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Entry version 181 (03 Jul 2019)
Sequence version 1 (13 Aug 1987)
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Protein

Elongation factor 1-alpha 1

Gene

EEF1A1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. With PARP1 and TXK, forms a complex that acts as a T helper 1 (Th1) cell-specific transcription factor and binds the promoter of IFN-gamma to directly regulate its transcription, and is thus involved importantly in Th1 cytokine production.1 Publication

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi14 – 21GTPBy similarity8
Nucleotide bindingi91 – 95GTPBy similarity5
Nucleotide bindingi153 – 156GTPBy similarity4

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionElongation factor
Biological processProtein biosynthesis, Transcription, Transcription regulation
LigandGTP-binding, Nucleotide-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-156842 Eukaryotic Translation Elongation
R-HSA-156902 Peptide chain elongation
R-HSA-3371511 HSF1 activation
R-HSA-6798695 Neutrophil degranulation
R-HSA-8876725 Protein methylation

SignaLink: a signaling pathway resource with multi-layered regulatory networks

More...
SignaLinki
P68104

SIGNOR Signaling Network Open Resource

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SIGNORi
P68104

Protein family/group databases

MoonProt database of moonlighting proteins

More...
MoonProti
P68104

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Elongation factor 1-alpha 1
Short name:
EF-1-alpha-1
Alternative name(s):
Elongation factor Tu
Short name:
EF-Tu
Eukaryotic elongation factor 1 A-1
Short name:
eEF1A-1
Leukocyte receptor cluster member 7
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:EEF1A1
Synonyms:EEF1A, EF1A, LENG7
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 6

Organism-specific databases

Human Gene Nomenclature Database

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HGNCi
HGNC:3189 EEF1A1

Online Mendelian Inheritance in Man (OMIM)

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MIMi
130590 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P68104

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi36K → R: No effect on methylation by EEF1AKMT2. Abolishes EEF1AKMT4-mediated methylation. 2 Publications1
Mutagenesisi55K → R: No effect on methylation by EEF1AKMT2. Abolishes methylation by EEF1AKNMT. 3 Publications1
Mutagenesisi79K → R: No effect on methylation by EEF1AKMT2. 1 Publication1
Mutagenesisi165K → A: Abolishes methylation by EEF1AKMT3. 1 Publication1
Mutagenesisi165K → R: No effect on methylation by EEF1AKMT2. 1 Publication1
Mutagenesisi318K → R: Abolishes methylation by EEF1AKMT2. 1 Publication1
Mutagenesisi432T → A: Abolishes phosphorylation by PASK. 1 Publication1

Organism-specific databases

DisGeNET

More...
DisGeNETi
1915

Open Targets

More...
OpenTargetsi
ENSG00000156508

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA27625

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL1795120

Drug and drug target database

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DrugBanki
DB04315 Guanosine-5'-Diphosphate

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
EEF1A1

Domain mapping of disease mutations (DMDM)

More...
DMDMi
55584035

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000908852 – 462Elongation factor 1-alpha 1Add BLAST461

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N,N,N-trimethylglycine2 Publications1
Modified residuei36N6,N6,N6-trimethyllysine; alternate; by EEF1AKMT41 Publication1
Modified residuei36N6,N6-dimethyllysine; alternate; by EEF1AKMT41 Publication1
Modified residuei36N6-methyllysine; alternate; by EEF1AKMT41 Publication1
Modified residuei55N6,N6-dimethyllysine3 Publications1
Modified residuei79N6,N6,N6-trimethyllysine; by EEF1AKMT11 Publication1
Modified residuei165N6,N6,N6-trimethyllysine; alternate; by EEF1AKMT31 Publication1
Modified residuei165N6,N6-dimethyllysine; alternate; by EEF1AKMT32 Publications1
Modified residuei165N6-acetyllysine; alternateBy similarity1
Modified residuei165N6-methyllysine; alternate; by EEF1AKMT31 Publication1
Modified residuei172N6-acetyllysineBy similarity1
Modified residuei273N6-acetyllysineBy similarity1
Modified residuei300Phosphoserine; by TGFBR11 Publication1
Modified residuei3015-glutamyl glycerylphosphorylethanolamine1 Publication1
Modified residuei318N6,N6,N6-trimethyllysine; by EEF1AKMT21 Publication1
Modified residuei3745-glutamyl glycerylphosphorylethanolamine1 Publication1
Modified residuei392N6-acetyllysine; alternateBy similarity1
Modified residuei392N6-succinyllysine; alternateBy similarity1
Modified residuei432Phosphothreonine; by PASK1 Publication1
Modified residuei439N6-acetyllysineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

