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EEF1E1 (eukaryotic translation elongation factor 1 epsilon 1)

Written2020-03Luigi Cristiano
Aesthetic and medical biotechnologies research unit, Prestige, Terranuova Bracciolini, Italy; -

Abstract Eukaryotic translation elongation factor 1 epsilon 1, alias EEF1E1, is a protein-coding gene that plays a role in the elongation step of translation. In particular, it is an auxiliary component of the macromolecular aminoacyl-tRNA synthase complex (MARS). Its expression is found frequently altered in human cancer cells and it is considered a putative tumor suppressor gene. This review collects the data on DNA/RNA, the protein encoded and the diseases where EEF1E1 is involved.

Keywords EEF1E1; eukaryotic translation elongation factor 1 epsilon 1; AIMP3; p18; Translation; Translation elongation factor; protein synthesis; cancer; oncogene; cancer marker

(Note : for Links provided by Atlas : click)


Alias (NCBI)P18
Aminoacyl tRNA synthetase complex-interacting multifunctional protein 3 (AIMP3)
ARS-interacting multifunctional protein 3
Multisynthase Complex Auxiliary Component P18
Elongation Factor P18
HGNC (Hugo) EEF1E1
HGNC Alias symbAIMP3
HGNC Alias nameaminoacyl tRNA synthetase complex-interacting multifunctional protein 3
HGNC Previous nameP18
LocusID (NCBI) 9521
Atlas_Id 40409
Location 6p24.3  [Link to chromosome band 6p24]
Location_base_pair Starts at 8079395 and ends at 8102548 bp from pter ( according to GRCh38/hg38-Dec_2013)  [Mapping EEF1E1.png]
Fusion genes
(updated 2017)
Data from Atlas, Mitelman, Cosmic Fusion, Fusion Cancer, TCGA fusion databases with official HUGO symbols (see references in chromosomal bands)


  Figure. 1. EEF1E1 gene and splicing variants/isoforms. The figure shows the locus on chromosome 6 of the EEF1E1 gene (reworked from;;
Description EEF1E1 (eukaryotic translation elongation factor 1 epsilon 1) was identified for the first time by Mao and colleagues in 1998 (Mao et al, 1998). EEF1E1 is a protein-coding gene that starts at 8,079,395 nt and ends at 8,102,595 nt from pter. It has a length of 23,201 bp, counts 5 exons, and the current reference sequence is NC_000006.12. It is proximal to BLOC1S5 (biogenesis of lysosomal organelles complex 1 subunit 5, alias MUTED) gene. Read-through transcription exists between BLOC1S5 gene and EEF1E1 gene with forming the read-through transcript EEF1E1-BLOC1S5 (alias EEF1E1-MUTED) that is a candidate for nonsense-mediated mRNA decay (NMD) and it is unlikely to produce a protein product (He et al, 2018).
Near to the genomic sequence of EEF1E1 there is a strong promoter transcriptional element that is located at +1.0 kb. Enhancer transcriptional elements are located at +22.0 Kb and at +18.1 Kb respectively.
Transcription Alternative splicing for EEF1E1 brings to multiple transcript variants. In addition, a read-through transcription is known between EEF1E1 and the neighboring downstream MUTED (muted homolog) gene. Two main alternative splicing transcript variants for EEF1E1 were detected although several others were reported. In addition, it was speculated the presence of six protein isoforms, but only two are properly described, i.e. the isoform 1 of 174 residues and the isoform 2 that counts 139 residues.
The main characteristics of the alternative splicing transcript variants are reported in Table.1.
The transcript variant 1 mRNA has reference sequence NM_004280.5 and it is 1047 bp long. The 5'UTR counts 27 nt, the CDS is extended from 28 to 552 nt, while the 3'UTR covers the last 495 nt.
The transcript variant 2 mRNA has reference sequence NM_001135650.2 and it is 562 bp long. The 5'UTR counts 27 nt, the CDS is extended from 28 to 447 nt, while the 3'UTR covers the last 115 nt.
NameVariantRefSeq (1) Transcript IDExons TypeLenght (bp)Isoform AliasRefSeq (2) Lenght (aa)MW (kDa)pI
EEF1E1-001--ENST00000488226.2  2protein coding443---94(?)(?)
EEF1E1-002Var.1NM_004280.5 ENST00000379715.5 4protein coding1077isoform 1O43324-1NP_004271.117419.818.55
EEF1E1-003--ENST00000507463.1 3protein coding654---15016.69(?)
EEF1E1-004Var.2NM_001135650.2ENST00000429723.24protein coding562isoform 2O43324-2NP_001129122.113915.557.95
EEF1E1-005--ENST00000502429.14protein coding591---136(?)(?)
EEF1E1-006--ENST00000515633.13protein coding460---565.89(?)

