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Reviewed, UniProtKB/Swiss-Prot P00546 (CDC28_YEAST)

Last modified June 16, 2009. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended 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
OrganismSaccharomyces cerevisiae (Baker's yeast) [Complete proteome]
Taxonomic identifier4932 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length298 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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. 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 processCell cycle
Cell division
Mitosis
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processcell 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 componentcellular 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 functionATP 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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 298298Cell division control protein 28
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 residue181Phosphothreonine By similarity
Modified residue191Phosphotyrosine Ref.6 Ref.7
Modified residue1691Phosphothreonine; by CAK By similarity

Sequences

Sequence LengthMass (Da)Tools
P00546-1 [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: 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. 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: 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

X00257 Genomic DNA. Translation: CAA25065.1.
Z36029 Genomic DNA. Translation: CAA85119.1.
X80224 Genomic DNA. Translation: CAA56509.1.
PIRTVBY8. A00657.
RefSeqNP_009718.1.

3D structure databases

HSSPHSSP built from PDB template 1P2A based on UniProtKB P24941.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:1039N.
IntActP00546. 66 interactions.

Proteomic databases

PeptideAtlasP00546.
PRIDEP00546.

Genome annotation databases

EnsemblYBR160W. Saccharomyces cerevisiae. [Contig view]
GeneID852457.
GenomeReviewsGene locus YBR160W in contig Y13134_GR.
KEGGsce:YBR160W.
NMPDRfig|4932.3.peg.424.

Organism-specific databases

CYGDYBR160w.
SGDS000000364. CDC28.
Yeast-GFPSearch...

Phylogenomic databases

HOGENOMP00546.
OMAP00546. GVPLRAY.

Enzyme and pathway databases

BRENDA2.7.11.22. 250.

Gene expression databases

GermOnlineYBR160W. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR000719. Prot_kinase_core.
IPR017441. Protein_kinase_ATP_BS.
IPR017442. Se/Thr_pkinase-rel.
IPR008271. Ser_thr_pkin_AS.
IPR002290. Ser_thr_pkinase.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
ProDomPD000001. Prot_kinase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio971387.

Entry information

Entry nameCDC28_YEAST
AccessionPrimary (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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Yeast

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

Yeast chromosome II

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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents