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P68104

- EF1A1_HUMAN

UniProt

P68104 - EF1A1_HUMAN

Protein

Elongation factor 1-alpha 1

Gene

EEF1A1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 1 (13 Aug 1987)
      Previous versions | rss
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    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 – 218GTPBy similarity
    Nucleotide bindingi91 – 955GTPBy similarity
    Nucleotide bindingi153 – 1564GTPBy similarity

    GO - Molecular functioni

    1. GTPase activity Source: InterPro
    2. GTP binding Source: UniProtKB
    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

    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

    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.

    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. membrane Source: UniProtKB
    7. nucleolus Source: UniProtKB
    8. nucleus Source: UniProtKB
    9. plasma membrane Source: Ensembl

    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 1PRO_0000090885Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei36 – 361N6,N6,N6-trimethyllysineBy similarity
    Modified residuei55 – 551N6,N6-dimethyllysine1 Publication
    Modified residuei79 – 791N6,N6,N6-trimethyllysineBy similarity
    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 TGFBR12 Publications
    Modified residuei301 – 30115-glutamyl glycerylphosphorylethanolamine1 Publication
    Modified residuei318 – 3181N6,N6,N6-trimethyllysineBy similarity
    Modified residuei374 – 37415-glutamyl glycerylphosphorylethanolamine1 Publication
    Modified residuei392 – 3921N6-acetyllysine; alternateBy similarity
    Modified residuei392 – 3921N6-succinyllysine; alternateBy similarity
    Modified residuei432 – 4321Phosphothreonine; by PASK2 Publications
    Modified residuei439 – 4391N6-acetyllysineBy 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.By similarity7 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

    1
    462
    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.
    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

    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.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti83 – 831S → A in CAA27325. (PubMed:3960725)Curated
    Sequence conflicti232 – 2321L → V in CAA34756. (PubMed:2183196)Curated

    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...
    MobiDBi 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

    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: October 1, 2014
    This is version 131 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