Table.1 Alterative splicing variants and isoforms of EEF1E1. (reworked from;;; ncRNA = non-coding RNA; nonsense md = nonsense mediated decay; (?) = undetermined; MW = molecular weight; pI = theoretical pI.
Pseudogene According to Entrez Gene, the analysis of the human genome revealed the presence of an EEF1E1-related pseudogene on chromosome 2. This pseudogene was appointed as eukaryotic translation elongation factor 1 epsilon 1 pseudogene 1, alias EEF1E1P1 and it is classified as a processed pseudogene ( Its gene ID is 100130388, its reference is NC_000002.12, and its location is 2q13. EEF1E1P1 starts at 111,887,890 nt and ends at 111,889,485 nt with a length of 1,596 nt. It virtually encodes a non-coding transcript of 430 bp named EEF1E1P1-201 (Ensembl Ref: ENST00000446998.2). The real presence of this transcript and its possible role in the cell are totally unknown.
If EEF1E1P1 has 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 this pseudogene in human cancers or in other diseases.


  Figure.2 eEF1E1 protein. Graphical representation of eEF1E1 protein isoforms with the evidence of the main verified post-translational modifications (reworked from;; ).
Description The eukaryotic translation elongation factor 1 epsilon 1 (alias eEF1E1, p18, AIMP3) is the smallest component of the Multiaminoacyl-tRNA Synthetase complex (alias MARS). The exact position of EEF1E1 in the MARS complex is still unknown. However, it seems to be localized on the surface of the MARS complex and it seems to interact with the eEF1H complex (Deineko V.V., 2008).
EEF1E1 is a small globular protein with a length of 174 amino acids and a molecular weight of 19,8 kDa.
eEF1E1 shows strong sequence similarity with eukaryotic translation elongation factor 1 beta 2 ( EEF1B2) and eukaryotic translation elongation factor 1 gamma ( EEF1G) (Quevillon and Mirande, 1996) and with the N-terminal sequence of valyl-tRNA synthetase (Deineko V.V., 2008).
eEF1E1 shows many domains in both isoforms: the amino half terminal is unique for both isoforms and shows an N-terminal-like domain not well characterized followed by a linker domain, while the major differences between the two isoforms are in the carboxyl half terminal. In fact, in the carboxyl half terminal of isoform 1 there are reported two domain overlapping, i.e. a Glutathione S-transferase C-terminal-like domain (GST_C_AIMP3), folded in alpha-helical, and a more general and not well characterized C-terminal domain. In isoform 2, there is a unique region called C-terminal domain of the Glutathione S-transferase family (GST_C_family). The fold of this domain is alpha-helical (see figure.2).
EEF1E1 interacts with other members of the MARS complex and one interactional model was proposed (Mirande, 2017) although its exact interactions need to be still clarified.
Post-translational modifications. Some post-translational modifications are observed, such as phosphorylation and acetylation (
Expression eEF1E1 is expressed widely in human tissues and normal cells (; while its expression is altered in many cancer types. Frequently it is downregulated in various cancer tissues (Park et al, 2005).
Cells that show overexpression of eEF1E1 show an acceleration of senescence and also defects in nuclear morphology (Oh et al, 2010).
Localisation EEF1E1 is located mostly in the cytoplasm but it was also found in the nucleus.
  Figure 3. Cellular localization of eEF1E1(p18). In the figure is reported the cellular localization of eEF1E1 obtaining by immunofluorescent staining (antibody HPA027901). In particular, eEF1E1 shows to be localized both in cytosol and nucleoplasm in (1) A-431 cell line and (2) U-2 OS cell line. In green: antiboy for eEF1E1; In red: microtubules (reworked from ENSG00000124802-EEF1E1/cell)
