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Q15119

- PDK2_HUMAN

UniProt

Q15119 - PDK2_HUMAN

Protein

[Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 2, mitochondrial

Gene

PDK2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 143 (01 Oct 2014)
      Sequence version 2 (06 Jun 2002)
      Previous versions | rss
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    Functioni

    Serine/threonine kinase that plays a key role in the 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. Inhibition of pyruvate dehydrogenase decreases glucose utilization and increases fat metabolism. Mediates cellular responses to insulin. Plays an important role in maintaining normal blood glucose levels and in metabolic adaptation to nutrient availability. Via its regulation of pyruvate dehydrogenase activity, plays an important role in maintaining normal blood pH and in preventing the accumulation of ketone bodies under starvation. Plays a role in the regulation of cell proliferation and in resistance to apoptosis under oxidative stress. Plays a role in p53/TP53-mediated apoptosis.6 Publications

    Catalytic activityi

    ATP + [pyruvate dehydrogenase (acetyl-transferring)] = ADP + [pyruvate dehydrogenase (acetyl-transferring)] phosphate.4 Publications

    Enzyme regulationi

    Activity is enhanced by binding to the pyruvate dehydrogenase subunit DLAT. Inhibited by ADP and pyruvate; these compounds interfere with DLAT binding and thereby inhibit kinase activity. Inhibited by dichloroacetate. Inhibited by AZD7545; this compound interferes with DLAT binding and thereby inhibits kinase activity.3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei290 – 2901ATP1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi251 – 2588ATP1 Publication
    Nucleotide bindingi309 – 3102ATPBy similarity
    Nucleotide bindingi325 – 3306ATP1 Publication

    GO - Molecular functioni

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

    GO - Biological processi

    1. cellular metabolic process Source: Reactome
    2. cellular response to nutrient Source: UniProtKB
    3. cellular response to reactive oxygen species Source: UniProtKB
    4. glucose homeostasis Source: UniProtKB
    5. glucose metabolic process Source: ProtInc
    6. insulin receptor signaling pathway Source: UniProtKB
    7. intrinsic apoptotic signaling pathway by p53 class mediator Source: UniProtKB
    8. protein phosphorylation Source: GOC
    9. pyruvate metabolic process Source: Reactome
    10. regulation of acetyl-CoA biosynthetic process from pyruvate Source: UniProtKB
    11. regulation of cellular ketone metabolic process Source: UniProtKB
    12. regulation of gluconeogenesis Source: UniProtKB
    13. regulation of glucose metabolic process Source: UniProtKB
    14. regulation of pH Source: UniProtKB
    15. 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.
    SignaLinkiQ15119.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    [Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 2, mitochondrial (EC:2.7.11.2)
    Alternative name(s):
    Pyruvate dehydrogenase kinase isoform 2
    Short name:
    PDH kinase 2
    Short name:
    PDKII
    Gene namesi
    Name:PDK2
    Synonyms:PDHK2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:8810. PDK2.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrial matrix Source: Reactome
    2. mitochondrial pyruvate dehydrogenase complex Source: UniProtKB

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33155.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini? – 407[Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 2, mitochondrialPRO_0000023440
    Transit peptidei1 – ?MitochondrionSequence Analysis

    Proteomic databases

    MaxQBiQ15119.
    PaxDbiQ15119.
    PRIDEiQ15119.

    Expressioni

    Tissue specificityi

    Expressed in many tissues, with the highest level in heart and skeletal muscle, intermediate levels in brain, kidney, pancreas and liver, and low levels in placenta and lung.1 Publication

    Inductioni

    Down-regulated by insulin. Up-regulated by reactive oxygen species and cigarette smoke extract. Up-regulated by PPARD.3 Publications

    Gene expression databases

    ArrayExpressiQ15119.
    BgeeiQ15119.
    CleanExiHS_PDK2.
    GenevestigatoriQ15119.

    Organism-specific databases

    HPAiHPA008287.

    Interactioni

    Subunit structurei

    Homodimer, and heterodimer with PDK1. 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

    BioGridi111190. 5 interactions.
    IntActiQ15119. 6 interactions.
    MINTiMINT-1379180.
    STRINGi9606.ENSP00000007708.