ISGylated.1 Publication
Phosphorylated by TXK. Phosphorylation by PASK increases translation efficiency. Phosphorylated by ROCK2 (PubMed:26497934).4 Publications
Trimethylated at Lys-79 by EEF1AKMT1 (PubMed:26545399). Methylated at Lys-165 by EEF1AKMT3, methylation by EEF1AKMT3 is dynamic as well as inducible by stress conditions, such as ER-stress, and plays a regulatory role on mRNA translation (PubMed:28108655). Trimethylated at Lys-318 by EEF1AKMT2 (PubMed:25144183). Mono-, di-, and trimethylated at Lys-36 by EEF1AKMT4; trimethylated form is predominant. Methylation by EEF1AKMT4 contributes to the fine-tuning of translation rates for a subset of tRNAs (PubMed:28520920). Trimethylated at Gly-2 by EEF1AKNMT (PubMed:30143613). Mono- and dimethylated at Lys-55 by EEF1AKNMT; dimethylated form is predominant (PubMed:30143613, PubMed:30612740).6 Publications

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P68104

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P68104

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
P68104

PeptideAtlas

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PeptideAtlasi
P68104

PRoteomics IDEntifications database

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PRIDEi
P68104

ProteomicsDB human proteome resource

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ProteomicsDBi
57529

2D gel databases

USC-OGP 2-DE database

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OGPi
P68104

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

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SWISS-2DPAGEi
P68104

University College Dublin 2-DE Proteome Database

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UCD-2DPAGEi
P68104

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P68104

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
P68104

SwissPalm database of S-palmitoylation events

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SwissPalmi
P68104

Miscellaneous databases

CutDB - Proteolytic event database

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PMAP-CutDBi
P68104

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Brain, placenta, lung, liver, kidney, pancreas but barely detectable in heart and skeletal muscle.

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

By homocysteine (HC), may mediate accelerated synthesis of free thiol-containing proteins in response to HC-induced oxidative stress.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000156508 Expressed in 215 organ(s), highest expression level in right ovary

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P68104 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P68104 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
HPA051759
HPA053862
HPA056990

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Found in a nuclear export complex with XPO5, EEF1A1, Ran and aminoacylated tRNA.

Interacts with PARP1, TXK, XPO5 and KARS. May interact with ERGIC2.

Interacts with IFIT1 (via TPR repeats 4-7) (By similarity).

Interacts with DLC1, facilitating distribution to the membrane periphery and ruffles upon growth factor stimulation.

Interacts with ZPR1; the interaction occurs in a epidermal growth factor (EGF)-dependent manner.

Interacts with PPP1R16B (PubMed:26497934).

Interacts with SPHK1 and SPHK2; both interactions increase SPHK1 and SPHK2 kinase activity (PubMed:18263879).

