EEF1B2 (eukaryotic translation elongation factor 1 beta 2)

2020-01-01   Luigi Cristiano 

Aesthetic and medical biotechnologies research unit, Prestige, Terranuova Bracciolini, Italy; prestige.infomed@gmail.com - luigicristiano@libero.it

Identity

HGNC
LOCATION
2q33.3
LOCUSID
ALIAS
EEF1B,EEF1B1,EF1B

Abstract

Eukaryotic translation elongation factor 1 beta 2, alias EEF1B2, is a protein-coding gene that plays a role in the elongation step of translation: In fact, it mediates GDP\/GTP exchange on eEF1A. Considering its importance it is found frequently overexpressed in human cancer cells. This review collects the data on DNA\/RNA, on the protein encoded and on the diseases where EEF1B2 is involved.

DNA/RNA

Atlas Image
Figure. 1. EEF1B2 gene and splicing variants/isoforms. The figure shows the locus on chromosome 2 of the EEF1B2 gene (reworked from https://www.ncbi.nlm.nih.gov/gene; http://grch37.ensembl.org; www.genecards.org)

Description

EEF1B2 (eukaryotic translation elongation factor 1 beta 2) was identified for the first time by Sanders and colleagues in 1991 (Sanders et al, 1991) and afterwards, its gene location was described by Pizzuti and colleagues in 1993 (Pizzuti et al, 1993). EEF1B2 is a protein-coding gene that starts at 206,159,594 nt and ends at 206,162,929 nt from pter. It has a length of 3,336 bp and the current reference sequence is NC_000002.12. It is proximal to SNORA41 (small nucleolar RNA, H/ACA box 41) gene, SNORD51 (small nucleolar RNA, C/D box 51) gene and NDUFS1 (NADH:ubiquinone oxidoreductase core subunit S1) gene. Near to the genomic sequence of EEF1B2 there is a strong promoter transcriptional element that is located at -0.2 kb.

Transcription

Three main alternative splicing transcript variants for EEF1B2 were detected although several others were reported. The three main transcript variants differ from each other only in the 5 UTR. In addition, it was speculated the presence of four protein isoforms, one main isoform of 225 amino acids and other three minor isoforms of 123 residues, 68 residues and 29 residues respectively. However, only the protein with the highest number of amino acids was detected. The main characteristics of the alternative splicing transcript variants are reported in Table.1.
>
NameVariantRefSeq (1)Transcript IDExonsTypeLenght (bp)IsoformAliasRefSeq (2)Lenght (aa)MW (kDa)pI
EEF1B2-201  (EEF1B2-001)Var.2NM_021121.3ENST00000236957.97protein coding844 (854)-P24534 NP_066944.122524.764.50
EEF1B2-202  (EEF1B2-201)Var.3NM_001037663.1ENST00000392221.57protein coding880 (900)-P24534 NP_001032752.122524.764.50
EEF1B2-203  (EEF1B2-003)Var.1NM_001959.4 ENST00000392222.76protein coding808-P24534 NP_001950.122524.764.50
EEF1B2-204  (EEF1B2-005)--ENST00000415904.14nonsense md649---68--
EEF1B2-205  (EEF1B2-007)--ENST00000429769.58nonsense md912---68--
EEF1B2-206 (EEF1B2-009)--ENST00000435123.1 3nonsense md389---29--
EEF1B2-207 (EEF1B2-004)--ENST00000445505.55protein coding515---123--
EEF1B2-208 (EEF1B2-010)--ENST00000455150.16nonsense md670---68--
EEF1B2-209  (EEF1B2-008)--ENST00000460760.12retained intron1025------
EEF1B2-210  (EEF1B2-006)--ENST00000479587.13retained intron701------
EEF1B2-211 (EEF1B2-002)-- ENST00000482103.12retained intron587------
Table.1 Alterative splicing variants and isoforms of EEF1B2.(reworked from http://grch37.ensembl.org; https://www.ncbi.nlm.nih.gov; https://web.expasy.org/protparam/; https://www.uniprot.org)
ncRNA = non-coding RNA; nonsense md = nonsense mediated decay;(?) = undetermined; MW = molecular weight; pI = theoretical pI
The main mRNA reference sequence is NM_001959.4 and it is 808 bp long. The 5UTR counts 85 nt, the CDS is extended from 86 to 763 nt, while the 3UTR covers the last 45 nt.

