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Protein

Elongation factor 2

Gene

EEF2

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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 (By similarity).By similarity

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi26 – 33GTPBy similarity8
Nucleotide bindingi104 – 108GTPBy similarity5
Nucleotide bindingi158 – 161GTPBy similarity4

GO - Molecular functioni

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

Names & Taxonomyi

Protein namesi
Recommended name:
Elongation factor 2
Short name:
EF-2
Gene namesi
Name:EEF2
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 7

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

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00002234862 – 858Elongation factor 2Add BLAST857

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei54PhosphothreonineBy similarity1
Modified residuei57Phosphothreonine; by EEF2KBy similarity1
Modified residuei59PhosphothreonineBy similarity1
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 residuei325PhosphoserineBy similarity1
Modified residuei373Phosphotyrosine; by CSKBy similarity1
Modified residuei435PhosphothreonineBy similarity1
Modified residuei439N6-acetyllysineBy similarity1
Modified residuei445N6-acetyllysineBy similarity1
Modified residuei502PhosphoserineBy similarity1
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 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.By similarity
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.By similarity
Proteolytically processed at two sites following phosphorylation by CSK.By similarity
SUMOylated following phosphorylation by CSK, promotes proteolytic cleavage.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei586 – 587CleavageBy similarity2
Sitei605 – 606CleavageBy similarity2

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ3SYU2.
PeptideAtlasiQ3SYU2.
PRIDEiQ3SYU2.

Expressioni

Gene expression databases

BgeeiENSBTAG00000004258.

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

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000005581.

Structurei

3D structure databases

ProteinModelPortaliQ3SYU2.
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.
InParanoidiQ3SYU2.
KOiK03234.
OMAiFTGHVTR.
OrthoDBiEOG091G0A2J.
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.

Q3SYU2-1 [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 EGQLGPAERA
260 270 280 290 300
KKVEDMMKKL WGDRYFDPAT GKFSKSANSP DGKKLPRTFC 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 FEETQVAGTP MFVVKAYLPV NESFGFTADL
810 820 830 840 850
RSNTGGQAFP QCVFDHWQIL PGDPFDNTSR PSQVVAETRK RKGLKEGIPA

LDNFLDKL
Length:858
Mass (Da):95,368
Last modified:January 23, 2007 - v3
Checksum:iC2A09963892992C6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC103385 mRNA. Translation: AAI03386.1.
RefSeqiNP_001068589.1. NM_001075121.1.
UniGeneiBt.39668.

Genome annotation databases

EnsembliENSBTAT00000005581; ENSBTAP00000005581; ENSBTAG00000004258.
GeneIDi281138.
KEGGibta:281138.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC103385 mRNA. Translation: AAI03386.1.
RefSeqiNP_001068589.1. NM_001075121.1.
UniGeneiBt.39668.

3D structure databases

ProteinModelPortaliQ3SYU2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000005581.

Proteomic databases

PaxDbiQ3SYU2.
PeptideAtlasiQ3SYU2.
PRIDEiQ3SYU2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000005581; ENSBTAP00000005581; ENSBTAG00000004258.
GeneIDi281138.
KEGGibta:281138.

Organism-specific databases

CTDi1938.

Phylogenomic databases

eggNOGiKOG0469. Eukaryota.
COG0480. LUCA.
GeneTreeiENSGT00860000133841.
HOGENOMiHOG000231589.
HOVERGENiHBG001838.
InParanoidiQ3SYU2.
KOiK03234.
OMAiFTGHVTR.
OrthoDBiEOG091G0A2J.
TreeFamiTF300575.

Enzyme and pathway databases

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

Gene expression databases

BgeeiENSBTAG00000004258.

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_BOVIN
AccessioniPrimary (citable) accession number: Q3SYU2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2006
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 89 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, 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.