CK2α2 or casein kinase II alpha 2 is a member of the CK2 family of Ser/Thr protein kinases. CK2a2 plays a fundamental role in cell function and is involved in DNA replication, regulation of basal and inducible transcription, translation and control of metabolism. CK2α2 prefers utilization of acidic proteins such as caseins as substrates. The CK2a2 holoenzyme is a tetramer composed of an alpha chain, an alpha′ and two beta chains. The alpha and alpha′ chains contain the catalytic site. CK2α2 is also a component of CK2-SPT16-SSRP1 complex comprised of SSRP1, SUPT16H, CSNK2A1, CSNK2A2 and CSNK2B. This complex associates following UV irradiation. CK2a2 act as a candidate gene for inherited abnormalities of sperm morphogenesis.
Protein kinase casein kinase II (Ck2) is a cyclic-AMP and calcium-independent serine-threonine kinase that is composed of two catalytic subunits (alpha and alpha') and two regulatory beta-subunits. Ck2 is not a casein kinase in vivo, but over 100 substrates are
Phosphorylation of the human p53 protein at Ser-392 has been shown to be responsive to UV but not gamma irradiation. Here we describe identification and purification of a mammalian UV-activated protein kinase complex that phosphorylates Ser-392 of p53 in vitro.
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