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Tyrosine-protein phosphatase non-receptor type 7 (EC 3.1.3.48) (Hematopoietic protein-tyrosine phosphatase) (HEPTP) (Protein-tyrosine phosphatase LC-PTP)

 PTN7_HUMAN              Reviewed;         360 AA.
P35236; B3KXE1; Q53XK4; Q5SXQ0; Q5SXQ1; Q9BV05;
01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
23-JAN-2002, sequence version 3.
28-FEB-2018, entry version 173.
RecName: Full=Tyrosine-protein phosphatase non-receptor type 7;
EC=3.1.3.48;
AltName: Full=Hematopoietic protein-tyrosine phosphatase;
Short=HEPTP;
AltName: Full=Protein-tyrosine phosphatase LC-PTP;
Name=PTPN7;
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), TISSUE SPECIFICITY, AND
FUNCTION.
PubMed=1510684; DOI=10.1016/S0006-291X(05)81592-X;
Adachi M., Sekiya M., Isobe M., Kumura Y., Ogita Z.I., Hinoda Y.,
Imai K., Yachi A.;
"Molecular cloning and chromosomal mapping of a human protein-tyrosine
phosphatase LC-PTP.";
Biochem. Biophys. Res. Commun. 186:1607-1615(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE
SPECIFICITY.
TISSUE=Lymphocyte;
PubMed=1530918; DOI=10.1002/eji.1830220134;
Zanke B., Suzuki H., Kishihara K., Mizzen L., Minden M., Pawson A.,
Mak T.W.;
"Cloning and expression of an inducible lymphoid-specific, protein
tyrosine phosphatase (HePTPase).";
Eur. J. Immunol. 22:235-239(1992).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Hippocampus;
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE
SPLICING.
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Lymph;
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]
FUNCTION, INTERACTION WITH MAPK1, ACTIVE SITE, AND MUTAGENESIS OF
CYS-291.
PubMed=9624114; DOI=10.1074/jbc.273.25.15340;
Saxena M., Williams S., Gilman J., Mustelin T.;
"Negative regulation of T cell antigen receptor signal transduction by
hematopoietic tyrosine phosphatase (HePTP).";
J. Biol. Chem. 273:15340-15344(1998).
[8]
FUNCTION, INTERACTION WITH MAPK1 AND MAPK3, PHOSPHORYLATION AT THR-66
AND SER-93, AND MUTAGENESIS OF THR-66 AND SER-93.
PubMed=10206983; DOI=10.1074/jbc.274.17.11693;
Saxena M., Williams S., Brockdorff J., Gilman J., Mustelin T.;
"Inhibition of T cell signaling by mitogen-activated protein kinase-
targeted hematopoietic tyrosine phosphatase (HePTP).";
J. Biol. Chem. 274:11693-11700(1999).
[9]
FUNCTION, INTERACTION WITH MAPK1, AND PHOSPHORYLATION AT SER-44.
PubMed=10559944; DOI=10.1038/13024;
Saxena M., Williams S., Tasken K., Mustelin T.;
"Crosstalk between cAMP-dependent kinase and MAP kinase through a
protein tyrosine phosphatase.";
Nat. Cell Biol. 1:305-311(1999).
[10]
FUNCTION, AND INTERACTION WITH MAPK1 AND MAPK3.
PubMed=10702794; DOI=10.1038/sj.onc.1203408;
Pettiford S.M., Herbst R.;
"The MAP-kinase ERK2 is a specific substrate of the protein tyrosine
phosphatase HePTP.";
Oncogene 19:858-869(2000).
[11]
SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-44, AND MUTAGENESIS OF
SER-44.
PubMed=14613483; DOI=10.1042/BJ20031244;
Nika K., Hyunh H., Williams S., Paul S., Bottini N., Tasken K.,
Lombroso P.J., Mustelin T.;
"Haematopoietic protein tyrosine phosphatase (HePTP) phosphorylation
by cAMP-dependent protein kinase in T-cells: dynamics and subcellular
location.";
Biochem. J. 378:335-342(2004).
