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Q15118

- PDK1_HUMAN

UniProt

Q15118 - PDK1_HUMAN

Protein

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

Gene

PDK1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 136 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      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.4 Publications

    Catalytic activityi

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

    Enzyme regulationi

    Activity is enhanced by binding to the pyruvate dehydrogenase subunit DLAT. Inhibited by AZD7545; this compound interferes with DLAT binding and thereby inhibits kinase activity. Inhibited by dichloroacetate and radicicol.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei318 – 3181ATPBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi279 – 2868ATPBy similarity
    Nucleotide bindingi337 – 3382ATPBy similarity
    Nucleotide bindingi354 – 3596ATPBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. cell proliferation Source: UniProtKB
    2. cellular metabolic process Source: Reactome
    3. glucose metabolic process Source: ProtInc
    4. hypoxia-inducible factor-1alpha signaling pathway Source: UniProtKB
    5. intrinsic apoptotic signaling pathway in response to oxidative stress Source: UniProtKB
    6. protein phosphorylation Source: GOC
    7. pyruvate metabolic process Source: Reactome
    8. regulation of acetyl-CoA biosynthetic process from pyruvate Source: Reactome
    9. regulation of glucose metabolic process Source: UniProtKB
    10. 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.
    SignaLinkiQ15118.

    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
    Synonyms:PDHK1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:8809. PDK1.

    Subcellular locationi

    Mitochondrion matrix 1 Publication

    GO - Cellular componenti

    1. mitochondrial matrix Source: Reactome
    2. mitochondrial pyruvate dehydrogenase complex Source: Ensembl
    3. mitochondrion Source: ProtInc

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33154.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 2828MitochondrionSequence AnalysisAdd
    BLAST
    Chaini29 – 436408[Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 1, mitochondrialPRO_0000023437Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei136 – 1361Phosphotyrosine; by FGFR11 Publication
    Modified residuei243 – 2431Phosphotyrosine; by FGFR1, ABL1, FLT3 and JAK21 Publication
    Modified residuei244 – 2441Phosphotyrosine; by FGFR11 Publication
    Modified residuei405 – 4051N6-succinyllysineBy similarity

    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-243 and Tyr-244 strongly increases kinase activity, while phosphorylation at Tyr-136 has a lesser effect.1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ15118.
    PaxDbiQ15118.
    PRIDEiQ15118.

    PTM databases

    PhosphoSiteiQ15118.

    Expressioni

    Tissue specificityi

    Expressed predominantly in the heart. Detected at lower levels in liver, skeletal muscle and pancreas.1 Publication

    Inductioni

    Up-regulated via the HIF1A signaling pathway in response to hypoxia.1 Publication

    Gene expression databases

    ArrayExpressiQ15118.
    BgeeiQ15118.
    CleanExiHS_PDK1.
    GenevestigatoriQ15118.

    Organism-specific databases

    HPAiCAB017554.
    HPA027376.

    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).1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PKN2Q165136EBI-7016221,EBI-2511350

    Protein-protein interaction databases

    BioGridi111189. 17 interactions.
    DIPiDIP-29497N.
    IntActiQ15118. 6 interactions.
    MINTiMINT-2881420.
    STRINGi9606.ENSP00000282077.

    Structurei

    Secondary structure

    1
    436
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi42 – 509
    Helixi59 – 679
    Helixi72 – 9423
    Helixi99 – 1024
    Helixi105 – 12218
    Beta strandi125 – 1273
    Helixi132 – 14817
    Turni149 – 1513
    Helixi152 – 16615
    Helixi171 – 20232
    Beta strandi219 – 2246
    Helixi225 – 24420
    Beta strandi250 – 25910
    Beta strandi265 – 2684
    Helixi270 – 29122
    Turni293 – 2953
    Beta strandi301 – 3077
    Beta strandi309 – 31810
    Helixi325 – 3284
    Helixi329 – 3324
    Turni334 – 3374
    Beta strandi352 – 3543
    Helixi358 – 36811
    Beta strandi372 – 3787
    Turni379 – 3813
    Beta strandi382 – 39211
    Turni393 – 3953
    Helixi405 – 4117