By similarity9 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
108237, 443 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P68104

Database of interacting proteins

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DIPi
DIP-31277N

Protein interaction database and analysis system

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IntActi
P68104, 205 interactors

Molecular INTeraction database

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MINTi
P68104

STRING: functional protein association networks

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STRINGi
9606.ENSP00000339063

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P68104

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P68104

Database of comparative protein structure models

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ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini5 – 242tr-type GAdd BLAST238

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni14 – 21G1By similarity8
Regioni70 – 74G2By similarity5
Regioni91 – 94G3By similarity4
Regioni153 – 156G4By similarity4
Regioni194 – 196G5By similarity3

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG0052 Eukaryota
COG5256 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00950000183029

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000229291

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P68104

KEGG Orthology (KO)

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KOi
K03231

Identification of Orthologs from Complete Genome Data

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OMAi
PAKETKM

Database of Orthologous Groups

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OrthoDBi
1150082at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P68104

TreeFam database of animal gene trees

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TreeFami
TF300304

Family and domain databases

HAMAP database of protein families

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HAMAPi
MF_00118_A EF_Tu_A, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR004161 EFTu-like_2
IPR031157 G_TR_CS
IPR027417 P-loop_NTPase
IPR000795 TF_GTP-bd_dom
IPR009000 Transl_B-barrel_sf
IPR009001 Transl_elong_EF1A/Init_IF2_C
IPR004539 Transl_elong_EF1A_euk/arc
IPR004160 Transl_elong_EFTu/EF1A_C

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00009 GTP_EFTU, 1 hit
PF03144 GTP_EFTU_D2, 1 hit
PF03143 GTP_EFTU_D3, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00315 ELONGATNFCT

Superfamily database of structural and functional annotation

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SUPFAMi
SSF50447 SSF50447, 1 hit
SSF50465 SSF50465, 1 hit
SSF52540 SSF52540, 1 hit

TIGRFAMs; a protein family database

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TIGRFAMsi
TIGR00483 EF-1_alpha, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00301 G_TR_1, 1 hit
PS51722 G_TR_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 4 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: P68104-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MGKEKTHINI VVIGHVDSGK STTTGHLIYK CGGIDKRTIE KFEKEAAEMG
60 70 80 90 100
KGSFKYAWVL DKLKAERERG ITIDISLWKF ETSKYYVTII DAPGHRDFIK
110 120 130 140 150
NMITGTSQAD CAVLIVAAGV GEFEAGISKN GQTREHALLA YTLGVKQLIV
160 170 180 190 200
GVNKMDSTEP PYSQKRYEEI VKEVSTYIKK IGYNPDTVAF VPISGWNGDN
210 220 230 240 250
MLEPSANMPW FKGWKVTRKD GNASGTTLLE ALDCILPPTR PTDKPLRLPL
260 270 280 290 300
QDVYKIGGIG TVPVGRVETG VLKPGMVVTF APVNVTTEVK SVEMHHEALS
310 320 330 340 350
EALPGDNVGF NVKNVSVKDV RRGNVAGDSK NDPPMEAAGF TAQVIILNHP
360 370 380 390 400
GQISAGYAPV LDCHTAHIAC KFAELKEKID RRSGKKLEDG PKFLKSGDAA
410 420 430 440 450
IVDMVPGKPM CVESFSDYPP LGRFAVRDMR QTVAVGVIKA VDKKAAGAGK
460
VTKSAQKAQK AK
Length:462
Mass (Da):50,141
Last modified:August 13, 1987 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iD465615545AF686A
GO
Isoform 2 (identifier: P68104-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     141-161: Missing.

Note: No experimental confirmation available.
Show »
Length:441
Mass (Da):47,869
Checksum:i7BF0B64CAEB4B0F6
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A087WV01A0A087WV01_HUMAN
Elongation factor 1-alpha
EEF1A1
426Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
Q5JR01Q5JR01_HUMAN
Elongation factor 1-alpha 1
EEF1A1
145Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A6PW80A6PW80_HUMAN
Elongation factor 1-alpha 1
EEF1A1
106Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A087WVQ9A0A087WVQ9_HUMAN
Elongation factor 1-alpha 1
EEF1A1
441Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAA52367 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti83S → A in CAA27325 (PubMed:3960725).Curated1
Sequence conflicti232L → V in CAA34756 (PubMed:2183196).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_057184141 – 161Missing in isoform 2. 1 PublicationAdd BLAST21

