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Protein

Elongation factor 2

Gene

Eef2

Organism
Rattus norvegicus (Rat)
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

  • 5S rRNA binding Source: RGD
  • actin filament binding Source: RGD
  • GTPase activity Source: Ensembl
  • GTP binding Source: UniProtKB-KW
  • p53 binding Source: RGD
  • protein kinase 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

Keywordsi

Molecular functionElongation factor
Biological processProtein biosynthesis
LigandGTP-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
R-RNO-8876725 Protein methylation

Names & Taxonomyi

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

Organism-specific databases

RGDi61979 Eef2

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

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-2DPAGEi0004: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 kinase binding Source: Ensembl

Protein-protein interaction databases

BioGridi248199, 5 interactors
IntActiP05197, 6 interactors
MINTiP05197
STRINGi10116.ENSRNOP00000041821

Structurei

3D structure databases

ProteinModelPortaliP05197
SMRiP05197
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
InParanoidiP05197
KOiK03234
OMAiEHLISGM
OrthoDBiEOG091G0A2J
PhylomeDBiP05197
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.

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

Similar proteinsi

Entry informationi

Entry nameiEF2_RAT
AccessioniPrimary (citable) accession number: P05197
Secondary accession number(s): P97619
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: June 20, 2018
This is version 169 of the entry and version 4 of the sequence. See 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

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