Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P04551 (CDK1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 149. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
EC=2.7.11.23
Alternative name(s):
Cell division control protein 2
Cell division protein kinase 1
p34 protein kinase
Gene names
Name:cdc2
Synonyms:cdk1, swo2
ORF Names:pi002, SPBC11B10.09
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length297 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays a key role in the control of the eukaryotic cell cycle. It is required for entry into S-phase and mitosis. When complexed with cig2, plays a role in G1-S phase transition. When activated and complexed with the cyclin cdc13, it leads to the onset of mitosis. p34 is a component of the kinase complex that phosphorylates the repetitive C-terminus of RNA polymerase II. Involved in cell cycle arrest induced by defective RNA splicing. Required for phosphorylation of dis1 to ensure accurate chromosome segregation and for the DNA damage checkpoint. Ref.8 Ref.10 Ref.12 Ref.13

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

ATP + [DNA-directed RNA polymerase] = ADP + [DNA-directed RNA polymerase] phosphate.

Enzyme regulation

Phosphorylation at Thr-14 or Tyr-15 inactivates the enzyme, while phosphorylation at Thr-167 activates it By similarity.

Subunit structure

Forms a stable but non-covalent complex with a regulatory subunit suc1 and with the cyclin cdc13. Also associates with cdc37 and cig2.

Subcellular location

Cytoplasm Ref.15.

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
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG2/M transition of mitotic cell cycle

Inferred from direct assay PubMed 958201. Source: PomBase

cellular response to nitrogen starvation

Inferred from mutant phenotype PubMed 19366728. Source: PomBase

mitosis

Inferred from electronic annotation. Source: UniProtKB-KW

mitotic DNA replication checkpoint

Traceable author statement PubMed 8355807. Source: PomBase

mitotic G2 DNA damage checkpoint

Traceable author statement PubMed 1549179. Source: PomBase

negative regulation of G0 to G1 transition

Inferred from mutant phenotype PubMed 19366728. Source: PomBase

negative regulation of induction of conjugation with cellular fusion

Inferred from experiment PubMed 18059475. Source: PomBase

positive regulation of G1/S transition of mitotic cell cycle

Inferred from mutant phenotype PubMed 7254352. Source: PomBase

positive regulation of G2/M transition of mitotic cell cycle

Inferred from mutant phenotype PubMed 7254352. Source: PomBase

protein phosphorylation

Inferred from direct assay PubMed 1756737Ref.4. Source: PomBase

regulation of cell size

Non-traceable author statement. Source: PomBase

traversing start control point of mitotic cell cycle

Non-traceable author statement. Source: PomBase

   Cellular_componentcyclin-dependent protein kinase holoenzyme complex

Inferred from direct assay Ref.4. Source: PomBase

cytosol

Inferred from direct assay Ref.15. Source: PomBase

nucleus

Inferred from direct assay PubMed 2569363. Source: PomBase

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

RNA polymerase II carboxy-terminal domain kinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

cyclin-dependent protein kinase activity

Inferred from direct assay Ref.4. Source: PomBase

cyclin-dependent protein serine/threonine kinase activity

Inferred from genetic interaction PubMed 2569363. Source: PomBase

protein kinase activity

Inferred from direct assay PubMed 11937031PubMed 1756737PubMed 2569363. Source: PomBase

protein serine/threonine kinase activity

Inferred from direct assay PubMed 10485849PubMed 10921876PubMed 11486016PubMed 11937031PubMed 16950791PubMed 18059475PubMed 19666868PubMed 7957097PubMed 9242669PubMed 9490630. Source: PomBase

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 297297Cyclin-dependent kinase 1
PRO_0000085720

Regions

Domain4 – 293290Protein kinase
Nucleotide binding10 – 189ATP By similarity

Sites

Active site1341Proton acceptor By similarity
Binding site331ATP By similarity

Amino acid modifications

Modified residue141Phosphothreonine By similarity
Modified residue151Phosphotyrosine Ref.5 Ref.16
Modified residue1671Phosphothreonine Ref.16

Experimental info

Mutagenesis151Y → F: Premature entry into mitosis. Ref.7
Mutagenesis671C → F in cdc2-4W. Ref.1
Mutagenesis671C → Y in cdc2-3W. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P04551 [UniParc].

Last modified August 13, 1987. Version 1.
Checksum: D04EF14BA1492875

FASTA29734,359
        10         20         30         40         50         60 
MENYQKVEKI GEGTYGVVYK ARHKLSGRIV AMKKIRLEDE SEGVPSTAIR EISLLKEVND 

        70         80         90        100        110        120 
ENNRSNCVRL LDILHAESKL YLVFEFLDMD LKKYMDRISE TGATSLDPRL VQKFTYQLVN 

       130        140        150        160        170        180 
GVNFCHSRRI IHRDLKPQNL LIDKEGNLKL ADFGLARSFG VPLRNYTHEI VTLWYRAPEV 

       190        200        210        220        230        240 
LLGSRHYSTG VDIWSVGCIF AEMIRRSPLF PGDSEIDEIF KIFQVLGTPN EEVWPGVTLL 