[12]
MUTAGENESIS OF TYR-125; ASP-257 AND GLN-335.
PubMed=15466470; DOI=10.1074/jbc.M407820200;
Huang Z., Zhou B., Zhang Z.-Y.;
"Molecular determinants of substrate recognition in hematopoietic
protein-tyrosine phosphatase.";
J. Biol. Chem. 279:52150-52159(2004).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-66, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44 AND SER-143, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44; THR-66; SER-110 AND
SER-143, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=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).
[16]
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 65-360 OF MUTANT ASP-246 IN
COMPLEX WITH SUBSTRATE ANALOG.
PubMed=16226275; DOI=10.1016/j.jmb.2005.09.049;
Mustelin T., Tautz L., Page R.;
"Structure of the hematopoietic tyrosine phosphatase (HePTP) catalytic
domain: structure of a KIM phosphatase with phosphate bound at the
active site.";
J. Mol. Biol. 354:150-163(2005).
[17]
X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 65-358 IN COMPLEX WITH
SUBSTRATE ANALOG, AND SUBUNIT.
PubMed=16441242; DOI=10.1042/BJ20051931;
Eswaran J., von Kries J.P., Marsden B., Longman E., Debreczeni J.E.,
Ugochukwu E., Turnbull A., Lee W.H., Knapp S., Barr A.J.;
"Crystal structures and inhibitor identification for PTPN5, PTPRR and
PTPN7: a family of human MAPK-specific protein tyrosine
phosphatases.";
Biochem. J. 395:483-491(2006).
[18]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 37-52 IN COMPLEX WITH MAPK1.
PubMed=16765894; DOI=10.1016/j.str.2006.04.006;
Zhou T., Sun L., Humphreys J., Goldsmith E.J.;
"Docking interactions induce exposure of activation loop in the MAP
kinase ERK2.";
Structure 14:1011-1019(2006).
-!- FUNCTION: Protein phosphatase that acts preferentially on
tyrosine-phosphorylated MAPK1. Plays a role in the regulation of T
and B-lymphocyte development and signal transduction.
{ECO:0000269|PubMed:10206983, ECO:0000269|PubMed:10559944,
ECO:0000269|PubMed:10702794, ECO:0000269|PubMed:1510684,
ECO:0000269|PubMed:1530918, ECO:0000269|PubMed:9624114}.
-!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
tyrosine + phosphate. {ECO:0000255|PROSITE-ProRule:PRU10044}.
-!- ENZYME REGULATION: Inhibited in cells after FCER1A triggering.
{ECO:0000250}.
-!- SUBUNIT: Monomer. Interacts with MAPK1, MAPK3 and several other
MAP kinases. {ECO:0000269|PubMed:10206983,
ECO:0000269|PubMed:10559944, ECO:0000269|PubMed:10702794,
ECO:0000269|PubMed:16226275, ECO:0000269|PubMed:16441242,
ECO:0000269|PubMed:16765894, ECO:0000269|PubMed:9624114}.
-!- INTERACTION:
Q2TAC2:CCDC57; NbExp=3; IntAct=EBI-2265723, EBI-2808286;
Q53SE7:FLJ13057; NbExp=3; IntAct=EBI-2265723, EBI-10172181;
P28482:MAPK1; NbExp=6; IntAct=EBI-2265723, EBI-959949;
P47811:Mapk14 (xeno); NbExp=2; IntAct=EBI-2265723, EBI-298727;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14613483}.
Cytoplasm, cytoskeleton {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P35236-1; Sequence=Displayed;
Name=2;
IsoId=P35236-2; Sequence=VSP_026925;
Name=3;
IsoId=P35236-3; Sequence=VSP_047275;
Note=Ref.4 (BAG54453) sequence is in conflict in position:
37:Q->R. {ECO:0000305};
-!- TISSUE SPECIFICITY: Expressed exclusively in thymus and spleen.
