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Q05639

- EF1A2_HUMAN

UniProt

Q05639 - EF1A2_HUMAN

Protein

Elongation factor 1-alpha 2

Gene

EEF1A2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 156 (01 Oct 2014)
      Sequence version 1 (01 Jun 1994)
      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.

    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-KW
    3. translation elongation factor activity Source: UniProtKB-KW
    4. translation factor activity, nucleic acid binding Source: ProtInc

    GO - Biological processi

    1. positive regulation of execution phase of apoptosis Source: Ensembl
    2. response to inorganic substance Source: Ensembl

    Keywords - Molecular functioni

    Elongation factor

    Keywords - Biological processi

    Protein biosynthesis

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_1477. Eukaryotic Translation Elongation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Elongation factor 1-alpha 2
    Short name:
    EF-1-alpha-2
    Alternative name(s):
    Eukaryotic elongation factor 1 A-2
    Short name:
    eEF1A-2
    Statin-S1
    Gene namesi
    Name:EEF1A2
    Synonyms:EEF1AL, STN
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:3192. EEF1A2.

    Subcellular locationi

    Nucleus By similarity

    GO - Cellular componenti

    1. eukaryotic translation elongation factor 1 complex Source: Ensembl
    2. neuronal cell body Source: Ensembl
    3. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA36219.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 463463Elongation factor 1-alpha 2PRO_0000090891Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei55 – 551N6,N6,N6-trimethyllysineBy similarity
    Modified residuei165 – 1651N6,N6,N6-trimethyllysineBy similarity
    Modified residuei179 – 1791N6-acetyllysine1 Publication
    Modified residuei301 – 30115-glutamyl glycerylphosphorylethanolamineBy similarity
    Modified residuei374 – 37415-glutamyl glycerylphosphorylethanolamineBy similarity
    Modified residuei439 – 4391N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation, Methylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ05639.
    PaxDbiQ05639.
    PeptideAtlasiQ05639.
    PRIDEiQ05639.

    PTM databases

    PhosphoSiteiQ05639.

    Expressioni

    Tissue specificityi

    Brain, heart, and skeletal muscle.

    Gene expression databases

    BgeeiQ05639.
    CleanExiHS_EEF1A2.
    GenevestigatoriQ05639.

    Organism-specific databases

    HPAiCAB034019.

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Protein-protein interaction databases

    BioGridi108238. 43 interactions.
    IntActiQ05639. 24 interactions.
    MINTiMINT-1141378.
    STRINGi9606.ENSP00000217182.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3C5JX-ray1.80C343-355[»]
    ProteinModelPortaliQ05639.
    SMRiQ05639. Positions 2-443.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ05639.

    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.
    InParanoidiQ05639.
    KOiK03231.
    OMAiVACTFES.
    OrthoDBiEOG7NKKK3.
    PhylomeDBiQ05639.
    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.

    Q05639-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGKEKTHINI VVIGHVDSGK STTTGHLIYK CGGIDKRTIE KFEKEAAEMG    50
    KGSFKYAWVL DKLKAERERG ITIDISLWKF ETTKYYITII DAPGHRDFIK 100
    NMITGTSQAD CAVLIVAAGV GEFEAGISKN GQTREHALLA YTLGVKQLIV 150
    GVNKMDSTEP AYSEKRYDEI VKEVSAYIKK IGYNPATVPF VPISGWHGDN 200
    MLEPSPNMPW FKGWKVERKE GNASGVSLLE ALDTILPPTR PTDKPLRLPL 250
    QDVYKIGGIG TVPVGRVETG ILRPGMVVTF APVNITTEVK SVEMHHEALS 300
    EALPGDNVGF NVKNVSVKDI RRGNVCGDSK SDPPQEAAQF TSQVIILNHP 350
    GQISAGYSPV IDCHTAHIAC KFAELKEKID RRSGKKLEDN PKSLKSGDAA 400
    IVEMVPGKPM CVESFSQYPP LGRFAVRDMR QTVAVGVIKN VEKKSGGAGK 450
    VTKSAQKAQK AGK 463
    Length:463
    Mass (Da):50,470
    Last modified:June 1, 1994 - v1
    Checksum:i31E4E341CEE797EC
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti427 – 4271R → P in AAA91835. (PubMed:7945283)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti70 – 701G → S Found in a patient with mental retardation, severe delay of psychomotor development, very limited speech, autistic features and aggressive behaviors. 1 Publication
    VAR_069395

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X70940 mRNA. Translation: CAA50280.1.
    AF163763 Genomic DNA. Translation: AAF80488.1.
    AB451389 mRNA. Translation: BAG70203.1.
    AL121829 Genomic DNA. Translation: CAC15522.1.
    CH471077 Genomic DNA. Translation: EAW75260.1.
    BC000432 mRNA. Translation: AAH00432.1.
    BC110409 mRNA. Translation: AAI10410.1.
    L10340 mRNA. Translation: AAA91835.1.
    CCDSiCCDS13522.1.
    PIRiS35033. EFHUA2.
    RefSeqiNP_001949.1. NM_001958.3.
    UniGeneiHs.433839.