Pseudogene

According to Entrez Gene, the analysis of the human genome revealed the presence of several pseudogenes for EEF1B2 (Table.2), which are perhaps related to recent retrotransposition events (Chambers et al, 2001). The alternative forms EEF1B3 and EEF1B4 previously designated for EEF1B2 (Pizzuti et al, 1993) have instead proved to be pseudogenes: i.e. EEF1B2P2 and EEF1B2P3 respectively.
If these elements have any regulatory role in the expression of the respective gene as described for others (Hirotsune et al., 2003), is only speculation in the absence of experimental evidence. Currently, there is no evidence about the involvement of these pseudogenes in human cancers or in other diseases.
GeneGene  nameGene IDRefSeqLocusLocationStartEndLenght (nt)Main diseasesReference
EEF1B2P1EEF1B2 pseudogene 11932NC_000015.10Chromosome 1515q21.25250502952505908880--
EEF1B2P2EEF1B2 pseudogene 21934NC_000005.10Chromosome 55q13.16815917568159977803--
EEF1B2P3EEF1B2 pseudogene 3644820NC_000023.11Chromosome XXp22.112478834724789110764--
EEF1B2P4EEF1B2 pseudogene 4100130631NC_000012.12Chromosome 1212q23.31069012381069023981161--
EEF1B2P5EEF1B2 pseudogene 5442227NC_000006.12Chromosome 66q1263480050634819261877--
EEF1B2P6EEF1B2 pseudogene 6647030NC_000007.14Chromosome 77q32.3131661900131662665766--
EEF1B2P7EEF1B2 pseudogene 7100421756NC_000002.12Chromosome 2 2q37.1232729478232730276799--
EEF1B2P8EEF1B2 pseudogene 8100421774NC_000003.12Chromosome 33q26.31175059315175060110796--
Table.2 EEF1B2 pseudogenes (reworked from https://www.ncbi.nlm.nih.gov/gene/1933; https://www.targetvalidation.org; https://www.ncbi.nlm.nih.gov/geoprofiles/)
[ (?) ] uncertain; [ - ] no reference

Proteins

Atlas Image
Figure.2 eEF1B2 protein. Graphical representation of eEF1B2 protein with the evidence of the main verified post-translational modifications (reworked from Le Sourd et al., 2006; http://grch37.ensembl.org; https://www.ncbi.nlm.nih.gov; http://bioinf.umbc.edu/dmdm/gene_prot_page.php; http://www.hprd.org/ptms?hprd_id=02804&isoform_id=02804_1&isoform_name=Isoform_1).