{ECO:0000269|PubMed:1510684, ECO:0000269|PubMed:1530918}.
-!- PTM: Phosphorylated on serine residues in resting T-cells.
Phosphorylation increases upon exposure to stimuli that increase
intracellular cAMP levels. Phosphorylation leads to dissociation
of bound MAP kinases. {ECO:0000269|PubMed:10206983,
ECO:0000269|PubMed:10559944, ECO:0000269|PubMed:14613483}.
-!- PTM: Oxidized at active site cysteine. Treatment with pervanadate
(vanadate and H(2)O(2)) or with antigen enhanced oxidation of
active site cysteine (By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
Non-receptor class subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA59531.1; Type=Frameshift; Positions=5; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/PTPN7ID41921ch1q32.html";
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EMBL; D11327; BAA01946.1; -; mRNA.
EMBL; M64322; AAA59531.1; ALT_FRAME; mRNA.
EMBL; BT009848; AAP88850.1; -; mRNA.
EMBL; AK127214; BAG54453.1; -; mRNA.
EMBL; AL592300; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC001746; AAH01746.2; -; mRNA.
CCDS; CCDS1422.1; -. [P35236-2]
CCDS; CCDS1423.2; -. [P35236-3]
PIR; JH0692; JH0692.
RefSeq; NP_002823.3; NM_002832.3. [P35236-3]
RefSeq; NP_542155.1; NM_080588.2. [P35236-2]
UniGene; Hs.402773; -.
PDB; 1ZC0; X-ray; 1.85 A; A=65-360.
PDB; 2A3K; X-ray; 2.55 A; A=65-358.
PDB; 2GP0; X-ray; 2.05 A; A=65-360.
PDB; 2GPH; X-ray; 1.90 A; B=37-52.
PDB; 2HVL; X-ray; 2.40 A; A=65-360.
PDB; 2QDC; X-ray; 2.00 A; A=65-360.
PDB; 2QDM; X-ray; 2.05 A; A=65-360.
PDB; 2QDP; X-ray; 2.72 A; A=65-360.
PDB; 3D42; X-ray; 2.46 A; A=65-360.
PDB; 3D44; X-ray; 1.90 A; A=65-360.
PDB; 3O4S; X-ray; 1.90 A; A=65-360.
PDB; 3O4T; X-ray; 2.60 A; A=65-360.
PDB; 3O4U; X-ray; 2.25 A; A=65-360.
PDBsum; 1ZC0; -.
PDBsum; 2A3K; -.
PDBsum; 2GP0; -.
PDBsum; 2GPH; -.
PDBsum; 2HVL; -.
PDBsum; 2QDC; -.
PDBsum; 2QDM; -.
PDBsum; 2QDP; -.
PDBsum; 3D42; -.
PDBsum; 3D44; -.
PDBsum; 3O4S; -.
PDBsum; 3O4T; -.
PDBsum; 3O4U; -.
ProteinModelPortal; P35236; -.
SMR; P35236; -.
BioGrid; 111743; 36.
DIP; DIP-29118N; -.
ELM; P35236; -.
IntAct; P35236; 10.
MINT; P35236; -.
STRING; 9606.ENSP00000309116; -.
BindingDB; P35236; -.
ChEMBL; CHEMBL2219; -.
DEPOD; P35236; -.
iPTMnet; P35236; -.
PhosphoSitePlus; P35236; -.
DMDM; 20141721; -.
EPD; P35236; -.
MaxQB; P35236; -.
PaxDb; P35236; -.
PeptideAtlas; P35236; -.
PRIDE; P35236; -.
DNASU; 5778; -.
