CDK2 is a member of the Cyclin-Dependent Kinase family that is ubiquitously expressed. CDK2 is a catalytic subunit of the cyclin-dependent protein kinase complex, whose activity is restricted to the G1-S phase, and essential for cell cycle G1/S phase transition. CDK2 associates with and is regulated by the regulatory subunits of the complex including Cyclin A or E, CDK inhibitor p21Cip1 (CDKN1A) and p27Kip1 (CDKN1B). CDK2 phosphorylates multiple cellular substrates including SMAD3 and FOXO1. Phosphorylation of FOXO1 leads to its inhibition.
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Apoptosis of human endothelial cells after growth factor deprivation is associated with rapid and dramatic up-regulation of cyclin A-associated cyclin-dependent kinase 2(cdk2) activity. In apoptotic cells, the C termini of the cdk inhibitors p21Cip1/Waf1 and p27Kip1 are truncated by specific
Science (New York, N.Y.), 314(5797), 294-297 (2006-10-14)
The function of cyclin-dependent kinase 2 (CDK2) is often abolished after DNA damage. The inhibition of CDK2 plays a central role in DNA damage-induced cell cycle arrest and DNA repair. However, whether CDK2 also influences the survival of cells under
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