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Protein

Elongation factor 1-alpha 2

Gene

EEF1A2

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi14 – 21GTPBy similarity8
Nucleotide bindingi91 – 95GTPBy similarity5
Nucleotide bindingi153 – 156GTPBy similarity4

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Elongation factor

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Elongation factor 1-alpha 2
Short name:
EF-1-alpha-2
Alternative name(s):
Eukaryotic elongation factor 1 A-2
Short name:
eEF1A-2
Statin-S1
Gene namesi
Name:EEF1A2
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
Proteomesi
  • UP000001811 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000908931 – 463Elongation factor 1-alpha 2Add BLAST463

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei55N6,N6,N6-trimethyllysine1 Publication1
Modified residuei79N6,N6,N6-trimethyllysineBy similarity1
Modified residuei165N6,N6,N6-trimethyllysine; alternate1 Publication1
Modified residuei165N6,N6-dimethyllysine; alternateBy similarity1
Modified residuei165N6-methyllysine; alternateBy similarity1
Modified residuei179N6-acetyllysineBy similarity1
Modified residuei224PhosphoserineBy similarity1
Modified residuei3015-glutamyl glycerylphosphorylethanolamine1 Publication1
Modified residuei3745-glutamyl glycerylphosphorylethanolamine1 Publication1
Modified residuei439N6-acetyllysineBy similarity1

Post-translational modificationi

Methylated.1 Publication

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

PRIDEiQ71V39.

Expressioni

Tissue specificityi

Expressed in skeletal muscle, heart, brain and aorta. Not expressed in liver, kidney, spleen and lung.

Interactioni

Subunit structurei

Monomer.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
PLCG1P191743EBI-7645815,EBI-79387From a different organism.
PTPN11Q061242EBI-7645815,EBI-297779From a different organism.

Protein-protein interaction databases

IntActiQ71V39. 5 interactors.
MINTiMINT-7302877.

Structurei

Secondary structure

1463
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi7 – 13Combined sources7
Helixi20 – 30Combined sources11
Helixi36 – 46Combined sources11
Turni55 – 57Combined sources3
Helixi58 – 65Combined sources8
Helixi76 – 78Combined sources3
Beta strandi79 – 81Combined sources3
Beta strandi86 – 91Combined sources6
Beta strandi93 – 95Combined sources3
Helixi98 – 103Combined sources6
Beta strandi110 – 116Combined sources7
Helixi122 – 127Combined sources6
Helixi132 – 142Combined sources11
Beta strandi147 – 152Combined sources6
Helixi155 – 157Combined sources3
Beta strandi158 – 160Combined sources3
Helixi164 – 181Combined sources18
Helixi185 – 187Combined sources3
Beta strandi190 – 192Combined sources3
Turni195 – 197Combined sources3
Beta strandi201 – 203Combined sources3
Beta strandi214 – 216Combined sources3
Beta strandi223 – 227Combined sources5
Helixi228 – 234Combined sources7
Helixi241 – 243Combined sources3
Beta strandi247 – 256Combined sources10
Turni257 – 259Combined sources3
Beta strandi260 – 266Combined sources7
Beta strandi277 – 281Combined sources5
Turni282 – 284Combined sources3
Beta strandi285 – 298Combined sources14
Beta strandi307 – 313Combined sources7
Helixi317 – 319Combined sources3
Beta strandi325 – 328Combined sources4
Beta strandi337 – 346Combined sources10
Beta strandi360 – 363Combined sources4
Beta strandi366 – 371Combined sources6
Beta strandi377 – 379Combined sources3
Turni381 – 383Combined sources3
Beta strandi386 – 390Combined sources5
Beta strandi392 – 394Combined sources3
Beta strandi399 – 408Combined sources10
Turni415 – 417Combined sources3
Helixi419 – 421Combined sources3
Beta strandi422 – 428Combined sources7
Beta strandi431 – 443Combined sources13
Turni452 – 454Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4C0SX-ray2.70A/B1-463[»]
ProteinModelPortaliQ71V39.
SMRiQ71V39.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini5 – 242tr-type GAdd BLAST238

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni14 – 21G1By similarity8
Regioni70 – 74G2By similarity5
Regioni91 – 94G3By similarity4
Regioni153 – 156G4By similarity4
Regioni194 – 196G5By similarity3

