EEF2

Eukaryotic translation elongation factor 2

Identifiers

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

RefSeq (mRNA)

RefSeq (protein)

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.^[1]^[2]^[3]

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.^[3]

It is the target of diphtheria toxin and exotoxin A.^[4]

References

^ Rapp G, Klaudiny J, Hagendorff G, Luck MR, Scheit KH (Mar 1990). "Complete sequence of the coding region of human elongation factor 2 (EF-2) by enzymatic amplification of cDNA from human ovarian granulosa cells". Biol Chem Hoppe Seyler 370 (10): 1071–5. PMID 2610926.
^ Kaneda Y, Yoshida MC, Kohno K, Uchida T, Okada Y (Jul 1984). "Chromosomal assignment of the gene for human elongation factor 2". Proc Natl Acad Sci U S A 81 (10): 3158–62. doi:10.1073/pnas.81.10.3158. PMC 345240. PMID 6427766. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=345240.
^ ^a ^b "Entrez Gene: EEF2 eukaryotic translation elongation factor 2". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1938.
^ Jørgensen R, Merrill AR, Andersen GR (February 2006). "The life and death of translation elongation factor 2". Biochem. Soc. Trans. 34 (Pt 1): 1–6. doi:10.1042/BST20060001. PMID 16246167. http://www.biochemsoctrans.org/bst/034/0001/bst0340001.htm.

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

Protein biosynthesis: translation (prokaryotic, eukaryotic)

Ribosomal proteins

Initiation factor

Prokaryotic	PIF-1 · PIF-2 · PIF-3

Archaeal	aIF1 · aIF2 · aIF5 · aIF6

Eukaryotic	eIF1 (EIF1AX, AY, 1B) eIF2 (EIF2S1, EIF2S2, EIF2S3) · EIF2B1, EIF2B2, EIF2B3, EIF2B4, EIF2B5 · EIF-2 kinase eIF3 (EIF3A, B, C, D, F, G, H, I, J, K, M, S6) eIF4 (EIF4A2, A3, B, E1, E2, G1, G2, G3, H) eIF5 (EIF5A, A2, B) eIF6 (EIF6)

Elongation factor

Prokaryotic	EF-Tu, EF-Ts, EF-G

Archaeal	aEF-1, aEF-2

Eukaryotic	EEF-1 (EEF1A1, EEF1A2, EEF1A3, EEF1B1, EEF1B2, EEF1B3, EEF1B4, EEF1D, EEF1E1, EEF1G) · EEF2

Release factor

Prokaryotic · Archaeal · Eukaryotic (ETF1)

Other

RPS1 · RPS2 · RPS3 · RPS4 · RPS5 · RPS6 · RPS7 · RPS8 · RPS9 · RPS10 · RPS11 · RPS12 · RPS13 · RPS14 · RPS15 · RPS16 · RPS17 · RPS18 · RPS19 · RPS20 · RPS21 · RPS22 · RPS23 · RPS24 · RPS25 · RPS26 · RPS27 · RPS28 · RPS29

Other concepts

Aminoacyl tRNA synthetase · Reading frame · Start codon · Stop codon · Shine-Dalgarno sequence/Kozak consensus sequence

see also disorders of translation and posttranslational modification
B bsyn: dna (repl, cycl, reco, repr) · tscr (fact, tcrg, nucl, rnat, rept, ptts) · tltn (risu, pttl, nexn) · dnab, rnab/runp · stru (domn, 1°, 2°, 3°, 4°)

EEF2

References

Further reading

External links