Phospho-CDK2 (pY15) peptide
Description
Application Data
Description
-
Antigenic peptide from the sequence of CDK2, phosphorylated on tyrosine 15
Application Data
-
Catalogue number crb1200296 Antibody Phospho-CDK2 (pY15) peptide Antigen Peptide Phosphorylated CDK2 (pY15) peptide Protein ID UnitProtKB - P24941 Aliases Cyclin-dependent kinase 2, CDK2, CDK-2, Cell division protein kinase 2, p33 protein kinase Cross-Reactivity Human, mouse, rat Target Protein Species Human, mouse, rat Storage Stabilisers -20°C Specificity Protein Storage -20°C Citations Hughes, B., Sidorova, J., Swanger, J., Monnat, R. and Clurman, B. (2013). Essential role for Cdk2 inhibitory phosphorylation during replication stress revealed by a human Cdk2 knockin mutation. PNAS, 110(22), 8954-8959. PMID: 23671119
Ji, X., Humenik, J., Yang, D. and Liebhaber, S. (2017). PolyC-binding proteins enhance expression of the CDK2 cell cycle regulatory protein via alternative splicing. Nucleic Acids Res, 46(4), 2030-2044. PMID: 29253178
References Hughes, B., Sidorova, J., Swanger, J., Monnat, R. and Clurman, B. (2013). Essential role for Cdk2 inhibitory phosphorylation during replication stress revealed by a human Cdk2 knockin mutation. PNAS, 110(22), 8954-8959. PMID: 23671119
Ji, X., Humenik, J., Yang, D. and Liebhaber, S. (2017). PolyC-binding proteins enhance expression of the CDK2 cell cycle regulatory protein via alternative splicing. Nucleic Acids Res, 46(4), 2030-2044. PMID: 29253178
Cyclin-dependent kinases (CDKs) are regulated by positive and negative phosphorylation. T14/Y15 phosphorylation by the WEE1 and MYT1 kinases inhibits CDKs by preventing ATP binding, and these conserved phosphorylations are highly regulated during the cell cycle and by signalling pathways. WEE1 and MYT1 are opposed by cell division cycle 25 (CDC25) phosphatases, which, in mammals, comprise three related enzymes that dephosphorylate T14/Y15 to promote CDK activity.
Cdk2 inhibition is involved in DNA replication and S-phase DNA damage checkpoints. CDK2 T14/Y15 phosphorylation is not required for DNA damage-induced cell cycle arrest, but instead has roles in S-phase entry and centrosome duplication.