EEF2

Protein-coding gene in the species Homo sapiens
EEF2
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

4V6X

Identifiers
AliasesEEF2, EEF-2, EF-2, EF2, SCA26, eukaryotic translation elongation factor 2, Eukaryotic elongation factor 2
External IDsOMIM: 130610 MGI: 95288 HomoloGene: 134867 GeneCards: EEF2
Gene location (Human)
Chromosome 19 (human)
Chr.Chromosome 19 (human)[1]
Chromosome 19 (human)
Genomic location for EEF2
Genomic location for EEF2
Band19p13.3Start3,976,056 bp[1]
End3,985,463 bp[1]
Gene location (Mouse)
Chromosome 10 (mouse)
Chr.Chromosome 10 (mouse)[2]
Chromosome 10 (mouse)
Genomic location for EEF2
Genomic location for EEF2
Band10|10 C1Start81,012,465 bp[2]
End81,018,332 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • parotid gland

  • stromal cell of endometrium

  • external globus pallidus

  • corpus epididymis

  • caput epididymis

  • Achilles tendon

  • germinal epithelium

  • lactiferous duct

  • nipple

  • cardia
Top expressed in
  • molar

  • lacrimal gland

  • maxillary prominence

  • somite

  • ankle

  • submandibular gland

  • crypt of lieberkuhn of small intestine

  • calvaria

  • dorsal tegmental nucleus

  • medulla oblongata
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
  • human 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
SpeciesHumanMouse
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 MbChr 10: 81.01 – 81.02 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

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.[5][6][7][8]

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]

aEF2/eEF2 found in most archaea and eukaryotes, including humans, contains a post translationally modified histidine diphthamide.[8] It is the target of diphtheria toxin (from Corynebacterium diphtheriae), and exotoxin A (from Pseudomonas aeruginosa).[9] 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. ^ a b c GRCh38: Ensembl release 89: ENSG00000167658 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000034994 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Rapp G, Klaudiny J, Hagendorff G, Luck MR, Scheit KH (October 1989). "Complete sequence of the coding region of human elongation factor 2 (EF-2) by enzymatic amplification of cDNA from human ovarian granulosa cells". Biological Chemistry Hoppe-Seyler. 370 (10): 1071–5. doi:10.1515/bchm3.1989.370.2.1071. PMID 2610926.
  6. ^ Kaneda Y, Yoshida MC, Kohno K, Uchida T, Okada Y (May 1984). "Chromosomal assignment of the gene for human elongation factor 2". Proceedings of the National Academy of Sciences of the United States of America. 81 (10): 3158–62. Bibcode:1984PNAS...81.3158K. doi:10.1073/pnas.81.10.3158. PMC 345240. PMID 6427766.
  7. ^ a b "Entrez Gene: EEF2 eukaryotic translation elongation factor 2".
  8. ^ a b Narrowe AB, Spang A, Stairs CW, Caceres EF, Baker BJ, Miller CS, Ettema TJ (September 2018). "Complex Evolutionary History of Translation Elongation Factor 2 and Diphthamide Biosynthesis in Archaea and Parabasalids". Genome Biology and Evolution. 10 (9): 2380–2393. doi:10.1093/gbe/evy154. PMC 6143161. PMID 30060184.
  9. ^ Jørgensen R, Merrill AR, Andersen GR (February 2006). "The life and death of translation elongation factor 2". Biochemical Society Transactions. 34 (Pt 1): 1–6. doi:10.1042/BST20060001. PMID 16246167.

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.
  • 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.
  • 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.
  • 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.
  • 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.
  • 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.
  • 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.
  • 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.
  • 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.
  • 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 14594813.
  • 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.
  • 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.
  • 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.
  • 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.
  • 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.
  • 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.

External links

  • v
  • t
  • e
Proteins
Initiation factor
Bacterial
Mitochondrial
Archaeal
  • aIF1
  • aIF2
  • aIF5
  • aIF6
Eukaryotic
eIF1
eIF2
eIF3
eIF4
eIF5
eIF6
Elongation factor
Bacterial/​Mitochondrial
Archaeal/​Eukaryotic
Release factor
Ribosomal Proteins
Cytoplasmic
60S subunit
40S subunit
Mitochondrial
39S subunit
28S subunit
Other concepts
Stub icon

This article on a gene on human chromosome 19 is a stub. You can help Wikipedia by expanding it.

  • v
  • t
  • e