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P68103 (EF1A1_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended 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 names
Name:EEF1A1
Synonyms:EEF1A, EF1A
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length462 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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.

Subunit structure

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 By similarity.

Subcellular location

Cytoplasm By similarity. Nucleus By similarity. Note: Colocalizes with DLC1 at actin-rich regions in the cell periphery By similarity.

Post-translational modification

ISGylated By similarity.

Phosphorylated by TXK. Phosphorylation by PASK increases translation efficiency By similarity.

Sequence similarities

Belongs to the GTP-binding elongation factor family. EF-Tu/EF-1A subfamily.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
Nucleus
   LigandGTP-binding
Nucleotide-binding
   Molecular functionElongation factor
   PTMMethylation
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processGTP catabolic process

Inferred from electronic annotation. Source: GOC

   Cellular_componentcytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionGTP binding

Inferred from electronic annotation. Source: UniProtKB-KW

GTPase activity

Inferred from electronic annotation. Source: InterPro

translation elongation factor activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 462462Elongation factor 1-alpha 1
PRO_0000090882

Regions

Nucleotide binding14 – 218GTP By similarity
Nucleotide binding91 – 955GTP By similarity
Nucleotide binding153 – 1564GTP By similarity

Amino acid modifications

Modified residue361N6,N6,N6-trimethyllysine By similarity
Modified residue551N6,N6-dimethyllysine By similarity
Modified residue791N6,N6,N6-trimethyllysine By similarity
Modified residue1651N6,N6-dimethyllysine By similarity
Modified residue3001Phosphoserine; by TGFBR1 By similarity
Modified residue30115-glutamyl glycerylphosphorylethanolamine By similarity
Modified residue3181N6,N6,N6-trimethyllysine By similarity
Modified residue37415-glutamyl glycerylphosphorylethanolamine By similarity
Modified residue4321Phosphothreonine; by PASK By similarity

Experimental info

Sequence conflict2321L → M in AAI05316. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P68103 [UniParc].

Last modified August 13, 1987. Version 1.
Checksum: D465615545AF686A

FASTA46250,141
        10         20         30         40         50         60 
MGKEKTHINI VVIGHVDSGK STTTGHLIYK CGGIDKRTIE KFEKEAAEMG KGSFKYAWVL 

        70         80         90        100        110        120 
DKLKAERERG ITIDISLWKF ETSKYYVTII DAPGHRDFIK NMITGTSQAD CAVLIVAAGV 

       130        140        150        160        170        180 
GEFEAGISKN GQTREHALLA YTLGVKQLIV GVNKMDSTEP PYSQKRYEEI VKEVSTYIKK 

       190        200        210        220        230        240 
IGYNPDTVAF VPISGWNGDN MLEPSANMPW FKGWKVTRKD GNASGTTLLE ALDCILPPTR 

       250        260        270        280        290        300 
PTDKPLRLPL QDVYKIGGIG TVPVGRVETG VLKPGMVVTF APVNVTTEVK SVEMHHEALS 

       310        320        330        340        350        360 
EALPGDNVGF NVKNVSVKDV RRGNVAGDSK NDPPMEAAGF TAQVIILNHP GQISAGYAPV 

       370        380        390        400        410        420 
LDCHTAHIAC KFAELKEKID RRSGKKLEDG PKFLKSGDAA IVDMVPGKPM CVESFSDYPP 

       430        440        450        460 
LGRFAVRDMR QTVAVGVIKA VDKKAAGAGK VTKSAQKAQK AK

« Hide

References

« Hide 'large scale' references
[1]"BVDV NS5A interacts with eEF1a."
Perez D.R., Johnson C.M., Donis R.O.
Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"cDNA of bovine elongation factor 1 alpha from endometrium."
Kojima T., Oshima K., Watanabe H., Komatsu M.
Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Japanese black.
Tissue: Endometrium.
[3]NIH - Mammalian Gene Collection (MGC) project
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Crossbred X Angus and Hereford.
Tissue: Ileum and Thymus.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AJ238405 mRNA. Translation: CAB88863.1.
AB060107 mRNA. Translation: BAB60846.1.
BC105315 mRNA. Translation: AAI05316.1.
BC142302 mRNA. Translation: AAI42303.1.
IPIIPI00712775.
RefSeqNP_776960.1. NM_174535.1.
UniGeneBt.63960.
Bt.64525.
Bt.95243.

3D structure databases

ProteinModelPortalP68103.
ModBaseSearch...

Protein-protein interaction databases

IntActP68103. 1 interaction.

Proteomic databases

PaxDbP68103.
PRIDEP68103.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000019318; ENSBTAP00000019318; ENSBTAG00000014534.
GeneID282220.
KEGGbta:282220.

Organism-specific databases

CTD1915.

Phylogenomic databases

eggNOGCOG5256.
GeneTreeENSGT00670000097815.
HOGENOMHOG000229291.
HOVERGENHBG000179.
InParanoidP68103.
KOK03231.
OMAIEMHHES.
OrthoDBEOG40K7ZP.

Family and domain databases

InterProIPR000795. EF_GTP-bd_dom.
IPR009001. Transl_elong_EF1A/Init_IF2_C.
IPR004539. Transl_elong_EF1A_euk/arc.
IPR004161. Transl_elong_EFTu/EF1A_2.
IPR004160. Transl_elong_EFTu/EF1A_C.
IPR009000. Transl_elong_init/rib_B-barrel.
[Graphical view]
PfamPF00009. GTP_EFTU. 1 hit.
PF03144. GTP_EFTU_D2. 1 hit.
PF03143. GTP_EFTU_D3. 1 hit.
[Graphical view]
PRINTSPR00315. ELONGATNFCT.
SUPFAMSSF50465. Elong_init_C. 1 hit.
SSF50447. Translat_factor. 1 hit.
TIGRFAMsTIGR00483. EF-1_alpha. 1 hit.
PROSITEPS00301. EFACTOR_GTP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

BindingDBP68103.
NextBio20806043.

Entry information

Entry nameEF1A1_BOVIN
AccessionPrimary (citable) accession number: P68103
Secondary accession number(s): A5PK01 expand/collapse secondary AC list , P04719, P04720, Q2KJJ3
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: May 1, 2013
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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