CK_II_betaCasein kinase II regulatory subunit
|SMART accession number:||SM01085|
|Interpro abstract (IPR000704):|
Casein kinase, a ubiquitous well-conserved protein kinase involved in cell metabolism and differentiation, is characterised by its preference for Ser or Thr in acidic stretches of amino acids. The enzyme is a tetramer of 2 alpha- and 2 beta-subunits [(PUBMED:2666134), (PUBMED:1856204)]. However, some species (e.g., mammals) possess 2 related forms of the alpha-subunit (alpha and alpha'), while others (e.g., fungi) possess 2 related beta-subunits (beta and beta') [(PUBMED:7737972)].
The alpha-subunit is the catalytic unit and contains regions characteristic of serine/threonine protein kinases. The beta-subunit is believed to be regulatory, possessing an N-terminal auto-phosphorylation site, an internal acidic domain, and a potential metal-binding motif [(PUBMED:7737972)]. The beta subunit contains, in its central section, a cysteine-rich motif, CX(n)C, that could be involved in binding a metal such as zinc [(PUBMED:8027080)]. The mammalian beta-subunit gene promoter shares common features with those of other mammalian protein kinases and is closely related to the promoter of the regulatory subunit of cAMP-dependent protein kinase [(PUBMED:7737972)].
|GO component:||protein kinase CK2 complex (GO:0005956)|
|GO function:||protein kinase regulator activity (GO:0019887)|
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- Evolution (species in which this domain is found)
- Structure (3D structures containing this domain)
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