    Genome annotation databases

    EnsembliENST00000217182; ENSP00000217182; ENSG00000101210.
    ENST00000298049; ENSP00000298049; ENSG00000101210.
    GeneIDi1917.
    KEGGihsa:1917.
    UCSCiuc002yfe.2. human.

    Polymorphism databases

    DMDMi544231.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X70940 mRNA. Translation: CAA50280.1 .
    AF163763 Genomic DNA. Translation: AAF80488.1 .
    AB451389 mRNA. Translation: BAG70203.1 .
    AL121829 Genomic DNA. Translation: CAC15522.1 .
    CH471077 Genomic DNA. Translation: EAW75260.1 .
    BC000432 mRNA. Translation: AAH00432.1 .
    BC110409 mRNA. Translation: AAI10410.1 .
    L10340 mRNA. Translation: AAA91835.1 .
    CCDSi CCDS13522.1.
    PIRi S35033. EFHUA2.
    RefSeqi NP_001949.1. NM_001958.3.
    UniGenei Hs.433839.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3C5J X-ray 1.80 C 343-355 [» ]
    ProteinModelPortali Q05639.
    SMRi Q05639. Positions 2-443.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108238. 43 interactions.
    IntActi Q05639. 24 interactions.
    MINTi MINT-1141378.
    STRINGi 9606.ENSP00000217182.

    Chemistry

    BindingDBi Q05639.
    ChEMBLi CHEMBL1795122.

    PTM databases

    PhosphoSitei Q05639.

    Polymorphism databases

    DMDMi 544231.

    Proteomic databases

    MaxQBi Q05639.
    PaxDbi Q05639.
    PeptideAtlasi Q05639.
    PRIDEi Q05639.

    Protocols and materials databases

    DNASUi 1917.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000217182 ; ENSP00000217182 ; ENSG00000101210 .
    ENST00000298049 ; ENSP00000298049 ; ENSG00000101210 .
    GeneIDi 1917.
    KEGGi hsa:1917.
    UCSCi uc002yfe.2. human.

    Organism-specific databases

    CTDi 1917.
    GeneCardsi GC20M062119.
    HGNCi HGNC:3192. EEF1A2.
    HPAi CAB034019.
    MIMi 602959. gene.
    neXtProti NX_Q05639.
    PharmGKBi PA36219.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5256.
    HOGENOMi HOG000229291.
    HOVERGENi HBG000179.
    InParanoidi Q05639.
    KOi K03231.
    OMAi VACTFES.
    OrthoDBi EOG7NKKK3.
    PhylomeDBi Q05639.
    TreeFami TF300304.

    Enzyme and pathway databases

    Reactomei REACT_1477. Eukaryotic Translation Elongation.

    Miscellaneous databases

    EvolutionaryTracei Q05639.
    GeneWikii EEF1A2.
    GenomeRNAii 1917.
    NextBioi 7803.
    PROi Q05639.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q05639.
    CleanExi HS_EEF1A2.
    Genevestigatori Q05639.

    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. "Tissue-dependent variation in the expression of elongation factor-1 alpha isoforms: isolation and characterisation of a cDNA encoding a novel variant of human elongation-factor 1 alpha."
      Knudsen S.M., Frydenberg J., Clark B.F.C., Leffers H.
      Eur. J. Biochem. 215:549-554(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "The human elongation factor 1 A-2 gene (EEF1A2): complete sequence and characterization of gene structure and promoter activity."
      Bischoff C., Kahns S., Lund A., Joergensen H.F., Praestegaard M., Clark B.F.C., Leffers H.
      Genomics 68:63-70(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
      Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.
      , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N.
      Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    4. "The DNA sequence and comparative analysis of human chromosome 20."
      Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
      , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
      Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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: Duodenum and Lung.
    7. "Cloning of human and mouse brain cDNAs coding for S1, the second member of the mammalian elongation factor-1 alpha gene family: analysis of a possible evolutionary pathway."
      Lee S., Ann D.K., Wang E.
      Biochem. Biophys. Res. Commun. 203:1371-1377(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 29-463.
      Tissue: Hippocampus.
    8. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-179 AND LYS-439, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "The structure of HLA-DR52c: comparison to other HLA-DRB3 alleles."
      Dai S., Crawford F., Marrack P., Kappler J.W.
      Proc. Natl. Acad. Sci. U.S.A. 105:11893-11897(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 343-355 IN COMPLEX WITH HLA-DRA/HLA-DRB3 HETERODIMER.
    11. Cited for: VARIANT SER-70.

    Entry informationi

    Entry nameiEF1A2_HUMAN
    AccessioniPrimary (citable) accession number: Q05639
    Secondary accession number(s): B5BUF3
    , E1P5J1, P54266, Q0VGC7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: June 1, 1994
    Last modified: October 1, 2014
    This is version 156 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, Reference proteome

    Documents

    1. Human chromosome 20
      Human chromosome 20: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3