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UniProtKB/Swiss-Prot entry Q12068


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

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Entry information
Entry name GRE2_YEAST
Primary accession number Q12068
Secondary accession numbers None
Integrated into Swiss-Prot on October 25, 2004
Sequence was last modified on November 1, 1996 (Sequence version 1)
Annotations were last modified on    December 16, 2008 (Entry version 60)
Name and origin of the protein
Protein name NADPH-dependent methylglyoxal reductase GRE2
Synonyms EC 1.1.1.283
Genes de respuesta a estres protein 2
Gene name
Name: GRE2
OrderedLocusNames: YOL151W
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].
STRAIN=ATCC 96604 / S288c / FY1679;
PubMed=8553699 [NCBI, ExPASy, EBI, Israel, Japan]
Casamayor A., Aldea M., Casas C., Herrero E., Gamo F.-J., Lafuente M.J., Gancedo C., Arino J.;
"DNA sequence analysis of a 13 kbp fragment of the left arm of yeast chromosome XV containing seven new open reading frames.";
Yeast 11:1281-1288(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 96604 / S288c / FY1679;
PubMed=9169874 [NCBI, ExPASy, EBI, Israel, Japan]
Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
Nature 387:98-102(1997).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
DOI=10.1101/gr.6037607; PubMed=17322287 [NCBI, ExPASy, EBI, Israel, Japan]
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.;
"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae.";
Genome Res. 17:536-543(2007).
[4]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=3896793 [NCBI, ExPASy, EBI, Israel, Japan]
Murata K., Fukuda Y., Simosaka M., Watanabe K., Saikusa T., Kimura A.;
"Metabolism of 2-oxoaldehyde in yeasts. Purification and characterization of NADPH-dependent methylglyoxal-reducing enzyme from Saccharomyces cerevisiae.";
Eur. J. Biochem. 151:631-636(1985).
[5]
FUNCTION, AND CATALYTIC ACTIVITY.
DOI=10.1002/yea.979; PubMed=12722185 [NCBI, ExPASy, EBI, Israel, Japan]
Chen C.N., Porubleva L., Shearer G., Svrakic M., Holden L.G., Dover J.L., Johnston M., Chitnis P.R., Kohl D.H.;
"Associating protein activities with their genes: rapid identification of a gene encoding a methylglyoxal reductase in the yeast Saccharomyces cerevisiae.";
Yeast 20:545-554(2003).
[6]
INDUCTION.
DOI=10.1002/(SICI)1097-0061(199907)15:10A<879::AID-YEA428>3.3.CO;2-H; PubMed=10407268 [NCBI, ExPASy, EBI, Israel, Japan]
Garay-Arroyo A., Covarrubias A.A.;
"Three genes whose expression is induced by stress in Saccharomyces cerevisiae.";
Yeast 15:879-892(1999).
[7]
INDUCTION.
DOI=10.1074/jbc.274.23.16040; PubMed=10347154 [NCBI, ExPASy, EBI, Israel, Japan]
Lee J., Godon C., Lagniel G., Spector D., Garin J., Labarre J., Toledano M.B.;
"Yap1 and Skn7 control two specialized oxidative stress response regulons in yeast.";
J. Biol. Chem. 274:16040-16046(1999).
[8]
INDUCTION.
PubMed=11401713 [NCBI, ExPASy, EBI, Israel, Japan]
Rep M., Proft M., Remize F., Tamas M., Serrano R., Thevelein J.M., Hohmann S.;
"The Saccharomyces cerevisiae Sko1p transcription factor mediates HOG pathway-dependent osmotic regulation of a set of genes encoding enzymes implicated in protection from oxidative damage.";
Mol. Microbiol. 40:1067-1083(2001).
[9]
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).
[10]
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).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333, 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
  • FUNCTION: Catalyzes the irreversible reduction of the cytotoxic compound methylglyoxal (MG) to (R)-lactaldehyde as an alternative to detoxification of MG by glyoxalase I GLO1. MG is synthesized via a bypath of glycolysis from dihydroxyacetone phosphate and is believed to play a role in cell cycle regulation and stress adaptation.
  • CATALYTIC ACTIVITY: Lactaldehyde + NADP+ = methylglyoxal + NADPH.
