Casein kinase II subunit beta is a protein that in humans is encoded by the CSNK2Bgene.[5][6]
This gene encodes the beta subunit of casein kinase II, 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 cellmetabolism 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 genepromoter 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]
^"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. PMID2276748.
^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. PMID9503014.
^ abLehner, Ben; Semple Jennifer I; Brown Stephanie E; Counsell Damian; Campbell R Duncan; Sanderson Christopher M (January 2004). "Analysis of a high-throughput yeast two-hybrid system and its use to predict the function of intracellular proteins encoded within the human MHC class III region". Genomics. United States. 83 (1): 153–67. doi:10.1016/S0888-7543(03)00235-0. ISSN0888-7543. PMID14667819.
^ abKim, M S; Lee Y T; Kim J M; Cha J Y; Bae Y S (February 1998). "Characterization of protein interaction among subunits of protein kinase CKII in vivo and in vitro". Mol. Cells. KOREA. 8 (1): 43–8. ISSN1016-8478. PMID9571630.
^ abMarin, O; Meggio F; Sarno S; Pinna L A (June 1997). "Physical dissection of the structural elements responsible for regulatory properties and intersubunit interactions of protein kinase CK2 beta-subunit". Biochemistry. UNITED STATES. 36 (23): 7192–8. doi:10.1021/bi962885q. ISSN0006-2960. PMID9188720.
^ abcAhn, B H; Kim T H; Bae Y S (October 2001). "Mapping of the interaction domain of the protein kinase CKII beta subunit with target proteins". Mol. Cells. Korea (South). 12 (2): 158–63. ISSN1016-8478. PMID11710515.
^Kusk, M; Ahmed R; Thomsen B; Bendixen C; Issinger O G; Boldyreff B (January 1999). "Interactions of protein kinase CK2beta subunit within the holoenzyme and with other proteins". Mol. Cell. Biochem. NETHERLANDS. 191 (1–2): 51–8. doi:10.1023/A:1006840613986. ISSN0300-8177. PMID10094392. S2CID257329.
^Kim, J M; Cha J Y; Marshak D R; Bae Y S (September 1996). "Interaction of the beta subunit of casein kinase II with the ribosomal protein L5". Biochem. Biophys. Res. Commun. UNITED STATES. 226 (1): 180–6. doi:10.1006/bbrc.1996.1330. ISSN0006-291X. PMID8806611.
^O'Brien, K A; Lemke S J; Cocke K S; Rao R N; Beckmann R P (July 1999). "Casein kinase 2 binds to and phosphorylates BRCA1". Biochem. Biophys. Res. Commun. UNITED STATES. 260 (3): 658–64. doi:10.1006/bbrc.1999.0892. ISSN0006-291X. PMID10403822.
Schubert U, Schneider T, Henklein P, et al. (1992). "Human-immunodeficiency-virus-type-1-encoded Vpu protein is phosphorylated by casein kinase II". Eur. J. Biochem. 204 (2): 875–83. doi:10.1111/j.1432-1033.1992.tb16707.x. PMID1541298.
Teitz T, Eli D, Penner M, et al. (1990). "Expression of the cDNA for the beta subunit of human casein kinase II confers partial UV resistance on xeroderma pigmentosum cells". Mutat. Res. 236 (1): 85–97. doi:10.1016/0921-8777(90)90036-5. PMID1694965.
Heller-Harrison RA, Meisner H, Czech MP (1990). "Cloning and characterization of a cDNA encoding the beta subunit of human casein kinase II". Biochemistry. 28 (23): 9053–8. doi:10.1021/bi00449a014. PMID2513884.
Jakobi R, Voss H, Pyerin W (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. PMID2666134.
Szebeni A, Herrera JE, Olson MO (1995). "Interaction of nucleolar protein B23 with peptides related to nuclear localization signals". Biochemistry. 34 (25): 8037–42. doi:10.1021/bi00025a009. PMID7794916.
Arnold SF, Obourn JD, Jaffe H, Notides AC (1995). "Serine 167 is the major estradiol-induced phosphorylation site on the human estrogen receptor". Mol. Endocrinol. 8 (9): 1208–14. doi:10.1210/me.8.9.1208. PMID7838153.
Pyerin W (1994). "Human casein kinase II: structures, genes, expression and requirement in cell growth stimulation". Adv. Enzyme Regul. 34: 225–46. doi:10.1016/0065-2571(94)90018-3. PMID7942276.
Schubert U, Henklein P, Boldyreff B, et al. (1994). "The human immunodeficiency virus type 1 encoded Vpu protein is phosphorylated by casein kinase-2 (CK-2) at positions Ser52 and Ser56 within a predicted alpha-helix-turn-alpha-helix-motif". J. Mol. Biol. 236 (1): 16–25. doi:10.1006/jmbi.1994.1114. PMID8107101.
Friborg J, Ladha A, Göttlinger H, et al. (1996). "Functional analysis of the phosphorylation sites on the human immunodeficiency virus type 1 Vpu protein". J. Acquir. Immune Defic. Syndr. Hum. Retrovirol. 8 (1): 10–22. doi:10.1097/00042560-199501000-00004. PMID8548340.
PDB gallery
1jwh: Crystal Structure of Human Protein Kinase CK2 Holoenzyme
1qf8: TRUNCATED FORM OF CASEIN KINASE II BETA SUBUNIT (2-182) FROM HOMO SAPIENS
1rqf: Structure of CK2 beta subunit crystallized in the presence of a p21WAF1 peptide