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EEF1B2 (eukaryotic translation elongation factor 1 beta 2)

Written2020-01Luigi Cristiano
Aesthetic and medical biotechnologies research unit, Prestige, Terranuova Bracciolini, Italy; -

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.

Keywords EEF1B2; Eukaryotic translation elongation factor 1 beta 2; Translation; Translation elongation factor; protein synthesis; cancer; oncogene; cancer marker

(Note : for Links provided by Atlas : click)


Alias (NCBI)EEF1B1
Elongation Factor 1-Beta
Eukaryotic Translation Elongation Factor 1 Beta 1
HGNC (Hugo) EEF1B2
LocusID (NCBI) 1932
Atlas_Id 43239
Location 2q33.3  [Link to chromosome band 2q33]
Location_base_pair Starts at 206159594 and ends at 206162929 bp from pter ( according to GRCh38/hg38-Dec_2013)  [Mapping EEF1B2.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)


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 5'UTR counts 85 nt, the CDS is extended from 86 to 763 nt, while the 3'UTR covers the last 45 nt.
  Figure. 1. EEF1B2 gene and splicing variants/isoforms. The figure shows the locus on chromosome 2 of the EEF1B2 gene (reworked from;;
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;;;
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;;
[ (?) ] uncertain; [ - ] no reference


  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;;;;
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 ( Phosphorylations of eEF1B2 are made by some protein kinases, including casein kinase 2 (CK2) (Browne and Proud, 2002).
  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;
Expression eEF1B2 is expressed widely in human tissues ( 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 ( 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 (%)
Mouse M.musculusEef1b289.295.6
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://


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.
  Figure 4. Circos plot for fusion events involving eEF1B2. The picture summarizes all fusion events concerning eEF1B2 and its fusion partners (from

Implicated in

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).
Name5' end3' endLoc1Loc2DescriptionTypeDiseaseOrganCodeRef.
CRIM1/EEF1B2CRIM1EEF1B22p22.32q33.3t(2;2)(p22;q33)TranslocationAdenocarcinomaKidneyKIRC Yoshihara et al 2015
EEF1B2/CDR1 EEF1B2CDR1 2q33.3Xq27.1t(X;2)(q27;q33)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:;;;;;
[ (?) ] unknown; [ - ] no reference
Entity 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 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 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 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 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 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 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 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 Lymphoma and other blood cancers
Note High expression levels of eEF1B2 were detected in follicular lymphoma, diffuse large B-Cell lymphoma and Burkitt's lymphoma (Hassan et al, 2018).
Entity 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 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 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 Prostate cancer
Note There are no significant differences in expression levels of eEF1B2 in prostate cancer respect normal one (Hassan et al, 2018).


