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Q8BMF4

- ODP2_MOUSE

UniProt

Q8BMF4 - ODP2_MOUSE

Protein

Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial

Gene

Dlat

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 94 (01 Oct 2014)
      Sequence version 2 (01 May 2007)
      Previous versions | rss
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    Functioni

    The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2, and thereby links the glycolytic pathway to the tricarboxylic cycle.By similarity

    Catalytic activityi

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

    Cofactori

    Binds 1 lipoyl cofactor covalently.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei615 – 6151Sequence Analysis
    Active sitei619 – 6191Sequence Analysis

    GO - Molecular functioni

    1. dihydrolipoyllysine-residue acetyltransferase activity Source: MGI

    GO - Biological processi

    1. acetyl-CoA biosynthetic process from pyruvate Source: MGI
    2. glucose metabolic process Source: UniProtKB-KW
    3. tricarboxylic acid cycle Source: UniProtKB-KW

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Keywords - Biological processi

    Carbohydrate metabolism, Glucose metabolism, Tricarboxylic acid cycle

    Enzyme and pathway databases

    ReactomeiREACT_226284. Regulation of pyruvate dehydrogenase (PDH) complex.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial (EC:2.3.1.12)
    Alternative name(s):
    Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
    Pyruvate dehydrogenase complex component E2
    Short name:
    PDC-E2
    Short name:
    PDCE2
    Gene namesi
    Name:Dlat
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 9

    Organism-specific databases

    MGIiMGI:2385311. Dlat.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrial pyruvate dehydrogenase complex Source: MGI
    2. mitochondrion Source: MGI
    3. pyruvate dehydrogenase complex Source: MGI

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 8585MitochondrionBy similarityAdd
    BLAST
    Chaini86 – 642557Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrialPRO_0000285717Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei258 – 2581N6-lipoyllysineBy similarity
    Modified residuei461 – 4611N6-acetyllysineBy similarity
    Modified residuei468 – 4681N6-succinyllysine1 Publication
    Modified residuei542 – 5421N6-succinyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ8BMF4.
    PaxDbiQ8BMF4.
    PRIDEiQ8BMF4.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00153660.
    UCD-2DPAGEQ8BMF4.

    PTM databases

    PhosphoSiteiQ8BMF4.

    Expressioni

    Gene expression databases

    BgeeiQ8BMF4.
    GenevestigatoriQ8BMF4.

    Interactioni

    Subunit structurei

    Part of the multimeric pyruvate dehydrogenase complex that contains multiple copies of pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (DLAT, E2) and lipoamide dehydrogenase (DLD, E3). These subunits are bound to an inner core composed of about 48 DLAT and 12 PDHX molecules. Interacts with PDK2 and PDK3 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi231646. 2 interactions.
    IntActiQ8BMF4. 7 interactions.
    MINTiMINT-135876.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8BMF4.
    SMRiQ8BMF4. Positions 91-181, 217-294, 349-388, 404-642.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini91 – 16575Lipoyl-binding 1Add
    BLAST
    Domaini218 – 29275Lipoyl-binding 2Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni353 – 38432E3- and/or E1-component binding domainSequence AnalysisAdd
    BLAST
    Regioni466 – 642177CatalyticBy similarityAdd
    BLAST
    Regioni610 – 62112CoA-bindingBy similarityAdd
    BLAST

    Sequence similaritiesi

    Belongs to the 2-oxoacid dehydrogenase family.Curated
    Contains 2 lipoyl-binding domains.Curated

    Keywords - Domaini

    Lipoyl, Repeat, Transit peptide

    Phylogenomic databases

    eggNOGiCOG0508.
    GeneTreeiENSGT00740000115255.
    HOGENOMiHOG000281566.
    HOVERGENiHBG005063.
    InParanoidiQ8BMF4.
    KOiK00627.
    OMAiPISNIRK.
    OrthoDBiEOG7K3TKW.
    PhylomeDBiQ8BMF4.
    TreeFamiTF106145.

    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.