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
X03558 mRNA Translation: CAA27245.1
J04617 Genomic DNA Translation: AAA52343.1
X16869 mRNA Translation: CAA34756.1
AY043301 mRNA Translation: AAK95378.1
BC008587 mRNA Translation: AAH08587.1
BC009733 mRNA Translation: AAH09733.1
BC009875 mRNA Translation: AAH09875.1
BC010735 mRNA Translation: AAH10735.1
BC012891 mRNA Translation: AAH12891.1
BC014224 mRNA Translation: AAH14224.1
BC018150 mRNA Translation: AAH18150.1
BC018641 mRNA Translation: AAH18641.1
BC021686 mRNA Translation: AAH21686.1
BC028674 mRNA Translation: AAH28674.1
BC038339 mRNA Translation: AAH38339.1
BC057391 mRNA Translation: AAH57391.1
BC066893 mRNA Translation: AAH66893.1
BC071619 mRNA Translation: AAH71619.1
BC072385 mRNA Translation: AAH72385.1
BC082268 mRNA Translation: AAH82268.1
X03689 mRNA Translation: CAA27325.1
M29548 mRNA Translation: AAA52367.1 Different initiation.

The Consensus CDS (CCDS) project

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CCDSi
CCDS4980.1 [P68104-1]

Protein sequence database of the Protein Information Resource

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PIRi
B24977 EFHU1

NCBI Reference Sequences

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RefSeqi
NP_001393.1, NM_001402.5 [P68104-1]
XP_011533816.1, XM_011535514.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000309268; ENSP00000339053; ENSG00000156508 [P68104-1]
ENST00000316292; ENSP00000339063; ENSG00000156508 [P68104-1]
ENST00000331523; ENSP00000330054; ENSG00000156508 [P68104-1]

Database of genes from NCBI RefSeq genomes

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GeneIDi
1915

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:1915

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03558 mRNA Translation: CAA27245.1
J04617 Genomic DNA Translation: AAA52343.1
X16869 mRNA Translation: CAA34756.1
AY043301 mRNA Translation: AAK95378.1
BC008587 mRNA Translation: AAH08587.1
BC009733 mRNA Translation: AAH09733.1
BC009875 mRNA Translation: AAH09875.1
BC010735 mRNA Translation: AAH10735.1
BC012891 mRNA Translation: AAH12891.1
BC014224 mRNA Translation: AAH14224.1
BC018150 mRNA Translation: AAH18150.1
BC018641 mRNA Translation: AAH18641.1
BC021686 mRNA Translation: AAH21686.1
BC028674 mRNA Translation: AAH28674.1
BC038339 mRNA Translation: AAH38339.1
BC057391 mRNA Translation: AAH57391.1
BC066893 mRNA Translation: AAH66893.1
BC071619 mRNA Translation: AAH71619.1
BC072385 mRNA Translation: AAH72385.1
BC082268 mRNA Translation: AAH82268.1
X03689 mRNA Translation: CAA27325.1
M29548 mRNA Translation: AAA52367.1 Different initiation.
CCDSiCCDS4980.1 [P68104-1]
PIRiB24977 EFHU1
RefSeqiNP_001393.1, NM_001402.5 [P68104-1]
XP_011533816.1, XM_011535514.2

3D structure databases

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Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1SYWmodel-A2-443[»]
3C5JX-ray1.80C343-355[»]
SMRiP68104
ModBaseiSearch...