Function It is well known that in eukaryotic cells the various components of translation machinery are properly organized into two main multienzyme structures: eEF1H (macromolecular eukaryotic translation elongation factor-1 complex), formed by the translation elongation factors (EEF1B2, EEF1D, EEF1G) and VARS (valyl-tRNA synthetase), and MARS (Multiaminoacyl-tRNA Synthetase complex or multi-tRNA synthetase complex, alias MSC), formed by nine aminoacyl-tRNA synthetases (AARSs) specific for amino acids Glu, Pro (EPRS1 (glutaminylprolyl-tRNA synthetase)), Ile (IARS1), Leu (LARS1), Met (MARS1, methionyl-tRNAsynthetase), Gln (QARS1), Lys (KARS1), Arg (RARS1), and Asp (DARS1) and other auxiliary non-synthetase protein components, called also aminoacyl-tRNA synthetase (ARS)-interacting multifunctional proteins (AIMPs), i.e AIMP1 (p43), AIMP2 (p38) and eEF1E1 (AIMP3, alias p18)( Cho et al, 2015; Shalak et al, 2007; Quevillon and Mirande, 1996).
It is well known that in eukaryotic cells the various components of translation machinery Therefore, the main canonical function of eEF1E1 is to play a role as an auxiliary component of the macromolecular aminoacyl-tRNA synthetases complex in the elongation step of translation, in particular, it interacts with several aminoacyl-tRNA synthetases (Tao et al, 2017) and it could contribute to the anchorage of MARS complex to EF1H complex (Quevillon and Mirande, 1996).
Other functions (non-canonical roles): in addition to what has already been said, it seems to play a role in embryonic development of the mammalian face and other structures (Fowles et al, 2003).
eEF1E1 has the ability to translocate into the nucleus in response to DNA damage where it has a role in the DNA damage response in association with serine/threonine kinases ATM / ATR and TP53. In fact, it was found a positive relationship between expression levels of eEF1E1 and TP53, i.e. high expression levels of eEF1E1 are correlated with elevated TP53 levels, while eEF1E1 depletion leads to the block of TP53 induction (Park et al, 2005). The eEF1E1 loss-of-function phenotype leads to various kinds of abnormalities: in particular, one allele inactivation increases the susceptibility to spontaneous tumors while the inactivation of both EEF1E1 alleles caused embryonic lethality (Park et al, 2005). The importance of eEF1E1 in embryogenesis is previously reported (Fowles et al, 2003) while in the context of the tumors, eEF1E1 could be a haploinsufficient tumor suppressor (Park et al, 2005) that can accelerate cellular senescence (Kang et al, 2012).
eEF1E1 in involved in the degradation of mature Lamin A ( LMNA) which is a major component of the nuclear envelope matrix (Tao et al, 2017).
Homology eEF1E1 is highly conserved and its homology between the species is reported in Table.2
OrganismSpeciesSymbolDNA Identity (%)PROT Identity (%)
Mouse M.musculusEef1e186.688.5
Xenopus tropicalisX.tropicalisEef1e167.669.6
Zebrafish D.rerioEef1e163.063.7

Table.2 EEF1E1 homology (reworked from ps://


Note A great number of mutations in the genomic sequence and in the amino acid sequence for EEF1E1 were discovered in cancer cells that are obviously genetically more unstable respect normal ones. However, depletion of EEF1E1 causes itself genomic instability in cells (Kim et al, 2018) and makes the cells susceptible to transformation by single oncogenes (Park et al, 2006).
The genomic alterations observed include also the formation of novel fusion genes. However, there are no sufficient experimental data yet to understand the repercussions on cellular behavior and so the implications in cancer of these alterations.
  Figure 4. Circos plot for fusion events involving eEF1E1. The picture summarizes all fusion events concerning eEF1E1 and its fusion partners (from

Implicated in

Note A different expression level of EEF1E1 was observed in many cancer types compared to noncancerous control tissue. It is considered as a putative tumor suppressor, in particular for its downregulation in gastric and colorectal cancers (Kim et al, 2011). In fact, high EEF1E1 expression seems to be related to better survival in these two tumor types (Hassan et al, 2018).
However, Hassan et colleagues reported that EEF1E1 is overexpressed in many other cancer types such as breast, lung, gastric, prostate, colorectal and liver tumors and this fact could predict poor survival (breast, lung, liver)(Hassan et al, 2018).
Interesting is the role of inorganic arsenic (iAs) in the epigenetic alteration of DNA methylation in arsenic-induced diseases such as cancer of the bladder, kidney, lung, liver, and prostate. It was revealed that EEF1E1 is one of many genes silenced and involved in iAs related-hypermethylation in an arsenic-methylated tumor suppressorome (Smeester et al, 2011).
In addition, eEF1E1 is involved in some genomic translocations with the creation of numerous fusion genes (Table.3).
Name5' end3' endLoc1Loc2DescriptionTypeOrganCodeRef.
CDYL/EEF1E1CDYLEEF1E16p256p24.3t(6;6)(p25;p24)TranslocationMalignant melanomaSkinSKCM1
EEF1E1-BLOC1S5EEF1E1BLOC1S56p24.36p24.3Readthrough transcriptionFusion gene----
EEF1E1/RREB1EEF1E1RREB16p24.36p24.3t(6;6)(p24;p24)Fusion gene----
INPP4A/EEF1E1INPP4AEEF1E12q116p24.3t(2;6)(q11;p24)TranslocationMesenchymal tumor, NOS--1
RREB1/EEF1E1RREB1EEF1E16p24.36p24.3t(6;6)(p24;p24)Fusion geneAstrocytoma, grade III-IV/GlioblastomaCentral Nervous SystemGBM2,3

Table.3 EEF1E1 rearrangements: translocations and fusion genes (reworked from:;;;; [ (?) ] unknown; [ 1 ] Hu et al, 2018; [ 2 ] Yoshihara et al, 2015; [ 3 ] Gao et al 2018; [ - ] no reference
Entity Ankylosing spondylitis
Note It is found that the expression levels of EEF1E1 are significantly upregulated in whole blood of ankylosing spondylitis (AS) patients respect control group and these findings could be attributed to genetic mutations on EEF1E1 gene. This may have an important significance in the pathogenesis of AS because eEF1E1 may be involved in AS related-inflammation by upregulating TP53 and pro-inflammatory cytokines. This may suggest the use of EEF1E1 as an underlying genetic biomarker for the diagnosis of AS but other research are needed to determine the exact role of eEF1E1 overexpression in AS (Fan et al, 2019)
Entity Autism spectrum disorders
Note EEF1E1 appears in research on developmental delay and autism spectrum disorders focused on deletions in chromosome 6p22.3-p24.3 (Celestino-Soper et al, 2012). However, is still not clear its role in these diseases.
Entity Bladder cancers
Note In general, eEF1E1 is found to be down-regulated in bladder cancers. eEF1E1 is expressed at moderate and high levels in all normal urothelium tissues while only a part of bladder cancers shows this expression's pattern. The loss of eEF1E1 expression is more evident in late-stage (≥ T2) bladder tumours and can be associated with survival in muscle-invasive bladder cancers (MIBC) patients following radiotherapy (Gurung et al, 2015).
Note EEF1E1 is upregulated in astrocytoma and oligodendroglioma while for glioblastoma and glioma no significant difference in expression levels was observed. High levels of EEF1E1 could be predicted better survival outcomes (Hassan et al, 2018). In addition, one genomic alteration was observed both in astrocytoma and glioblastoma, i.e. the fusion gene t(6;6)(p24;p24) RREB1 /EEF1E1 (Gao et al, 2018; Yoshihara et al, 2015). There are no data about the respective chimeric transcript or protein and so this genomic alteration is still poorly understood.
Entity Breast cancer
Note Currently, for EEF1E1 there is no significant difference in expression, between breast cancer and normal breast tissues (Hassan et al, 2018; Guglielmi et al, 2013). The prognostic significance for EEF1E1 is that a higher expression level has a significant correlation with relapse-free survival (RFS) and distant metastasis-free survival (DMFS) but not with either overall survival (OS) or post-progression survival (PPS) while high expression levels of EEF1E1 are strongly associated with poor RFS in the luminal A and B subtypes (Hassan et al, 2018).
Other authors reported that EEF1E1 is down-regulated in breast cancer and linked to the genomic instability of these cells (Iofrida et al, 2012). In addition, some genomic alteration was observed in breast adenocarcinoma such as the translocation t(6;6)(p24;q12) EEF1E1/ EYS and t(6;6)(p25;p24) PSMG4 /EEF1E1 (Hu et al., 2018). There are no data about the respective chimeric transcripts or proteins and so these genomic alterations are still poorly understood.
Entity Colorectal cancer
Note EEF1E1 was found to be upregulated in rectal mucinous adenocarcinoma subtype and, in general in colorectal cancers compared to normal tissues. A reduction of its expression level correlates with a worst prognosis and poor survival (Hassan et al, 2018). Other studies found that normal colon mucosa expressed EEF1E1 in nearly all of the cases while EEF1E1 expression is significantly decreased in the majority of colorectal cancer (CRC) cases. This suggests that the downregulation of EEF1E1 may be related to inactivation of its tumour suppressor function and so might play a role in the development of CRC (Chen et al, 2018; Kim et al, 2011)
