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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)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi14 – 218GTPBy similarity
Nucleotide bindingi91 – 955GTPBy similarity
Nucleotide bindingi153 – 1564GTPBy similarity

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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 463463Elongation factor 1-alpha 2PRO_0000090893Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei55 – 551N6,N6,N6-trimethyllysine1 Publication
Modified residuei165 – 1651N6,N6,N6-trimethyllysine1 Publication
Modified residuei179 – 1791N6-acetyllysineBy similarity
Modified residuei224 – 2241PhosphoserineBy similarity
Modified residuei301 – 30115-glutamyl glycerylphosphorylethanolamine1 Publication
Modified residuei374 – 37415-glutamyl glycerylphosphorylethanolamine1 Publication
Modified residuei439 – 4391N6-acetyllysineBy similarity

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 interactions.
MINTiMINT-7302877.

Structurei

Secondary structure

1
463
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 137Combined sources
Helixi20 – 3011Combined sources
Helixi36 – 4611Combined sources
Turni55 – 573Combined sources
Helixi58 – 658Combined sources
Helixi76 – 783Combined sources
Beta strandi79 – 813Combined sources
Beta strandi86 – 916Combined sources
Beta strandi93 – 953Combined sources
Helixi98 – 1036Combined sources
Beta strandi110 – 1167Combined sources
Helixi122 – 1276Combined sources
Helixi132 – 14211Combined sources
Beta strandi147 – 1526Combined sources
Helixi155 – 1573Combined sources
Beta strandi158 – 1603Combined sources
Helixi164 – 18118Combined sources
Helixi185 – 1873Combined sources
Beta strandi190 – 1923Combined sources
Turni195 – 1973Combined sources
Beta strandi201 – 2033Combined sources
Beta strandi214 – 2163Combined sources
Beta strandi223 – 2275Combined sources
Helixi228 – 2347Combined sources
Helixi241 – 2433Combined sources
Beta strandi247 – 25610Combined sources
Turni257 – 2593Combined sources
Beta strandi260 – 2667Combined sources
Beta strandi277 – 2815Combined sources
Turni282 – 2843Combined sources
Beta strandi285 – 29814Combined sources
Beta strandi307 – 3137Combined sources
Helixi317 – 3193Combined sources
Beta strandi325 – 3284Combined sources
Beta strandi337 – 34610Combined sources
Beta strandi360 – 3634Combined sources
Beta strandi366 – 3716Combined sources
Beta strandi377 – 3793Combined sources
Turni381 – 3833Combined sources
Beta strandi386 – 3905Combined sources
Beta strandi392 – 3943Combined sources
Beta strandi399 – 40810Combined sources
Turni415 – 4173Combined sources
Helixi419 – 4213Combined sources
Beta strandi422 – 4287Combined sources
Beta strandi431 – 44313Combined sources
Turni452 – 4543Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4C0SX-ray2.70A/B1-463[»]
ProteinModelPortaliQ71V39.
SMRiQ71V39. Positions 4-445.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 242238tr-type GAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni14 – 218G1By similarity
Regioni70 – 745G2By similarity
Regioni91 – 944G3By similarity
Regioni153 – 1564G4By similarity
Regioni194 – 1963G5By similarity

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
EntryMethodResolution (Å)ChainPositionsPDBsum
4C0SX-ray2.70A/B1-463[»]
ProteinModelPortaliQ71V39.
SMRiQ71V39. Positions 4-445.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ71V39. 5 interactions.
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: July 6, 2016
This is version 80 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.