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| http://www.biopax.org/relea... | |
| http://www.biopax.org/relea... |
Cyclin-dependent kinase 1
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| http://www.biopax.org/relea... |
CDK1_MOUSE
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| http://www.biopax.org/relea... | |
| http://www.biopax.org/relea... |
2.7.11.22,
2.7.11.23,
CDK1,
Cell division control protein 2 homolog,
Cell division protein kinase 1,
p34 protein kinase
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| http://www.biopax.org/relea... |
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. CATALYTIC ACTIVITY: 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: 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. Interacts with FANCC (By similarity). SUBCELLULAR LOCATION: Nucleus (By similarity). PTM: 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). Phosphorylation at Tyr-15 by WEE1 takes place during mitosis. Phosphorylation at Tyr-15 by WEE2 during oogenesis is required to maintain meiotic arrest in oocytes during the germinal vesicle (GV) stage, a long period of quiescence at dictyate prophase I, leading to prevent meiotic reentry. Phosphorylation by WEE2 is also required for metaphase II exit during egg activation to ensure exit from meiosis in oocytes and promote pronuclear formation. SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily. SIMILARITY: Contains 1 protein kinase domain. GENE SYNONYMS: Cdc2 Cdc2a. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
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