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Protein

Elongation factor 2

Gene

Eef2

Organism
Rattus norvegicus (Rat)
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)DescriptionActionsGraphical viewLength
Nucleotide bindingi26 – 33GTPBy similarity8
Nucleotide bindingi104 – 108GTPBy similarity5
Nucleotide bindingi158 – 161GTPBy similarity4

GO - Molecular functioni

  • 5S rRNA binding Source: RGD
  • actin filament binding Source: RGD
  • GTPase activity Source: GO_Central
  • GTP binding Source: UniProtKB-KW
  • p53 binding Source: RGD
  • poly(A) RNA binding Source: Ensembl
  • ribosome binding Source: RGD
  • RNA binding Source: RGD
  • translation elongation factor activity Source: RGD

GO - Biological processi

  • aging Source: RGD
  • cellular response to brain-derived neurotrophic factor stimulus Source: RGD
  • glial cell proliferation Source: RGD
  • hematopoietic progenitor cell differentiation Source: Ensembl
  • positive regulation of cytoplasmic translation Source: RGD
  • positive regulation of translation Source: RGD
  • response to drug Source: RGD
  • response to endoplasmic reticulum stress Source: RGD
  • response to estradiol Source: RGD
  • response to ethanol Source: RGD
  • response to folic acid Source: RGD
  • response to hydrogen peroxide Source: RGD
  • response to ischemia Source: RGD
  • skeletal muscle cell differentiation Source: RGD
  • skeletal muscle contraction Source: RGD
  • translational elongation Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Elongation factor

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-RNO-156902. Peptide chain elongation.
R-RNO-5358493. Synthesis of diphthamide-EEF2.
R-RNO-6798695. Neutrophil degranulation.

Names & Taxonomyi

Protein namesi
Recommended name:
Elongation factor 2
Short name:
EF-2
Gene namesi
Name:Eef2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 7

Organism-specific databases

RGDi61979. Eef2.

Subcellular locationi

  • Cytoplasm By similarity
  • Nucleus By similarity

  • Note: Phosphorylation by CSK promotes cleavage and SUMOylation-dependent nuclear translocation of the C-terminal cleavage product.By similarity

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000910042 – 858Elongation factor 2Add BLAST857

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei54PhosphothreonineBy similarity1
Modified residuei57Phosphothreonine; by EEF2KCombined sources1 Publication1
Modified residuei59PhosphothreonineCombined sources1
Modified residuei152N6-succinyllysineBy similarity1
Modified residuei235N6-acetyllysineBy similarity1
Modified residuei239N6-acetyllysine; alternateBy similarity1
Cross-linki239Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity
Modified residuei265Phosphotyrosine; by CSKBy similarity1
Modified residuei272N6-acetyllysine; alternateBy similarity1
Modified residuei272N6-succinyllysine; alternateBy similarity1
Modified residuei275N6-acetyllysineBy similarity1
Cross-linki322Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei325PhosphoserineCombined sources1
Modified residuei373Phosphotyrosine; by CSKBy similarity1
Modified residuei435PhosphothreonineCombined sources1
Modified residuei439N6-acetyllysineBy similarity1
Modified residuei445N6-acetyllysineBy similarity1
Modified residuei502PhosphoserineCombined sources1
Modified residuei525N6,N6,N6-trimethyllysine; by EEF2KMTBy similarity1
Cross-linki529Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei572N6-succinyllysineBy similarity1
Modified residuei595Phosphoserine; by CDK2By similarity1
Modified residuei619N6-acetyllysineBy similarity1
Modified residuei715Diphthamide1 Publication1

Post-translational modificationi

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.1 Publication
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.By similarity
Proteolytically processed at two sites following phosphorylation by CSK.By similarity
SUMOylated following phosphorylation by CSK, promotes proteolytic cleavage.By similarity
ISGylated.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP05197.
PRIDEiP05197.

2D gel databases

World-2DPAGE0004:P05197.

PTM databases

iPTMnetiP05197.
PhosphoSitePlusiP05197.

Expressioni

Gene expression databases

BgeeiENSRNOG00000020266.
GenevisibleiP05197. RN.

