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UniProtKB/Swiss-Prot entry P00546


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

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Entry information
Entry name CDC28_YEAST
Primary accession number P00546
Secondary accession numbers None
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on July 21, 1986 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 95)
Name and origin of the protein
Protein name Cell division control protein 28
Synonym EC 2.7.11.22
Gene name
Name: CDC28
Synonyms: CDK1, HSL5, SRM5
OrderedLocusNames: YBR160W
ORFNames: YBR1211
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].
DOI=10.1038/307183a0; PubMed=6361575 [NCBI, ExPASy, EBI, Israel, Japan]
Lorincz A.T., Reed S.I.;
"Primary structure homology between the product of yeast cell division control gene CDC28 and vertebrate oncogenes.";
Nature 307:183-185(1984).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=7597849 [NCBI, ExPASy, EBI, Israel, Japan]
Baur S., Becker J., Li Z., Niegemann E., Wehner E., Wolter R., Brendel M.;
"Sequence analysis of a 5.6 kb fragment of chromosome II from Saccharomyces cerevisiae reveals two new open reading frames next to CDC28.";
Yeast 11:455-458(1995).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=7813418 [NCBI, ExPASy, EBI, Israel, Japan]
Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.;
"Complete DNA sequence of yeast chromosome II.";
EMBO J. 13:5795-5809(1994).
[4]
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).
[5]
PHOSPHORYLATION SUBSTRATES.
DOI=10.1038/nature02062; PubMed=14574415 [NCBI, ExPASy, EBI, Israel, Japan]
Ubersax J.A., Woodbury E.L., Quang P.N., Paraz M., Blethrow J.D., Shah K., Shokat K.M., Morgan D.O.;
"Targets of the cyclin-dependent kinase Cdk1.";
Nature 425:859-864(2003).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-19 AND THR-169, 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 TYR-19, 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
X00257; CAA25065.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z36029; CAA85119.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X80224; CAA56509.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A00657; TVBY8.
RefSeq NP_009718.1; -.
3D structure databases
HSSP P24941; 1P2A. [HSSP ENTRY / PDB]
ModBase P00546.
Protein-protein interaction databases
DIP DIP:1039N; -.
IntAct P00546; -.
Organism-specific databases
CYGD YBR160w; -.
SGD S000000364; CDC28.
Yeast-GFP YBR160W.
Gene expression databases
GermOnline YBR160W; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005935; Cellular component: cellular bud neck (inferred from direct assay from SGD).
GO:0000307; Cellular component: cyclin-dependent protein kinase holoenzyme complex (inferred from direct assay from SGD).
GO:0005783; Cellular component: endoplasmic reticulum (inferred from direct assay from SGD).
GO:0005634; Cellular component: nucleus (inferred from direct assay from SGD).
GO:0004693; Molecular function: cyclin-dependent protein kinase activity (inferred from direct assay from SGD).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0051447; Biological process: negative regulation of meiotic cell cycle (inferred from mutant phenotype from SGD).
GO:0045930; Biological process: negative regulation of mitotic cell cycle (inferred from direct assay from SGD).
GO:0045892; Biological process: negative regulation of transcription, DNA-dependent (inferred from direct assay from SGD).
GO:0010571; Biological process: positive regulation of DNA replication during S phase (inferred from direct assay from SGD).
GO:0051446; Biological process: positive regulation of meiotic cell cycle (inferred from direct assay from SGD).
GO:0045931; Biological process: positive regulation of mitotic cell cycle (inferred from mutant phenotype from SGD).
GO:0045893; Biological process: positive regulation of transcription, DNA-dependent (inferred from direct assay from SGD).
GO:0006468; Biological process: protein amino acid phosphorylation (inferred from direct assay from SGD).
GO:0010568; Biological process: regulation of budding cell apical growth (inferred from genetic interaction from SGD).
GO:0010569; Biological process: regulation of double-strand break repair via homologous recombination (inferred from mutant phenotype from SGD).
GO:0010570; Biological process: regulation of filamentous growth (inferred from mutant phenotype from SGD).
QuickGo view.
Family and domain databases
InterPro IPR000719; Prot_kinase_core.
IPR017441; Protein_kinase_ATP_bd_CS.
IPR017442; Se/Thr_pkinase-rel.
IPR008271; Ser_thr_pkin_AS.
IPR002290; Ser_thr_pkinase.
Graphical view of domain structure.
Pfam PF00069; Pkinase; 1.
Pfam graphical view of domain structure.
ProDom PD000001; Prot_kinase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00220; S_TKc; 1.
SMART graphical view of domain structure.
PROSITE PS00107; PROTEIN_KINASE_ATP; 1.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00108; PROTEIN_KINASE_ST; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P00546.
ProtoNet P00546.
Proteomic databases
PeptideAtlas P00546; -.
Genome annotation databases
Ensembl YBR160W; Saccharomyces cerevisiae. [Contig view]
GeneID 852457; -.
GenomeReviews Y13134_GR; YBR160W.
KEGG sce:YBR160W; -.
NMPDR fig|4932.3.peg.424; -.
Phylogenomic databases
HOGENOM P00546; -.
Other
LinkHub P00546; -.
NextBio 971387; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
ATP-binding; Cell cycle; Cell division; Complete proteome; Kinase; Mitosis; Nucleotide-binding; Phosphoprotein; Serine/threonine-protein kinase; Transferase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   298  298     Cell division control protein 28. PRO_0000085722
DOMAIN   8   295  288     Protein kinase. 
NP_BIND   14    22  9     ATP (By similarity). 
ACT_SITE   136   136        Proton acceptor (By similarity). 
BINDING   40    40        ATP (By similarity). 
MOD_RES   18    18        Phosphothreonine (By similarity). 
MOD_RES   19    19        Phosphotyrosine. 
MOD_RES   169   169        Phosphothreonine; by CAK (By similarity). 
Sequence information
Length: 298 AA [This is the length of the unprocessed precursor] Molecular weight: 34061 Da [This is the MW of the unprocessed precursor] CRC64: 57A7A2B97A90DC6C [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSGELANYKR LEKVGEGTYG VVYKALDLRP GQGQRVVALK KIRLESEDEG VPSTAIREIS 

        70         80         90        100        110        120 
LLKELKDDNI VRLYDIVHSD AHKLYLVFEF LDLDLKRYME GIPKDQPLGA DIVKKFMMQL 

       130        140        150        160        170        180 
CKGIAYCHSH RILHRDLKPQ NLLINKDGNL KLGDFGLARA FGVPLRAYTH EIVTLWYRAP 

       190        200        210        220        230        240 
EVLLGGKQYS TGVDTWSIGC IFAEMCNRKP IFSGDSEIDQ IFKIFRVLGT PNEAIWPDIV 

       250        260        270        280        290 
YLPDFKPSFP QWRRKDLSQV VPSLDPRGID LLDKLLAYDP INRISARRAA IHPYFQES 

P00546 in FASTA format

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