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P68104 (EF1A1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

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
Leukocyte receptor cluster member 7
Gene names
Name:EEF1A1
Synonyms:EEF1A, EF1A, LENG7
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length462 AA.
Sequence statusComplete.
Protein existenceEvidence at protein 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. Ref.8

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) 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. Ref.8 Ref.12 Ref.14 Ref.15 Ref.18 Ref.19 Ref.20

Subcellular location

Cytoplasm. Nucleus. Nucleusnucleolus. 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. Ref.8 Ref.12 Ref.20

Tissue specificity

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

Induction

By homocysteine (HC), may mediate accelerated synthesis of free thiol-containing proteins in response to HC-induced oxidative stress. Ref.13

Post-translational modification

ISGylated. Ref.16

Phosphorylated by TXK. Phosphorylation by PASK increases translation efficiency. Ref.8 Ref.17 Ref.21

Sequence similarities

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

Sequence caution

The sequence AAA52367.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processProtein biosynthesis
Transcription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   LigandGTP-binding
Nucleotide-binding
   Molecular functionElongation factor
   PTMAcetylation
Methylation
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcellular protein metabolic process

Traceable author statement. Source: Reactome

cellular response to epidermal growth factor stimulus

Inferred from direct assay PubMed 9852145. Source: UniProtKB

gene expression

Traceable author statement. Source: Reactome

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

translation

Traceable author statement. Source: Reactome

translational elongation

Traceable author statement PubMed 8812466. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 9852145. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

eukaryotic translation elongation factor 1 complex

Traceable author statement Ref.2. Source: UniProtKB

extracellular space

Inferred from direct assay PubMed 23580065. Source: UniProt

extracellular vesicular exosome

Inferred from direct assay PubMed 12519789PubMed 19056867PubMed 19199708PubMed 20458337PubMed 23376485. Source: UniProt

nucleolus

Inferred from direct assay PubMed 9852145. Source: UniProtKB

nucleus

Inferred from direct assay PubMed 9852145. Source: UniProtKB

plasma membrane

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionGTP binding

Traceable author statement Ref.1. Source: UniProtKB

GTPase activity

Inferred from electronic annotation. Source: InterPro

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 9852145. Source: UniProtKB

protein kinase binding

Inferred from physical interaction Ref.17. Source: UniProtKB

translation elongation factor activity

Traceable author statement Ref.17. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 462462Elongation factor 1-alpha 1 HAMAP-Rule MF_00118_A
PRO_0000090885

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 Ref.7
Modified residue791N6,N6,N6-trimethyllysine By similarity
Modified residue1651N6,N6-dimethyllysine; alternate Ref.7
Modified residue1651N6-acetyllysine; alternate By similarity
Modified residue1721N6-acetyllysine By similarity
Modified residue2731N6-acetyllysine By similarity
Modified residue3001Phosphoserine; by TGFBR1 Ref.21
Modified residue30115-glutamyl glycerylphosphorylethanolamine HAMAP-Rule MF_00118_A
Modified residue3181N6,N6,N6-trimethyllysine By similarity
Modified residue37415-glutamyl glycerylphosphorylethanolamine HAMAP-Rule MF_00118_A
Modified residue3921N6-acetyllysine; alternate By similarity
Modified residue3921N6-succinyllysine; alternate By similarity
Modified residue4321Phosphothreonine; by PASK Ref.17
Modified residue4391N6-acetyllysine By similarity

Experimental info

Mutagenesis4321T → A: Abolishes phosphorylation by PASK. Ref.17
Sequence conflict831S → A in CAA27325. Ref.6
Sequence conflict2321L → V in CAA34756. Ref.3

