EEF2

Eukaryotic elongation factor 2 is a protein that in humans is encoded by the EEF2 gene. It is the archaeal and eukaryotic counterpart of bacterial EF-G.

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	OMIM: 130610; MGI: 95288; HomoloGene: 134867; GeneCards: EEF2; OMA:EEF2 - orthologs
Gene location (Human) Chr. Chromosome 19 (human) Band 19p13.3 Start 3,976,056 bp End 3,985,463 bp
Gene location (Mouse) Chr. Chromosome 10 (mouse) Band 10|10 C1 Start 81,012,465 bp End 81,018,332 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in parotid gland cartilage tissue stromal cell of endometrium external globus pallidus corpus epididymis caput epididymis lateral nuclear group of thalamus pars reticulata Achilles tendon epithelium of colon Top expressed in Gonadal ridge molar lacrimal gland transitional epithelium of urinary bladder maxillary prominence mandibular prominence dentate gyrus of hippocampal formation granule cell somite ankle mesenteric lymph nodes More reference expression data BioGPS 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 aggresome membrane raft extracellular exosome nucleus polysomal ribosome extracellular matrix extracellular region cytosol secretory granule lumen ficolin-1-rich granule lumen synapse ribonucleoprotein complex Biological process response to estradiol positive regulation of cytoplasmic translation skeletal muscle contraction translational elongation ageing 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 protein biosynthesis protein methylation neutrophil degranulation Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 1938 13629 Ensembl ENSG00000167658 ENSMUSG00000034994 UniProt P13639 P58252 RefSeq (mRNA) NM_001961 NM_007907 RefSeq (protein) NP_001952 NP_031933 Location (UCSC) Chr 19: 3.98 – 3.99 Mb Chr 10: 81.01 – 81.02 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

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.

aEF2/eEF2 found in most archaea and eukaryotes, including humans, contains a post translationally modified histidine diphthamide. It is the target of diphtheria toxin (from Corynebacterium diphtheriae), and exotoxin A (from Pseudomonas aeruginosa). The inactivation of EF-2 by toxins inhibits protein production in the host, causing symptoms due to loss of function in affected cells.

