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Protein

Elongation factor 2

Gene

EEF2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi26 – 338GTPBy similarity
Nucleotide bindingi104 – 1085GTPBy similarity
Nucleotide bindingi158 – 1614GTPBy similarity

GO - Molecular functioni

  • 5S rRNA binding Source: Ensembl
  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
  • GTPase activity Source: GO_Central
  • GTP binding Source: UniProtKB-KW
  • poly(A) RNA binding Source: UniProtKB
  • protein kinase binding Source: UniProtKB
  • ribosome binding Source: Ensembl
  • translation elongation factor activity Source: UniProtKB-KW

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Elongation factor

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

GTP-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.
SIGNORiP13639.

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

HGNCiHGNC:3214. EEF2.

Subcellular locationi

GO - Cellular componenti

  • aggresome Source: HPA
  • cell-cell adherens junction Source: BHF-UCL
  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • extracellular matrix Source: BHF-UCL
  • intracellular ribonucleoprotein complex Source: MGI
  • membrane Source: UniProtKB
  • membrane raft Source: Ensembl
  • nucleus Source: UniProtKB
  • plasma membrane Source: HPA
  • polysomal ribosome Source: Ensembl
Complete GO annotation...

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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti596 – 5961P → H in SCA26; compromises the mechanics of translocation. 1 Publication
Corresponds to variant rs587777052 [ dbSNP | Ensembl ].
VAR_070792

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi595 – 5951S → A: Strongly reduced phosphorylation at Thr-57. 1 Publication
Mutagenesisi599 – 5991H → P: Strongly reduced phosphorylation at Thr-57. 1 Publication

Keywords - Diseasei

Disease mutation, Neurodegeneration, Spinocerebellar ataxia

Organism-specific databases

MalaCardsiEEF2.
MIMi609306. phenotype.
Orphaneti101112. Spinocerebellar ataxia type 26.
PharmGKBiPA27650.

Chemistry

ChEMBLiCHEMBL1795108.

Polymorphism and mutation databases

BioMutaiEEF2.
DMDMi119172.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources1 Publication
Chaini2 – 858857Elongation factor 2PRO_0000091000Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei54 – 541PhosphothreonineCombined sources
Modified residuei57 – 571Phosphothreonine; by EEF2KCombined sources1 Publication
Modified residuei59 – 591PhosphothreonineCombined sources
Modified residuei152 – 1521N6-succinyllysineBy similarity
Modified residuei235 – 2351N6-acetyllysineCombined sources
Modified residuei239 – 2391N6-acetyllysine; alternateCombined sources
Cross-linki239 – 239Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources
Modified residuei265 – 2651Phosphotyrosine; by CSK1 Publication
Modified residuei272 – 2721N6-acetyllysine; alternateCombined sources
Modified residuei272 – 2721N6-succinyllysine; alternateBy similarity
Modified residuei275 – 2751N6-acetyllysineCombined sources
Cross-linki322 – 322Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Modified residuei325 – 3251PhosphoserineBy similarity
Modified residuei373 – 3731Phosphotyrosine; by CSK1 Publication
Modified residuei435 – 4351PhosphothreonineCombined sources
Modified residuei439 – 4391N6-acetyllysineBy similarity
Modified residuei445 – 4451N6-acetyllysineCombined sources
Modified residuei502 – 5021PhosphoserineCombined sources
Modified residuei525 – 5251N6,N6,N6-trimethyllysine; by EEF2KMT1 Publication
Cross-linki529 – 529Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Modified residuei572 – 5721N6-succinyllysineBy similarity
Modified residuei595 – 5951Phosphoserine; by CDK2Combined sources1 Publication
Modified residuei619 – 6191N6-acetyllysineBy similarity
Modified residuei715 – 7151DiphthamideBy similarity

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)LengthDescriptionGraphical viewFeature identifierActions
Sitei586 – 5872Cleavage1 Publication
Sitei605 – 6062Cleavage1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP13639.
MaxQBiP13639.
PaxDbiP13639.
PeptideAtlasiP13639.
PRIDEiP13639.

2D gel databases

REPRODUCTION-2DPAGEIPI00186290.

PTM databases

iPTMnetiP13639.
PhosphoSiteiP13639.
SwissPalmiP13639.

Expressioni

Gene expression databases

BgeeiENSG00000167658.
CleanExiHS_EEF2.
ExpressionAtlasiP13639. baseline and differential.
GenevisibleiP13639. HS.

Organism-specific databases

HPAiCAB007795.
HPA040534.

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 a different organism.

