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CSNK2A2

From Wikipedia, the free encyclopedia

CSNK2A2
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesCSNK2A2, CK2A2, CSNK2A1, CK2alpha', casein kinase 2 alpha 2
External IDsOMIM: 115442; MGI: 88547; HomoloGene: 20444; GeneCards: CSNK2A2; OMA:CSNK2A2 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001896

NM_009974

RefSeq (protein)

NP_001887

NP_034104

Location (UCSC)Chr 16: 58.16 – 58.2 MbChr 8: 96.17 – 96.22 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Casein kinase II subunit alpha' is an enzyme that in humans is encoded by the CSNK2A2 gene.[5][6]

Interactions

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CSNK2A2 has been shown to interact with over 160 different substrates.[7]

CSNK2A2 has been shown to interact with:

References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000070770Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000046707Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Lozeman FJ, Litchfield DW, Piening C, Takio K, Walsh KA, Krebs EG (Jan 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.
  6. ^ Yang-Feng TL, Zheng K, Kopatz I, Naiman T, Canaani D (Feb 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.
  7. ^ Faust M, Montenarh M (September 2000). "Subcellular localization of protein kinase CK2. A key to its function?". Cell Tissue Res. 301 (3): 329–40. doi:10.1007/s004410000256. PMID 10994779. S2CID 11394831.
  8. ^ a b c d 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.
  9. ^ 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. doi:10.1016/S1016-8478(23)13390-5. PMID 9571630.
  10. ^ 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.
  11. ^ 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.
  12. ^ a b Skjerpen CS, Nilsen Trine, Wesche Jørgen, Olsnes Sjur (Aug 2002). "Binding of FGF-1 variants to protein kinase CK2 correlates with mitogenicity". EMBO J. 21 (15). England: 4058–69. doi:10.1093/emboj/cdf402. ISSN 0261-4189. PMC 126148. PMID 12145206.
  13. ^ Li D, Dobrowolska G, Krebs EG (June 1996). "The physical association of casein kinase 2 with nucleolin". J. Biol. Chem. 271 (26): 15662–8. doi:10.1074/jbc.271.26.15662. PMID 8663258.
  14. ^ 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.
  15. ^ 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. S2CID 1093672.
  16. ^ 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.
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Further reading

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