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P49411

- EFTU_HUMAN

UniProt

P49411 - EFTU_HUMAN

Protein

Elongation factor Tu, mitochondrial

Gene

TUFM

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 155 (01 Oct 2014)
      Sequence version 2 (01 Oct 1996)
      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 bindingi64 – 718GTPBy similarity
    Nucleotide bindingi126 – 1305GTPBy similarity
    Nucleotide bindingi181 – 1844GTPBy similarity

    GO - Molecular functioni

    1. GTPase activity Source: InterPro
    2. GTP binding Source: UniProtKB-KW
    3. poly(A) RNA binding Source: UniProtKB
    4. translation elongation factor activity Source: UniProtKB

    GO - Biological processi

    1. translational elongation Source: UniProtKB

    Keywords - Molecular functioni

    Elongation factor

    Keywords - Biological processi

    Protein biosynthesis

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Enzyme and pathway databases

    SignaLinkiP49411.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Elongation factor Tu, mitochondrial
    Short name:
    EF-Tu
    Alternative name(s):
    P43
    Gene namesi
    Name:TUFM
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:12420. TUFM.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt
    2. membrane Source: UniProtKB
    3. mitochondrial nucleoid Source: BHF-UCL
    4. mitochondrion Source: UniProtKB

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Involvement in diseasei

    Combined oxidative phosphorylation deficiency 4 (COXPD4) [MIM:610678]: A mitochondrial disease resulting in neonatal lactic acidosis, rapidly progressive encephalopathy, severely decreased mitochondrial protein synthesis, and combined deficiency of mtDNA-related mitochondrial respiratory chain complexes.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti336 – 3361R → Q in COXPD4. 1 Publication
    VAR_031902

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi610678. phenotype.
    Orphaneti254925. Combined oxidative phosphorylation defect type 4.
    PharmGKBiPA37082.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 4343Mitochondrion2 PublicationsAdd
    BLAST
    Chaini44 – 452409Elongation factor Tu, mitochondrialPRO_0000007462Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei79 – 791N6-acetyllysine1 Publication
    Modified residuei88 – 881N6-acetyllysine1 Publication
    Modified residuei256 – 2561N6-acetyllysine1 Publication
    Modified residuei418 – 4181N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP49411.
    PaxDbiP49411.
    PRIDEiP49411.

    2D gel databases

    DOSAC-COBS-2DPAGEP49411.
    OGPiP49411.
    REPRODUCTION-2DPAGEIPI00027107.
    SWISS-2DPAGEP49411.
    UCD-2DPAGEP49411.

    PTM databases

    PhosphoSiteiP49411.

    Expressioni

    Gene expression databases

    ArrayExpressiP49411.
    BgeeiP49411.
    CleanExiHS_TUFM.
    GenevestigatoriP49411.

    Organism-specific databases

    HPAiHPA018991.
    HPA024087.

    Interactioni

    Protein-protein interaction databases

    BioGridi113135. 119 interactions.
    IntActiP49411. 24 interactions.
    MINTiMINT-224570.
    STRINGi9606.ENSP00000322439.

    Structurei

    3D structure databases

    ProteinModelPortaliP49411.
    SMRiP49411. Positions 24-451.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini55 – 251197tr-type GPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni64 – 718G1PROSITE-ProRule annotation
    Regioni105 – 1095G2PROSITE-ProRule annotation
    Regioni126 – 1294G3PROSITE-ProRule annotation
    Regioni181 – 1844G4PROSITE-ProRule annotation
    Regioni219 – 2213G5PROSITE-ProRule annotation

