EEF1G (Eukaryotic translation elongation factor 1 gamma)

2019-03-01   Luigi Cristiano 

Aesthetic and medical biotechnologies research unit, Prestige, Terranuova Bracciolini, Italy;




Eukaryotic translation elongation factor 1 gamma, alias eEF1G, is a protein that plays a main function in the elongation step of translation process but also covers numerous moonlighting roles. Considering its importance in the cell it is found frequently overexpressed in human cancer cells and thus this review wants to collect the state of the art about EEF1G, with insights on DNA, RNA, protein encoded and the diseases where it is implicated.


Atlas Image
Figure. 1. Splice variants of EEF1G. The figure shows the locus on chromosome 11 of the EEF1G gene and its splicing variants (grey/blue box). The primary transcript is EEF1G-001 mRNA (green/red box), but also EEF1G-201 variant is able to codify for a protein (reworked from;;


EEF1G (Eukaryotic Translation Elongation Factor 1 Gamma) is a protein coding gene that starts at 62,559,601 nt and ends at 62,573,988 nt from qter and with a length of 14388 bp. The current reference sequence is NC_000011.10 and contains 10 exons. It is proximal to the nucleotidyl transferase TUT1 (terminal uridylyl transferase 1) gene and to the AHNAK nucleoprotein gene. Inside the nucleotidic sequence of EEF1G there is also a short non-coding sequence of the microRNA MIR6747 that starts from 62567011 bp and ends at 62567071 bp and is 61 bp long. Around the genomic locus of EEF1G take place different promoter or enhancer transcriptional elements. Two strong elements are closer to the sequence of EEF1G gene and are located at -1.4 kb and at +2.4 kb respectively and have a high influence of different kind of genes in their proximity, such as EEF1G1 and TUT1.


EEF1G mRNA is 1446 bp long with a reference sequence reported in GeneBank as NM_001404.5. The 5UTR sequence is not very long and counts 49 nt. The CDS is extended from 50 to 1363 nt, while the 3UTR starts from 1364 until 1446 nt. EEF1G is expressed ubiquitously in human tissues with a different expression level in relation to the specific tissue type. Minor expression levels are reported for brain, liver, lung, pancreas, salivary glands and testis while on the contrary a significantly higher expression level is found in the ovary (Fagerberg et al., 2014).
Five splice variants for EEF1G were observed (Table.1): the main reference variant is EEF1G-001 and the others are EEF1G-002, EEF1G-003, EEF1G-004 and EEF1G-201 (Figure.1). Only two of which codify for a protein, i.e. EEF1G-001 and EEF1G-201, while the others are non-coding RNA sequences (ncRNAs), classified as processed transcripts, i.e. nucleotide sequences that do not contain an open reading frame (ORF) and alternatively spliced transcripts, i.e. retained intron sequences. Furthermore, there is a potential readthrough with the inclusion of TUT1 gene.
VariantNameRefSeq (1)Transcript IDExonsTypeLenght (bp)RefSeq (2) Lenght (aa)
1EEF1G-001NM_001404.5-10Protein coding1446NP_001395.1437
2EEF1G-002 (EEF1G-203)AK092787.1ENST00000525340.59Retained intron2496--
3EEF1G-003 (EEF1G-204)-ENST00000532986.15Processed transcript578--
4EEF1G-004 (EEF1G-202)-ENST00000524420.55Processed transcript557--
5EEF1G-201AK300203.1-10Protein coding1631BAG61974.1487

