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P68104

- EF1A1_HUMAN

UniProt

P68104 - EF1A1_HUMAN

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Protein
Elongation factor 1-alpha 1
Gene
EEF1A1, EEF1A, EF1A, LENG7
Organism
Homo sapiens (Human)
Status
Reviewed - 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.1 Publication

Regions

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

GO - Molecular functioni

  1. GTP binding Source: UniProtKB
  2. GTPase activity Source: InterPro
  3. poly(A) RNA binding Source: UniProtKB
  4. protein binding Source: UniProtKB
  5. protein kinase binding Source: UniProtKB
  6. translation elongation factor activity Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. cellular protein metabolic process Source: Reactome
  2. cellular response to epidermal growth factor stimulus Source: UniProtKB
  3. gene expression Source: Reactome
  4. regulation of transcription, DNA-templated Source: UniProtKB-KW
  5. transcription, DNA-templated Source: UniProtKB-KW
  6. translation Source: Reactome
  7. translational elongation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Elongation factor

Keywords - Biological processi

Protein biosynthesis, Transcription, Transcription regulation

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_1404. Peptide chain elongation.
REACT_1477. Eukaryotic Translation Elongation.
REACT_200744. HSF1 activation.
SignaLinkiP68104.

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
Leukocyte receptor cluster member 7
Gene namesi
Name:EEF1A1
Synonyms:EEF1A, EF1A, LENG7
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:3189. EEF1A1.

Subcellular locationi

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.3 Publications

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: Reactome
  3. eukaryotic translation elongation factor 1 complex Source: UniProtKB
  4. extracellular space Source: UniProt
  5. extracellular vesicular exosome Source: UniProt
  6. nucleolus Source: UniProtKB
  7. nucleus Source: UniProtKB
  8. plasma membrane Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi432 – 4321T → A: Abolishes phosphorylation by PASK. 1 Publication

Organism-specific databases

PharmGKBiPA27625.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 462462Elongation factor 1-alpha 1UniRule annotation
PRO_0000090885Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei36 – 361N6,N6,N6-trimethyllysine By similarity
Modified residuei55 – 551N6,N6-dimethyllysine1 Publication
Modified residuei79 – 791N6,N6,N6-trimethyllysine By similarity
Modified residuei165 – 1651N6,N6-dimethyllysine; alternate1 Publication
Modified residuei165 – 1651N6-acetyllysine; alternate By similarity
Modified residuei172 – 1721N6-acetyllysine By similarity
Modified residuei273 – 2731N6-acetyllysine By similarity
Modified residuei300 – 3001Phosphoserine; by TGFBR11 Publication
Modified residuei301 – 30115-glutamyl glycerylphosphorylethanolamineUniRule annotation
Modified residuei318 – 3181N6,N6,N6-trimethyllysine By similarity
Modified residuei374 – 37415-glutamyl glycerylphosphorylethanolamineUniRule annotation
Modified residuei392 – 3921N6-acetyllysine; alternate By similarity
Modified residuei392 – 3921N6-succinyllysine; alternate By similarity
Modified residuei432 – 4321Phosphothreonine; by PASK1 Publication
Modified residuei439 – 4391N6-acetyllysine By similarity

Post-translational modificationi

ISGylated.1 Publication
Phosphorylated by TXK. Phosphorylation by PASK increases translation efficiency.3 Publications

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP68104.
PaxDbiP68104.
PRIDEiP68104.

2D gel databases

OGPiP68104.
SWISS-2DPAGEP68104.
UCD-2DPAGEP68104.

PTM databases

PhosphoSiteiP68104.

Miscellaneous databases

PMAP-CutDBP68104.

Expressioni

Tissue specificityi

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

Inductioni

By homocysteine (HC), may mediate accelerated synthesis of free thiol-containing proteins in response to HC-induced oxidative stress.1 Publication

Gene expression databases

ArrayExpressiP68104.
BgeeiP68104.
CleanExiHS_EEF1A1.
GenevestigatoriP68104.

Organism-specific databases

HPAiHPA051759.
HPA053862.
HPA056990.

