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UniProtKB/Swiss-Prot entry P53839


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

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Entry information
Entry name YN14_YEAST
Primary accession number P53839
Secondary accession numbers None
Integrated into Swiss-Prot on October 1, 1996
Sequence was last modified on October 1, 1996 (Sequence version 1)
Annotations were last modified on    December 16, 2008 (Entry version 70)
Name and origin of the protein
Protein name Putative 2-hydroxyacid dehydrogenase YNL274C
Synonym EC 1.-.-.-
Gene name
OrderedLocusNames: YNL274C
ORFNames: N0631
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 [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169873 [NCBI, ExPASy, EBI, Israel, Japan]
Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications.";
Nature 387:93-98(1997).
[2]
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).
[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 THR-31 AND SER-35, 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
Z71550; CAA96182.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY692660; AAT92679.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S63248; S63248.
RefSeq NP_014125.1; -.
3D structure databases
ModBase P53839.
Protein-protein interaction databases
IntAct P53839; 4.
Organism-specific databases
CYGD YNL274c; -.
SGD S000005218; YNL274C.
Yeast-GFP YNL274C.
Gene expression databases
ArrayExpress P53839; -.
GermOnline YNL274C; 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:0047964; Molecular function: glyoxylate reductase activity (inferred from mutant phenotype from SGD).
GO:0051287; Molecular function: NAD binding (inferred from electronic annotation from InterPro).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0009436; Biological process: glyoxylate catabolic process (inferred from mutant phenotype from SGD).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR006139; D-isomer_2_OHA_DHase.
IPR006140; D-isomer_2_OHA_DHase_NAD-bd.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.720; NAD(P)-bd; 1.
Pfam PF00389; 2-Hacid_dh; 1.
PF02826; 2-Hacid_dh_C; 1.
Pfam graphical view of domain structure.
PROSITE PS00065; D_2_HYDROXYACID_DH_1; 1.
PS00670; D_2_HYDROXYACID_DH_2; 1.
PS00671; D_2_HYDROXYACID_DH_3; 1.
Proteomic databases
PeptideAtlas P53839; -.
Genome annotation databases
Ensembl YNL274C; Saccharomyces cerevisiae. [Contig view]
GeneID 855447; -.
GenomeReviews Y13139_GR; YNL274C.
KEGG sce:YNL274C; -.
NMPDR fig|4932.3.peg.5190; -.
Phylogenomic databases
HOGENOM P53839; -.
Other
LinkHub P53839; -.
NextBio 979349; -.
ProtoNet P53839.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; NAD; Oxidoreductase; Phosphoprotein.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   350  350     Putative 2-hydroxyacid dehydrogenase YNL274C. PRO_0000076040
ACT_SITE   254   254        By similarity. 
ACT_SITE   283   283        By similarity. 
ACT_SITE   301   301        Proton donor (By similarity). 
MOD_RES   31    31        Phosphothreonine. 
MOD_RES   35    35        Phosphoserine. 
Sequence information
Length: 350 AA [This is the length of the unprocessed precursor] Molecular weight: 38831 Da [This is the MW of the unprocessed precursor] CRC64: 5E934D00E8A9BB13 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSKKPIVLKL GKDAFGDQAW GELEKIADVI TIPESTTREQ FLREVKDPQN KLSQVQVITR 

        70         80         90        100        110        120 
TARSVKNTGR FDEELALALP SSVVAVCHTG AGYDQIDVEP FKKRHIQVAN VPDLVSNATA 

       130        140        150        160        170        180 
DTHVFLLLGA LRNFGIGNRR LIEGNWPEAG PACGSPFGYD PEGKTVGILG LGRIGRCILE 

       190        200        210        220        230        240 
RLKPFGFENF IYHNRHQLPS EEEHGCEYVG FEEFLKRSDI VSVNVPLNHN THHLINAETI 

       250        260        270        280        290        300 
EKMKDGVVIV NTARGAVIDE QAMTDALRSG KIRSAGLDVF EYEPKISKEL LSMSQVLGLP 

       310        320        330        340        350 
HMGTHSVETR KKMEELVVEN AKNVILTGKV LTIVPELQNE DWPNESKPLV 

P53839 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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BLAST logo BLAST submission on ExPASy/SIB
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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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