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UniProtKB/Swiss-Prot entry Q03558


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

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Entry information
Entry name OYE2_YEAST
Primary accession number Q03558
Secondary accession numbers None
Integrated into Swiss-Prot on October 1, 1993
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    September 2, 2008 (Entry version 71)
Name and origin of the protein
Protein name NADPH dehydrogenase 2
Synonyms EC 1.6.99.1
Old yellow enzyme 2
Gene name
Name: OYE2
OrderedLocusNames: YHR179W
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.
PubMed=8454584 [NCBI, ExPASy, EBI, Israel, Japan]
Stott K., Saito K., Thiels D.J., Massey V.;
"Old Yellow Enzyme. The discovery of multiple isozymes and a family of related proteins.";
J. Biol. Chem. 268:6097-6106(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204511 / S288c / AB972;
PubMed=8091229 [NCBI, ExPASy, EBI, Israel, Japan]
Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z., Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T., Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J., Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L., St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P., Waterston R., Wilson R., Vaudin M.;
"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome VIII.";
Science 265:2077-2082(1994).
[3]
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).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-353, 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).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-353, 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).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137; TYR-305; SER-353; SER-379 AND THR-388, 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
L06124; AAA83386.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U00027; AAB68024.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A46009; A46009.
RefSeq NP_012049.1; -.
3D structure databases
HSSP Q02899; 1OYC. [HSSP ENTRY / PDB]
SMR Q03558; 3-399.
ModBase Q03558.
Protein-protein interaction databases
DIP DIP:213N; -.
IntAct Q03558; -.
Organism-specific databases
CYGD YHR179w; -.
SGD S000001222; OYE2.
Yeast-GFP YHR179W.
Gene expression databases
GermOnline YHR179W; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005739; Cellular component: mitochondrion (inferred from direct assay from SGD).
GO:0005634; Cellular component: nucleus (inferred from direct assay from SGD).
GO:0003959; Molecular function: NADPH dehydrogenase activity (inferred from direct assay from SGD).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
QuickGo view.
Family and domain databases
InterPro IPR013785; Aldolase_TIM.
IPR001155; OxRdtase_FMN_N.
Graphical view of domain structure.
Gene3D G3DSA:3.20.20.70; Aldolase_TIM; 1.
Pfam PF00724; Oxidored_FMN; 1.
Pfam graphical view of domain structure.
BLOCKS Q03558.
Proteomic databases
PeptideAtlas Q03558; -.
Genome annotation databases
Ensembl YHR179W; Saccharomyces cerevisiae. [Contig view]
GeneID 856584; -.
GenomeReviews U00093_GR; YHR179W.
KEGG sce:YHR179W; -.
NMPDR fig|4932.3.peg.3215; -.
Phylogenomic databases
HOGENOM Q03558; -.
Other
LinkHub Q03558; -.
ProtoNet Q03558.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Direct protein sequencing; Flavoprotein; FMN; NADP; Oxidoreductase; Phosphoprotein.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   400  399     NADPH dehydrogenase 2. PRO_0000194474
ACT_SITE   197   197        Proton donor (By similarity). 
BINDING   38    38        FMN (By similarity). 
BINDING   192   192        FMN (By similarity). 
BINDING   192   192        Substrate (By similarity). 
BINDING   195   195        Substrate (By similarity). 
BINDING   244   244        FMN (By similarity). 
BINDING   349   349        FMN (By similarity). 
BINDING   376   376        Substrate (By similarity). 
MOD_RES   137   137        Phosphoserine. 
MOD_RES   305   305        Phosphotyrosine. 
MOD_RES   353   353        Phosphoserine. 
MOD_RES   379   379        Phosphoserine. 
MOD_RES   388   388        Phosphothreonine. 
Sequence information
Length: 400 AA [This is the length of the unprocessed precursor] Molecular weight: 45011 Da [This is the MW of the unprocessed precursor] CRC64: 67D4FF141B40324E [This is a checksum on the sequence]
        10         20         30         40         50         60 
MPFVKDFKPQ ALGDTNLFKP IKIGNNELLH RAVIPPLTRM RAQHPGNIPN RDWAVEYYAQ 

        70         80         90        100        110        120 
RAQRPGTLII TEGTFPSPQS GGYDNAPGIW SEEQIKEWTK IFKAIHENKS FAWVQLWVLG 

       130        140        150        160        170        180 
WAAFPDTLAR DGLRYDSASD NVYMNAEQEE KAKKANNPQH SITKDEIKQY VKEYVQAAKN 

       190        200        210        220        230        240 
SIAAGADGVE IHSANGYLLN QFLDPHSNNR TDEYGGSIEN RARFTLEVVD AVVDAIGPEK 

       250        260        270        280        290        300 
VGLRLSPYGV FNSMSGGAET GIVAQYAYVL GELERRAKAG KRLAFVHLVE PRVTNPFLTE 

       310        320        330        340        350        360 
GEGEYNGGSN KFAYSIWKGP IIRAGNFALH PEVVREEVKD PRTLIGYGRF FISNPDLVDR 

       370        380        390        400 
LEKGLPLNKY DRDTFYKMSA EGYIDYPTYE EALKLGWDKN 

Q03558 in FASTA format

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