A5K; -.
DR PDBsum; 3CWE; -.
DR PDBsum; 3D9C; -.
DR PDBsum; 3EAX; -.
DR PDBsum; 3EB1; -.
DR PDBsum; 3EU0; -.
DR PDBsum; 3I7Z; -.
DR PDBsum; 3I80; -.
DR PDBsum; 3QKP; -.
DR PDBsum; 3QKQ; -.
DR PDBsum; 3SME; -.
DR PDBsum; 3ZMP; -.
DR PDBsum; 3ZMQ; -.
DR PDBsum; 3ZV2; -.
DR PDBsum; 4BJO; -.
DR PDBsum; 4I8N; -.
DR PDBsum; 4QAH; -.
DR PDBsum; 4QAP; -.
DR PDBsum; 4QBE; -.
DR PDBsum; 4QBW; -.
DR PDBsum; 4Y14; -.
DR PDBsum; 4ZRT; -.
DR PDBsum; 5K9V; -.
DR PDBsum; 5K9W; -.
DR PDBsum; 5KA0; -.
DR PDBsum; 5KA1; -.
DR PDBsum; 5KA2; -.
DR PDBsum; 5KA3; -.
DR PDBsum; 5KA4; -.
DR PDBsum; 5KA7; -.
DR PDBsum; 5KA8; -.
DR PDBsum; 5KA9; -.
DR PDBsum; 5KAA; -.
DR PDBsum; 5KAB; -.
DR PDBsum; 5KAC; -.
DR PDBsum; 5KAD; -.
DR PDBsum; 5QDE; -.
DR PDBsum; 5QDF; -.
DR PDBsum; 5QDG; -.
DR PDBsum; 5QDH; -.
DR PDBsum; 5QDI; -.
DR PDBsum; 5QDJ; -.
DR PDBsum; 5QDK; -.
DR PDBsum; 5QDL; -.
DR PDBsum; 5QDM; -.
DR PDBsum; 5QDN; -.
DR PDBsum; 5QDO; -.
DR PDBsum; 5QDP; -.
DR PDBsum; 5QDQ; -.
DR PDBsum; 5QDR; -.
DR PDBsum; 5QDS; -.
DR PDBsum; 5QDT; -.
DR PDBsum; 5QDU; -.
DR PDBsum; 5QDV; -.
DR PDBsum; 5QDW; -.
DR PDBsum; 5QDX; -.
DR PDBsum; 5QDY; -.
DR PDBsum; 5QDZ; -.
DR PDBsum; 5QE0; -.
DR PDBsum; 5QE1; -.
DR PDBsum; 5QE2; -.
DR PDBsum; 5QE3; -.
DR PDBsum; 5QE4; -.
DR PDBsum; 5QE5; -.
DR PDBsum; 5QE6; -.
DR PDBsum; 5QE7; -.
DR PDBsum; 5QE8; -.
DR PDBsum; 5QE9; -.
DR PDBsum; 5QEA; -.
DR PDBsum; 5QEB; -.
DR PDBsum; 5QEC; -.
DR PDBsum; 5QED; -.
DR PDBsum; 5QEE; -.
DR PDBsum; 5QEF; -.
DR PDBsum; 5QEG; -.
DR PDBsum; 5QEH; -.
DR PDBsum; 5QEI; -.
DR PDBsum; 5QEJ; -.
DR PDBsum; 5QEK; -.
DR PDBsum; 5QEL; -.
DR PDBsum; 5QEM; -.
DR PDBsum; 5QEN; -.
DR PDBsum; 5QEO; -.
DR PDBsum; 5QEP; -.
DR PDBsum; 5QEQ; -.
DR PDBsum; 5QER; -.
DR PDBsum; 5QES; -.
DR PDBsum; 5QET; -.
DR PDBsum; 5QEU; -.
DR PDBsum; 5QEV; -.
DR PDBsum; 5QEW; -.
DR PDBsum; 5QEX; -.
DR PDBsum; 5QEY; -.
DR PDBsum; 5QEZ; -.
DR PDBsum; 5QF0; -.
DR PDBsum; 5QF1; -.
