Full text data of PTPN7
PTPN7
[Confidence: low (only semi-automatic identification from reviews)]
Tyrosine-protein phosphatase non-receptor type 7; 3.1.3.48 (Hematopoietic protein-tyrosine phosphatase; HEPTP; Protein-tyrosine phosphatase LC-PTP)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Tyrosine-protein phosphatase non-receptor type 7; 3.1.3.48 (Hematopoietic protein-tyrosine phosphatase; HEPTP; Protein-tyrosine phosphatase LC-PTP)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P35236
ID PTN7_HUMAN Reviewed; 360 AA.
AC P35236; B3KXE1; Q53XK4; Q5SXQ0; Q5SXQ1; Q9BV05;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2002, sequence version 3.
DT 22-JAN-2014, entry version 137.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
RP 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.,
RA Imai K., 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
RP 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
RT tyrosine 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
RT 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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
RP SPLICING.
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA 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.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA 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.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP FUNCTION, INTERACTION WITH MAPK1, ACTIVE SITE, AND MUTAGENESIS OF
RP 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
RP AND 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
RT protein 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
RP 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
RT by 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
RT protein-tyrosine phosphatase.";
RL J. Biol. Chem. 279:52150-52159(2004).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-66, AND MASS
RP SPECTROMETRY.
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 MASS
RP SPECTROMETRY.
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 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
RT active site.";
RL J. Mol. Biol. 354:150-163(2005).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 65-358 IN COMPLEX WITH
RP SUBSTRATE 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
RT phosphatases.";
RL Biochem. J. 395:483-491(2006).
RN [17]
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
RT kinase ERK2.";
RL Structure 14:1011-1019(2006).
CC -!- FUNCTION: Protein phosphatase that acts preferentially on
CC tyrosine-phosphorylated MAPK1. Plays a role in the regulation of T
CC and B-lymphocyte development and signal transduction.
CC -!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
CC tyrosine + phosphate.
CC -!- ENZYME REGULATION: Inhibited in cells after FCER1A triggering (By
CC similarity).
CC -!- SUBUNIT: Monomer. Interacts with MAPK1, MAPK3 and several other
CC MAP kinases.
CC -!- INTERACTION:
CC P28482:MAPK1; NbExp=5; IntAct=EBI-2265723, EBI-959949;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton (By
CC similarity).
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 Note=Ref.4 (BAG54453) sequence is in conflict in position:
CC 37:R->Q;
CC -!- TISSUE SPECIFICITY: Expressed exclusively in thymus and spleen.
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
CC of bound MAP kinases.
CC -!- PTM: Oxidized at active site cysteine. Treatment with pervanadate
CC (vanadate and H(2)O(2)) or with antigen enhanced oxidation of
CC active site cysteine (By similarity).
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC Non-receptor class subfamily.
CC -!- SIMILARITY: Contains 1 tyrosine-protein phosphatase domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA59531.1; Type=Frameshift; Positions=5;
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and 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; CAI13108.1; -; Genomic_DNA.
DR EMBL; BC001746; AAH01746.2; -; mRNA.
DR PIR; JH0692; JH0692.
DR RefSeq; NP_542155.1; NM_080588.2.
DR UniGene; Hs.402773; -.
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=37-51.
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 ProteinModelPortal; P35236; -.
DR SMR; P35236; 65-357.
DR DIP; DIP-29118N; -.
DR IntAct; P35236; 4.
DR MINT; MINT-8206881; -.
DR STRING; 9606.ENSP00000356248; -.
DR BindingDB; P35236; -.
DR ChEMBL; CHEMBL2219; -.
DR PhosphoSite; P35236; -.
DR PaxDb; P35236; -.
DR PRIDE; P35236; -.
DR DNASU; 5778; -.
DR Ensembl; ENST00000308986; ENSP00000311133; ENSG00000143851.
DR Ensembl; ENST00000367279; ENSP00000356248; ENSG00000143851.
DR Ensembl; ENST00000495688; ENSP00000420506; ENSG00000143851.
DR GeneID; 5778; -.
DR KEGG; hsa:5778; -.
DR UCSC; uc001gxo.1; human.
DR CTD; 5778; -.
DR GeneCards; GC01M202116; -.
DR H-InvDB; HIX0001472; -.
DR HGNC; HGNC:9659; PTPN7.
DR HPA; CAB009530; -.
