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Q15120

- PDK3_HUMAN

UniProt

Q15120 - PDK3_HUMAN

Protein

[Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 3, mitochondrial

Gene

PDK3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 148 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Inhibits pyruvate dehydrogenase activity by phosphorylation of the E1 subunit PDHA1, and thereby regulates glucose metabolism and aerobic respiration. Can also phosphorylate PDHA2. Decreases glucose utilization and increases fat metabolism in response to prolonged fasting, and as adaptation to a high-fat diet. Plays a role in glucose homeostasis and in maintaining normal blood glucose levels in function of nutrient levels and under starvation. Plays a role in the generation of reactive oxygen species.7 Publications

    Catalytic activityi

    ATP + [pyruvate dehydrogenase (acetyl-transferring)] = ADP + [pyruvate dehydrogenase (acetyl-transferring)] phosphate.3 Publications

    Enzyme regulationi

    Activated by interaction with DLAT. Inhibited by AZD7545, dichloroacetate and radicicol.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei287 – 2871ATP1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi247 – 2548ATP1 Publication
    Nucleotide bindingi306 – 3072ATP1 Publication
    Nucleotide bindingi323 – 3286ATP1 Publication

    GO - Molecular functioni

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

    GO - Biological processi

    1. cell death Source: UniProtKB-KW
    2. cellular metabolic process Source: Reactome
    3. cellular response to fatty acid Source: UniProtKB
    4. cellular response to glucose stimulus Source: UniProtKB
    5. glucose metabolic process Source: UniProtKB-KW
    6. hypoxia-inducible factor-1alpha signaling pathway Source: UniProtKB
    7. peptidyl-serine phosphorylation Source: UniProtKB
    8. peroxisome proliferator activated receptor signaling pathway Source: UniProtKB
    9. pyruvate metabolic process Source: Reactome
    10. regulation of acetyl-CoA biosynthetic process from pyruvate Source: UniProtKB
    11. regulation of glucose metabolic process Source: UniProtKB
    12. regulation of reactive oxygen species metabolic process Source: UniProtKB
    13. small molecule metabolic process Source: Reactome

    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_12528. Regulation of pyruvate dehydrogenase (PDH) complex.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    [Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 3, mitochondrial (EC:2.7.11.2)
    Alternative name(s):
    Pyruvate dehydrogenase kinase isoform 3
    Gene namesi
    Name:PDK3
    Synonyms:PDHK3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:8811. PDK3.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrial matrix Source: Reactome
    2. mitochondrion Source: ProtInc

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Involvement in diseasei

    Charcot-Marie-Tooth disease, X-linked dominant, 6 (CMTX6) [MIM:300905]: A form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies characterized by severely reduced motor nerve conduction velocities (NCVs) (less than 38m/s) and segmental demyelination and remyelination, and primary peripheral axonal neuropathies characterized by normal or mildly reduced NCVs and chronic axonal degeneration and regeneration on nerve biopsy.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti158 – 1581R → H in CMTX6; gain of function; results in a 5-fold increase in kinase activity, decreased sensitivity to pyruvate inhibition, reduced affinity for nucleotides and increased affinity for pyruvate dehydrogenase complex component E2 (PDC-E2), leading to PDC hyperphosphorylation and increased inactivation. 1 Publication
    VAR_070082

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi120 – 1201N → H: No effect on kinase activity; when associated with N-121. 1 Publication
    Mutagenesisi121 – 1211D → N: No effect on kinase activity; when associated with H-120. 1 Publication

    Keywords - Diseasei

    Charcot-Marie-Tooth disease, Disease mutation, Neurodegeneration, Neuropathy

    Organism-specific databases

    MIMi300905. phenotype.
    Orphaneti352675. X-linked Charcot-Marie-Tooth disease type 6.
    PharmGKBiPA33156.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini? – 406[Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 3, mitochondrialPRO_0000023443
    Transit peptidei1 – ?MitochondrionSequence Analysis

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei278 – 2781N6-succinyllysineBy similarity

    Proteomic databases

    MaxQBiQ15120.
    PaxDbiQ15120.
    PRIDEiQ15120.

    PTM databases

    PhosphoSiteiQ15120.

    Expressioni

    Tissue specificityi

    Expressed in heart, skeletal muscle, spinal cord, as well as fetal and adult brain.1 Publication

    Inductioni

    Up-regulated in response to hypoxia. Up-regulated in response to fatty acids. Up-regulated by PPARD.3 Publications

    Gene expression databases

    BgeeiQ15120.
    CleanExiHS_PDK3.
    GenevestigatoriQ15120.

    Organism-specific databases

    HPAiHPA046583.

    Interactioni

    Subunit structurei

    Homodimer. 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).5 Publications

    Protein-protein interaction databases

    BioGridi111191. 8 interactions.
    DIPiDIP-29498N.
    IntActiQ15120. 2 interactions.
    STRINGi9606.ENSP00000387536.

    Structurei

    Secondary structure

    1
    406
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi14 – 218
    Helixi29 – 3810
    Helixi42 – 6423
    Helixi69 – 724
    Helixi75 – 9218
    Helixi93 – 964
    Beta strandi99 – 1013
    Helixi102 – 11817
    Helixi119 – 1213
    Helixi122 – 13716
    Helixi141 – 17232
    Beta strandi179 – 1846
    Beta strandi187 – 1926
    Helixi193 – 21220
    Beta strandi218 – 2247
    Beta strandi233 – 2364
    Helixi238 – 26023
    Beta strandi262 – 2654
    Beta strandi270 – 2767
    Beta strandi278 – 28710
    Helixi294 – 2974
    Helixi298 – 3014
    Turni303 – 3053
    Beta strandi323 – 3253
    Helixi327 – 33711
    Beta strandi341 – 3477
    Turni348 – 3503
    Beta strandi351 – 36010
    Helixi362 – 3643
    Helixi374 – 3807

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1Y8NX-ray2.60A9-406[»]
    1Y8OX-ray2.48A9-406[»]
    1Y8PX-ray2.63A9-406[»]
    2PNRX-ray2.50A/B/E/F9-406[»]
    2Q8IX-ray2.60A9-406[»]
    ProteinModelPortaliQ15120.
    SMRiQ15120. Positions 12-401.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ15120.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini131 – 362232Histidine 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.
    HOGENOMiHOG000164315.
    HOVERGENiHBG000511.
    InParanoidiQ15120.
    KOiK00898.
    OMAiDPHVLDD.
    OrthoDBiEOG71VSSV.
    PhylomeDBiQ15120.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q15120-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MRLFRWLLKQ PVPKQIERYS RFSPSPLSIK QFLDFGRDNA CEKTSYMFLR    50
    KELPVRLANT MREVNLLPDN LLNRPSVGLV QSWYMQSFLE LLEYENKSPE 100
    DPQVLDNFLQ VLIKVRNRHN DVVPTMAQGV IEYKEKFGFD PFISTNIQYF 150
    LDRFYTNRIS FRMLINQHTL LFGGDTNPVH PKHIGSIDPT CNVADVVKDA 200
    YETAKMLCEQ YYLVAPELEV EEFNAKAPDK PIQVVYVPSH LFHMLFELFK 250
    NSMRATVELY EDRKEGYPAV KTLVTLGKED LSIKISDLGG GVPLRKIDRL 300
    FNYMYSTAPR PSLEPTRAAP LAGFGYGLPI SRLYARYFQG DLKLYSMEGV 350
    GTDAVIYLKA LSSESFERLP VFNKSAWRHY KTTPEADDWS NPSSEPRDAS 400
    KYKAKQ 406
    Length:406
    Mass (Da):46,939
    Last modified:November 1, 1996 - v1
    Checksum:iEF2415D3F9D8D61E
    GO
    Isoform 2 (identifier: Q15120-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         406-406: Q → QDKIKTNRTF

    Note: No experimental confirmation available.

    Show »
    Length:415
    Mass (Da):48,043
    Checksum:iBDE814D88CE6A279
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti114 – 1141K → T.1 Publication
    Corresponds to variant rs146331370 [ dbSNP | Ensembl ].
    VAR_070081
    Natural varianti158 – 1581R → H in CMTX6; gain of function; results in a 5-fold increase in kinase activity, decreased sensitivity to pyruvate inhibition, reduced affinity for nucleotides and increased affinity for pyruvate dehydrogenase complex component E2 (PDC-E2), leading to PDC hyperphosphorylation and increased inactivation. 1 Publication
    VAR_070082
    Natural varianti219 – 2191E → A in a head & neck squamous cell carcinoma sample; somatic mutation. 1 Publication
    VAR_042297
    Natural varianti334 – 3341Y → S.1 Publication
    VAR_070083

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei406 – 4061Q → QDKIKTNRTF in isoform 2. 1 PublicationVSP_043365

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L42452 mRNA. Translation: AAC42011.1.
    AK301965 mRNA. Translation: BAG63378.1.
    CH471074 Genomic DNA. Translation: EAW99019.1.
    BC015948 mRNA. Translation: AAH15948.1.
    CCDSiCCDS14212.1. [Q15120-1]
    CCDS48088.1. [Q15120-2]
    PIRiI70160.
    RefSeqiNP_001135858.1. NM_001142386.2. [Q15120-2]
    NP_005382.1. NM_005391.4. [Q15120-1]
    UniGeneiHs.296031.

    Genome annotation databases

    EnsembliENST00000379162; ENSP00000368460; ENSG00000067992. [Q15120-1]
    ENST00000441463; ENSP00000387536; ENSG00000067992. [Q15120-2]
    GeneIDi5165.
    KEGGihsa:5165.
    UCSCiuc004dbg.3. human. [Q15120-1]
    uc004dbh.3. human. [Q15120-2]

    Polymorphism databases

    DMDMi3183119.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L42452 mRNA. Translation: AAC42011.1 .
    AK301965 mRNA. Translation: BAG63378.1 .
    CH471074 Genomic DNA. Translation: EAW99019.1 .
    BC015948 mRNA. Translation: AAH15948.1 .
    CCDSi CCDS14212.1. [Q15120-1 ]
    CCDS48088.1. [Q15120-2 ]
    PIRi I70160.
    RefSeqi NP_001135858.1. NM_001142386.2. [Q15120-2 ]
    NP_005382.1. NM_005391.4. [Q15120-1 ]
    UniGenei Hs.296031.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1Y8N X-ray 2.60 A 9-406 [» ]
    1Y8O X-ray 2.48 A 9-406 [» ]
    1Y8P X-ray 2.63 A 9-406 [» ]
    2PNR X-ray 2.50 A/B/E/F 9-406 [» ]
    2Q8I X-ray 2.60 A 9-406 [» ]
    ProteinModelPortali Q15120.
    SMRi Q15120. Positions 12-401.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111191. 8 interactions.
    DIPi DIP-29498N.
    IntActi Q15120. 2 interactions.
    STRINGi 9606.ENSP00000387536.

    Chemistry

    BindingDBi Q15120.
    ChEMBLi CHEMBL2096665.

    PTM databases

    PhosphoSitei Q15120.

    Polymorphism databases

    DMDMi 3183119.

    Proteomic databases

    MaxQBi Q15120.
    PaxDbi Q15120.
    PRIDEi Q15120.

    Protocols and materials databases

    DNASUi 5165.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000379162 ; ENSP00000368460 ; ENSG00000067992 . [Q15120-1 ]
    ENST00000441463 ; ENSP00000387536 ; ENSG00000067992 . [Q15120-2 ]
    GeneIDi 5165.
    KEGGi hsa:5165.
    UCSCi uc004dbg.3. human. [Q15120-1 ]
    uc004dbh.3. human. [Q15120-2 ]

    Organism-specific databases

    CTDi 5165.
    GeneCardsi GC0XP024393.
    HGNCi HGNC:8811. PDK3.
    HPAi HPA046583.
    MIMi 300905. phenotype.
    300906. gene.
    neXtProti NX_Q15120.
    Orphaneti 352675. X-linked Charcot-Marie-Tooth disease type 6.
    PharmGKBi PA33156.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0642.
    HOGENOMi HOG000164315.
    HOVERGENi HBG000511.
    InParanoidi Q15120.
    KOi K00898.
    OMAi DPHVLDD.
    OrthoDBi EOG71VSSV.
    PhylomeDBi Q15120.
    TreeFami TF314918.

    Enzyme and pathway databases

    Reactomei REACT_12528. Regulation of pyruvate dehydrogenase (PDH) complex.

    Miscellaneous databases

    EvolutionaryTracei Q15120.
    GeneWikii PDK3.
    GenomeRNAii 5165.
    NextBioi 19982.
    PROi Q15120.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q15120.
    CleanExi HS_PDK3.
    Genevestigatori Q15120.

    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. "Diversity of the pyruvate dehydrogenase kinase gene family in humans."
      Gudi R., Bowker-Kinley M.M., Kedishvili N.Y., Zhao Y., Popov K.M.
      J. Biol. Chem. 270:28989-28994(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Liver.
    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.-O., 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 [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Testis.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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] (ISOFORM 1).
      Tissue: Skin.
    5. "Marked differences between two isoforms of human pyruvate dehydrogenase kinase."
      Baker J.C., Yan X., Peng T., Kasten S., Roche T.E.
      J. Biol. Chem. 275:15773-15781(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, FUNCTION, INTERACTION WITH DLAT, ENZYME REGULATION.
    6. "Site specificity of four pyruvate dehydrogenase kinase isoenzymes toward the three phosphorylation sites of human pyruvate dehydrogenase."
      Korotchkina L.G., Patel M.S.
      J. Biol. Chem. 276:37223-37229(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, FUNCTION.
    7. "Interaction between the individual isoenzymes of pyruvate dehydrogenase kinase and the inner lipoyl-bearing domain of transacetylase component of pyruvate dehydrogenase complex."
      Tuganova A., Boulatnikov I., Popov K.M.
      Biochem. J. 366:129-136(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DLAT.
    8. "Characterization of testis-specific isoenzyme of human pyruvate dehydrogenase."
      Korotchkina L.G., Sidhu S., Patel M.S.
      J. Biol. Chem. 281:9688-9696(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, FUNCTION.
    9. "Three members of the human pyruvate dehydrogenase kinase gene family are direct targets of the peroxisome proliferator-activated receptor beta/delta."
      Degenhardt T., Saramaki A., Malinen M., Rieck M., Vaisanen S., Huotari A., Herzig K.H., Muller R., Carlberg C.
      J. Mol. Biol. 372:341-355(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION BY PPARD.
    10. "Induction of pyruvate dehydrogenase kinase-3 by hypoxia-inducible factor-1 promotes metabolic switch and drug resistance."
      Lu C.W., Lin S.C., Chen K.F., Lai Y.Y., Tsai S.J.
      J. Biol. Chem. 283:28106-28114(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INDUCTION.
    11. "Butyrate elicits a metabolic switch in human colon cancer cells by targeting the pyruvate dehydrogenase complex."
      Blouin J.M., Penot G., Collinet M., Nacfer M., Forest C., Laurent-Puig P., Coumoul X., Barouki R., Benelli C., Bortoli S.
      Int. J. Cancer 128:2591-2601(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    12. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Inactivation of the HIF-1alpha/PDK3 signaling axis drives melanoma toward mitochondrial oxidative metabolism and potentiates the therapeutic activity of pro-oxidants."
      Kluza J., Corazao-Rozas P., Touil Y., Jendoubi M., Maire C., Guerreschi P., Jonneaux A., Ballot C., Balayssac S., Valable S., Corroyer-Dulmont A., Bernaudin M., Malet-Martino M., de Lassalle E.M., Maboudou P., Formstecher P., Polakowska R., Mortier L., Marchetti P.
      Cancer Res. 72:5035-5047(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    14. "Crystal structure of pyruvate dehydrogenase kinase 3 bound to lipoyl domain 2 of human pyruvate dehydrogenase complex."
      Kato M., Chuang J.L., Tso S.C., Wynn R.M., Chuang D.T.
      EMBO J. 24:1763-1774(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.48 ANGSTROMS) OF 9-406 IN COMPLEX WITH ATP, FUNCTION, INTERACTION WITH DLAT.
    15. "Crystal structure of an asymmetric complex of pyruvate dehydrogenase kinase 3 with lipoyl domain 2 and its biological implications."
      Devedjiev Y., Steussy C.N., Vassylyev D.G.
      J. Mol. Biol. 370:407-416(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 9-406, INTERACTION WITH DLAT.
    16. "Distinct structural mechanisms for inhibition of pyruvate dehydrogenase kinase isoforms by AZD7545, dichloroacetate, and radicicol."
      Kato M., Li J., Chuang J.L., Chuang D.T.
      Structure 15:992-1004(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 9-406 IN COMPLEX WITH THE INHIBITOR RADICICOL, FUNCTION, ENZYME REGULATION, INTERACTION WITH DLAT.
    17. "Patterns of somatic mutation in human cancer genomes."
      Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
      , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
      Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT [LARGE SCALE ANALYSIS] ALA-219.
    18. "A new locus for X-linked dominant Charcot-Marie-Tooth disease (CMTX6) is caused by mutations in the pyruvate dehydrogenase kinase isoenzyme 3 (PDK3) gene."
      Kennerson M.L., Yiu E.M., Chuang D.T., Kidambi A., Tso S.C., Ly C., Chaudhry R., Drew A.P., Rance G., Delatycki M.B., Zuchner S., Ryan M.M., Nicholson G.A.
      Hum. Mol. Genet. 22:1404-1416(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CMTX6 HIS-158, VARIANTS THR-114 AND SER-334, CHARACTERIZATION OF VARIANT CMTX6 HIS-158, TISSUE SPECIFICITY, MUTAGENESIS OF ASN-120 AND ASP-121.

    Entry informationi

    Entry nameiPDK3_HUMAN
    AccessioniPrimary (citable) accession number: Q15120
    Secondary accession number(s): B4DXG6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 148 of the entry and version 1 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3