ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q04458


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

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name YM00_YEAST
Primary accession number Q04458
Secondary accession numbers None
Integrated into Swiss-Prot on November 1, 1997
Sequence was last modified on November 1, 1997 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 65)
Name and origin of the protein
Protein name Putative aldehyde dehydrogenase-like protein YMR110C
Synonym EC 1.2.1.-
Gene name
OrderedLocusNames: YMR110C
ORFNames: YM9718.09C
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 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).
[2]
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).
[3]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-111, 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).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-111, 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-111, 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
Z49702; CAA89746.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S54571; S54571.
RefSeq NP_013828.1; -.
3D structure databases
HSSP P11883; 1AD3. [HSSP ENTRY / PDB]
ModBase Q04458.
Protein-protein interaction databases
DIP DIP:4437N; -.
IntAct Q04458; -.
Organism-specific databases
CYGD YMR110c; -.
SGD S000004716; HFD1.
Yeast-GFP YMR110C.
Gene expression databases
GermOnline YMR110C; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005768; Cellular component: endosome (inferred from direct assay from SGD).
GO:0031307; Cellular component: integral to mitochondrial outer membrane (inferred from direct assay from SGD).
GO:0005811; Cellular component: lipid particle (inferred from direct assay from SGD).
GO:0004030; Molecular function: aldehyde dehydrogenase [NAD(P)+] activity (inferred from electronic annotation from InterPro).
GO:0042802; Molecular function: identical protein binding (inferred from physical interaction from IntAct).
GO:0006081; Biological process: cellular aldehyde metabolic process (inferred from electronic annotation from InterPro).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR016160; Ald_DHase_CS.
IPR016162; Ald_DHase_N.
IPR012394; Ald_DHase_NAD(P).
IPR015590; Aldehyde_DHase.
Graphical view of domain structure.
Gene3D G3DSA:3.40.605.10; Aldehyde_dehydrogenase_N; 1.
PANTHER PTHR11699; Aldehyde_dehyd; 1.
PTHR11699:SF15; ALDH; 1.
Pfam PF00171; Aldedh; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF036492; ALDH; 1.
PROSITE PS00070; ALDEHYDE_DEHYDR_CYS; FALSE_NEG.
PS00687; ALDEHYDE_DEHYDR_GLU; 1.
ProtoNet Q04458.
Proteomic databases
PeptideAtlas Q04458; -.
Genome annotation databases
Ensembl YMR110C; Saccharomyces cerevisiae. [Contig view]
GeneID 855137; -.
GenomeReviews Z71257_GR; YMR110C.
KEGG sce:YMR110C; -.
NMPDR fig|4932.3.peg.4876; -.
Phylogenomic databases
HOGENOM Q04458; -.
Other
LinkHub Q04458; -.
NextBio 978519; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Oxidoreductase; Phosphoprotein.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   532  532     Putative aldehyde dehydrogenase-like protein YMR110C. PRO_0000056597
ACT_SITE   236   236        By similarity. 
ACT_SITE   273   273        By similarity. 
MOD_RES   111   111        Phosphoserine. 
Sequence information
Length: 532 AA [This is the length of the unprocessed precursor] Molecular weight: 59979 Da [This is the MW of the unprocessed precursor] CRC64: 6CAF4BFCF963AF88 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSNDGSKILN YTPVSKIDEI VEISRNFFFE KQLKLSHENN PRKKDLEFRQ LQLKKLYYAV 

        70         80         90        100        110        120 
KDHEEELIDA MYKDFHRNKI ESVLNETTKL MNDILHLIEI LPKLIKPRRV SDSSPPFMFG 

       130        140        150        160        170        180 
KTIVEKISRG SVLIIAPFNF PLLLAFAPLA AALAAGNTIV LKPSELTPHT AVVMENLLTT 

       190        200        210        220        230        240 
AGFPDGLIQV VQGAIDETTR LLDCGKFDLI FYTGSPRVGS IVAEKAAKSL TPCVLELGGK 

       250        260        270        280        290        300 
SPTFITENFK ASNIKIALKR IFFGAFGNSG QICVSPDYLL VHKSIYPKVI KECESVLNEF 

       310        320        330        340        350        360 
YPSFDEQTDF TRMIHEPAYK KAVASINSTN GSKIVPSKIS INSDTEDLCL VPPTIVYNIG 

       370        380        390        400        410        420 
WDDPLMKQEN FAPVLPIIEY EDLDETINKI IEEHDTPLVQ YIFSDSQTEI NRILTRLRSG 

       430        440        450        460        470        480 
DCVVGDTVIH VGITDAPFGG IGTSGYGNYG GYYGFNTFSH ERTIFKQPYW NDFTLFMRYP 

       490        500        510        520        530 
PNSAQKEKLV RFAMERKPWF DRNGNNKWGL RQYFSLSAAV ILISTIYAHC SS 

Q04458 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ca flag CBR Canada Mirror sites: Australia  Brazil  China  Korea  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!