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UniProtKB/Swiss-Prot entry P00331


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

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Entry information
Entry name ADH2_YEAST
Primary accession number P00331
Secondary accession numbers None
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    July 22, 2008 (Entry version 91)
Name and origin of the protein
Protein name Alcohol dehydrogenase 2
Synonyms EC 1.1.1.1
YADH-2
Alcohol dehydrogenase II
Gene name
Name: ADH2
Synonyms: ADR2
OrderedLocusNames: YMR303C
ORFNames: YM9952.05C
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].
PubMed=6337160 [NCBI, ExPASy, EBI, Israel, Japan]
Russell D.W., Smith M., Williamson V.M., Young E.T.;
"Nucleotide sequence of the yeast alcohol dehydrogenase II gene.";
J. Biol. Chem. 258:2674-2682(1983).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6279086 [NCBI, ExPASy, EBI, Israel, Japan]
Young E.T., Williamson V.M., Taguchi A., Smith M., Sledziewski A., Russell D.W., Osterman J., Denis C., Cox D., Beier D.;
"The alcohol dehydrogenase genes of the yeast, Saccharomyces cerevisiae: isolation, structure, and regulation.";
Basic Life Sci. 19:335-361(1982).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204511 / S288c / AB972;
PubMed=9169872 [NCBI, ExPASy, EBI, Israel, Japan]
Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P., Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
Nature 387:90-93(1997).
[4]
PROTEIN SEQUENCE OF 193-207 AND 227-234.
STRAIN=ATCC 204508 / S288c;
PubMed=7895733 [NCBI, ExPASy, EBI, Israel, Japan]
Garrels J.I., Futcher B., Kobayashi R., Latter G.I., Schwender B., Volpe T., Warner J.R., McLaughlin C.S.;
"Protein identifications for a Saccharomyces cerevisiae protein database.";
Electrophoresis 15:1466-1486(1994).
[5]
ACETYLATION AT SER-2.
DOI=10.1002/elps.1150180810; PubMed=9298649 [NCBI, ExPASy, EBI, Israel, Japan]
Garrels J.I., McLaughlin C.S., Warner J.R., Futcher B., Latter G.I., Kobayashi R., Schwender B., Volpe T., Anderson D.S., Mesquita-Fuentes R., Payne W.E.;
"Proteome studies of Saccharomyces cerevisiae: identification and characterization of abundant proteins.";
Electrophoresis 18:1347-1360(1997).
[6]
REVIEW.
DOI=10.1016/S1567-1356(02)00157-5; PubMed=12702265 [NCBI, ExPASy, EBI, Israel, Japan]
Leskovac V., Trivic S., Pericin D.;
"The three zinc-containing alcohol dehydrogenases from baker's yeast, Saccharomyces cerevisiae.";
FEMS Yeast Res. 2:481-494(2002).
[7]
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).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-290, 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).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-316, AND MASS SPECTROMETRY.
DOI=10.1021/pr060559j; PubMed=17330950 [NCBI, ExPASy, EBI, Israel, Japan]
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-290; SER-294 AND THR-302, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0607084104; PubMed=17287358 [NCBI, ExPASy, EBI, Israel, Japan]
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-288; SER-290 AND SER-316, 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 0:0-0(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
J01314; AAA34408.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M38457; AAA34411.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z49212; CAA89136.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A00340; DEBYA2.
RefSeq NP_014032.1; -.
3D structure databases
HSSP P39462; 1JVB. [HSSP ENTRY / PDB]
SMR P00331; 2-348.
ModBase P00331.
Protein-protein interaction databases
DIP DIP:1181N; -.
IntAct P00331; -.
Enzyme and pathway databases
BioCyc MetaCyc:MON-11726; -.
Organism-specific databases
CYGD YMR303c; -.
SGD S000004918; ADH2.
Yeast-GFP YMR303C.
Gene expression databases
ArrayExpress P00331; -.
GermOnline YMR303C; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from direct assay from SGD).
GO:0004022; Molecular function: alcohol dehydrogenase activity (inferred from direct assay from SGD).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0000947; Biological process: amino acid catabolic process to alcohol via Ehrlich pathway (inferred from genetic interaction from SGD).
GO:0006067; Biological process: ethanol metabolic process (inferred from direct assay from SGD).
GO:0006116; Biological process: NADH oxidation (inferred from direct assay from SGD).
QuickGo view.
Family and domain databases
InterPro IPR013154; AlcDHase_GroES-like.
IPR002085; AlcDHase_SF_Zn.
IPR013149; AlcDHase_Zn-bd.
IPR002328; AlcDHase_Zn_CS.
Graphical view of domain structure.
PANTHER PTHR11695; ADH_Sf_Zn; 1.
Pfam PF08240; ADH_N; 1.
PF00107; ADH_zinc_N; 1.
Pfam graphical view of domain structure.
PROSITE PS00059; ADH_ZINC; 1.
BLOCKS P00331.
Proteomic databases
PeptideAtlas P00331; -.
Genome annotation databases
Ensembl YMR303C; Saccharomyces cerevisiae. [Contig view]
GeneID 855349; -.
GenomeReviews Z71257_GR; YMR303C.
KEGG sce:YMR303C; -.
NMPDR fig|4932.3.peg.5090; -.
Phylogenomic databases
HOGENOM P00331; -.
Other
LinkHub P00331; -.
ProtoNet P00331.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing; Metal-binding; NAD; Oxidoreductase; Phosphoprotein; Zinc.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   348  347     Alcohol dehydrogenase 2. PRO_0000160731
METAL   44    44        Zinc 1 (catalytic). 
METAL   67    67        Zinc 1 (catalytic). 
METAL   98    98        Zinc 2. 
METAL   101   101        Zinc 2. 
METAL   104   104        Zinc 2. 
METAL   112   112        Zinc 2. 
METAL   154   154        Zinc 1 (catalytic). 
MOD_RES   2     2        N-acetylserine. 
MOD_RES   288   288        Phosphoserine. 
MOD_RES   290   290        Phosphoserine. 
MOD_RES   294   294        Phosphoserine. 
MOD_RES   302   302        Phosphothreonine. 
MOD_RES   316   316        Phosphoserine. 
CONFLICT   16    16        N -> H (in Ref. 2; AAA34411). 
CONFLICT   31    31        P -> A (in Ref. 2; AAA34411). 
CONFLICT   233   233        V -> K (in Ref. 4; AA sequence). 
Sequence information
Length: 348 AA [This is the length of the unprocessed precursor] Molecular weight: 36732 Da [This is the MW of the unprocessed precursor] CRC64: 54535FC3258B10EA [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSIPETQKAI IFYESNGKLE HKDIPVPKPK PNELLINVKY SGVCHTDLHA WHGDWPLPTK 

        70         80         90        100        110        120 
LPLVGGHEGA GVVVGMGENV KGWKIGDYAG IKWLNGSCMA CEYCELGNES NCPHADLSGY 

       130        140        150        160        170        180 
THDGSFQEYA TADAVQAAHI PQGTDLAEVA PILCAGITVY KALKSANLRA GHWAAISGAA 

       190        200        210        220        230        240 
GGLGSLAVQY AKAMGYRVLG IDGGPGKEEL FTSLGGEVFI DFTKEKDIVS AVVKATNGGA 

       250        260        270        280        290        300 
HGIINVSVSE AAIEASTRYC RANGTVVLVG LPAGAKCSSD VFNHVVKSIS IVGSYVGNRA 

       310        320        330        340 
DTREALDFFA RGLVKSPIKV VGLSSLPEIY EKMEKGQIAG RYVVDTSK 

P00331 in FASTA format

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