Protein-protein interaction databases

BioGridi108237, 443 interactors
CORUMiP68104
DIPiDIP-31277N
IntActiP68104, 205 interactors
MINTiP68104
STRINGi9606.ENSP00000339063

Chemistry databases

BindingDBiP68104
ChEMBLiCHEMBL1795120
DrugBankiDB04315 Guanosine-5'-Diphosphate

Protein family/group databases

MoonProtiP68104

PTM databases

iPTMnetiP68104
PhosphoSitePlusiP68104
SwissPalmiP68104

Polymorphism and mutation databases

BioMutaiEEF1A1
DMDMi55584035

2D gel databases

OGPiP68104
SWISS-2DPAGEiP68104
UCD-2DPAGEiP68104

Proteomic databases

EPDiP68104
jPOSTiP68104
PaxDbiP68104
PeptideAtlasiP68104
PRIDEiP68104
ProteomicsDBi57529

Protocols and materials databases

The DNASU plasmid repository

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DNASUi
1915
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000309268; ENSP00000339053; ENSG00000156508 [P68104-1]
ENST00000316292; ENSP00000339063; ENSG00000156508 [P68104-1]
ENST00000331523; ENSP00000330054; ENSG00000156508 [P68104-1]
GeneIDi1915
KEGGihsa:1915

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
1915
DisGeNETi1915

GeneCards: human genes, protein and diseases

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GeneCardsi
EEF1A1

H-Invitational Database, human transcriptome db

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H-InvDBi
HIX0020005
HIX0032108
HIX0033669
HIX0169110
HGNCiHGNC:3189 EEF1A1
HPAiHPA051759
HPA053862
HPA056990
MIMi130590 gene
neXtProtiNX_P68104
OpenTargetsiENSG00000156508
PharmGKBiPA27625

GenAtlas: human gene database

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GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0052 Eukaryota
COG5256 LUCA
GeneTreeiENSGT00950000183029
HOGENOMiHOG000229291
InParanoidiP68104
KOiK03231
OMAiPAKETKM
OrthoDBi1150082at2759
PhylomeDBiP68104
TreeFamiTF300304

Enzyme and pathway databases

ReactomeiR-HSA-156842 Eukaryotic Translation Elongation
R-HSA-156902 Peptide chain elongation
R-HSA-3371511 HSF1 activation
R-HSA-6798695 Neutrophil degranulation
R-HSA-8876725 Protein methylation
SignaLinkiP68104
SIGNORiP68104

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

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ChiTaRSi
EEF1A1 human

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
Eukaryotic_translation_elongation_factor_1_alpha_1

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

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GenomeRNAii
1915
PMAP-CutDBiP68104

Protein Ontology

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PROi
PR:P68104

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSG00000156508 Expressed in 215 organ(s), highest expression level in right ovary
ExpressionAtlasiP68104 baseline and differential
GenevisibleiP68104 HS

Family and domain databases

HAMAPiMF_00118_A EF_Tu_A, 1 hit
InterProiView protein in InterPro
IPR004161 EFTu-like_2
IPR031157 G_TR_CS
IPR027417 P-loop_NTPase
IPR000795 TF_GTP-bd_dom
IPR009000 Transl_B-barrel_sf
IPR009001 Transl_elong_EF1A/Init_IF2_C
IPR004539 Transl_elong_EF1A_euk/arc
IPR004160 Transl_elong_EFTu/EF1A_C
PfamiView protein in Pfam
PF00009 GTP_EFTU, 1 hit
PF03144 GTP_EFTU_D2, 1 hit
PF03143 GTP_EFTU_D3, 1 hit
PRINTSiPR00315 ELONGATNFCT
SUPFAMiSSF50447 SSF50447, 1 hit
SSF50465 SSF50465, 1 hit
SSF52540 SSF52540, 1 hit
TIGRFAMsiTIGR00483 EF-1_alpha, 1 hit
PROSITEiView protein in PROSITE
PS00301 G_TR_1, 1 hit
PS51722 G_TR_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiEF1A1_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P68104
Secondary accession number(s): P04719, P04720, Q6IQ15
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: July 3, 2019
This is version 181 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
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