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EEF1G (Eukaryotic translation elongation factor 1 gamma)

Written2019-03Luigi Cristiano
Aesthetic and medical biotechnologies research unit, Prestige, Terranuova Bracciolini, Italy;

Abstract 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.

Keywords EEF1G; Eukaryotic translation elongation factor 1 gamma; Translation; Translation elongation factor; protein synthesis; cancer; oncogene; cancer marker

(Note : for Links provided by Atlas : click)


Alias (NCBI)EF1G
EEF-1B Gamma
Elongation Factor 1-Gamma
Translation Elongation Factor EEF-1 Gamma Chain
Pancreatic Tumor-Related Protein
HGNC Alias symbEF1G
LocusID (NCBI) 1937
Atlas_Id 54272
Location 11q12.3  [Link to chromosome band 11q12]
Location_base_pair Starts at 62559596 and ends at 62573891 bp from pter ( according to GRCh38/hg38-Dec_2013)  [Mapping EEF1G.png]
Fusion genes
(updated 2017)
Data from Atlas, Mitelman, Cosmic Fusion, Fusion Cancer, TCGA fusion databases with official HUGO symbols (see references in chromosomal bands)


  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;;
Description 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.
Transcription EEF1G mRNA is 1446 bp long with a reference sequence reported in GeneBank as NM_001404.5. The 5'UTR sequence is not very long and counts 49 nt. The CDS is extended from 50 to 1363 nt, while the 3'UTR 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
Pseudogene 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


Note 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.
  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
Description 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;
  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;
Expression 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).
Localisation 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).
Function 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 3'UTR 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).
Homology 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;


Note 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

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.
Entity EEF1G/ ALK
Disease (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).
Prognosis The prognosis is very poor, in fact patients expressing EEF1G/ALK fusion gene have shown an unfavorable clinical course with fatal outcome.
Hybrid/Mutated 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 5'EEF1G / 3'ALK 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).
Abnormal 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).
Entity Acute myeloid leukemia (AML)
Note 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).
Entity Brain and central nervous system (CNS) cancer
Note 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).
Entity Breast Cancer
Note 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).
Entity Cervical carcinoma
Note EEF1G is observed to be highly expressed in cervical intraepithelial neoplasia (Shadeo et al., 2008).
Entity Colorectal cancer
Note 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).
Entity Esophageal carcinoma
Note 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).
Entity Gastric cancer
Note 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.
Entity Head and neck squamous cell carcinoma
Note 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).
Entity Kidney cancer
Note 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).
Entity Liver cancer
Note 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).
Entity Lung cancer
Note 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/Mutated Gene In squamous cell carcinoma of the lung was discovered the fusion gene t(11;11)(q12;q13) EEF1G/PPP6R3 (Hammerman et al., 2012).
Entity Lymphoma
Note EEF1G is significant overexpressed in Burkitt's lymphoma and diffuse large B-Cell Lymphoma (Hassan et al., 2018).
Hybrid/Mutated 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).
Entity Melanoma
Note EEF1G gene is relevantly co-expressed with other genes in melanoma subtype 6 (Gan et al., 2018).
Hybrid/Mutated Gene 5'EEF1G /3'NXF1 fusion gene is observed in skin cutaneous melanoma (
Entity Multiple myeloma
Note EEF1G is significant overexpressed in myeloma cells in the bone marrow of multiple myeloma patients (Sariman et al., 2019).
Entity Ovarian cancer
Note 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).
Entity Pancreatic cancer
Note 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).
Entity Pleomorphic adenoma of the human parotid gland
Note There is one study in which were found down-expressed levels for this gene (Mutlu et al., 2017).
Entity Prostate cancer
Note 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).

