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Protein

Elongation factor 1-alpha 1

Gene

EEF1A1

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed-Annotation score: Annotation score: 5 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. With PARP1 and TXK, forms a complex that acts as a T helper 1 (Th1) cell-specific transcription factor and binds the promoter of IFN-gamma to directly regulate its transcription, and is thus involved importantly in Th1 cytokine production.By similarity

Regions

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

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionElongation factor
Biological processProtein biosynthesis
LigandGTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Elongation factor 1-alpha 1
Short name:
EF-1-alpha-1
Alternative name(s):
Elongation factor Tu
Short name:
EF-Tu
Eukaryotic elongation factor 1 A-1
Short name:
eEF1A-1
Gene namesi
Name:EEF1A1
Synonyms:EEF1A, EF1A
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
Proteomesi
  • UP000001811 Componenti: Chromosome 12

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

Cell membrane, Cytoplasm, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000908892 – 462Elongation factor 1-alpha 1Add BLAST461

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N,N,N-trimethylglycineBy similarity1
Modified residuei36N6,N6,N6-trimethyllysine1 Publication1
Modified residuei55N6,N6-dimethyllysine1 Publication1
Modified residuei79N6,N6,N6-trimethyllysine; by EEF1AKMT11 Publication1
Modified residuei165N6,N6,N6-trimethyllysine; alternate; by EEF1AKMT3By similarity1
Modified residuei165N6,N6-dimethyllysine; alternate; by EEF1AKMT31 Publication1
Modified residuei165N6-acetyllysine; alternateBy similarity1
Modified residuei165N6-methyllysine; alternate; by EEF1AKMT3By similarity1
Modified residuei172N6-acetyllysineBy similarity1
Modified residuei224PhosphoserineBy similarity1
Modified residuei273N6-acetyllysineBy similarity1
Modified residuei300Phosphoserine; by TGFBR1By similarity1
Modified residuei3015-glutamyl glycerylphosphorylethanolamine1 Publication1
Modified residuei318N6,N6,N6-trimethyllysine; by EEF1AKMT21 Publication1
Modified residuei3745-glutamyl glycerylphosphorylethanolamine1 Publication1
Modified residuei392N6-acetyllysine; alternateBy similarity1
Modified residuei392N6-succinyllysine; alternateBy similarity1
Modified residuei432Phosphothreonine; by PASKBy similarity1
Modified residuei439N6-acetyllysineBy similarity1

Post-translational modificationi

The N-terminus is blocked.1 Publication
ISGylated.By similarity
Phosphorylated by TXK. Phosphorylation by PASK increases translation efficiency. Phosphorylated by ROCK2.By similarity
Trimethylated at Lys-79 by EEF1AKMT1. Methylated at Lys-165 by EEF1AKMT3, methylation by EEF1AKMT3 is dynamic as well as inducible by stress conditions, such as ER-stress, and plays a regulatory role on mRNA translation. Trimethylated at Lys-318 by EEF1AKMT2.By similarity

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PRIDEiP68105.

PTM databases

iPTMnetiP68105.

Expressioni

Tissue specificityi

Brain, placenta, lung, liver, kidney, pancreas but barely detectable in heart and skeletal muscle.

Gene expression databases

BgeeiENSOCUG00000008481.

Interactioni

Subunit structurei

Found in a nuclear export complex with XPO5, EEF1A1, Ran and aminoacylated tRNA. Interacts with PARP1, TXK, XPO5 and KARS. May interact with ERGIC2. Interacts with IFIT1 (via TPR repeats 4-7) (By similarity). Interacts with DLC1, facilitating distribution to the membrane periphery and ruffles upon growth factor stimulation. Interacts with ZPR1; the interaction occurs in a epidermal growth factor (EGF)-dependent manner (By similarity). Interacts with PPP1R16B (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
PTPN11Q061242EBI-7645934,EBI-297779From Homo sapiens.

GO - Molecular functioni

Protein-protein interaction databases

IntActiP68105. 6 interactors.
MINTiMINT-233670.
STRINGi9986.ENSOCUP00000007327.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5LZSelectron microscopy3.31jj1-462[»]
ProteinModelPortaliP68105.
SMRiP68105.
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

eggNOGiKOG0052. Eukaryota.
COG5256. LUCA.
GeneTreeiENSGT00670000097815.
HOVERGENiHBG000179.
InParanoidiP68105.
KOiK03231.
OMAiPAKETKM.
OrthoDBiEOG091G05LW.
TreeFamiTF300304.

Family and domain databases

HAMAPiMF_00118_A. EF_Tu_A. 1 hit.
InterProiView protein in InterPro
IPR004161. EFTu-like_2.
IPR031157. G_TR_CS.
IPR027417. P-loop_NTPase.
IPR000795. TF_GTP-bd_dom.
IPR009000. Transl_B-barrel_sf.
IPR009001. Transl_elong_EF1A/Init_IF2_C.
IPR004539. Transl_elong_EF1A_euk/arc.
IPR004160. Transl_elong_EFTu/EF1A_C.
PfamiView protein in Pfam
PF00009. GTP_EFTU. 1 hit.
PF03144. GTP_EFTU_D2. 1 hit.
PF03143. GTP_EFTU_D3. 1 hit.
PRINTSiPR00315. ELONGATNFCT.
SUPFAMiSSF50447. SSF50447. 1 hit.
SSF50465. SSF50465. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00483. EF-1_alpha. 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.

P68105-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGKEKTHINI VVIGHVDSGK STTTGHLIYK CGGIDKRTIE KFEKEAAEMG
60 70 80 90 100
KGSFKYAWVL DKLKAERERG ITIDISLWKF ETSKYYVTII DAPGHRDFIK
110 120 130 140 150
NMITGTSQAD CAVLIVAAGV GEFEAGISKN GQTREHALLA YTLGVKQLIV
160 170 180 190 200
GVNKMDSTEP PYSQKRYEEI VKEVSTYIKK IGYNPDTVAF VPISGWNGDN
210 220 230 240 250
MLEPSANMPW FKGWKVTRKD GNASGTTLLE ALDCILPPTR PTDKPLRLPL
260 270 280 290 300
QDVYKIGGIG TVPVGRVETG VLKPGMVVTF APVNVTTEVK SVEMHHEALS
310 320 330 340 350
EALPGDNVGF NVKNVSVKDV RRGNVAGDSK NDPPMEAAGF TAQVIILNHP
360 370 380 390 400
GQISAGYAPV LDCHTAHIAC KFAELKEKID RRSGKKLEDG PKFLKSGDAA
410 420 430 440 450
IVDMVPGKPM CVESFSDYPP LGRFAVRDMR QTVAVGVIKA VDKKAAGAGK
460
VTKSAQKAQK AK
Length:462
Mass (Da):50,141
Last modified:August 13, 1987 - v1
Checksum:iD465615545AF686A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X62245 mRNA. Translation: CAA44162.1.
U09823 mRNA. Translation: AAA18502.1.
PIRiS22583. EFRB1.
RefSeqiNP_001075808.1. NM_001082339.1.
UniGeneiOcu.1580.

Genome annotation databases

EnsembliENSOCUT00000008477; ENSOCUP00000007327; ENSOCUG00000008481.
GeneIDi100009189.
KEGGiocu:100009189.

Similar proteinsi

Entry informationi

Entry nameiEF1A1_RABIT
AccessioniPrimary (citable) accession number: P68105
Secondary accession number(s): P04719, P04720
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: November 22, 2017
This is version 106 of the entry and version 1 of the sequence. See 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