EEF1A1 eukaryotic translation elongation factor 1 alpha 1 [Homo sapiens (human)] - Gene

Summary

Official Symbol: EEF1A1provided by HGNC
Official Full Name: eukaryotic translation elongation factor 1 alpha 1provided by HGNC
Primary source: HGNC:HGNC:3189
See related: Ensembl:ENSG00000156508 MIM:130590; AllianceGenome:HGNC:3189
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Homo sapiens
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
Also known as: CCS3; EF1A; PTI1; CCS-3; EE1A1; EEF-1; EEF1A; EF-Tu; EF1A1; LENG7; eEF1A-1; GRAF-1EF; EF1alpha1
Summary: This gene encodes an isoform of the alpha subunit of the elongation factor-1 complex, which is responsible for the enzymatic delivery of aminoacyl tRNAs to the ribosome. This isoform (alpha 1) is expressed in brain, placenta, lung, liver, kidney, and pancreas, and the other isoform (alpha 2) is expressed in brain, heart and skeletal muscle. This isoform is identified as an autoantigen in 66% of patients with Felty syndrome. This gene has been found to have multiple copies on many chromosomes, some of which, if not all, represent different pseudogenes. [provided by RefSeq, Jul 2008]
Expression: Ubiquitous expression in ovary (RPKM 2994.9), thyroid (RPKM 2551.7) and 25 other tissues See more
Orthologs: mouse all
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Genomic context

Location:: 6q13

Exon count:: 8

Annotation release	Status	Assembly	Chr	Location
RS_2024_08	current	GRCh38.p14 (GCF_000001405.40)	6	NC_000006.12 (73515750..73521032, complement)
RS_2024_08	current	T2T-CHM13v2.0 (GCF_009914755.1)	6	NC_060930.1 (74692854..74698136, complement)
RS_2024_09	previous assembly	GRCh37.p13 (GCF_000001405.25)	6	NC_000006.11 (74225473..74230755, complement)

Chromosome 6 - NC_000006.12 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

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See details

Project title: HPA RNA-seq normal tissues HPA RNA-seq normal tissues
Description: RNA-seq was performed of tissue samples from 95 human individuals representing 27 different tissues in order to determine tissue-specificity of all protein-coding genes
BioProject: PRJEB4337
Publication: PMID 24309898
Analysis date: Wed Apr 4 07:08:55 2018

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

N-Acetylcysteine Inhibits Coxsackievirus B3 Replication by Downregulating Eukaryotic Translation Elongation Factor 1 Alpha 1.
Title: N-Acetylcysteine Inhibits Coxsackievirus B3 Replication by Downregulating Eukaryotic Translation Elongation Factor 1 Alpha 1.
UCHL3 promotes hepatocellular carcinoma progression by stabilizing EEF1A1 through deubiquitination.
Title: UCHL3 promotes hepatocellular carcinoma progression by stabilizing EEF1A1 through deubiquitination.
Elongation factor 1A1 regulates metabolic substrate preference in mammalian cells.
Title: Elongation factor 1A1 regulates metabolic substrate preference in mammalian cells.
Methylation of elongation factor 1A by yeast Efm4 or human eEF1A-KMT2 involves a beta-hairpin recognition motif and crosstalks with phosphorylation.
Title: Methylation of elongation factor 1A by yeast Efm4 or human eEF1A-KMT2 involves a beta-hairpin recognition motif and crosstalks with phosphorylation.
Chp1 is a dedicated chaperone at the ribosome that safeguards eEF1A biogenesis.
Title: Chp1 is a dedicated chaperone at the ribosome that safeguards eEF1A biogenesis.
Understanding functions of eEF1 translation elongation factors beyond translation. A proteomic approach.
Title: Understanding functions of eEF1 translation elongation factors beyond translation. A proteomic approach.
RNA-dependent RNA polymerase of SARS-CoV-2 regulate host mRNA translation efficiency by hijacking eEF1A factors.
Title: RNA-dependent RNA polymerase of SARS-CoV-2 regulate host mRNA translation efficiency by hijacking eEF1A factors.
Dynamic regulation of eEF1A1 acetylation affects colorectal carcinogenesis.
Title: Dynamic regulation of eEF1A1 acetylation affects colorectal carcinogenesis.
Epigenetic Control of Translation Checkpoint and Tumor Progression via RUVBL1-EEF1A1 Axis.
Title: Epigenetic Control of Translation Checkpoint and Tumor Progression via RUVBL1-EEF1A1 Axis.
eEF1A1 promotes colorectal cancer progression and predicts poor prognosis of patients.
Title: eEF1A1 promotes colorectal cancer progression and predicts poor prognosis of patients.

