Casein kinase II subunit beta is a
protein that in humans is encoded by the CSNK2Bgene.[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
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]
^
abLehner B, 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. 83 (1). United States: 153–67.
doi:
10.1016/S0888-7543(03)00235-0.
ISSN0888-7543.
PMID14667819.
^
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. 36 (23). UNITED STATES: 7192–8.
doi:
10.1021/bi962885q.
ISSN0006-2960.
PMID9188720.
^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. 191 (1–2). NETHERLANDS: 51–8.
doi:
10.1023/A:1006840613986.
ISSN0300-8177.
PMID10094392.
S2CID257329.
^O'Brien KA, 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. 260 (3). UNITED STATES: 658–64.
doi:
10.1006/bbrc.1999.0892.
ISSN0006-291X.
PMID10403822.
PDBe-KB provides an overview of all the structure information available in the PDB for Human Casein kinase II subunit beta (CSNK2B)
Further reading
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.
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.
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.
Casein kinase II subunit beta is a
protein that in humans is encoded by the CSNK2Bgene.[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
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]
^
abLehner B, 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. 83 (1). United States: 153–67.
doi:
10.1016/S0888-7543(03)00235-0.
ISSN0888-7543.
PMID14667819.
^
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. 36 (23). UNITED STATES: 7192–8.
doi:
10.1021/bi962885q.
ISSN0006-2960.
PMID9188720.
^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. 191 (1–2). NETHERLANDS: 51–8.
doi:
10.1023/A:1006840613986.
ISSN0300-8177.
PMID10094392.
S2CID257329.
^O'Brien KA, 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. 260 (3). UNITED STATES: 658–64.
doi:
10.1006/bbrc.1999.0892.
ISSN0006-291X.
PMID10403822.
PDBe-KB provides an overview of all the structure information available in the PDB for Human Casein kinase II subunit beta (CSNK2B)
Further reading
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.
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.
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.