Secondary structure

.......................................................................................... 462
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P68104 [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]"The primary structure of the alpha subunit of human elongation factor 1. Structural aspects of guanine-nucleotide-binding sites."
Brands J.H.G.M., Maassen J.A., van Hemert F.J., Amons R., Moeller W.
Eur. J. Biochem. 155:167-171(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Isolation and characterization of the human chromosomal gene for polypeptide chain elongation factor-1 alpha."
Uetsuki T., Naito A., Nagata S., Kaziro Y.
J. Biol. Chem. 264:5791-5798(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Retropseudogenes constitute the major part of the human elongation factor 1 alpha gene family."
Madsen H.O., Poulsen K., Dahl O., Clark B.F.C., Hjorth J.P.
Nucleic Acids Res. 18:1513-1516(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[4]"Postnatal expression of a novel mRNA isoform from the human elongation factor-1a gene."
Shimazu T., Koike K.
Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: B-cell, Bone marrow, Cervix, Colon, Hippocampus, Lung, Lymph, Mammary gland, Ovary, Pancreas, Placenta, Testis and Uterus.
[6]"Structure of the amino-terminal end of mammalian elongation factor Tu."
Rao T.R., Slobin L.I.
Nucleic Acids Res. 14:2409-2409(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-94.
[7]Bienvenut W.V., Zebisch A., Kolch W.
Submitted (JAN-2010) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 6-30; 52-62; 85-96; 101-129; 135-180; 248-313; 396-423 AND 431-439, METHYLATION AT LYS-55 AND LYS-165, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Colon carcinoma and Ovarian carcinoma.
[8]"Txk, a member of the non-receptor tyrosine kinase of the Tec family, forms a complex with poly(ADP-ribose) polymerase 1 and elongation factor 1alpha and regulates interferon-gamma gene transcription in Th1 cells."
Maruyama T., Nara K., Yoshikawa H., Suzuki N.
Clin. Exp. Immunol. 147:164-175(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 7-16 AND 85-96, INTERACTION WITH PARP1 AND TXK, PHOSPHORYLATION BY TXK, SUBCELLULAR LOCATION, FUNCTION AS A TRANSCRIPTION FACTOR.
[9]Bienvenut W.V.
Submitted (JUN-2005) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 38-44; 70-79; 85-96; 135-172; 248-290; 386-392 AND 428-439.
Tissue: B-cell lymphoma.
[10]"Retinol-regulated gene expression in human tracheobronchial epithelial cells. Enhanced expression of elongation factor EF-1 alpha."
Ann D.K., Wu M.M.J., Huang T., Carlson D.M., Wu R.
J. Biol. Chem. 263:3546-3549(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 138-462.
[11]"Murine elongation factor 1 alpha (EF-1 alpha) is posttranslationally modified by novel amide-linked ethanolamine-phosphoglycerol moieties. Addition of ethanolamine-phosphoglycerol to specific glutamic acid residues on EF-1 alpha."
Whiteheart S.W., Shenbagarmurthi P., Chen L., Cotter R.J., Hart G.W.
J. Biol. Chem. 264:14334-14341(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: ETHANOLAMINYLATION AT GLU-301 AND GLU-374.
[12]"Binding of zinc finger protein ZPR1 to the epidermal growth factor receptor."
Galcheva-Gargova Z., Konstantinov K.N., Wu I.-H., Klier F.G., Barrett T., Davis R.J.
Science 272:1797-1802(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ZPR1, SUBCELLULAR LOCATION.
[13]"Induction of acute translational response genes by homocysteine. Elongation factors-1alpha, -beta, and -delta."
Chacko G., Ling Q., Hajjar K.A.
J. Biol. Chem. 273:19840-19846(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION BY HOMOCYSTEINE.
[14]"Exp5 exports eEF1A via tRNA from nuclei and synergizes with other transport pathways to confine translation to the cytoplasm."
Bohnsack M.T., Regener K., Schwappach B., Saffrich R., Paraskeva E., Hartmann E., Goerlich D.
EMBO J. 21:6205-6215(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A NUCLEAR EXPORT RECEPTOR COMPLEX WITH XPO5; RAN AND TRNA, INTERACTION WITH XPO5.
[15]"Exportin-5-mediated nuclear export of eukaryotic elongation factor 1A and tRNA."
Calado A., Treichel N., Mueller E.-C., Otto A., Kutay U.
EMBO J. 21:6216-6224(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A NUCLEAR EXPORT RECEPTOR COMPLEX WITH XPO5; RAN AND TRNA, INTERACTION WITH XPO5.
[16]"Proteomic identification of proteins conjugated to ISG15 in mouse and human cells."
Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J., Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E.
Biochem. Biophys. Res. Commun. 336:496-506(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: ISGYLATION.
[17]"Male germ cell expression of the PAS domain kinase PASKIN and its novel target eukaryotic translation elongation factor eEF1A1."
Eckhardt K., Troger J., Reissmann J., Katschinski D.M., Wagner K.F., Stengel P., Paasch U., Hunziker P., Borter E., Barth S., Schlafli P., Spielmann P., Stiehl D.P., Camenisch G., Wenger R.H.
Cell. Physiol. Biochem. 20:227-240(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-432, MUTAGENESIS OF THR-432.
[18]"Lysyl-tRNA synthetase interacts with EF1alpha, aspartyl-tRNA synthetase and p38 in vitro."
Guzzo C.M., Yang D.C.H.
Biochem. Biophys. Res. Commun. 365:718-723(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KARS.
[19]"The possible interaction of CDA14 and protein elongation factor 1alpha."
Yang Y.F., Chou M.Y., Fan C.Y., Chen S.F., Lyu P.C., Liu C.C., Tseng T.L.
Biochim. Biophys. Acta 1784:312-318(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ERGIC2.
[20]"The SAM domain of the RhoGAP DLC1 binds EF1A1 to regulate cell migration."
Zhong D., Zhang J., Yang S., Soh U.J., Buschdorf J.P., Zhou Y.T., Yang D., Low B.C.
J. Cell Sci. 122:414-424(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DLC1, SUBCELLULAR LOCATION.
[21]"Phosphorylation of eEF1A1 at Ser300 by TbetaR-I results in inhibition of mRNA translation."
Lin K.W., Yakymovych I., Jia M., Yakymovych M., Souchelnytskyi S.
Curr. Biol. 20:1615-1625(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-300.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X03558 mRNA. Translation: CAA27245.1.
J04617 Genomic DNA. Translation: AAA52343.1.
X16869 mRNA. Translation: CAA34756.1.
AY043301 mRNA. Translation: AAK95378.1.
BC008587 mRNA. Translation: AAH08587.1.
BC009733 mRNA. Translation: AAH09733.1.
BC009875 mRNA. Translation: AAH09875.1.
BC010735 mRNA. Translation: AAH10735.1.
BC012891 mRNA. Translation: AAH12891.1.
BC014224 mRNA. Translation: AAH14224.1.
BC018150 mRNA. Translation: AAH18150.1.
BC018641 mRNA. Translation: AAH18641.1.
BC021686 mRNA. Translation: AAH21686.1.
BC028674 mRNA. Translation: AAH28674.1.
BC038339 mRNA. Translation: AAH38339.1.
BC057391 mRNA. Translation: AAH57391.1.
BC066893 mRNA. Translation: AAH66893.1.
BC072385 mRNA. Translation: AAH72385.1.
BC082268 mRNA. Translation: AAH82268.1.
X03689 mRNA. Translation: CAA27325.1.
M29548 mRNA. Translation: AAA52367.1. Different initiation.
CCDSCCDS4980.1.
PIREFHU1. B24977.
RefSeqNP_001393.1. NM_001402.5.
UniGeneHs.535192.
Hs.586423.
Hs.745122.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1SYWmodel-A2-443[»]
ProteinModelPortalP68104.
SMRP68104. Positions 2-443.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108237. 288 interactions.
IntActP68104. 165 interactions.
MINTMINT-1180846.
STRING9606.ENSP00000330054.

