Elongation factor 1-alpha 1 (EEF1A1)

The protein contains 462 amino acids for an estimated molecular weight of 50141 Da.

 

This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. Plays a role in the positive regulation of IFNG transcription in T-helper 1 cells as part of an IFNG promoter-binding complex with TXK and PARP1 (PubMed:17177976).', '(Microbial infection) Required for the translation of viral proteins and viral replication during human coronavirus SARS-CoV-2 infection. (updated: June 2, 2021)

Protein identification was indicated in the following studies:

  1. Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
  2. Lange and co-workers. (2014) Annotating N termini for the human proteome project: N termini and Nα-acetylation status differentiate stable cleaved protein species from degradation remnants in the human erythrocyte proteome. J Proteome Res. 13(4), 2028-2044.
  3. Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
  4. Wilson and co-workers. (2016) Comparison of the Proteome of Adult and Cord Erythroid Cells, and Changes in the Proteome Following Reticulocyte Maturation. Mol Cell Proteomics. 15(6), 1938-1946.
  5. Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
  6. D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
  7. Chu and co-workers. (2018) Quantitative mass spectrometry of human reticulocytes reveal proteome-wide modifications during maturation. Br J Haematol. 180(1), 118-133.

Methods

The following articles were analysed to gather the proteome content of erythrocytes.

The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.

PublicationIdentification 1Uniprot mapping 2Not mapped /
Obsolete		TrEMBLSwiss-Prot
Goodman (2013)2289 (gene list)227853205992269
Lange (2014)123412347281224
Hegedus (2015)2638262202352387
Wilson (2016)165815281702911068
d'Alessandro (2017)18261817201815
Bryk (2017)20902060101081942
Chu (2018)18531804553621387

1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry

The compilation of older studies can be retrieved from the Red Blood Cell Collection database.

The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.

No sequence conservation computed yet.
Protein sequence (FASTA)
Protein coevolution profile (FreeContact)
Multiple Sequence Alignment (Muscle)

This protein is annotated as membranous in Gene Ontology, is annotated as membranous in UniProt.


Interpro domains
Total structural coverage: 100%
Model score: 178
MODL_MODELLER-9.18

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The reference OMIM entry for this protein is 130590

Eukaryotic translation elongation factor 1, alpha-1; eef1a1
Elongation factor 1, alpha-1
Elongation factor 1, alpha; ef1a; eef1a cervical cancer suppressor 3 isoform, included; ccs3, included

DESCRIPTION

Eukaryotic elongation factor-1 (EF1) consists of 4 subunits, EF1-alpha, EF1-beta (EEF1B2; 600655), EF1-gamma (EEF1G; 130593), and EF1-delta (EEF1D; 130592). EIF-alpha-GTP transfers aminoacyl-tRNA to the ribosome, and the release of animoacyl-tRNA from EIF-alpha-GTP is driven by GTP hydrolysis. EF1-alpha-GDP is recycled to EF1-alpha-GTP by the EF1-beta, -gamma, and -delta subunits (Sanders et al., 1996).

CLONING

Brands et al. (1986) determined the primary structure of human EEF1A by cDNA sequencing. The deduced 462-amino acid protein shows conservation of more than 80% when compared with yeast and Artema Ef1-alpha. By immunofluorescence analysis, Sanders et al. (1996) found that EF1-alpha showed strong nuclear staining and diffuse cytoplasmic staining in human foreskin fibroblasts. In contrast, EF1-beta, -gamma, and -delta showed a perinuclear distribution and colocalized with an endoplasmic reticulum resident protein. - CCS3 Splice Variant Using PLZF (ZNF145; 176797) as bait in a yeast 2-hybrid screen of an ovary cDNA library, Rho et al. (2006) cloned an EEF1A1 splice variant that they called CCS3. The deduced 361-amino acid CCS3 protein lacks the 101 N-terminal amino acids of full-length EEF1A1. Western blot analysis detected both CCS3 and full-length EEF1A1 in human cell lines.

GENE FUNCTION

Using human tissue culture cells, Morris et al. (2004) showed that promoter-directed small interfering RNA (siRNA) inhibits transcription of an integrated, proviral EF1A promoter-green fluorescent protein reporter gene and of endogenous EF1A. Silencing was associated with DNA methylation of the targeted sequence, and it required either active transport of siRNA into the nucleus or permeabilization of the nuclear envelope by lentiviral transduction. Morris et al. (2004) concluded that siRNA-directed transcriptional silencing is conserved in mammals, providing a means to inhibit mammalian gene function. The heat-shock transcription factor HSF1 (140580) is present in unstressed cells in an inactive monomeric form and becomes activated by heat and other stress stimuli. HSF1 activation involves trimerization and acquisition of a site-specific DNA-binding activity, which is negatively regulated by interaction with certain heat-shock proteins. Shamovsky et al. (2006) showed that HSF1 activation by heat shock is an active process that is mediated by a ribonucleoprotein complex containing translation elongation factor eEF1A and a previously unknown noncoding RNA that they termed heat-shock RNA-1 (HSR1; 610157). HSR1 is constitutively expressed in human and rodent cells and its homologs are functionally interchangeable. Both HSR1 and eEF1A are required for HSF1 activation in vitro; antisense oligonucleotides or short interfering RNA against HSR1 impaired the heat-shock response in vivo, rendering cells thermosensitive. Shamovsky et al. (2006) suggested that the central role of HSR1 during heat shock implies that targeting this RNA could serve as a new therapeutic model for cancer, inflammation, and other conditions associated with HSF1 deregulation. Using mass spectrometric analysis, Belyi et al. (2006) identified EF1A as the protein glucosylated after infection with Legionella pneumophila, the causative agent of Legionnaire disease (see 608556). Glucosylation occurs at ser53 in the GTPase domain of EF1A and results in inhibition of eukaryotic protein synthesis and target cell death. - CCS3 Isoform Using yeast 2- ... More on the omim web site

Subscribe to this protein entry history

July 1, 2021: Protein entry updated
Automatic update: Entry updated from uniprot information.

Oct. 20, 2020: Protein entry updated
Automatic update: Entry updated from uniprot information.

Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated

Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated

Nov. 23, 2017: Protein entry updated
Automatic update: Uniprot description updated

June 20, 2017: Protein entry updated
Automatic update: comparative model was added.

March 25, 2017: Additional information
No protein expression data in P. Mayeux work for EEF1A1

March 16, 2016: Protein entry updated
Automatic update: OMIM entry 130590 was added.

Jan. 28, 2016: Protein entry updated
Automatic update: model status changed

Jan. 24, 2016: Protein entry updated
Automatic update: model status changed