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Protein

Elongation factor 2

Gene

EEF2

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

Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 bindingi26 – 33GTPBy similarity8
Nucleotide bindingi104 – 108GTPBy similarity5
Nucleotide bindingi158 – 161GTPBy 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

  • 5S rRNA binding Source: Ensembl
  • actin filament binding Source: Ensembl
  • cadherin binding Source: BHF-UCL
  • GTPase activity Source: GO_Central
  • GTP binding Source: UniProtKB-KW
  • p53 binding Source: Ensembl
  • protein kinase binding Source: UniProtKB
  • ribosome binding Source: GO_Central
  • RNA binding Source: UniProtKB
  • translation elongation factor activity Source: GO_Central

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
LigandGTP-binding, Nucleotide-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-156902 Peptide chain elongation
R-HSA-5336415 Uptake and function of diphtheria toxin
R-HSA-5358493 Synthesis of diphthamide-EEF2
R-HSA-6798695 Neutrophil degranulation
R-HSA-8876725 Protein methylation

SIGNOR Signaling Network Open Resource

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SIGNORi
P13639

Protein family/group databases

MoonProt database of moonlighting proteins

More...
MoonProti
P13639

<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 2
Short name:
EF-2
<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:EEF2
Synonyms:EF2
<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 19

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000167658.15

Human Gene Nomenclature Database

More...
HGNCi
HGNC:3214 EEF2

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
130610 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P13639

<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; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, 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

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Spinocerebellar ataxia 26 (SCA26)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of spinocerebellar ataxia, a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord.
See also OMIM:609306
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_070792596P → H in SCA26; compromises the mechanics of translocation. 1 PublicationCorresponds to variant dbSNP:rs587777052EnsemblClinVar.1

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>Mutagenesisi595S → A: Strongly reduced phosphorylation at Thr-57. 1 Publication1
Mutagenesisi599H → P: Strongly reduced phosphorylation at Thr-57. 1 Publication1

Keywords - Diseasei

Disease mutation, Neurodegeneration, Spinocerebellar ataxia

Organism-specific databases

DisGeNET

More...
DisGeNETi
1938

MalaCards human disease database

More...
MalaCardsi
EEF2
MIMi609306 phenotype

Open Targets

More...
OpenTargetsi
ENSG00000167658

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...
Orphaneti
101112 Spinocerebellar ataxia type 26

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA27650

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL1795108

Drug and drug target database

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DrugBanki
DB02059 Adenosine-5-Diphosphoribose
DB03223 Diphthamide
DB04315 Guanosine-5'-Diphosphate

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
EEF2

Domain mapping of disease mutations (DMDM)

More...
DMDMi
119172

<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 methionineiRemovedCombined sources1 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_00000910002 – 858Elongation factor 2Add BLAST857

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 residuei54PhosphothreonineCombined sources1
Modified residuei57Phosphothreonine; by EEF2KCombined sources1 Publication1
Modified residuei59PhosphothreonineCombined sources1
Modified residuei152N6-succinyllysineBy similarity1
Modified residuei235N6-acetyllysineCombined sources1
Modified residuei239N6-acetyllysine; alternateCombined sources1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki239Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources
Modified residuei265Phosphotyrosine; by CSK1 Publication1
Modified residuei272N6-acetyllysine; alternateCombined sources1
Modified residuei272N6-succinyllysine; alternateBy similarity1
Modified residuei275N6-acetyllysineCombined sources1
Cross-linki322Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Modified residuei325PhosphoserineBy similarity1
Modified residuei373Phosphotyrosine; by CSK1 Publication1
Modified residuei435PhosphothreonineCombined sources1
Modified residuei439N6-acetyllysineBy similarity1
Modified residuei445N6-acetyllysineCombined sources1
Modified residuei502PhosphoserineCombined sources1
Modified residuei525N6,N6,N6-trimethyllysine; by EEF2KMT1 Publication1
Cross-linki529Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Modified residuei572N6-succinyllysineBy similarity1
Modified residuei595Phosphoserine; by CDK2Combined sources1 Publication1
Modified residuei619N6-acetyllysineBy similarity1
Modified residuei715DiphthamideBy 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