Ensembl; ENST00000309017; ENSP00000309116; ENSG00000143851. [P35236-3]
Ensembl; ENST00000367279; ENSP00000356248; ENSG00000143851. [P35236-2]
Ensembl; ENST00000495688; ENSP00000420506; ENSG00000143851. [P35236-1]
GeneID; 5778; -.
KEGG; hsa:5778; -.
UCSC; uc001gxl.2; human. [P35236-1]
CTD; 5778; -.
DisGeNET; 5778; -.
EuPathDB; HostDB:ENSG00000143851.15; -.
GeneCards; PTPN7; -.
H-InvDB; HIX0001472; -.
HGNC; HGNC:9659; PTPN7.
HPA; CAB009530; -.
HPA; HPA019118; -.
MIM; 176889; gene.
neXtProt; NX_P35236; -.
OpenTargets; ENSG00000143851; -.
PharmGKB; PA34003; -.
eggNOG; KOG0789; Eukaryota.
eggNOG; COG5599; LUCA.
GeneTree; ENSGT00910000144001; -.
HOGENOM; HOG000294188; -.
HOVERGEN; HBG001594; -.
InParanoid; P35236; -.
KO; K18019; -.
OrthoDB; EOG091G0HLB; -.
PhylomeDB; P35236; -.
TreeFam; TF331016; -.
BRENDA; 3.1.3.48; 2681.
Reactome; R-HSA-9008059; Interleukin-37 signaling.
SABIO-RK; P35236; -.
SIGNOR; P35236; -.
ChiTaRS; PTPN7; human.
EvolutionaryTrace; P35236; -.
GeneWiki; PTPN7; -.
GenomeRNAi; 5778; -.
PRO; PR:P35236; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000143851; -.
CleanEx; HS_PTPN7; -.
ExpressionAtlas; P35236; baseline and differential.
Genevisible; P35236; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:UniProtKB.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; IDA:BHF-UCL.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0004725; F:protein tyrosine phosphatase activity; TAS:ProtInc.
GO; GO:0071345; P:cellular response to cytokine stimulus; TAS:Reactome.
GO; GO:0006470; P:protein dephosphorylation; TAS:ProtInc.
Gene3D; 3.90.190.10; -; 1.
InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
InterPro; IPR000242; PTPase_domain.
InterPro; IPR016130; Tyr_Pase_AS.
InterPro; IPR003595; Tyr_Pase_cat.
InterPro; IPR008356; Tyr_Pase_KIM-con.
InterPro; IPR000387; TYR_PHOSPHATASE_dom.
Pfam; PF00102; Y_phosphatase; 1.
PRINTS; PR01778; KIMPTPASE.
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; Complete proteome; Cytoplasm;
Cytoskeleton; Hydrolase; Oxidation; Phosphoprotein;
Protein phosphatase; Reference proteome.
CHAIN 1 360 Tyrosine-protein phosphatase non-receptor
type 7.
/FTId=PRO_0000094761.
DOMAIN 97 350 Tyrosine-protein phosphatase.
{ECO:0000255|PROSITE-ProRule:PRU00160}.
REGION 38 51 Interaction with MAP kinases.
REGION 291 297 Substrate binding.
ACT_SITE 291 291 Phosphocysteine intermediate.
{ECO:0000255|PROSITE-ProRule:PRU00160,
ECO:0000255|PROSITE-ProRule:PRU10044,
ECO:0000269|PubMed:9624114}.
BINDING 257 257 Substrate.
BINDING 335 335 Substrate.
MOD_RES 44 44 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:10559944,
ECO:0000269|PubMed:14613483}.
MOD_RES 66 66 Phosphothreonine.
{ECO:0000244|PubMed:18088087,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:10206983}.
MOD_RES 93 93 Phosphoserine.
{ECO:0000269|PubMed:10206983}.
MOD_RES 110 110 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 143 143 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 291 291 Cysteine sulfenic acid (-SOH).
{ECO:0000250}.
VAR_SEQ 1 1 M -> MGASFWPIRQAREQQRRALSFRQTSWLSEPPLGPAP
HLSM (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_026925.
