PTN7_HUMAN
ID PTN7_HUMAN Reviewed; 360 AA.
AC P35236; B3KXE1; Q53XK4; Q5SXQ0; Q5SXQ1; Q9BV05;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 3.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Tyrosine-protein phosphatase non-receptor type 7;
DE EC=3.1.3.48;
DE AltName: Full=Hematopoietic protein-tyrosine phosphatase;
DE Short=HEPTP;
DE AltName: Full=Protein-tyrosine phosphatase LC-PTP;
GN Name=PTPN7;
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] (ISOFORM 1), TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=1510684; DOI=10.1016/s0006-291x(05)81592-x;
RA Adachi M., Sekiya M., Isobe M., Kumura Y., Ogita Z.I., Hinoda Y., Imai K.,
RA Yachi A.;
RT "Molecular cloning and chromosomal mapping of a human protein-tyrosine
RT phosphatase LC-PTP.";
RL Biochem. Biophys. Res. Commun. 186:1607-1615(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Lymphocyte;
RX PubMed=1530918; DOI=10.1002/eji.1830220134;
RA Zanke B., Suzuki H., Kishihara K., Mizzen L., Minden M., Pawson A.,
RA Mak T.W.;
RT "Cloning and expression of an inducible lymphoid-specific, protein tyrosine
RT phosphatase (HePTPase).";
RL Eur. J. Immunol. 22:235-239(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Hippocampus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=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 [7]
RP FUNCTION, INTERACTION WITH MAPK1, ACTIVE SITE, AND MUTAGENESIS OF CYS-291.
RX PubMed=9624114; DOI=10.1074/jbc.273.25.15340;
RA Saxena M., Williams S., Gilman J., Mustelin T.;
RT "Negative regulation of T cell antigen receptor signal transduction by
RT hematopoietic tyrosine phosphatase (HePTP).";
RL J. Biol. Chem. 273:15340-15344(1998).
RN [8]
RP FUNCTION, INTERACTION WITH MAPK1 AND MAPK3, PHOSPHORYLATION AT THR-66 AND
RP SER-93, AND MUTAGENESIS OF THR-66 AND SER-93.
RX PubMed=10206983; DOI=10.1074/jbc.274.17.11693;
RA Saxena M., Williams S., Brockdorff J., Gilman J., Mustelin T.;
RT "Inhibition of T cell signaling by mitogen-activated protein kinase-
RT targeted hematopoietic tyrosine phosphatase (HePTP).";
RL J. Biol. Chem. 274:11693-11700(1999).
RN [9]
RP FUNCTION, INTERACTION WITH MAPK1, AND PHOSPHORYLATION AT SER-44.
RX PubMed=10559944; DOI=10.1038/13024;
RA Saxena M., Williams S., Tasken K., Mustelin T.;
RT "Crosstalk between cAMP-dependent kinase and MAP kinase through a protein
RT tyrosine phosphatase.";
RL Nat. Cell Biol. 1:305-311(1999).
RN [10]
RP FUNCTION, AND INTERACTION WITH MAPK1 AND MAPK3.
RX PubMed=10702794; DOI=10.1038/sj.onc.1203408;
RA Pettiford S.M., Herbst R.;
RT "The MAP-kinase ERK2 is a specific substrate of the protein tyrosine
RT phosphatase HePTP.";
RL Oncogene 19:858-869(2000).
RN [11]
RP SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-44, AND MUTAGENESIS OF SER-44.
RX PubMed=14613483; DOI=10.1042/bj20031244;
RA Nika K., Hyunh H., Williams S., Paul S., Bottini N., Tasken K.,
RA Lombroso P.J., Mustelin T.;
RT "Haematopoietic protein tyrosine phosphatase (HePTP) phosphorylation by
RT cAMP-dependent protein kinase in T-cells: dynamics and subcellular
RT location.";
RL Biochem. J. 378:335-342(2004).
RN [12]
RP MUTAGENESIS OF TYR-125; ASP-257 AND GLN-335.
RX PubMed=15466470; DOI=10.1074/jbc.m407820200;
RA Huang Z., Zhou B., Zhang Z.-Y.;
RT "Molecular determinants of substrate recognition in hematopoietic protein-
RT tyrosine phosphatase.";
RL J. Biol. Chem. 279:52150-52159(2004).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-66, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44 AND SER-143, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44; THR-66; SER-110 AND
RP SER-143, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [16]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 65-360 OF MUTANT ASP-246 IN
RP COMPLEX WITH SUBSTRATE ANALOG.