DR PDBsum; 5QF2; -.
DR PDBsum; 5QF3; -.
DR PDBsum; 5QF4; -.
DR PDBsum; 5QF5; -.
DR PDBsum; 5QF6; -.
DR PDBsum; 5QF7; -.
DR PDBsum; 5QF8; -.
DR PDBsum; 5QF9; -.
DR PDBsum; 5QFA; -.
DR PDBsum; 5QFB; -.
DR PDBsum; 5QFC; -.
DR PDBsum; 5QFD; -.
DR PDBsum; 5QFE; -.
DR PDBsum; 5QFF; -.
DR PDBsum; 5QFG; -.
DR PDBsum; 5QFH; -.
DR PDBsum; 5QFI; -.
DR PDBsum; 5QFJ; -.
DR PDBsum; 5QFK; -.
DR PDBsum; 5QFL; -.
DR PDBsum; 5QFM; -.
DR PDBsum; 5QFN; -.
DR PDBsum; 5QFO; -.
DR PDBsum; 5QFP; -.
DR PDBsum; 5QFQ; -.
DR PDBsum; 5QFR; -.
DR PDBsum; 5QFS; -.
DR PDBsum; 5QFT; -.
DR PDBsum; 5QFU; -.
DR PDBsum; 5QFV; -.
DR PDBsum; 5QFW; -.
DR PDBsum; 5QFX; -.
DR PDBsum; 5QFY; -.
DR PDBsum; 5QFZ; -.
DR PDBsum; 5QG0; -.
DR PDBsum; 5QG1; -.
DR PDBsum; 5QG2; -.
DR PDBsum; 5QG3; -.
DR PDBsum; 5QG4; -.
DR PDBsum; 5QG5; -.
DR PDBsum; 5QG6; -.
DR PDBsum; 5QG7; -.
DR PDBsum; 5QG8; -.
DR PDBsum; 5QG9; -.
DR PDBsum; 5QGA; -.
DR PDBsum; 5QGB; -.
DR PDBsum; 5QGC; -.
DR PDBsum; 5QGD; -.
DR PDBsum; 5QGE; -.
DR PDBsum; 5QGF; -.
DR PDBsum; 5T19; -.
DR PDBsum; 6B8E; -.
DR PDBsum; 6B8T; -.
DR PDBsum; 6B8X; -.
DR PDBsum; 6B8Z; -.
DR PDBsum; 6B90; -.
DR PDBsum; 6B95; -.
DR PDBsum; 6BAI; -.
DR PDBsum; 6CWU; -.
DR PDBsum; 6CWV; -.
DR PDBsum; 6NTP; -.
DR PDBsum; 6OL4; -.
DR PDBsum; 6OLQ; -.
DR PDBsum; 6OLV; -.
DR PDBsum; 6OMY; -.
DR PDBsum; 6PFW; -.
DR PDBsum; 6PG0; -.
DR PDBsum; 6PGT; -.
DR PDBsum; 6PHA; -.
DR PDBsum; 6PHS; -.
DR PDBsum; 6PM8; -.
DR PDBsum; 6W30; -.
DR PDBsum; 6XE8; -.
DR PDBsum; 6XEA; -.
DR PDBsum; 6XED; -.
DR PDBsum; 6XEE; -.
DR PDBsum; 6XEF; -.
DR PDBsum; 6XEG; -.
DR PDBsum; 7KEN; -.
DR PDBsum; 7KEY; -.
DR PDBsum; 7KLX; -.
DR PDBsum; 7L0C; -.
DR PDBsum; 7L0H; -.
DR PDBsum; 7LFO; -.
DR PDBsum; 7MM1; -.
DR PDBsum; 7RIN; -.
DR AlphaFoldDB; P18031; -.
DR BMRB; P18031; -.
DR SMR; P18031; -.
DR BioGRID; 111736; 578.
DR DIP; DIP-38014N; -.
DR IntAct; P18031; 224.
DR MINT; P18031; -.
DR STRING; 9606.ENSP00000360683; -.
DR BindingDB; P18031; -.
DR ChEMBL; CHEMBL335; -.