Up-regulation of eukaryotic elongation factor-1 subunits in breast carcinoma
Al-Maghrebi M, Anim JT, Olalu AA
Anticancer Res 2005 May-Jun;25(3c):2573-7
PMID 16080495
Elongation factors in protein biosynthesis
Andersen GR, Nissen P, Nyborg J
Trends Biochem Sci 2003 Aug;28(8):434-41
PMID 12932732
Reconstitution in vitro of the valyl-tRNA synthetase-elongation factor (EF) 1 beta gamma delta complex
Bec G, Kerjan P, Waller JP
Essential roles of the NH2-terminal extension of valyl-tRNA synthetase and of the EF-1 delta subunit in complex formation J Biol Chem
PMID 8294461
Alterations in Eukaryotic Elongation Factor complex proteins (EEF1s) in cancer and their implications in epigenetic regulation
Biterge-Sut B
Life Sci 2019 Dec 1;238:116977
Regulation of peptide-chain elongation in mammalian cells
Browne GJ, Proud CG
Eur J Biochem 2002 Nov;269(22):5360-8
PMID 12423334
Cathepsin D and eukaryotic translation elongation factor 1 as promising markers of cellular senescence
Byun HO, Han NK, Lee HJ, Kim KB, Ko YG, Yoon G, Lee YS, Hong SI, Lee JS
Cancer Res 2009 Jun 1;69(11):4638-47
PMID 19487283
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
Comparative genomic analysis of genes encoding translation elongation factor 1B(alpha) in human and mouse shows EEF1B1 to be a recent retrotransposition event
Chambers DM, Rouleau GA, Abbott CM
Genomics 2001 Oct;77(3):145-8
PMID 11597139
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
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
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
Translation elongation factor eEF1Bα is identified as a novel prognostic marker of gastric cancer
Jia L, Yang T, Gu X, Zhao W, Tang Q, Wang X, Zhu J, Feng Z
Int J Biol Macromol 2019 Apr 1;126:345-351
PMID 30572058
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
New evidence that biallelic loss of function in EEF1B2 gene leads to intellectual disability
Larcher L, Buratti J, Héron-Longe B, Benzacken B, Pipiras E, Keren B, Delahaye-Duriez A
Clin Genet 2019 Dec 16
PMID 31845318
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
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
Multiple 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, Mulner-Lorillon O, Bec G, Cormier P, Bellé R
Biosci Rep 1998 Jun;18(3):119-27
PMID 9798784
Role of eEF1B subunits in regulation phosphorylation and some functions
N Khudhair, Y Cuiping, A Khalid, X Gao
Journal of Genetic and Environmental Resources Conservation 2014; 2(3): 270-282
Mg2+ and a key lysine modulate exchange activity of eukaryotic translation elongation factor 1B alpha
Pittman YR, Valente L, Jeppesen MG, Andersen GR, Patel S, Kinzy TG
J Biol Chem 2006 Jul 14;281(28):19457-68
PMID 16675455
Human 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, Gennarelli M, Novelli G, Colosimo A, Lo Cicero S, Caskey CT, Dallapiccola B
Biochem Biophys Res Commun 1993 Nov 30;197(1):154-62
PMID 8250921
Eukaryotic protein elongation factors
Riis B, Rattan SI, Clark BF, Merrick WC
Trends Biochem Sci 1990 Nov;15(11):420-4
PMID 2278101
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
Nucleotide sequence of human elongation factor-1 beta cDNA
Sanders J, Maassen JA, Amons R, Möller W
Nucleic Acids Res 1991 Aug 25;19(16):4551
PMID 1886777
The many roles of the eukaryotic elongation factor 1 complex
Sasikumar AN, Perez WB, Kinzy TG
Wiley Interdiscip Rev RNA 2012 Jul-Aug;3(4):543-55
PMID 22555874
Recombinant subunits of mammalian elongation factor 1 expressed in Escherichia coli
Sheu GT, Traugh JA
Subunit interactions, elongation activity, and phosphorylation by protein kinase CKII J Biol Chem
PMID 9407120
A non-catalytic N-terminal domain negatively influences the nucleotide exchange activity of translation elongation factor 1Bα
Trosiuk TV, Shalak VF, Szczepanowski RH, Negrutskii BS, El'skaya AV
FEBS J 2016 Feb;283(3):484-97
PMID 26587907
Unbalanced expression of the translation complex eEF1 subunits in human cardioesophageal carcinoma
Veremieva M, Khoruzhenko A, Zaicev S, Negrutskii B, El'skaya A
Eur J Clin Invest 2011 Mar;41(3):269-76
PMID 20964681
Evolutionarily conserved binding of translationally controlled tumor protein to eukaryotic elongation factor 1B
Wu H, Gong W, Yao X, Wang J, Perrett S, Feng Y
J Biol Chem 2015 Apr 3;290(14):8694-710
PMID 25635048
The landscape and therapeutic relevance of cancer-associated transcript fusions
Yoshihara K, Wang Q, Torres-Garcia W, Zheng S, Vegesna R, Kim H, Verhaak RG
Oncogene 2015 Sep 10;34(37):4845-54
PMID 25500544
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


This paper should be referenced as such :
Luigi Cristiano
EEF1B2 (eukaryotic translation elongation factor 1 beta 2)
Atlas Genet Cytogenet Oncol Haematol. 2020;24(9):337-345.
Free journal version : [ pdf ]   [ DOI ]