Description

The eukaryotic translation elongation factor 1 beta 2 (alias eEF1B2, eEF1β, eEF1Bα) is the smallest subunit of the macromolecular eukaryotic translation elongation factor-1 complex (alias eEF1, also called eEF1H)(Cao et al, 2014), a high-molecular-weight form made up of an aggregation of different protein subunits: EEF1A1 (alias eEF1α), EEF1B2, EEF1G (alias eEF1γ, heEF1γ, eEF1Bγ), EEF1D (alias eEF1δ, eEF1Bδ) and VARS2 (valyl t-RNA synthetase val-RS). eEF1H protein complex plays a central role in peptide elongation during eukaryotic protein biosynthesis, in particular for the delivery of aminoacyl-tRNAs to the 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 through GTP hydrolysis. Thus eEF1BGD-complex acts as a guanine nucleotide exchange factor (GEF) for the regeneration of eEF1A-GTP for the next elongation cycle. The physiological role of eEF1B2 in the translation is fundamental to permit the conversion of the inactive form eEF1A-GDP into its corresponding active form eEF1A-GTP. In particular, eEF1B2 strictly collaborate with eEF1D and eEF1G in the conversion of eEF1A from its inactive GDP-bound form to its active GTP-bound form and so it covers a role as a guanine nucleotide exchange factor (GEF) for eEF1A (Le Sourd et al., 2006; Browne and Proud, 2002).
It was shown that the nucleotide exchange reaction by eEF1B2 is inhibited by Mg2+ that binds on K205 residue. Only after the displacing of Mg2+ from its binding site eEF1B2 can function correctly (Pittmann et al, 2006).
In prokaryotes, the homolog of eEF1B2 is known as EF-Ts, while in eukaryotes it is known only one functional protein form with the reference sequence NP_001950.1 by 225 residues. It is found in the eEF1H protein complex and it shows many domains: in the carboxyl half terminal there is an EF-1 guanine nucleotide exchange domain (EF1-GNE domain / GEF) while in the amino half terminal there is a region called GST-C-eEF1b-like domain (Glutathione S-transferase C-terminal-like domain)(see figure.2).
The fold of the C-terminal domain of eEF1B2 is found very similar to that many ribosomal proteins, i.e. it shows two so-called split b-a-b motifs (Andersen et al, 2003). This region possesses nucleotide exchange activity and interacts with eEF1A (Le Sourd et al., 2006).
The non-catalytic N-terminal domain of eEF1B2, that interacts with the N-terminal domain of eEF1G (Le Sourd et al., 2006; van Damme et al, 1991), has a regulatory role on the eEF1B2 itself because it can interfere with the guanine nucleotide exchange activity located on the C-terminal domain. In fact, the non-catalytic N-terminal domain of eEF1B2 brings to the reduction in the overall rate of the guanine nucleotide exchange reaction mediated by eEF1B2. It is only thanks to the bond of eEF1B2 with eEF1G that this inhibitory effect is abolished (Trosiuk et al, 2016).
EEF1B2 interacts primarily with eEF1A1/ EEF1A2 and eEF1G but also with valyl -tRNA synthetase (Val-RS)(Le Sourd et al., 2006; Bec et al., 1994). Seems that there are no direct interactions between eEF1B2 and eEF1D (Cao et al, 2014; Sheu and Traugh, 1997), although different interactional models were proposed (Le Sourd et al., 2006; Jiang et al.,2005; Sheu and Traugh, 1999; Minella et al., 1998).
In addition, eEF1B2 interact with translationally controlled tumor protein (TCTP) but the nature of this interaction is still poorly understood (Wu et al, 2015).
Post-translational modifications. Some post-translational modifications are observed, such as phosphorylation and acetylation (https://www.ncbi.nlm.nih.gov). Phosphorylations of eEF1B2 are made by some protein kinases, including casein kinase 2 (CK2) (Browne and Proud, 2002).
Atlas Image
Figure 3. The translation elongation mechanism. The active form of eukaryotic translation elongation factor 1 alpha (eEF1A) in complex with GTP delivers an aminoacylated tRNA to the A site of the ribosome. Following the proper codon-anticodon recognition the GTP 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 Li et al., 2013; Ejiri, 2002; Riis et al, 1990; https://reactome.org)

Expression

eEF1B2 is expressed widely in human tissues (https://www.genecards.org) although its expression is not uniform in either tissues or cell lines (Cao et al, 2014).

Localisation

eEF1B2 is located mostly in the cytoplasm but it was also found in the nucleus (https://www.genecards.org/cgi-bin/carddisp.pl?gene=EEF1B2). It shows a perinuclear distribution (Sanders et al, 1996) and it is found on the endoplasmic reticulum (Cho et al, 2003; Sanders et al, 1996).

Function

eEF1B2 plays a fundamental role in the cell, in particular in the translation elongation step. In fact, eEF1B2 shows canonical functions and multiple non-canonical roles (moonlighting roles) inside the cell.
Canonical function: eEF1B2 binds to eEF1D and eEF1G in the eEF1B2DG macromolecular complex and contributes to catalyze the exchange of GDP/GTP for eEF1A during the translation elongation cycle. It was shown that eEF1B2 has the ability to disrupt eEF1A-induced actin organization and so engage eEF1A for protein synthesis (Pittman et al, 2009).
Non-canonical roles: eEF1B2 seems to have other functions inside the cell besides its involvement in translation. Together with eEF1D and eEF1G, it controls the translation fidelity (Le Sourd et al, 2006) and in response to stressors such as heat shock, oxidative stress, and toxins, it mediates the inhibition of protein synthesis. In addition, it seems to have interaction with the cytoskeleton (Khudhair et al., 2014), but the effect of eEF1B2 on actin filaments is still poorly understood (Sasikumar et al, 2012).

Homology

eEF1B2 is highly conserved and its homology between the species is reported in Table.3
OrganismSpeciesSymbol DNA Identity (%)PROT Identity (%)
HumanH.sapiensEEF1B2100100
ChimpanzeeP.troglodytesEEF1B299.9100
MacacoM.mulattaEEF1B297.699.6
WolfC.lupusEEF1B293.098.2
CattleB.taurusEEF1B291.197.8
Mouse M.musculusEef1b289.295.6
RatR.norvegicusEef1b289.294.7
ChickenG.gallusEEF1B282.093.3
Xenopus tropicalisX.tropicaliseef1b278.185.3
Zebrafish D.rerioeef1b273.882.6
Fruit flyD.melanogasterEf1beta58.758.8
Mosquito (Anopheles)A.gambiae AgaP_AGAP01061260.262.0
 Caenorhabditis C.elegans eef-1B.155.153.1

Table.3 EEF1B2 homology (reworked from htpps://www.ncbi.nlm.nih.gov/homologene)

Mutations

Note

A great number of mutations in the genomic sequence and in the amino acid sequence for EEF1B2 were discovered in cancer cells that are obviously genetically more unstable respect normal ones. The genomic alterations observed include the formation of novel fusion genes. However, there are no sufficient experimental data yet to understand the repercussions on cellular behaviour and so the implications in cancer of these alterations.
Atlas Image
Figure 4. Circos plot for fusion events involving eEF1B2. The picture summarizes all fusion events concerning eEF1B2 and its fusion partners (from https://fusionhub.persistent.co.in/search_genewise.html).

Implicated in

Top note
A different expression level of EEF1B2 was observed in many cancer types, i.e. some cancer types show an increase of its expression levels, whereas others show a significant reduction of its expression level, compared to noncancerous control tissue. Therefore, eEF1B2 seems to be involved in tumorigenesis like the other members of eEF1H complex (Hassan et al., 2018; Le Sourd et al., 2006) but not only: it was revealed that all subunits of eEF1B2GD complex, included eEF1B2, can function separately from the eEF1B2GD complex or the eEF1H complex in cancer tissues (Veremieva et al, 2011).
In addition, eEF1B2 is involved in some genomic translocations with the creation of numerous fusion genes (Table.4).
CRIM1/EEF1B2CRIM1EEF1B22p22.32q33.3t(2;2)(p22;q33)TranslocationAdenocarcinomaKidneyKIRC Yoshihara et al 2015 ZEB1/EEF1B2ZEB1EEF1B210p11.222q33.3t(2;10)(q33;p11)Translocation(?)--- NDUFS1/EEF1B2NDUFS1EEF1B22q33.32q33.3Readthrough transcriptionFusion gene-Cell line (urinary bladder)BFTC-905Klijn et al., 2015 ZNF620/EEF1B2ZNF620EEF1B2 3p22.12q33.3t(2;3)(q33;p22)Translocation(?)--Klijn et al., 2015
Table.4 EEF1B2 rearrangements: translocations and fusion genes (reworked from: http://www.tumorfusions.org; https://mitelmandatabase.isb-cgc.org/; http://quiver.archerdx.com; http://atlasgeneticsoncology.org//Bands/2q33.html#REFERENCES; https://fusionhub.persistent.co.in/home.html; https://ccsm.uth.edu/FusionGDB/index.html)
[ (?) ] unknown; [ - ] no reference
Entity name
Brain and central nervous system (CNS) cancers
Note
Significative high expression levels for eEF1B2 were observed in atypical teratoid/rhabdoid tumor and oligodendroglioma (Hassan et al, 2018).
Prognosis
Lower protein levels of eEF1B2 were correlated with poor survival in glioma patients (Biterge-Sut, 2019; Hassan et al, 2018)
Entity name
Breast cancer
Note
It was reported that eEF1B2 is overexpressed in breast carcinoma (Al-Maghrebi et al, 2005). On the contrary, Hassan et colleagues reported that eEF1B2 expression levels are reduced both in invasive ductal breast carcinoma and invasive lobular breast carcinoma (Hassan et al, 2018). In addition, it is downregulated in IR-induced senescence in MCF7 breast cancer cell line (Byun et al, 2009).
Prognosis
According to Hassan et colleagues, elevated levels of eEF1B2 expression predict a better overall survival (OS) in luminal B subtype breast cancer, a better overall survival (OS) and distant metastasis free survival (DMFS) in luminal A subtype breast cancer, but a worse DMFS in basal type (Hassan et al, 2018).
Entity name
Colorectal cancer
Note