Chemistry

BindingDBP68104.
ChEMBLCHEMBL1795120.

PTM databases

PhosphoSiteP68104.

Polymorphism databases

DMDM55584035.

2D gel databases

OGPP68104.
SWISS-2DPAGEP68104.
UCD-2DPAGEP68104.

Proteomic databases

MaxQBP68104.
PaxDbP68104.
PRIDEP68104.

Protocols and materials databases

DNASU1915.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000309268; ENSP00000339053; ENSG00000156508.
ENST00000316292; ENSP00000339063; ENSG00000156508.
ENST00000331523; ENSP00000330054; ENSG00000156508.
GeneID1915.
KEGGhsa:1915.
UCSCuc003phi.3. human.

Organism-specific databases

CTD1915.
GeneCardsGC06M074225.
H-InvDBHIX0020005.
HIX0032108.
HIX0033669.
HIX0169110.
HGNCHGNC:3189. EEF1A1.
HPAHPA051759.
HPA053862.
HPA056990.
MIM130590. gene.
neXtProtNX_P68104.
PharmGKBPA27625.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5256.
HOGENOMHOG000229291.
HOVERGENHBG000179.
InParanoidP68104.
KOK03231.
OMAADKPHMN.
OrthoDBEOG7NKKK3.
PhylomeDBP68104.
TreeFamTF300304.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.
REACT_71. Gene Expression.
SignaLinkP68104.

Gene expression databases

ArrayExpressP68104.
BgeeP68104.
CleanExHS_EEF1A1.
GenevestigatorP68104.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
HAMAPMF_00118_A. EF_Tu_A.
InterProIPR000795. EF_GTP-bd_dom.
IPR027417. P-loop_NTPase.
IPR009000. Transl_B-barrel.
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.
[Graphical view]
PfamPF00009. GTP_EFTU. 1 hit.
PF03144. GTP_EFTU_D2. 1 hit.
PF03143. GTP_EFTU_D3. 1 hit.
[Graphical view]
PRINTSPR00315. ELONGATNFCT.
SUPFAMSSF50447. SSF50447. 1 hit.
SSF50465. SSF50465. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00483. EF-1_alpha. 1 hit.
PROSITEPS00301. EFACTOR_GTP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSEEF1A1. human.
GeneWikiEukaryotic_translation_elongation_factor_1_alpha_1.
GenomeRNAi1915.
NextBio7799.
PMAP-CutDBP68104.
PROP68104.
SOURCESearch...

Entry information

Entry nameEF1A1_HUMAN
AccessionPrimary (citable) accession number: P68104
Secondary accession number(s): P04719, P04720
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: July 9, 2014
This is version 129 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM