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Q8BFP9

- PDK1_MOUSE

UniProt

Q8BFP9 - PDK1_MOUSE

Protein

[Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 1, mitochondrial

Gene

Pdk1

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 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Serine/threonine kinase that plays a key role in regulation of glucose and fatty acid metabolism and homeostasis via phosphorylation of the pyruvate dehydrogenase subunits PDHA1 and PDHA2. This inhibits pyruvate dehydrogenase activity, and thereby regulates metabolite flux through the tricarboxylic acid cycle, down-regulates aerobic respiration and inhibits the formation of acetyl-coenzyme A from pyruvate. Plays an important role in cellular responses to hypoxia and is important for cell proliferation under hypoxia. Protects cells against apoptosis in response to hypoxia and oxidative stress By similarity.By similarity

    Catalytic activityi

    ATP + [pyruvate dehydrogenase (acetyl-transferring)] = ADP + [pyruvate dehydrogenase (acetyl-transferring)] phosphate.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei316 – 3161ATPBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi277 – 2848ATPBy similarity
    Nucleotide bindingi335 – 3362ATPBy similarity
    Nucleotide bindingi352 – 3576ATPBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. protein serine/threonine kinase activity Source: UniProtKB-KW
    3. pyruvate dehydrogenase (acetyl-transferring) kinase activity Source: UniProtKB

    GO - Biological processi

    1. cell proliferation Source: UniProtKB
    2. glucose metabolic process Source: UniProtKB-KW
    3. hypoxia-inducible factor-1alpha signaling pathway Source: UniProtKB
    4. intracellular signal transduction Source: MGI
    5. intrinsic apoptotic signaling pathway in response to oxidative stress Source: UniProtKB
    6. regulation of acetyl-CoA biosynthetic process from pyruvate Source: UniProtKB
    7. regulation of glucose metabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Carbohydrate metabolism, Glucose metabolism

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_226284. Regulation of pyruvate dehydrogenase (PDH) complex.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    [Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 1, mitochondrial (EC:2.7.11.2)
    Alternative name(s):
    Pyruvate dehydrogenase kinase isoform 1
    Short name:
    PDH kinase 1
    Gene namesi
    Name:Pdk1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 2

    Organism-specific databases

    MGIiMGI:1926119. Pdk1.

    Subcellular locationi

    Mitochondrion matrix By similarity

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 2626MitochondrionSequence AnalysisAdd
    BLAST
    Chaini27 – 434408[Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 1, mitochondrialPRO_0000023438Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei136 – 1361Phosphotyrosine; by FGFR1By similarity
    Modified residuei241 – 2411Phosphotyrosine; by FGFR1, ABL1, FLT3 and JAK2By similarity
    Modified residuei242 – 2421Phosphotyrosine; by FGFR1By similarity
    Modified residuei403 – 4031N6-succinyllysine1 Publication

    Post-translational modificationi

    Phosphorylated by constitutively activated ABL1, FGFR1, FLT3 and JAK2 (in vitro), and this may also occur in cancer cells that express constitutively activated ABL1, FGFR1, FLT3 and JAK2. Phosphorylation at Tyr-241 and Tyr-242 strongly increases kinase activity, while phosphorylation at Tyr-136 has a lesser effect By similarity.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ8BFP9.
    PaxDbiQ8BFP9.
    PRIDEiQ8BFP9.

    PTM databases

    PhosphoSiteiQ8BFP9.

    Expressioni

    Inductioni

    Up-regulated by glucose and palmitate. Up- regulated via the HIF1A signaling pathway in response to hypoxia.2 Publications

    Gene expression databases

    ArrayExpressiQ8BFP9.
    BgeeiQ8BFP9.
    CleanExiMM_PDK1.
    GenevestigatoriQ8BFP9.

    Interactioni

    Subunit structurei

    Homodimer, and heterodimer with PDK2. Interacts with the pyruvate dehydrogenase complex subunit DLAT, and is part of the multimeric pyruvate dehydrogenase complex that contains multiple copies of pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (DLAT, E2) and lipoamide dehydrogenase (DLD, E3) By similarity.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ8BFP9.
    SMRiQ8BFP9. Positions 41-421.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini161 – 391231Histidine kinasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the PDK/BCKDK protein kinase family.Curated
    Contains 1 histidine kinase domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0642.
    GeneTreeiENSGT00550000074574.
    HOGENOMiHOG000164315.
    HOVERGENiHBG000511.
    InParanoidiQ3U5E5.
    KOiK12077.
    OMAiEDAKTIY.
    OrthoDBiEOG71VSSV.
    TreeFamiTF314918.

    Family and domain databases

    Gene3Di1.20.140.20. 1 hit.
    3.30.565.10. 1 hit.
    InterProiIPR018955. BCDHK/PDK_N.
    IPR003594. HATPase_ATP-bd.
    IPR005467. Sig_transdc_His_kinase_core.
    [Graphical view]
    PfamiPF10436. BCDHK_Adom3. 1 hit.
    PF02518. HATPase_c. 1 hit.
    [Graphical view]
    SMARTiSM00387. HATPase_c. 1 hit.
    [Graphical view]
    SUPFAMiSSF55874. SSF55874. 1 hit.
    SSF69012. SSF69012. 1 hit.
    PROSITEiPS50109. HIS_KIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q8BFP9-1 [UniParc]FASTAAdd to Basket

