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P34556 (CDK1_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 122. 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·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 homolog
Cell division protein kinase 1
p34 protein kinase
Gene names
Name:cdk-1
Synonyms:ncc-1
ORF Names:T05G5.3
OrganismCaenorhabditis elegans [Reference proteome]
Taxonomic identifier6239 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis

Protein attributes

Sequence length332 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 in higher cells for entry into S-phase and mitosis. p34 is a component of the kinase complex that phosphorylates the repetitive C-terminus of RNA polymerase II By similarity.

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

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

Enzyme regulation

Phosphorylation both activates and inactivates the enzyme depending on the site of phosphorylation. Ref.6

Subunit structure

Forms a stable but non-covalent complex with a regulatory subunit and with a cyclin. Interacts with cks-1. Ref.6

Subcellular location

Nucleus By similarity. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity.

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
Cytoskeleton
Nucleus
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell division

Inferred from mutant phenotype Ref.3. Source: UniProtKB

meiotic nuclear division

Inferred from mutant phenotype Ref.3. Source: WormBase

mitosis

Inferred from mutant phenotype Ref.3. Source: WormBase

oocyte maturation

Inferred from mutant phenotype PubMed 16421191. Source: WormBase

positive regulation of meiosis

Inferred from mutant phenotype PubMed 16421191. Source: WormBase

positive regulation of meiotic cell cycle

Inferred from mutant phenotype Ref.3. Source: UniProtKB

positive regulation of protein serine/threonine kinase activity

Inferred from mutant phenotype PubMed 19879842. Source: WormBase

protein phosphorylation

Inferred from direct assay PubMed 19829076. Source: WormBase

   Cellular_componentcytoplasm

Inferred from direct assay Ref.3. Source: WormBase

microtubule organizing center

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay Ref.3. Source: WormBase

   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 serine/threonine kinase activity

Inferred from direct assay PubMed 19829076. Source: WormBase

protein kinase binding

Inferred from physical interaction Ref.6. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 332332Cyclin-dependent kinase 1
PRO_0000085738

Regions

Domain22 – 312291Protein kinase
Nucleotide binding28 – 369ATP By similarity

Sites

Active site1461Proton acceptor By similarity
Binding site511ATP By similarity

Amino acid modifications

Modified residue321Phosphothreonine By similarity
Modified residue331Phosphotyrosine By similarity

Experimental info

Mutagenesis1731I → F: No affect on cks-1 binding. Ref.6
Sequence conflict1761R → P in AAC60520. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P34556 [UniParc].

Last modified February 1, 1994. Version 1.
Checksum: B6297E92949C8206

FASTA33238,295
        10         20         30         40         50         60 
MDPIREGEVA HEGDSVYTLN DFTKLEKIGE GTYGVVYKGK NRRTNAMVAM KKIRLESEDE 

        70         80         90        100        110        120 
GVPSTAVREI SLLKELQHPN VVGLEAVIMQ ENRLFLIFEF LSFDLKRYMD QLGKDEYLPL 

       130        140        150        160        170        180 
ETLKSYTFQI LQAMCFCHQR RVIHRDLKPQ NLLVDNNGAI KLADFGLARA IGIPIRVYTH 

       190        200        210        220        230        240 
EVVTLWYRAP EILMGAQRYS MGVDMWSIGC IFAEMATKKP LFQGDSEIDE LFRIFRVLGT 

       250        260        270        280        290        300 
PTELEWNGVE SLPDYKATFP KWRENFLRDK FYDKKTGKHL LDDTAFSLLE GLLIYDPSLR 

       310        320        330 
LNAKKALVHP YFDNMDTSKL PAGNYRGELE LF 

« Hide

References

« Hide 'large scale' references
[1]"Complete nucleotide sequence of a cDNA coding for a p34-cdc2-like protein from Caenorhabiditis elegans."
Ferraz C., Thierry-Mieg D., Le Peuch C.J.
Submitted (SEP-1992) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Bristol N2.
[2]"The identification of a Caenorhabditis elegans homolog of p34cdc2 kinase."
Mori H., Palmer R.E., Sternberg P.W.
Mol. Gen. Genet. 245:781-786(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"The Caenorhabditis elegans gene ncc-1 encodes a cdc2-related kinase required for M phase in meiotic and mitotic cell divisions, but not for S phase."
Boxem M., Srinivasan D.G., van den Heuvel S.
Development 126:2227-2239(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Bristol N2.
[4]"2.2 Mb of contiguous nucleotide sequence from chromosome III of C. elegans."
Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J., Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M., Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L. expand/collapse author list , Gardner A., Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M., Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C., Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A., Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M., Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K., Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L., Wilkinson-Sproat J., Wohldman P.
Nature 368:32-38(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Bristol N2.
[5]"Genome sequence of the nematode C. elegans: a platform for investigating biology."
The C. elegans sequencing consortium
Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Bristol N2.
[6]"The conserved kinases CDK-1, GSK-3, KIN-19, and MBK-2 promote OMA-1 destruction to regulate the oocyte-to-embryo transition in C. elegans."
Shirayama M., Soto M.C., Ishidate T., Kim S., Nakamura K., Bei Y., van den Heuvel S., Mello C.C.
Curr. Biol. 16:47-55(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CKS-1, ENZYME REGULATION, MUTAGENESIS OF ILE-173.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X68384 mRNA. Translation: CAA48455.1.
S75262 mRNA. Translation: AAC60520.1.
AF129109 mRNA. Translation: AAD37119.1.
Z27079 Genomic DNA. Translation: CAA81590.1.
PIRS41003.
RefSeqNP_001022747.1. NM_001027576.3.
UniGeneCel.23379.

3D structure databases

ProteinModelPortalP34556.
SMRP34556. Positions 18-315.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid41569. 3 interactions.
DIPDIP-26477N.
IntActP34556. 4 interactions.
MINTMINT-1082928.
STRING6239.T05G5.3.3.

Proteomic databases

PaxDbP34556.
PRIDEP34556.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaT05G5.3.1; T05G5.3.1; T05G5.3.
T05G5.3.2; T05G5.3.2; T05G5.3.
GeneID176374.
KEGGcel:CELE_T05G5.3.
UCSCT05G5.3.1. c. elegans.

Organism-specific databases

CTD176374.
WormBaseT05G5.3; CE00315; WBGene00000405; cdk-1.

Phylogenomic databases

eggNOGCOG0515.
InParanoidP34556.
KOK02087.
OMANIIHADY.
PhylomeDBP34556.

Enzyme and pathway databases

BRENDA2.7.11.22. 1045.
SignaLinkP34556.

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

NextBio892302.
PROP34556.

Entry information

Entry nameCDK1_CAEEL
AccessionPrimary (citable) accession number: P34556
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: April 16, 2014
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Caenorhabditis elegans

Caenorhabditis elegans: entries, gene names and cross-references to WormBase