Entity Gastric cancer
Note In gastric cancers is found an upregulation of EEF1E1 transcript and this predicts a better overall survival (OS) and first progression (FP)(Hassan et al, 2018). Other studies revealed that normal gastric mucosa expressed EEF1E1 in nearly all of the cases while EEF1E1 expression is significantly decreased in the majority of gastric cancer (GC) cases. This suggests that the downregulation of EEF1E1 may be related to the inactivation of its tumour suppressor function and so might play a role in the development of GC (Kim et al, 2011).
Entity Head and neck squamous cell carcinoma (HNSC)
Note EEF1E1 is found to be overexpressed in head and neck cancers (Hassan et al, 2018). Wiest and colleagues (Wiest et al, 2002) have found an interesting feature in the HPV16 infection in some samples of head and neck cancer in relation to EEF1E1. In detail, the integration site of E6/E7 region of HPV16 falls on chromosome 6 in the proximity of some human genes included EEF1E1. This could contribute to explain the oncogene property of HPV16 or one of the oncogenesis mechanisms of head and neck cancer. However, it is still unclear if the viral integration can affect the regulation of expression of EEF1E1.
Entity Kidney cancer
Note EEF1E1 was found to be downregulated in chromophobe renal cell carcinoma and in kidney clear cell carcinoma (Hassan et al, 2018).
Entity Liver cancer
Note It was documented that eEF1E1 is down-regulated in hepatocellular carcinoma (HCC)( Yu et al, 2017; Du et al, 2012). In particular, there is a high relation between the expression levels of highly up-regulated in liver cancer ( HULC) long non-coding RNA and eEF1E1 in HCC. In fact, if HULC is over-expressed the expression levels of eEF1E1 fall down and on the contrary if expression levels of HULC decrease, eEF1E1 is expressed normally. EEF1E1 gene is in close proximity to HULC gene and with high probability the second can mediate the expression levels of the first (Yu et al, 2017). Other authors reported that EEF1E1 expression levels are higher in liver cancer and that this could predict worse survival although they did not tell precisely the cancer type (Hassan et al, 2018).
Entity Lung cancer
Note EEF1E1 expression levels were reported to be high in small cell lung carcinoma ID: 51 lung carcinoid tumor 42>, in , in squamous cell lung carcinoma subtypes, and in . These high expression levels seem to be correlated with poor overall survival (OS) and first progression (FP) in lung cancers (Hassan et al, 2018). In addition, were reported some somatic mutations for EEF1E1 gene in lung cancer cell lines (Kim et al, 2011).
Entity Lymphoma and other blood cancers
Note EEF1E1 is found to be overexpressed in Burkitt's lymphoma and in diffuse large B-Cell lymphoma. On the contrary, it is found to be downregulated in marginal zone B-Cell lymphoma (Hassan et al, 2018), acute promyelocytic leukemia and chronic myelogenous leukemia (Gurung et al, 2015). In chronic myelogenous leukemia was observed some somatic mutations for EEF1E1 (Kim et al, 2011). In addition, EEF1E1 shows an increased expression in pyothorax-associated lymphoma (PAL), a lymphoma developing in long-standing inflammation (Nishiu et al, 2004).
Entity Ovarian cancer
Note It is detected that EEF1E1 is frequently upregulated in ovarian serous adenocarcinoma (Hassan et al, 2018).
Entity Pancreatic cancer
Note EEF1E1 expression levels were found to be significantly downregulated in pancreatic cancers (Hassan et al, 2008).
Entity Prostate cancer
Note EEF1E1 is significantly overexpressed in prostate cancer. Currently, there is not sufficient data about the prognostic significance of the upregulation of EEF1E1 in prostate cancer (Hassan et al, 2018).