DR HPA; HPA019118; -.
DR MIM; 176889; gene.
DR neXtProt; NX_P35236; -.
DR PharmGKB; PA34003; -.
DR eggNOG; COG5599; -.
DR HOGENOM; HOG000294188; -.
DR HOVERGEN; HBG001594; -.
DR InParanoid; P35236; -.
DR KO; K04458; -.
DR OrthoDB; EOG7288QX; -.
DR BRENDA; 3.1.3.48; 2681.
DR ChiTaRS; PTPN7; human.
DR EvolutionaryTrace; P35236; -.
DR GeneWiki; PTPN7; -.
DR GenomeRNAi; 5778; -.
DR NextBio; 22472; -.
DR PRO; PR:P35236; -.
DR ArrayExpress; P35236; -.
DR Bgee; P35236; -.
DR CleanEx; HS_PTPN7; -.
DR Genevestigator; P35236; -.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA:BHF-UCL.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; TAS:ProtInc.
DR InterPro; IPR000387; Tyr/Dual-sp_Pase.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR008356; Tyr_Pase_KIM-con.
DR InterPro; IPR000242; Tyr_Pase_rcpt/non-rcpt.
DR Pfam; PF00102; Y_phosphatase; 1.
DR PRINTS; PR01778; KIMPTPASE.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM00194; PTPc; 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; Complete proteome; Cytoplasm;
KW Cytoskeleton; Hydrolase; Oxidation; Phosphoprotein;
KW Protein phosphatase; Reference proteome.
FT CHAIN 1 360 Tyrosine-protein phosphatase non-receptor
FT type 7.
FT /FTId=PRO_0000094761.
FT DOMAIN 97 350 Tyrosine-protein phosphatase.
FT REGION 38 51 Interaction with MAP kinases.
FT REGION 291 297 Substrate binding.
FT ACT_SITE 291 291 Phosphocysteine intermediate.
FT BINDING 257 257 Substrate.
FT BINDING 335 335 Substrate.
FT MOD_RES 44 44 Phosphoserine.
FT MOD_RES 66 66 Phosphothreonine.
FT MOD_RES 93 93 Phosphoserine.
FT MOD_RES 143 143 Phosphoserine.
FT MOD_RES 291 291 Cysteine sulfenic acid (-SOH) (By
FT similarity).
FT VAR_SEQ 1 1 M -> MGASFWPIRQAREQQRRALSFRQTSWLSEPPLGPAP
FT HLSM (in isoform 2).
FT /FTId=VSP_026925.
FT VAR_SEQ 1 1 M -> MVGKAWPLTHSQGTGPWAPEGHRREAADPWWQRQQA
FT REGRMQLGCAWVAARRGGGRKLASWSLLSPQRQTDRQTDSW
FT QEAAWGPQLLQQTSWLSEPPLGPAPHLSM (in isoform
FT 3).
FT /FTId=VSP_047275.
FT MUTAGEN 44 44 S->A: Prevents dissociation of bound MAP
FT kinase and enhances their
FT dephosphorylation.
FT MUTAGEN 44 44 S->D: Reduces binding of MAP kinase.
FT MUTAGEN 66 66 T->A: Prevents dissociation of bound MAP
FT kinase and enhances their
FT dephosphorylation; when associated with
FT A-93.
FT MUTAGEN 93 93 S->A: Prevents dissociation of bound MAP
FT kinase and enhances their
FT dephosphorylation; when associated with
FT A-66.
FT MUTAGEN 125 125 Y->A: Strongly reduced catalytic
FT activity.
FT MUTAGEN 257 257 D->A: Loss of catalytic activity.
FT MUTAGEN 291 291 C->S: Loss of catalytic activity.
FT MUTAGEN 335 335 Q->A: Reduced catalytic activity.
FT CONFLICT 235 236 QL -> HV (in Ref. 2; AAA59531).
FT CONFLICT 337 337 A -> D (in Ref. 1; BAA01946).