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. Interacts with RBPMS2.By similarity

GO - Molecular functioni

  • actin filament binding Source: RGD
  • p53 binding Source: RGD

Protein-protein interaction databases

BioGridi248199. 5 interactors.
IntActiP05197. 4 interactors.
MINTiMINT-4568758.
STRINGi10116.ENSRNOP00000041821.

Structurei

3D structure databases

ProteinModelPortaliP05197.
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
Contains 1 tr-type G (guanine nucleotide-binding) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0469. Eukaryota.
COG0480. LUCA.
GeneTreeiENSGT00860000133841.
HOGENOMiHOG000231589.
HOVERGENiHBG001838.
InParanoidiP05197.
KOiK03234.
OMAiFTGHVTR.
OrthoDBiEOG091G0A2J.
PhylomeDBiP05197.
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.

P05197-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVNFTVDQIR AIMDKKANIR NMSVIAHVDH GKSTLTDSLV CKAGIIASAR
60 70 80 90 100
AGETRFTDTR KDEQERCITI KSTAISLFYE LSENDLNFIK QSKDGSGFLI
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 EGQLGAAERA
260 270 280 290 300
KKVEDMMKKL WGDRYFDPAN GKFSKSANSP DGKKLPRTFC QLILDPIFKV
310 320 330 340 350
FDAIMNFRKE ETAKLIEKLD IKLDSEDKDK EGKPLLKAVM RRWLPAGDAL
360 370 380 390 400
LQMITIHLPS PVTAQKYRCE LLYEGPPDDE AAMGIKSCDP KGPLMMYISK
410 420 430 440 450
MVPTSDKGRF YAFGRVFSGV 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 EVSARQELKA 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):95,284
Last modified:January 23, 2007 - v4
Checksum:iD6F7A61BADD4B137
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC066661 mRNA. Translation: AAH66661.1.
K03502 mRNA. Translation: AAA41106.1.
Y07504 mRNA. Translation: CAA68805.1.
U75403 mRNA. Translation: AAB19107.1.
AF000576 mRNA. Translation: AAD05363.1.
PIRiS04007. EFRT2.
RefSeqiNP_058941.1. NM_017245.2.
UniGeneiRn.55145.

Genome annotation databases

EnsembliENSRNOT00000047450; ENSRNOP00000041821; ENSRNOG00000020266.
GeneIDi29565.
KEGGirno:29565.
UCSCiRGD:61979. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC066661 mRNA. Translation: AAH66661.1.
K03502 mRNA. Translation: AAA41106.1.
Y07504 mRNA. Translation: CAA68805.1.
U75403 mRNA. Translation: AAB19107.1.
AF000576 mRNA. Translation: AAD05363.1.
PIRiS04007. EFRT2.
RefSeqiNP_058941.1. NM_017245.2.
UniGeneiRn.55145.

3D structure databases

ProteinModelPortaliP05197.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi248199. 5 interactors.
IntActiP05197. 4 interactors.
MINTiMINT-4568758.
STRINGi10116.ENSRNOP00000041821.

PTM databases

iPTMnetiP05197.
PhosphoSitePlusiP05197.

2D gel databases

World-2DPAGE0004:P05197.

Proteomic databases

PaxDbiP05197.
PRIDEiP05197.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000047450; ENSRNOP00000041821; ENSRNOG00000020266.
GeneIDi29565.
KEGGirno:29565.
UCSCiRGD:61979. rat.

Organism-specific databases

CTDi1938.
RGDi61979. Eef2.

Phylogenomic databases

eggNOGiKOG0469. Eukaryota.
COG0480. LUCA.
GeneTreeiENSGT00860000133841.
HOGENOMiHOG000231589.
HOVERGENiHBG001838.
InParanoidiP05197.
KOiK03234.
OMAiFTGHVTR.
OrthoDBiEOG091G0A2J.
PhylomeDBiP05197.
TreeFamiTF300575.

Enzyme and pathway databases

ReactomeiR-RNO-156902. Peptide chain elongation.
R-RNO-5358493. Synthesis of diphthamide-EEF2.
R-RNO-6798695. Neutrophil degranulation.

Miscellaneous databases

PROiP05197.

Gene expression databases

BgeeiENSRNOG00000020266.
GenevisibleiP05197. RN.

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_RAT
AccessioniPrimary (citable) accession number: P05197
Secondary accession number(s): P97619
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 155 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. 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.