RX PubMed=16226275; DOI=10.1016/j.jmb.2005.09.049;
RA Mustelin T., Tautz L., Page R.;
RT "Structure of the hematopoietic tyrosine phosphatase (HePTP) catalytic
RT domain: structure of a KIM phosphatase with phosphate bound at the active
RT site.";
RL J. Mol. Biol. 354:150-163(2005).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 65-358 IN COMPLEX WITH SUBSTRATE
RP ANALOG, AND SUBUNIT.
RX PubMed=16441242; DOI=10.1042/bj20051931;
RA Eswaran J., von Kries J.P., Marsden B., Longman E., Debreczeni J.E.,
RA Ugochukwu E., Turnbull A., Lee W.H., Knapp S., Barr A.J.;
RT "Crystal structures and inhibitor identification for PTPN5, PTPRR and
RT PTPN7: a family of human MAPK-specific protein tyrosine phosphatases.";
RL Biochem. J. 395:483-491(2006).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 37-52 IN COMPLEX WITH MAPK1.
RX PubMed=16765894; DOI=10.1016/j.str.2006.04.006;
RA Zhou T., Sun L., Humphreys J., Goldsmith E.J.;
RT "Docking interactions induce exposure of activation loop in the MAP kinase
RT ERK2.";
RL Structure 14:1011-1019(2006).
CC -!- FUNCTION: Protein phosphatase that acts preferentially on tyrosine-
CC phosphorylated MAPK1. Plays a role in the regulation of T and B-
CC lymphocyte development and signal transduction.
CC {ECO:0000269|PubMed:10206983, ECO:0000269|PubMed:10559944,
CC ECO:0000269|PubMed:10702794, ECO:0000269|PubMed:1510684,
CC ECO:0000269|PubMed:1530918, ECO:0000269|PubMed:9624114}.
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 -!- ACTIVITY REGULATION: Inhibited in cells after FCER1A triggering.
CC {ECO:0000250}.
CC -!- SUBUNIT: Monomer. Interacts with MAPK1, MAPK3 and several other MAP
CC kinases. {ECO:0000269|PubMed:10206983, ECO:0000269|PubMed:10559944,
CC ECO:0000269|PubMed:10702794, ECO:0000269|PubMed:16226275,
CC ECO:0000269|PubMed:16441242, ECO:0000269|PubMed:16765894,
CC ECO:0000269|PubMed:9624114}.
CC -!- INTERACTION:
CC P35236; Q2TAC2: CCDC57; NbExp=3; IntAct=EBI-2265723, EBI-2808286;
CC P35236; Q53SE7: FLJ13057; NbExp=3; IntAct=EBI-2265723, EBI-10172181;
CC P35236; P28482: MAPK1; NbExp=6; IntAct=EBI-2265723, EBI-959949;
CC P35236; P47811: Mapk14; Xeno; NbExp=2; IntAct=EBI-2265723, EBI-298727;
CC P35236-2; Q96IK5: GMCL1; NbExp=3; IntAct=EBI-12281408, EBI-2548508;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14613483}.
CC Cytoplasm, cytoskeleton {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P35236-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P35236-2; Sequence=VSP_026925;
CC Name=3;
CC IsoId=P35236-3; Sequence=VSP_047275;
CC -!- TISSUE SPECIFICITY: Expressed exclusively in thymus and spleen.
CC {ECO:0000269|PubMed:1510684, ECO:0000269|PubMed:1530918}.
CC -!- PTM: Phosphorylated on serine residues in resting T-cells.
CC Phosphorylation increases upon exposure to stimuli that increase
CC intracellular cAMP levels. Phosphorylation leads to dissociation of
CC bound MAP kinases. {ECO:0000269|PubMed:10206983,
CC ECO:0000269|PubMed:10559944, ECO:0000269|PubMed:14613483}.
CC -!- PTM: Oxidized at active site cysteine. Treatment with pervanadate
CC (vanadate and H(2)O(2)) or with antigen enhanced oxidation of active
CC site cysteine (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA59531.1; Type=Frameshift; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/PTPN7ID41921ch1q32.html";
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DR EMBL; D11327; BAA01946.1; -; mRNA.
