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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).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi14 – 218GTPBy similarity
Nucleotide bindingi91 – 955GTPBy similarity
Nucleotide bindingi153 – 1564GTPBy similarity

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

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

  • Cytoplasm By similarity
  • Nucleus By similarity
  • Nucleusnucleolus By similarity

  • Note: Colocalizes with DLC1 at actin-rich regions in the cell periphery. Translocates together with ZPR1 from the cytoplasm to the nucleus and nucleolus after treatment with mitogens (By similarity).By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 462462Elongation factor 1-alpha 1PRO_0000090889Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei36 – 361N6,N6,N6-trimethyllysine1 Publication
Modified residuei55 – 551N6,N6-dimethyllysine1 Publication
Modified residuei79 – 791N6,N6,N6-trimethyllysine1 Publication
Modified residuei165 – 1651N6,N6-dimethyllysine; alternate1 Publication
Modified residuei165 – 1651N6-acetyllysine; alternateBy similarity
Modified residuei172 – 1721N6-acetyllysineBy similarity
Modified residuei273 – 2731N6-acetyllysineBy similarity
Modified residuei300 – 3001Phosphoserine; by TGFBR1By similarity
Modified residuei301 – 30115-glutamyl glycerylphosphorylethanolamine1 Publication
Modified residuei318 – 3181N6,N6,N6-trimethyllysine1 Publication
Modified residuei374 – 37415-glutamyl glycerylphosphorylethanolamine1 Publication
Modified residuei392 – 3921N6-acetyllysine; alternateBy similarity
Modified residuei392 – 3921N6-succinyllysine; alternateBy similarity
Modified residuei432 – 4321Phosphothreonine; by PASKBy similarity
Modified residuei439 – 4391N6-acetyllysineBy similarity

Post-translational modificationi

The N-terminus is blocked.
ISGylated.By similarity
Phosphorylated by TXK. Phosphorylation by PASK increases translation efficiency (By similarity).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.

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). 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).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
PTPN11Q061242EBI-7645934,EBI-297779From a different organism.

Protein-protein interaction databases

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

Structurei

3D structure databases

ProteinModelPortaliP68105.
SMRiP68105. Positions 4-455.
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

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

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.

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.

Cross-referencesi

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.

3D structure databases

ProteinModelPortaliP68105.
SMRiP68105. Positions 4-455.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

PTM databases

iPTMnetiP68105.

Proteomic databases

PRIDEiP68105.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi1915.

Phylogenomic databases

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

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 nameiEF1A1_RABIT
AccessioniPrimary (citable) accession number: P68105
Secondary accession number(s): P04719, P04720
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: September 7, 2016
This is version 94 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

Complete proteome, Direct protein sequencing, 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.