Table.1. Splice variants of EEF1G gene (reworked from


According to Entrez Gene, the analysis of the human genome revealed the presence of nine pseudogenes for EEF1G (Table.2) classified as processed pseudogenes and probably originated by retrotransposition. If these elements have any regulatory roles on the expression of the respective gene as described for others (Hirotsune et al., 2003), is only speculation in the absence of experimental evidence.
GeneGene  nameGene IDRefSeqLocusLocationStartEndLenght (nt)
EEF1GP1  EEF1G1 Pseudogene 1  646837  NC_000007.14  Chromosome 7  7q31.33  125033433  125035389  1957
EEF1GP2  EEF1G1 Pseudogene 2  100130260  NC_000005.10  Chromosome 5  5q32  147922182  147923422  1241
EEF1GP3  EEF1G1 Pseudogene 3  651628  NC_000003.12  Chromosome 3  3p22.1  40596122  40597519  1398
EEF1GP4  EEF1G1 Pseudogene 4  100129403  NC_000003.12  Chromosome 3  3q26.1  161324837  161326238  1402
EEF1GP5  EEF1G1 Pseudogene 5  642357  NC_000023.11  Chromosome X  Xq23  115702791  115704195  1405
EEF1GP6  EEF1G1 Pseudogene 6  100421733  NC_000006.12  Chromosome 6  6q16.1  96750800  96751728  929
EEF1GP7  EEF1G1 Pseudogene 7  645311  NC_000001.11  Chromosome 1  1p32.3  52573115  52573818  704
EEF1GP8  EEF1G1 Pseudogene 8  391698  NC_000004.12  Chromosome 4  4q28.2  129903001  129904244  1244
LOC729998  EEF1G1 Pseudogene 9  729998  NC_000007.14  Chromosome 7  7q33  133034515  133035940  1426

Table.2 EEF1G pseudogene (reworked from



Are described two isoforms for eEF1G and it is shown that this protein has a glutathione S-transferase activity. In addition, eEF1G is a structural constituent of a more greater protein complex that is in relation to the ribosome and plays a role in the elongation step of protein synthesis.
Atlas Image
Figure.2 eEF1G protein structure analysis. (1) Primary structure of eEF1G with emphasis on its three principal domains (reworked from Achilonu et al.,2014;;;; (2) Secondary structure (from; (3) Tertiary structure: above, front view and below, top view (from


