Casein kinase II subunit alpha is an enzyme that in humans is encoded by the CSNK2A1gene.[1][2]
Casein kinase II is a serine/threonine protein kinase that phosphorylates acidic proteins such as casein. The kinase exists as a tetramer and is composed of an alpha, an alpha-prime, and two beta subunits. The alpha subunits contain the catalytic activity while the beta subunits undergo autophosphorylation. The protein encoded by this gene represents the alpha subunit. While this gene is found on chromosome 20, a related transcribed pseudogene is found on chromosome 11. Three transcript variants encoding two different proteins have been found for this gene.[3]
Interactions
Casein kinase 2, alpha 1 has been shown to interact with:
↑Lozeman FJ, Litchfield DW, Piening C, Takio K, Walsh KA, Krebs EG (January 1991). "Isolation and characterization of human cDNA clones encoding the alpha and the alpha' subunits of casein kinase II". Biochemistry. 29 (36): 8436–47. doi:10.1021/bi00488a034. PMID2174700.
↑Theis-Febvre N, Filhol O, Froment C, Cazales M, Cochet C, Monsarrat B, Ducommun B, Baldin V (January 2003). "Protein kinase CK2 regulates CDC25B phosphatase activity". Oncogene. 22 (2): 220–32. doi:10.1038/sj.onc.1206107. PMID12527891.
↑Kristensen LP, Larsen MR, Højrup P, Issinger OG, Guerra B (July 2004). "Phosphorylation of the regulatory beta-subunit of protein kinase CK2 by checkpoint kinase Chk1: identification of the in vitro CK2beta phosphorylation site". FEBS Lett. 569 (1–3): 217–23. doi:10.1016/j.febslet.2004.05.069. PMID15225637.
↑Guerra B, Issinger OG, Wang JY (August 2003). "Modulation of human checkpoint kinase Chk1 by the regulatory beta-subunit of protein kinase CK2". Oncogene. 22 (32): 4933–42. doi:10.1038/sj.onc.1206721. PMID12902976.
↑ 9.09.1Bosc DG, Graham KC, Saulnier RB, Zhang C, Prober D, Gietz RD, Litchfield DW (May 2000). "Identification and characterization of CKIP-1, a novel pleckstrin homology domain-containing protein that interacts with protein kinase CK2". J. Biol. Chem. 275 (19): 14295–306. doi:10.1074/jbc.275.19.14295. PMID10799509.
↑Kim MS, Lee YT, Kim JM, Cha JY, Bae YS (February 1998). "Characterization of protein interaction among subunits of protein kinase CKII in vivo and in vitro". Mol. Cells. 8 (1): 43–8. PMID9571630.
↑Marin O, Meggio F, Sarno S, Pinna LA (June 1997). "Physical dissection of the structural elements responsible for regulatory properties and intersubunit interactions of protein kinase CK2 beta-subunit". Biochemistry. 36 (23): 7192–8. doi:10.1021/bi962885q. PMID9188720.
↑Ahn BH, Kim TH, Bae YS (October 2001). "Mapping of the interaction domain of the protein kinase CKII beta subunit with target proteins". Mol. Cells. 12 (2): 158–63. PMID11710515.
↑Kusk M, Ahmed R, Thomsen B, Bendixen C, Issinger OG, Boldyreff B (January 1999). "Interactions of protein kinase CK2beta subunit within the holoenzyme and with other proteins". Mol. Cell. Biochem. 191 (1–2): 51–8. doi:10.1023/A:1006840613986. PMID10094392.
↑Ubeda M, Habener JF (October 2003). "CHOP transcription factor phosphorylation by casein kinase 2 inhibits transcriptional activation". J. Biol. Chem. 278 (42): 40514–20. doi:10.1074/jbc.M306404200. PMID12876286.
↑Pancetti F, Bosser R, Krehan A, Pyerin W, Itarte E, Bachs O (June 1999). "Heterogeneous nuclear ribonucleoprotein A2 interacts with protein kinase CK2". Biochem. Biophys. Res. Commun. 260 (1): 17–22. doi:10.1006/bbrc.1999.0849. PMID10381337.
↑Sayed M, Kim SO, Salh BS, Issinger OG, Pelech SL (June 2000). "Stress-induced activation of protein kinase CK2 by direct interaction with p38 mitogen-activated protein kinase". J. Biol. Chem. 275 (22): 16569–73. doi:10.1074/jbc.M000312200. PMID10747897.
↑Messenger MM, Saulnier RB, Gilchrist AD, Diamond P, Gorbsky GJ, Litchfield DW (June 2002). "Interactions between protein kinase CK2 and Pin1. Evidence for phosphorylation-dependent interactions". J. Biol. Chem. 277 (25): 23054–64. doi:10.1074/jbc.M200111200. PMID11940573.
↑Miller SJ, Lou DY, Seldin DC, Lane WS, Neel BG (September 2002). "Direct identification of PTEN phosphorylation sites". FEBS Lett. 528 (1–3): 145–53. doi:10.1016/s0014-5793(02)03274-x. PMID12297295.
↑Wang D, Westerheide SD, Hanson JL, Baldwin AS (October 2000). "Tumor necrosis factor alpha-induced phosphorylation of RelA/p65 on Ser529 is controlled by casein kinase II". J. Biol. Chem. 275 (42): 32592–7. doi:10.1074/jbc.M001358200. PMID10938077.
↑Allende-Vega N, McKenzie L, Meek D (September 2008). "Transcription factor TAFII250 phosphorylates the acidic domain of Mdm2 through recruitment of protein kinase CK2". Mol. Cell. Biochem. 316 (1–2): 99–106. doi:10.1007/s11010-008-9816-3. PMID18548200.
Allende JE, Allende CC (1995). "Protein kinases. 4. Protein kinase CK2: an enzyme with multiple substrates and a puzzling regulation". FASEB J. 9 (5): 313–23. PMID7896000.
Faust M, Montenarh M (2001). "Subcellular localization of protein kinase CK2. A key to its function?". Cell Tissue Res. 301 (3): 329–40. doi:10.1007/s004410000256. PMID10994779.