Anti-CSNK2A2 antibody

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Catalytic subunit of a constitutively active serine/threonine-protein kinase complex that phosphorylates a large number of substrates containing acidic residues C-terminal to the phosphorylated serine or threonine (PubMed : 11239457, PubMed : 11704824, PubMed : 16193064, PubMed : 30898438). Regulates numerous cellular processes, such as cell cycle progression, apoptosis and transcription, as well as viral infection (PubMed : 11704824, PubMed : 16193064, PubMed : 30898438). May act as a regulatory node which integrates and coordinates numerous signals leading to an appropriate cellular response (PubMed : 12631575, PubMed : 19387551, PubMed : 19387552). During mitosis, functions as a component of the p53/TP53-dependent spindle assembly checkpoint (SAC) that maintains cyclin-B-CDK1 activity and G2 arrest in response to spindle damage (PubMed : 12631575, PubMed : 19387551, PubMed : 19387552). Also required for p53/TP53-mediated apoptosis, phosphorylating 'Ser-392' of p53/TP53 following UV irradiation (PubMed : 11239457). Phosphorylates a number of DNA repair proteins in response to DNA damage, such as MDC1, RAD9A, RAD51 and HTATSF1, promoting their recruitment to DNA damage sites (PubMed : 20545769, PubMed : 21482717, PubMed : 22325354, PubMed : 26811421, PubMed : 30898438, PubMed : 35597237). Can also negatively regulate apoptosis (PubMed : 19387551, PubMed : 19387552). Phosphorylates the caspases CASP9 and CASP2 and the apoptotic regulator NOL3 (PubMed : 12631575, PubMed : 19387551, PubMed : 19387552). Phosphorylation protects CASP9 from cleavage and activation by CASP8, and inhibits the dimerization of CASP2 and activation of CASP8 (PubMed : 12631575, PubMed : 19387551, PubMed : 19387552). Regulates transcription by direct phosphorylation of RNA polymerases I, II, III and IV (PubMed : 12631575, PubMed : 19387551, PubMed : 19387552). Also phosphorylates and regulates numerous transcription factors including NF-kappa-B, STAT1, CREB1, IRF1, IRF2, ATF1, SRF, MAX, JUN, FOS, MYC and MYB (PubMed : 12631575, PubMed : 19387551, PubMed : 19387552). Phosphorylates Hsp90 and its co-chaperones FKBP4 and CDC37, which is essential for chaperone function (PubMed : 19387550). Regulates Wnt signaling by phosphorylating CTNNB1 and the transcription factor LEF1 (PubMed : 19387549). Acts as an ectokinase that phosphorylates several extracellular proteins (PubMed : 12631575, PubMed : 19387551, PubMed : 19387552). During viral infection, phosphorylates various proteins involved in the viral life cycles of EBV, HSV, HBV, HCV, HIV, CMV and HPV (PubMed : 12631575, PubMed : 19387551, PubMed : 19387552). May phosphorylate histone H2A on 'Ser-1' (PubMed : 38334665).