| Casein kinase II regulatory subunit | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 structure of ck2 beta subunit crystallized in the presence of a p21waf1 peptide | |||||||||
| Identifiers | |||||||||
| Symbol | CK_II_beta | ||||||||
| Pfam | PF01214 | ||||||||
| InterPro | IPR000704 | ||||||||
| PROSITE | PDOC00845 | ||||||||
| SCOP2 | 1qf8 / SCOPe / SUPFAM | ||||||||
| |||||||||
Casein kinase II subunit beta is a protein that in humans is encoded by the CSNK2B gene.[5][6] It is a ubiquitous protein kinase which regulates metabolic pathways, signal transduction, transcription, translation, and replication. The enzyme localizes to the endoplasmic reticulum and the Golgi apparatus.[7]
Casein kinase, a ubiquitous, well-conserved protein kinase involved in cell metabolism and differentiation, is characterised by its preference for Serine or Threonine in acidic stretches of amino acids. The enzyme is a tetramer of 2 alpha- and 2 beta-subunits.[8][9] 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').[10] 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.[10] The beta subunit is a highly conserved protein of about 25kDa that contains, in its central section, a cysteine-rich motif, CX(n)C, that could be involved in binding a metal such as zinc.[11] 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.[10]
- ^ a b c ENSG00000204435, ENSG00000232960, ENSG00000206406, ENSG00000224774, ENSG00000230700, ENSG00000224398 GRCh38: Ensembl release 89: ENSG00000228875, ENSG00000204435, ENSG00000232960, ENSG00000206406, ENSG00000224774, ENSG00000230700, ENSG00000224398 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000024387 – Ensembl, May 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ Yang-Feng TL, Teitz T, Cheung MC, Kan YW, Canaani D (March 1991). "Assignment of the human casein kinase II beta-subunit gene to 6p12----p21". Genomics. 8 (4): 741–2. doi:10.1016/0888-7543(90)90266-W. PMID 2276748.
- ^ Mucher G, Becker J, Knapp M, Buttner R, Moser M, Rudnik-Schoneborn S, Somlo S, Germino G, Onuchic L, Avner E, Guay-Woodford L, Zerres K (April 1998). "Fine mapping of the autosomal recessive polycystic kidney disease locus (PKHD1) and the genes MUT, RDS, CSNK2 beta, and GSTA1 at 6p21.1-p12". Genomics. 48 (1): 40–5. doi:10.1006/geno.1997.5145. PMID 9503014.
- ^ "Entrez Gene: CSNK2B casein kinase 2, beta polypeptide".
- ^ Jakobi R, Voss H, Pyerin W (July 1989). "Human phosvitin/casein kinase type II. Molecular cloning and sequencing of full-length cDNA encoding subunit beta". Eur. J. Biochem. 183 (1): 227–33. doi:10.1111/j.1432-1033.1989.tb14917.x. PMID 2666134.
- ^ Voss H, Wirkner U, Jakobi R, Hewitt NA, Schwager C, Zimmermann J, Ansorge W, Pyerin W (July 1991). "Structure of the gene encoding human casein kinase II subunit beta". J. Biol. Chem. 266 (21): 13706–11. doi:10.1016/S0021-9258(18)92756-0. PMID 1856204.
- ^ a b c Bidwai AP, Reed JC, Glover CV (May 1995). "Cloning and disruption of CKB1, the gene encoding the 38-kDa beta subunit of Saccharomyces cerevisiae casein kinase II (CKII). Deletion of CKII regulatory subunits elicits a salt-sensitive phenotype". J. Biol. Chem. 270 (18): 10395–404. doi:10.1074/jbc.270.18.10395. PMID 7737972.
- ^ Reed JC, Bidwai AP, Glover CV (July 1994). "Cloning and disruption of CKB2, the gene encoding the 32-kDa regulatory beta'-subunit of Saccharomyces cerevisiae casein kinase II". J. Biol. Chem. 269 (27): 18192–200. doi:10.1016/S0021-9258(17)32434-1. PMID 8027080.