The eukaryotic elongation factor 1-gamma (alias eEF1G, eEF1γ, heEF1γ, eEF1Bγ) is a subunit of the macromolecular eukaryotic elongation factor-1 complex (alias eEF1, also called eEF1H), a high-molecular-weight form made up of an aggregation of different protein subunits: eEF1A (alias eEF1α), eEF1B (alias eEF1 β, eEF1Bα, eEF1B2), eEF1G, eEF1D (alias eEF1δ, eEF1Bδ) and valyl t-RNA synthetase (valRS). eEF1H protein complex plays central roles in peptide elongation during eukaryotic protein biosynthesis, in particular for the delivery of aminoacyl-tRNAs to ribosome mediated by the hydrolysis of GTP. In fact, during the translation elongation step, the inactive GDP-bound form of eEF1A (eEF1A-GDP) is converted to its active GTP-bound form (eEF1A-GTP) by eEF1BGD complex-mediated GTP hydrolysis so it acts as a guanine nucleotide exchange factor (GEF), regenerating eEF1A-GTP for the successive elongation cycle. The physiological role of eEF1G in the translation context is still not well defined, however eEF1G seems to be necessary for this nucleotide exchange. Studies did not confirm its direct involvement in this process but it is supposed that it may stimulate the activity of eEF1B and guarantee stability to entire eEF1H complex (Ejiri, 2002; Mansilla et al., 2002). In addition, studies revealed that eEF1G sequence does not contain any consensus sequence for ATP or GTP binding (Maessen et al., 1987).
There are known two isoforms produced by alternative splicing: the isoform 1 (RefSeq NP_001395.1; UniParc, P26641-1), that has been chosen as the canonical sequence, is formed by 437 residues and has an overall molecular weight of 50.12 kDa, while the isoform 2 (RefSeq BAG61974.1; UniParc, P26641-2) is 487 amino acids long with 56.15 kDa of molecular weight. The sequence of this isoform differs from the canonical sequence for the substitution of the first four amino acids (MAAG) by the insertion of other fifty residues (MAERWVAPAVLRRARFASTFFLSPQIYAHKDGDLRSAFFILSFKRGEFIPFLNW) with the creation of an alternative amino acid sequence (Ota et al., 2004). No experimental data or other studies were performed for this isoform, so its biological role is totally unknown.
eEF1G shown hydrophobic properties, has a relatively high isoelectric point (pI ≈ 7) (van Damme et al., 1991) and the analysis of its primary and secondary structures revealed some interesting characteristics. In fact, it is a multi-domain protein which consists of three main domains: from the amino to carboxyl half terminal there are a glutathione S-transferase (GST)-like N-terminus domain (NT-eEF1G), a glutathione S-transferase (GST)-like C-terminus domain (CT-eEF1G) and a conserved C-terminal domain (CD-eEF1G) (Achilonu et al.,2014). NT-eEF1G and CT-eEF1G domains show a homology to the theta class of glutathione S-transferases (GSTs) (Koonin et al., 1994; Janssen and Möller, 1988).
The NT-eEF1G domain of eEF1G, by using secondary structure prediction algorithms, seems to have a predominant α-helix secondary structure (Achilonu et al.,2014) and it was demonstrated that interacts directly with the N-terminal domain of eEF1B (van Damme et al., 1991) and also with the N-terminal domain of eEF1D in independent manner (Cao et al., 2014; Mansilla et al., 2002; Janssen et al., 1994), although different interactional models were proposed (Le Sourd et al., 2006; Jiang et al.,2005; Sheu and Traugh, 1999; Minella et al., 1998). It does not seem to have a direct interaction with other eEF1H elements. In addition, the presence of an enzymatically active GST element could be involved in detoxification of oxygen radicals and the over-expression of eEF1G in cancer cells could influence their response to oxidative stress and their aggressiveness (Koonin et al., 1994).