  • ENZYME REGULATION: Activated by glutathione.
  • SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
  • INDUCTION: Repressed by SKO1. During osmotic stress, this repression is relieved. Induced by transcription factor YAP1 during oxidative stress, and induced by ionic and heat stress.
  • MISCELLANEOUS: Present with 5458 molecules/cell in log phase SD medium.
  • MISCELLANEOUS: 'De respuesta a estres' means stress response in Spanish.
  • SIMILARITY: Belongs to the dihydroflavonol-4-reductase family.
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
Z48239; CAA88277.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z74893; CAA99172.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY558040; AAS56366.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S60386; S60386.
RefSeq NP_014490.1; -.
3D structure databases
ModBase Q12068.
Protein-protein interaction databases
DIP DIP:2645N; -.
IntAct Q12068; 2.
Enzyme and pathway databases
BioCyc MetaCyc:MON-12909; -.
Organism-specific databases
CYGD YOL151w; -.
SGD S000005511; GRE2.
Yeast-GFP YOL151W.
Gene expression databases
GermOnline YOL151W; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0005634; Cellular component: nucleus (inferred from electronic annotation from UniProtKB-KW).
GO:0046568; Molecular function: 3-methylbutanal reductase activity (inferred from mutant phenotype from SGD).
GO:0050662; Molecular function: coenzyme binding (inferred from electronic annotation from InterPro).
GO:0043892; Molecular function: methylglyoxal reductase (NADPH-dependent) activity (inferred from electronic annotation from EC).
GO:0008204; Biological process: ergosterol metabolic process (inferred from genetic interaction from SGD).
GO:0030447; Biological process: filamentous growth (inferred from mutant phenotype from SGD).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006950; Biological process: response to stress (inferred from expression pattern from SGD).
QuickGo view.
Family and domain databases
InterPro IPR001509; Epimerase_deHydtase.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.720; NAD(P)-bd; 1.
Pfam PF01370; Epimerase; 1.
Pfam graphical view of domain structure.
Proteomic databases
PeptideAtlas Q12068; -.
Genome annotation databases
Ensembl YOL151W; Saccharomyces cerevisiae. [Contig view]
GeneID 854014; -.
GenomeReviews Y13140_GR; YOL151W.
KEGG sce:YOL151W; -.
NMPDR fig|4932.3.peg.5576; -.
Phylogenomic databases
HOGENOM Q12068; -.
Other
LinkHub Q12068; -.
NextBio 975535; -.
ProtoNet Q12068.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Cytoplasm; NADP; Nucleus; Oxidoreductase; Phosphoprotein.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   342  342     NADPH-dependent methylglyoxal reductase GRE2. PRO_0000215576
MOD_RES   333   333        Phosphoserine. 
Sequence information
Length: 342 AA [This is the length of the unprocessed precursor] Molecular weight: 38170 Da [This is the MW of the unprocessed precursor] CRC64: 84DC286AAD8C88D2 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSVFVSGANG FIAQHIVDLL LKEDYKVIGS ARSQEKAENL TEAFGNNPKF SMEVVPDISK 

        70         80         90        100        110        120 
LDAFDHVFQK HGKDIKIVLH TASPFCFDIT DSERDLLIPA VNGVKGILHS IKKYAADSVE 

       130        140        150        160        170        180 
RVVLTSSYAA VFDMAKENDK SLTFNEESWN PATWESCQSD PVNAYCGSKK FAEKAAWEFL 

       190        200        210        220        230        240 
EENRDSVKFE LTAVNPVYVF GPQMFDKDVK KHLNTSCELV NSLMHLSPED KIPELFGGYI 

       250        260        270        280        290        300 
DVRDVAKAHL VAFQKRETIG QRLIVSEARF TMQDVLDILN EDFPVLKGNI PVGKPGSGAT 

       310        320        330        340 
HNTLGATLDN KKSKKLLGFK FRNLKETIDD TASQILKFEG RI 

Q12068 in FASTA format

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View entry in raw text format (no links)
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