To be noted

Roles of eEF1G in viral replication and pathogenesis
eEF1G is an abundant cellular resource that seems to play an important role in the genomic replication, DNA synthesis, transcription and in the pathogenesis of a variety of viruses, such as HIV-1 and influenza A virus, by interacting with viral polymerases, structural and nonstructural proteins, and viral genome. When eEF1G is downregulated using a small interfering RNA (siRNA) also the viral replication is negatively affected and becomes more unstable and less efficient. However, the molecular interaction between the virus components and eEF1G or other translation factors remains to be determined (Sammaibashi et al., 2018; Dongsheng et al., 2013 ; Warren et al., 2012).
Reduction of cell viability after causing the down-regulation by RNAi
The knockdown of eEF1G subunit by a specific siRNA shown a slightly reduced cell viability/cell metabolism. In addition, was observed that its depletion can affect the expression of the eEF1B and eEF1D subunits (Cao et al., 2014).
Down-regulation of EEF1G in response to enterovirus 71 (EV71) infection.
The transcriptomic and proteomic analyses of the rhabdomyosarcoma cells infected by enterovirus 71 (EV71) has revealed a change in gene expression profiles of several genes in response to infection. In particular, was observed the down-regulation of EEF1G (Leong and Chow, 2006) although its significance remain unclear.