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.7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BBS1Q8NFJ93EBI-352162,EBI-1805484
MDM2Q009879EBI-352162,EBI-389668
RAD23AP547252EBI-352162,EBI-746453
SPHK1Q9NYA12EBI-352162,EBI-985303
YWHAZP631042EBI-352162,EBI-347088
ZBTB16Q055164EBI-352162,EBI-711925
ZDHHC17Q8IUH52EBI-352162,EBI-524753

Protein-protein interaction databases

BioGridi108237. 289 interactions.
IntActiP68104. 166 interactions.
MINTiMINT-1180846.
STRINGi9606.ENSP00000330054.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 148
Helixi20 – 3112
Turni34 – 363
Helixi37 – 4610
Turni47 – 493
Helixi51 – 533
Helixi56 – 605
Helixi61 – 633
Turni64 – 663
Beta strandi76 – 816
Beta strandi86 – 916
Helixi96 – 1016
Helixi103 – 1064
Beta strandi110 – 1167
Helixi124 – 1274
Helixi132 – 1343
Helixi136 – 1438
Beta strandi148 – 1525
Turni160 – 1623
Helixi164 – 1663
Helixi168 – 17811
Turni179 – 1813
Helixi185 – 1873
Beta strandi188 – 1925
Turni195 – 1984
Beta strandi199 – 2035
Beta strandi214 – 2185
Beta strandi221 – 2277
Helixi228 – 2325
Beta strandi243 – 2453
Beta strandi247 – 25610
Turni257 – 2593
Beta strandi260 – 2656
Beta strandi277 – 2837
Beta strandi286 – 2938
Beta strandi300 – 3023
Beta strandi309 – 3146
Turni317 – 3193
Beta strandi325 – 3284
Turni329 – 3313
Beta strandi337 – 34610
Beta strandi352 – 3543
Beta strandi360 – 3634
Beta strandi366 – 38015
Turni381 – 3833
Beta strandi392 – 3954
Beta strandi398 – 40811
Turni415 – 4173
Helixi419 – 4224
Beta strandi423 – 4286
Beta strandi431 – 44212

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SYWmodel-A2-443[»]
ProteinModelPortaliP68104.
SMRiP68104. Positions 2-443.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 242238tr-type G
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni14 – 218G1 By similarity
Regioni70 – 745G2 By similarity
Regioni91 – 944G3 By similarity
Regioni153 – 1564G4 By similarity
Regioni194 – 1963G5 By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG5256.
HOGENOMiHOG000229291.
HOVERGENiHBG000179.
InParanoidiP68104.
KOiK03231.
OMAiADKPHMN.
OrthoDBiEOG7NKKK3.
PhylomeDBiP68104.
TreeFamiTF300304.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00118_A. EF_Tu_A.
InterProiIPR000795. 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]
PfamiPF00009. GTP_EFTU. 1 hit.
PF03144. 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.

P68104-1 [UniParc]FASTAAdd to Basket

« Hide

MGKEKTHINI VVIGHVDSGK STTTGHLIYK CGGIDKRTIE KFEKEAAEMG    50
KGSFKYAWVL DKLKAERERG ITIDISLWKF ETSKYYVTII DAPGHRDFIK 100
NMITGTSQAD CAVLIVAAGV GEFEAGISKN GQTREHALLA YTLGVKQLIV 150
GVNKMDSTEP PYSQKRYEEI VKEVSTYIKK IGYNPDTVAF VPISGWNGDN 200
MLEPSANMPW FKGWKVTRKD GNASGTTLLE ALDCILPPTR PTDKPLRLPL 250
QDVYKIGGIG TVPVGRVETG VLKPGMVVTF APVNVTTEVK SVEMHHEALS 300
EALPGDNVGF NVKNVSVKDV RRGNVAGDSK NDPPMEAAGF TAQVIILNHP 350
GQISAGYAPV LDCHTAHIAC KFAELKEKID RRSGKKLEDG PKFLKSGDAA 400
IVDMVPGKPM CVESFSDYPP LGRFAVRDMR QTVAVGVIKA VDKKAAGAGK 450
VTKSAQKAQK AK 462
Length:462
Mass (Da):50,141
Last modified:August 13, 1987 - v1
Checksum:iD465615545AF686A
GO

Sequence cautioni

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti83 – 831S → A in CAA27325. 1 Publication
Sequence conflicti232 – 2321L → V in CAA34756. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS4980.1.
PIRiB24977. EFHU1.
RefSeqiNP_001393.1. NM_001402.5.
UniGeneiHs.535192.
Hs.586423.
Hs.745122.

