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P00546 (CDK1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 161. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cyclin-dependent kinase 1

Short name=CDK1
EC=2.7.11.22
Alternative name(s):
Cell division control protein 28
Cell division protein kinase 1
Gene names
Name:CDC28
Synonyms:CDK1, HSL5, SRM5
Ordered Locus Names:YBR160W
ORF Names:YBR1211
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length298 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This protein is essential for the completion of the start, the controlling event, in the cell cycle. More than 200 substrates have been identified.

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulation

Phosphorylation at Thr-18 or Tyr-19 inactivates the enzyme, while phosphorylation at Thr-169 activates it By similarity.

Subunit structure

Forms a stable but non-covalent complex with the CKS1 protein and with a cyclin.

Miscellaneous

Present with 6670 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Mitosis
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_process7-methylguanosine mRNA capping

Inferred from mutant phenotype PubMed 22689984. Source: SGD

chromatin remodeling

Inferred from mutant phenotype PubMed 20855529. Source: SGD

meiotic DNA double-strand break processing

Inferred from genetic interaction PubMed 20150422. Source: SGD

mitotic nuclear division

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of double-strand break repair via nonhomologous end joining

Inferred from mutant phenotype PubMed 19699692. Source: SGD

negative regulation of meiotic cell cycle

Inferred from mutant phenotype PubMed 12081645. Source: SGD

negative regulation of mitotic cell cycle

Inferred from direct assay PubMed 10074450. Source: SGD

negative regulation of sister chromatid cohesion

Inferred from mutant phenotype PubMed 21549314. Source: SGD

negative regulation of transcription, DNA-templated

Inferred from direct assay PubMed 14993267. Source: SGD

phosphorylation of RNA polymerase II C-terminal domain

Inferred from direct assay PubMed 22689984. Source: SGD

positive regulation of meiotic cell cycle

Inferred from direct assay PubMed 16814718. Source: SGD

positive regulation of mitotic cell cycle

Inferred from mutant phenotype PubMed 2165600PubMed 7002718. Source: SGD

positive regulation of nuclear cell cycle DNA replication

Inferred from direct assay PubMed 14747467. Source: SGD

positive regulation of spindle pole body separation

Inferred from mutant phenotype PubMed 16688214PubMed 8887667. Source: SGD

positive regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 22689984. Source: SGD

positive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 1652372. Source: SGD

positive regulation of triglyceride catabolic process

Inferred from mutant phenotype PubMed 19150427. Source: SGD

regulation of budding cell apical bud growth

Inferred from mutant phenotype PubMed 17417630. Source: SGD

regulation of double-strand break repair via homologous recombination

Inferred from mutant phenotype PubMed 15496928. Source: SGD

regulation of filamentous growth

Inferred from mutant phenotype PubMed 9891070. Source: SGD

regulation of protein localization

Inferred from mutant phenotype PubMed 19188495PubMed 20702586. Source: SGD

synaptonemal complex assembly

Inferred from mutant phenotype PubMed 20825495. Source: SGD

vesicle-mediated transport

Inferred from mutant phenotype PubMed 22767578. Source: SGD

   Cellular_componentcellular bud neck

Inferred from direct assay PubMed 12554645. Source: SGD

cyclin-dependent protein kinase holoenzyme complex

Inferred from direct assay PubMed 1849458PubMed 2142620. Source: SGD

cytoplasm

Inferred from direct assay PubMed 3312233. Source: SGD

endoplasmic reticulum

Inferred from direct assay PubMed 17560371. Source: SGD

nucleus

Inferred from direct assay PubMed 14685274. Source: SGD

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

RNA polymerase II core binding

Inferred from direct assay PubMed 22689984. Source: SGD

cyclin-dependent protein serine/threonine kinase activity

Inferred from direct assay PubMed 2142620. Source: SGD

histone binding

Inferred from direct assay PubMed 20855529. Source: SGD

protein binding

Inferred from physical interaction PubMed 10688190PubMed 11283351PubMed 11805826PubMed 14690591PubMed 16429126PubMed 20489023PubMed 23217712PubMed 23267104PubMed 7815540. Source: IntAct

protein serine/threonine kinase activity

Inferred from direct assay PubMed 22689984PubMed 24319056. Source: SGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.10
Chain2 – 298297Cyclin-dependent kinase 1
PRO_0000085722

Regions

Domain8 – 295288Protein kinase
Nucleotide binding14 – 229ATP By similarity

Sites

Active site1361Proton acceptor By similarity
Binding site401ATP By similarity

Amino acid modifications

Modified residue21N-acetylserine Ref.10
Modified residue191Phosphotyrosine Ref.9
Modified residue1691Phosphothreonine; alternate Ref.9
Modified residue1691Phosphothreonine; by CAK; alternate By similarity

Sequences

Sequence LengthMass (Da)Tools
P00546 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 57A7A2B97A90DC6C

FASTA29834,061
        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 

« Hide

References

« Hide 'large scale' references
[1]"Primary structure homology between the product of yeast cell division control gene CDC28 and vertebrate oncogenes."
Lorincz A.T., Reed S.I.
Nature 307:183-185(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Sequence analysis of a 5.6 kb fragment of chromosome II from Saccharomyces cerevisiae reveals two new open reading frames next to CDC28."
Baur S., Becker J., Li Z., Niegemann E., Wehner E., Wolter R., Brendel M.
Yeast 11:455-458(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"Complete DNA sequence of yeast chromosome II."
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. expand/collapse author list , 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.
EMBO J. 13:5795-5809(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[5]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[6]"Targets of the cyclin-dependent kinase Cdk1."
Ubersax J.A., Woodbury E.L., Quang P.N., Paraz M., Blethrow J.D., Shah K., Shokat K.M., Morgan D.O.
Nature 425:859-864(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION SUBSTRATES.
[7]"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway."
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.
Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: YAL6B.
[8]"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[9]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-19 AND THR-169, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X00257 Genomic DNA. Translation: CAA25065.1.
Z36029 Genomic DNA. Translation: CAA85119.1.
X80224 Genomic DNA. Translation: CAA56509.1.
BK006936 Genomic DNA. Translation: DAA07275.1.
PIRTVBY8. A00657.
RefSeqNP_009718.3. NM_001178508.3.

3D structure databases

ProteinModelPortalP00546.
SMRP00546. Positions 17-297.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid32859. 565 interactions.
DIPDIP-1039N.
IntActP00546. 71 interactions.
MINTMINT-569037.
STRING4932.YBR160W.

Chemistry

BindingDBP00546.
ChEMBLCHEMBL5213.

Proteomic databases

MaxQBP00546.
PaxDbP00546.
PeptideAtlasP00546.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYBR160W; YBR160W; YBR160W.
GeneID852457.
KEGGsce:YBR160W.

Organism-specific databases

CYGDYBR160w.
SGDS000000364. CDC28.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00720000108415.
KOK04563.
OMALVHRFFR.
OrthoDBEOG7K3TWD.

Enzyme and pathway databases

BioCycYEAST:G3O-29110-MONOMER.
BRENDA2.7.11.22. 984.

Gene expression databases

GenevestigatorP00546.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio971387.

Entry information

Entry nameCDK1_YEAST
AccessionPrimary (citable) accession number: P00546
Secondary accession number(s): D6VQF5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: June 11, 2014
This is version 161 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome II

Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families