EEF2
Available structures
PDBOrtholog search: PDBe RCSB
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
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. 1 2 3 GRCh38: Ensembl release 89: ENSG00000167658 - Ensembl, May 2017
  2. 1 2 3 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. 1 2 "Entrez Gene: EEF2 eukaryotic translation elongation factor 2".
  8. 1 2 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

This article is issued from Wikipedia. The text is licensed under Creative Commons - Attribution - Sharealike. Additional terms may apply for the media files.