The calculated secondary structure of the CT-eEF1G domain of eEF1G shows both α-helix and β-strand secondary structure elements (Achilonu et al.,2014) and does not interact with eEF1B but instead is the candidate domain to has transient interactions with other proteins or cell structures.
The CD-eEF1G domain of eEF1G seems to be mostly in α-helix secondary structure with few β-strands (Achilonu et al.,2014) and currently it does not show particular elements or interactions.
It is interesting that eEF1G shows two internal repeats of eight amino acids (VFGEXNXS) at positions 35 - 42 and 355 - 362 respectively, that are located in its amino-terminal and carboxy-terminal halves. The roles of these two octapeptides are still unknown even if they could cover the function of binding-sites (van Damme et al., 1991; Maessen et al., 1987).
eEF1G seems to have in human cells a dimeric nature, forming homodimers, while in rabbit shows a trimeric nature and in yeast was observed that it acts as a monomer (Achilonu et al.,2014; Koonin et al., 1994). Furthermore, it has hydrophobic properties that enable it to attach to membranes (Mansilla et al., 2002).
eEF1G interacts mainly with EEF1B2 and EEF1D, even if other interactions are documented in protein databases and in literature, i.e. with the histidyl-tRNA synthetase ( HARS), leucyl-tRNA synthetase ( LARS), cysteine-tRNA synthetase ( CARS), leucine zipper putative tumor suppressor 1 ( LZTS1), enoyl-CoA hydratase 1( ECH1), plasminogen receptor ( PLGRKT), small ubiquitin-related modifier 2 ( SUMO2), ATP-binding cassette sub-family C member 9 ( ABCC9), tripartite motif containing 55 ( TRIM55), E3 ubiquitin-protein ligase ( TRIM63), interleukin enhancer binding factor 2 ( ILF2), vascular cell adhesion protein 1 ( VCAM1), eukaryotic translation elongation factor 1 delta pseudogene 3 ( EEF1DP3), RNA-binding protein 6 ( RBM6) (HuRI database -, ATP-dependent DNA helicase Q5 ( RECQL5) and fasciculation and elongation protein zeta 1 ( FEZ1)(Ishii et al., 2001) although the nature of these interactions are poorly understood.
Post-translational modifications. Some post-translational modifications are observed, such as phosphorylation, acetylation and S-nitrosylation.
1) Phosphorylation: it was demonstrated that eEF1G is a target of the kinases, in particular the cell cycle protein kinase CDK1 /cyclin B (Le Sourd et al., 2006; Mansilla et al., 2002). There are at least four positions for phosphorylation: two on threonine residues (T43, T230) and two on serine residues (S286, S406) (Olsen et al., 2010; It is assumed that these phosphorylations play a regulatory role, but their exact functional significance is poorly understood.
2) Acetylation: there are three positions for acetylation on lysine residues (K132, K147, K434) (Choudhary et al., 2009;
3) S-nitrosylation: there is one most probable position for S-Nitrosylation on a cysteine residue (C194) (Han and Chen, 2008;
Atlas Image
Figure 3. Translation elongation mechanism. The active form of eukaryotic elongation factor 1 (eEF1A) in complex with GTP delivers an aminoacylated tRNA to the A site of the ribosome. Following the proper codon-anticodon recognition the GDP is hydrolyzed and the inactive eEF1A-GDP is released from the ribosome and then it is bound by eEF1B2GD complex forming the macromolecular protein aggregate eEF1H. eEF1H is formed previously by the binding of three subunits: eEF1B2, eEF1G and eEF1D. This complex promotes the exchange between GDP and GTP to regenerate active form of eEF1A (reworked from Dongsheng et al., 2013; Ejiri, 2002; Riis et al, 1990;