Phosphorylation by EF-2 kinase completely inactivates EF-2; it requires prior phosphorylation by CDK2 at Ser-595 during mitotic prometaphase. Phosphorylation by CSK promotes SUMOylation, proteolytic cleavage, and nuclear translocation if the C-terminal fragment.2 Publications
Diphthamide is 2-[3-carboxyamido-3-(trimethyl-ammonio)propyl]histidine. Diphthamide can be ADP-ribosylated by diphtheria toxin and by Pseudomonas exotoxin A, thus arresting protein synthesis (By similarity).By similarity
ISGylated.1 Publication
Proteolytically processed at two sites following phosphorylation by CSK.1 Publication
SUMOylated following phosphorylation by CSK, promotes proteolytic cleavage.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei586 – 587Cleavage1 Publication2
Sitei605 – 606Cleavage1 Publication2

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P13639

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P13639

MaxQB - The MaxQuant DataBase

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MaxQBi
P13639

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

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PaxDbi
P13639

PeptideAtlas

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PeptideAtlasi
P13639

PRoteomics IDEntifications database

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PRIDEi
P13639

ProteomicsDB human proteome resource

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ProteomicsDBi
52947

2D gel databases

REPRODUCTION-2DPAGE

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REPRODUCTION-2DPAGEi
IPI00186290

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P13639

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

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PhosphoSitePlusi
P13639

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
P13639

<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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000167658 Expressed in 245 organ(s), highest expression level in testis

CleanEx database of gene expression profiles

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CleanExi
HS_EEF2

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P13639 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P13639 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
CAB007795
HPA040534
HPA057351

<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

Component of the mRNA surveillance SURF complex, at least composed of ERF1, ERF3 (ERF3A or ERF3B), EEF2, UPF1/RENT1, SMG1, SMG8 and SMG9 (PubMed:19417104). Interacts with RBPMS2 (PubMed:25064856).2 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)

More...
BioGridi
108258, 212 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P13639

Protein interaction database and analysis system

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IntActi
P13639, 83 interactors

Molecular INTeraction database

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MINTi
P13639

STRING: functional protein association networks

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STRINGi
9606.ENSP00000307940

<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

Select the link destinations:

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
4V6Xelectron microscopy5.00Az1-858[»]
6D9Jelectron microscopy3.2093-858[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P13639

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

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SMRi
P13639

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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>Domaini17 – 362tr-type GPROSITE-ProRule annotationAdd BLAST346

<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
KOG0469 Eukaryota
COG0480 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000154662

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000231589

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG001838

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P13639

KEGG Orthology (KO)

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KOi
K03234

Identification of Orthologs from Complete Genome Data

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OMAi
HLISGMG

Database of Orthologous Groups

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OrthoDBi
140796at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P13639

TreeFam database of animal gene trees

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TreeFami
TF300575

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
3.30.230.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR035647 EFG_III/V
IPR000640 EFG_V-like
IPR004161 EFTu-like_2
IPR031157 G_TR_CS
IPR027417 P-loop_NTPase
IPR020568 Ribosomal_S5_D2-typ_fold
IPR014721 Ribosomal_S5_D2-typ_fold_subgr
IPR005225 Small_GTP-bd_dom
IPR000795 TF_GTP-bd_dom
IPR009000 Transl_B-barrel_sf
IPR005517 Transl_elong_EFG/EF2_IV

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00679 EFG_C, 1 hit
PF03764 EFG_IV, 1 hit
PF00009 GTP_EFTU, 1 hit
PF03144 GTP_EFTU_D2, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00315 ELONGATNFCT

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00838 EFG_C, 1 hit
SM00889 EFG_IV, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF50447 SSF50447, 1 hit
SSF52540 SSF52540, 1 hit
SSF54211 SSF54211, 1 hit
SSF54980 SSF54980, 2 hits

TIGRFAMs; a protein family database

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TIGRFAMsi
TIGR00231 small_GTP, 1 hit

PROSITE; a protein domain and family database

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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>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)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 has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

