P00546 (CDK1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	298 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Cell cycle Cell division Mitosis
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	7-methylguanosine mRNA capping Inferred from mutant phenotype PubMed 22689984. Source: SGD cell division Inferred from electronic annotation. Source: UniProtKB-KW chromatin remodeling Inferred from mutant phenotype PubMed 20855529. Source: SGD meiotic DNA double-strand break processing Inferred from genetic interaction PubMed 20150422. Source: SGD mitosis 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-dependent 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 DNA replication involved in S phase Inferred from direct assay PubMed 14747467. 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 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 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_component	cellular 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 endoplasmic reticulum Inferred from direct assay PubMed 17560371. Source: SGD nucleus Inferred from direct assay PubMed 14685274. Source: SGD
Molecular_function	ATP 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
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CAK1	P43568	3	EBI-4253,EBI-3953
CDC6	P09119	2	EBI-4253,EBI-4447
CKS1	P20486	8	EBI-4253,EBI-4746
CLB2	P24869	3	EBI-4253,EBI-4515
CLB5	P30283	3	EBI-4253,EBI-4538
CLN1	P20437	7	EBI-4253,EBI-4479
CLN3	P13365	4	EBI-4253,EBI-4490

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 298	298	Cyclin-dependent kinase 1		PRO_0000085722
Regions
	Domain	8 – 295	288	Protein kinase
	Nucleotide binding	14 – 22	9	ATP By similarity
Sites
	Active site	136	1	Proton acceptor By similarity
	Binding site	40	1	ATP By similarity
Amino acid modifications
	Modified residue	18	1	Phosphothreonine By similarity
	Modified residue	19	1	Phosphotyrosine Ref.7 Ref.8
	Modified residue	169	1	Phosphothreonine; by CAK By similarity

Sequences

	Sequence		Length	Mass (Da)
	P00546 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: 57A7A2B97A90DC6C	FASTA	298	34,061
	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

References

	« Hide 'large scale' referencesShow '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. , 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]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-19 AND THR-169, MASS SPECTROMETRY. Strain: YAL6B.
[8]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-19, MASS SPECTROMETRY.
+	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.
PIR	TVBY8. A00657.
RefSeq	NP_009718.3. NM_001178508.3.
3D structure databases
ProteinModelPortal	P00546.
SMR	P00546. Positions 17-297.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-1039N.
IntAct	P00546. 70 interactions.
MINT	MINT-569037.
STRING	4932.YBR160W.
Proteomic databases
PaxDb	P00546.
PeptideAtlas	P00546.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YBR160W; YBR160W; YBR160W.
GeneID	852457.
KEGG	sce:YBR160W. sce:YBR163W.
Organism-specific databases
CYGD	YBR160w.
SGD	S000000364. CDC28.
Phylogenomic databases
eggNOG	COG0515.
GeneTree	ENSGT00690000101791.
KO	K04563.
OMA	YLEVAAS.
OrthoDB	EOG4J40RS.
Enzyme and pathway databases
BRENDA	2.7.11.22. 984.
Gene expression databases
Genevestigator	P00546.
GermOnline	YBR160W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR002290. Ser/Thr_dual-sp_kinase_dom. IPR008271. Ser/Thr_kinase_AS. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	P00546.
ChEMBL	CHEMBL5213.
NextBio	971387.

Entry information

Entry name

CDK1_YEAST

Accession

Primary (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:	May 1, 2013
This is version 149 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program