DR DrugBank; DB08549; (3R)-METHYLCARBAMOYL-7-SULFOAMINO-3,4-DIHYDRO-1H-ISOQUINOLINE-2-CARBOXYLIC ACID BENZYL ESTER.
DR DrugBank; DB08783; (4-{(2S)-2-[(tert-butoxycarbonyl)amino]-3-methoxy-3-oxopropyl}phenyl)methaneseleninic acid.
DR DrugBank; DB03483; (4S)-5-[[(2S)-1-[[(2S)-1-Amino-3-[4-[difluoro(phosphono)methyl]phenyl]-1-oxopropan-2-yl]amino]-3-[4-[difluoro(phosphono)methyl]phenyl]-1-oxopropan-2-yl]amino]-4-benzamido-5-oxopentanoic acid.
DR DrugBank; DB08593; 1,2,5-THIADIAZOLIDIN-3-ONE-1,1-DIOXIDE.
DR DrugBank; DB04800; 1-METHYL-3-PHENYL-1H-PYRAZOL-5-YLSULFAMIC ACID.
DR DrugBank; DB03670; 2-(Oxalyl-Amino)-4,5,6,7-Tetrahydro-Thieno[2,3-C]Pyridine-3-Carboxylic Acid.
DR DrugBank; DB03102; 2-(Oxalyl-Amino)-4,7-Dihydro-5h-Thieno[2,3-C]Pyran-3-Carboxylic Acid.
DR DrugBank; DB02072; 2-(Oxalyl-Amino)-4,7-Dihydro-5h-Thieno[2,3-C]Thiopyran-3-Carboxylic Acid.
DR DrugBank; DB02622; 2-(Oxalyl-Amino)-Benzoic Acid.
DR DrugBank; DB07295; 2-[(7-HYDROXY-NAPHTHALEN-1-YL)-OXALYL-AMINO]-BENZOIC ACID.
DR DrugBank; DB04088; 2-[{4-[(2S)-2-{[(Allyloxy)carbonyl]amino}-3-({4-[3-hydroxy-2-(methoxycarbonyl)phenoxy]butyl}amino)-3-oxopropyl]phenyl}(carboxycarbonyl)amino]benzoic acid.
DR DrugBank; DB01820; 2-{[4-(2-Acetylamino-2-pentylcarbamoyl-ethyl)-naphthalen-1-YL]-oxalyl-amino}-benzoic acid.
DR DrugBank; DB02259; 3-(3,5-Dibromo-4-Hydroxy-Benzoyl)-2-Ethyl-Benzofuran-6-Sulfonic Acid (4-Sulfamoyl-Phenyl)-Amide.
DR DrugBank; DB03311; 3-(3,5-Dibromo-4-Hydroxy-Benzoyl)-2-Ethyl-Benzofuran-6-Sulfonic Acid [4-(Thiazol-2-Ylsulfamoyl)-Phenyl]-Amide.
DR DrugBank; DB04142; 3-(3,5-Dibromo-4-Hydroxy-Benzoyl)-2-Ethyl-Benzofuran-6-Sulfonic Acid Dimethylamide.
DR DrugBank; DB02620; 3-(4-{2-[2-(2-bromo-acetylamino)-ethyldisulfanyl]-ethylcarbamoyl}-cyclohexylcarbamoyl)-pyrazine-2-carboxylic acid.
DR DrugBank; DB07298; 3-(CARBOXYMETHOXY)THIENO[2,3-B]PYRIDINE-2-CARBOXYLIC ACID.
DR DrugBank; DB01734; 3-(Oxalyl-Amino)-Naphthalene-2-Carboxylic Acid.
DR DrugBank; DB08147; 4-[3-(dibenzylamino)phenyl]-2,4-dioxobutanoic acid.
DR DrugBank; DB03557; 4-[[(2S)-1-[[6-[(1-Amino-1-oxo-3-sulfanylpropan-2-yl)amino]-6-oxohexyl]amino]-3-[4-[difluoro(phosphono)methyl]phenyl]-1-oxopropan-2-yl]amino]-3-[[2-[4-[difluoro(phosphono)methyl]phenyl]acetyl]amino]-4-oxobutanoic acid.
