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UniProtKB/Swiss-Prot entry P31688


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name TPS2_YEAST
Primary accession number P31688
Secondary accession numbers None
Integrated into Swiss-Prot on July 1, 1993
Sequence was last modified on October 1, 1996 (Sequence version 3)
Annotations were last modified on    November 25, 2008 (Entry version 84)
Name and origin of the protein
Protein name Trehalose-phosphatase
Synonyms EC 3.1.3.12
Trehalose-6-phosphate phosphatase
TPP
Trehalose synthase complex catalytic subunit TPS2
Gene name
Name: TPS2
Synonyms: PFK3
OrderedLocusNames: YDR074W
ORFNames: YD8554.07
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
STRAIN=C13-ABYS86;
PubMed=8444170 [NCBI, ExPASy, EBI, Israel, Japan]
de Virgilio C., Buerckert N., Bell W., Jenoe P., Boller T., Wiemken A.;
"Disruption of TPS2, the gene encoding the 100-kDa subunit of the trehalose-6-phosphate synthase/phosphatase complex in Saccharomyces cerevisiae, causes accumulation of trehalose-6-phosphate and loss of trehalose-6-phosphate phosphatase activity.";
Eur. J. Biochem. 212:315-323(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204511 / S288c / AB972;
PubMed=9169867 [NCBI, ExPASy, EBI, Israel, Japan]
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
Nature 387:75-78(1997).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 608-896.
STRAIN=ATCC 208353 / W303-1A;
PubMed=1656215 [NCBI, ExPASy, EBI, Israel, Japan]
Ronne H., Carlberg M., Hu G.-Z., Nehlin J.O.;
"Protein phosphatase 2A in Saccharomyces cerevisiae: effects on cell growth and bud morphogenesis.";
Mol. Cell. Biol. 11:4876-4884(1991).
[4]
BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=2546763 [NCBI, ExPASy, EBI, Israel, Japan]
Vandercammen A., Francois J., Hers H.-G.;
"Characterization of trehalose-6-phosphate synthase and trehalose-6-phosphate phosphatase of Saccharomyces cerevisiae.";
Eur. J. Biochem. 182:613-620(1989).
[5]
FUNCTION, AND INTERACTION WITH TPS1; TPS3 AND TSL1.
PubMed=9194697 [NCBI, ExPASy, EBI, Israel, Japan]
Reinders A., Buerckert N., Hohmann S., Thevelein J.M., Boller T., Wiemken A., De Virgilio C.;
"Structural analysis of the subunits of the trehalose-6-phosphate synthase/phosphatase complex in Saccharomyces cerevisiae and their function during heat shock.";
Mol. Microbiol. 24:687-695(1997).
[6]
SUBUNIT.
DOI=10.1074/jbc.273.50.33311; PubMed=9837904 [NCBI, ExPASy, EBI, Israel, Japan]
Bell W., Sun W., Hohmann S., Wera S., Reinders A., De Virgilio C., Wiemken A., Thevelein J.M.;
"Composition and functional analysis of the Saccharomyces cerevisiae trehalose synthase complex.";
J. Biol. Chem. 273:33311-33319(1998).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-890, AND MASS SPECTROMETRY.
DOI=10.1038/nbt0302-301; PubMed=11875433 [NCBI, ExPASy, EBI, Israel, Japan]
Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M., Shabanowitz J., Hunt D.F., White F.M.;
"Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae.";
Nat. Biotechnol. 20:301-305(2002).
[8]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02026; PubMed=14562095 [NCBI, ExPASy, EBI, Israel, Japan]
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[9]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan]
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-890, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M400219-MCP200; PubMed=15665377 [NCBI, ExPASy, EBI, Israel, Japan]
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.;
"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway.";
Mol. Cell. Proteomics 4:310-327(2005).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-890, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0701622104; PubMed=17563356 [NCBI, ExPASy, EBI, Israel, Japan]
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases.";
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-890, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M700468-MCP200; PubMed=18407956 [NCBI, ExPASy, EBI, Israel, Japan]
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X70694; CAA50025.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z46796; CAA86796.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z74370; CAA98893.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X58858; CAA41661.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S48761; S48761.
RefSeq NP_010359.1; -.
3D structure databases
ModBase P31688.
Protein-protein interaction databases
DIP DIP:823N; -.
IntAct P31688; -.
Enzyme and pathway databases
BioCyc MetaCyc:MON-595; -.
Organism-specific databases
CYGD YDR074w; -.
SGD S000002481; TPS2.
Yeast-GFP YDR074W.
Gene expression databases
ArrayExpress P31688; -.
GermOnline YDR074W; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005946; Cellular component: alpha,alpha-trehalose-phosphate synthase complex (UDP-forming) (inferred from genetic interaction from SGD).
GO:0005739; Cellular component: mitochondrion (inferred from direct assay from SGD).
GO:0004805; Molecular function: trehalose-phosphatase activity (inferred from electronic annotation from EC).
GO:0006950; Biological process: response to stress (inferred from electronic annotation from UniProtKB-KW).
GO:0005992; Biological process: trehalose biosynthetic process (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR001830; Glyco_trans_20.
IPR006379; HAD-SF_hydro_IIB.
IPR003337; Trehalose_PPase.
Graphical view of domain structure.
Pfam PF00982; Glyco_transf_20; 1.
PF02358; Trehalose_PPase; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR01484; HAD-SF-IIB; 1.
TIGR00685; T6PP; 1.
BLOCKS P31688.
ProtoNet P31688.
Proteomic databases
PeptideAtlas P31688; -.
Genome annotation databases
Ensembl YDR074W; Saccharomyces cerevisiae. [Contig view]
GeneID 851646; -.
GenomeReviews Z71256_GR; YDR074W.
KEGG sce:YDR074W; -.
NMPDR fig|4932.3.peg.1104; -.
Phylogenomic databases
HOGENOM P31688; -.
Other
LinkHub P31688; -.
NextBio 969224; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Cytoplasm; Direct protein sequencing; Hydrolase; Phosphoprotein; Stress response.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   896  896     Trehalose-phosphatase. PRO_0000122509
REGION   1   554  554     Glycosyltransferase. 
MOD_RES   890   890        Phosphoserine. 
CONFLICT   48    48        F -> Y (in Ref. 1; CAA50025). 
CONFLICT   289   289        N -> D (in Ref. 1; CAA50025). 
CONFLICT   542   542        Q -> K (in Ref. 1; CAA50025). 
CONFLICT   546   546        N -> D (in Ref. 1; CAA50025). 
CONFLICT   549   549        M -> V (in Ref. 1; CAA50025). 
Sequence information
Length: 896 AA [This is the length of the unprocessed precursor] Molecular weight: 102976 Da [This is the MW of the unprocessed precursor] CRC64: E349672CCCDA9349 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MTTTAQDNSP KKRQRIINCV TQLPYKIQLG ESNDDWKISA TTGNSALFSS LEYLQFDSTE 