VAR_SEQ 1 1 M -> MVGKAWPLTHSQGTGPWAPEGHRREAADPWWQRQQA
QEGRMQLGCAWVAARRGGGRKLASWSLLSPQRQTDRQTDSW
QEAAWGPQLLQQTSWLSEPPLGPAPHLSM (in isoform
3). {ECO:0000303|PubMed:14702039}.
/FTId=VSP_047275.
MUTAGEN 44 44 S->A: Prevents dissociation of bound MAP
kinase and enhances their
dephosphorylation.
{ECO:0000269|PubMed:14613483}.
MUTAGEN 44 44 S->D: Reduces binding of MAP kinase.
{ECO:0000269|PubMed:14613483}.
MUTAGEN 66 66 T->A: Prevents dissociation of bound MAP
kinase and enhances their
dephosphorylation; when associated with
A-93. {ECO:0000269|PubMed:10206983}.
MUTAGEN 93 93 S->A: Prevents dissociation of bound MAP
kinase and enhances their
dephosphorylation; when associated with
A-66. {ECO:0000269|PubMed:10206983}.
MUTAGEN 125 125 Y->A: Strongly reduced catalytic
activity. {ECO:0000269|PubMed:15466470}.
MUTAGEN 257 257 D->A: Loss of catalytic activity.
{ECO:0000269|PubMed:15466470}.
MUTAGEN 291 291 C->S: Loss of catalytic activity.
{ECO:0000269|PubMed:9624114}.
MUTAGEN 335 335 Q->A: Reduced catalytic activity.
{ECO:0000269|PubMed:15466470}.
CONFLICT 235 236 QL -> HV (in Ref. 2; AAA59531).
{ECO:0000305}.
CONFLICT 337 337 A -> D (in Ref. 1; BAA01946).
{ECO:0000305}.
HELIX 38 41 {ECO:0000244|PDB:2GPH}.
HELIX 67 77 {ECO:0000244|PDB:1ZC0}.
STRAND 81 83 {ECO:0000244|PDB:3D44}.
HELIX 84 89 {ECO:0000244|PDB:1ZC0}.
HELIX 94 103 {ECO:0000244|PDB:1ZC0}.
HELIX 111 113 {ECO:0000244|PDB:1ZC0}.
HELIX 119 122 {ECO:0000244|PDB:1ZC0}.
HELIX 132 134 {ECO:0000244|PDB:1ZC0}.
STRAND 135 137 {ECO:0000244|PDB:1ZC0}.
STRAND 149 155 {ECO:0000244|PDB:1ZC0}.
HELIX 158 160 {ECO:0000244|PDB:1ZC0}.
STRAND 164 169 {ECO:0000244|PDB:1ZC0}.
HELIX 173 175 {ECO:0000244|PDB:1ZC0}.
HELIX 176 185 {ECO:0000244|PDB:1ZC0}.
STRAND 190 194 {ECO:0000244|PDB:1ZC0}.
STRAND 199 201 {ECO:0000244|PDB:3O4S}.
STRAND 210 215 {ECO:0000244|PDB:1ZC0}.
STRAND 218 227 {ECO:0000244|PDB:1ZC0}.
STRAND 229 240 {ECO:0000244|PDB:1ZC0}.
STRAND 243 252 {ECO:0000244|PDB:1ZC0}.
HELIX 264 275 {ECO:0000244|PDB:1ZC0}.
STRAND 281 283 {ECO:0000244|PDB:3D44}.
STRAND 287 295 {ECO:0000244|PDB:1ZC0}.
HELIX 296 314 {ECO:0000244|PDB:1ZC0}.
STRAND 315 317 {ECO:0000244|PDB:1ZC0}.
HELIX 319 329 {ECO:0000244|PDB:1ZC0}.
HELIX 337 353 {ECO:0000244|PDB:1ZC0}.
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


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