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000229291.
HOVERGENiHBG000179.
InParanoidiQ71V39.
KOiK03231.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00118_A. EF_Tu_A. 1 hit.
InterProiIPR004161. EFTu-like_2.
IPR031157. G_TR_CS.
IPR027417. P-loop_NTPase.
IPR000795. TF_GTP-bd_dom.
IPR009000. Transl_B-barrel.
IPR009001. Transl_elong_EF1A/Init_IF2_C.
IPR004539. Transl_elong_EF1A_euk/arc.
IPR004160. Transl_elong_EFTu/EF1A_C.
[Graphical view]
PfamiPF03144. GTP_EFTU_D2. 1 hit.
PF03143. GTP_EFTU_D3. 1 hit.
[Graphical view]
PRINTSiPR00315. ELONGATNFCT.
SUPFAMiSSF50447. SSF50447. 1 hit.
SSF50465. SSF50465. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00483. EF-1_alpha. 1 hit.
PROSITEiPS00301. G_TR_1. 1 hit.
PS51722. G_TR_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q71V39-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGKEKTHINI VVIGHVDSGK STTTGHLIYK CGGIDKRTIE KFEKEAAEMG
60 70 80 90 100
KGSFKYAWVL DKLKAERERG ITIDISLWKF ETTKYYITII DAPGHRDFIK
110 120 130 140 150
NMITGTSQAD CAVLIVAAGV GEFEAGISKN GQTREHALLA YTLGVKQLIV
160 170 180 190 200
GVNKMDSTEP AYSEKRYDEI VKEVSAYIKK IGYNPATVPF VPISGWHGDN
210 220 230 240 250
MLEPSPNMPW FKGWKVERKE GNASGVSLLE ALDTILPPTR PTDKPLRLPL
260 270 280 290 300
QDVYKIGGIG TVPVGRVETG ILRPGMVVTF APVNITTEVK SVEMHHEALS
310 320 330 340 350
EALPGDNVGF NVKNVSVKDI RRGNVCGDSK SDPPQEAAQF TSQVIILNHP
360 370 380 390 400
GQISAGYSPV IDCHTAHIAC KFAELKEKID RRSGKKLEDN PKSLKSGDAA
410 420 430 440 450
IVEMVPGKPM CVESFSQYPP LGRFAVRDMR QTVAVGVIKN VEKKSGGAGK
460
VTKSAQKAQK AGK
Length:463
Mass (Da):50,470
Last modified:July 5, 2004 - v1
Checksum:i31E4E341CEE797EC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF035178 mRNA. Translation: AAC39252.1.
RefSeqiNP_001075500.1. NM_001082031.1.
UniGeneiOcu.6265.

Genome annotation databases

GeneIDi100008677.
KEGGiocu:100008677.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF035178 mRNA. Translation: AAC39252.1.
RefSeqiNP_001075500.1. NM_001082031.1.
UniGeneiOcu.6265.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4C0SX-ray2.70A/B1-463[»]
ProteinModelPortaliQ71V39.
SMRiQ71V39.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ71V39. 5 interactors.
MINTiMINT-7302877.

Proteomic databases

PRIDEiQ71V39.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100008677.
KEGGiocu:100008677.

Organism-specific databases

CTDi1917.

Phylogenomic databases

HOGENOMiHOG000229291.
HOVERGENiHBG000179.
InParanoidiQ71V39.
KOiK03231.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00118_A. EF_Tu_A. 1 hit.
InterProiIPR004161. EFTu-like_2.
IPR031157. G_TR_CS.
IPR027417. P-loop_NTPase.
IPR000795. TF_GTP-bd_dom.
IPR009000. Transl_B-barrel.
IPR009001. Transl_elong_EF1A/Init_IF2_C.
IPR004539. Transl_elong_EF1A_euk/arc.
IPR004160. Transl_elong_EFTu/EF1A_C.
[Graphical view]
PfamiPF03144. GTP_EFTU_D2. 1 hit.
PF03143. GTP_EFTU_D3. 1 hit.
[Graphical view]
PRINTSiPR00315. ELONGATNFCT.
SUPFAMiSSF50447. SSF50447. 1 hit.
SSF50465. SSF50465. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00483. EF-1_alpha. 1 hit.
PROSITEiPS00301. G_TR_1. 1 hit.
PS51722. G_TR_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiEF1A2_RABIT
AccessioniPrimary (citable) accession number: Q71V39
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 25, 2004
Last sequence update: July 5, 2004
Last modified: November 2, 2016
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

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

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.