    Sequence similaritiesi

    Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A subfamily.PROSITE-ProRule annotation
    Contains 1 tr-type G (guanine nucleotide-binding) domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0050.
    HOGENOMiHOG000229290.
    HOVERGENiHBG001535.
    InParanoidiP49411.
    KOiK02358.
    OrthoDBiEOG73BVCN.
    PhylomeDBiP49411.
    TreeFamiTF300432.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    InterProiIPR000795. EF_GTP-bd_dom.
    IPR027417. P-loop_NTPase.
    IPR009000. Transl_B-barrel.
    IPR009001. Transl_elong_EF1A/Init_IF2_C.
    IPR004161. Transl_elong_EFTu/EF1A_2.
    IPR004541. Transl_elong_EFTu/EF1A_bac/org.
    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.
    TIGRFAMsiTIGR00485. EF-Tu. 1 hit.
    PROSITEiPS00301. G_TR_1. 1 hit.
    PS51722. G_TR_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P49411-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAATLLRAT PHFSGLAAGR TFLLQGLLRL LKAPALPLLC RGLAVEAKKT    50
    YVRDKPHVNV GTIGHVDHGK TTLTAAITKI LAEGGGAKFK KYEEIDNAPE 100
    ERARGITINA AHVEYSTAAR HYAHTDCPGH ADYVKNMITG TAPLDGCILV 150
    VAANDGPMPQ TREHLLLARQ IGVEHVVVYV NKADAVQDSE MVELVELEIR 200
    ELLTEFGYKG EETPVIVGSA LCALEGRDPE LGLKSVQKLL DAVDTYIPVP 250
    ARDLEKPFLL PVEAVYSVPG RGTVVTGTLE RGILKKGDEC ELLGHSKNIR 300
    TVVTGIEMFH KSLERAEAGD NLGALVRGLK REDLRRGLVM VKPGSIKPHQ 350
    KVEAQVYILS KEEGGRHKPF VSHFMPVMFS LTWDMACRII LPPEKELAMP 400
    GEDLKFNLIL RQPMILEKGQ RFTLRDGNRT IGTGLVTNTL AMTEEEKNIK 450
    WG 452
    Length:452
    Mass (Da):49,542
    Last modified:October 1, 1996 - v2
    Checksum:iE37274ABFFDB5FC7
    GO

    Sequence cautioni

    The sequence AAC60647.1 differs from that shown. Reason: Erroneous initiation.
    The sequence AAH01633.2 differs from that shown. Reason: Erroneous initiation.
    The sequence AAH10041.2 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti195 – 1973Missing in AAC60647. (PubMed:7828719)Curated
    Sequence conflicti384 – 3841D → N in AAB00499. (PubMed:8547323)Curated
    Sequence conflicti384 – 3841D → N in CAA72493. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti336 – 3361R → Q in COXPD4. 1 Publication
    VAR_031902

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L38995 mRNA. Translation: AAB00499.1.
    S75463 mRNA. Translation: AAC60647.1. Different initiation.
    X84694 mRNA. Translation: CAA59169.1.
    AC133550 Genomic DNA. No translation available.
    BC001633 mRNA. Translation: AAH01633.2. Different initiation.
    BC010041 mRNA. Translation: AAH10041.2. Different initiation.
    Y11797 Genomic DNA. Translation: CAA72493.1.
    PIRiS62767.
    S68466.
    RefSeqiNP_003312.3. NM_003321.4.
    UniGeneiHs.12084.

    Genome annotation databases

    EnsembliENST00000313511; ENSP00000322439; ENSG00000178952.
    GeneIDi7284.
    KEGGihsa:7284.
    UCSCiuc002drh.2. human.

    Polymorphism databases

    DMDMi1706611.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L38995 mRNA. Translation: AAB00499.1 .
    S75463 mRNA. Translation: AAC60647.1 . Different initiation.
    X84694 mRNA. Translation: CAA59169.1 .
    AC133550 Genomic DNA. No translation available.
    BC001633 mRNA. Translation: AAH01633.2 . Different initiation.
    BC010041 mRNA. Translation: AAH10041.2 . Different initiation.
    Y11797 Genomic DNA. Translation: CAA72493.1 .
    PIRi S62767.
    S68466.
    RefSeqi NP_003312.3. NM_003321.4.
    UniGenei Hs.12084.

    3D structure databases

    ProteinModelPortali P49411.
    SMRi P49411. Positions 24-451.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113135. 119 interactions.
    IntActi P49411. 24 interactions.
    MINTi MINT-224570.
    STRINGi 9606.ENSP00000322439.

    PTM databases

    PhosphoSitei P49411.

    Polymorphism databases

    DMDMi 1706611.