Gene expression profiling of peripheral blood cells for early detection of breast cancer
Aarøe J, Lindahl T, Dumeaux V, Saebø S, Tobin D, Hagen N, Skaane P, Lönneborg A, Sharma P, Børresen-Dale AL
Breast Cancer Res 2010;12(1):R7
PMID 20078854
Purification and characterisation of recombinant human eukaryotic elongation factor 1 gamma
Achilonu I, Siganunu TP, Dirr HW
Protein Expr Purif 2014 Jul;99:70-7
PMID 24732582
Comprehensive analysis of transcriptome variation uncovers known and novel driver events in T-cell acute lymphoblastic leukemia
Atak ZK, Gianfelici V, Hulselmans G, De Keersmaecker K, Devasia AG, Geerdens E, Mentens N, Chiaretti S, Durinck K, Uyttebroeck A, Vandenberghe P, Wlodarska I, Cloos J, Foà R, Speleman F, Cools J, Aerts S
PLoS Genet 2013;9(12):e1003997
PMID 24367274
Comprehensive genomic characterization of squamous cell lung cancers
Cancer Genome Atlas Research Network
Nature 2012 Sep 27;489(7417):519-25
PMID 22960745
Characterisation of translation elongation factor eEF1B subunit expression in mammalian cells and tissues and co-localisation with eEF1A2
Cao Y, Portela M, Janikiewicz J, Doig J, Abbott CM
PLoS One 2014 Dec 1;9(12):e114117
PMID 25436608
Expression of an elongation factor 1 gamma-related sequence in adenocarcinomas of the colon
Chi K, Jones DV, Frazier ML
Gastroenterology 1992 Jul;103(1):98-102
PMID 1612363
Direct and biochemical interaction between dopamine D3 receptor and elongation factor-1Bbetagamma
Cho DI, Oak MH, Yang HJ, Choi HK, Janssen GM, Kim KM
Life Sci 2003 Oct 24;73(23):2991-3004
PMID 14519448
Lysine acetylation targets protein complexes and co-regulates major cellular functions
Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M
Science 2009 Aug 14;325(5942):834-40
PMID 19608861
The eEF1γ subunit contacts RNA polymerase II and binds vimentin promoter region
Corbi N, Batassa EM, Pisani C, Onori A, Di Certo MG, Strimpakos G, Fanciulli M, Mattei E, Passananti C
PLoS One 2010 Dec 31;5(12):e14481
PMID 21217813
Green fluorescent protein expression triggers proteome changes in breast cancer cells
Coumans JV, Gau D, Poljak A, Wasinger V, Roy P, Moens P
Exp Cell Res 2014 Jan 1;320(1):33-45
PMID 23899627
Moonlighting functions of polypeptide elongation factor 1: from actin bundling to zinc finger protein R1-associated nuclear localization
Ejiri S
Biosci Biotechnol Biochem 2002 Jan;66(1):1-21
PMID 11866090
Overexpression of an elongation factor-1 gamma-hybridizing RNA in colorectal adenomas
Ender B, Lynch P, Kim YH, Inamdar NV, Cleary KR, Frazier ML
Mol Carcinog 1993;7(1):18-20
PMID 8382068
Analysis of the human tissue-specific expression by genome-wide integration of transcriptomics and antibody-based proteomics
Fagerberg L, Hallström BM, Oksvold P, Kampf C, Djureinovic D, Odeberg J, Habuka M, Tahmasebpoor S, Danielsson A, Edlund K, Asplund A, Sjöstedt E, Lundberg E, Szigyarto CA, Skogs M, Takanen JO, Berling H, Tegel H, Mulder J, Nilsson P, Schwenk JM, Lindskog C, Danielsson F, Mardinoglu A, Sivertsson A, von Feilitzen K, Forsberg M, Zwahlen M, Olsson I, Navani S, Huss M, Nielsen J, Ponten F, Uhlén M
Mol Cell Proteomics 2014 Feb;13(2):397-406
PMID 24309898
Few point mutations in elongation factor-1gamma gene in gastrointestinal carcinoma
Frazier ML, Inamdar N, Alvula S, Wu E, Kim YH
Mol Carcinog 1998 May;22(1):9-15
PMID 9609096
Identification of cancer subtypes from single-cell RNA-seq data using a consensus clustering method
