EEF1G (Eukaryotic translation elongation factor 1 gamma)
2019-03-01 Luigi Cristiano, MSc AffiliationAesthetic and medical biotechnologies research unit, Prestige, Terranuova Bracciolini, Italy; [email protected]
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.
DNA/RNA
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 https://www.ncbi.nlm.nih.gov/gene/1937; http://grch37.ensembl.org; www.genecards.org)
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 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.
Table.1. Splice variants of EEF1G gene (reworked from http://grch37.ensembl.org)
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.
| Variant | Name | RefSeq (1) | Transcript ID | Exons | Type | Lenght (bp) | RefSeq (2) | Lenght (aa) |
| 1 | EEF1G-001 | NM_001404.5 | - | 10 | Protein coding | 1446 | NP_001395.1 | 437 |
| 2 | EEF1G-002 (EEF1G-203) | AK092787.1 | ENST00000525340.5 | 9 | Retained intron | 2496 | - | - |
| 3 | EEF1G-003 (EEF1G-204) | - | ENST00000532986.1 | 5 | Processed transcript | 578 | - | - |
| 4 | EEF1G-004 (EEF1G-202) | - | ENST00000524420.5 | 5 | Processed transcript | 557 | - | - |
| 5 | EEF1G-201 | AK300203.1 | - | 10 | Protein coding | 1631 | BAG61974.1 | 487 |
Table.1. Splice variants of EEF1G gene (reworked from http://grch37.ensembl.org)
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.
Table.2 EEF1G pseudogene (reworked from https://www.ncbi.nlm.nih.gov/gene/1937)
| Gene | Gene name | Gene ID | RefSeq | Locus | Location | Start | End | Lenght (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 https://www.ncbi.nlm.nih.gov/gene/1937)
Proteins
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; https://www.uniprot.org; https://www.proteomicsdb.org; https://prosite.expasy.org); (2) Secondary structure (from https://www.ebi.ac.uk); (3) Tertiary structure: above, front view and below, top view (from http://www.cathdb.info)
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 - http://interactome.baderlab.org/), 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; http://hprd.org). 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; http://hprd.org).
3) S-nitrosylation: there is one most probable position for S-Nitrosylation on a cysteine residue (C194) (Han and Chen, 2008; http://hprd.org).
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 - http://interactome.baderlab.org/), 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; http://hprd.org). 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; http://hprd.org).
3) S-nitrosylation: there is one most probable position for S-Nitrosylation on a cysteine residue (C194) (Han and Chen, 2008; http://hprd.org).
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; https://reactome.org)
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) (https://www.proteomicsdb.org).
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).
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 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).
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).
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
Table.3 eEF1G homology (reworked from https://cgap.nci.nih.gov;
| 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 https://cgap.nci.nih.gov;
Mutations
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; http://atlasgeneticsoncology.org/Bands/11q12.html; http://quiver.archerdx.com), 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.
Entity name
t(2;11)(p23;q12.3) EEF1G/ ALK
Disease
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).
Prognosis
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).
Entity name
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 name
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 name
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 name
Cervical carcinoma
Note
EEF1G is observed to be highly expressed in cervical intraepithelial neoplasia (Shadeo et al., 2008).
Entity name
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).
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 name
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 name
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 name
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 name
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 name
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 name
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 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 name
Lymphoma
Note
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).
Entity name
Melanoma
Note
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 (https://www.empiregenomics.com).
Entity name
Note
EEF1G is significant overexpressed in myeloma cells in the bone marrow of multiple myeloma patients (Sariman et al., 2019).
Entity name
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 name
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 name
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 name
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).