Genome annotation databases

EnsembliENST00000309268; ENSP00000339053; ENSG00000156508.
ENST00000316292; ENSP00000339063; ENSG00000156508.
ENST00000331523; ENSP00000330054; ENSG00000156508.
GeneIDi1915.
KEGGihsa:1915.
UCSCiuc003phi.3. human.

Polymorphism databases

DMDMi55584035.

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSi CCDS4980.1.
PIRi B24977. EFHU1.
RefSeqi NP_001393.1. NM_001402.5.
UniGenei Hs.535192.
Hs.586423.
Hs.745122.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1SYW model - A 2-443 [» ]
ProteinModelPortali P68104.
SMRi P68104. Positions 2-443.
ModBasei Search...

Protein-protein interaction databases

BioGridi 108237. 289 interactions.
IntActi P68104. 166 interactions.
MINTi MINT-1180846.
STRINGi 9606.ENSP00000330054.

Chemistry

BindingDBi P68104.
ChEMBLi CHEMBL1795120.

PTM databases

PhosphoSitei P68104.

Polymorphism databases

DMDMi 55584035.

2D gel databases

OGPi P68104.
SWISS-2DPAGE P68104.
UCD-2DPAGE P68104.

Proteomic databases

MaxQBi P68104.
PaxDbi P68104.
PRIDEi P68104.

Protocols and materials databases

DNASUi 1915.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000309268 ; ENSP00000339053 ; ENSG00000156508 .
ENST00000316292 ; ENSP00000339063 ; ENSG00000156508 .
ENST00000331523 ; ENSP00000330054 ; ENSG00000156508 .
GeneIDi 1915.
KEGGi hsa:1915.
UCSCi uc003phi.3. human.

Organism-specific databases

CTDi 1915.
GeneCardsi GC06M074225.
H-InvDB HIX0020005.
HIX0032108.
HIX0033669.
HIX0169110.
HGNCi HGNC:3189. EEF1A1.
HPAi HPA051759.
HPA053862.
HPA056990.
MIMi 130590. gene.
neXtProti NX_P68104.
PharmGKBi PA27625.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5256.
HOGENOMi HOG000229291.
HOVERGENi HBG000179.
InParanoidi P68104.
KOi K03231.
OMAi ADKPHMN.
OrthoDBi EOG7NKKK3.
PhylomeDBi P68104.
TreeFami TF300304.

Enzyme and pathway databases

Reactomei REACT_1404. Peptide chain elongation.
REACT_1477. Eukaryotic Translation Elongation.
REACT_200744. HSF1 activation.
SignaLinki P68104.

Miscellaneous databases

ChiTaRSi EEF1A1. human.
GeneWikii Eukaryotic_translation_elongation_factor_1_alpha_1.
GenomeRNAii 1915.
NextBioi 7799.
PMAP-CutDB P68104.
PROi P68104.
SOURCEi Search...

Gene expression databases

ArrayExpressi P68104.
Bgeei P68104.
CleanExi HS_EEF1A1.
Genevestigatori P68104.

Family and domain databases

Gene3Di 3.40.50.300. 1 hit.
HAMAPi MF_00118_A. EF_Tu_A.
InterProi IPR000795. 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 ]
Pfami PF00009. GTP_EFTU. 1 hit.
PF03144. GTP_EFTU_D2. 1 hit.
PF03143. GTP_EFTU_D3. 1 hit.
[Graphical view ]
PRINTSi PR00315. ELONGATNFCT.
SUPFAMi SSF50447. SSF50447. 1 hit.
SSF50465. SSF50465. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsi TIGR00483. EF-1_alpha. 1 hit.
PROSITEi PS00301. G_TR_1. 1 hit.
PS51722. G_TR_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiEF1A1_HUMAN
AccessioniPrimary (citable) accession number: P68104
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 3, 2014
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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