Further reading

• Hanes J, Freudenstein J, Rapp G, Scheit KH (April 1992). "Construction of a plasmid containing the complete coding region of human elongation factor 2". Biological Chemistry Hoppe-Seyler. 373 (4): 201–4. doi:10.1515/bchm3.1992.373.1.201. PMID 1596361.201-4&rft.date=1992-04&rft_id=info:doi/10.1515/bchm3.1992.373.1.201&rft_id=info:pmid/1596361&rft.aulast=Hanes&rft.aufirst=J&rft.au=Freudenstein, J&rft.au=Rapp, G&rft.au=Scheit, KH&rfr_id=info:sid/en.wikipedia.org:EEF2" class="Z3988">
• Nygård O, Nilsson L (April 1990). "Kinetic determination of the effects of ADP-ribosylation on the interaction of eukaryotic elongation factor 2 with ribosomes". The Journal of Biological Chemistry. 265 (11): 6030–4. doi:10.1016/S0021-9258(19)39286-5. PMID 2318846.6030-4&rft.date=1990-04&rft_id=info:doi/10.1016/S0021-9258(19)39286-5&rft_id=info:pmid/2318846&rft.aulast=Nygård&rft.aufirst=O&rft.au=Nilsson, L&rft_id=https://doi.org/10.1016%2FS0021-9258%2819%2939286-5&rfr_id=info:sid/en.wikipedia.org:EEF2" class="Z3988">
• Rapp G, Mucha J, Einspanier R, Luck M, Scheit KH (April 1988). "Cloning and sequence analysis of a cDNA from human ovarian granulosa cells encoding the C-terminal part of human elongation factor 2". Biological Chemistry Hoppe-Seyler. 369 (4): 247–50. doi:10.1515/bchm3.1988.369.1.247. PMID 2840927.247-50&rft.date=1988-04&rft_id=info:doi/10.1515/bchm3.1988.369.1.247&rft_id=info:pmid/2840927&rft.aulast=Rapp&rft.aufirst=G&rft.au=Mucha, J&rft.au=Einspanier, R&rft.au=Luck, M&rft.au=Scheit, KH&rfr_id=info:sid/en.wikipedia.org:EEF2" class="Z3988">
• Kaneda Y, Hayes H, Uchida T, Yoshida MC, Okada Y (1987). "Regional assignment of five genes on human chromosome 19". Chromosoma. 95 (1): 8–12. doi:10.1007/BF00293835. PMID 3034518. S2CID 33919242.8-12&rft.date=1987&rft_id=https://api.semanticscholar.org/CorpusID:33919242#id-name=S2CID&rft_id=info:pmid/3034518&rft_id=info:doi/10.1007/BF00293835&rft.aulast=Kaneda&rft.aufirst=Y&rft.au=Hayes, H&rft.au=Uchida, T&rft.au=Yoshida, MC&rft.au=Okada, Y&rfr_id=info:sid/en.wikipedia.org:EEF2" class="Z3988">
• Nairn AC, Palfrey HC (December 1987). "Identification of the major Mr 100,000 substrate for calmodulin-dependent protein kinase III in mammalian cells as elongation factor-2". The Journal of Biological Chemistry. 262 (36): 17299–303. doi:10.1016/S0021-9258(18)45377-X. PMID 3693353.17299-303&rft.date=1987-12&rft_id=info:doi/10.1016/S0021-9258(18)45377-X&rft_id=info:pmid/3693353&rft.aulast=Nairn&rft.aufirst=AC&rft.au=Palfrey, HC&rft_id=https://doi.org/10.1016%2FS0021-9258%2818%2945377-X&rfr_id=info:sid/en.wikipedia.org:EEF2" class="Z3988">
• Shestakova EA, Motuz LP, Minin AA, Gavrilova LP (April 1993). "Study of localization of the protein-synthesizing machinery along actin filament bundles". Cell Biology International. 17 (4): 409–16. doi:10.1006/cbir.1993.1079. PMID 8318952. S2CID 37430592.409-16&rft.date=1993-04&rft_id=https://api.semanticscholar.org/CorpusID:37430592#id-name=S2CID&rft_id=info:pmid/8318952&rft_id=info:doi/10.1006/cbir.1993.1079&rft.aulast=Shestakova&rft.aufirst=EA&rft.au=Motuz, LP&rft.au=Minin, AA&rft.au=Gavrilova, LP&rfr_id=info:sid/en.wikipedia.org:EEF2" class="Z3988">
• Redpath NT, Price NT, Severinov KV, Proud CG (April 1993). "Regulation of elongation factor-2 by multisite phosphorylation". European Journal of Biochemistry. 213 (2): 689–99. doi:10.1111/j.1432-1033.1993.tb17809.x. PMID 8386634.689-99&rft.date=1993-04&rft_id=info:doi/10.1111/j.1432-1033.1993.tb17809.x&rft_id=info:pmid/8386634&rft.aulast=Redpath&rft.aufirst=NT&rft.au=Price, NT&rft.au=Severinov, KV&rft.au=Proud, CG&rft_id=https://doi.org/10.1111%2Fj.1432-1033.1993.tb17809.x&rfr_id=info:sid/en.wikipedia.org:EEF2" class="Z3988">
• Knebel A, Haydon CE, Morrice N, Cohen P (October 2002). "Stress-induced regulation of eukaryotic elongation factor 2 kinase by SB 203580-sensitive and -insensitive pathways". The Biochemical Journal. 367 (Pt 2): 525–32. doi:10.1042/BJ20020916. PMC 1222910. PMID 12171600.525-32&rft.date=2002-10&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1222910#id-name=PMC&rft_id=info:pmid/12171600&rft_id=info:doi/10.1042/BJ20020916&rft.aulast=Knebel&rft.aufirst=A&rft.au=Haydon, CE&rft.au=Morrice, N&rft.au=Cohen, P&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1222910&rfr_id=info:sid/en.wikipedia.org:EEF2" class="Z3988">
• Yin X, Fontoura BM, Morimoto T, Carroll RB (September 2003). "Cytoplasmic complex of p53 and eEF2". Journal of Cellular Physiology. 196 (3): 474–82. doi:10.1002/jcp.10329. PMID 12891704. S2CID 25241366.474-82&rft.date=2003-09&rft_id=https://api.semanticscholar.org/CorpusID:25241366#id-name=S2CID&rft_id=info:pmid/12891704&rft_id=info:doi/10.1002/jcp.10329&rft.aulast=Yin&rft.aufirst=X&rft.au=Fontoura, BM&rft.au=Morimoto, T&rft.au=Carroll, RB&rfr_id=info:sid/en.wikipedia.org:EEF2" class="Z3988">
• Ryazanova LV, Dorovkov MV, Ansari A, Ryazanov AG (January 2004). "Characterization of the protein kinase activity of TRPM7/ChaK1, a protein kinase fused to the transient receptor potential ion channel". The Journal of Biological Chemistry. 279 (5): 3708–16. doi:10.1074/jbc.M308820200. PMID 14863813.3708-16&rft.date=2004-01&rft_id=info:doi/10.1074/jbc.M308820200&rft_id=info:pmid/14863813&rft.aulast=Ryazanova&rft.aufirst=LV&rft.au=Dorovkov, MV&rft.au=Ansari, A&rft.au=Ryazanov, AG&rft_id=https://doi.org/10.1074%2Fjbc.M308820200&rfr_id=info:sid/en.wikipedia.org:EEF2" class="Z3988">
• Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villén J, Li J, et al. (August 2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proceedings of the National Academy of Sciences of the United States of America. 101 (33): 12130–5. Bibcode:2004PNAS..10112130B. doi:10.1073/pnas.0404720101. PMC 514446. PMID 15302935.12130-5&rft.date=2004-08&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC514446#id-name=PMC&rft_id=info:pmid/15302935&rft_id=info:doi/10.1073/pnas.0404720101&rft_id=info:bibcode/2004PNAS..10112130B&rft.aulast=Beausoleil&rft.aufirst=SA&rft.au=Jedrychowski, M&rft.au=Schwartz, D&rft.au=Elias, JE&rft.au=Villén, J&rft.au=Li, J&rft.au=Cohn, MA&rft.au=Cantley, LC&rft.au=Gygi, SP&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC514446&rfr_id=info:sid/en.wikipedia.org:EEF2" class="Z3988">
• Elo MA, Karjalainen HM, Sironen RK, Valmu L, Redpath NT, Browne GJ, et al. (February 2005). "High hydrostatic pressure inhibits the biosynthesis of eukaryotic elongation factor-2". Journal of Cellular Biochemistry. 94 (3): 497–507. doi:10.1002/jcb.20333. PMID 15534876. S2CID 25000605.497-507&rft.date=2005-02&rft_id=https://api.semanticscholar.org/CorpusID:25000605#id-name=S2CID&rft_id=info:pmid/15534876&rft_id=info:doi/10.1002/jcb.20333&rft.aulast=Elo&rft.aufirst=MA&rft.au=Karjalainen, HM&rft.au=Sironen, RK&rft.au=Valmu, L&rft.au=Redpath, NT&rft.au=Browne, GJ&rft.au=Kalkkinen, N&rft.au=Helminen, HJ&rft.au=Lammi, MJ&rfr_id=info:sid/en.wikipedia.org:EEF2" class="Z3988">
• Andersen JS, Lam YW, Leung AK, Ong SE, Lyon CE, Lamond AI, Mann M (January 2005). "Nucleolar proteome dynamics". Nature. 433 (7021): 77–83. Bibcode:2005Natur.433...77A. doi:10.1038/nature03207. PMID 15635413. S2CID 4344740.77-83&rft.date=2005-01&rft_id=info:doi/10.1038/nature03207&rft_id=https://api.semanticscholar.org/CorpusID:4344740#id-name=S2CID&rft_id=info:pmid/15635413&rft_id=info:bibcode/2005Natur.433...77A&rft.aulast=Andersen&rft.aufirst=JS&rft.au=Lam, YW&rft.au=Leung, AK&rft.au=Ong, SE&rft.au=Lyon, CE&rft.au=Lamond, AI&rft.au=Mann, M&rfr_id=info:sid/en.wikipedia.org:EEF2" class="Z3988">
• Shibatani T, David LL, McCormack AL, Frueh K, Skach WR (April 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 15835887.5982-92&rft.date=2005-04&rft_id=info:doi/10.1021/bi047328f&rft_id=info:pmid/15835887&rft.aulast=Shibatani&rft.aufirst=T&rft.au=David, LL&rft.au=McCormack, AL&rft.au=Frueh, K&rft.au=Skach, WR&rfr_id=info:sid/en.wikipedia.org:EEF2" class="Z3988">
• Ahmed M, Forsberg J, Bergsten P (2005). "Protein profiling of human pancreatic islets by two-dimensional gel electrophoresis and mass spectrometry". Journal of Proteome Research. 4 (3): 931–40. doi:10.1021/pr050024a. PMID 15952740.931-40&rft.date=2005&rft_id=info:doi/10.1021/pr050024a&rft_id=info:pmid/15952740&rft.aulast=Ahmed&rft.aufirst=M&rft.au=Forsberg, J&rft.au=Bergsten, P&rfr_id=info:sid/en.wikipedia.org:EEF2" class="Z3988">
• Gevaert K, Staes A, Van Damme J, De Groot S, Hugelier K, Demol H, et al. (September 2005). "Global phosphoproteome analysis on human HepG2 hepatocytes using reversed-phase diagonal LC". Proteomics. 5 (14): 3589–99. doi:10.1002/pmic.200401217. PMID 16097034. S2CID 895879.3589-99&rft.date=2005-09&rft_id=https://api.semanticscholar.org/CorpusID:895879#id-name=S2CID&rft_id=info:pmid/16097034&rft_id=info:doi/10.1002/pmic.200401217&rft.aulast=Gevaert&rft.aufirst=K&rft.au=Staes, A&rft.au=Van Damme, J&rft.au=De Groot, S&rft.au=Hugelier, K&rft.au=Demol, H&rft.au=Martens, L&rft.au=Goethals, M&rft.au=Vandekerckhove, J&rfr_id=info:sid/en.wikipedia.org:EEF2" class="Z3988">

External links

• Peptide Elongation Factor 2 at the U.S. National Library of Medicine Medical Subject Headings (MeSH)