Gan Y, Li N, Zou G, Xin Y, Guan J
BMC Med Genomics 2018 Dec 31;11(Suppl 6):117
PMID 30598115
Detergent-free biotin switch combined with liquid chromatography/tandem mass spectrometry in the analysis of S-nitrosylated proteins
Han P, Chen C
Rapid Commun Mass Spectrom 2008 Apr;22(8):1137-45
PMID 18335467
Gene expression profiling of acute myeloid leukemia samples from adult patients with AML-M1 and -M2 through boutique microarrays, real-time PCR and droplet digital PCR
Handschuh L, Kamierczak M, Milewski MC, Góralski M, uczak M, Wojtaszewska M, Uszczyńska-Ratajczak B, Lewandowski K, Komarnicki M, Figlerowicz M
Int J Oncol 2018 Mar;52(3):656-678
PMID 29286103
The expression profile and prognostic significance of eukaryotic translation elongation factors in different cancers
Hassan MK, Kumar D, Naik M, Dixit M
PLoS One 2018 Jan 17;13(1):e0191377
PMID 29342219
An expressed pseudogene regulates the messenger-RNA stability of its homologous coding gene
Hirotsune S, Yoshida N, Chen A, Garrett L, Sugiyama F, Takahashi S, Yagami K, Wynshaw-Boris A, Yoshiki A
Nature 2003 May 1;423(6935):91-6
PMID 12721631
FEZ1/LZTS1 gene at 8p22 suppresses cancer cell growth and regulates mitosis
Ishii H, Vecchione A, Murakumo Y, Baldassarre G, Numata S, Trapasso F, Alder H, Baffa R, Croce CM
Proc Natl Acad Sci U S A 2001 Aug 28;98(18):10374-9
PMID 11504921
The subunit structure of elongation factor 1 from Artemia
Janssen GM, van Damme HT, Kriek J, Amons R, Möller W
Why two alpha-chains in this complex? J Biol Chem 1994 Dec 16;269(50):31410-7
PMID 7989307
Three-dimensional reconstruction of the valyl-tRNA synthetase/elongation factor-1H complex and localization of the delta subunit
Jiang S, Wolfe CL, Warrington JA, Norcum MT
FEBS Lett 2005 Nov 7;579(27):6049-54
PMID 16229838
Interaction between the keratin cytoskeleton and eEF1Bgamma affects protein synthesis in epithelial cells
Kim S, Kellner J, Lee CH, Coulombe PA
Nat Struct Mol Biol 2007 Oct;14(10):982-3
PMID 17906640
A comprehensive transcriptional portrait of human cancer cell lines
Klijn C, Durinck S, Stawiski EW, Haverty PM, Jiang Z, Liu H, Degenhardt J, Mayba O, Gnad F, Liu J, Pau G, Reeder J, Cao Y, Mukhyala K, Selvaraj SK, Yu M, Zynda GJ, Brauer MJ, Wu TD, Gentleman RC, Manning G, Yauch RL, Bourgon R, Stokoe D, Modrusan Z, Neve RM, de Sauvage FJ, Settleman J, Seshagiri S, Zhang Z
Nat Biotechnol 2015 Mar;33(3):306-12
PMID 25485619
Eukaryotic translation elongation factor 1 gamma contains a glutathione transferase domain--study of a diverse, ancient protein superfamily using motif search and structural modeling
Koonin EV, Mushegian AR, Tatusov RL, Altschul SF, Bryant SH, Bork P, Valencia A
Protein Sci 1994 Nov;3(11):2045-54
PMID 7703850
eEF1B: At the dawn of the 21st century
Le Sourd F, Boulben S, Le Bouffant R, Cormier P, Morales J, Belle R, Mulner-Lorillon O
Biochim Biophys Acta 2006 Jan-Feb;1759(1-2):13-31
PMID 16624425
Transcriptomic and proteomic analyses of rhabdomyosarcoma cells reveal differential cellular gene expression in response to enterovirus 71 infection
Leong WF, Chow VT
Cell Microbiol 2006 Apr;8(4):565-80
PMID 16548883
Expression of elongation factor-1 gamma-related sequence in human pancreatic cancer
Lew Y, Jones DV, Mars WM, Evans D, Byrd D, Frazier ML
Pancreas 1992;7(2):144-52
PMID 1372736
The unexpected roles of eukaryotic translation elongation factors in RNA virus replication and pathogenesis