EEF1G mRNA is expressed widely as previous reported while the presence of eEF1G protein in human tissues shows unexpected differences i.e. higher levels of protein are observed in cerebellum, hippocampus, esophagus, stomach, small intestine and pancreas while its low expression levels are reported in oral mucosa, bronchus, lung, parathyroid glands, adrenal glands, smooth muscle, prostate and urinary bladder. No protein presence is found in bone marrow, heart muscle, kidney, liver and skeletal muscle (Fagerberg et al., 2014). Furthermore was revealed the presence of the protein both in the human physiological secretions (cerumen, saliva, milk, urine, seminal plasma) and in pathological intercellular fluids (ascites) (
The expression pattern in cell lines tested for its presence is similar and without significantly differences except in one study that revealed a higher expression in human embryonic kidney HEK293 cell line and in human liver hepatocellular carcinoma HepG2 cell line (Cao et al, 2014).


eEF1G is located mostly in the cytoplasm where forming a gradient from the nucleus to the periphery of the cell, but some studies find it also in cellular nucleus, nucleolus, mitochondria and in relation with endoplasmic reticulum and plasma membrane (Cho et al., 2003; Minella et al., 1996; Sanders et al., 1996). It was reported also its localization in extracellular exosomes (Principe et al., 2013).


eEF1G shows canonical functions and multiple non-canonical roles (moonlighting roles) inside the cell.
Canonical function: eEF1G binds to eEF1B and eEF1D and is supposed that its primary role may be to ensure the proper scaffolding and stability of its binding partners in the eEF1BDG macromolecular complex and then it could anchors the entire EF1H complex to the endoplasmic reticulum together with the ribosome (Mansilla et al., 2002; Janssen et al., 1994). However, the complete significance of the role of human eEF1G remains unknown and needs to be more studied.
Non-canonical roles: eEF1G has shown to interact with cytoskeleton, RNA polymerase II, TNF receptor-associated protein 1 ( TRAP1) and membrane-bound receptors. In addition, it was observed that it has mRNA binding properties and it is a positive regulator of NF-kB signaling pathway.
1) eEF1G and cytoskeleton: it was discovered that eEF1G is a structural component of the cytoskeleton (Coumans et al., 2014), in fact it can bind both keratin intermediate filaments (Kim et al., 2017) and the tubulin (Janssen and Möller, 1988). This suggests that it may have an influence on cytoskeletal architecture, cell morphology and motility, but these implications and the roles of these bindings are still need to clarify.
2) eEF1G and interaction with RNA polymerase II: it physically interacts with RNA polymerase II (pol II) core subunit 3 ( POLR2C), both in isolation and in the context of the holo-enzyme (Corbi et al., 2010).
3) interaction between eEF1G and TNF receptor-associated protein 1 (TRAP1): TRAP1 is the main mitochondrial member of the heat shock protein (HSP) 90 family and it was revealed that there is an interaction between this protein and some members of eEF1H complex, including eEF1G. The role of the interaction between eEF1G and TRAP1 is related to the translational control (Matassa et al., 2013) and maybe also in the protection to oxidative stress (Pisani et al., 2016).
4) eEF1G and membrane-bound receptors (dopamine D3 receptor): it was observed that there is an interaction between eEF1G and dopamine D3 receptor ( DRD3) and that they have a co-localization on the plasma membrane. This interaction involve also eEF1B subunit after its protein kinase-mediated phosphorylation on its serine residues. eEF1G acts as a bridge for the relation between eEF1B and DRD3 and these three factors together forming a new macromolecular complex on the plasma membrane that obviously play some roles even if its functional meaning is still understood (Cho et al., 2003).
5) mRNA binding properties: the presence of eEF1G was detected on the genomic locus corresponding to the promoter region of human vimentin gene VIM and this permits to suppose that eEF1G regulates vimentin gene by contacting both pol II and the vimentin promoter region. In addition was shown that it can bind to 3UTR of vimentin mRNA and so it can shuttling/nursing the vimentin mRNA from its gene locus to its appropriate cellular compartment for translation. In fact, depletion of eEF1G causes the incorrect compartmentalizing of the vimentin protein and seriously compromise cellular shape and mitochondria localization (Corbi et al., 2010). Furthermore, was shown that eEF1G can bind also AATF (Che-1) and transcription and their promoter regions (Pisani et al., 2016).
6) regulation of NF-kB signaling pathway: eEF1G can binds to the CARD domain of mitochondrial antiviral-signaling protein ( MAVS) and thus significantly promotes the activities of transcription factor NF-kB functioning as its positive regulator. The discover offers a new regulating mechanism of the antiviral responses that promotes the downstream pro-inflammatory cytokines CXCL8 (interleukin-8 (IL8)) and interleukin-6 ( IL6) (Liu et al., 2014).


eEF1G is highly and abundant conserved in many species, with sometimes the lack of NT-eEF1G domain. The homology for eEF1G protein between species is reported in Table.3
Organism (1)  Organism (2)  Symbol   Similarity (%)
Human  H.sapiens  eEF1G  100
Chimpanzee  P.troglodytes  eEF1G  100
Gorilla  G.gorilla gorilla  eEF1G  99
Cat  Felis catus  eEF1G  99
Mouse   M.musculus  eEF1G  98
Rat  R.norvegicus  eEF1G  98
Zebrafish  D.rerio  eEF1G  75
Drosophila  D.melanogaster  Ef1gamma  58
 Caenorhabditis   C.elegans  F17C11.9  52
Yeast  S.cerevisiae  TEF4  38

Table.3 eEF1G homology (reworked from;



The great number of mutations in the genomic sequence or in the amino acid sequence for EEF1G was discovered in cancer cells that are obviously genetically more unstable respect normal cells. The genomic alterations observed include the formation of novel fusion genes as EBF3/EEF1G, EEF1G/ALK, EEF1G/ENG, EEF1G/GFAP, EEF1G/MTA2, EEF1G/MYH9, EEF1G/NXF1, EEF1G/OOEP [t(6;11)(q13;q12) EEF1G/OOEP], EEF1G/PPP6R3 [t(11;11)(q12;q13) EEF1G/PPP6R3], EEF1G/TOX2, EEF1G/UBXN1, ETFB/EEF1G, HNRNPUL2/EEF1G, IGHG1/EEF1G, IGHM/EEF1G and NCEH1/EEF1G (Klijn et al., 2015;;, however there are no experimental data yet to understand the repercussions on cellular behavior and so the implications in cancer of these fusion genes are unclear. There is one chromosomic translocations with production of a novel fusion gene that is more investigated and it is t(2;11)(p23;q12.3) EEF1G/ALK.