    Structurei

    Secondary structure

    1
    407
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi16 – 238
    Helixi33 – 375
    Helixi43 – 6826
    Helixi73 – 764
    Helixi79 – 9618
    Turni97 – 1004
    Helixi106 – 12217
    Turni123 – 1253
    Helixi126 – 14116
    Helixi145 – 17531
    Beta strandi177 – 1793
    Beta strandi191 – 1966
    Helixi197 – 21620
    Beta strandi222 – 2309
    Beta strandi237 – 2404
    Helixi242 – 26221
    Turni263 – 2664
    Beta strandi273 – 2797
    Beta strandi281 – 29010
    Helixi297 – 2993
    Helixi301 – 3044
    Turni306 – 3094
    Helixi329 – 33911
    Beta strandi343 – 3497
    Turni350 – 3523
    Beta strandi353 – 36311
    Turni364 – 3663
    Helixi376 – 3816

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2BTZX-ray2.20A16-407[»]
    2BU2X-ray2.40A16-407[»]
    2BU5X-ray2.35A16-407[»]
    2BU6X-ray2.40A16-407[»]
    2BU7X-ray2.40A16-407[»]
    2BU8X-ray2.50A16-407[»]
    4MP2X-ray1.75A9-407[»]
    4MP7X-ray1.80A9-407[»]
    4MPCX-ray1.70A9-407[»]
    4MPEX-ray1.95A9-407[»]
    4MPNX-ray1.75A9-407[»]
    ProteinModelPortaliQ15119.
    SMRiQ15119. Positions 16-383.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ15119.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini135 – 364230Histidine 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.
    InParanoidiQ15119.
    KOiK00898.
    OMAiNLFSYMY.
    OrthoDBiEOG71VSSV.
    PhylomeDBiQ15119.
    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: Q15119-1) [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

    MRWVWALLKN ASLAGAPKYI EHFSKFSPSP LSMKQFLDFG SSNACEKTSF    50
    TFLRQELPVR LANIMKEINL LPDRVLSTPS VQLVQSWYVQ SLLDIMEFLD 100
    KDPEDHRTLS QFTDALVTIR NRHNDVVPTM AQGVLEYKDT YGDDPVSNQN 150
    IQYFLDRFYL SRISIRMLIN QHTLIFDGST NPAHPKHIGS IDPNCNVSEV 200
    VKDAYDMAKL LCDKYYMASP DLEIQEINAA NSKQPIHMVY VPSHLYHMLF 250
    ELFKNAMRAT VESHESSLIL PPIKVMVALG EEDLSIKMSD RGGGVPLRKI 300
    ERLFSYMYST APTPQPGTGG TPLAGFGYGL PISRLYAKYF QGDLQLFSME 350
    GFGTDAVIYL KALSTDSVER LPVYNKSAWR HYQTIQEAGD WCVPSTEPKN 400
    TSTYRVS 407
    Length:407
    Mass (Da):46,154
    Last modified:June 6, 2002 - v2
    Checksum:i77DBA03EF922EF03
    GO
    Isoform 2 (identifier: Q15119-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-64: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:343
    Mass (Da):38,864
    Checksum:i27A955EC48BCA113
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti80 – 801S → T in AAC42010. (PubMed:7499431)Curated
    Sequence conflicti407 – 4071S → T in AAC42010. (PubMed:7499431)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti342 – 3421G → R in a glioblastoma multiforme sample; somatic mutation. 2 Publications
    Corresponds to variant rs17855787 [ dbSNP | Ensembl ].
    VAR_042296

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 6464Missing in isoform 2. 1 PublicationVSP_042549Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L42451 mRNA. Translation: AAC42010.1.
    AK055119 mRNA. Translation: BAG51472.1.
    AK290522 mRNA. Translation: BAF83211.1.
    AC002401 Genomic DNA. No translation available.
    CH471109 Genomic DNA. Translation: EAW94642.1.
    CH471109 Genomic DNA. Translation: EAW94644.1.
    BC005811 mRNA. Translation: AAH05811.1.
    BC040478 mRNA. Translation: AAH40478.1.
    BC063137 mRNA. Translation: AAH63137.1.
    CCDSiCCDS11559.1. [Q15119-1]
    CCDS56039.1. [Q15119-2]
    PIRiI70159.
    RefSeqiNP_001186827.1. NM_001199898.1. [Q15119-2]
    NP_001186828.1. NM_001199899.1. [Q15119-2]
    NP_002602.2. NM_002611.4. [Q15119-1]
    UniGeneiHs.256667.

