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Q86YI5

- Q86YI5_HUMAN

UniProt

Q86YI5 - Q86YI5_HUMAN

Protein

Acetyltransferase component of pyruvate dehydrogenase complex

Gene

DLAT

Organism
Homo sapiens (Human)
Status
Unreviewed - Annotation score: 2 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 101 (01 Oct 2014)
      Sequence version 1 (01 Jun 2003)
      Previous versions | rss
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    Functioni

    The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2.UniRule annotation

    Catalytic activityi

    Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine.

    Cofactori

    Binds 1 lipoyl cofactor covalently.UniRule annotation
    Binds 2 lipoyl cofactors covalently.UniRule annotation
    Binds 3 lipoyl cofactors covalently.UniRule annotation

    GO - Molecular functioni

    1. dihydrolipoyllysine-residue acetyltransferase activity Source: UniProtKB-EC

    GO - Biological processi

    1. pyruvate metabolic process Source: InterPro

    Keywords - Molecular functioni

    AcyltransferaseUniRule annotation, Transferase

    Keywords - Ligandi

    PyruvateImported

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Acetyltransferase component of pyruvate dehydrogenase complexUniRule annotation (EC:2.3.1.12UniRule annotation)
    Gene namesi
    Name:DLATImported
    OrganismiHomo sapiens (Human)Imported
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

    Subcellular locationi

    Mitochondrion matrix UniRule annotation

    GO - Cellular componenti

    1. mitochondrial matrix Source: UniProtKB-SubCell
    2. mitochondrion Source: HPA
    3. pyruvate dehydrogenase complex Source: InterPro

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27350.

    PTM / Processingi

    Miscellaneous databases

    PMAP-CutDBQ86YI5.

    Structurei

    3D structure databases

    SMRiQ86YI5. Positions 92-182, 214-306, 354-393, 409-647.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Contains 2 lipoyl-binding domains.UniRule annotation

    Keywords - Domaini

    LipoylUniRule annotation

    Phylogenomic databases

    HOVERGENiHBG005063.
    KOiK00627.
    OMAiPISNIRK.
    PhylomeDBiQ86YI5.

    Family and domain databases

    Gene3Di3.30.559.10. 1 hit.
    4.10.320.10. 1 hit.
    InterProiIPR003016. 2-oxoA_DH_lipoyl-BS.
    IPR001078. 2-oxoacid_DH_actylTfrase.
    IPR000089. Biotin_lipoyl.
    IPR023213. CAT-like_dom.
    IPR004167. E3-bd.
    IPR006257. LAT1.
    IPR011053. Single_hybrid_motif.
    [Graphical view]
    PfamiPF00198. 2-oxoacid_dh. 1 hit.
    PF00364. Biotin_lipoyl. 2 hits.
    PF02817. E3_binding. 1 hit.
    [Graphical view]
    SUPFAMiSSF47005. SSF47005. 1 hit.
    SSF51230. SSF51230. 2 hits.
    TIGRFAMsiTIGR01349. PDHac_trf_mito. 1 hit.
    PROSITEiPS50968. BIOTINYL_LIPOYL. 2 hits.
    PS00189. LIPOYL. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q86YI5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MWRVCARRAQ NVAPWAGLEA RWTALQEVPG TPRVTSRSGP APARRNSVTT    50
    GYGGVRALCG WTPSSGATPR NRLLLQLLGS PGRRYYSLPP HQKVPLPSLS 100
    PTMQAGTIAR WEKKEGDKIN EGDLIAEVET DKATVGFESL EECYMAKILV 150
    AEGTRDVPIG AIICITVGKP EDIEAFKNYT LDSSAAPTPQ AAPAPTPAAT 200
    ASPPTPSAQA PGSSYPPHMQ VLLPALSPTM TMGTVQRWEK KVGEKLSEGD 250
    LLAEIETDKA TIGFEVQEEG YLAKILVPEG TRDVPLGTPL CIIVEKEADI 300
    SAFADYRPTE VTDLKPQVPP PTPPPVAAVP PTPQPLAPTP SAPCPATPAG 350
    PKGRVFVSPL AKKLAVEKGI DLTQVKGTGP DGRITKKDID SFVPSKVAPA 400
    PAAVVPPTGP GMAPVPTGVF TDIPISNIRR VIAQRLMQSK QTIPHYYLSI 450
    DVNMGEVLLV RKELNKILEG RSKISVNDFI IKASALACLK VPEANSSWMD 500
    TVIRQNHVVD VSVAVSTPAG LITPIVFNAH IKGVETIAND VVSLATKARE 550
    GKLQPHEFQG GTFTISNLGM FGIKNFSAII NPPQACILAI GASEDKLVPA 600
    DNEKGFDVAS MMSVTLSCDH RVVDGAVGAQ WLAEFRKYLE KPITMLL 647
    Length:647
    Mass (Da):68,997
    Last modified:June 1, 2003 - v1
    Checksum:iDD93A8E666E377C2
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC039084 mRNA. Translation: AAH39084.1.
    EF444972 Genomic DNA. Translation: ACA05975.1.
    AK057299 mRNA. Translation: BAG51900.1.
    RefSeqiNP_001922.2. NM_001931.4.
    UniGeneiHs.335551.

