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 P27515


[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 URK1_YEAST
Primary accession number P27515
Secondary accession numbers None
Integrated into Swiss-Prot on August 1, 1992
Sequence was last modified on August 1, 1992 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 71)
Name and origin of the protein
Protein name Uridine kinase
Synonyms EC 2.7.1.48
Uridine monophosphokinase
Gene name
Name: URK1
OrderedLocusNames: YNR012W
ORFNames: N2050
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 FUNCTION.
STRAIN=ATCC 28383 / FL100 / VTT C-80102;
DOI=10.1093/nar/18.17.5279; PubMed=2169608 [NCBI, ExPASy, EBI, Israel, Japan]
Kern L.;
"The URK1 gene of Saccharomyces cerevisiae encoding uridine kinase.";
Nucleic Acids Res. 18:5279-5279(1990).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 96604 / S288c / FY1679;
DOI=10.1002/yea.320101013; PubMed=7900425 [NCBI, ExPASy, EBI, Israel, Japan]
Verhasselt P., Aert R., Voet M., Volckaert G.;
"Twelve open reading frames revealed in the 23.6 kb segment flanking the centromere on the Saccharomyces cerevisiae chromosome XIV right arm.";
Yeast 10:1355-1361(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 96604 / S288c / FY1679;
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).
[4]
FUNCTION.
DOI=10.1007/s002940050482; PubMed=10501935 [NCBI, ExPASy, EBI, Israel, Japan]
Kurtz J.-E., Exinger F., Erbs P., Jund R.;
"New insights into the pyrimidine salvage pathway of Saccharomyces cerevisiae: requirement of six genes for cytidine metabolism.";
Curr. Genet. 36:130-136(1999).
[5]
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).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, 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).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17, 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).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, 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).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-276 AND SER-278, 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
X53998; CAA37946.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X77395; CAA54580.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z71627; CAA96289.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S29374; S29374.
RefSeq NP_014409.1; -.
3D structure databases
HSSP Q26998; 1BD3. [HSSP ENTRY / PDB]
ModBase P27515.
Protein-protein interaction databases
DIP DIP:1720N; -.
IntAct P27515; -.
Organism-specific databases
CYGD YNR012w; -.
SGD S000005295; URK1.
Yeast-GFP YNR012W.
Gene expression databases
ArrayExpress P27515; -.
GermOnline YNR012W; 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:0005524; Molecular function: ATP binding (inferred from electronic annotation from InterPro).
GO:0042802; Molecular function: identical protein binding (inferred from physical interaction from IntAct).
GO:0016773; Molecular function: phosphotransferase activity, alcohol group as acceptor (inferred from electronic annotation from InterPro).
GO:0004849; Molecular function: uridine kinase activity (inferred from electronic annotation from EC).
GO:0008655; Biological process: pyrimidine salvage (inferred from genetic interaction from SGD).
QuickGo view.
Family and domain databases
InterPro IPR006083; PRK_URK.
IPR000764; Uridine_kin.
Graphical view of domain structure.
PANTHER PTHR10285:SF6; Uridine_kin; 1.
Pfam PF00485; PRK; 1.
Pfam graphical view of domain structure.
PRINTS PR00988; URIDINKINASE.
TIGRFAMs TIGR00235; udk; 1.
BLOCKS P27515.
ProtoNet P27515.
Proteomic databases
PeptideAtlas P27515; -.
Genome annotation databases
Ensembl YNR012W; Saccharomyces cerevisiae. [Contig view]
GeneID 855746; -.
GenomeReviews Y13139_GR; YNR012W.
KEGG sce:YNR012W; -.
NMPDR fig|4932.3.peg.5489; -.
Phylogenomic databases
HOGENOM P27515; -.
Other
LinkHub P27515; -.
NextBio 980151; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
ATP-binding; Complete proteome; Cytoplasm; Kinase; Nucleotide-binding; Nucleus; Phosphoprotein; Transferase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   501  501     Uridine kinase. PRO_0000164462
NP_BIND   63    70  8     ATP (Potential). 
MOD_RES   14    14        Phosphoserine. 
MOD_RES   17    17        Phosphoserine. 
MOD_RES   276   276        Phosphoserine. 
MOD_RES   278   278        Phosphoserine. 
Sequence information
Length: 501 AA [This is the length of the unprocessed precursor] Molecular weight: 56296 Da [This is the MW of the unprocessed precursor] CRC64: 30A0592899BCD040 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSHRIAPSKE RSSSFISILD DETRDTLKAN AVMDGEVDVK KTKGKSSRYI PPWTTPYIIG 

        70         80         90        100        110        120 
IGGASGSGKT SVAAKIVSSI NVPWTVLISL DNFYNPLGPE DRARAFKNEY DFDEPNAINL 

       130        140        150        160        170        180 
DLAYKCILNL KEGKRTNIPV YSFVHHNRVP DKNIVIYGAS VVVIEGIYAL YDRRLLDLMD 

       190        200        210        220        230        240 
LKIYVDADLD VCLARRLSRD IVSRGRDLDG CIQQWEKFVK PNAVKFVKPT MKNADAIIPS 

       250        260        270        280        290        300 
MSDNATAVNL IINHIKSKLE LKSNEHLREL IKLGSSPSQD VLNRNIIHEL PPTNQVLSLH 

       310        320        330        340        350        360 
TMLLNKNLNC ADFVFYFDRL ATILLSWALD DIPVAHTNII TPGEHTMENV IACQFDQVTA 

       370        380        390        400        410        420 
VNIIRSGDCF MKSLRKTIPN ITIGKLLIQS DSQTGEPQLH CEFLPPNIEK FGKVFLMEGQ 

       430        440        450        460        470        480 
IISGAAMIMA IQVLLDHGID LEKISVVVYL ATEVGIRRIL NAFDNKVNIF AGMIISREKL 

       490        500 
QNHQYKWALT RFFDSKYFGC D 

P27515 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 au flag APAF Australia Mirror sites: Brazil  Canada  China  Korea  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!