EEF2 information

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)
End	3,985,463 bp
Gene location (Mouse)
Chr.	Chromosome 10 (mouse)
End	81,018,332 bp
RNA expression pattern
	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
	; ;
	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
	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. 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.

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000167658 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000034994 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ 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.
^ 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.
^ ^a ^b "Entrez Gene: EEF2 eukaryotic translation elongation factor 2".
^ ^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.
^ 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.

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

[refGRCm38Ensembl-2] 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.

[pmid2610926-5] 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.

[pmid6427766-6] 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.

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

[dph-8] 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.

[pmid16246167-9] 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.

EEF2 information

and 22 Related for: EEF2 information

EEF2

Ketamine

Exercise

Diaphoretickes

Diphtheria

Glaucophyte

Viridiplantae

Chromista

DPH1

Eukaryotic translation

Translational regulation

Reference genes

Lopinavir

Elongation factor 2 kinase

Labidostomis longimana

MTOR

Red algae

Chromalveolata

Archaeplastida

Eukaryotic ribosome

EEF2K

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