EEF2

Eukaryotic translation elongation factor 2
Identifiers
Symbols	EEF2; EEF-2; EF2
External IDs	OMIM: 130610 MGI: 95288 HomoloGene: 100816 GeneCards: EEF2 Gene
Gene Ontology Molecular function • nucleotide binding • translation elongation factor activity • GTPase activity • protein binding • GTP binding Cellular component • cytoplasm • cytosol • ribonucleoprotein complex Biological process • translation • translational elongation • gene expression • cellular protein metabolic process Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	1938	13629
Ensembl	ENSG00000167658	ENSMUSG00000034994
UniProt	P13639	O89069
RefSeq (mRNA)	NM_001961	NM_007907.2
RefSeq (protein)	NP_001952	NP_031933.1
Location (UCSC)	Chr 19: 3.97 – 3.99 Mb	Chr 10: 80.64 – 80.65 Mb
PubMed search	[1]	[2]

Elongation factor 2 is a protein that in humans is encoded by the EEF2 gene.

This gene encodes a member of the GTP-binding translation elongation factor family. This protein is an essential factor for protein synthesis. It promotes the GTP-dependent translocation of the nascent protein chain from the A-site to the P-site of the ribosome. This protein is completely inactivated by EF-2 kinase phosporylation.

It is the target of diphtheria toxin and exotoxin A.

Further reading

• Hanes J, Freudenstein J, Rapp G, Scheit KH (1992). "Construction of a plasmid containing the complete coding region of human elongation factor 2.". Biol. Chem. Hoppe-Seyler 373 (4): 201–4. PMID 1596361. 
• Nygård O, Nilsson L (1990). "Kinetic determination of the effects of ADP-ribosylation on the interaction of eukaryotic elongation factor 2 with ribosomes.". J. Biol. Chem. 265 (11): 6030–4. PMID 2318846. 
• Rapp G, Mucha J, Einspanier R, et al. (1988). "Cloning and sequence analysis of a cDNA from human ovarian granulosa cells encoding the C-terminal part of human elongation factor 2.". Biol. Chem. Hoppe-Seyler 369 (4): 247–50. PMID 2840927. 
• Kaneda Y, Hayes H, Uchida T, et al. (1987). "Regional assignment of five genes on human chromosome 19.". Chromosoma 95 (1): 8–12. doi:10.1007/BF00293835. PMID 3034518. 
• 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. 
• Shestakova EA, Motuz LP, Minin AA, Gavrilova LP (1993). "Study of localization of the protein-synthesizing machinery along actin filament bundles.". Cell Biol. Int. 17 (4): 409–16. doi:10.1006/cbir.1993.1079. PMID 8318952. 
• Redpath NT, Price NT, Severinov KV, Proud CG (1993). "Regulation of elongation factor-2 by multisite phosphorylation.". Eur. J. Biochem. 213 (2): 689–99. doi:10.1111/j.1432-1033.1993.tb17809.x. PMID 8386634. 
• 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. PMC 1222910. PMID 12171600. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1222910. 
• 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. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241. 
• Yin X, Fontoura BM, Morimoto T, Carroll RB (2003). "Cytoplasmic complex of p53 and eEF2.". J. Cell. Physiol. 196 (3): 474–82. doi:10.1002/jcp.10329. PMID 12891704. 
• Ryazanova LV, Dorovkov MV, Ansari A, Ryazanov AG (2004). "Characterization of the protein kinase activity of TRPM7/ChaK1, a protein kinase fused to the transient receptor potential ion channel.". J. Biol. Chem. 279 (5): 3708–16. doi:10.1074/jbc.M308820200. PMID 14594813. 
• Beausoleil SA, Jedrychowski M, Schwartz D, et al. (2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins.". Proc. Natl. Acad. Sci. U.S.A. 101 (33): 12130–5. doi:10.1073/pnas.0404720101. PMC 514446. PMID 15302935. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=514446. 
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928. 
• Elo MA, Karjalainen HM, Sironen RK, et al. (2005). "High hydrostatic pressure inhibits the biosynthesis of eukaryotic elongation factor-2.". J. Cell. Biochem. 94 (3): 497–507. doi:10.1002/jcb.20333. PMID 15534876. 
• Andersen JS, Lam YW, Leung AK, et al. (2005). "Nucleolar proteome dynamics.". Nature 433 (7021): 77–83. doi:10.1038/nature03207. PMID 15635413. 
• Shibatani T, David LL, McCormack AL, et al. (2005). "Proteomic analysis of mammalian oligosaccharyltransferase reveals multiple subcomplexes that contain Sec61, TRAP, and two potential new subunits.". Biochemistry 44 (16): 5982–92. doi:10.1021/bi047328f. PMID 15835887. 
• Ahmed M, Forsberg J, Bergsten P (2005). "Protein profiling of human pancreatic islets by two-dimensional gel electrophoresis and mass spectrometry.". J. Proteome Res. 4 (3): 931–40. doi:10.1021/pr050024a. PMID 15952740. 
• Gevaert K, Staes A, Van Damme J, et al. (2006). "Global phosphoproteome analysis on human HepG2 hepatocytes using reversed-phase diagonal LC.". Proteomics 5 (14): 3589–99. doi:10.1002/pmic.200401217. PMID 16097034. 

External links

• MeSH Peptide+Elongation+Factor+2