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. Regulates numerous cellular processes, such as cell cycle progression, apoptosis and transcription, as well as viral infection. May act as a regulatory node which integrates and coordinates numerous signals leading to an appropriate cellular response. 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. Also required for p53/TP53-mediated apoptosis, phosphorylating 'Ser-392' of p53/TP53 following UV irradiation. Can also negatively regulate apoptosis. Phosphorylates the caspases CASP9 and CASP2 and the apoptotic regulator NOL3. Phosphorylation protects CASP9 from cleavage and activation by CASP8, and inhibits the dimerization of CASP2 and activation of CASP8. Regulates transcription by direct phosphorylation of RNA polymerases I, II, III and IV. Also phosphorylates and regulates numerous transcription factors including NF-kappa-B, STAT1, CREB1, IRF1, IRF2, ATF1, SRF, MAX, JUN, FOS, MYC and MYB. Phosphorylates Hsp90 and its co-chaperones FKBP4 and CDC37, which is essential for chaperone function. Regulates Wnt signaling by phosphorylating CTNNB1 and the transcription factor LEF1. Acts as an ectokinase that phosphorylates several extracellular proteins. During viral infection, phosphorylates various proteins involved in the viral life cycles of EBV, HSV, HBV, HCV, HIV, CMV and HPV. Phosphorylates PML at 'Ser-565' and primes it for ubiquitin-mediated degradation. Plays an important role in the circadian clock function by phosphorylating ARNTL/BMAL1 at 'Ser-90' which is pivotal for its interaction with CLOCK and which controls CLOCK nuclear entry. Phosphorylates CCAR2 at 'Thr-454' in gastric carcinoma tissue. Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. CK2 subfamily. Expressed in gastric carcinoma tissue and the expression gradually increases with the progression of the carcinoma (at protein level). 2 alternatively spliced human isoforms have been reported. Note: This description may include information from UniProtKB.
Protein type: CK2 family; EC 126.96.36.199; Kinase, protein; Other group; Protein kinase, Other; Protein kinase, Ser/Thr (non-receptor)
Molecular Function: ATP binding; beta-catenin binding; identical protein binding; kinase activity; protein N-terminus binding; protein phosphatase regulator activity; protein serine/threonine kinase activity; ribonucleoprotein complex binding
Biological Process: apoptotic process; cerebral cortex development; liver regeneration; negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; negative regulation of ubiquitin-dependent protein catabolic process; peptidyl-serine phosphorylation; peptidyl-threonine phosphorylation; positive regulation of cell growth; positive regulation of cell proliferation; positive regulation of protein catabolic process; positive regulation of Wnt signaling pathway; protein autophosphorylation; protein phosphorylation; regulation of chromosome separation; regulation of protein localization to plasma membrane; response to testosterone; rhythmic process; Wnt signaling pathway