Reviewed, UniProtKB/Swiss-Prot P00546 (CDC28_YEAST)

Names and origin

Protein names

Recommended name:
    Cell division control protein 28
    EC=2.7.11.22

Gene names

Name:	CDC28
Synonyms:	CDK1, HSL5, SRM5
Ordered Locus Names:	YBR160W
ORF Names:	YBR1211

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	298 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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. Ref.4
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
Gene Ontology (GO)
Biological process	cell division Inferred from electronic annotation. Source: UniProtKB-KW mitosis Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of meiotic cell cycle Inferred from mutant phenotype. Source: SGD negative regulation of mitotic cell cycle Inferred from direct assay. Source: SGD negative regulation of transcription, DNA-dependent Inferred from direct assay. Source: SGD positive regulation of DNA replication during S phase Inferred from direct assay. Source: SGD positive regulation of meiotic cell cycle Inferred from direct assay. Source: SGD positive regulation of mitotic cell cycle Inferred from mutant phenotype. Source: SGD positive regulation of spindle pole body separation Inferred from mutant phenotype. Source: SGD positive regulation of transcription, DNA-dependent Inferred from direct assay. Source: SGD positive regulation of triglyceride catabolic process Inferred from genetic interaction. Source: SGD protein amino acid phosphorylation Inferred from direct assay. Source: SGD regulation of budding cell apical growth Inferred from genetic interaction. Source: SGD regulation of double-strand break repair via homologous recombination Inferred from mutant phenotype. Source: SGD regulation of filamentous growth Inferred from mutant phenotype. Source: SGD
Cellular component	cellular bud neck Inferred from direct assay. Source: SGD cyclin-dependent protein kinase holoenzyme complex Inferred from direct assay. Source: SGD endoplasmic reticulum Inferred from direct assay. Source: SGD nucleus Inferred from direct assay. Source: SGD
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW cyclin-dependent protein kinase activity Inferred from direct assay. Source: SGD protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CDC13	P32797	1	EBI-4253,EBI-4187
CKS1	P20486	1	EBI-4253,EBI-4746
CLB2	P24869	1	EBI-4253,EBI-4515
RNR2	P09938	1	EBI-4253,EBI-15240

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 298	298	Cell division control protein 28		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.6 Ref.7
	Modified residue	169	1	Phosphothreonine; by CAK By similarity

Sequences

	Sequence		Length	Mass (Da)
	P00546-1 [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: 6361575] [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: 7597849] [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: 7813418] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[4]	"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: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[5]	"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: 14574415] [Abstract] Cited for: PHOSPHORYLATION SUBSTRATES.
[6]	"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: 15665377] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-19 AND THR-169, MASS SPECTROMETRY.
[7]	"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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-19, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X00257 Genomic DNA. Translation: CAA25065.1. Z36029 Genomic DNA. Translation: CAA85119.1. X80224 Genomic DNA. Translation: CAA56509.1.
PIR	TVBY8. A00657.
RefSeq	NP_009718.1.
3D structure databases
HSSP	HSSP built from PDB template 1P2A based on UniProtKB P24941.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:1039N.
IntAct	P00546. 66 interactions.
Proteomic databases
PeptideAtlas	P00546.
PRIDE	P00546.
Genome annotation databases
Ensembl	YBR160W. Saccharomyces cerevisiae. [Contig view]
GeneID	852457.
GenomeReviews	Gene locus YBR160W in contig Y13134_GR.
KEGG	sce:YBR160W.
NMPDR	fig|4932.3.peg.424.
Organism-specific databases
CYGD	YBR160w.
SGD	S000000364. CDC28.
Yeast-GFP	Search...
Phylogenomic databases
HOGENOM	P00546.
OMA	P00546. GVPLRAY.
Enzyme and pathway databases
BRENDA	2.7.11.22. 250.
Gene expression databases
GermOnline	YBR160W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR000719. Prot_kinase_core. IPR017441. Protein_kinase_ATP_BS. IPR017442. Se/Thr_pkinase-rel. IPR008271. Ser_thr_pkin_AS. IPR002290. Ser_thr_pkinase. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
ProDom	PD000001. Prot_kinase. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	971387.

Entry information

Entry name

CDC28_YEAST

Accession

Primary (citable) accession number: P00546

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	June 16, 2009
This is version 104 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)