    Genome annotation databases

    EnsembliENST00000007708; ENSP00000007708; ENSG00000005882. [Q15119-2]
    ENST00000503176; ENSP00000420927; ENSG00000005882. [Q15119-1]
    GeneIDi5164.
    KEGGihsa:5164.
    UCSCiuc002iqb.3. human. [Q15119-1]

    Polymorphism databases

    DMDMi21431820.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L42451 mRNA. Translation: AAC42010.1 .
    AK055119 mRNA. Translation: BAG51472.1 .
    AK290522 mRNA. Translation: BAF83211.1 .
    AC002401 Genomic DNA. No translation available.
    CH471109 Genomic DNA. Translation: EAW94642.1 .
    CH471109 Genomic DNA. Translation: EAW94644.1 .
    BC005811 mRNA. Translation: AAH05811.1 .
    BC040478 mRNA. Translation: AAH40478.1 .
    BC063137 mRNA. Translation: AAH63137.1 .
    CCDSi CCDS11559.1. [Q15119-1 ]
    CCDS56039.1. [Q15119-2 ]
    PIRi I70159.
    RefSeqi NP_001186827.1. NM_001199898.1. [Q15119-2 ]
    NP_001186828.1. NM_001199899.1. [Q15119-2 ]
    NP_002602.2. NM_002611.4. [Q15119-1 ]
    UniGenei Hs.256667.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2BTZ X-ray 2.20 A 16-407 [» ]
    2BU2 X-ray 2.40 A 16-407 [» ]
    2BU5 X-ray 2.35 A 16-407 [» ]
    2BU6 X-ray 2.40 A 16-407 [» ]
    2BU7 X-ray 2.40 A 16-407 [» ]
    2BU8 X-ray 2.50 A 16-407 [» ]
    4MP2 X-ray 1.75 A 9-407 [» ]
    4MP7 X-ray 1.80 A 9-407 [» ]
    4MPC X-ray 1.70 A 9-407 [» ]
    4MPE X-ray 1.95 A 9-407 [» ]
    4MPN X-ray 1.75 A 9-407 [» ]
    ProteinModelPortali Q15119.
    SMRi Q15119. Positions 16-383.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111190. 5 interactions.
    IntActi Q15119. 6 interactions.
    MINTi MINT-1379180.
    STRINGi 9606.ENSP00000007708.

    Chemistry

    BindingDBi Q15119.
    ChEMBLi CHEMBL2096665.

    Polymorphism databases

    DMDMi 21431820.

    Proteomic databases

    MaxQBi Q15119.
    PaxDbi Q15119.
    PRIDEi Q15119.

    Protocols and materials databases

    DNASUi 5164.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000007708 ; ENSP00000007708 ; ENSG00000005882 . [Q15119-2 ]
    ENST00000503176 ; ENSP00000420927 ; ENSG00000005882 . [Q15119-1 ]
    GeneIDi 5164.
    KEGGi hsa:5164.
    UCSCi uc002iqb.3. human. [Q15119-1 ]

    Organism-specific databases

    CTDi 5164.
    GeneCardsi GC17P048172.
    HGNCi HGNC:8810. PDK2.
    HPAi HPA008287.
    MIMi 602525. gene.
    neXtProti NX_Q15119.
    PharmGKBi PA33155.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0642.
    HOGENOMi HOG000164315.
    HOVERGENi HBG000511.
    InParanoidi Q15119.
    KOi K00898.
    OMAi NLFSYMY.
    OrthoDBi EOG71VSSV.
    PhylomeDBi Q15119.
    TreeFami TF314918.

    Enzyme and pathway databases

    Reactomei REACT_12528. Regulation of pyruvate dehydrogenase (PDH) complex.
    SignaLinki Q15119.