Submit: New GeneRIF Correction See all GeneRIFs (117)

Phenotypes

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Find tests for this gene in the NIH Genetic Testing Registry (GTR)

Review eQTL and phenotype association data in this region using PheGenI

Variation

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See variants in ClinVar

See studies and variants in dbVar

See Variation Viewer (GRCh37.p13)

See Variation Viewer (GRCh38)

HIV-1 interactions

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Replication interactions

Interaction	Pubs
HIV-1 NL4-3 replication is restricted by EEF1A1 as enhanced replication was discovered when EEF1A1 is deleted through CRISPR/Cas9 genome editing in primary CD4+ T cells	PubMed

Protein interactions

Protein	Gene	Interaction	Pubs
Envelope surface glycoprotein gp120	env	Tandem affinity purification and mass spectrometry analysis identify eukaryotic translation elongation factor 1 alpha 1 (EEF1A1), HIV-1 Gag, Gag/Pol, gp120, and Nef incorporated into staufen1 RNP complexes isolated from HIV-1-expressing cells	PubMed
Gag-Pol	gag-pol	Tandem affinity purification and mass spectrometry analysis identify eukaryotic translation elongation factor 1 alpha 1 (EEF1A1), HIV-1 Gag, Gag/Pol, gp120, and Nef incorporated into staufen1 RNP complexes isolated from HIV-1-expressing cells	PubMed
Nef	nef	eEF1A/Nef complexes contain tRNAs and block stress-induced apoptosis in monocyte-derived macrophages through tRNA binding to cytochrome c	PubMed
	nef	Exp-t-mediated nuclear-cytoplasmic transport of the eEF1A/Nef complexes in monocyte-derived macrophages is invloved in the inhibition of apoptosis triggered by stress	PubMed
	nef	HIV-1 Nef binds eEF1A in cells. Amino acids 55 to 206 in Nef and amino acids 1-74 in eEF1A are sufficient for the binding	PubMed
	nef	Yeast two hybrid assay identifies the HIV-1 Nef-interacting protein translational elongation factor 1	PubMed
	nef	Tandem affinity purification and mass spectrometry analysis identify eukaryotic translation elongation factor 1 alpha 1 (EEF1A1), HIV-1 Gag, Gag/Pol, gp120, and Nef incorporated into staufen1 RNP complexes isolated from HIV-1-expressing cells	PubMed
Pr55(Gag)	gag	Cellular biotinylated eukaryotic translation elongation factor 1 alpha 1 (EEF1A1) protein is incorporated into HIV-1 Gag virus-like particles	PubMed
	gag	Tandem affinity purification and mass spectrometry analysis identify eukaryotic translation elongation factor 1 alpha 1 (EEF1A1), HIV-1 Gag, Gag/Pol, gp120, and Nef incorporated into staufen1 RNP complexes isolated from HIV-1-expressing cells	PubMed