In colorectal cancer the involvement of eEF1B2 is controversial. Although there are no significant difference in expression levels of eEF1B2 in tumor samples respect normal ones, it is believed that a reduction of its expression level in colorectal cancer can be related to poor patients survival (Hassan et al, 2018)
Entity name
Gastric cancer
Note
It is found that eEF1B2 is expressed at levels about three times higher in gastric cancer tissues compared with respective normal ones and that the high expression of eEF1B2 seems to be significantly associated with histological type, TNM stage, tumor size, and distant metastases (Jia et al, 2019). This could suggest that eEF1B2 participate in gastric tumorigenesis and progression and so it may a possible prognostic biomarker for gastric cancer. On the contrary, a previous study reported that eEF1B2 levels in gastric cancer were significantly downregulated (Hassan et al, 2018).
Prognosis
High expression levels for eEF1B2 in gastric cancer patients predict poor overall survival (Jia et al, 2019). On the contrary, Hassan and colleagues, reported that its elevated transcript levels may predict better overall survival (OS) and better first progression (FP) (Hassan et al, 2018).
Entity name
Head and neck squamous cell carcinoma (HNSC)
Note
eEF1B2 expression levels are significantly lower in tongue squamous cell carcinoma, salivary gland adenoid cystic carcinoma, and hypopharyngeal squamous cell carcinoma respect normal ones (Hassan et al, 2018).
Entity name
Kidney cancer
Note
EEF1B2 mRNA levels were found to be upregulated in cancer samples, in particular in kidney clear cell carcinoma (Hassan et al., 2018). In addition, the yet poorly understood translocation t(2;2)(p22;q33) CRIM1/EEF1B2 was reported in kidney clear cell carcinoma (Yoshihara et al, 2015).
Entity name
Liver cancer
Note
There is not much data on the expression levels of eEF1B2 in liver tumors however lower protein levels for eEF1B2 seems to be correlated with better survival in hepatocellular carcinoma patients (Biterge-Sut, 2019; Hassan et al, 2018).
Entity name
Lung cancer
Note
eEF1B2 expression levels seem to not show any significant difference between tumor and normal tissue (Hassan et al, 2018) although other research revealed that it is overexpressed in 8% of cancer samples examined (Veremieva et al, 2014).
Prognosis
An overexpression of EEF1B2 predicts poor prognosis in lung cancer, in particular in adenocarcinoma (Hassan et al, 2018).
Entity name
Lymphoma and other blood cancers
Note
High expression levels of eEF1B2 were detected in follicular lymphoma, diffuse large B-Cell lymphoma and Burkitts lymphoma (Hassan et al, 2018).
Entity name
Neurological and neurodevelopmental disorders
Note
Loss of function of EEF1B2 brings to defects in the elongation process and it is involved in autosomal recessive intellectual disability (ID) (Larcher et al., 2019).
Entity name
Oesophageal carcinoma
Note
It was detected that eEF1B2 is overexpressed in about 20% of cardioesophageal carcinoma samples examined respect noncancerous ones (Veremieva et al., 2014).
Entity name
Pancreatic cancer
Note
EEF1B2 mRNA is found to be down-regulated in pancreatic cancer tissue samples and this can be correlated to a better survival (Hassan et al., 2018).
Entity name
Prostate cancer
Note
There are no significant differences in expression levels of eEF1B2 in prostate cancer respect normal one (Hassan et al, 2018).

