PTP2_YEAST
ID PTP2_YEAST Reviewed; 750 AA.
AC P29461; D6W2R4;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Tyrosine-protein phosphatase 2;
DE EC=3.1.3.48;
DE AltName: Full=Protein-tyrosine phosphatase 2;
DE Short=PTPase 2;
GN Name=PTP2; OrderedLocusNames=YOR208W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1577774; DOI=10.1016/s0021-9258(19)50194-6;
RA Guan K., Deschenes R.J., Dixon J.E.;
RT "Isolation and characterization of a second protein tyrosine phosphatase
RT gene, PTP2, from Saccharomyces cerevisiae.";
RL J. Biol. Chem. 267:10024-10030(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1549598; DOI=10.1073/pnas.89.6.2355;
RA Ota I.M., Varshavsky A.;
RT "A gene encoding a putative tyrosine phosphatase suppresses lethality of an
RT N-end rule-dependent mutant.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:2355-2359(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1452018; DOI=10.1016/0378-1119(92)90037-p;
RA James P., Hall B.D., Whelen S., Craig E.A.;
RT "Multiple protein tyrosine phosphatase-encoding genes in the yeast
RT Saccharomyces cerevisiae.";
RL Gene 122:101-110(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [6]
RP FUNCTION, AND INTERACTION WITH HOG1.
RX PubMed=9032256; DOI=10.1128/mcb.17.3.1289;
RA Wurgler-Murphy S.M., Maeda T., Witten E.A., Saito H.;
RT "Regulation of the Saccharomyces cerevisiae HOG1 mitogen-activated protein
RT kinase by the PTP2 and PTP3 protein tyrosine phosphatases.";
RL Mol. Cell. Biol. 17:1289-1297(1997).
RN [7]
RP FUNCTION, AND INTERACTION WITH HOG1.
RX PubMed=9211927; DOI=10.1074/jbc.272.28.17749;
RA Jacoby T., Flanagan H., Faykin A., Seto A.G., Mattison C.P., Ota I.M.;
RT "Two protein-tyrosine phosphatases inactivate the osmotic stress response
RT pathway in yeast by targeting the mitogen-activated protein kinase, Hog1.";
RL J. Biol. Chem. 272:17749-17755(1997).
RN [8]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [9]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258 AND SER-430, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-430, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Major phosphatase responsible with PTP3 for tyrosine
CC dephosphorylation of MAP kinase HOG1 to inactivate its activity. May
CC also be involved in the regulation of MAP kinase FUS3. May be
CC implicated in the ubiquitin-mediated protein degradation.
CC {ECO:0000269|PubMed:9032256, ECO:0000269|PubMed:9211927}.
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 HOG1. {ECO:0000269|PubMed:9032256,
CC ECO:0000269|PubMed:9211927}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 149 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class subfamily. {ECO:0000305}.
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DR EMBL; M85287; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; M82872; AAA34922.1; -; Genomic_DNA.
DR EMBL; M38723; AAB59323.1; -; Genomic_DNA.
DR EMBL; Z75116; CAA99423.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10980.1; -; Genomic_DNA.
DR PIR; S67100; S67100.
DR RefSeq; NP_014851.3; NM_001183627.3.
DR AlphaFoldDB; P29461; -.
DR SMR; P29461; -.
DR BioGRID; 34603; 84.
DR DIP; DIP-2369N; -.
DR IntAct; P29461; 4.
DR MINT; P29461; -.
DR STRING; 4932.YOR208W; -.
DR iPTMnet; P29461; -.
DR MaxQB; P29461; -.
DR PaxDb; P29461; -.
DR PRIDE; P29461; -.
DR EnsemblFungi; YOR208W_mRNA; YOR208W; YOR208W.
DR GeneID; 854383; -.
DR KEGG; sce:YOR208W; -.
DR SGD; S000005734; PTP2.
DR VEuPathDB; FungiDB:YOR208W; -.
DR eggNOG; KOG0789; Eukaryota.
DR HOGENOM; CLU_009242_0_0_1; -.
DR InParanoid; P29461; -.
DR OMA; RKWDIYW; -.
DR BioCyc; YEAST:YOR208W-MON; -.
DR Reactome; R-SCE-5675221; Negative regulation of MAPK pathway.
DR PRO; PR:P29461; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P29461; protein.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IBA:GO_Central.
DR GO; GO:0051457; P:maintenance of protein location in nucleus; IMP:SGD.
DR GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; IMP:SGD.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR GO; GO:0043937; P:regulation of sporulation; IGI:SGD.
DR Gene3D; 3.90.190.10; -; 1.
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 Pfam; PF00102; Y_phosphatase; 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 Cytoplasm; Hydrolase; Nucleus; Phosphoprotein; Protein phosphatase;
KW Reference proteome.
FT CHAIN 1..750
FT /note="Tyrosine-protein phosphatase 2"
FT /id="PRO_0000094856"
FT DOMAIN 383..737
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 327..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 425..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..348
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 666
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160,
FT ECO:0000255|PROSITE-ProRule:PRU10044"
FT MOD_RES 258
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 430
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT CONFLICT 371
FT /note="L -> S (in Ref. 3; AAB59323)"
FT /evidence="ECO:0000305"
FT CONFLICT 474..475
FT /note="KL -> NV (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 660..661
FT /note="SP -> GA (in Ref. 3; AAB59323)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 750 AA; 85868 MW; 1033D2F0AA23BD35 CRC64;
MDRIAQQYRN GKRDNNGNRM ASSAISEKGH IQVNQTRTPG QMPVYRGETI NLSNLPQNQI
KPCKDLDDVN IRRNNSNRHS KILLLDLCAG PNTNSFLGNT NAKDITVLSL PLPSTLVKRS
NYPFENLLKN YLGSDEKYIE FTKIIKDYDI FIFSDSFSRI SSCLKTTFCL IEKFKKFICH
FFPSPYLKFF LLEGSLNDSK APSLGKNKKN CILPKLDLNL NVNLTSRSTL NLRINIPPPN
DSNKIFLQSL KKDLIHYSPN SLQKFFQFNM PADLAPNDTI LPNWLKFCSV KENEKVILKK
LFNNFETLEN FEMQRLEKCL KFKKKPLHQK QLSQKQRGPQ STDDSKLYSL TSLQRQYKSS
LKSNIQKNQK LKLIIPKNNT SSSPSPLSSD DTIMSPINDY ELTEGIQSFT KNRYSNILPY
EHSRVKLPHS PKPPAVSEAS TTETKTDKSY PMCPVDAKNH SCKPNDYINA NYLKLTQINP
DFKYIATQAP LPSTMDDFWK VITLNKVKVI ISLNSDDELN LRKWDIYWNN LSYSNHTIKL
QNTWENICNI NGCVLRVFQV KKTAPQNDNI SQDCDLPHNG DLTSITMAVS EPFIVYQLQY
KNWLDSCGVD MNDIIKLHKV KNSLLFNPQS FITSLEKDVC KPDLIDDNNS ELHLDTANSS
PLLVHCSAGC GRTGVFVTLD FLLSILSPTT NHSNKIDVWN MTQDLIFIIV NELRKQRISM
VQNLTQYIAC YEALLNYFAL QKQIKNALPC