Li D, Wei T, Abbott CM, Harrich D
Microbiol Mol Biol Rev 2013 Jun;77(2):253-66
PMID 23699257
eEF1Bγ is a positive regulator of NF-B signaling pathway
Liu D, Sheng C, Gao S, Jiang W, Li J, Yao C, Chen H, Wu J, Chen S, Huang W
Biochem Biophys Res Commun 2014 Apr 4;446(2):523-8
PMID 24613846
Primary structure of elongation factor 1 gamma from Artemia
Maessen GD, Amons R, Zeelen JP, Möller W
FEBS Lett 1987 Oct 19;223(1):181-6
PMID 3666137
Mapping the human translation elongation factor eEF1H complex using the yeast two-hybrid system
Mansilla F, Friis I, Jadidi M, Nielsen KM, Clark BF, Knudsen CR
Biochem J 2002 Aug 1;365(Pt 3):669-76
PMID 11985494
Translational control in the stress adaptive response of cancer cells: a novel role for the heat shock protein TRAP1
Matassa DS, Amoroso MR, Agliarulo I, Maddalena F, Sisinni L, Paladino S, Romano S, Romano MF, Sagar V, Loreni F, Landriscina M, Esposito F
Cell Death Dis 2013 Oct 10;4:e851
PMID 24113185
Overexpression of elongation factor-1gamma protein in colorectal carcinoma
Mathur S, Cleary KR, Inamdar N, Kim YH, Steck P, Frazier ML
Cancer 1998 Mar 1;82(5):816-21
PMID 9486568
The overexpression of elongation factor 1 gamma mRNA in gastric carcinoma
Mimori K, Mori M, Tanaka S, Akiyoshi T, Sugimachi K
Cancer 1995 Mar 15;75(6 Suppl):1446-9
PMID 7889472
Major intracellular localization of elongation factor-1
Minella O, Mulner-Lorillon O, De Smedt V, Hourdez S, Cormier P, Bellé R
Cell Mol Biol (Noisy-le-grand) 1996 Sep;42(6):805-10
PMID 8891347
Proteomics analysis of pleomorphic adenoma of the human parotid gland
Mutlu A, Ozturk M, Akpinar G, Kasap M, Kanli A
Eur Arch Otorhinolaryngol 2017 Aug;274(8):3183-3195
PMID 28497265
Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis
Olsen JV, Vermeulen M, Santamaria A, Kumar C, Miller ML, Jensen LJ, Gnad F, Cox J, Jensen TS, Nigg EA, Brunak S, Mann M
Sci Signal 2010 Jan 12;3(104):ra3
PMID 20068231
Complete sequencing and characterization of 21,243 full-length human cDNAs
Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S
Nat Genet 2004 Jan;36(1):40-5
PMID 14702039
Novel ALK fusion in anaplastic large cell lymphoma involving EEF1G, a subunit of the eukaryotic elongation factor-1 complex
Palacios G, Shaw TI, Li Y, Singh RK, Valentine M, Sandlund JT, Lim MS, Mullighan CG, Leventaki V
Leukemia 2017 Mar;31(3):743-747
PMID 27840423
eEF1Bγ binds the Che-1 and TP53 gene promoters and their transcripts
Pisani C, Onori A, Gabanella F, Delle Monache F, Borreca A, Ammassari-Teule M, Fanciulli M, Di Certo MG, Passananti C, Corbi N
J Exp Clin Cancer Res 2016 Sep 17;35(1):146
PMID 27639846
In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine
Principe S, Jones EE, Kim Y, Sinha A, Nyalwidhe JO, Brooks J, Semmes OJ, Troyer DA, Lance RS, Kislinger T, Drake RR
Proteomics 2013 May;13(10-11):1667-1671
PMID 23533145
Eukaryotic protein elongation factors
Riis B, Rattan SI, Clark BF, Merrick WC
Trends Biochem Sci 1990 Nov;15(11):420-4
PMID 2278101
Strain-Specific Contribution of Eukaryotic Elongation Factor 1 Gamma to the Translation of Influenza A Virus Proteins
Sammaibashi S, Yamayoshi S, Kawaoka Y
Front Microbiol 2018 Jun 29;9:1446
PMID 30008712
Immunofluorescence studies of human fibroblasts demonstrate the presence of the complex of elongation factor-1 beta gamma delta in the endoplasmic reticulum
Sanders J, Brandsma M, Janssen GM, Dijk J, Möller W