P13639-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MVNFTVDQIR AIMDKKANIR NMSVIAHVDH GKSTLTDSLV CKAGIIASAR
60 70 80 90 100
AGETRFTDTR KDEQERCITI KSTAISLFYE LSENDLNFIK QSKDGAGFLI
110 120 130 140 150
NLIDSPGHVD FSSEVTAALR VTDGALVVVD CVSGVCVQTE TVLRQAIAER
160 170 180 190 200
IKPVLMMNKM DRALLELQLE PEELYQTFQR IVENVNVIIS TYGEGESGPM
210 220 230 240 250
GNIMIDPVLG TVGFGSGLHG WAFTLKQFAE MYVAKFAAKG EGQLGPAERA
260 270 280 290 300
KKVEDMMKKL WGDRYFDPAN GKFSKSATSP EGKKLPRTFC QLILDPIFKV
310 320 330 340 350
FDAIMNFKKE ETAKLIEKLD IKLDSEDKDK EGKPLLKAVM RRWLPAGDAL
360 370 380 390 400
LQMITIHLPS PVTAQKYRCE LLYEGPPDDE AAMGIKSCDP KGPLMMYISK
410 420 430 440 450
MVPTSDKGRF YAFGRVFSGL VSTGLKVRIM GPNYTPGKKE DLYLKPIQRT
460 470 480 490 500
ILMMGRYVEP IEDVPCGNIV GLVGVDQFLV KTGTITTFEH AHNMRVMKFS
510 520 530 540 550
VSPVVRVAVE AKNPADLPKL VEGLKRLAKS DPMVQCIIEE SGEHIIAGAG
560 570 580 590 600
ELHLEICLKD LEEDHACIPI KKSDPVVSYR ETVSEESNVL CLSKSPNKHN
610 620 630 640 650
RLYMKARPFP DGLAEDIDKG EVSARQELKQ RARYLAEKYE WDVAEARKIW
660 670 680 690 700
CFGPDGTGPN ILTDITKGVQ YLNEIKDSVV AGFQWATKEG ALCEENMRGV
710 720 730 740 750
RFDVHDVTLH ADAIHRGGGQ IIPTARRCLY ASVLTAQPRL MEPIYLVEIQ
760 770 780 790 800
CPEQVVGGIY GVLNRKRGHV FEESQVAGTP MFVVKAYLPV NESFGFTADL
810 820 830 840 850
RSNTGGQAFP QCVFDHWQIL PGDPFDNSSR PSQVVAETRK RKGLKEGIPA

LDNFLDKL
Length:858
Mass (Da):95,338
Last modified:January 23, 2007 - v4
<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:i78BD1710236C0D9C
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 is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
M0R0I6M0R0I6_HUMAN
Elongation factor 2
EEF2
85Annotation 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>

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_070792596P → H in SCA26; compromises the mechanics of translocation. 1 PublicationCorresponds to variant dbSNP:rs587777052EnsemblClinVar.1

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
X51466 mRNA Translation: CAA35829.1
Z11692 mRNA Translation: CAA77750.1
AY942181 mRNA Translation: AAX34409.1
CH471139 Genomic DNA Translation: EAW69274.1
CH471139 Genomic DNA Translation: EAW69275.1
BC126259 mRNA Translation: AAI26260.1
BC136313 mRNA Translation: AAI36314.1
M19997 mRNA Translation: AAA50388.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS12117.1

Protein sequence database of the Protein Information Resource

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PIRi
S18294 EFHU2

NCBI Reference Sequences

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RefSeqi
NP_001952.1, NM_001961.3

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.515070

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000309311; ENSP00000307940; ENSG00000167658

Database of genes from NCBI RefSeq genomes

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GeneIDi
1938

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:1938

UCSC genome browser

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UCSCi
uc002lze.4 human

<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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X51466 mRNA Translation: CAA35829.1
Z11692 mRNA Translation: CAA77750.1
AY942181 mRNA Translation: AAX34409.1
CH471139 Genomic DNA Translation: EAW69274.1
CH471139 Genomic DNA Translation: EAW69275.1
BC126259 mRNA Translation: AAI26260.1
BC136313 mRNA Translation: AAI36314.1
M19997 mRNA Translation: AAA50388.1
CCDSiCCDS12117.1
PIRiS18294 EFHU2
RefSeqiNP_001952.1, NM_001961.3
UniGeneiHs.515070

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4V6Xelectron microscopy5.00Az1-858[»]
6D9Jelectron microscopy3.2093-858[»]
ProteinModelPortaliP13639
SMRiP13639
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108258, 212 interactors
CORUMiP13639
IntActiP13639, 83 interactors
MINTiP13639
STRINGi9606.ENSP00000307940