GO - Molecular functioni

  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
  • protein kinase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi108258. 176 interactions.
IntActiP13639. 62 interactions.
MINTiMINT-4999025.
STRINGi9606.ENSP00000307940.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Xelectron microscopy5.00Az1-858[»]
ProteinModelPortaliP13639.
SMRiP13639. Positions 2-858.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini17 – 362346tr-type GPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 subfamily.PROSITE-ProRule annotation
Contains 1 tr-type G (guanine nucleotide-binding) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0469. Eukaryota.
COG0480. LUCA.
GeneTreeiENSGT00840000129841.
HOGENOMiHOG000231589.
HOVERGENiHBG001838.
InParanoidiP13639.
KOiK03234.
OMAiFTGHVTR.
OrthoDBiEOG091G0A2J.
PhylomeDBiP13639.
TreeFamiTF300575.

Family and domain databases

Gene3Di3.30.230.10. 1 hit.
3.30.70.240. 1 hit.
3.40.50.300. 1 hit.
InterProiIPR009022. EFG_III-V.
IPR000640. EFG_V.
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.
IPR005517. Transl_elong_EFG/EF2_IV.
[Graphical view]
PfamiPF00679. EFG_C. 1 hit.
PF14492. EFG_II. 1 hit.
PF03764. EFG_IV. 1 hit.
PF03144. GTP_EFTU_D2. 1 hit.
[Graphical view]
PRINTSiPR00315. ELONGATNFCT.
SMARTiSM00838. EFG_C. 1 hit.
SM00889. EFG_IV. 1 hit.
[Graphical view]
SUPFAMiSSF50447. SSF50447. 1 hit.
SSF52540. SSF52540. 1 hit.
SSF54211. SSF54211. 1 hit.
SSF54980. SSF54980. 2 hits.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS00301. G_TR_1. 1 hit.
PS51722. G_TR_2. 1 hit.
[Graphical view]

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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti596 – 5961P → H in SCA26; compromises the mechanics of translocation. 1 Publication
Corresponds to variant rs587777052 [ dbSNP | Ensembl ].
VAR_070792

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.

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
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Xelectron microscopy5.00Az1-858[»]
ProteinModelPortaliP13639.
SMRiP13639. Positions 2-858.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108258. 176 interactions.
IntActiP13639. 62 interactions.
MINTiMINT-4999025.
STRINGi9606.ENSP00000307940.

Chemistry

ChEMBLiCHEMBL1795108.

PTM databases

iPTMnetiP13639.
PhosphoSiteiP13639.
SwissPalmiP13639.

Polymorphism and mutation databases

BioMutaiEEF2.
DMDMi119172.

2D gel databases

REPRODUCTION-2DPAGEIPI00186290.

Proteomic databases

EPDiP13639.
MaxQBiP13639.
PaxDbiP13639.
PeptideAtlasiP13639.
PRIDEiP13639.

Protocols and materials databases

DNASUi1938.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi1938.
GeneCardsiEEF2.
HGNCiHGNC:3214. EEF2.
HPAiCAB007795.
HPA040534.
MalaCardsiEEF2.
MIMi130610. gene.
609306. phenotype.
neXtProtiNX_P13639.
Orphaneti101112. Spinocerebellar ataxia type 26.
PharmGKBiPA27650.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0469. Eukaryota.
COG0480. LUCA.
GeneTreeiENSGT00840000129841.
HOGENOMiHOG000231589.
HOVERGENiHBG001838.
InParanoidiP13639.
KOiK03234.
OMAiFTGHVTR.
OrthoDBiEOG091G0A2J.
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.
SIGNORiP13639.

Miscellaneous databases

ChiTaRSiEEF2. human.
GeneWikiiEEF2.
GenomeRNAii1938.
PROiP13639.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000167658.
CleanExiHS_EEF2.
ExpressionAtlasiP13639. baseline and differential.
GenevisibleiP13639. HS.

Family and domain databases

Gene3Di3.30.230.10. 1 hit.
3.30.70.240. 1 hit.
3.40.50.300. 1 hit.
InterProiIPR009022. EFG_III-V.
IPR000640. EFG_V.
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.
IPR005517. Transl_elong_EFG/EF2_IV.
[Graphical view]
PfamiPF00679. EFG_C. 1 hit.
PF14492. EFG_II. 1 hit.
PF03764. EFG_IV. 1 hit.
PF03144. GTP_EFTU_D2. 1 hit.
[Graphical view]
PRINTSiPR00315. ELONGATNFCT.
SMARTiSM00838. EFG_C. 1 hit.
SM00889. EFG_IV. 1 hit.
[Graphical view]
SUPFAMiSSF50447. SSF50447. 1 hit.
SSF52540. SSF52540. 1 hit.
SSF54211. SSF54211. 1 hit.
SSF54980. SSF54980. 2 hits.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS00301. G_TR_1. 1 hit.
PS51722. G_TR_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiEF2_HUMAN
AccessioniPrimary (citable) accession number: P13639
Secondary accession number(s): B2RMP5, D6W618, Q58J86
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 23, 2007
Last modified: September 7, 2016
This is version 185 of the entry and version 4 of the sequence. [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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.