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P13863 (CDK1_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:CDK1
Synonyms:CDC2
OrganismGallus gallus (Chicken) [Reference proteome]
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus

Protein attributes

Sequence length303 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.

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

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

Enzyme regulation

Thr-14 and Tyr-15 are phosphorylated maximally during G2 phase, but dephosphorylated abruptly at the G2/M transition. Phosphorylation at Thr-14 and Tyr-15 inactivates the enzyme. During M phase it is also phosphorylated on Thr-161. Finally during G1 phase it is phosphorylated on Ser-277.

Subunit structure

Forms a stable but non-covalent complex with a regulatory subunit and with a cyclin. Interacts with catalytically active CCNB1 and RALBP1 during mitosis to form an endocytotic complex during interphase.

Subcellular location

Nucleus By similarity. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity.

Post-translational modification

Phosphorylation at Tyr-15 by WEE1 and WEE2 inhibits the protein kinase activity and acts negative regulator of entry into mitosis (G2 to M transition) By similarity.

Sequence similarities

Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily.

Contains 1 protein kinase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 303303Cyclin-dependent kinase 1
PRO_0000085728

Regions

Domain4 – 287284Protein kinase
Nucleotide binding10 – 189ATP By similarity

Sites

Active site1281Proton acceptor By similarity
Binding site331ATP By similarity

Amino acid modifications

Modified residue141Phosphothreonine
Modified residue151Phosphotyrosine; by WEE1 and WEE2
Modified residue1611Phosphothreonine; by CAK By similarity
Modified residue2771Phosphoserine

Sequences

Sequence LengthMass (Da)Tools
P13863 [UniParc].

Last modified January 1, 1990. Version 1.
Checksum: 976740ECC4741D69

FASTA30334,688
        10         20         30         40         50         60 
MEDYTKIEKI GEGTYGVVYK GRHKTTGQVV AMKKIRLESE EEGVPSTAIR EISLLKELHH 

        70         80         90        100        110        120 
PNIVCLQDVL MQDARLYLIF EFLSMDLKKY LDTIPSGQYL DRSRVKSYLY QILQGIVFCH 

       130        140        150        160        170        180 
SRRVLHRDLK PQNLLIDDKG VIKLADFGLA RAFGIPVRVY THEVVTLWYR SPEVLLGSAL 

       190        200        210        220        230        240 
YSTPVDIWSI GTIFAELATK KPLFHGDSEI DQLFRIFRAL GTPNNDVWPD VESLQDYKNT 

       250        260        270        280        290        300 
FPKWKPGSLG THVQNLDEDG LDLLSKMLIY DPAKRISGKM ALNHPYFDDL DKSTLPANLI 


KKF 

« Hide

References

[1]"Structure and developmental expression of the chicken CDC2 kinase."
Krek W., Nigg E.A.
EMBO J. 8:3071-3078(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Differential phosphorylation of vertebrate p34cdc2 kinase at the G1/S and G2/M transitions of the cell cycle: identification of major phosphorylation sites."
Krek W., Nigg E.A.
EMBO J. 10:305-316(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X16881 mRNA. Translation: CAA34764.1.
PIRS06011.
RefSeqNP_990645.1. NM_205314.1.
UniGeneGga.726.

3D structure databases

ProteinModelPortalP13863.
SMRP13863. Positions 1-292.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid676512. 1 interaction.
STRING9031.ENSGALP00000004867.

Proteomic databases

PaxDbP13863.
PRIDEP13863.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID396252.
KEGGgga:396252.

Organism-specific databases

CTD983.

Phylogenomic databases

eggNOGCOG0515.
HOVERGENHBG014652.
InParanoidP13863.
KOK02087.
PhylomeDBP13863.

Enzyme and pathway databases

BRENDA2.7.11.22. 1306.
ReactomeREACT_115612. DNA replication and repair.

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

NextBio20816304.
PROP13863.

Entry information

Entry nameCDK1_CHICK
AccessionPrimary (citable) accession number: P13863
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: April 16, 2014
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families