EEF1G

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
1PBU

Identifiers

Aliases

EEF1G, EF1G, GIG35, eukaryotic translation elongation factor 1 gamma

External IDs

MGI: 1914410 HomoloGene: 20363 GeneCards: EEF1G

Gene ontology
Molecular function	• protein binding • cadherin binding • translation elongation factor activity • glutathione transferase activity
Cellular component	• cytoplasm • cytosol • extracellular exosome • membrane • endoplasmic reticulum • nucleus
Biological process	• translational elongation • response to virus • translation • glutathione metabolic process
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


1937


67160

Ensembl


ENSG00000254772


ENSMUSG00000071644

UniProt


P26641


Q9D8N0

RefSeq (mRNA)


NM_001404


NM_026007

RefSeq (protein)


NP_001395


NP_080283

Location (UCSC)

Chr 11: 62.56 – 62.57 Mb

Chr 19: 8.97 – 8.98 Mb

PubMed search

^[1]

^[2]

Wikidata

View/Edit Human

View/Edit Mouse

Elongation factor 1-gamma is a protein that in humans is encoded by the EEF1G gene.^[3]^[4]^[5]

Function

This gene encodes a subunit of the elongation factor-1 complex, which is responsible for the enzymatic delivery of aminoacyl tRNAs to the ribosome. This subunit contains an N-terminal glutathione transferase domain, which may be involved in regulating the assembly of multisubunit complexes containing this elongation factor and aminoacyl-tRNA synthetases.^[5]

Interactions

EEF1G has been shown to interact with:

References

↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ Kumabe T, Sohma Y, Yamamoto T (July 1992). "Human cDNAs encoding elongation factor 1 gamma and the ribosomal protein L19". Nucleic Acids Res. 20 (10): 2598. PMC 312399 . PMID 1598220. doi:10.1093/nar/20.10.2598.
↑ Sanders J, Maassen JA, Möller W (January 1993). "Elongation factor-1 messenger-RNA levels in cultured cells are high compared to tissue and are not drastically affected further by oncogenic transformation". Nucleic Acids Res. 20 (22): 5907–10. PMC 334453 . PMID 1461723. doi:10.1093/nar/20.22.5907.
1 2 "Entrez Gene: EEF1G eukaryotic translation elongation factor 1 gamma".
1 2 3 Stelzl U, Worm U, Lalowski M, Haenig C, Brembeck FH, Goehler H, Stroedicke M, Zenkner M, Schoenherr A, Koeppen S, Timm J, Mintzlaff S, Abraham C, Bock N, Kietzmann S, Goedde A, Toksöz E, Droege A, Krobitsch S, Korn B, Birchmeier W, Lehrach H, Wanker EE (September 2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell. 122 (6): 957–68. PMID 16169070. doi:10.1016/j.cell.2005.08.029.
1 2 Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (October 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. PMID 16189514. doi:10.1038/nature04209.
1 2 Sang Lee J, Gyu Park S, Park H, Seol W, Lee S, Kim S (February 2002). "Interaction network of human aminoacyl-tRNA synthetases and subunits of elongation factor 1 complex". Biochem. Biophys. Res. Commun. 291 (1): 158–64. PMID 11829477. doi:10.1006/bbrc.2002.6398.
↑ Ishii H, Vecchione A, Murakumo Y, Baldassarre G, Numata S, Trapasso F, Alder H, Baffa R, Croce CM (August 2001). "FEZ1/LZTS1 gene at 8p22 suppresses cancer cell growth and regulates mitosis". Proc. Natl. Acad. Sci. U.S.A. 98 (18): 10374–9. PMC 56968 . PMID 11504921. doi:10.1073/pnas.181222898.

