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-MAY-2013, entry version 109.
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;
RG Saccharomyces Genome Database;
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
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).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-664, AND MASS
RP SPECTROMETRY.
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass
RT spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
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.
CC -!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
CC tyrosine + phosphate.
CC -!- CATALYTIC ACTIVITY: A phosphoprotein + H(2)O = a protein +
CC phosphate.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC Non-receptor class dual specificity subfamily.
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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; 455-529, 580-805.
DR DIP; DIP-6546N; -.
DR IntAct; P38148; 2.
DR MINT; MINT-702219; -.
DR STRING; 4932.YBR276C; -.
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 KO; K01104; -.
DR OrthoDB; EOG4Q8866; -.
DR BioCyc; YEAST:G3O-29197-MONOMER; -.
DR NextBio; 971721; -.
DR Genevestigator; P38148; -.
DR GermOnline; YBR276C; Saccharomyces cerevisiae.
DR GO; GO:0005829; C:cytosol; IBA:RefGenome.
DR GO; GO:0005634; C:nucleus; IBA:RefGenome.
DR GO; GO:0017017; F:MAP kinase tyrosine/serine/threonine phosphatase activity; IBA:RefGenome.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:EC.
DR GO; GO:0000754; P:adaptation of signaling pathway by response to pheromone involved in conjugation with cellular fusion; IBA:RefGenome.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; IEA:GOC.
DR GO; GO:0010969; P:regulation of pheromone-dependent signal transduction involved in conjugation with cellular fusion; IBA:RefGenome.
DR GO; GO:0007090; P:regulation of S phase of mitotic cell cycle; IGI:SGD.
DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR InterPro; IPR020422; Dual-sp_phosphatase_subgr_cat.
DR InterPro; IPR024950; DUSP.
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 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; 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 (By
FT similarity).
FT MOD_RES 664 664 Phosphothreonine.
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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