DR EMBL; M64322; AAA59531.1; ALT_FRAME; mRNA.
DR EMBL; BT009848; AAP88850.1; -; mRNA.
DR EMBL; AK127214; BAG54453.1; -; mRNA.
DR EMBL; AL592300; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC001746; AAH01746.2; -; mRNA.
DR CCDS; CCDS1422.1; -. [P35236-2]
DR CCDS; CCDS1423.2; -. [P35236-1]
DR PIR; JH0692; JH0692.
DR RefSeq; NP_002823.3; NM_002832.3. [P35236-1]
DR RefSeq; NP_542155.1; NM_080588.2. [P35236-2]
DR PDB; 1ZC0; X-ray; 1.85 A; A=65-360.
DR PDB; 2A3K; X-ray; 2.55 A; A=65-358.
DR PDB; 2GP0; X-ray; 2.05 A; A=65-360.
DR PDB; 2GPH; X-ray; 1.90 A; B=37-52.
DR PDB; 2HVL; X-ray; 2.40 A; A=65-360.
DR PDB; 2QDC; X-ray; 2.00 A; A=65-360.
DR PDB; 2QDM; X-ray; 2.05 A; A=65-360.
DR PDB; 2QDP; X-ray; 2.72 A; A=65-360.
DR PDB; 3D42; X-ray; 2.46 A; A=65-360.
DR PDB; 3D44; X-ray; 1.90 A; A=65-360.
DR PDB; 3O4S; X-ray; 1.90 A; A=65-360.
DR PDB; 3O4T; X-ray; 2.60 A; A=65-360.
DR PDB; 3O4U; X-ray; 2.25 A; A=65-360.
DR PDBsum; 1ZC0; -.
DR PDBsum; 2A3K; -.
DR PDBsum; 2GP0; -.
DR PDBsum; 2GPH; -.
DR PDBsum; 2HVL; -.
DR PDBsum; 2QDC; -.
DR PDBsum; 2QDM; -.
DR PDBsum; 2QDP; -.
DR PDBsum; 3D42; -.
DR PDBsum; 3D44; -.
DR PDBsum; 3O4S; -.
DR PDBsum; 3O4T; -.
DR PDBsum; 3O4U; -.
DR AlphaFoldDB; P35236; -.
DR BMRB; P35236; -.
DR SMR; P35236; -.
DR BioGRID; 111743; 64.
DR DIP; DIP-29118N; -.
DR ELM; P35236; -.
DR IntAct; P35236; 24.
DR MINT; P35236; -.
DR STRING; 9606.ENSP00000309116; -.
DR BindingDB; P35236; -.
DR ChEMBL; CHEMBL2219; -.
DR DrugCentral; P35236; -.
DR DEPOD; PTPN7; -.
DR GlyGen; P35236; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; P35236; -.
DR PhosphoSitePlus; P35236; -.
DR BioMuta; PTPN7; -.
DR DMDM; 20141721; -.
DR EPD; P35236; -.
DR jPOST; P35236; -.
DR MassIVE; P35236; -.
DR MaxQB; P35236; -.
DR PaxDb; P35236; -.
DR PeptideAtlas; P35236; -.
DR PRIDE; P35236; -.
DR ProteomicsDB; 54996; -. [P35236-1]
DR ProteomicsDB; 54997; -. [P35236-2]
DR Antibodypedia; 20651; 350 antibodies from 30 providers.
DR DNASU; 5778; -.
DR Ensembl; ENST00000309017.8; ENSP00000309116.4; ENSG00000143851.16. [P35236-1]
DR Ensembl; ENST00000367279.8; ENSP00000356248.4; ENSG00000143851.16. [P35236-2]
DR Ensembl; ENST00000477554.6; ENSP00000418416.2; ENSG00000143851.16. [P35236-1]
DR Ensembl; ENST00000495688.5; ENSP00000420506.1; ENSG00000143851.16. [P35236-1]
DR Ensembl; ENST00000691036.1; ENSP00000509436.1; ENSG00000143851.16. [P35236-1]
DR GeneID; 5778; -.
DR KEGG; hsa:5778; -.
DR MANE-Select; ENST00000691036.1; ENSP00000509436.1; NM_002832.4; NP_002823.4.
DR UCSC; uc001gxl.2; human. [P35236-1]
DR CTD; 5778; -.