To be noted

HIV-1 interactions: It is reported that HIV-1 MA protein interacts with EEF1E1 in human HEK293 and Jurkat cell lines (Jäger et al, 2011) and that EEF1E1 is subject to cleavage by the HIV-1 protease (Impens et al, 2012).


Deletions in chromosome 6p22
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3-p24 3, including ATXN1, are associated with developmental delay and autism spectrum disorders
PMID 22480366
Long non-coding RNAs: crucial regulators of gastrointestinal cancer cell proliferation
Chen J, Liu S, Hu X
Cell Death Discov 2018 Apr 27;4:50
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Direct and biochemical interaction between dopamine D3 receptor and elongation factor-1Bbetagamma
Cho DI, Oak MH, Yang HJ, Choi HK, Janssen GM, Kim KM
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PMID 14519448
Assembly of Multi-tRNA Synthetase Complex via Heterotetrameric Glutathione Transferase-homology Domains
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On ARS-interacting multifunctional protein p18
Deineko V.V.
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J Biol Chem 2012 Jul 27;287(31):26302-11
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Screening of underlying genetic biomarkers for ankylosing spondylitis
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Genes (Basel) 2018 Jan 16;9(1)
PMID 29337901
Role of Pseudogenes in Tumorigenesis
Hu X, Yang L, Mo YY
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PMID 22944692
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BMC Cancer 2012 May 30;12:207
PMID 22646717
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PMID 22190034
AIMP3/p18 controls translational initiation by mediating the delivery of charged initiator tRNA to initiation complex
Kang T, Kwon NH, Lee JY, Park MC, Kang E, Kim HH, Kang TJ, Kim S
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PMID 22867704
AIMP3 depletion causes genome instability and loss of stemness in mouse embryonic stem cells
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Cell Death Dis 2018 Sep 24;9(10):972
PMID 30250065
Expression of AIMP1, 2 and 3, the scaffolds for the multi-tRNA synthetase complex, is downregulated in gastric and colorectal cancer
Kim SS, Hur SY, Kim YR, Yoo NJ, Lee SH
Tumori 2011 May-Jun;97(3):380-5
PMID 21789020
Identification of genes expressed in human CD34(+) hematopoietic stem/progenitor cells by expressed sequence tags and efficient full-length cDNA cloning
Mao M, Fu G, Wu JS, Zhang QH, Zhou J, Kan LX, Huang QH, He KL, Gu BW, Han ZG, Shen Y, Gu J, Yu YP, Xu SH, Wang YX, Chen SJ, Chen Z
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Cancer Sci 2004 Oct;95(10):828-34
PMID 15504251
Downregulation of lamin A by tumor suppressor AIMP3/p18 leads to a progeroid phenotype in mice
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PMID 19095653
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Quevillon S, Mirande M
FEBS Lett 1996 Oct 14;395(1):63-7
PMID 8849690
Characterization of p43(ARF), a derivative of the p43 component of multiaminoacyl-tRNA synthetase complex released during apoptosis
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Epigenetic changes in individuals with arsenicosis
Smeester L, Rager JE, Bailey KA, Guan X, Smith N, García-Vargas G, Del Razo LM, Drobná Z, Kelkar H, Stýblo M, Fry RC
Chem Res Toxicol 2011 Feb 18;24(2):165-7
PMID 21291286
Mapping the contact surfaces in the Lamin A:AIMP3 complex by hydrogen/deuterium exchange FT-ICR mass spectrometry
Tao Y, Fang P, Kim S, Guo M, Young NL, Marshall AG
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Involvement of intact HPV16 E6/E7 gene expression in head and neck cancers with unaltered p53 status and perturbed pRb cell cycle control
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This paper should be referenced as such :
Luigi Cristiano
EEF1E1 (eukaryotic translation elongation factor 1 epsilon 1)
Atlas Genet Cytogenet Oncol Haematol. 2020;24(11):387-395.
Free journal version : [ pdf ]   [ DOI ]