Implicated in

Top note
High expression levels of eEF1G are observed in many cancer types and, clinically, the overexpression of EEF1G was correlated with a poor or better prognosis of cancers in relation to a specific cancer type (Hassan et al., 2018). It is unclear if EFF1G overexpression concurs to the tumoral process or it is a simply consequence and when it occurs the mechanism of overexpression of EEF1G is not known (Frazier et al., 1998). In addition, was observed a few translocations with creation of fusion genes with other proteins in some cancer cell types.
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Anaplastic lymphoma kinase (ALK)-positive anaplastic large cell lymphoma (ALCL) is characterized by many genomic aberrations and chromosomal rearrangements that make the cellular caryotype much complicated. There are revealed many ALK aberrations and rearrangements with several variant of partner fusion genes (van der Krogt et al., 2017; van Krieken, 2017).
The prognosis is very poor, in fact patients expressing EEF1G/ALK fusion gene have shown an unfavorable clinical course with fatal outcome.
Hybrid gene
It was observed in some ALK+ ALCL pediatric patients the presence of an in-frame fusion transcript between an intronic region among exons 8 and 9 of EEF1G with the middle part of exon 20 of ALK. The resulting novel fusion chimeric gene 5EEF1G / 3ALK was revealed to be a coding-gene (van der Krogt et al., 2017). On the contrary, other authors found a fusion gene originated by the fusion of exon 6 of EEF1G with the exon 20 of ALK (Palacios et al., 2017).
Fusion protein
The chimeric protein eEF1G/ALK is active and has the complete GST-like N-terminal domain and part of the CT domain of EEF1G fused to the complete intracellular protein tyrosine kinase (PTK) domain of ALK. Cytoplasm is the subcellular localization for this chimera (van der Krogt et al., 2017; van Krieken, 2017) but its biological activities, its oncogenic potential and its roles in proliferation and cancer aggressiveness are still poor understood although it is supposed that eEF1G/ALK fusion protein has a cell-transforming activity due to the activation of ALK kinase (Palacios et al., 2017).
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Acute myeloid leukemia (AML)
Acute myeloid leukemia (AML) is the most common and severe form of acute leukemia diagnosed in adults. EEF1G was find over-expressed in AML-M1 and AML-M2 samples from adult patients (Handschuh et al, 2017).
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Brain and central nervous system (CNS) cancer
EEF1G mRNA levels are significantly upregulated in brain and CNS cancers. It is found over-expressed in glioblastoma and glioma, however higher levels of expression are found also in low-risk patients, so this can predict favourable survival outcome (Hassan et al., 2018). On the contrary, another study observed a down-regulation of EEF1G in glioblastoma multiform (Vastrad and Vastrad, 2018).
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Breast Cancer
High expression of EEF1G is observed in breast cancer cells and also in peripheral blood samples of breast cancer patients respect to healthy subjects (Coumans et al., 2014 ; Aarøe et al., 2010), although other studies shown that it is down-regulated and instead an increase of EEF1G transcript levels have positive correlation with distant metastasis free survival (DMFS) and relapse free survival (RFS) and so seems that over-expression of EEF1G is correlated with a significantly good prognosis in luminal A subtype (Hassan et al., 2018). EEF1G is considered a negative marker for ERPR positive breast cancer (Tyanova et al., 2016).
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Cervical carcinoma
EEF1G is observed to be highly expressed in cervical intraepithelial neoplasia (Shadeo et al., 2008).
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Colorectal cancer
EEF1G is over-expressed by twofold to tenfold in a great percentage of colorectal adenomas and by twofold to 26-fold in the colorectal carcinoma compared to normal tissue and also its relative protein eEF1G was found over-expressed, suggesting that early modification of its expression levels occurs and so it may be a useful marker for the detection of an early stage of tumor development (Frazier et al., 1998; Ender et al., 1993; Chi et al., 1992 ; Mathur et al., 1988).
The overexpression of eEF1G in the colorectal cancers seems to be not due to gene amplification, genome rearrangements or an increase in the number of cycling cells (Frazier et al., 1998).
Interestingly is the positive correlation that was found in this cancer type between co-expression levels of TNF Receptor Associated Protein 1 (TRAP1) and eEF1G: the majority of the TRAP1-positive tumors exhibit an upregulation of eEF1G and, on the contrary, tumors with low expression of TRAP1 also exhibit low levels of expression of eEF1G (Matassa et al., 2013). This evidence may have an interesting significance in the increase or decrease of tumor aggressiveness and in the development of new anti-cancer strategies. Moreover, the reduction of expression levels of eEF1G in high-risk patients can predict poor survival (Hassan et al., 2018).
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Esophageal carcinoma
