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Protein

Elongation factor 2

Gene

EEF2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

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
Nucleotide bindingi26 – 33GTPBy similarity8
Nucleotide bindingi104 – 108GTPBy similarity5
Nucleotide bindingi158 – 161GTPBy similarity4

GO - Molecular functioni

GO - Biological processi

Keywordsi

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

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

Protein family/group databases

MoonProtiP13639

Names & Taxonomyi

Protein namesi
Recommended name:
Elongation factor 2
Short name:
EF-2
Gene namesi
Name:EEF2
Synonyms:EF2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

EuPathDBiHostDB:ENSG00000167658.15
HGNCiHGNC:3214 EEF2
MIMi130610 gene
neXtProtiNX_P13639

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

Pathology & Biotechi

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
Natural variantiVAR_070792596P → H in SCA26; compromises the mechanics of translocation. 1 PublicationCorresponds to variant dbSNP:rs587777052EnsemblClinVar.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

DisGeNETi1938
MalaCardsiEEF2
MIMi609306 phenotype
OpenTargetsiENSG00000167658
Orphaneti101112 Spinocerebellar ataxia type 26
PharmGKBiPA27650

Chemistry databases

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

Polymorphism and mutation databases

BioMutaiEEF2
DMDMi119172

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources1 Publication
ChainiPRO_00000910002 – 858Elongation factor 2Add BLAST857

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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
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

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
Sitei586 – 587Cleavage1 Publication2
Sitei605 – 606Cleavage1 Publication2

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP13639
MaxQBiP13639
PaxDbiP13639
PeptideAtlasiP13639
PRIDEiP13639

2D gel databases

REPRODUCTION-2DPAGEiIPI00186290

PTM databases

iPTMnetiP13639
PhosphoSitePlusiP13639
SwissPalmiP13639

Expressioni

Gene expression databases

BgeeiENSG00000167658
CleanExiHS_EEF2
ExpressionAtlasiP13639 baseline and differential
GenevisibleiP13639 HS

Organism-specific databases

HPAiCAB007795
HPA040534
HPA057351

Interactioni

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

Binary interactionsi

WithEntry#Exp.IntActNotes
Akt2Q608232EBI-352560,EBI-400263From Mus musculus.

GO - Molecular functioni

  • actin filament binding Source: Ensembl
  • cadherin binding Source: BHF-UCL
  • protein kinase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi108258, 193 interactors
CORUMiP13639
IntActiP13639, 69 interactors
MINTiP13639
STRINGi9606.ENSP00000307940

Structurei

3D structure databases

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini17 – 362tr-type GPROSITE-ProRule annotationAdd BLAST346

Sequence similaritiesi

Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 subfamily.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0469 Eukaryota
COG0480 LUCA
GeneTreeiENSGT00900000141114
HOGENOMiHOG000231589
HOVERGENiHBG001838
InParanoidiP13639
KOiK03234
OMAiEHLISGM
OrthoDBiEOG091G0A2J
PhylomeDBiP13639
TreeFamiTF300575

Family and domain databases

Gene3Di3.30.230.10, 2 hits
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

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

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
Checksum:i78BD1710236C0D9C
GO

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:
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

Genome annotation databases

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

Similar proteinsi

Entry informationi

Entry nameiEF2_HUMAN
AccessioniPrimary (citable) accession number: P13639
Secondary accession number(s): B2RMP5, D6W618, Q58J86
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 23, 2007
Last modified: May 23, 2018
This is version 204 of the entry and version 4 of the sequence. See complete history.
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.

Miscellaneousi

Keywords - Technical termi

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

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  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. SIMILARITY comments
    Index of protein domains and families

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