External links


HGNC (Hugo)EEF1E1   3212
Entrez_Gene (NCBI)EEF1E1    eukaryotic translation elongation factor 1 epsilon 1
AliasesAIMP3; P18
GeneCards (Weizmann)EEF1E1
Ensembl hg19 (Hinxton)ENSG00000124802 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000124802 [Gene_View]  ENSG00000124802 [Sequence]  chr6:8079395-8102548 [Contig_View]  EEF1E1 [Vega]
ICGC DataPortalENSG00000124802
TCGA cBioPortalEEF1E1
AceView (NCBI)EEF1E1
Genatlas (Paris)EEF1E1
SOURCE (Princeton)EEF1E1
Genetics Home Reference (NIH)EEF1E1
Genomic and cartography
GoldenPath hg38 (UCSC)EEF1E1  -     chr6:8079395-8102548 -  6p24.3   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)EEF1E1  -     6p24.3   [Description]    (hg19-Feb_2009)
GoldenPathEEF1E1 - 6p24.3 [CytoView hg19]  EEF1E1 - 6p24.3 [CytoView hg38]
Genome Data Viewer NCBIEEF1E1 [Mapview hg19]  
Gene and transcription
Genbank (Entrez)AB011079 AF054186 AI374688 AI394376 AV714140
RefSeq transcript (Entrez)NM_001135650 NM_004280
Consensus coding sequences : CCDS (NCBI)EEF1E1
Gene ExpressionEEF1E1 [ NCBI-GEO ]   EEF1E1 [ EBI - ARRAY_EXPRESS ]   EEF1E1 [ SEEK ]   EEF1E1 [ MEM ]
Gene Expression Viewer (FireBrowse)EEF1E1 [ Firebrowse - Broad ]
GenevisibleExpression of EEF1E1 in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)9521
GTEX Portal (Tissue expression)EEF1E1
Human Protein AtlasENSG00000124802-EEF1E1 [pathology]   [cell]   [tissue]
Protein : pattern, domain, 3D structure
UniProt/SwissProtO43324   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtO43324  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProO43324
Domaine pattern : Prosite (Expaxy)GST_CTER (PS50405)   
Domains : Interpro (EBI)EEF1E1    Glutathione-S-Trfase_C-like    Glutathione-S-Trfase_C_sf    GST_C   
Domain families : Pfam (Sanger)GST_C (PF00043)   
Domain families : Pfam (NCBI)pfam00043   
Conserved Domain (NCBI)EEF1E1
PDB (RSDB)2UZ8    4BL7    4BVX    4BVY    5BMU    5Y6L   
PDB Europe2UZ8    4BL7    4BVX    4BVY    5BMU    5Y6L   
PDB (PDBSum)2UZ8    4BL7    4BVX    4BVY    5BMU    5Y6L   
PDB (IMB)2UZ8    4BL7    4BVX    4BVY    5BMU    5Y6L   
Structural Biology KnowledgeBase2UZ8    4BL7    4BVX    4BVY    5BMU    5Y6L   
SCOP (Structural Classification of Proteins)2UZ8    4BL7    4BVX    4BVY    5BMU    5Y6L   
CATH (Classification of proteins structures)2UZ8    4BL7    4BVX    4BVY    5BMU    5Y6L   
AlphaFold pdb e-kbO43324   
Human Protein Atlas [tissue]ENSG00000124802-EEF1E1 [tissue]
Protein Interaction databases
IntAct (EBI)O43324
Ontologies - Pathways
Ontology : AmiGOprotein binding  nucleus  nucleoplasm  nucleolus  cytoplasm  cytosol  cytosol  tRNA aminoacylation for protein translation  negative regulation of cell population proliferation  aminoacyl-tRNA synthetase multienzyme complex  positive regulation of apoptotic process  positive regulation of DNA damage response, signal transduction by p53 class mediator  positive regulation of cellular senescence  
Ontology : EGO-EBIprotein binding  nucleus  nucleoplasm  nucleolus  cytoplasm  cytosol  cytosol  tRNA aminoacylation for protein translation  negative regulation of cell population proliferation  aminoacyl-tRNA synthetase multienzyme complex  positive regulation of apoptotic process  positive regulation of DNA damage response, signal transduction by p53 class mediator  positive regulation of cellular senescence  
REACTOMEO43324 [protein]
REACTOME PathwaysR-HSA-379716 [pathway]   
NDEx NetworkEEF1E1
Atlas of Cancer Signalling NetworkEEF1E1
Wikipedia pathwaysEEF1E1
Orthology - Evolution
GeneTree (enSembl)ENSG00000124802
Phylogenetic Trees/Animal Genes : TreeFamEEF1E1
Homologs : HomoloGeneEEF1E1
Homology/Alignments : Family Browser (UCSC)EEF1E1
Gene fusions - Rearrangements
Fusion : MitelmanEEF1E1::EYS [6p24.3/6q12]  
Fusion : MitelmanRREB1::EEF1E1 [6p24.3/6p24.3]  
Fusion : QuiverEEF1E1
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerEEF1E1 [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)EEF1E1
Exome Variant ServerEEF1E1
GNOMAD BrowserENSG00000124802
Varsome BrowserEEF1E1
ACMGEEF1E1 variants
Genomic Variants (DGV)EEF1E1 [DGVbeta]
DECIPHEREEF1E1 [patients]   [syndromes]   [variants]   [genes]  
CONAN: Copy Number AnalysisEEF1E1 
ICGC Data PortalEEF1E1 
TCGA Data PortalEEF1E1 
Broad Tumor PortalEEF1E1
OASIS PortalEEF1E1 [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICEEF1E1  [overview]  [genome browser]  [tissue]  [distribution]  
Somatic Mutations in Cancer : COSMIC3DEEF1E1
Mutations and Diseases : HGMDEEF1E1
LOVD (Leiden Open Variation Database)[gene] [transcripts] [variants]
DgiDB (Drug Gene Interaction Database)EEF1E1
DoCM (Curated mutations)EEF1E1
CIViC (Clinical Interpretations of Variants in Cancer)EEF1E1
NCG (London)EEF1E1
Impact of mutations[PolyPhen2] [Provean] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
Genetic Testing Registry EEF1E1
NextProtO43324 [Medical]
Target ValidationEEF1E1
Huge Navigator EEF1E1 [HugePedia]
Clinical trials, drugs, therapy
Protein Interactions : CTDEEF1E1
Pharm GKB GenePA27648
Clinical trialEEF1E1
DataMed IndexEEF1E1
PubMed71 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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