DR DisGeNET; 5778; -.
DR GeneCards; PTPN7; -.
DR HGNC; HGNC:9659; PTPN7.
DR HPA; ENSG00000143851; Group enriched (bone marrow, lymphoid tissue).
DR MIM; 176889; gene.
DR neXtProt; NX_P35236; -.
DR OpenTargets; ENSG00000143851; -.
DR PharmGKB; PA34003; -.
DR VEuPathDB; HostDB:ENSG00000143851; -.
DR eggNOG; KOG0789; Eukaryota.
DR GeneTree; ENSGT00940000160979; -.
DR HOGENOM; CLU_001645_10_3_1; -.
DR InParanoid; P35236; -.
DR OMA; GYDGREK; -.
DR OrthoDB; 411281at2759; -.
DR PhylomeDB; P35236; -.
DR TreeFam; TF331016; -.
DR BRENDA; 3.1.3.48; 2681.
DR PathwayCommons; P35236; -.
DR Reactome; R-HSA-5675221; Negative regulation of MAPK pathway.
DR Reactome; R-HSA-9008059; Interleukin-37 signaling.
DR SABIO-RK; P35236; -.
DR SignaLink; P35236; -.
DR SIGNOR; P35236; -.
DR BioGRID-ORCS; 5778; 24 hits in 1075 CRISPR screens.
DR ChiTaRS; PTPN7; human.
DR EvolutionaryTrace; P35236; -.
DR GeneWiki; PTPN7; -.
DR GenomeRNAi; 5778; -.
DR Pharos; P35236; Tchem.
DR PRO; PR:P35236; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P35236; protein.
DR Bgee; ENSG00000143851; Expressed in granulocyte and 115 other tissues.
DR ExpressionAtlas; P35236; baseline and differential.
DR Genevisible; P35236; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:BHF-UCL.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:HPA.
DR GO; GO:0072686; C:mitotic spindle; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0004726; F:non-membrane spanning protein tyrosine phosphatase activity; TAS:Reactome.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IBA:GO_Central.
DR GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR DisProt; DP01646; -.
DR Gene3D; 3.90.190.10; -; 1.
DR IDEAL; IID00617; -.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000242; PTP_cat.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR008356; Tyr_Pase_KIM-con.
DR PANTHER; PTHR46198; PTHR46198; 1.
DR Pfam; PF00102; Y_phosphatase; 1.
DR PRINTS; PR01778; KIMPTPASE.
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; Alternative splicing; Cytoplasm; Cytoskeleton; Hydrolase;
KW Oxidation; Phosphoprotein; Protein phosphatase; Reference proteome.
FT CHAIN 1..360
FT /note="Tyrosine-protein phosphatase non-receptor type 7"
FT /id="PRO_0000094761"
FT DOMAIN 97..350
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 38..51
FT /note="Interaction with MAP kinases"
FT ACT_SITE 291
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160,
FT ECO:0000255|PROSITE-ProRule:PRU10044,
FT ECO:0000269|PubMed:9624114"
FT BINDING 257
FT /ligand="substrate"
FT BINDING 291..297
FT /ligand="substrate"
FT BINDING 335
FT /ligand="substrate"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:10559944,
FT ECO:0000269|PubMed:14613483, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 66
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:10206983,
FT ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:23186163"
FT MOD_RES 93
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:10206983"
FT MOD_RES 110
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 143
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 291
FT /note="Cysteine sulfenic acid (-SOH)"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1
FT /note="M -> MGASFWPIRQAREQQRRALSFRQTSWLSEPPLGPAPHLSM (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_026925"
FT VAR_SEQ 1
FT /note="M -> MVGKAWPLTHSQGTGPWAPEGHRREAADPWWQRQQAQEGRMQLGCAW
FT VAARRGGGRKLASWSLLSPQRQTDRQTDSWQEAAWGPQLLQQTSWLSEPPLGPAPHLSM
FT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_047275"
FT MUTAGEN 44
FT /note="S->A: Prevents dissociation of bound MAP kinase and
FT enhances their dephosphorylation."
FT /evidence="ECO:0000269|PubMed:14613483"
FT MUTAGEN 44
FT /note="S->D: Reduces binding of MAP kinase."
FT /evidence="ECO:0000269|PubMed:14613483"
FT MUTAGEN 66
FT /note="T->A: Prevents dissociation of bound MAP kinase and
FT enhances their dephosphorylation; when associated with A-
FT 93."