	gag	The interaction between the Matrix protein of HIV-1 Gag and elongation factor 1-alpha impairs translation in vitro, suggesting a role for this interaction in releasing viral RNA from polysomes, permitting the RNA to be packaged into virions	PubMed
	gag	The basic region of the Matrix protein of HIV-1 Gag (amino acids 15-35) mediates binding to amino acids 1-74 of elongation factor 1-alpha	PubMed
	gag	Binding of elongation factor 1-alpha to HIV-1 Gag proteins (Matrix and Nucleocapsid) appears to be mediated by RNA	PubMed
	gag	Elongation factor 1-alpha binds to HIV-1 Matrix, as well as to HIV-1 Gag and Nucleocapsid and is incorporated into HIV-1 virion membranes	PubMed
Rev	rev	HIV-1 Rev interacting protein, eukaryotic translation elongation factor 1 alpha 1 (EEF1A1), is identified by the in-vitro binding experiments involving cytosolic or nuclear extracts from HeLa cells	PubMed
Tat	tat	Eukaryotic translation elongation factor 1 alpha 1 (EEF1A1) is identified to interact with HIV-1 Tat mutant Nullbasic in HeLa cells by LC MS/MS	PubMed
	tat	EF-1alpha stimulates the binding of RNA Polymerase II and TRP-185 to HIV-1 TAR RNA, suggesting an interaction between EF-1alpha and HIV-1 Tat	PubMed
integrase	gag-pol	HIV-1 IN co-immunoprecipitates with eEF1A through an interaction with the viral RTCs	PubMed
	gag-pol	Using acetylated HIV-1 IN as bait in yeast two-hybrid screening identifies translation regulatory and RNA binding proteins eIF3h, eEF1A-1, and hnRNPA2 as IN-binding partners	PubMed
	gag-pol	Interaction of human EF1alpha with HIV-1 integrase is presumed based on a reported binding interaction between yeast TEF1alpha and integrase	PubMed
matrix	gag	The interaction between HIV-1 Matrix and elongation factor 1-alpha impairs translation in vitro, suggesting a role for this interaction in releasing viral RNA from polysomes, permitting the RNA to be packaged into virions	PubMed
	gag	The basic region of HIV-1 Matrix (amino acids 15-35) mediates binding to amino acids 1-74 of elongation factor 1-alpha	PubMed
	gag	Binding of elongation factor 1-alpha to HIV-1 Gag proteins (Matrix and Nucleocapsid) appears to be mediated by RNA	PubMed
	gag	Elongation factor 1-alpha binds to HIV-1 Matrix, as well as to HIV-1 Gag and Nucleocapsid and is incorporated into HIV-1 virion membranes	PubMed
reverse transcriptase p51 subunit	gag-pol	HIV-1 RT interacts with EEF1A1 as shown through biolayer interferometry and co-immunoprecipitation and can be abrogated by mutating amino acid W252 in RT	PubMed
	gag-pol	HIV-1 RT p51 subunit co-immunoprecipitates with eEF1A through an interaction with the viral RTCs	PubMed

