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Protein

Cyclin-dependent kinase 1

Gene

CDC28

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei40 – 401ATPPROSITE-ProRule annotation
Active sitei136 – 1361Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi14 – 229ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. cyclin-dependent protein serine/threonine kinase activity Source: SGD
  3. histone binding Source: SGD
  4. protein serine/threonine kinase activity Source: SGD
  5. RNA polymerase II core binding Source: SGD

GO - Biological processi

  1. 7-methylguanosine mRNA capping Source: SGD
  2. cell division Source: UniProtKB-KW
  3. chromatin remodeling Source: SGD
  4. meiotic DNA double-strand break processing Source: SGD
  5. mitotic nuclear division Source: UniProtKB-KW
  6. negative regulation of double-strand break repair via nonhomologous end joining Source: SGD
  7. negative regulation of meiotic cell cycle Source: SGD
  8. negative regulation of mitotic cell cycle Source: SGD
  9. negative regulation of sister chromatid cohesion Source: SGD
  10. negative regulation of transcription, DNA-templated Source: SGD
  11. peptidyl-serine phosphorylation Source: SGD
  12. phosphorylation of RNA polymerase II C-terminal domain Source: SGD
  13. positive regulation of meiotic cell cycle Source: SGD
  14. positive regulation of mitotic cell cycle Source: SGD
  15. positive regulation of nuclear cell cycle DNA replication Source: SGD
  16. positive regulation of spindle pole body separation Source: SGD
  17. positive regulation of transcription, DNA-templated Source: SGD
  18. positive regulation of transcription from RNA polymerase II promoter Source: SGD
  19. positive regulation of triglyceride catabolic process Source: SGD
  20. regulation of budding cell apical bud growth Source: SGD
  21. regulation of double-strand break repair via homologous recombination Source: SGD
  22. regulation of filamentous growth Source: SGD
  23. regulation of protein localization Source: SGD
  24. synaptonemal complex assembly Source: SGD
  25. vesicle-mediated transport Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-29110-MONOMER.
BRENDAi2.7.11.22. 984.
ReactomeiREACT_245912. CDK-mediated phosphorylation and removal of Cdc6.

Names & Taxonomyi

Protein namesi
Recommended name:
Cyclin-dependent kinase 1 (EC:2.7.11.22)
Short name:
CDK1
Alternative name(s):
Cell division control protein 28
Cell division protein kinase 1
Gene namesi
Name:CDC28
Synonyms:CDK1, HSL5, SRM5
Ordered Locus Names:YBR160W
ORF Names:YBR1211
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome II

Organism-specific databases

CYGDiYBR160w.
SGDiS000000364. CDC28.

Subcellular locationi

GO - Cellular componenti

  1. cellular bud neck Source: SGD
  2. cyclin-dependent protein kinase holoenzyme complex Source: SGD
  3. cytoplasm Source: SGD
  4. endoplasmic reticulum Source: SGD
  5. nucleus Source: SGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 298297Cyclin-dependent kinase 1PRO_0000085722Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei19 – 191Phosphotyrosine1 Publication
Modified residuei169 – 1691Phosphothreonine; alternate1 Publication
Modified residuei169 – 1691Phosphothreonine; by CAK; alternateBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP00546.
PaxDbiP00546.
PeptideAtlasiP00546.

Expressioni

Gene expression databases

GenevestigatoriP00546.

Interactioni

Subunit structurei

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

Binary interactionsi

WithEntry#Exp.IntActNotes
P030703EBI-4253,EBI-617698From a different organism.
CAK1P435683EBI-4253,EBI-3953
CDC6P091192EBI-4253,EBI-4447
CKS1P204867EBI-4253,EBI-4746
CLB5P302833EBI-4253,EBI-4538
CLN1P204376EBI-4253,EBI-4479
CLN3P133655EBI-4253,EBI-4490

Protein-protein interaction databases

BioGridi32859. 578 interactions.
DIPiDIP-1039N.
IntActiP00546. 71 interactions.
MINTiMINT-569037.
STRINGi4932.YBR160W.

Structurei

3D structure databases

ProteinModelPortaliP00546.
SMRiP00546. Positions 17-297.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini8 – 295288Protein kinasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00780000121869.
InParanoidiP00546.
KOiK04563.
OMAiFAEMVMR.
OrthoDBiEOG7K3TWD.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00546-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSGELANYKR LEKVGEGTYG VVYKALDLRP GQGQRVVALK KIRLESEDEG
60 70 80 90 100
VPSTAIREIS LLKELKDDNI VRLYDIVHSD AHKLYLVFEF LDLDLKRYME
110 120 130 140 150
GIPKDQPLGA DIVKKFMMQL CKGIAYCHSH RILHRDLKPQ NLLINKDGNL
160 170 180 190 200
KLGDFGLARA FGVPLRAYTH EIVTLWYRAP EVLLGGKQYS TGVDTWSIGC
210 220 230 240 250
IFAEMCNRKP IFSGDSEIDQ IFKIFRVLGT PNEAIWPDIV YLPDFKPSFP
260 270 280 290
QWRRKDLSQV VPSLDPRGID LLDKLLAYDP INRISARRAA IHPYFQES
Length:298
Mass (Da):34,061
Last modified:July 21, 1986 - v1
Checksum:i57A7A2B97A90DC6C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X00257 Genomic DNA. Translation: CAA25065.1.
Z36029 Genomic DNA. Translation: CAA85119.1.
X80224 Genomic DNA. Translation: CAA56509.1.
BK006936 Genomic DNA. Translation: DAA07275.1.
PIRiA00657. TVBY8.
RefSeqiNP_009718.3. NM_001178508.3.

Genome annotation databases

EnsemblFungiiYBR160W; YBR160W; YBR160W.
GeneIDi852457.
KEGGisce:YBR160W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X00257 Genomic DNA. Translation: CAA25065.1.
Z36029 Genomic DNA. Translation: CAA85119.1.
X80224 Genomic DNA. Translation: CAA56509.1.
BK006936 Genomic DNA. Translation: DAA07275.1.
PIRiA00657. TVBY8.
RefSeqiNP_009718.3. NM_001178508.3.

3D structure databases

ProteinModelPortaliP00546.
SMRiP00546. Positions 17-297.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32859. 578 interactions.
DIPiDIP-1039N.
IntActiP00546. 71 interactions.
MINTiMINT-569037.
STRINGi4932.YBR160W.

Chemistry

BindingDBiP00546.
ChEMBLiCHEMBL5213.

Proteomic databases

MaxQBiP00546.
PaxDbiP00546.
PeptideAtlasiP00546.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYBR160W; YBR160W; YBR160W.
GeneIDi852457.
KEGGisce:YBR160W.

Organism-specific databases

CYGDiYBR160w.
SGDiS000000364. CDC28.

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00780000121869.
InParanoidiP00546.
KOiK04563.
OMAiFAEMVMR.
OrthoDBiEOG7K3TWD.

Enzyme and pathway databases

BioCyciYEAST:G3O-29110-MONOMER.
BRENDAi2.7.11.22. 984.
ReactomeiREACT_245912. CDK-mediated phosphorylation and removal of Cdc6.

Miscellaneous databases

NextBioi971387.

Gene expression databases

GenevestigatoriP00546.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  6. 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. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCDK1_YEAST
AccessioniPrimary (citable) accession number: P00546
Secondary accession number(s): D6VQF5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: February 4, 2015
This is version 167 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 6670 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome II
    Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.