Article Bibliography
| Pubmed ID | Last Year | Title | Authors |
|---|---|---|---|
| 20078854 | 2010 | Gene expression profiling of peripheral blood cells for early detection of breast cancer. | Aarøe J et al |
| 24732582 | 2014 | Purification and characterisation of recombinant human eukaryotic elongation factor 1 gamma. | Achilonu I et al |
| 24367274 | 2013 | Comprehensive analysis of transcriptome variation uncovers known and novel driver events in T-cell acute lymphoblastic leukemia. | Atak ZK et al |
| 22960745 | 2012 | Comprehensive genomic characterization of squamous cell lung cancers. | |
| 25436608 | 2014 | Characterisation of translation elongation factor eEF1B subunit expression in mammalian cells and tissues and co-localisation with eEF1A2. | Cao Y et al |
| 1612363 | 1992 | Expression of an elongation factor 1 gamma-related sequence in adenocarcinomas of the colon. | Chi K et al |
| 14519448 | 2003 | Direct and biochemical interaction between dopamine D3 receptor and elongation factor-1Bbetagamma. | Cho DI et al |
| 19608861 | 2009 | Lysine acetylation targets protein complexes and co-regulates major cellular functions. | Choudhary C et al |
| 21217813 | 2010 | The eEF1γ subunit contacts RNA polymerase II and binds vimentin promoter region. | Corbi N et al |
| 23899627 | 2014 | Green fluorescent protein expression triggers proteome changes in breast cancer cells. | Coumans JV et al |
| 11866090 | 2002 | Moonlighting functions of polypeptide elongation factor 1: from actin bundling to zinc finger protein R1-associated nuclear localization. | Ejiri S et al |
| 8382068 | 1993 | Overexpression of an elongation factor-1 gamma-hybridizing RNA in colorectal adenomas. | Ender B et al |
| 24309898 | 2014 | Analysis of the human tissue-specific expression by genome-wide integration of transcriptomics and antibody-based proteomics. | Fagerberg L et al |
| 9609096 | 1998 | Few point mutations in elongation factor-1gamma gene in gastrointestinal carcinoma. | Frazier ML et al |
| 30598115 | 2018 | Identification of cancer subtypes from single-cell RNA-seq data using a consensus clustering method. | Gan Y et al |
| 18335467 | 2008 | Detergent-free biotin switch combined with liquid chromatography/tandem mass spectrometry in the analysis of S-nitrosylated proteins. | Han P et al |
| 29286103 | 2018 | 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 et al |
| 29342219 | 2018 | The expression profile and prognostic significance of eukaryotic translation elongation factors in different cancers. | Hassan MK et al |
| 12721631 | 2003 | An expressed pseudogene regulates the messenger-RNA stability of its homologous coding gene. | Hirotsune S et al |
| 11504921 | 2001 | FEZ1/LZTS1 gene at 8p22 suppresses cancer cell growth and regulates mitosis. | Ishii H et al |
| 7989307 | 1994 | The subunit structure of elongation factor 1 from Artemia. Why two alpha-chains in this complex? | Janssen GM et al |
| 16229838 | 2005 | Three-dimensional reconstruction of the valyl-tRNA synthetase/elongation factor-1H complex and localization of the delta subunit. | Jiang S et al |
| 17906640 | 2007 | Interaction between the keratin cytoskeleton and eEF1Bgamma affects protein synthesis in epithelial cells. | Kim S et al |
| 25485619 | 2015 | A comprehensive transcriptional portrait of human cancer cell lines. | Klijn C et al |
| 7703850 | 1994 | 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 et al |
| 16624425 | 2006 | eEF1B: At the dawn of the 21st century. | Le Sourd F et al |
| 16548883 | 2006 | Transcriptomic and proteomic analyses of rhabdomyosarcoma cells reveal differential cellular gene expression in response to enterovirus 71 infection. | Leong WF et al |
| 1372736 | 1992 | Expression of elongation factor-1 gamma-related sequence in human pancreatic cancer. | Lew Y et al |
| 23699257 | 2013 | The unexpected roles of eukaryotic translation elongation factors in RNA virus replication and pathogenesis. | Li D et al |
| 24613846 | 2014 | eEF1Bγ is a positive regulator of NF-кB signaling pathway. | Liu D et al |
| 3666137 | 1987 | Primary structure of elongation factor 1 gamma from Artemia. | Maessen GD et al |
| 11985494 | 2002 | Mapping the human translation elongation factor eEF1H complex using the yeast two-hybrid system. | Mansilla F et al |
| 24113185 | 2013 | Translational control in the stress adaptive response of cancer cells: a novel role for the heat shock protein TRAP1. | Matassa DS et al |
| 9486568 | 1998 | Overexpression of elongation factor-1gamma protein in colorectal carcinoma. | Mathur S et al |
