ID MSG5_YEAST Reviewed; 489 AA. AC P38590; DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 2. DT 20-JAN-2009, entry version 72. DE RecName: Full=Tyrosine-protein phosphatase MSG5; DE EC=3.1.3.48; GN Name=MSG5; OrderedLocusNames=YNL053W; ORFNames=N2480, YNL2480W; OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=94139675; PubMed=8306972; RA Doi K., Gartner A., Ammerer G., Errede B., Shinkawa H., Sugimoto K., RA Matsumoto K.; RT "MSG5, a novel protein phosphatase promotes adaptation to pheromone RT response in S. cerevisiae."; RL EMBO J. 13:61-70(1994). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=S288c / FY1676; RX MEDLINE=96021608; PubMed=8533472; DOI=10.1002/yea.320111008; RA Bergez P., Doignon F., Crouzet M.; RT "The sequence of a 44 420 bp fragment located on the left arm of RT chromosome XIV from Saccharomyces cerevisiae."; RL Yeast 11:967-974(1995). RN [3] RP ERRATUM. RX MEDLINE=97060022; PubMed=8904343; RX DOI=10.1002/(SICI)1097-0061(19960315)12:3<297::AID-YEA940>3.0.CO;2-D; RA Bergez P., Doignon F., Crouzet M.; RL Yeast 12:297-297(1996). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S288c / FY1676; RX MEDLINE=97313269; PubMed=9169873; RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F., RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., RA Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., RA Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., RA Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., RA Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., RA Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., RA Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., RA Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., RA Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., RA Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., RA Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., RA Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., RA Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., RA Wambutt R., Wedler H., Zollner A., Hani J.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV RT and its evolutionary implications."; RL Nature 387:93-98(1997). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 415-489. RX MEDLINE=88223509; PubMed=2836092; DOI=10.1007/BF00434047; RA Seraphin B., Simon M., Faye G.; RT "Primary structure of a gene for subunit V of the cytochrome c oxidase RT from Saccharomyces cerevisiae."; RL Curr. Genet. 9:435-439(1985). RN [6] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX MEDLINE=22923965; PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., RA Dephoure N., O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22; SER-151 AND THR-178, RP AND MASS SPECTROMETRY. 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 [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-151; SER-422 AND RP THR-437, AND MASS SPECTROMETRY. 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 RT phosphoproteome analysis."; RL Mol. Cell. Proteomics 7:1389-1396(2008). CC -!- FUNCTION: Dual specificity phosphatase that dephosphorylates MAP CC kinase FUS3 on both a Tyr and a Ser or Thr. Has a role in CC adaptation to pheromone. CC -!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein CC tyrosine + phosphate. CC -!- INDUCTION: By pheromone. CC -!- MISCELLANEOUS: Present with 538 molecules/cell in log phase SD CC medium. CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. CC Non-receptor class dual specificity subfamily. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; D17548; BAA04485.1; -; Genomic_DNA. DR EMBL; U12141; AAA99659.1; -; Genomic_DNA. DR EMBL; Z71329; CAA95922.1; -; Genomic_DNA. DR EMBL; X02561; CAA26402.1; -; Genomic_DNA. DR PIR; S58725; S58725. DR RefSeq; NP_014345.1; -. DR HSSP; Q16828; 1MKP. DR DIP; DIP:5538N; -. DR IntAct; P38590; 5. DR Ensembl; YNL053W; Saccharomyces cerevisiae. DR GeneID; 855674; -. DR GenomeReviews; Y13139_GR; YNL053W. DR KEGG; sce:YNL053W; -. DR NMPDR; fig|4932.3.peg.5421; -. DR CYGD; YNL053w; -. DR SGD; S000004998; MSG5. DR HOGENOM; P38590; -. DR BRENDA; 3.1.3.48; 250. DR LinkHub; P38590; -. DR NextBio; 979960; -. DR GermOnline; YNL053W; Saccharomyces cerevisiae. DR GO; GO:0005737; C:cytoplasm; IDA:SGD. DR GO; GO:0005634; C:nucleus; IDA:SGD. DR GO; GO:0004727; F:prenylated protein tyrosine phosphatase act...; IMP:SGD. DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphata...; IEA:InterPro. DR GO; GO:0000754; P:adaptation to pheromone during conjugation ...; IMP:SGD. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0006470; P:protein amino acid dephosphorylation; IEA:InterPro. DR InterPro; IPR000387; Tyr_Pase. DR InterPro; IPR016130; Tyr_Pase_AS. DR InterPro; IPR000340; Tyr_Pase_dual_specific. DR Pfam; PF00782; DSPc; 1. DR SMART; SM00195; DSPc; 1. DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1. DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1. DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1. PE 1: Evidence at protein level; KW Cell cycle; Complete proteome; Hydrolase; Phosphoprotein; KW Protein phosphatase. FT CHAIN 1 489 Tyrosine-protein phosphatase MSG5. FT /FTId=PRO_0000094916. FT ACT_SITE 319 319 Phosphocysteine intermediate. FT MOD_RES 22 22 Phosphoserine. FT MOD_RES 151 151 Phosphoserine. FT MOD_RES 178 178 Phosphothreonine. FT MOD_RES 422 422 Phosphoserine. FT MOD_RES 437 437 Phosphothreonine. FT MUTAGEN 319 319 C->A: Loss of activity. FT CONFLICT 347 348 NK -> DE (in Ref. 1; BAA04485). SQ SEQUENCE 489 AA; 54217 MW; 0D02380B62EA48DC CRC64; MQFHSDKQHL DSKTDIDFKP NSPRSLQNRN TKNLSLDIAA LHPLMEFSSP SQDVPGSVKF PSPTPLNLFM KPKPIVLEKC PPKVSPRPTP PSLSMRRSEA SIYTLPTSLK NRTVSPSVYT KSSTVSSISK LSSSSPLSSF SEKPHLNRVH SLSVKTKDLK LKGIRGRSQT ISGLETSTPI SSTREGTLDS TDVNRFSNQK NMQTTLIFPE EDSDLNIDMV HAEIYQRTVY LDGPLLVLPP NLYLYSEPKL EDILSFDLVI NVAKEIPNLE FLIPPEMAHK IKYYHIEWTH TSKIVKDLSR LTRIIHTAHS QGKKILVHCQ CGVSRSASLI VAYIMRYYGL SLNDAYNKLK GVAKDISPNM GLIFQLMEWG TMLSKNSPGE EGETVHMPEE DDIGNNEVSS TTKSYSSASF RSFPMVTNLS SSPNDSSVNS SEVTPRTPAT LTGARTALAT ERGEDDEHCK SLSQPADSLE ASVDNESIST APEQMMFLP //