DR DrugBank; DB07197; 4-BROMO-3-(CARBOXYMETHOXY)-5-(4-HYDROXYPHENYL)THIOPHENE-2-CARBOXYLIC ACID.
DR DrugBank; DB06829; 4-BROMO-3-(CARBOXYMETHOXY)-5-[3-(CYCLOHEXYLAMINO)PHENYL]THIOPHENE-2-CARBOXYLIC ACID.
DR DrugBank; DB07130; 4-BROMO-3-(CARBOXYMETHOXY)-5-PHENYLTHIOPHENE-2-CARBOXYLIC ACID.
DR DrugBank; DB03714; 4-Carbamoyl-4-{[6-(Difluoro-Phosphono-Methyl)-Naphthalene-2-Carbonyl]-Amino}-Butyric Acid.
DR DrugBank; DB07480; 4-PHOSPHONOOXY-PHENYL-METHYL-[4-PHOSPHONOOXY]BENZEN.
DR DrugBank; DB02014; 5-(2-Fluoro-5-{(1E)-3-[3-hydroxy-2-(methoxycarbonyl)phenoxy]-1-propen-1-yl}phenyl)-1,2-oxazole-3-carboxylic acid.
DR DrugBank; DB07730; 5-(3-HYDROXYPHENYL)ISOTHIAZOL-3(2H)-ONE 1,1-DIOXIDE.
DR DrugBank; DB08001; 5-(3-{3-[3-HYDROXY-2-(METHOXYCARBONYL)PHENOXY]PROPENYL}PHENYL)-4-(HYDROXYMETHYL)ISOXAZOLE-3-CARBOXYLIC ACID.
DR DrugBank; DB07134; 5-(4-CHLORO-5-PHENYL-3-THIENYL)-1,2,5-THIADIAZOLIDIN-3-ONE 1,1-DIOXIDE.
DR DrugBank; DB08591; 5-(4-METHOXYBIPHENYL-3-YL)-1,2,5-THIADIAZOLIDIN-3-ONE 1,1-DIOXIDE.
DR DrugBank; DB07289; 5-[3-(BENZYLAMINO)PHENYL]-4-BROMO-3-(CARBOXYMETHOXY)THIOPHENE-2-CARBOXYLIC ACID.
DR DrugBank; DB08397; 6-(DIFLUORO-PHOSPHONO-METHYL)-NAPHTHALENE-2-CARBOXYLIC ACID.
DR DrugBank; DB04001; 6-(Oxalyl-Amino)-1h-Indole-5-Carboxylic Acid.
DR DrugBank; DB02827; 7-(1,1-Dioxo-1h-Benzo[D]Isothiazol-3-Yloxymethyl)-2-(Oxalyl-Amino)-4,7-Dihydro-5h-Thieno[2,3-C]Pyran-3-Carboxylic Acid.
DR DrugBank; DB07719; [(3R)-3-(Methylcarbamoyl)-2-{[(2-methyl-2-propanyl)oxy]carbonyl}-1,2,3,4-tetrahydro-7-isoquinolinyl]sulfamic acid.
DR DrugBank; DB06887; [(3S)-3-(Methylcarbamoyl)-2-{[(2-methyl-2-propanyl)oxy]carbonyl}-1,2,3,4-tetrahydro-7-isoquinolinyl]sulfamic acid.
DR DrugBank; DB04204; [(4-{4-[4-(Difluoro-Phosphono-Methyl)-Phenyl]-Butyl}-Phenyl)-Difluoro-Methyl]-Phosphonic Acid.
DR DrugBank; DB02420; [[4-(Aminomethyl)Phenyl]Amino]Oxo-Acetic Acid.
DR DrugBank; DB07263; [{2-bromo-4-[(2R)-3-oxo-2,3-diphenylpropyl]phenyl}(difluoro)methyl]phosphonic acid.
DR DrugBank; DB02615; Compound 19.
DR DrugBank; DB03982; Compound 5, 2-(Naphthalen-1-Yl-Oxalyl-Amino)-Benzoicacid.
DR DrugBank; DB06521; Ertiprotafib.
DR DrugBank; DB05506; ISIS 113715.
DR DrugBank; DB08003; ISOTHIAZOLIDINONE ANALOG.
DR DrugBank; DB03661; L-cysteic acid.
DR DrugBank; DB04525; N-(3-Carboxypropanoyl)-L-phenylalanyl-3-carboxy-O-(carboxymethyl)-N-pentyl-L-tyrosinamide.
DR DrugBank; DB02784; N-(Bromoacetyl)-beta-alanyl-N-(2-{4-[(carboxycarbonyl)amino]phenyl}ethyl)-L-serinamide.
DR DrugBank; DB07651; N-ACETYL-L-PHENYLALANYL-4-[DIFLUORO(PHOSPHONO)METHYL]-L-PHENYLALANINAMIDE.
DR DrugBank; DB02662; Novo Nordisk a/S Compound.
DR DrugBank; DB08371; p-Benzoyl-L-phenylalanine.
DR DrugBank; DB02977; PNU177836.
DR DrugBank; DB06333; Trodusquemine.
DR DrugBank; DB02436; {4-[(2S)-2-({[(1S)-1-Carboxy-2-phenylethyl]carbamoyl}amino)-3-oxo-3-(pentylamino)propyl]phenoxy}malonic acid.
DR DrugBank; DB04285; {4-[(2s,4e)-2-(1,3-Benzothiazol-2-Yl)-2-(1h-1,2,3-Benzotriazol-1-Yl)-5-Phenylpent-4-Enyl]Phenyl}(Difluoro)Methylphosphonic Acid.
DR DrugBank; DB02651; {[2-(1h-1,2,3-Benzotriazol-1-Yl)-2-(3,4-Difluorophenyl)Propane-1,3-Diyl]Bis[4,1-Phenylene(Difluoromethylene)]}Bis(Phosphonic Acid).
DR DrugBank; DB03154; {[7-(Difluoro-Phosphono-Methyl)-Naphthalen-2-Yl]-Difluoro-Methyl}-Phosphonic Acid.
DR DrugCentral; P18031; -.
DR GuidetoPHARMACOLOGY; 2976; -.
DR DEPOD; PTPN1; -.
DR GlyGen; P18031; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P18031; -.
DR MetOSite; P18031; -.
DR PhosphoSitePlus; P18031; -.
DR SwissPalm; P18031; -.
DR BioMuta; PTPN1; -.
DR DMDM; 131467; -.
DR OGP; P18031; -.
DR CPTAC; CPTAC-578; -.
DR CPTAC; CPTAC-579; -.
DR EPD; P18031; -.
DR jPOST; P18031; -.
DR MassIVE; P18031; -.
DR MaxQB; P18031; -.
DR PaxDb; P18031; -.
DR PeptideAtlas; P18031; -.
DR PRIDE; P18031; -.
DR ProteomicsDB; 53539; -.
DR ABCD; P18031; 21 sequenced antibodies.
DR Antibodypedia; 2724; 788 antibodies from 43 providers.
DR DNASU; 5770; -.
DR Ensembl; ENST00000371621.5; ENSP00000360683.3; ENSG00000196396.10.
DR GeneID; 5770; -.
DR KEGG; hsa:5770; -.
DR MANE-Select; ENST00000371621.5; ENSP00000360683.3; NM_002827.4; NP_002818.1.
DR UCSC; uc002xvl.5; human.
DR CTD; 5770; -.
DR DisGeNET; 5770; -.
DR GeneCards; PTPN1; -.
DR HGNC; HGNC:9642; PTPN1.
DR HPA; ENSG00000196396; Low tissue specificity.
DR MalaCards; PTPN1; -.
DR MIM; 176885; gene.
DR neXtProt; NX_P18031; -.
DR OpenTargets; ENSG00000196396; -.
DR PharmGKB; PA33985; -.
DR VEuPathDB; HostDB:ENSG00000196396; -.
DR eggNOG; KOG0789; Eukaryota.
DR GeneTree; ENSGT00940000158041; -.
DR HOGENOM; CLU_001645_9_0_1; -.
DR InParanoid; P18031; -.
DR OMA; WSPLLAN; -.
DR OrthoDB; 411281at2759; -.
DR PhylomeDB; P18031; -.
DR TreeFam; TF315897; -.
DR BRENDA; 3.1.3.48; 2681.
DR PathwayCommons; P18031; -.
DR Reactome; R-HSA-354192; Integrin signaling.
DR Reactome; R-HSA-6807004; Negative regulation of MET activity.
DR Reactome; R-HSA-877312; Regulation of IFNG signaling.
DR Reactome; R-HSA-8849472; PTK6 Down-Regulation.
DR Reactome; R-HSA-9022699; MECP2 regulates neuronal receptors and channels.
DR Reactome; R-HSA-912694; Regulation of IFNA/IFNB signaling.
DR Reactome; R-HSA-982772; Growth hormone receptor signaling.
DR SABIO-RK; P18031; -.
DR SignaLink; P18031; -.
DR SIGNOR; P18031; -.
DR BioGRID-ORCS; 5770; 92 hits in 1095 CRISPR screens.
DR ChiTaRS; PTPN1; human.
DR EvolutionaryTrace; P18031; -.
DR GeneWiki; PTPN1; -.
DR GenomeRNAi; 5770; -.
DR Pharos; P18031; Tchem.
DR PRO; PR:P18031; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; P18031; protein.
DR Bgee; ENSG00000196396; Expressed in upper lobe of left lung and 148 other tissues.
DR ExpressionAtlas; P18031; baseline and differential.
DR Genevisible; P18031; HS.
DR GO; GO:0005737; C:cytoplasm; ISS:ARUK-UCL.
DR GO; GO:0098554; C:cytoplasmic side of endoplasmic reticulum membrane; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005769; C:early endosome; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
DR GO; GO:0030061; C:mitochondrial crista; IEA:Ensembl.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:Ensembl.
DR GO; GO:0032991; C:protein-containing complex; IDA:MGI.
DR GO; GO:0097443; C:sorting endosome; ISS:BHF-UCL.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0046875; F:ephrin receptor binding; IPI:UniProtKB.
DR GO; GO:0005158; F:insulin receptor binding; IEA:Ensembl.
DR GO; GO:0004726; F:non-membrane spanning protein tyrosine phosphatase activity; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0051721; F:protein phosphatase 2A binding; IEA:Ensembl.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:UniProtKB.
DR GO; GO:0030971; F:receptor tyrosine kinase binding; IPI:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; IMP:UniProtKB.
DR GO; GO:0034620; P:cellular response to unfolded protein; TAS:ParkinsonsUK-UCL.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IDA:UniProtKB.
DR GO; GO:0060397; P:growth hormone receptor signaling pathway via JAK-STAT; TAS:Reactome.
DR GO; GO:0008286; P:insulin receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0036498; P:IRE1-mediated unfolded protein response; ISS:ARUK-UCL.
DR GO; GO:1902236; P:negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway; ISS:ARUK-UCL.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; ISS:BHF-UCL.
DR GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; NAS:BHF-UCL.
DR GO; GO:0043407; P:negative regulation of MAP kinase activity; IMP:CACAO.
DR GO; GO:1903898; P:negative regulation of PERK-mediated unfolded protein response; IDA:ParkinsonsUK-UCL.
DR GO; GO:0009968; P:negative regulation of signal transduction; TAS:Reactome.
DR GO; GO:0030948; P:negative regulation of vascular endothelial growth factor receptor signaling pathway; ISS:BHF-UCL.
DR GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; IDA:UniProtKB.
DR GO; GO:1990264; P:peptidyl-tyrosine dephosphorylation involved in inactivation of protein kinase activity; ISS:BHF-UCL.
DR GO; GO:0035791; P:platelet-derived growth factor receptor-beta signaling pathway; IMP:UniProtKB.
DR GO; GO:1903896; P:positive regulation of IRE1-mediated unfolded protein response; TAS:ParkinsonsUK-UCL.
DR GO; GO:0043507; P:positive regulation of JUN kinase activity; ISS:ARUK-UCL.
DR GO; GO:0061098; P:positive regulation of protein tyrosine kinase activity; IDA:ParkinsonsUK-UCL.
DR GO; GO:2000646; P:positive regulation of receptor catabolic process; IMP:CACAO.
DR GO; GO:0006470; P:protein dephosphorylation; IMP:CACAO.
DR GO; GO:0030100; P:regulation of endocytosis; IDA:UniProtKB.
DR GO; GO:1902202; P:regulation of hepatocyte growth factor receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0033157; P:regulation of intracellular protein transport; IMP:CACAO.
DR GO; GO:0009966; P:regulation of signal transduction; IMP:UniProtKB.
DR GO; GO:0060338; P:regulation of type I interferon-mediated signaling pathway; TAS:Reactome.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000242; PTP_cat.
DR InterPro; IPR012265; Ptpn1/Ptpn2.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR Pfam; PF00102; Y_phosphatase; 1.
DR PIRSF; PIRSF000926; Tyr-Ptase_nr1; 1.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM00194; PTPc; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing;
KW Endoplasmic reticulum; Hydrolase; Membrane; Oxidation; Phosphoprotein;
KW Protein phosphatase; Reference proteome; S-nitrosylation.
FT CHAIN 1..435
FT /note="Tyrosine-protein phosphatase non-receptor type 1"
FT /id="PRO_0000094748"
FT DOMAIN 3..277
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 338..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 378..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 215
FT /note="Phosphocysteine intermediate"
FT BINDING 181
FT /ligand="substrate"
FT BINDING 215..221
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 262
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|PubMed:2546149"
FT MOD_RES 20
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455"
FT MOD_RES 50
FT /note="Phosphoserine; by PKB/AKT1, CLK1 and CLK2"
FT /evidence="ECO:0000269|PubMed:10480872,
FT ECO:0000269|PubMed:11579209, ECO:0007744|PubMed:23186163"
FT MOD_RES 66
FT /note="Phosphotyrosine; by EGFR"
FT /evidence="ECO:0000269|PubMed:9355745"
FT MOD_RES 215
FT /note="Cysteine persulfide; alternate"
FT /evidence="ECO:0000269|PubMed:22169477"
FT MOD_RES 215
FT /note="Cysteine sulfenic acid (-SOH); alternate"
FT /evidence="ECO:0000269|PubMed:12802338,
FT ECO:0000269|PubMed:12802339"
FT MOD_RES 215
FT /note="Cysteine sulfinic acid (-SO2H); alternate"
FT /evidence="ECO:0000269|PubMed:12802339"
FT MOD_RES 215
FT /note="S-nitrosocysteine; in reversibly inhibited form"
FT /evidence="ECO:0000269|PubMed:22169477"
FT MOD_RES 242
FT /note="Phosphoserine; by CLK1 and CLK2"
FT /evidence="ECO:0000269|PubMed:10480872"
FT MOD_RES 243
FT /note="Phosphoserine; by CLK1 and CLK2"
FT /evidence="ECO:0000269|PubMed:10480872"
FT MOD_RES 352
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8491187,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 363
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 365
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 368
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 378
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000269|PubMed:8491187,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 386
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000269|PubMed:8491187,
FT ECO:0007744|PubMed:23186163"
FT CROSSLNK 215..216
FT /note="N,N-(cysteine-1,S-diyl)serine (Cys-Ser); in
FT inhibited form"
FT /evidence="ECO:0000269|PubMed:12802338,
FT ECO:0000269|PubMed:12802339"
FT VARIANT 381
FT /note="G -> S (in dbSNP:rs16995304)"
FT /id="VAR_022013"
FT VARIANT 387
FT /note="P -> L (associated with low glucose tolerance;
FT dbSNP:rs16995309)"
FT /id="VAR_022014"
FT MUTAGEN 50
FT /note="S->A,D: No phosphorylation."
FT /evidence="ECO:0000269|PubMed:10480872,
FT ECO:0000269|PubMed:11579209"
FT MUTAGEN 181
FT /note="D->A: Substrate-trapping mutant."
FT /evidence="ECO:0000269|PubMed:22169477"
FT MUTAGEN 215
FT /note="C->S: Catalytically inactive mutant; abolishes
FT sulfhydration."
