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Q8BKZ9

- ODPX_MOUSE

UniProt

Q8BKZ9 - ODPX_MOUSE

Protein

Pyruvate dehydrogenase protein X component, mitochondrial

Gene

Pdhx

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 102 (01 Oct 2014)
      Sequence version 1 (01 Mar 2003)
      Previous versions | rss
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    Functioni

    Required for anchoring dihydrolipoamide dehydrogenase (E3) to the dihydrolipoamide transacetylase (E2) core of the pyruvate dehydrogenase complexes of eukaryotes. This specific binding is essential for a functional PDH complex By similarity.By similarity

    GO - Molecular functioni

    1. transferase activity, transferring acyl groups Source: InterPro

    Enzyme and pathway databases

    ReactomeiREACT_226284. Regulation of pyruvate dehydrogenase (PDH) complex.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Pyruvate dehydrogenase protein X component, mitochondrial
    Alternative name(s):
    Dihydrolipoamide dehydrogenase-binding protein of pyruvate dehydrogenase complex
    Lipoyl-containing pyruvate dehydrogenase complex component X
    Gene namesi
    Name:Pdhx
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 2

    Organism-specific databases

    MGIiMGI:1351627. Pdhx.

    Subcellular locationi

    Mitochondrion matrix By similarity

    GO - Cellular componenti

    1. mitochondrial matrix Source: UniProtKB-SubCell
    2. mitochondrion Source: MGI

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 5353MitochondrionBy similarityAdd
    BLAST
    Chaini54 – 501448Pyruvate dehydrogenase protein X component, mitochondrialPRO_0000020485Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei97 – 971N6-lipoyllysineBy similarity
    Modified residuei194 – 1941N6-acetyllysineBy similarity
    Modified residuei394 – 3941N6-succinyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ8BKZ9.
    PaxDbiQ8BKZ9.
    PRIDEiQ8BKZ9.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00222767.

    PTM databases

    PhosphoSiteiQ8BKZ9.

    Expressioni

    Gene expression databases

    BgeeiQ8BKZ9.
    CleanExiMM_PDHX.
    GenevestigatoriQ8BKZ9.

    Interactioni

    Subunit structurei

    Part of the inner core of the multimeric pyruvate dehydrogenase complex that is composed of about 48 DLAT and 12 PDHX molecules. This core binds multiple copies of pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (DLAT, E2) and lipoamide dehydrogenase (DLD, E3) By similarity.By similarity

    Protein-protein interaction databases

    IntActiQ8BKZ9. 2 interactions.
    MINTiMINT-1867323.
    STRINGi10090.ENSMUSP00000011058.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8BKZ9.
    SMRiQ8BKZ9. Positions 57-144, 183-224, 266-500.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini57 – 13175Lipoyl-bindingAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni183 – 21432Interaction with DLDBy similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi150 – 17122Pro-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the 2-oxoacid dehydrogenase family.Curated
    Contains 1 lipoyl-binding domain.Curated

    Keywords - Domaini

    Lipoyl, Transit peptide

    Phylogenomic databases

    eggNOGiCOG0508.
    GeneTreeiENSGT00740000115591.
    HOGENOMiHOG000281566.
    HOVERGENiHBG005063.
    InParanoidiQ8BKZ9.
    KOiK13997.
    OMAiSWRLGCD.
    OrthoDBiEOG7K3TKW.
    PhylomeDBiQ8BKZ9.
    TreeFamiTF332256.

    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.
    IPR011053. Single_hybrid_motif.
    [Graphical view]
    PfamiPF00198. 2-oxoacid_dh. 1 hit.
    PF00364. Biotin_lipoyl. 1 hit.
    PF02817. E3_binding. 1 hit.
    [Graphical view]
    SUPFAMiSSF47005. SSF47005. 1 hit.
    SSF51230. SSF51230. 1 hit.
    PROSITEiPS50968. BIOTINYL_LIPOYL. 1 hit.
    PS00189. LIPOYL. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q8BKZ9-1 [UniParc]FASTAAdd to Basket