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

    Q8BMF4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MWRVCARRAR SAVPRDGFRA RWAALKEGPG APCGSPRIGP AAVRCGSGIP    50
    RYGVRSLCGW SSGSGTVPRN RLLRQLLGSP SRRSYSLPPH QKVPLPSLSP 100
    TMQAGTIARW EKKEGEKISE GDLIAEVETD KATVGFESLE ECYMAKILVP 150
    EGTRDVPVGS IICITVEKPQ DIEAFKNYTL DLAAAAAPQA APAAAPAPAA 200
    APAAPSASAP GSSYPTHMQI VLPALSPTMT MGTVQRWEKK VGEKLSEGDL 250
    LAEIETDKAT IGFEVQEEGY LAKILVPEGT RDVPLGAPLC IIVEKQEDIA 300
    AFADYRPTEV TSLKPQAAPP APPPVAAVPP TPQPVAPTPS AAPAGPKGRV 350
    FVSPLAKKLA AEKGIDLTQV KGTGPEGRII KKDIDSFVPS KAAPAAAAAM 400
    APPGPRVAPA PAGVFTDIPI SNIRRVIAQR LMQSKQTIPH YYLSVDVNMG 450
    EVLLVRKELN KMLEGKGKIS VNDFIIKASA LACLKVPEAN SSWMDTVIRQ 500
    NHVVDVSVAV STPAGLITPI VFNAHIKGLE TIASDVVSLA SKAREGKLQP 550
    HEFQGGTFTI SNLGMFGIKN FSAIINPPQA CILAIGASED KLIPADNEKG 600
    FDVASVMSVT LSCDHRVVDG AVGAQWLAEF KKYLEKPITM LL 642
    Length:642
    Mass (Da):67,942
    Last modified:May 1, 2007 - v2
    Checksum:i1294FAC4857FC29C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti84 – 841S → Y in AAL02400. (PubMed:12108679)Curated
    Sequence conflicti198 – 1981P → T in BAC27715. (PubMed:16141072)Curated
    Sequence conflicti225 – 2251L → P in AAL02400. (PubMed:12108679)Curated
    Sequence conflicti393 – 3931A → V in AAH31495. (PubMed:15489334)Curated
    Sequence conflicti604 – 6041A → V in AAH31495. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK032124 mRNA. Translation: BAC27715.1.
    BC026680 mRNA. Translation: AAH26680.1.
    BC031495 mRNA. Translation: AAH31495.1.
    BC069862 mRNA. Translation: AAH69862.1.
    AY044265 mRNA. Translation: AAL02400.1.
    CCDSiCCDS23168.1.
    RefSeqiNP_663589.3. NM_145614.4.
    UniGeneiMm.285076.
    Mm.471144.

    Genome annotation databases

    EnsembliENSMUST00000034567; ENSMUSP00000034567; ENSMUSG00000000168.
    GeneIDi235339.
    KEGGimmu:235339.
    UCSCiuc009pka.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK032124 mRNA. Translation: BAC27715.1 .
    BC026680 mRNA. Translation: AAH26680.1 .
    BC031495 mRNA. Translation: AAH31495.1 .
    BC069862 mRNA. Translation: AAH69862.1 .
    AY044265 mRNA. Translation: AAL02400.1 .
    CCDSi CCDS23168.1.
    RefSeqi NP_663589.3. NM_145614.4.
    UniGenei Mm.285076.
    Mm.471144.

    3D structure databases

    ProteinModelPortali Q8BMF4.
    SMRi Q8BMF4. Positions 91-181, 217-294, 349-388, 404-642.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 231646. 2 interactions.
    IntActi Q8BMF4. 7 interactions.
    MINTi MINT-135876.

    PTM databases

    PhosphoSitei Q8BMF4.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00153660.
    UCD-2DPAGE Q8BMF4.

    Proteomic databases

    MaxQBi Q8BMF4.
    PaxDbi Q8BMF4.
    PRIDEi Q8BMF4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000034567 ; ENSMUSP00000034567 ; ENSMUSG00000000168 .
    GeneIDi 235339.
    KEGGi mmu:235339.
    UCSCi uc009pka.2. mouse.

    Organism-specific databases

    CTDi 1737.
    MGIi MGI:2385311. Dlat.

    Phylogenomic databases

    eggNOGi COG0508.
    GeneTreei ENSGT00740000115255.
    HOGENOMi HOG000281566.
    HOVERGENi HBG005063.
    InParanoidi Q8BMF4.
    KOi K00627.
    OMAi PISNIRK.
    OrthoDBi EOG7K3TKW.
    PhylomeDBi Q8BMF4.
    TreeFami TF106145.

    Enzyme and pathway databases

    Reactomei REACT_226284. Regulation of pyruvate dehydrogenase (PDH) complex.

    Miscellaneous databases

    ChiTaRSi DLAT. mouse.
    NextBioi 382617.
    PROi Q8BMF4.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q8BMF4.
    Genevestigatori Q8BMF4.

    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 transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Medulla oblongata.
    2. "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].
      Strain: Czech II, FVB/N-3 and NMRI.
      Tissue: Mammary tumor.
    3. "Molecular cloning, and characterization and expression of dihydrolipoamide acetyltransferase component of murine pyruvate dehydrogenase complex in bile duct cancer cells."
      Wang L., Kaneko S., Kagaya M., Ohno H., Honda M., Kobayashi K.
      J. Gastroenterol. 37:449-454(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 84-642.
      Tissue: Hepatoma.
    4. Lubec G., Klug S., Sunyer B., Chen W.-Q.
      Submitted (JAN-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 93-109; 147-176; 282-295; 383-424; 469-477; 486-499; 528-542; 548-569; 600-631 AND 633-642, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: OF1.
      Tissue: Hippocampus.
    5. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
      Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
      Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain.
    6. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-468 AND LYS-542, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiODP2_MOUSE
    AccessioniPrimary (citable) accession number: Q8BMF4
    Secondary accession number(s): Q8K2G8, Q8R339, Q91ZB1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 2007
    Last sequence update: May 1, 2007
    Last modified: October 1, 2014
    This is version 94 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3