FT /evidence="ECO:0000269|PubMed:22169477"
FT HELIX 3..13
FT /evidence="ECO:0007829|PDB:2CM2"
FT HELIX 16..26
FT /evidence="ECO:0007829|PDB:2CM2"
FT TURN 33..36
FT /evidence="ECO:0007829|PDB:2CM2"
FT HELIX 38..43
FT /evidence="ECO:0007829|PDB:2CM2"
FT STRAND 45..48
FT /evidence="ECO:0007829|PDB:2FJM"
FT TURN 53..55
FT /evidence="ECO:0007829|PDB:2CM2"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:2CM2"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:2F71"
FT STRAND 66..74
FT /evidence="ECO:0007829|PDB:2CM2"
FT TURN 75..78
FT /evidence="ECO:0007829|PDB:2CM2"
FT STRAND 79..84
FT /evidence="ECO:0007829|PDB:2CM2"
FT TURN 89..91
FT /evidence="ECO:0007829|PDB:5QGF"
FT HELIX 92..102
FT /evidence="ECO:0007829|PDB:2CM2"
FT STRAND 106..109
FT /evidence="ECO:0007829|PDB:2CM2"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:2CM2"
FT STRAND 118..121
FT /evidence="ECO:0007829|PDB:2CMB"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:2CNE"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:2CM2"
FT TURN 136..139
FT /evidence="ECO:0007829|PDB:2CM2"
FT STRAND 140..149
FT /evidence="ECO:0007829|PDB:2CM2"
FT STRAND 151..162
FT /evidence="ECO:0007829|PDB:2CM2"
FT TURN 163..165
FT /evidence="ECO:0007829|PDB:2CM2"
FT STRAND 168..176
FT /evidence="ECO:0007829|PDB:2CM2"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:2CM2"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:2CM2"
FT HELIX 189..200
FT /evidence="ECO:0007829|PDB:2CM2"
FT TURN 201..204
FT /evidence="ECO:0007829|PDB:2CM2"
FT STRAND 211..220
FT /evidence="ECO:0007829|PDB:2CM2"
FT HELIX 221..237
FT /evidence="ECO:0007829|PDB:2CM2"
FT STRAND 238..240
FT /evidence="ECO:0007829|PDB:3A5J"
FT HELIX 241..243
FT /evidence="ECO:0007829|PDB:2CM2"
FT HELIX 246..253
FT /evidence="ECO:0007829|PDB:2CM2"
FT TURN 254..256
FT /evidence="ECO:0007829|PDB:2CM2"
FT HELIX 264..281
FT /evidence="ECO:0007829|PDB:2CM2"
FT TURN 282..284
FT /evidence="ECO:0007829|PDB:2FJM"
FT HELIX 287..295
FT /evidence="ECO:0007829|PDB:6XEA"
FT TURN 296..298
FT /evidence="ECO:0007829|PDB:6XEA"
SQ SEQUENCE 435 AA; 49967 MW; 802377DCD33F41FD CRC64;
MEMEKEFEQI DKSGSWAAIY QDIRHEASDF PCRVAKLPKN KNRNRYRDVS PFDHSRIKLH
QEDNDYINAS LIKMEEAQRS YILTQGPLPN TCGHFWEMVW EQKSRGVVML NRVMEKGSLK
CAQYWPQKEE KEMIFEDTNL KLTLISEDIK SYYTVRQLEL ENLTTQETRE ILHFHYTTWP
DFGVPESPAS FLNFLFKVRE SGSLSPEHGP VVVHCSAGIG RSGTFCLADT CLLLMDKRKD
PSSVDIKKVL LEMRKFRMGL IQTADQLRFS YLAVIEGAKF IMGDSSVQDQ WKELSHEDLE
PPPEHIPPPP RPPKRILEPH NGKCREFFPN HQWVKEETQE DKDCPIKEEK GSPLNAAPYG
IESMSQDTEV RSRVVGGSLR GAQAASPAKG EPSLPEKDED HALSYWKPFL VNMCVATVLT
AGAYLCYRFL FNSNT