    Miscellaneous databases

    ChiTaRSi PDK2. human.
    EvolutionaryTracei Q15119.
    GeneWikii PDK2.
    GenomeRNAii 5164.
    NextBioi 19978.
    PROi Q15119.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q15119.
    Bgeei Q15119.
    CleanExi HS_PDK2.
    Genevestigatori Q15119.

    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), FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY.
      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] (ISOFORMS 1 AND 2).
      Tissue: Brain.
    3. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
      Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
      , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
      Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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), VARIANT ARG-342.
      Tissue: Lung, Prostate and Skin.
    6. "Insulin downregulates pyruvate dehydrogenase kinase (PDK) mRNA: potential mechanism contributing to increased lipid oxidation in insulin-resistant subjects."
      Majer M., Popov K.M., Harris R.A., Bogardus C., Prochazka M.
      Mol. Genet. Metab. 65:181-186(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION BY INSULIN, FUNCTION.
    7. "Facilitated interaction between the pyruvate dehydrogenase kinase isoform 2 and the dihydrolipoyl acetyltransferase."
      Hiromasa Y., Roche T.E.
      J. Biol. Chem. 278:33681-33693(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT, INTERACTION WITH DLAT.
    8. "Pyruvate dehydrogenase kinase isoform 2 activity limited and further inhibited by slowing down the rate of dissociation of ADP."
      Bao H., Kasten S.A., Yan X., Roche T.E.
      Biochemistry 43:13432-13441(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, SUBUNIT, ENZYME REGULATION.
    9. "Ligand-induced effects on pyruvate dehydrogenase kinase isoform 2."
      Hiromasa Y., Hu L., Roche T.E.
      J. Biol. Chem. 281:12568-12579(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, INTERACTION WITH DLAT, SUBUNIT, ENZYME REGULATION.
    10. "A mitochondria-K+ channel axis is suppressed in cancer and its normalization promotes apoptosis and inhibits cancer growth."
      Bonnet S., Archer S.L., Allalunis-Turner J., Haromy A., Beaulieu C., Thompson R., Lee C.T., Lopaschuk G.D., Puttagunta L., Bonnet S., Harry G., Hashimoto K., Porter C.J., Andrade M.A., Thebaud B., Michelakis E.D.
      Cancer Cell 11:37-51(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. "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.
    12. "Pivotal role of the C-terminal DW-motif in mediating inhibition of pyruvate dehydrogenase kinase 2 by dichloroacetate."
      Li J., Kato M., Chuang D.T.
      J. Biol. Chem. 284:34458-34467(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, FUNCTION, ENZYME REGULATION, INTERACTION WITH DLAT, SUBUNIT.
    13. "Chronic CSE treatment induces the growth of normal oral keratinocytes via PDK2 upregulation, increased glycolysis and HIF1alpha stabilization."
      Sun W., Chang S.S., Fu Y., Liu Y., Califano J.A.
      PLoS ONE 6:E16207-E16207(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INDUCTION BY CIGARETTE SMOKE EXTRACT AND REACTIVE OXYGEN SPECIES.
    14. "p53 negatively regulates transcription of the pyruvate dehydrogenase kinase Pdk2."
      Contractor T., Harris C.R.
      Cancer Res. 72:560-567(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    15. "Regulatory roles of the N-terminal domain based on crystal structures of human pyruvate dehydrogenase kinase 2 containing physiological and synthetic ligands."
      Knoechel T.R., Tucker A.D., Robinson C.M., Phillips C., Taylor W., Bungay P.J., Kasten S.A., Roche T.E., Brown D.G.
      Biochemistry 45:402-415(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 16-407 IN COMPLEX WITH ATP AND THE INHIBITORS AZD7545; NOV3R; PFZ3 AND DICHLOROACETATE.
    16. "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] ARG-342.

    Entry informationi

    Entry nameiPDK2_HUMAN
    AccessioniPrimary (citable) accession number: Q15119
    Secondary accession number(s): A8K3A7
    , B3KNW0, Q6P515, Q9BS05
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: June 6, 2002
    Last modified: October 1, 2014
    This is version 143 of the entry and version 2 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 17
      Human chromosome 17: 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