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Reviewed, UniProtKB/Swiss-Prot P39951 (CDC2_RAT)

Last modified February 9, 2010. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Cell division control protein 2 homolog
    EC=2.7.11.22
    EC=2.7.11.23
Alternative name(s):
    p34 protein kinase
    Cyclin-dependent kinase 1
      Short name=CDK1
Gene names
Name: Cdc2
Synonyms: Cdc2a
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length297 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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

Phosphorylation at Thr-14 or Tyr-15 inactivates the enzyme, while phosphorylation at Thr-161 activates it By similarity.

Subunit structure

Forms a stable but non-covalent complex with a regulatory subunit and with a cyclin. Interacts with DLGAP5. Interacts with catalytically active CCNB1 and RALBP1 during mitosis to form an endocytotic complex during interphase.

Subcellular location

Nucleus Ref.3.

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 componentNucleus
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMAcetylation
Isopeptide bond
Phosphoprotein
Ubl conjugation
Gene Ontology (GO)
   Biological processG1 phase of mitotic cell cycle

Traceable author statement. Source: RGD

cell aging

Inferred from direct assay. Source: RGD

cell division

Inferred from electronic annotation. Source: UniProtKB-KW

chromosome condensation

Inferred from mutant phenotype. Source: RGD

mitosis

Inferred from electronic annotation. Source: UniProtKB-KW

organ regeneration

Inferred from mutant phenotype. Source: RGD

positive regulation of cardiac muscle cell proliferation

Inferred from mutant phenotype. Source: RGD

positive regulation of mitotic cell cycle

Inferred from mutant phenotype. Source: RGD

response to cadmium ion

Inferred from expression pattern. Source: RGD

response to drug

Inferred from expression pattern. Source: RGD

response to ethanol

Inferred from direct assay. Source: RGD

response to hydrogen peroxide

Inferred from expression pattern. Source: RGD

response to organic nitrogen

Inferred from direct assay. Source: RGD

   Cellular componentnucleus

Inferred from direct assay. Source: RGD

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

RNA polymerase II carboxy-terminal domain kinase activity

Inferred from electronic annotation. Source: EC

cyclin binding

Inferred from physical interaction. Source: RGD

cyclin-dependent protein kinase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 297297Cell division control protein 2 homolog
PRO_0000085727

Regions

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

Sites

Active site1281Proton acceptor By similarity
Binding site331ATP By similarity

Amino acid modifications

Modified residue41Phosphotyrosine By similarity
Modified residue61N6-acetyllysine By similarity
Modified residue141Phosphothreonine By similarity
Modified residue151Phosphotyrosine By similarity
Modified residue191Phosphotyrosine By similarity
Modified residue391Phosphoserine By similarity
Modified residue461Phosphoserine By similarity
Modified residue771Phosphotyrosine By similarity
Modified residue1411Phosphothreonine By similarity
Modified residue1601Phosphotyrosine By similarity
Modified residue1611Phosphothreonine By similarity
Modified residue1781Phosphoserine By similarity
Modified residue1811Phosphotyrosine By similarity
Modified residue2221Phosphothreonine By similarity
Modified residue2331Phosphoserine By similarity
Modified residue2481Phosphoserine By similarity
Cross-link89Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Sequences

Sequence LengthMass (Da)Tools
P39951-1 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 73695017E127178A

FASTA29734,135
        10         20         30         40         50         60 
MEDYIKIEKI GEGTYGVVYK GRHRTTGQIV AMKKIRLESE EEGVPSTAIR EISLLKELRH 

        70         80         90        100        110        120 
PNIVSLQDVL MQDSRLYLIF EFLSMDLKKY LDSIPPGQFM DSSLVKSYLY QILQGIVFCH 

       130        140        150        160        170        180 
SRRVLHRDLK PQNLLIDDKG TIKLADFGLA RAFGIPIRVY THEVVTLWYR SPEVLLGSAR 

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

       250        260        270        280        290 
FPKWKPGSLA SHVKNLDENG LDLLSKMLVY DPAKRISGKM ALKHPYFDDL DNQIKKM 

« Hide

References

« Hide 'large scale' references
[1]Kanaoka Y., Nojima H., Okayama H.
Submitted (JUL-1991) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Thymus.
[3]"The cdc2 kinase is a nuclear protein that is essential for mitosis in mammalian cells."
Riabowol K., Draetta G., Brizuela L., Vandre D., Beach D.
Cell 57:393-401(1989) [PubMed: 2541912] [Abstract]
Cited for: SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X60767 mRNA. Translation: CAA43177.1.
BC091549 mRNA. Translation: AAH91549.1.
IPIIPI00190390.
PIRS24913.
RefSeqNP_062169.1.
UniGeneRn.6934

3D structure databases

SMRP39951. Positions 1-294.
ModBaseSearch...

Protein-protein interaction databases

IntActP39951. 3 interactions.
STRINGP39951.

PTM databases

PhosphoSiteP39951.

Genome annotation databases

EnsemblENSRNOT00000000783; ENSRNOP00000000783; ENSRNOG00000000632; Rattus norvegicus. [Genome view]
GeneID54237.
KEGGrno:54237.
UCSCNM_019296. rat.

Organism-specific databases

CTD54237.
RGD2319. Cdc2a.

Phylogenomic databases

eggNOGroNOG07497.
HOVERGENP39951.
InParanoidP39951.
OMAMLIYDPA.
OrthoDBEOG95QKZV.
PhylomeDBP39951.

Enzyme and pathway databases

BRENDA2.7.11.22. 248.
2.7.11.23. 248.

Gene expression databases

ArrayExpressP39951.
GenevestigatorP39951.
GermOnlineENSRNOG00000000632. Rattus norvegicus.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR017442. Se/Thr_prot_kinase-like_dom.
IPR008271. Ser/Thr_prot_kinase_AS.
IPR002290. Ser/Thr_prot_kinase_dom.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
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

NextBio610684.

Entry information

Entry nameCDC2_RAT
AccessionPrimary (citable) accession number: P39951
Secondary accession number(s): Q5BJB4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: February 9, 2010
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

SIMILARITY comments

Index of protein domains and families

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