Bibliography

Pubmed IDLast YearTitleAuthors
160804952005Up-regulation of eukaryotic elongation factor-1 subunits in breast carcinoma.Al-Maghrebi M et al
129327322003Elongation factors in protein biosynthesis.Andersen GR et al
82944611994Reconstitution in vitro of the valyl-tRNA synthetase-elongation factor (EF) 1 beta gamma delta complex. Essential roles of the NH2-terminal extension of valyl-tRNA synthetase and of the EF-1 delta subunit in complex formation.Bec G et al
124233342002Regulation of peptide-chain elongation in mammalian cells.Browne GJ et al
194872832009Cathepsin D and eukaryotic translation elongation factor 1 as promising markers of cellular senescence.Byun HO et al
254366082014Characterisation of translation elongation factor eEF1B subunit expression in mammalian cells and tissues and co-localisation with eEF1A2.Cao Y et al
115971392001Comparative genomic analysis of genes encoding translation elongation factor 1B(alpha) in human and mouse shows EEF1B1 to be a recent retrotransposition event.Chambers DM et al
145194482003Direct and biochemical interaction between dopamine D3 receptor and elongation factor-1Bbetagamma.Cho DI et al
118660902002Moonlighting functions of polypeptide elongation factor 1: from actin bundling to zinc finger protein R1-associated nuclear localization.Ejiri S et al
293422192018The expression profile and prognostic significance of eukaryotic translation elongation factors in different cancers.Hassan MK et al
127216312003An expressed pseudogene regulates the messenger-RNA stability of its homologous coding gene.Hirotsune S et al
305720582019Translation elongation factor eEF1Bα is identified as a novel prognostic marker of gastric cancer.Jia L et al
162298382005Three-dimensional reconstruction of the valyl-tRNA synthetase/elongation factor-1H complex and localization of the delta subunit.Jiang S et al
318453182020New evidence that biallelic loss of function in EEF1B2 gene leads to intellectual disability.Larcher L et al
166244252006eEF1B: At the dawn of the 21st century.Le Sourd F et al
236992572013The unexpected roles of eukaryotic translation elongation factors in RNA virus replication and pathogenesis.Li D et al
97987841998Multiple phosphorylation sites and quaternary organization of guanine-nucleotide exchange complex of elongation factor-1 (EF-1betagammadelta/ValRS) control the various functions of EF-1alpha.Minella O et al
166754552006Mg2+ and a key lysine modulate exchange activity of eukaryotic translation elongation factor 1B alpha.Pittman YR et al
82509211993Human elongation factor EF-1 beta: cloning and characterization of the EF1 beta 5a gene and assignment of EF-1 beta isoforms to chromosomes 2,5,15 and X.Pizzuti A et al
22781011990Eukaryotic protein elongation factors.Riis B et al
87439581996Immunofluorescence 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
18867771991Nucleotide sequence of human elongation factor-1 beta cDNA.Sanders J et al
225558742012The many roles of the eukaryotic elongation factor 1 complex.Sasikumar AN et al
94071201997Recombinant subunits of mammalian elongation factor 1 expressed in Escherichia coli. Subunit interactions, elongation activity, and phosphorylation by protein kinase CKII.Sheu GT et al
265879072016A non-catalytic N-terminal domain negatively influences the nucleotide exchange activity of translation elongation factor 1Bα.Trosiuk TV et al
209646812011Unbalanced expression of the translation complex eEF1 subunits in human cardioesophageal carcinoma.Veremieva M et al
256350482015Evolutionarily conserved binding of translationally controlled tumor protein to eukaryotic elongation factor 1B.Wu H et al
255005442015The landscape and therapeutic relevance of cancer-associated transcript fusions.Yoshihara K et al
20261711991Mapping the functional domains of the eukaryotic elongation factor 1 beta gamma.van Damme H et al

Other Information

Locus ID:

NCBI: 1933
MIM: 600655
HGNC: 3208
Ensembl: ENSG00000114942

Variants:

dbSNP: 1933
ClinVar: 1933
TCGA: ENSG00000114942
COSMIC: EEF1B2

RNA/Proteins

Gene IDTranscript IDUniprot
ENSG00000114942ENST00000236957P24534
ENSG00000114942ENST00000236957A0A024R3W7
ENSG00000114942ENST00000392221P24534
ENSG00000114942ENST00000392221A0A024R3W7
ENSG00000114942ENST00000392222P24534
ENSG00000114942ENST00000392222A0A024R3W7
ENSG00000114942ENST00000415904F2Z2G2
ENSG00000114942ENST00000429769F2Z2G2
ENSG00000114942ENST00000435123F8WF65
ENSG00000114942ENST00000445505C9JZW3
ENSG00000114942ENST00000455150F8WFC9

Expression (GTEx)

0
500
1000
1500

Pathways

PathwaySourceExternal ID
Metabolism of proteinsREACTOMER-HSA-392499
TranslationREACTOMER-HSA-72766
Eukaryotic Translation ElongationREACTOMER-HSA-156842
Gene ExpressionREACTOMER-HSA-74160

Protein levels (Protein atlas)

Not detected
Low
Medium
High

References

Pubmed IDYearTitleCitations
146239682003Translationally controlled tumor protein acts as a guanine nucleotide dissociation inhibitor on the translation elongation factor eEF1A.52
153417332004Solution structure of human initiation factor eIF2alpha reveals homology to the elongation factor eEF1B.31
194872832009Cathepsin D and eukaryotic translation elongation factor 1 as promising markers of cellular senescence.31
254366082014Characterisation of translation elongation factor eEF1B subunit expression in mammalian cells and tissues and co-localisation with eEF1A2.3
295729822018An update on the biophysical character of the human eukaryotic elongation factor 1 beta: Perspectives from interaction with elongation factor 1 gamma.1
305720582019Translation elongation factor eEF1Bα is identified as a novel prognostic marker of gastric cancer.1
305901472019The protein-binding N-terminal domain of human translation elongation factor 1Bβ possesses a dynamic α-helical structural organization.1

Citation

Luigi Cristiano

EEF1B2 (eukaryotic translation elongation factor 1 beta 2)

Atlas Genet Cytogenet Oncol Haematol. 2020-01-01

Online version: http://atlasgeneticsoncology.org/gene/43239/eef1b2