Cyclin-dependent kinase 1 - Gallus gallus (Chicken)

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P13863 (CDK1_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 107. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Gallus gallus (Chicken) [Reference proteome]

Taxonomic identifier

9031 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus

Protein attributes

Sequence length	303 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Cytoplasm › cytoskeleton › centrosome 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.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis
Cellular component	Cytoplasm Cytoskeleton Nucleus
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell division Inferred from electronic annotation. Source: UniProtKB-KW double-strand break repair via homologous recombination Traceable author statement. Source: Reactome mitosis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW microtubule organizing center Inferred from electronic annotation. Source: UniProtKB-SubCell nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW RNA polymerase II carboxy-terminal domain kinase activity Inferred from electronic annotation. Source: EC cyclin-dependent protein serine/threonine kinase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 303

303

Cyclin-dependent kinase 1

PRO_0000085728

Regions

Domain

4 – 287

284

Protein kinase

Nucleotide binding

10 – 18

ATP By similarity

Sites

Active site

128

Proton acceptor By similarity

Binding site

ATP By similarity

Amino acid modifications

Modified residue

Phosphothreonine

Modified residue

Phosphotyrosine; by WEE1 and WEE2

Modified residue

161

Phosphothreonine; by CAK By similarity

Modified residue

277

Phosphoserine

Sequences

Sequence

Length

Mass (Da)

Tools

P13863 [UniParc].

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

303

34,688

        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

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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.
IPI	IPI00604039.
PIR	S06011.
RefSeq	NP_990645.1. NM_205314.1.
UniGene	Gga.726.
3D structure databases
ProteinModelPortal	P13863.
SMR	P13863. Positions 1-292.
ModBase	Search...
Protein-protein interaction databases
STRING	9031.ENSGALP00000004867.
Proteomic databases
PaxDb	P13863.
PRIDE	P13863.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	396252.
KEGG	gga:396252.
Organism-specific databases
CTD	983.
Phylogenomic databases
eggNOG	COG0515.
HOVERGEN	HBG014652.
InParanoid	P13863.
KO	K02087.
OrthoDB	EOG41NTMH.
Enzyme and pathway databases
BRENDA	2.7.11.22. 1306.
Reactome	REACT_115612. DNA replication and repair.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR002290. Ser/Thr_dual-sp_kinase_dom. IPR008271. Ser/Thr_kinase_AS. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	20816304.

Entry information

Entry name

CDK1_CHICK

Accession

Primary (citable) accession number: P13863

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	January 1, 1990
Last modified:	May 1, 2013
This is version 107 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Other

Entry information

Relevant documents