External links


HGNC (Hugo)EEF1B2   3208
Atlas Explorer : (Salamanque)EEF1B2
Entrez_Gene (NCBI)EEF1B2    eukaryotic translation elongation factor 1 beta 2
AliasesEEF1B; EEF1B1; EF1B
GeneCards (Weizmann)EEF1B2
Ensembl hg19 (Hinxton)ENSG00000114942 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000114942 [Gene_View]  ENSG00000114942 [Sequence]  chr2:206159594-206162929 [Contig_View]  EEF1B2 [Vega]
ICGC DataPortalENSG00000114942
TCGA cBioPortalEEF1B2
AceView (NCBI)EEF1B2
Genatlas (Paris)EEF1B2
SOURCE (Princeton)EEF1B2
Genetics Home Reference (NIH)EEF1B2
Genomic and cartography
GoldenPath hg38 (UCSC)EEF1B2  -     chr2:206159594-206162929 +  2q33.3   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)EEF1B2  -     2q33.3   [Description]    (hg19-Feb_2009)
GoldenPathEEF1B2 - 2q33.3 [CytoView hg19]  EEF1B2 - 2q33.3 [CytoView hg38]
Genome Data Viewer NCBIEEF1B2 [Mapview hg19]  
Gene and transcription
Genbank (Entrez)AK291910 AK310096 BC000211 BC004931 BC029316
RefSeq transcript (Entrez)NM_001037663 NM_001959 NM_021121
Consensus coding sequences : CCDS (NCBI)EEF1B2
Gene ExpressionEEF1B2 [ NCBI-GEO ]   EEF1B2 [ EBI - ARRAY_EXPRESS ]   EEF1B2 [ SEEK ]   EEF1B2 [ MEM ]
Gene Expression Viewer (FireBrowse)EEF1B2 [ Firebrowse - Broad ]
GenevisibleExpression of EEF1B2 in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)1932
GTEX Portal (Tissue expression)EEF1B2
Human Protein AtlasENSG00000114942-EEF1B2 [pathology]   [cell]   [tissue]
Protein : pattern, domain, 3D structure
UniProt/SwissProtP24534   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtP24534  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProP24534
Domaine pattern : Prosite (Expaxy)EF1BD_1 (PS00824)    EF1BD_2 (PS00825)   
Domains : Interpro (EBI)eEF-1beta-like_sf    EF-1_beta_acid_region_euk    EF1B_bsu/dsu_GNE    Glutathione-S-Trfase_C_sf    Transl_elong_EF1B/ribosomal_S6    Transl_elong_EF1B_B/D_CS   
Domain families : Pfam (Sanger)EF-1_beta_acid (PF10587)    EF1_GNE (PF00736)   
Domain families : Pfam (NCBI)pfam10587    pfam00736   
Domain families : Smart (EMBL)EF-1_beta_acid (SM01182)  EF1_GNE (SM00888)  
Conserved Domain (NCBI)EEF1B2
PDB (RSDB)1B64    5DQS   
PDB Europe1B64    5DQS   
PDB (PDBSum)1B64    5DQS   
PDB (IMB)1B64    5DQS   
Structural Biology KnowledgeBase1B64    5DQS   
SCOP (Structural Classification of Proteins)1B64    5DQS   
CATH (Classification of proteins structures)1B64    5DQS   
AlphaFold pdb e-kbP24534   
Human Protein Atlas [tissue]ENSG00000114942-EEF1B2 [tissue]
Protein Interaction databases
IntAct (EBI)P24534
Ontologies - Pathways
Ontology : AmiGOtranslation elongation factor activity  guanyl-nucleotide exchange factor activity  protein binding  nucleus  cytoplasm  endoplasmic reticulum  cytosol  cytosol  eukaryotic translation elongation factor 1 complex  translational elongation  translational elongation  regulation of catalytic activity  
Ontology : EGO-EBItranslation elongation factor activity  guanyl-nucleotide exchange factor activity  protein binding  nucleus  cytoplasm  endoplasmic reticulum  cytosol  cytosol  eukaryotic translation elongation factor 1 complex  translational elongation  translational elongation  regulation of catalytic activity  
REACTOMEP24534 [protein]
REACTOME PathwaysR-HSA-156842 [pathway]   
NDEx NetworkEEF1B2
Atlas of Cancer Signalling NetworkEEF1B2
Wikipedia pathwaysEEF1B2
Orthology - Evolution
GeneTree (enSembl)ENSG00000114942
Phylogenetic Trees/Animal Genes : TreeFamEEF1B2
Homologs : HomoloGeneEEF1B2
Homology/Alignments : Family Browser (UCSC)EEF1B2
Gene fusions - Rearrangements
Fusion : MitelmanCRIM1::EEF1B2 [2p22.3/2q33.3]  
Fusion : FusionHubACACA--EEF1B2    BLCAP--EEF1B2    CRIM1--EEF1B2    EEF1B2--CDR1    EEF1B2--EEF1B2P1    EEF1B2--EEF1B2P3    EEF1B2--H3F3B    EEF1B2--MBP    MICAL2--EEF1B2    NDUFS1--EEF1B2   
Fusion : QuiverEEF1B2
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerEEF1B2 [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)EEF1B2
Exome Variant ServerEEF1B2
GNOMAD BrowserENSG00000114942
Varsome BrowserEEF1B2
ACMGEEF1B2 variants
Genomic Variants (DGV)EEF1B2 [DGVbeta]
DECIPHEREEF1B2 [patients]   [syndromes]   [variants]   [genes]  
CONAN: Copy Number AnalysisEEF1B2 
ICGC Data PortalEEF1B2 
TCGA Data PortalEEF1B2 
Broad Tumor PortalEEF1B2
OASIS PortalEEF1B2 [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICEEF1B2  [overview]  [genome browser]  [tissue]  [distribution]  
Somatic Mutations in Cancer : COSMIC3DEEF1B2
Mutations and Diseases : HGMDEEF1B2
intOGen PortalEEF1B2
LOVD (Leiden Open Variation Database)[gene] [transcripts] [variants]
DgiDB (Drug Gene Interaction Database)EEF1B2
DoCM (Curated mutations)EEF1B2
CIViC (Clinical Interpretations of Variants in Cancer)EEF1B2
Impact of mutations[PolyPhen2] [Provean] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
Genetic Testing Registry EEF1B2
NextProtP24534 [Medical]
Target ValidationEEF1B2
Huge Navigator EEF1B2 [HugePedia]
Clinical trials, drugs, therapy
Protein Interactions : CTDEEF1B2
Pharm GKB GenePA27644
Clinical trialEEF1B2
DataMed IndexEEF1B2
PubMed137 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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indexed on : Thu Jan 20 14:06:07 CET 2022

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