EEF2

EEF2
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	4V6X
Identifiers
Aliases	EEF2, EEF-2, EF-2, EF2, SCA26, eukaryotic translation elongation factor 2, Eukaryotic elongation factor 2
External IDs	MGI: 95288 HomoloGene: 134867 GeneCards: EEF2
Gene location (Human)
Chr.	Chromosome 19 (human)[1]
End	3,985,469 bp[1]
Gene location (Mouse)
Chr.	Chromosome 10 (mouse)[2]
End	81,182,498 bp[2]
RNA expression pattern
	; ;
	More reference expression data
Gene ontology
Molecular function	• nucleotide binding; • ribosome binding; • GTP binding; • p53 binding; • translation elongation factor activity; • actin filament binding; • protein binding; • 5S rRNA binding; • protein kinase binding; • RNA binding; • GTPase activity; • cadherin binding;
Cellular component	• cytoplasm; • polysome; • membrane; • plasma membrane; • intracellular ribonucleoprotein complex; • aggresome; • membrane raft; • extracellular exosome; • cell nucleus; • polysomal ribosome; • extracellular matrix; • extracellular region; • cytosol; • secretory granule lumen; • ficolin-1-rich granule lumen;
Biological process	• response to estradiol; • positive regulation of cytoplasmic translation; • skeletal muscle contraction; • translational elongation; • aging; • positive regulation of translation; • response to endoplasmic reticulum stress; • cellular response to brain-derived neurotrophic factor stimulus; • response to ischemia; • hematopoietic progenitor cell differentiation; • peptidyl-diphthamide biosynthetic process from peptidyl-histidine; • glial cell proliferation; • skeletal muscle cell differentiation; • response to folic acid; • response to ethanol; • response to hydrogen peroxide; • translation; • protein methylation; • response to drug; • neutrophil degranulation;
	Sources:Amigo / QuickGO
Orthologs
	1938
	13629
	ENSG00000167658
	ENSMUSG00000034994
	P13639
	P58252
	NM_001961
	NM_007907
	NP_001952
	NP_031933
	Wikidata
View/Edit Human	View/Edit Mouse

Eukaryotic elongation factor 2 is a protein that in humans is encoded by the EEF2 gene.^[5]^[6]^[7]

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 ribosome. This protein is completely inactivated by EF-2 kinase phosphorylation.^[7]

It is the target of diphtheria toxin (from Corynebacterium diphtheriae), and exotoxin A (from Pseudomonas aeruginosa).^[8] The inactivation of EF-2 by toxins inhibits protein production in the host, causing symptoms due to loss of function in affected cells.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000167658 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000034994 - Ensembl, May 2017
↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ 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. doi:10.1515/bchm3.1989.370.2.1071. 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.
1 2 "Entrez Gene: EEF2 eukaryotic translation elongation factor 2".
↑ 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.

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. doi:10.1515/bchm3.1992.373.1.201. 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. doi:10.1515/bchm3.1988.369.1.247. 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.
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.
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.
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.
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

Peptide+Elongation+Factor+2 at the US National Library of Medicine Medical Subject Headings (MeSH)

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000167658 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000034994 - Ensembl, May 2017

[3] "Human PubMed Reference:".

[4] "Mouse PubMed Reference:".

[pmid2610926-5] 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. doi:10.1515/bchm3.1989.370.2.1071. PMID 2610926.

[pmid6427766-6] 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.

[entrez-7] 1 2 "Entrez Gene: EEF2 eukaryotic translation elongation factor 2".

[pmid16246167-8] 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.

EEF2

References

Further reading

External links