       250        260        270        280        290 
QDYKSTFPRW KRMDLHKVVP NGEEDAIELL SAMLVYDPAH RISAKRALQQ NYLRDFH 

« Hide

References

« Hide 'large scale' references
[1]"Sequence of the cell division gene CDC2 from Schizosaccharomyces pombe; patterns of splicing and homology to protein kinases."
Hindley J., Phear G.A.
Gene 31:129-134(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF CYS-67.
[2]"A 38 kb segment containing the cdc2 gene from the left arm of fission yeast chromosome II: sequence analysis and characterization of the genomic DNA and cDNAs encoded on the segment."
Machida M., Yamazaki S., Kunihiro S., Tanaka T., Kushida N., Jinno K., Haikawa Y., Yamazaki J., Yamamoto S., Sekine M., Oguchi A., Nagai Y., Sakai M., Aoki K., Ogura K., Kudoh Y., Kikuchi H., Zhang M.Q., Yanagida M.
Yeast 16:71-80(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
[3]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
[4]"p13suc1 acts in the fission yeast cell division cycle as a component of the p34cdc2 protein kinase."
Brizuela L., Draetta G., Beach D.
EMBO J. 6:3507-3515(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: ASSOCIATION WITH SUC1.
[5]"Tyrosine phosphorylation of the fission yeast cdc2+ protein kinase regulates entry into mitosis."
Gould K.L., Nurse P.
Nature 342:39-45(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-15.
[6]"Two fission yeast B-type cyclins, cig2 and Cdc13, have different functions in mitosis."
Bueno A., Russell P.
Mol. Cell. Biol. 13:2286-2297(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CIG2.
[7]"Mutational analysis of the fission yeast p34cdc2 protein kinase gene."
McNeill S.A., Nurse P.
Mol. Gen. Genet. 236:415-426(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF TYR-15.
[8]"Temporal order of S phase and mitosis in fission yeast is determined by the state of the p34cdc2-mitotic B cyclin complex."
Hayles J., Fisher D., Woollard A., Nurse P.
Cell 78:813-822(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"A quantitative model for the cdc2 control of S phase and mitosis in fission yeast."
Stern B., Nurse P.
Trends Genet. 12:345-350(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[10]"Cdc2 tyrosine phosphorylation is required for the DNA damage checkpoint in fission yeast."
Rhind N., Furnari B., Russell P.
Genes Dev. 11:504-511(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[11]"The spike of S phase cyclin Cig2 expression at the G1-S border in fission yeast requires both APC and SCF ubiquitin ligases."
Yamano H., Kitamura K., Kominami K., Lehmann A., Hunt T., Toda T.
Mol. Cell 6:1377-1387(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CIG2.
[12]"Regulation of Cdc2p and Cdc13p is required for cell cycle arrest induced by defective RNA splicing in fission yeast."
Shimada M., Namikawa-Yamada C., Nakanishi M., Murakami H.
J. Biol. Chem. 280:32640-32648(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[13]"CDC2 phosphorylation of the fission yeast dis1 ensures accurate chromosome segregation."
Aoki K., Nakaseko Y., Kinoshita K., Goshima G., Yanagida M.
Curr. Biol. 16:1627-1635(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[14]"Activity of Cdc2 and its interaction with the cyclin Cdc13 depend on the molecular chaperone Cdc37 in Schizosaccharomyces pombe."
Turnbull E.L., Martin I.V., Fantes P.A.
J. Cell Sci. 119:292-302(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CDC13 AND CDC37.
[15]"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[16]"Phosphoproteome analysis of fission yeast."
Wilson-Grady J.T., Villen J., Gygi S.P.
J. Proteome Res. 7:1088-1097(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-15 AND THR-167, IDENTIFICATION BY MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M12912 Genomic DNA. Translation: AAA35293.1.
AB004534 Genomic DNA. Translation: BAA21379.1.
CU329671 Genomic DNA. Translation: CAC37513.1.
PIRTVZP2. A23359.
RefSeqNP_595629.1. NM_001021523.2.

3D structure databases

ProteinModelPortalP04551.
SMRP04551. Positions 1-295.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid276415. 80 interactions.
DIPDIP-1076N.
IntActP04551. 6 interactions.
MINTMINT-4686713.
STRING4896.SPBC11B10.09-1.

Proteomic databases

PRIDEP04551.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPBC11B10.09.1; SPBC11B10.09.1:pep; SPBC11B10.09.
GeneID2539869.
KEGGspo:SPBC11B10.09.

Organism-specific databases

PomBaseSPBC11B10.09.

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000233024.
KOK04563.
OMACHRHRII.
OrthoDBEOG7K3TWD.
PhylomeDBP04551.

Enzyme and pathway databases

BRENDA2.7.11.22. 5615.

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

NextBio20801014.

Entry information

Entry nameCDK1_SCHPO
AccessionPrimary (citable) accession number: P04551
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: April 16, 2014
This is version 149 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names