EEF2K

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Eukaryotic elongation factor-2 kinase
Identifiers
Symbols EEF2K ; HSU93850; MGC45041; eEF-2K
External IDs Template:OMIM5 Template:MGI HomoloGene7299
RNA expression pattern
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

Eukaryotic elongation factor-2 kinase, also known as EEF2K, is a human gene.[1]

This gene encodes a highly conserved protein kinase in the calmodulin-mediated signaling pathway that links activation of cell surface receptors to cell division. This kinase is involved in the regulation of protein synthesis. It phosphorylates eukaryotic elongation factor 2 (EEF2) and thus inhibits the EEF2 function. The activity of this kinase is increased in many cancers and may be a valid target for anti-cancer treatment.[1]

References

  1. 1.0 1.1 "Entrez Gene: EEF2K eukaryotic elongation factor-2 kinase".

Further reading

  • Nairn AC, Palfrey HC (1988). "Identification of the major Mr 100,000 substrate for calmodulin-dependent protein kinase III in mammalian cells as elongation factor-2". J. Biol. Chem. 262 (36): 17299–303. PMID 3693353.
  • Redpath NT, Price NT, Severinov KV, Proud CG (1993). "Regulation of elongation factor-2 by multisite phosphorylation". Eur. J. Biochem. 213 (2): 689–99. PMID 8386634.
  • Ryazanov AG, Ward MD, Mendola CE; et al. (1997). "Identification of a new class of protein kinases represented by eukaryotic elongation factor-2 kinase". Proc. Natl. Acad. Sci. U.S.A. 94 (10): 4884–9. PMID 9144159.
  • Pavur KS, Petrov AN, Ryazanov AG (2000). "Mapping the functional domains of elongation factor-2 kinase". Biochemistry. 39 (40): 12216–24. PMID 11015200.
  • Diggle TA, Subkhankulova T, Lilley KS; et al. (2001). "Phosphorylation of elongation factor-2 kinase on serine 499 by cAMP-dependent protein kinase induces Ca2+/calmodulin-independent activity". Biochem. J. 353 (Pt 3): 621–6. PMID 11171059.
  • Knebel A, Morrice N, Cohen P (2001). "A novel method to identify protein kinase substrates: eEF2 kinase is phosphorylated and inhibited by SAPK4/p38delta". EMBO J. 20 (16): 4360–9. doi:10.1093/emboj/20.16.4360. PMID 11500363.
  • Wang X, Li W, Williams M; et al. (2001). "Regulation of elongation factor 2 kinase by p90(RSK1) and p70 S6 kinase". EMBO J. 20 (16): 4370–9. doi:10.1093/emboj/20.16.4370. PMID 11500364.
  • Arora S, Yang JM, Craft J, Hait W (2002). "Detection of anti-elongation factor 2 kinase (calmodulin-dependent protein kinase III) antibodies in patients with systemic lupus erythematosus". Biochem. Biophys. Res. Commun. 293 (3): 1073–6. doi:10.1016/S0006-291X(02)00324-8. PMID 12051769.
  • Wistow G, Bernstein SL, Wyatt MK; et al. (2002). "Expressed sequence tag analysis of human RPE/choroid for the NEIBank Project: over 6000 non-redundant transcripts, novel genes and splice variants". Mol. Vis. 8: 205–20. PMID 12107410.
  • Knebel A, Haydon CE, Morrice N, Cohen P (2002). "Stress-induced regulation of eukaryotic elongation factor 2 kinase by SB 203580-sensitive and -insensitive pathways". Biochem. J. 367 (Pt 2): 525–32. doi:10.1042/BJ20020916. PMID 12171600.
  • Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
  • Ota T, Suzuki Y, Nishikawa T; et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
  • Browne GJ, Finn SG, Proud CG (2004). "Stimulation of the AMP-activated protein kinase leads to activation of eukaryotic elongation factor 2 kinase and to its phosphorylation at a novel site, serine 398". J. Biol. Chem. 279 (13): 12220–31. doi:10.1074/jbc.M309773200. PMID 14709557.
  • Browne GJ, Proud CG (2004). "A novel mTOR-regulated phosphorylation site in elongation factor 2 kinase modulates the activity of the kinase and its binding to calmodulin". Mol. Cell. Biol. 24 (7): 2986–97. PMID 15024086.
  • Brill LM, Salomon AR, Ficarro SB; et al. (2004). "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry". Anal. Chem. 76 (10): 2763–72. doi:10.1021/ac035352d. PMID 15144186.
  • Li X, Alafuzoff I, Soininen H; et al. (2005). "Levels of mTOR and its downstream targets 4E-BP1, eEF2, and eEF2 kinase in relationships with tau in Alzheimer's disease brain". FEBS J. 272 (16): 4211–20. doi:10.1111/j.1742-4658.2005.04833.x. PMID 16098202.
  • Kimura K, Wakamatsu A, Suzuki Y; et al. (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMID 16344560.
  • Hait WN, Wu H, Jin S, Yang JM (2007). "Elongation factor-2 kinase: its role in protein synthesis and autophagy". Autophagy. 2 (4): 294–6. PMID 16921268.
  • Beausoleil SA, Villén J, Gerber SA; et al. (2006). "A probability-based approach for high-throughput protein phosphorylation analysis and site localization". Nat. Biotechnol. 24 (10): 1285–92. doi:10.1038/nbt1240. PMID 16964243.
  • Olsen JV, Blagoev B, Gnad F; et al. (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983.

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