eEF1G is overexpressed in only a minimum part of esophageal carcinoma tissues examined respect normal counterpart and there is not any evidence between its expression level and the growth rates of tumor. However, cancers over-expressing eEF1G show more aggressiveness and show a more metastatic behavior respect cancer cells that not overexpressing this gene. On the contrary, eEF1G is over-expressed in all esophageal cancer cell lines tested (Frazier et al., 1998; Mimori et al., 1996).
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Gastric cancer
EEF1G was found significantly overexpressed in low-grade gastric adenomas (Takenawa et al., 2004) while on the contrary in another study was observed that its expression level is down-regulated in gastric cancer cells and that higher levels of its expression could predict a poor overall survival (OS) and first progression (FP)(Hassan et al., 2018). Other authors found not only an overexpression of this gene in gastric carcinomas but also that tumors overexpressing EEF1G have more vascular permeation/angiogenesis than the others (Frazier et al., 1998; Mimori et al., 1995). This evidence is very significant and could be suppose that an overexpression of EEF1G may be compatible with more aggressiveness of the gastric cancer cells that show a higher expression levels for this protein.
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Head and neck squamous cell carcinoma
mRNA levels of EEF1G are downregulated in tumor tissues than normal but in high-risk patients these levels become significantly higher (Hassan et al., 2018).
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Kidney cancer
EEF1G expression level is significantly upregulated in kidney clear cell carcinoma. These high expression levels may predict better survival in low-risk patients (Hassan et al., 2018).
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Liver cancer
mRNA levels of EEF1G are significantly upregulated in liver cancer cells respect normal ones and this may predict worse survival in high-risk patients (Hassan et al., 2018 ; Wang et al., 2009). In particular, mRNA expression levels of EEF1G remain at basal levels in a well to moderately differentiated (W/M-) primary human hepatocellular carcinoma (HCC), while they are further up-regulated in moderately to poorly differentiated (M/P-) HCC according their histological grading (Shuda et al, 2000). In contrast, in vitro studies on cell cultures of HBV- or HCV-HCC have shown in most cases a down-regulation of EEF1G expression levels (Yoon et al., 2006).
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Lung cancer
The expression levels of EEF1G are slightly higher in lung cancer cells respect normal ones and this lead to poor overall survival (OS) and first progression (FP) in lung cancer and thus are significantly correlated with worse survival outcome in lung adenocarcinoma (Hassan et al., 2018). In addition, from a preliminary study was observed an EEF1G differential expression between stage I from stage II lung squamous carcinoma: in the second EEF1G has high expression levels and this may be one of the causes of the increase of grade of malignancy. However, other investigations are needed to confirm this preliminary evidence (Wang et al., 2018).
Hybrid gene
In squamous cell carcinoma of the lung was discovered the fusion gene t(11;11)(q12;q13) EEF1G/PPP6R3 (Hammerman et al., 2012).
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EEF1G is significant overexpressed in Burkitts lymphoma and diffuse large B-Cell Lymphoma (Hassan et al., 2018).
Hybrid gene
In acute lymphoblastic leukemia/lymphoblastic lymphoma was discovered the fusion gene t(6;11)(q13;q12) EEF1G/OOEP (Atak et al., 2013) and the presence of translocation t (2;11)(p23; q12.3) EEF1G/ALK was observed in pediatric anaplastic lymphoma kinase (ALK)-positive anaplastic large cell lymphoma (ALCL).
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EEF1G gene is relevantly co-expressed with other genes in melanoma subtype 6 (Gan et al., 2018).
Hybrid gene
5EEF1G /3NXF1 fusion gene is observed in skin cutaneous melanoma (
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EEF1G is significant overexpressed in myeloma cells in the bone marrow of multiple myeloma patients (Sariman et al., 2019).
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Ovarian cancer
High expression of EEF1G is found in ovarian cancer and this may predict a better overall survival (OS) and progression-free survival (PFS)(Hassan et al., 2018).
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Pancreatic cancer
From collected data seem to be no significantly difference between the expression levels of EEF1G in pancreatic cancer cells compared with normal ones (Hassan et al., 2018), however in some studies were evidenced that EEF1G is over-expressed (Frazier et al., 1998 ; Chi et al., 1992 ; Lew et al., 1992). The presence of a higher level of its expression may become a marker of poor survivability for high-risk patients (Hassan et al., 2018).
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Pleomorphic adenoma of the human parotid gland
There is one study in which were found down-expressed levels for this gene (Mutlu et al., 2017).
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Prostate cancer
A significant overexpression of EEF1G is seen in prostate tumor tissues although this evidence seems not to affect the survival outcomes (Hassan et al., 2018). Remarkable is the discovery of presence of eEF1G in exosomes contained in expressed prostatic secretions (EPS) that could be utilized as diagnostic and/or prognostic markers for prostate cancer (Principe et al., 2013).