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    MRLARLLRGG TSVRPLCAVP CASRSLASAS ASGSGPASEL GVPGQVDFYA    50
    RFSPSPLSMK QFLDFGSVNA CEKTSFMFLR QELPVRLANI MKEISLLPDN 100
    LLRTPSVQLV QSWYIQSLQE LLDFKDKSAE DAKTIYEFTD TVIRIRNRHN 150
    DVIPTMAQGV TEYKESFGVD PVTSQNVQYF LDRFYMSRIS IRMLLNQHSL 200
    LFGGKGSPSH RKHIGSINPN CDVVEVIKDG YENARRLCDL YYVNSPELEL 250
    EELNAKSPGQ TIQVVYVPSH LYHMVFELFK NAMRATMEHH ADKGVYPPIQ 300
    VHVTLGEEDL TVKMSDRGGG VPLRKIDRLF NYMYSTAPRP RVETSRAVPL 350
    AGFGYGLPIS RLYAQYFQGD LKLYSLEGYG TDAVIYIKAL STESVERLPV 400
    YNKAAWKHYK ANHEADDWCV PSREPKDMTT FRSS 434
    Length:434
    Mass (Da):48,995
    Last modified:July 27, 2011 - v2
    Checksum:i8A514C863E751040
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti324 – 3241R → S in BAC32879. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK046805 mRNA. Translation: BAC32879.1.
    AK153649 mRNA. Translation: BAE32134.1.
    AL928963 Genomic DNA. Translation: CAM26372.1.
    CH466519 Genomic DNA. Translation: EDL27100.1.
    CH466519 Genomic DNA. Translation: EDL27102.1.
    CH466519 Genomic DNA. Translation: EDL27104.1.
    CCDSiCCDS16119.1.
    RefSeqiNP_766253.2. NM_172665.5.
    UniGeneiMm.34411.

    Genome annotation databases

    EnsembliENSMUST00000006669; ENSMUSP00000006669; ENSMUSG00000006494.
    GeneIDi228026.
    KEGGimmu:228026.
    UCSCiuc008kbh.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK046805 mRNA. Translation: BAC32879.1 .
    AK153649 mRNA. Translation: BAE32134.1 .
    AL928963 Genomic DNA. Translation: CAM26372.1 .
    CH466519 Genomic DNA. Translation: EDL27100.1 .
    CH466519 Genomic DNA. Translation: EDL27102.1 .
    CH466519 Genomic DNA. Translation: EDL27104.1 .
    CCDSi CCDS16119.1.
    RefSeqi NP_766253.2. NM_172665.5.
    UniGenei Mm.34411.

    3D structure databases

    ProteinModelPortali Q8BFP9.
    SMRi Q8BFP9. Positions 41-421.
    ModBasei Search...
    MobiDBi Search...

    PTM databases

    PhosphoSitei Q8BFP9.

    Proteomic databases

    MaxQBi Q8BFP9.
    PaxDbi Q8BFP9.
    PRIDEi Q8BFP9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000006669 ; ENSMUSP00000006669 ; ENSMUSG00000006494 .
    GeneIDi 228026.
    KEGGi mmu:228026.
    UCSCi uc008kbh.1. mouse.

    Organism-specific databases

    CTDi 5163.
    MGIi MGI:1926119. Pdk1.

    Phylogenomic databases

    eggNOGi COG0642.
    GeneTreei ENSGT00550000074574.
    HOGENOMi HOG000164315.
    HOVERGENi HBG000511.
    InParanoidi Q3U5E5.
    KOi K12077.
    OMAi EDAKTIY.
    OrthoDBi EOG71VSSV.
    TreeFami TF314918.

    Enzyme and pathway databases

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

    Miscellaneous databases

    ChiTaRSi Pdk1. mouse.
    NextBioi 378903.
    PROi Q8BFP9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8BFP9.
    Bgeei Q8BFP9.
    CleanExi MM_PDK1.
    Genevestigatori Q8BFP9.

    Family and domain databases

    Gene3Di 1.20.140.20. 1 hit.
    3.30.565.10. 1 hit.
    InterProi IPR018955. BCDHK/PDK_N.
    IPR003594. HATPase_ATP-bd.
    IPR005467. Sig_transdc_His_kinase_core.
    [Graphical view ]
    Pfami PF10436. BCDHK_Adom3. 1 hit.
    PF02518. HATPase_c. 1 hit.
    [Graphical view ]
    SMARTi SM00387. HATPase_c. 1 hit.
    [Graphical view ]
    SUPFAMi SSF55874. SSF55874. 1 hit.
    SSF69012. SSF69012. 1 hit.
    PROSITEi PS50109. HIS_KIN. 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: Medulla oblongata and Thymus.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "Regulation of PDK mRNA by high fatty acid and glucose in pancreatic islets."
      Xu J., Han J., Epstein P.N., Liu Y.Q.
      Biochem. Biophys. Res. Commun. 344:827-833(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION BY PALMITATE AND GLUCOSE.
    5. "HIF-1 mediates adaptation to hypoxia by actively downregulating mitochondrial oxygen consumption."
      Papandreou I., Cairns R.A., Fontana L., Lim A.L., Denko N.C.
      Cell Metab. 3:187-197(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION BY HYPOXIA, FUNCTION.
    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-403, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.

    Entry informationi

    Entry nameiPDK1_MOUSE
    AccessioniPrimary (citable) accession number: Q8BFP9
    Secondary accession number(s): Q3U5E5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 15, 2005
    Last sequence update: July 27, 2011
    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, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3