Go to the HIV-1, Human Interaction Database

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

REN33095 (e-PCR)
- UniSTS:357895

REN33096 (e-PCR)
- UniSTS:357896

REN33097 (e-PCR)
- UniSTS:357897

REN33098 (e-PCR)
- UniSTS:357898

REN33099 (e-PCR)
- UniSTS:357899

REN33100 (e-PCR)
- UniSTS:357900

REN33101 (e-PCR)
- UniSTS:357901

REN33102 (e-PCR)
- UniSTS:357902

REN33103 (e-PCR)
- UniSTS:357903

GDB:632624 (e-PCR)
- UniSTS:158480

REN33104 (e-PCR)
- UniSTS:357904

REN33105 (e-PCR)
- UniSTS:357905

REN33106 (e-PCR)
- UniSTS:357906

REN33107 (e-PCR)
- UniSTS:357907

REN33108 (e-PCR)
- UniSTS:357908

REN33109 (e-PCR)
- UniSTS:357909

REN33110 (e-PCR)
- UniSTS:357910

REN33111 (e-PCR)
- UniSTS:357911

REN33112 (e-PCR)
- UniSTS:357912

REN33113 (e-PCR)
- UniSTS:357913

ECD22912 (e-PCR)
- UniSTS:303897

REN33114 (e-PCR)
- UniSTS:357914

REN33115 (e-PCR)
- UniSTS:357915

REN33116 (e-PCR)
- UniSTS:357916

REN33117 (e-PCR)
- UniSTS:357917

REN33118 (e-PCR)
- UniSTS:357918

REN33119 (e-PCR)
- UniSTS:357919

REN33120 (e-PCR)
- UniSTS:357920

REN33121 (e-PCR)
- UniSTS:357921

REN33122 (e-PCR)
- UniSTS:357922

REN33123 (e-PCR)
- UniSTS:357923

REN33124 (e-PCR)
- UniSTS:357924

REN33125 (e-PCR)
- UniSTS:357925

ECD04407 (e-PCR)
- UniSTS:285479

D11S2560 (e-PCR)
- UniSTS:37928

MARC_24185-24186:1034710364:1 (e-PCR)
- UniSTS:268853

EEF1A1 (e-PCR)
- UniSTS:278329

ECD10862 (e-PCR)
- UniSTS:291901

SHGC-178 (e-PCR)
- UniSTS:91474

ECD01606 (e-PCR)
- UniSTS:282708

STS-W63684 (e-PCR)
- UniSTS:65109

EEF1A1_3552 (e-PCR)
- UniSTS:462171

D7S723 (e-PCR)
- UniSTS:5218

ECD03690 (e-PCR)
- UniSTS:284770

ECD01365 (e-PCR)
- UniSTS:282471

ECD01636 (e-PCR)
- UniSTS:282737

D1S3313 (e-PCR)
- UniSTS:63106

ECD15572 (e-PCR)
- UniSTS:296589

stSG625946 (e-PCR)
- UniSTS:457112

stSG625947 (e-PCR)
- UniSTS:457113

stSG625950 (e-PCR)
- UniSTS:457116

ECD01451 (e-PCR)
- UniSTS:282554

PMC26240P1 (e-PCR)
- UniSTS:272315

ECD07388 (e-PCR)
- UniSTS:288443

RH47178 (e-PCR)
- UniSTS:90057

MARC_7355-7356:996687810:1 (e-PCR)
- UniSTS:269771

ECD08182 (e-PCR)
- UniSTS:289230

ECD01988 (e-PCR)
- UniSTS:283089

RH65848 (e-PCR)
- UniSTS:84955

GDB:555019 (e-PCR)
- UniSTS:157667

ECD00205 (e-PCR)
- UniSTS:281319

ECD14640 (e-PCR)
- UniSTS:295660

ECD03587 (e-PCR)
- UniSTS:284668

Clone Names

FLJ25721, MGC16224, MGC102687, MGC131894

Gene Ontology Provided by GOA

Function	Evidence Code	Pubs
enables GTP binding	TAS Traceable Author Statement more info	PubMed
enables GTPase activity	IBA Inferred from Biological aspect of Ancestor more info
enables GTPase activity	IDA Inferred from Direct Assay more info	PubMed
enables RNA binding	HDA more info	PubMed
enables calmodulin binding	IEA Inferred from Electronic Annotation more info
enables kinase activator activity	IDA Inferred from Direct Assay more info	PubMed
enables kinase binding	IPI Inferred from Physical Interaction more info	PubMed
enables molecular adaptor activity	IDA Inferred from Direct Assay more info	PubMed
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein kinase binding	IPI Inferred from Physical Interaction more info	PubMed
enables tRNA binding	IDA Inferred from Direct Assay more info	PubMed
enables translation elongation factor activity	IBA Inferred from Biological aspect of Ancestor more info
enables translation elongation factor activity	IDA Inferred from Direct Assay more info	PubMed
enables translation elongation factor activity	TAS Traceable Author Statement more info	PubMed

Process	Evidence Code	Pubs
involved_in cellular response to epidermal growth factor stimulus	IDA Inferred from Direct Assay more info	PubMed
involved_in positive regulation by host of viral genome replication	IDA Inferred from Direct Assay more info	PubMed
involved_in regulation of chaperone-mediated autophagy	NAS Non-traceable Author Statement more info	PubMed
involved_in translation	IBA Inferred from Biological aspect of Ancestor more info
involved_in translational elongation	IBA Inferred from Biological aspect of Ancestor more info
involved_in translational elongation	IDA Inferred from Direct Assay more info	PubMed
involved_in translational elongation	TAS Traceable Author Statement more info	PubMed