FT HELIX 38 41
FT HELIX 67 77
FT STRAND 81 83
FT HELIX 84 89
FT HELIX 94 103
FT HELIX 111 113
FT HELIX 119 122
FT HELIX 132 134
FT STRAND 135 137
FT STRAND 149 155
FT HELIX 158 160
FT STRAND 164 169
FT HELIX 173 175
FT HELIX 176 185
FT STRAND 190 194
FT STRAND 199 201
FT STRAND 210 215
FT STRAND 218 227
FT STRAND 229 240
FT STRAND 243 252
FT HELIX 264 275
FT STRAND 281 283
FT STRAND 287 295
FT HELIX 296 314
FT STRAND 315 317
FT HELIX 319 329
FT HELIX 337 353
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
//
ID PTN7_HUMAN Reviewed; 360 AA.
AC P35236; B3KXE1; Q53XK4; Q5SXQ0; Q5SXQ1; Q9BV05;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2002, sequence version 3.
DT 22-JAN-2014, entry version 137.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
RP 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.,
RA Imai K., 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
RP 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
RT tyrosine 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
RT 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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
RP SPLICING.
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA 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.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA 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.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP FUNCTION, INTERACTION WITH MAPK1, ACTIVE SITE, AND MUTAGENESIS OF
RP 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
RP AND 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
RT protein 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
RP 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
RT by 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
RT protein-tyrosine phosphatase.";
RL J. Biol. Chem. 279:52150-52159(2004).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-66, AND MASS
RP SPECTROMETRY.
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 MASS
RP SPECTROMETRY.
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 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
RT active site.";
RL J. Mol. Biol. 354:150-163(2005).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 65-358 IN COMPLEX WITH
RP SUBSTRATE 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
RT phosphatases.";
RL Biochem. J. 395:483-491(2006).
RN [17]
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
RT kinase ERK2.";
RL Structure 14:1011-1019(2006).
CC -!- FUNCTION: Protein phosphatase that acts preferentially on
CC tyrosine-phosphorylated MAPK1. Plays a role in the regulation of T
CC and B-lymphocyte development and signal transduction.
CC -!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
CC tyrosine + phosphate.
CC -!- ENZYME REGULATION: Inhibited in cells after FCER1A triggering (By
CC similarity).
CC -!- SUBUNIT: Monomer. Interacts with MAPK1, MAPK3 and several other
CC MAP kinases.
CC -!- INTERACTION:
CC P28482:MAPK1; NbExp=5; IntAct=EBI-2265723, EBI-959949;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton (By
CC similarity).
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 Note=Ref.4 (BAG54453) sequence is in conflict in position:
CC 37:R->Q;
CC -!- TISSUE SPECIFICITY: Expressed exclusively in thymus and spleen.
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
CC of bound MAP kinases.
CC -!- PTM: Oxidized at active site cysteine. Treatment with pervanadate
CC (vanadate and H(2)O(2)) or with antigen enhanced oxidation of
CC active site cysteine (By similarity).
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC Non-receptor class subfamily.
CC -!- SIMILARITY: Contains 1 tyrosine-protein phosphatase domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA59531.1; Type=Frameshift; Positions=5;
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and 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; CAI13108.1; -; Genomic_DNA.
DR EMBL; BC001746; AAH01746.2; -; mRNA.
DR PIR; JH0692; JH0692.
DR RefSeq; NP_542155.1; NM_080588.2.
DR UniGene; Hs.402773; -.
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=37-51.
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 ProteinModelPortal; P35236; -.
DR SMR; P35236; 65-357.
DR DIP; DIP-29118N; -.
DR IntAct; P35236; 4.
DR MINT; MINT-8206881; -.
DR STRING; 9606.ENSP00000356248; -.
DR BindingDB; P35236; -.
DR ChEMBL; CHEMBL2219; -.
DR PhosphoSite; P35236; -.
DR PaxDb; P35236; -.
DR PRIDE; P35236; -.
DR DNASU; 5778; -.
DR Ensembl; ENST00000308986; ENSP00000311133; ENSG00000143851.
DR Ensembl; ENST00000367279; ENSP00000356248; ENSG00000143851.
DR Ensembl; ENST00000495688; ENSP00000420506; ENSG00000143851.
DR GeneID; 5778; -.
DR KEGG; hsa:5778; -.
DR UCSC; uc001gxo.1; human.
DR CTD; 5778; -.
DR GeneCards; GC01M202116; -.
DR H-InvDB; HIX0001472; -.
DR HGNC; HGNC:9659; PTPN7.
DR HPA; CAB009530; -.
DR HPA; HPA019118; -.
DR MIM; 176889; gene.
DR neXtProt; NX_P35236; -.
DR PharmGKB; PA34003; -.
