Casein kinase 2, alpha 1

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See also: Casein kinase 2
Casein kinase 2, alpha 1 polypeptide
Protein CSNK2A1 PDB 1jwh.png
PDB rendering based on 1jwh.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols CSNK2A1 ; CK2A1; CKII; CSNK2A3
External IDs OMIM115440 MGI88543 HomoloGene90874 ChEMBL: 3629 GeneCards: CSNK2A1 Gene
EC number 2.7.11.1
RNA expression pattern
PBB GE CSNK2A1 212072 s at tn.png
PBB GE CSNK2A1 206075 s at tn.png
PBB GE CSNK2A1 212073 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 1457 12995
Ensembl ENSG00000101266 ENSMUSG00000074698
UniProt P68400 Q60737
RefSeq (mRNA) NM_001895 NM_007788
RefSeq (protein) NP_001886 NP_031814
Location (UCSC) Chr 20:
0.46 – 0.52 Mb
Chr 2:
152.23 – 152.28 Mb
PubMed search [1] [2]

Casein kinase II subunit alpha is an enzyme that in humans is encoded by the CSNK2A1 gene.[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[edit]

Casein kinase 2, alpha 1 has been shown to interact with:

References[edit]

  1. ^ 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. PMID 2174700. 
  2. ^ Yang-Feng TL, Zheng K, Kopatz I, Naiman T, Canaani D (February 1992). "Mapping of the human casein kinase II catalytic subunit genes: two loci carrying the homologous sequences for the alpha subunit". Nucleic Acids Res 19 (25): 7125–9. doi:10.1093/nar/19.25.7125. PMC 332535. PMID 1766873. 
  3. ^ "Entrez Gene: CSNK2A1 casein kinase 2, alpha 1 polypeptide". 
  4. ^ Homma MK, Li D, Krebs EG, Yuasa Y, Homma Y (April 2002). "Association and regulation of casein kinase 2 activity by adenomatous polyposis coli protein". Proc. Natl. Acad. Sci. U.S.A. 99 (9): 5959–64. doi:10.1073/pnas.092143199. PMC 122884. PMID 11972058. 
  5. ^ a b c d e Yamaguchi Y, Wada T, Suzuki F, Takagi T, Hasegawa J, Handa H (August 1998). "Casein kinase II interacts with the bZIP domains of several transcription factors". Nucleic Acids Res. 26 (16): 3854–61. doi:10.1093/nar/26.16.3854. PMC 147779. PMID 9685505. 
  6. ^ 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. PMID 12527891. 
  7. ^ 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. PMID 15225637. 
  8. ^ 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. PMID 12902976. 
  9. ^ a b Bosc 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. PMID 10799509. 
  10. ^ 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. PMID 9571630. 
  11. ^ 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. PMID 9188720. 
  12. ^ 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. PMID 11710515. 
  13. ^ 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. PMID 10094392. 
  14. ^ 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. PMID 12876286. 
  15. ^ a b Skjerpen CS, Nilsen T, Wesche J, Olsnes S (August 2002). "Binding of FGF-1 variants to protein kinase CK2 correlates with mitogenicity". EMBO J. 21 (15): 4058–69. doi:10.1093/emboj/cdf402. PMC 126148. PMID 12145206. 
  16. ^ 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. PMID 10381337. 
  17. ^ 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. PMID 10747897. 
  18. ^ 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. PMID 11940573. 
  19. ^ 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. PMID 12297295. 
  20. ^ 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. PMID 10938077. 
  21. ^ 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. PMID 18548200. 
  22. ^ Voit R, Kuhn A, Sander EE, Grummt I (July 1995). "Activation of mammalian ribosomal gene transcription requires phosphorylation of the nucleolar transcription factor UBF". Nucleic Acids Res. 23 (14): 2593–9. doi:10.1093/nar/23.14.2593. PMC 307079. PMID 7651819. 

Further reading[edit]

  • ole-MoiYoi OK (1995). "Casein kinase II in theileriosis.". Science 267 (5199): 834–6. doi:10.1126/science.7846527. PMID 7846527. 
  • 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. PMID 7896000. 
  • 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. PMID 10994779.