Component	Evidence Code	Pubs
located_in cortical actin cytoskeleton	IDA Inferred from Direct Assay more info	PubMed
located_in cytoplasm	IDA Inferred from Direct Assay more info	PubMed
located_in cytoplasm	ISS Inferred from Sequence or Structural Similarity more info
located_in cytoplasm	TAS Traceable Author Statement more info	PubMed
located_in cytoplasmic side of lysosomal membrane	NAS Non-traceable Author Statement more info	PubMed
located_in cytosol	IDA Inferred from Direct Assay more info	PubMed
located_in cytosol	TAS Traceable Author Statement more info
is_active_in cytosolic ribosome	IDA Inferred from Direct Assay more info	PubMed
part_of eukaryotic translation elongation factor 1 complex	TAS Traceable Author Statement more info	PubMed
located_in extracellular exosome	HDA more info	PubMed
located_in extracellular region	TAS Traceable Author Statement more info
located_in extracellular space	HDA more info	PubMed
located_in ficolin-1-rich granule lumen	TAS Traceable Author Statement more info
located_in membrane	HDA more info	PubMed
located_in nucleolus	IDA Inferred from Direct Assay more info	PubMed
located_in nucleus	HDA more info	PubMed
NOT located_in nucleus	IDA Inferred from Direct Assay more info	PubMed
located_in nucleus	IDA Inferred from Direct Assay more info	PubMed
located_in plasma membrane	IDA Inferred from Direct Assay more info	PubMed
is_active_in ribosome	IDA Inferred from Direct Assay more info	PubMed
located_in ruffle membrane	IDA Inferred from Direct Assay more info	PubMed
located_in secretory granule lumen	TAS Traceable Author Statement more info

General protein information

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Preferred Names: elongation factor 1-alpha 1

Names: CTCL tumor antigen; EF-1-alpha-1; EF1a-like protein; cervical cancer suppressor 3; elongation factor 1 alpha subunit; elongation factor Tu; epididymis secretory sperm binding protein; eukaryotic elongation factor 1 A-1; eukaryotic translation elongation factor 1 alpha 1-like 14; glucocorticoid receptor AF-1 specific elongation factor; leukocyte receptor cluster (LRC) member 7; leukocyte receptor cluster member 7; prostate tumor-inducing protein 1; translation elongation factor 1 alpha 1-like 14

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

NM_001402.6 → NP_001393.1 elongation factor 1-alpha 1

See identical proteins and their annotated locations for NP_001393.1

Status: REVIEWED

Source sequence(s)

AJ420488, AL603910, BC066893

Consensus CDS

CCDS4980.1

UniProtKB/Swiss-Prot

P04719, P04720, P68104, Q6IQ15

UniProtKB/TrEMBL

A8K9C4, Q53G85, Q53GA1, Q53GE9, Q53HM9, Q53HQ7, Q53HR5, Q6IPN6, Q6IPS9, Q6IPT9

Related

ENSP00000339053.4, ENST00000309268.11

Conserved Domains (1) summary

PTZ00141
Location:1 → 460

PTZ00141; elongation factor 1- alpha; Provisional

RefSeqs of Annotated Genomes: GCF_000001405.40-RS_2024_08

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference GRCh38.p14 Primary Assembly

Genomic

NC_000006.12 Reference GRCh38.p14 Primary Assembly

Range

73515750..73521032 complement

Download

GenBank, FASTA, Sequence Viewer (Graphics)

Alternate T2T-CHM13v2.0

Genomic

NC_060930.1 Alternate T2T-CHM13v2.0

Range

74692854..74698136 complement

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

XM_054354427.1 → XP_054210402.1 elongation factor 1-alpha 1 isoform X1

UniProtKB/Swiss-Prot

P04719, P04720, P68104, Q6IQ15

UniProtKB/TrEMBL

Q6IPS9

Suppressed Reference Sequence(s)

The following Reference Sequences have been suppressed. Explain

NM_001403.1: Suppressed sequence

Description

NM_001403.1: This RefSeq was permanently suppressed because it was based on a chimeric sequence and represented a partial CDS.