Pubmed IDLast YearTitleAuthors
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243672742013Comprehensive analysis of transcriptome variation uncovers known and novel driver events in T-cell acute lymphoblastic leukemia.Atak ZK et al
229607452012Comprehensive genomic characterization of squamous cell lung cancers.
254366082014Characterisation of translation elongation factor eEF1B subunit expression in mammalian cells and tissues and co-localisation with eEF1A2.Cao Y et al
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145194482003Direct and biochemical interaction between dopamine D3 receptor and elongation factor-1Bbetagamma.Cho DI et al
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Other Information

Locus ID:

NCBI: 1937
MIM: 130593
HGNC: 3213
Ensembl: ENSG00000254772


dbSNP: 1937
ClinVar: 1937
TCGA: ENSG00000254772


Gene IDTranscript IDUniprot

Expression (GTEx)



PathwaySourceExternal ID
Metabolism of proteinsREACTOMER-HSA-392499
Eukaryotic Translation ElongationREACTOMER-HSA-156842
Gene ExpressionREACTOMER-HSA-74160

Protein levels (Protein atlas)

Not detected


Pubmed IDYearTitleCitations
212178132010The eEF1γ subunit contacts RNA polymerase II and binds vimentin promoter region.10
278404232017Novel ALK fusion in anaplastic large cell lymphoma involving EEF1G, a subunit of the eukaryotic elongation factor-1 complex.4
276398462016eEF1Bγ binds the Che-1 and TP53 gene promoters and their transcripts.2


Luigi Cristiano

EEF1G (Eukaryotic translation elongation factor 1 gamma)

Atlas Genet Cytogenet Oncol Haematol. 2019-03-01

Online version: