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Database: UniProt
Entry: P38148
LinkDB: P38148
Original site: P38148 
ID   PPS1_YEAST              Reviewed;         807 AA.
AC   P38148; D6VQS2;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   29-OCT-2014, entry version 121.
DE   RecName: Full=Dual specificity protein phosphatase PPS1;
DE            EC=3.1.3.16;
DE            EC=3.1.3.48;
GN   Name=PPS1; OrderedLocusNames=YBR276C; ORFNames=YBR2013;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8091861; DOI=10.1002/yea.320100007;
RA   Holmstroem K., Brandt T., Kallesoe T.;
RT   "The sequence of a 32,420 bp segment located on the right arm of
RT   chromosome II from Saccharomyces cerevisiae.";
RL   Yeast 10:S47-S62(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7813418;
RA   Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA   Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA   Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA   Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA   Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA   Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J.,
RA   Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C.,
RA   Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M.,
RA   Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L.,
RA   Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J.,
RA   Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T.,
RA   Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A.,
RA   Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B.,
RA   Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I.,
RA   Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M.,
RA   Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A.,
RA   van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I.,
RA   Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H.,
RA   Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.;
RT   "Complete DNA sequence of yeast chromosome II.";
RL   EMBO J. 13:5795-5809(1994).
RN   [3]
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.,
RA   Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and
RT   now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   FUNCTION.
RX   PubMed=9083070; DOI=10.1074/jbc.272.14.9332;
RA   Ernsting B.R., Dixon J.E.;
RT   "The PPS1 gene of Saccharomyces cerevisiae codes for a dual
RT   specificity protein phosphatase with a role in the DNA synthesis phase
RT   of the cell cycle.";
RL   J. Biol. Chem. 272:9332-9343(1997).
CC   -!- FUNCTION: Protein phosphatase with specificity for serine,
CC       threonine, and tyrosine residues; has a role in the DNA synthesis
CC       phase of the cell cycle. {ECO:0000269|PubMed:9083070}.
CC   -!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
CC       tyrosine + phosphate. {ECO:0000255|PROSITE-ProRule:PRU10044}.
CC   -!- CATALYTIC ACTIVITY: [a protein]-serine/threonine phosphate + H(2)O
CC       = [a protein]-serine/threonine + phosphate.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC       Non-receptor class dual specificity subfamily. {ECO:0000305}.
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DR   EMBL; X76053; CAA53639.1; -; Genomic_DNA.
DR   EMBL; Z36145; CAA85239.1; -; Genomic_DNA.
DR   EMBL; BK006936; DAA07392.1; -; Genomic_DNA.
DR   PIR; S44538; S44538.
DR   RefSeq; NP_009835.3; NM_001178624.3.
DR   ProteinModelPortal; P38148; -.
DR   SMR; P38148; 646-777.
DR   BioGrid; 32971; 20.
DR   DIP; DIP-6546N; -.
DR   IntAct; P38148; 2.
DR   MINT; MINT-702219; -.
DR   STRING; 4932.YBR276C; -.
DR   MaxQB; P38148; -.
DR   PaxDb; P38148; -.
DR   PeptideAtlas; P38148; -.
DR   EnsemblFungi; YBR276C; YBR276C; YBR276C.
DR   GeneID; 852579; -.
DR   KEGG; sce:YBR276C; -.
DR   CYGD; YBR276c; -.
DR   SGD; S000000480; PPS1.
DR   eggNOG; COG2453; -.
DR   HOGENOM; HOG000115673; -.
DR   InParanoid; P38148; -.
DR   KO; K04459; -.
DR   OrthoDB; EOG7R5725; -.
DR   BioCyc; YEAST:G3O-29197-MONOMER; -.
DR   NextBio; 971721; -.
DR   Genevestigator; P38148; -.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IDA:SGD.
DR   GO; GO:0000188; P:inactivation of MAPK activity; IDA:SGD.
DR   GO; GO:0033260; P:nuclear cell cycle DNA replication; IMP:SGD.
DR   GO; GO:0006470; P:protein dephosphorylation; IDA:SGD.
DR   Gene3D; 3.90.190.10; -; 3.
DR   InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR   InterPro; IPR020422; Dual-sp_phosphatase_subgr_cat.
DR   InterPro; IPR024950; DUSP.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR000387; Tyr/Dual-sp_Pase.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   PANTHER; PTHR10159; PTHR10159; 1.
DR   Pfam; PF00782; DSPc; 1.
DR   SMART; SM00195; DSPc; 1.
DR   SUPFAM; SSF52799; SSF52799; 2.
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; Protein phosphatase;
KW   Reference proteome.
FT   CHAIN         1    807       Dual specificity protein phosphatase
FT                                PPS1.
FT                                /FTId=PRO_0000094921.
FT   REGION      593    807       Catalytic.
FT   ACT_SITE    725    725       Phosphocysteine intermediate.
FT                                {ECO:0000255|PROSITE-ProRule:PRU10044}.
SQ   SEQUENCE   807 AA;  91685 MW;  17840CF7256EF785 CRC64;
     MVLEVPSITP GELHDLMRLH QDAEWPECKK MFPWAHDISF GQPPDFPHSL AIVKSQSDAN
     NSALLRNSLE VNDIFQSWKV RTSFHREGDT CETGNDSNGF QYPNNTKELL NLLKFQIRQL
     ELQVDDVALE NAATYCHNHS ILPFLKVDPR GLSLELKRYS RNKVGSNTTL KRSGQDVWGR
     RGLFRRFDLQ CAKMIEMVDN IVIYCSRTGG STDMQTESAP ACSHEGNCPN CTTLALLLQI
     CLMFVQKGYV GSGGSLYKTN LFICTYQNFN TDIPQTLIGT PLLDNEFFKN NTPLNLCSSP
     SEIVCFNNVD KNMVLCEKLE LNKLTSATRL EETGLICGNT TDWHNYQIIK KNNISLTHRF
     EENTSIVNLK SLNYDTDNPT TSISQLYNIP NTKEVWKLII KCTSNSQMPS LTKIRTYLDL
     LLDDDASKSQ EHLHLTFPAS GSIGLGNLNI QSVEILLNVC YLIFQVSQVQ ELLTFMYCED
     GYTETSLLLT AYIIFHFNIP LQDALLRIHP RPFFLFPSDL QILGHLQPVL REFSPQNGSN
     LKLYANALKF RDKSFQLHIS SELFSSIFFM KIPLESNFVN LKGPLPSRIL RHLYLGSLDH
     AQNPALLKSL GITHIVSVGE VVSWTLNKDK IAHPVRPHRA ITMTNTNEVA GNTTCNKSRN
     RADTVVSDKQ ENGSNVVISE NSGFQICQIE NLDDNGKDPL FHQIDKVLDF ISNSEATGGK
     VLVHCMVGVS RSATVCIAEC MRYLQCDLAS AYLFVRVRRL NVIIQPNLFF VYELFKWWKK
     HYNREKDKTM DWHIICRGIA EVNMKYT
//
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