FT /evidence="ECO:0000269|PubMed:10206983"
FT MUTAGEN 93
FT /note="S->A: Prevents dissociation of bound MAP kinase and
FT enhances their dephosphorylation; when associated with A-
FT 66."
FT /evidence="ECO:0000269|PubMed:10206983"
FT MUTAGEN 125
FT /note="Y->A: Strongly reduced catalytic activity."
FT /evidence="ECO:0000269|PubMed:15466470"
FT MUTAGEN 257
FT /note="D->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:15466470"
FT MUTAGEN 291
FT /note="C->S: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:9624114"
FT MUTAGEN 335
FT /note="Q->A: Reduced catalytic activity."
FT /evidence="ECO:0000269|PubMed:15466470"
FT CONFLICT 235..236
FT /note="QL -> HV (in Ref. 2; AAA59531)"
FT /evidence="ECO:0000305"
FT CONFLICT 337
FT /note="A -> D (in Ref. 1; BAA01946)"
FT /evidence="ECO:0000305"
FT HELIX 38..41
FT /evidence="ECO:0007829|PDB:2GPH"
FT HELIX 67..77
FT /evidence="ECO:0007829|PDB:1ZC0"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:3D44"
FT HELIX 84..89
FT /evidence="ECO:0007829|PDB:1ZC0"
FT HELIX 94..103
FT /evidence="ECO:0007829|PDB:1ZC0"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:1ZC0"
FT HELIX 119..122
FT /evidence="ECO:0007829|PDB:1ZC0"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:1ZC0"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:1ZC0"
FT STRAND 149..155
FT /evidence="ECO:0007829|PDB:1ZC0"
FT HELIX 158..160
FT /evidence="ECO:0007829|PDB:1ZC0"
FT STRAND 164..169
FT /evidence="ECO:0007829|PDB:1ZC0"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:1ZC0"
FT HELIX 176..185
FT /evidence="ECO:0007829|PDB:1ZC0"
FT STRAND 190..194
FT /evidence="ECO:0007829|PDB:1ZC0"
FT STRAND 199..201
FT /evidence="ECO:0007829|PDB:3O4S"
FT STRAND 210..215
FT /evidence="ECO:0007829|PDB:1ZC0"
FT STRAND 218..227
FT /evidence="ECO:0007829|PDB:1ZC0"
FT STRAND 229..240
FT /evidence="ECO:0007829|PDB:1ZC0"
FT STRAND 243..252
FT /evidence="ECO:0007829|PDB:1ZC0"
FT HELIX 264..275
FT /evidence="ECO:0007829|PDB:1ZC0"
FT STRAND 281..283
FT /evidence="ECO:0007829|PDB:3D44"
FT STRAND 287..295
FT /evidence="ECO:0007829|PDB:1ZC0"
FT HELIX 296..314
FT /evidence="ECO:0007829|PDB:1ZC0"
FT STRAND 315..317
FT /evidence="ECO:0007829|PDB:1ZC0"
FT HELIX 319..329
FT /evidence="ECO:0007829|PDB:1ZC0"
FT HELIX 337..353
FT /evidence="ECO:0007829|PDB:1ZC0"
FT CONFLICT P35236-3:37
FT /note="Q -> R (in Ref. 4; BAG54453)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 360 AA; 40529 MW; 388A154CC55AC0EE CRC64;
MVQAHGGRSR AQPLTLSLGA AMTQPPPEKT PAKKHVRLQE RRGSNVALML DVRSLGAVEP
ICSVNTPREV TLHFLRTAGH PLTRWALQRQ PPSPKQLEEE FLKIPSNFVS PEDLDIPGHA
SKDRYKTILP NPQSRVCLGR AQSQEDGDYI NANYIRGYDG KEKVYIATQG PMPNTVSDFW
EMVWQEEVSL IVMLTQLREG KEKCVHYWPT EEETYGPFQI RIQDMKECPE YTVRQLTIQY
QEERRSVKHI LFSAWPDHQT PESAGPLLRL VAEVEESPET AAHPGPIVVH CSAGIGRTGC
FIATRIGCQQ LKARGEVDIL GIVCQLRLDR GGMIQTAEQY QFLHHTLALY AGQLPEEPSP