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    MAASWRLHCN QPLLRYLLGF SSRRSLGLAQ GAAAWPVDRG ASWRWFHSTQ    50
    LLQADPIKVL MPSLSPTMEQ GNIVKWLRKE GEAVSAGDSL CEIETDKAVV 100
    TLDANDDGIL AKIVVEEGAK NIQLGSLIAL MVEEGEDWKQ VEIPKDVSAP 150
    PPVSKPPAPT QPSPQPQIPC PARKEHKGTA RFRLSPAARN ILEKHSLDAS 200
    QGTATGPRGI FTKEDALKLV ELKQMGKITE SRPASAPPPS LSASVPPQAT 250
    AGPSYPRPMT PPVSIPGQPN AAGTFTEIPA SNIRRVIAKR LTESKSTVPH 300
    AYATADCDLG AVLKVRRDLV KDDIKVSVND FIIRAAAVTL KQMPGVNVTW 350
    DGEGPKQLPS VDISVAVATD KGLITPIIKD AAAKGIQEIA DSVKVLSKKA 400
    RDGKLMPEEY QGGSFSISNL GMFGIDEFAA VINPPQACIL AVGRFRPVLK 450
    LTEDEEGNPQ LQQHQLITVT MSSDSRVVDD ELATRFLETF KANLENPMRL 500
    G 501
    Length:501
    Mass (Da):53,999
    Last modified:March 1, 2003 - v1
    Checksum:i3FD1FA752EAC5092
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK047670 mRNA. Translation: BAC33120.1.
    BC061231 mRNA. Translation: AAH61231.1.
    CCDSiCCDS16473.1.
    RefSeqiNP_780303.1. NM_175094.5.
    UniGeneiMm.315011.

    Genome annotation databases

    EnsembliENSMUST00000011058; ENSMUSP00000011058; ENSMUSG00000010914.
    GeneIDi27402.
    KEGGimmu:27402.
    UCSCiuc008lil.3. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK047670 mRNA. Translation: BAC33120.1 .
    BC061231 mRNA. Translation: AAH61231.1 .
    CCDSi CCDS16473.1.
    RefSeqi NP_780303.1. NM_175094.5.
    UniGenei Mm.315011.

    3D structure databases

    ProteinModelPortali Q8BKZ9.
    SMRi Q8BKZ9. Positions 57-144, 183-224, 266-500.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q8BKZ9. 2 interactions.
    MINTi MINT-1867323.
    STRINGi 10090.ENSMUSP00000011058.

    PTM databases

    PhosphoSitei Q8BKZ9.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00222767.

    Proteomic databases

    MaxQBi Q8BKZ9.
    PaxDbi Q8BKZ9.
    PRIDEi Q8BKZ9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000011058 ; ENSMUSP00000011058 ; ENSMUSG00000010914 .
    GeneIDi 27402.
    KEGGi mmu:27402.
    UCSCi uc008lil.3. mouse.

    Organism-specific databases

    CTDi 8050.
    MGIi MGI:1351627. Pdhx.

    Phylogenomic databases

    eggNOGi COG0508.
    GeneTreei ENSGT00740000115591.
    HOGENOMi HOG000281566.
    HOVERGENi HBG005063.
    InParanoidi Q8BKZ9.
    KOi K13997.
    OMAi SWRLGCD.
    OrthoDBi EOG7K3TKW.
    PhylomeDBi Q8BKZ9.
    TreeFami TF332256.

    Enzyme and pathway databases

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

    Miscellaneous databases

    ChiTaRSi PDHX. mouse.
    NextBioi 305398.
    PROi Q8BKZ9.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q8BKZ9.
    CleanExi MM_PDHX.
    Genevestigatori Q8BKZ9.

    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.
    IPR011053. Single_hybrid_motif.
    [Graphical view ]
    Pfami PF00198. 2-oxoacid_dh. 1 hit.
    PF00364. Biotin_lipoyl. 1 hit.
    PF02817. E3_binding. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47005. SSF47005. 1 hit.
    SSF51230. SSF51230. 1 hit.
    PROSITEi PS50968. BIOTINYL_LIPOYL. 1 hit.
    PS00189. LIPOYL. 1 hit.
    [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: Corpus striatum.
    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].
      Tissue: Brain.
    3. "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-394, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiODPX_MOUSE
    AccessioniPrimary (citable) accession number: Q8BKZ9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 4, 2005
    Last sequence update: March 1, 2003
    Last modified: October 1, 2014
    This is version 102 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, 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