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UniProtKB - P10126 (EF1A1_MOUSE)

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Protein

Elongation factor 1-alpha 1

Gene

Eef1a1

Organism
Mus musculus (Mouse)
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

Complete GO annotation...

GO - Biological processi

Complete GO annotation...

Keywordsi

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

Enzyme and pathway databases

ReactomeiR-MMU-156842. Eukaryotic Translation Elongation.
R-MMU-3371511. HSF1 activation.
R-MMU-6798695. Neutrophil degranulation.
R-MMU-8876725. Protein methylation.

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:1096881. Eef1a1.

Subcellular locationi

  • Cytoplasm 1 Publication
  • Nucleus By similarity
  • Nucleus › nucleolus By similarity
  • Cell membrane 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. Localization at the cell membrane depends on EEF1A1 phosphorylation status and the presence of PPP1R16B.By similarity

GO - Cellular componenti

  • cortical actin cytoskeleton Source: MGI
  • cytoplasm Source: UniProtKB
  • cytosol Source: MGI
  • extracellular exosome Source: MGI
  • extracellular space Source: MGI
  • membrane Source: MGI
  • myelin sheath Source: UniProtKB
  • nucleolus Source: UniProtKB
  • nucleus Source: UniProtKB
  • plasma membrane Source: MGI
  • ruffle membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000908862 – 462Elongation factor 1-alpha 1Add BLAST461

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N,N,N-trimethylglycineBy similarity1
Modified residuei36N6,N6,N6-trimethyllysineBy similarity1
Modified residuei55N6,N6-dimethyllysineBy similarity1
Modified residuei79N6,N6,N6-trimethyllysine; by EEF1AKMT1By similarity1
Modified residuei165N6,N6,N6-trimethyllysine; alternate; by EEF1AKMT31 Publication1
Modified residuei165N6,N6-dimethyllysine; alternate; by EEF1AKMT3By similarity1
Modified residuei165N6-acetyllysine; alternateCombined sources1
Modified residuei165N6-methyllysine; alternate; by EEF1AKMT3By similarity1
Modified residuei172N6-acetyllysineCombined sources1
Modified residuei273N6-acetyllysineCombined sources1
Modified residuei300Phosphoserine; by TGFBR1By similarity1
Modified residuei3015-glutamyl glycerylphosphorylethanolamine1 Publication1
Modified residuei318N6,N6,N6-trimethyllysine; by EEF1AKMT2By similarity1
Modified residuei3745-glutamyl glycerylphosphorylethanolamine1 Publication1
Modified residuei392N6-acetyllysine; alternateCombined sources1
Modified residuei392N6-succinyllysine; alternateCombined sources1
Modified residuei432Phosphothreonine; by PASKBy similarity1
Modified residuei439N6-acetyllysineCombined sources1

Post-translational modificationi

ISGylated.1 Publication
Phosphorylated by TXK. Phosphorylation by PASK increases translation efficiency. Phosphorylated by ROCK2.By similarity
Trimethylated at Lys-79 by EEF1AKMT1 (By similarity). 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 (PubMed:28108655). Trimethylated at Lys-318 by EEF1AKMT2 (By similarity).By similarity1 Publication

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP10126.
PaxDbiP10126.
PeptideAtlasiP10126.
PRIDEiP10126.
TopDownProteomicsiP10126.

2D gel databases

SWISS-2DPAGEiP10126.

PTM databases

iPTMnetiP10126.
PhosphoSitePlusiP10126.
SwissPalmiP10126.

Expressioni

Gene expression databases

BgeeiENSMUSG00000037742.
ExpressionAtlasiP10126. baseline and differential.
GenevisibleiP10126. MM.

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 (By similarity). Interacts with IFIT1 (via TPR repeats 4-7) (PubMed:19856081). 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 similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
TSPY1Q015345EBI-773865,EBI-1973142From Homo sapiens.

GO - Molecular functioni

Complete GO annotation...

Protein-protein interaction databases

BioGridi199385. 50 interactors.
DIPiDIP-46609N.
IntActiP10126. 62 interactors.
MINTiMINT-1862449.
STRINGi10090.ENSMUSP00000042457.

Structurei

3D structure databases

ProteinModelPortaliP10126.
SMRiP10126.
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

Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A subfamily.Curated

Phylogenomic databases

eggNOGiKOG0052. Eukaryota.
COG5256. LUCA.
GeneTreeiENSGT00670000097815.
HOGENOMiHOG000229291.
HOVERGENiHBG000179.
InParanoidiP10126.
KOiK03231.
OMAiPAKETKM.
OrthoDBiEOG091G05LW.
PhylomeDBiP10126.
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.
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.

P10126-1 [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 GSASGTTLLE 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):50,114
Last modified:October 25, 2004 - v3
Checksum:i71072871DE7405DC
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti7H → R in AAA37538 (PubMed:3481036).Curated1
Sequence conflicti15H → L in AAA37538 (PubMed:3481036).Curated1
Sequence conflicti23T → S in AAA37538 (PubMed:3481036).Curated1
Sequence conflicti77 – 78LW → QR in CAA31957 (PubMed:2911475).Curated2
Sequence conflicti83S → A in CAA27324 (PubMed:3960725).Curated1
Sequence conflicti91 – 92DA → ES in CAA31957 (PubMed:2911475).Curated2
Sequence conflicti108Q → R in AAA37538 (PubMed:3481036).Curated1
Sequence conflicti156D → G in BAC28085 (PubMed:16141072).Curated1
Sequence conflicti222S → H in AAA50406 (PubMed:3215517).Curated1
Sequence conflicti224 – 226SGT → VAP in CAA31957 (PubMed:2911475).Curated3
Sequence conflicti225G → D in AAH04005 (PubMed:15489334).Curated1
Sequence conflicti239Missing in CAA31957 (PubMed:2911475).Curated1
Sequence conflicti350P → T in BAC36446 (PubMed:16141072).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M22432 mRNA. Translation: AAA50406.1.
X13661 mRNA. Translation: CAA31957.1.
AK032914 mRNA. Translation: BAC28085.1.
AK076696 mRNA. Translation: BAC36446.1.
AK081725 mRNA. Translation: BAC38311.1.
AK083361 mRNA. Translation: BAC38884.1.
BC004005 mRNA. Translation: AAH04005.1.
BC004067 mRNA. Translation: AAH04067.1.
BC005660 mRNA. Translation: AAH05660.1.
BC018223 mRNA. Translation: AAH18223.1.
BC018485 mRNA. Translation: AAH18485.1.
BC083069 mRNA. Translation: AAH83069.1.
M17878 Genomic DNA. Translation: AAA37538.1.
X03688 mRNA. Translation: CAA27324.1.
CCDSiCCDS40703.1.
PIRiS02114. EFMS1.
RefSeqiNP_034236.2. NM_010106.2.
UniGeneiMm.138471.
Mm.335315.
Mm.360075.
Mm.391071.
Mm.485669.
Mm.491424.

Genome annotation databases

EnsembliENSMUST00000042235; ENSMUSP00000042457; ENSMUSG00000037742.
GeneIDi13627.
KEGGimmu:13627.
UCSCiuc009qun.1. mouse.

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.

Entry informationi

Entry nameiEF1A1_MOUSE
AccessioniPrimary (citable) accession number: P10126
Secondary accession number(s): Q61511
, Q6ZWN2, Q8BMB8, Q8BVS8, Q99KU5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: October 25, 2004
Last modified: July 5, 2017
This is version 188 of the entry and version 3 of the sequence. See 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families