Chemistry databases

ChEMBLiCHEMBL1795108
DrugBankiDB02059 Adenosine-5-Diphosphoribose
DB03223 Diphthamide
DB04315 Guanosine-5'-Diphosphate

Protein family/group databases

MoonProtiP13639

PTM databases

iPTMnetiP13639
PhosphoSitePlusiP13639
SwissPalmiP13639

Polymorphism and mutation databases

BioMutaiEEF2
DMDMi119172

2D gel databases

REPRODUCTION-2DPAGEiIPI00186290

Proteomic databases

EPDiP13639
jPOSTiP13639
MaxQBiP13639
PaxDbiP13639
PeptideAtlasiP13639
PRIDEiP13639
ProteomicsDBi52947

Protocols and materials databases

The DNASU plasmid repository

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DNASUi
1938
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000309311; ENSP00000307940; ENSG00000167658
GeneIDi1938
KEGGihsa:1938
UCSCiuc002lze.4 human

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
1938
DisGeNETi1938
EuPathDBiHostDB:ENSG00000167658.15

GeneCards: human genes, protein and diseases

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GeneCardsi
EEF2
HGNCiHGNC:3214 EEF2
HPAiCAB007795
HPA040534
HPA057351
MalaCardsiEEF2
MIMi130610 gene
609306 phenotype
neXtProtiNX_P13639
OpenTargetsiENSG00000167658
Orphaneti101112 Spinocerebellar ataxia type 26
PharmGKBiPA27650

GenAtlas: human gene database

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GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0469 Eukaryota
COG0480 LUCA
GeneTreeiENSGT00940000154662
HOGENOMiHOG000231589
HOVERGENiHBG001838
InParanoidiP13639
KOiK03234
OMAiHLISGMG
OrthoDBi140796at2759
PhylomeDBiP13639
TreeFamiTF300575

Enzyme and pathway databases

ReactomeiR-HSA-156902 Peptide chain elongation
R-HSA-5336415 Uptake and function of diphtheria toxin
R-HSA-5358493 Synthesis of diphthamide-EEF2
R-HSA-6798695 Neutrophil degranulation
R-HSA-8876725 Protein methylation
SIGNORiP13639

Miscellaneous databases

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

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ChiTaRSi
EEF2 human

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
EEF2

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

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GenomeRNAii
1938

Protein Ontology

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PROi
PR:P13639

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSG00000167658 Expressed in 245 organ(s), highest expression level in testis
CleanExiHS_EEF2
ExpressionAtlasiP13639 baseline and differential
GenevisibleiP13639 HS

Family and domain databases

Gene3Di3.30.230.10, 1 hit
InterProiView protein in InterPro
IPR035647 EFG_III/V
IPR000640 EFG_V-like
IPR004161 EFTu-like_2
IPR031157 G_TR_CS
IPR027417 P-loop_NTPase
IPR020568 Ribosomal_S5_D2-typ_fold
IPR014721 Ribosomal_S5_D2-typ_fold_subgr
IPR005225 Small_GTP-bd_dom
IPR000795 TF_GTP-bd_dom
IPR009000 Transl_B-barrel_sf
IPR005517 Transl_elong_EFG/EF2_IV
PfamiView protein in Pfam
PF00679 EFG_C, 1 hit
PF03764 EFG_IV, 1 hit
PF00009 GTP_EFTU, 1 hit
PF03144 GTP_EFTU_D2, 1 hit
PRINTSiPR00315 ELONGATNFCT
SMARTiView protein in SMART
SM00838 EFG_C, 1 hit
SM00889 EFG_IV, 1 hit
SUPFAMiSSF50447 SSF50447, 1 hit
SSF52540 SSF52540, 1 hit
SSF54211 SSF54211, 1 hit
SSF54980 SSF54980, 2 hits
TIGRFAMsiTIGR00231 small_GTP, 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...

<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 nameiEF2_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: P13639
Secondary accession number(s): B2RMP5, D6W618, Q58J86
<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: January 1, 1990
Last sequence update: January 23, 2007
Last modified: January 16, 2019
This is version 211 of the entry and version 4 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. SIMILARITY comments
    Index of protein domains and families
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
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