Lew Y, Jones DV, Mars WM, Evans D, Byrd D, Frazier ML (1992). "Expression of elongation factor-1 gamma-related sequence in human pancreatic cancer.". Pancreas. 7 (2): 144–52. PMID 1372736. doi:10.1097/00006676-199203000-00003.
Koonin EV, Mushegian AR, Tatusov RL, Altschul SF, Bryant SH, Bork P, Valencia A (1995). "Eukaryotic translation elongation factor 1 gamma contains a glutathione transferase domain--study of a diverse, ancient protein superfamily using motif search and structural modeling.". Protein Sci. 3 (11): 2045–54. PMC 2142650 . PMID 7703850. doi:10.1002/pro.5560031117.
Sheu GT, Traugh JA (1998). "Recombinant subunits of mammalian elongation factor 1 expressed in Escherichia coli. Subunit interactions, elongation activity, and phosphorylation by protein kinase CKII.". J. Biol. Chem. 272 (52): 33290–7. PMID 9407120. doi:10.1074/jbc.272.52.33290.
Sheu GT, Traugh JA (1999). "A structural model for elongation factor 1 (EF-1) and phosphorylation by protein kinase CKII.". Mol. Cell. Biochem. 191 (1-2): 181–6. PMID 10094407. doi:10.1023/A:1006802125856.
Kim JE, Kim KH, Lee SW, Seol W, Shiba K, Kim S (2000). "An elongation factor-associating domain is inserted into human cysteinyl-tRNA synthetase by alternative splicing.". Nucleic Acids Res. 28 (15): 2866–72. PMC 102683 . PMID 10908348. doi:10.1093/nar/28.15.2866.
Ishii H, Vecchione A, Murakumo Y, Baldassarre G, Numata S, Trapasso F, Alder H, Baffa R, Croce CM (2001). "FEZ1/LZTS1 gene at 8p22 suppresses cancer cell growth and regulates mitosis.". Proc. Natl. Acad. Sci. U.S.A. 98 (18): 10374–9. PMC 56968 . PMID 11504921. doi:10.1073/pnas.181222898.
Sang Lee J, Gyu Park S, Park H, Seol W, Lee S, Kim S (2002). "Interaction network of human aminoacyl-tRNA synthetases and subunits of elongation factor 1 complex.". Biochem. Biophys. Res. Commun. 291 (1): 158–64. PMID 11829477. doi:10.1006/bbrc.2002.6398.
Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J (2004). "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides.". Nat. Biotechnol. 21 (5): 566–9. PMID 12665801. doi:10.1038/nbt810.
Vanwetswinkel S, Kriek J, Andersen GR, Dijk J, Siegal G (2004). "1H, 15N and 13C resonance assignments of the highly conserved 19 kDa C-terminal domain from human elongation factor 1Bgamma.". J. Biomol. NMR. 26 (2): 189–90. PMID 12766415. doi:10.1023/A:1023504611632.
Zhang C, Dowd DR, Staal A, Gu C, Lian JB, van Wijnen AJ, Stein GS, MacDonald PN (2003). "Nuclear coactivator-62 kDa/Ski-interacting protein is a nuclear matrix-associated coactivator that may couple vitamin D receptor-mediated transcription and RNA splicing.". J. Biol. Chem. 278 (37): 35325–36. PMID 12840015. doi:10.1074/jbc.M305191200.
Colland F, Jacq X, Trouplin V, Mougin C, Groizeleau C, Hamburger A, Meil A, Wojcik J, Legrain P, Gauthier JM (2004). "Functional proteomics mapping of a human signaling pathway.". Genome Res. 14 (7): 1324–32. PMC 442148 . PMID 15231748. doi:10.1101/gr.2334104.
Jin J, Smith FD, Stark C, Wells CD, Fawcett JP, Kulkarni S, Metalnikov P, O'Donnell P, Taylor P, Taylor L, Zougman A, Woodgett JR, Langeberg LK, Scott JD, Pawson T (2004). "Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization.". Curr. Biol. 14 (16): 1436–50. PMID 15324660. doi:10.1016/j.cub.2004.07.051.
Goehler H, Lalowski M, Stelzl U, Waelter S, Stroedicke M, Worm U, Droege A, Lindenberg KS, Knoblich M, Haenig C, Herbst M, Suopanki J, Scherzinger E, Abraham C, Bauer B, Hasenbank R, Fritzsche A, Ludewig AH, Büssow K, Buessow K, Coleman SH, Gutekunst CA, Landwehrmeyer BG, Lehrach H, Wanker EE (2004). "A protein interaction network links GIT1, an enhancer of huntingtin aggregation, to Huntington's disease.". Mol. Cell. 15 (6): 853–65. PMID 15383276. doi:10.1016/j.molcel.2004.09.016.
Andersen JS, Lam YW, Leung AK, Ong SE, Lyon CE, Lamond AI, Mann M (2005). "Nucleolar proteome dynamics.". Nature. 433 (7021): 77–83. PMID 15635413. doi:10.1038/nature03207.

PDB gallery

1pbu: Solution structure of the C-terminal domain of the human eEF1Bgamma subunit

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EEF1G

Function

Interactions

References

Further reading