DR eggNOG; COG5599; -.
DR HOGENOM; HOG000294188; -.
DR HOVERGEN; HBG001594; -.
DR InParanoid; P35236; -.
DR KO; K04458; -.
DR OrthoDB; EOG7288QX; -.
DR BRENDA; 3.1.3.48; 2681.
DR ChiTaRS; PTPN7; human.
DR EvolutionaryTrace; P35236; -.
DR GeneWiki; PTPN7; -.
DR GenomeRNAi; 5778; -.
DR NextBio; 22472; -.
DR PRO; PR:P35236; -.
DR ArrayExpress; P35236; -.
DR Bgee; P35236; -.
DR CleanEx; HS_PTPN7; -.
DR Genevestigator; P35236; -.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA:BHF-UCL.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; TAS:ProtInc.
DR InterPro; IPR000387; Tyr/Dual-sp_Pase.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR008356; Tyr_Pase_KIM-con.
DR InterPro; IPR000242; Tyr_Pase_rcpt/non-rcpt.
DR Pfam; PF00102; Y_phosphatase; 1.
DR PRINTS; PR01778; KIMPTPASE.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM00194; PTPc; 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; Complete proteome; Cytoplasm;
KW Cytoskeleton; Hydrolase; Oxidation; Phosphoprotein;
KW Protein phosphatase; Reference proteome.
FT CHAIN 1 360 Tyrosine-protein phosphatase non-receptor
FT type 7.
FT /FTId=PRO_0000094761.
FT DOMAIN 97 350 Tyrosine-protein phosphatase.
FT REGION 38 51 Interaction with MAP kinases.
FT REGION 291 297 Substrate binding.
FT ACT_SITE 291 291 Phosphocysteine intermediate.
FT BINDING 257 257 Substrate.
FT BINDING 335 335 Substrate.
FT MOD_RES 44 44 Phosphoserine.
FT MOD_RES 66 66 Phosphothreonine.
FT MOD_RES 93 93 Phosphoserine.
FT MOD_RES 143 143 Phosphoserine.
FT MOD_RES 291 291 Cysteine sulfenic acid (-SOH) (By
FT similarity).
FT VAR_SEQ 1 1 M -> MGASFWPIRQAREQQRRALSFRQTSWLSEPPLGPAP
FT HLSM (in isoform 2).
FT /FTId=VSP_026925.
FT VAR_SEQ 1 1 M -> MVGKAWPLTHSQGTGPWAPEGHRREAADPWWQRQQA
FT REGRMQLGCAWVAARRGGGRKLASWSLLSPQRQTDRQTDSW
FT QEAAWGPQLLQQTSWLSEPPLGPAPHLSM (in isoform
FT 3).
FT /FTId=VSP_047275.
FT MUTAGEN 44 44 S->A: Prevents dissociation of bound MAP
FT kinase and enhances their
FT dephosphorylation.
FT MUTAGEN 44 44 S->D: Reduces binding of MAP kinase.
FT MUTAGEN 66 66 T->A: Prevents dissociation of bound MAP
FT kinase and enhances their
FT dephosphorylation; when associated with
FT A-93.
FT MUTAGEN 93 93 S->A: Prevents dissociation of bound MAP
FT kinase and enhances their
FT dephosphorylation; when associated with
FT A-66.
FT MUTAGEN 125 125 Y->A: Strongly reduced catalytic
FT activity.
FT MUTAGEN 257 257 D->A: Loss of catalytic activity.
FT MUTAGEN 291 291 C->S: Loss of catalytic activity.
FT MUTAGEN 335 335 Q->A: Reduced catalytic activity.
FT CONFLICT 235 236 QL -> HV (in Ref. 2; AAA59531).
FT CONFLICT 337 337 A -> D (in Ref. 1; BAA01946).