J Cell Sci 1996 May;109 ( Pt 5):1113-7
PMID 8743958
Investigation of Gene Expressions of Myeloma Cells in the Bone Marrow of Multiple Myeloma Patients by Transcriptome Analysis
Sariman M, Abaci N, Sirma Ekmekçi S, akiris A, Perçin Paçal F, Üstek D, Ayer M, Yenerel MN, Bek S, efle K, Palandüz , Öztürk
Balkan Med J 2019 Jan 1;36(1):23-31
PMID 30079703
Up regulation in gene expression of chromatin remodelling factors in cervical intraepithelial neoplasia
Shadeo A, Chari R, Lonergan KM, Pusic A, Miller D, Ehlen T, Van Niekerk D, Matisic J, Richards-Kortum R, Follen M, Guillaud M, Lam WL, MacAulay C
BMC Genomics 2008 Feb 4;9:64
PMID 18248679
A structural model for elongation factor 1 (EF-1) and phosphorylation by protein kinase CKII
Sheu GT, Traugh JA
Mol Cell Biochem 1999 Jan;191(1-2):181-6
PMID 10094407
Enhanced expression of translation factor mRNAs in hepatocellular carcinoma
Shuda M, Kondoh N, Tanaka K, Ryo A, Wakatsuki T, Hada A, Goseki N, Igari T, Hatsuse K, Aihara T, Horiuchi S, Shichita M, Yamamoto N, Yamamoto M
Anticancer Res 2000 Jul-Aug;20(4):2489-94
PMID 10953316
Differential gene-expression profiles associated with gastric adenoma
Takenawa H, Kurosaki M, Enomoto N, Miyasaka Y, Kanazawa N, Sakamoto N, Ikeda T, Izumi N, Sato C, Watanabe M
Br J Cancer 2004 Jan 12;90(1):216-23
PMID 14710232
Proteomic maps of breast cancer subtypes
Tyanova S, Albrechtsen R, Kronqvist P, Cox J, Mann M, Geiger T
Nat Commun 2016 Jan 4;7:10259
PMID 26725330
Bioinformatics analysis of gene expression profiles to diagnose crucial and novel genes in glioblastoma multiform
Vastrad C, Vastrad B
Pathol Res Pract 2018 Sep;214(9):1395-1461
PMID 30097214
Cross-species hybridization of woodchuck hepatitis viral infection-induced woodchuck hepatocellular carcinoma using human, rat and mouse oligonucleotide microarrays
Wang F, Kuang Y, Salem N, Anderson PW, Lee Z
J Gastroenterol Hepatol 2009 Apr;24(4):605-17
PMID 19175833
A 16-gene expression signature to distinguish stage I from stage II lung squamous carcinoma
Wang R, Cai Y, Zhang B, Wu Z
Int J Mol Med 2018 Mar;41(3):1377-1384
Eukaryotic elongation factor 1 complex subunits are critical HIV-1 reverse transcription cofactors
Warren K, Wei T, Li D, Qin F, Warrilow D, Lin MH, Sivakumaran H, Apolloni A, Abbott CM, Jones A, Anderson JL, Harrich D
Proc Natl Acad Sci U S A 2012 Jun 12;109(24):9587-92
PMID 22628567
Gene expression profiling of human HBV- and/or HCV-associated hepatocellular carcinoma cells using expressed sequence tags
Yoon SY, Kim JM, Oh JH, Jeon YJ, Lee DS, Kim JH, Choi JY, Ahn BM, Kim S, Yoo HS, Kim YS, Kim NS
Int J Oncol 2006 Aug;29(2):315-27
PMID 16820872
Mapping the functional domains of the eukaryotic elongation factor 1 beta gamma
van Damme H, Amons R, Janssen G, Möller W
Eur J Biochem 1991 Apr 23;197(2):505-11
PMID 2026171
New developments in the pathology of malignant lymphoma: a review of the literature published from May to August 2017
van Krieken JH
J Hematop 2017 Sep 30;10(2):65-73
PMID 29057015
Anaplastic lymphoma kinase-positive anaplastic large cell lymphoma with the variant RNF213-, ATIC- and TPM3-ALK fusions is characterized by copy number gain of the rearranged ALK gene
van der Krogt JA, Bempt MV, Ferreiro JF, Mentens N, Jacobs K, Pluys U, Doms K, Geerdens E, Uyttebroeck A, Pierre P, Michaux L, Devos T, Vandenberghe P, Tousseyn T, Cools J, Wlodarska I
Haematologica 2017 Sep;102(9):1605-1616
PMID 28659337


This paper should be referenced as such :
Luigi Cristiano
EEF1G (Eukaryotic translation elongation factor 1 gamma)
Atlas Genet Cytogenet Oncol Haematol. 2020;24(2):58-68.
Free journal version : [ pdf ]   [ DOI ]

Other Leukemias implicated (Data extracted from papers in the Atlas) [ 2 ]
  t(2;11)(p23;q12.3) EEF1G::ALK
t(6;11)(q13;q12) EEF1G::OOEP

External links


HGNC (Hugo)EEF1G   3213
Entrez_Gene (NCBI)EEF1G    eukaryotic translation elongation factor 1 gamma
AliasesEF1G; GIG35
GeneCards (Weizmann)EEF1G
Ensembl hg19 (Hinxton)ENSG00000254772 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000254772 [Gene_View]  ENSG00000254772 [Sequence]  chr11:62559596-62573891 [Contig_View]  EEF1G [Vega]
ICGC DataPortalENSG00000254772
TCGA cBioPortalEEF1G
Genatlas (Paris)EEF1G
SOURCE (Princeton)EEF1G
Genetics Home Reference (NIH)EEF1G
Genomic and cartography
GoldenPath hg38 (UCSC)EEF1G  -     chr11:62559596-62573891 -  11q12.3   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)EEF1G  -     11q12.3   [Description]    (hg19-Feb_2009)
GoldenPathEEF1G - 11q12.3 [CytoView hg19]  EEF1G - 11q12.3 [CytoView hg38]
Genome Data Viewer NCBIEEF1G [Mapview hg19]  
Gene and transcription
Genbank (Entrez)AK092787 AK129569 AK129618 AK130026 AK299876
RefSeq transcript (Entrez)NM_001404
Consensus coding sequences : CCDS (NCBI)EEF1G
Gene ExpressionEEF1G [ NCBI-GEO ]   EEF1G [ EBI - ARRAY_EXPRESS ]   EEF1G [ SEEK ]   EEF1G [ MEM ]
Gene Expression Viewer (FireBrowse)EEF1G [ Firebrowse - Broad ]
GenevisibleExpression of EEF1G in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)1937
GTEX Portal (Tissue expression)EEF1G
Human Protein AtlasENSG00000254772-EEF1G [pathology]   [cell]   [tissue]
Protein : pattern, domain, 3D structure
UniProt/SwissProtP26641   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtP26641  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProP26641
Domaine pattern : Prosite (Expaxy)EF1G_C (PS50040)    GST_CTER (PS50405)    GST_NTER (PS50404)   
Domains : Interpro (EBI)EF1B_G_C    EF1B_G_C_sf    Glutathione-S-Trfase_C-like    Glutathione-S-Trfase_C_sf    Glutathione_S-Trfase    Glutathione_S-Trfase_N    GST_C    Thioredoxin-like_sf   
Domain families : Pfam (Sanger)EF1G (PF00647)    GST_C (PF00043)    GST_N (PF02798)   
Domain families : Pfam (NCBI)pfam00647    pfam00043    pfam02798   
Domain families : Smart (EMBL)EF1G (SM01183)  
Conserved Domain (NCBI)EEF1G
PDB (RSDB)1PBU    5DQS    5JPO   
PDB Europe1PBU    5DQS    5JPO   
PDB (PDBSum)1PBU    5DQS    5JPO   
PDB (IMB)1PBU    5DQS    5JPO   
Structural Biology KnowledgeBase1PBU    5DQS    5JPO   
SCOP (Structural Classification of Proteins)1PBU    5DQS    5JPO   
CATH (Classification of proteins structures)1PBU    5DQS    5JPO   
AlphaFold pdb e-kbP26641   
Human Protein Atlas [tissue]ENSG00000254772-EEF1G [tissue]
Protein Interaction databases
IntAct (EBI)P26641
Ontologies - Pathways
Ontology : AmiGOtranslation elongation factor activity  protein binding  nucleus  nucleus  cytoplasm  cytoplasm  endoplasmic reticulum  cytosol  translational elongation  translational elongation  glutathione metabolic process  response to virus  membrane  cadherin binding  extracellular exosome  
Ontology : EGO-EBItranslation elongation factor activity  protein binding  nucleus  nucleus  cytoplasm  cytoplasm  endoplasmic reticulum  cytosol  translational elongation  translational elongation  glutathione metabolic process  response to virus  membrane  cadherin binding  extracellular exosome  
Pathways : KEGGLegionellosis   
REACTOMEP26641 [protein]
REACTOME PathwaysR-HSA-156842 [pathway]   
NDEx NetworkEEF1G
Atlas of Cancer Signalling NetworkEEF1G
Wikipedia pathwaysEEF1G
Orthology - Evolution
GeneTree (enSembl)ENSG00000254772
Phylogenetic Trees/Animal Genes : TreeFamEEF1G
Homologs : HomoloGeneEEF1G
Homology/Alignments : Family Browser (UCSC)EEF1G
Gene fusions - Rearrangements
Fusion : MitelmanEEF1G::OOEP [11q12.3/6q13]  
Fusion : MitelmanEEF1G::PPP6R3 [11q12.3/11q13.2]  
Fusion : QuiverEEF1G
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerEEF1G [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)EEF1G
Exome Variant ServerEEF1G
GNOMAD BrowserENSG00000254772
Varsome BrowserEEF1G
ACMGEEF1G variants
Genomic Variants (DGV)EEF1G [DGVbeta]
DECIPHEREEF1G [patients]   [syndromes]   [variants]   [genes]  
CONAN: Copy Number AnalysisEEF1G 
ICGC Data PortalEEF1G 
TCGA Data PortalEEF1G 
Broad Tumor PortalEEF1G
OASIS PortalEEF1G [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICEEF1G  [overview]  [genome browser]  [tissue]  [distribution]  
Somatic Mutations in Cancer : COSMIC3DEEF1G
Mutations and Diseases : HGMDEEF1G
LOVD (Leiden Open Variation Database)[gene] [transcripts] [variants]
DgiDB (Drug Gene Interaction Database)EEF1G
DoCM (Curated mutations)EEF1G
CIViC (Clinical Interpretations of Variants in Cancer)EEF1G
NCG (London)EEF1G
Impact of mutations[PolyPhen2] [Provean] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
Genetic Testing Registry EEF1G
NextProtP26641 [Medical]
Target ValidationEEF1G
Huge Navigator EEF1G [HugePedia]
Clinical trials, drugs, therapy
Protein Interactions : CTDEEF1G
Pharm GKB GenePA27649
Clinical trialEEF1G
DataMed IndexEEF1G
PubMed172 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

Search in all EBI   NCBI

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indexed on : Fri Oct 8 21:16:46 CEST 2021

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