    Genome annotation databases

    GeneIDi1737.
    KEGGihsa:1737.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC039084 mRNA. Translation: AAH39084.1 .
    EF444972 Genomic DNA. Translation: ACA05975.1 .
    AK057299 mRNA. Translation: BAG51900.1 .
    RefSeqi NP_001922.2. NM_001931.4.
    UniGenei Hs.335551.

    3D structure databases

    SMRi Q86YI5. Positions 92-182, 214-306, 354-393, 409-647.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    DNASUi 1737.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 1737.
    KEGGi hsa:1737.

    Organism-specific databases

    CTDi 1737.
    PharmGKBi PA27350.

    Phylogenomic databases

    HOVERGENi HBG005063.
    KOi K00627.
    OMAi PISNIRK.
    PhylomeDBi Q86YI5.

    Miscellaneous databases

    GenomeRNAii 1737.
    NextBioi 7043.
    PMAP-CutDB Q86YI5.

    Family and domain databases

    Gene3Di 3.30.559.10. 1 hit.
    4.10.320.10. 1 hit.
    InterProi IPR003016. 2-oxoA_DH_lipoyl-BS.
    IPR001078. 2-oxoacid_DH_actylTfrase.
    IPR000089. Biotin_lipoyl.
    IPR023213. CAT-like_dom.
    IPR004167. E3-bd.
    IPR006257. LAT1.
    IPR011053. Single_hybrid_motif.
    [Graphical view ]
    Pfami PF00198. 2-oxoacid_dh. 1 hit.
    PF00364. Biotin_lipoyl. 2 hits.
    PF02817. E3_binding. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47005. SSF47005. 1 hit.
    SSF51230. SSF51230. 2 hits.
    TIGRFAMsi TIGR01349. PDHac_trf_mito. 1 hit.
    PROSITEi PS50968. BIOTINYL_LIPOYL. 2 hits.
    PS00189. LIPOYL. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H., Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M., Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M.
      , Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F., Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T., Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F., Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E., Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y., Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E., Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y., Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W., Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J., Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J., Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W., Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I., Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U., Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A., Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: TestisImported.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE.
      Tissue: TestisImported.
    3. Stockwell T.B., Busam D.A., Ferriera S.M., Brownley A.N., Strausberg R.L., Kirkness E.F., Rogers Y.-H., Levy S.
      Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE.

    Entry informationi

    Entry nameiQ86YI5_HUMAN
    AccessioniPrimary (citable) accession number: Q86YI5
    Entry historyi
    Integrated into UniProtKB/TrEMBL: June 1, 2003
    Last sequence update: June 1, 2003
    Last modified: October 1, 2014
    This is version 101 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiUnreviewed (UniProtKB/TrEMBL)
    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.