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   02-SEP-2026, entry version 196.
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; DOI=10.1038/387s098;
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=O-phospho-L-tyrosyl-[protein] + H2O = L-tyrosyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:20101, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:61978; 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; 97.
DR   DIP; DIP-2369N; -.
DR   FunCoup; P29461; 224.
DR   IntAct; P29461; 8.
DR   MINT; P29461; -.
DR   STRING; 4932.YOR208W; -.
DR   iPTMnet; P29461; -.
DR   PaxDb; 4932-YOR208W; -.
DR   PeptideAtlas; P29461; -.
DR   EnsemblFungi; YOR208W_mRNA; YOR208W; YOR208W.
DR   GeneID; 854383; -.
DR   KEGG; sce:YOR208W; -.
DR   AGR; SGD:S000005734; -.
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   OrthoDB; 6058203at2759; -.
DR   BioCyc; YEAST:YOR208W-MONOMER; -.
DR   BioGRID-ORCS; 854383; 1 hit in 10 CRISPR screens.
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; IDA:SGD.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:SGD.
DR   GO; GO:0071474; P:cellular hyperosmotic response; IMP:SGD.
DR   GO; GO:0071852; P:fungal-type cell wall organization or biogenesis; IMP:SGD.
DR   GO; GO:0051457; P:maintenance of protein location in nucleus; IMP:SGD.
DR   GO; GO:1903138; P:negative regulation of cell integrity MAPK cascade; IDA:SGD.
DR   GO; GO:0071507; P:pheromone response MAPK cascade; IMP:SGD.
DR   GO; GO:0043937; P:regulation of sporulation; IGI:SGD.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   CDD; cd18533; PTP_fungal; 1.
DR   FunFam; 3.90.190.10:FF:000158; Tyrosine phosphatase; 1.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR050348; Protein-Tyr_Phosphatase.
DR   InterPro; IPR000242; PTP_cat.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR003595; Tyr_Pase_cat.
DR   InterPro; IPR000387; Tyr_Pase_dom.
DR   PANTHER; PTHR19134:SF561; PROTEIN TYROSINE PHOSPHATASE 36E, ISOFORM A; 1.
DR   PANTHER; PTHR19134; RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE; 1.
DR   Pfam; PF00102; Y_phosphatase; 1.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00194; PTPc; 1.
DR   SMART; SM00404; PTPc_motif; 1.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 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        330..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
//