FT HELIX 38 41
FT HELIX 67 77
FT STRAND 81 83
FT HELIX 84 89
FT HELIX 94 103
FT HELIX 111 113
FT HELIX 119 122
FT HELIX 132 134
FT STRAND 135 137
FT STRAND 149 155
FT HELIX 158 160
FT STRAND 164 169
FT HELIX 173 175
FT HELIX 176 185
FT STRAND 190 194
FT STRAND 199 201
FT STRAND 210 215
FT STRAND 218 227
FT STRAND 229 240
FT STRAND 243 252
FT HELIX 264 275
FT STRAND 281 283
FT STRAND 287 295
FT HELIX 296 314
FT STRAND 315 317
FT HELIX 319 329
FT HELIX 337 353
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
//
MIM
176889
*RECORD*
*FIELD* NO
176889
*FIELD* TI
*176889 PROTEIN-TYROSINE PHOSPHATASE, NONRECEPTOR-TYPE, 7; PTPN7
;;PROTEIN-TYROSINE PHOSPHATASE, NONRECEPTOR-TYPE, STRESS-INDUCED; PTPNI
read more*FIELD* TX
Adachi et al. (1992) identified a protein-tyrosine phosphatase expressed
in pre-B cells by reverse transcriptase-polymerase chain reaction
technique. Adachi et al. (1992) reported the sequence of the full-length
cDNA of this leukocyte PTP and showed that the mRNA was predominantly
expressed in hematopoietic cells. Furthermore, they found by
fluorescence in situ hybridization that the PTPN7 gene maps to region
1q32.1 where chromosomal deletions are observed in non-Hodgkin
lymphomas. Leukocyte PTP, which Adachi et al. (1992) referred to as
LC-PTP, showed 53.8% nucleotide sequence similarity in the catalytic
domains to leukocyte-common antigen (LCA; 151460). Since both PTPs are
predominantly expressed in hematopoietic cells and both genes map to
1q32, the 2 genes probably arose from a common ancestral gene and the
transcriptional machinery of the 2 genes may be similarly regulated.
*FIELD* SA
Adachi et al. (1992); Zanke et al. (1992)
*FIELD* RF
1. Adachi, M.; Sekiya, M.; Arimura, Y.; Takekawa, M.; Itoh, F.; Hinoda,
Y.; Imai, K.; Yachi, A.: Protein-tyrosine phosphatase expression
in pre-B cell NALM-6. Cancer Res. 52: 737-740, 1992.
2. Adachi, M.; Sekiya, M.; Isobe, M.; Kumura, Y.; Ogita, Z.; 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.
3. 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). Europ. J. Immun. 22: 235-239,
1992.
*FIELD* CD
Victor A. McKusick: 11/2/1992
*FIELD* ED
carol: 07/16/1998
terry: 8/4/1995
carol: 4/16/1993
carol: 11/2/1992
*RECORD*
*FIELD* NO
176889
*FIELD* TI
*176889 PROTEIN-TYROSINE PHOSPHATASE, NONRECEPTOR-TYPE, 7; PTPN7
;;PROTEIN-TYROSINE PHOSPHATASE, NONRECEPTOR-TYPE, STRESS-INDUCED; PTPNI
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Adachi et al. (1992) identified a protein-tyrosine phosphatase expressed
in pre-B cells by reverse transcriptase-polymerase chain reaction
technique. Adachi et al. (1992) reported the sequence of the full-length
cDNA of this leukocyte PTP and showed that the mRNA was predominantly
expressed in hematopoietic cells. Furthermore, they found by
fluorescence in situ hybridization that the PTPN7 gene maps to region
1q32.1 where chromosomal deletions are observed in non-Hodgkin
lymphomas. Leukocyte PTP, which Adachi et al. (1992) referred to as
LC-PTP, showed 53.8% nucleotide sequence similarity in the catalytic
domains to leukocyte-common antigen (LCA; 151460). Since both PTPs are
predominantly expressed in hematopoietic cells and both genes map to
1q32, the 2 genes probably arose from a common ancestral gene and the
transcriptional machinery of the 2 genes may be similarly regulated.
*FIELD* SA
Adachi et al. (1992); Zanke et al. (1992)
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1. Adachi, M.; Sekiya, M.; Arimura, Y.; Takekawa, M.; Itoh, F.; Hinoda,
Y.; Imai, K.; Yachi, A.: Protein-tyrosine phosphatase expression
in pre-B cell NALM-6. Cancer Res. 52: 737-740, 1992.
2. Adachi, M.; Sekiya, M.; Isobe, M.; Kumura, Y.; Ogita, Z.; 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.
3. 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). Europ. J. Immun. 22: 235-239,
1992.
*FIELD* CD
Victor A. McKusick: 11/2/1992
*FIELD* ED
carol: 07/16/1998
terry: 8/4/1995
carol: 4/16/1993
carol: 11/2/1992