    2D gel databases

    DOSAC-COBS-2DPAGE P49411.
    OGPi P49411.
    REPRODUCTION-2DPAGE IPI00027107.
    SWISS-2DPAGE P49411.
    UCD-2DPAGE P49411.

    Proteomic databases

    MaxQBi P49411.
    PaxDbi P49411.
    PRIDEi P49411.

    Protocols and materials databases

    DNASUi 7284.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000313511 ; ENSP00000322439 ; ENSG00000178952 .
    GeneIDi 7284.
    KEGGi hsa:7284.
    UCSCi uc002drh.2. human.

    Organism-specific databases

    CTDi 7284.
    GeneCardsi GC16M028853.
    HGNCi HGNC:12420. TUFM.
    HPAi HPA018991.
    HPA024087.
    MIMi 602389. gene.
    610678. phenotype.
    neXtProti NX_P49411.
    Orphaneti 254925. Combined oxidative phosphorylation defect type 4.
    PharmGKBi PA37082.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0050.
    HOGENOMi HOG000229290.
    HOVERGENi HBG001535.
    InParanoidi P49411.
    KOi K02358.
    OrthoDBi EOG73BVCN.
    PhylomeDBi P49411.
    TreeFami TF300432.

    Enzyme and pathway databases

    SignaLinki P49411.

    Miscellaneous databases

    GeneWikii TUFM.
    GenomeRNAii 7284.
    NextBioi 28481.
    PROi P49411.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P49411.
    Bgeei P49411.
    CleanExi HS_TUFM.
    Genevestigatori P49411.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    InterProi IPR000795. EF_GTP-bd_dom.
    IPR027417. P-loop_NTPase.
    IPR009000. Transl_B-barrel.
    IPR009001. Transl_elong_EF1A/Init_IF2_C.
    IPR004161. Transl_elong_EFTu/EF1A_2.
    IPR004541. Transl_elong_EFTu/EF1A_bac/org.
    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 TIGR00485. EF-Tu. 1 hit.
    PROSITEi PS00301. G_TR_1. 1 hit.
    PS51722. G_TR_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning, sequence analysis and expression of mammalian mitochondrial protein synthesis elongation factor Tu."
      Woriax V.L., Burkhart W.A., Spremulli L.L.
      Biochim. Biophys. Acta 1264:347-356(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.
    2. "A mitochondrial elongation factor-like protein is over-expressed in tumours and differentially expressed in normal tissues."
      Wells J., Henkler F., Leversha M., Koshy R.
      FEBS Lett. 358:119-125(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.
    3. "The human mitochondrial elongation factor Tu (EF-Tu) gene: cDNA sequence, genomic localization, genomic structure, and identification of a pseudogene."
      Ling M., Merante F., Chen H.-S., Duff C., Duncan A.M.V., Robinson B.H.
      Gene 197:325-336(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Heart and Kidney.
    4. "The sequence and analysis of duplication-rich human chromosome 16."
      Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
      , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
      Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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: Lung and Placenta.
    6. Dunn M.J.
      Submitted (MAR-1996) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 44-54.
      Tissue: Heart.
    7. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
      Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
      Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 44-53.
      Tissue: Platelet.
    8. Lubec G., Vishwanath V.
      Submitted (MAR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 239-271, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain and Cajal-Retzius cell.
    9. "Human genomic sequences encoding mitochondrial elongation factor EF-Tu: evidence for post-endosymbiotic intron insertion."
      Jacobs H.T., Smurthwaite L., Koshy R.
      Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 379-395.
    10. "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-79; LYS-88; LYS-256 AND LYS-418, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Infantile encephalopathy and defective mitochondrial DNA translation in patients with mutations of mitochondrial elongation factors EFG1 and EFTu."
      Valente L., Tiranti V., Marsano R.M., Malfatti E., Fernandez-Vizarra E., Donnini C., Mereghetti P., De Gioia L., Burlina A., Castellan C., Comi G.P., Savasta S., Ferrero I., Zeviani M.
      Am. J. Hum. Genet. 80:44-58(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT COXPD4 GLN-336.

    Entry informationi

    Entry nameiEFTU_HUMAN
    AccessioniPrimary (citable) accession number: P49411
    Secondary accession number(s): O15276
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 155 of the entry and version 2 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

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 16
      Human chromosome 16: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3