| 7889472 | 1995 | The overexpression of elongation factor 1 gamma mRNA in gastric carcinoma. | Mimori K et al |
| 8891347 | 1996 | Major intracellular localization of elongation factor-1. | Minella O et al |
| 28497265 | 2017 | Proteomics analysis of pleomorphic adenoma of the human parotid gland. | Mutlu A et al |
| 20068231 | 2010 | Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. | Olsen JV et al |
| 14702039 | 2004 | Complete sequencing and characterization of 21,243 full-length human cDNAs. | Ota T et al |
| 27840423 | 2017 | Novel ALK fusion in anaplastic large cell lymphoma involving EEF1G, a subunit of the eukaryotic elongation factor-1 complex. | Palacios G et al |
| 27639846 | 2016 | eEF1Bγ binds the Che-1 and TP53 gene promoters and their transcripts. | Pisani C et al |
| 23533145 | 2013 | In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine. | Principe S et al |
| 2278101 | 1990 | Eukaryotic protein elongation factors. | Riis B et al |
| 30008712 | 2018 | Strain-Specific Contribution of Eukaryotic Elongation Factor 1 Gamma to the Translation of Influenza A Virus Proteins. | Sammaibashi S et al |
| 8743958 | 1996 | Immunofluorescence studies of human fibroblasts demonstrate the presence of the complex of elongation factor-1 beta gamma delta in the endoplasmic reticulum. | Sanders J et al |
| 30079703 | 2019 | Investigation of Gene Expressions of Myeloma Cells in the Bone Marrow of Multiple Myeloma Patients by Transcriptome Analysis. | Sarıman M et al |
| 18248679 | 2008 | Up regulation in gene expression of chromatin remodelling factors in cervical intraepithelial neoplasia. | Shadeo A et al |
| 10094407 | 1999 | A structural model for elongation factor 1 (EF-1) and phosphorylation by protein kinase CKII. | Sheu GT et al |
| 10953316 | 2000 | Enhanced expression of translation factor mRNAs in hepatocellular carcinoma. | Shuda M et al |
| 14710232 | 2004 | Differential gene-expression profiles associated with gastric adenoma. | Takenawa H et al |
| 26725330 | 2016 | Proteomic maps of breast cancer subtypes. | Tyanova S et al |
| 30097214 | 2018 | Bioinformatics analysis of gene expression profiles to diagnose crucial and novel genes in glioblastoma multiform. | Vastrad C et al |
| 19175833 | 2009 | Cross-species hybridization of woodchuck hepatitis viral infection-induced woodchuck hepatocellular carcinoma using human, rat and mouse oligonucleotide microarrays. | Wang F et al |
| 22628567 | 2012 | Eukaryotic elongation factor 1 complex subunits are critical HIV-1 reverse transcription cofactors. | Warren K et al |
| 16820872 | 2006 | Gene expression profiling of human HBV- and/or HCV-associated hepatocellular carcinoma cells using expressed sequence tags. | Yoon SY et al |
| 2026171 | 1991 | Mapping the functional domains of the eukaryotic elongation factor 1 beta gamma. | van Damme H et al |
| 29057015 | 2017 | New developments in the pathology of malignant lymphoma: a review of the literature published from May to August 2017. | van Krieken JH et al |
| 28659337 | 2017 | 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 et al |
Other Information
Locus ID:
NCBI: 1937
MIM: 130593
HGNC: 3213
Ensembl: ENSG00000254772
Variants:
dbSNP: 1937
ClinVar: 1937
TCGA: ENSG00000254772
COSMIC: EEF1G
RNA/Proteins
| Gene ID | Transcript ID | Uniprot |
|---|---|---|
| ENSG00000254772 | ENST00000329251 | P26641 |
| ENSG00000254772 | ENST00000329251 | Q53YD7 |
Expression (GTEx)
Pathways
Protein levels (Protein atlas)
References
| Pubmed ID | Year | Title | Citations |
|---|---|---|---|
| 27840423 | 2017 | Novel ALK fusion in anaplastic large cell lymphoma involving EEF1G, a subunit of the eukaryotic elongation factor-1 complex. | 8 |
| 27840423 | 2017 | Novel ALK fusion in anaplastic large cell lymphoma involving EEF1G, a subunit of the eukaryotic elongation factor-1 complex. | 8 |
| 27639846 | 2016 | eEF1Bγ binds the Che-1 and TP53 gene promoters and their transcripts. | 5 |
| 27639846 | 2016 | eEF1Bγ binds the Che-1 and TP53 gene promoters and their transcripts. | 5 |
| 21217813 | 2010 | The eEF1γ subunit contacts RNA polymerase II and binds vimentin promoter region. | 12 |
| 21217813 | 2010 | The eEF1γ subunit contacts RNA polymerase II and binds vimentin promoter region. | 12 |
Citation
Luigi Cristiano, MSc
EEF1G (Eukaryotic translation elongation factor 1 gamma)
Atlas Genet Cytogenet Oncol Haematol. 2019-03-01
Online version: http://atlasgeneticsoncology.org/gene/54272/eef1g-(eukaryotic-translation-elongation-factor-1-gamma)