        70         80         90        100        110        120 
YEQHVVGWTG EITRTERNLF TREAKEKPQD LDDDPLYLTK EQINGLTTTL QDHMKSDKEA 

       130        140        150        160        170        180 
KTDTTQTAPV TNNVHPVWLL RKNQSRWRNY AEKVIWPTFH YILNPSNEGE QEKNWWYDYV 

       190        200        210        220        230        240 
KFNEAYAQKI GEVYRKGDII WIHDYYLLLL PQLLRMKFND ESIIIGYFHH APWPSNEYFR 

       250        260        270        280        290        300 
CLPRRKQILD GLVGANRICF QNESFSRHFV SSCKRLLDAT AKKSKNSSNS DQYQVSVYGG 

       310        320        330        340        350        360 
DVLVDSLPIG VNTTQILKDA FTKDIDSKVL SIKQAYQNKK IIIGRDRLDS VRGVVQKLRA 

       370        380        390        400        410        420 
FETFLAMYPE WRDQVVLIQV SSPTANRNSP QTIRLEQQVN ELVNSINSEY GNLNFSPVQH 

       430        440        450        460        470        480 
YYMRIPKDVY LSLLRVADLC LITSVRDGMN TTALEYVTVK SHMSNFLCYG NPLILSEFSG 

       490        500        510        520        530        540 
SSNVLKDAIV VNPWDSVAVA KSINMALKLD KEEKSNLESK LWKEVPTIQD WTNKFLSSLK 

       550        560        570        580        590        600 
EQASSNDDME RKMTPALNRP VLLENYKQAK RRLFLFDYDG TLTPIVKDPA AAIPSARLYT 

       610        620        630        640        650        660 
ILQKLCADPH NQIWIISGRD QKFLNKWLGG KLPQLGLSAE HGCFMKDVSC QDWVNLTEKV 

       670        680        690        700        710        720 
DMSWQVRVNE VMEEFTTRTP GSFIERKKVA LTWHYRRTVP ELGEFHAKEL KEKLLSFTDD 

       730        740        750        760        770        780 
FDLEVMDGKA NIEVRPRFVN KGEIVKRLVW HQHGKPQDML KGISEKLPKD EMPDFVLCLG 

       790        800        810        820        830        840 
DDFTDEDMFR QLNTIETCWK EKYPDQKNQW GNYGFYPVTV GSASKKTVAK AHLTDPQQVL 

       850        860        870        880        890 
ETLGLLVGDV SLFQSAGTVD LDSRGHVKNS ESSLKSKLAS KAYVMKRSAS YTGAKV 

P31688 in FASTA format

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View entry in raw text format (no links)
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