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2Q8FX-ray2.03A30-436[»]
    2Q8GX-ray1.90A30-436[»]
    2Q8HX-ray2.00A30-436[»]
    ProteinModelPortaliQ15118.
    SMRiQ15118. Positions 41-423.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ15118.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini163 – 393231Histidine 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.
    KOiK12077.
    OrthoDBiEOG71VSSV.
    PhylomeDBiQ15118.
    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: Q15118-1) [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

    MRLARLLRGA ALAGPGPGLR AAGFSRSFSS DSGSSPASER GVPGQVDFYA    50
    RFSPSPLSMK QFLDFGSVNA CEKTSFMFLR QELPVRLANI MKEISLLPDN 100
    LLRTPSVQLV QSWYIQSLQE LLDFKDKSAE DAKAIYDFTD TVIRIRNRHN 150
    DVIPTMAQGV IEYKESFGVD PVTSQNVQYF LDRFYMSRIS IRMLLNQHSL 200
    LFGGKGKGSP SHRKHIGSIN PNCNVLEVIK DGYENARRLC DLYYINSPEL 250
    ELEELNAKSP GQPIQVVYVP SHLYHMVFEL FKNAMRATME HHANRGVYPP 300
    IQVHVTLGNE DLTVKMSDRG GGVPLRKIDR LFNYMYSTAP RPRVETSRAV 350
    PLAGFGYGLP ISRLYAQYFQ GDLKLYSLEG YGTDAVIYIK ALSTDSIERL 400
    PVYNKAAWKH YNTNHEADDW CVPSREPKDM TTFRSA 436
    Length:436
    Mass (Da):49,244
    Last modified:November 1, 1996 - v1
    Checksum:iD14CD594E0EA45A2
    GO
    Isoform 2 (identifier: Q15118-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         137-137: D → ERPRRTWLQVSSLCCMACKMI

    Show »
    Length:456
    Mass (Da):51,623
    Checksum:i067A55C29B224B48
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti8 – 81R → L in ABB29979. 1 PublicationCurated
    Sequence conflicti96 – 961L → R in BAH14173. (PubMed:14702039)Curated
    Sequence conflicti363 – 3631R → C in ABB29979. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti134 – 1341A → T.
    Corresponds to variant rs35661499 [ dbSNP | Ensembl ].
    VAR_050477
    Natural varianti412 – 4121N → T.1 Publication
    Corresponds to variant rs34250425 [ dbSNP | Ensembl ].
    VAR_042295

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei137 – 1371D → ERPRRTWLQVSSLCCMACKM I in isoform 2. 2 PublicationsVSP_055172

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L42450 mRNA. Translation: AAC42009.1.
    DQ234350 mRNA. Translation: ABB29979.1.
    AK304388 mRNA. Translation: BAH14173.1.
    AK312700 mRNA. Translation: BAG35578.1.
    AC018712 Genomic DNA. No translation available.
    AC093818 Genomic DNA. No translation available.
    CH471058 Genomic DNA. Translation: EAX11173.1.
    CH471058 Genomic DNA. Translation: EAX11174.1.
    BC039158 mRNA. Translation: AAH39158.1.
    CCDSiCCDS2250.1. [Q15118-1]
    CCDS63059.1. [Q15118-2]
    PIRiI55465.
    RefSeqiNP_001265478.1. NM_001278549.1.
    NP_002601.1. NM_002610.4.
    UniGeneiHs.470633.
    Hs.733780.

    Genome annotation databases

    EnsembliENST00000282077; ENSP00000282077; ENSG00000152256. [Q15118-1]
    ENST00000392571; ENSP00000376352; ENSG00000152256. [Q15118-2]
    ENST00000410055; ENSP00000386985; ENSG00000152256. [Q15118-1]
    GeneIDi5163.
    KEGGihsa:5163.
    UCSCiuc002uhs.3. human. [Q15118-1]

    Polymorphism databases

    DMDMi3183117.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L42450 mRNA. Translation: AAC42009.1 .
    DQ234350 mRNA. Translation: ABB29979.1 .
    AK304388 mRNA. Translation: BAH14173.1 .
    AK312700 mRNA. Translation: BAG35578.1 .
    AC018712 Genomic DNA. No translation available.
    AC093818 Genomic DNA. No translation available.
    CH471058 Genomic DNA. Translation: EAX11173.1 .
    CH471058 Genomic DNA. Translation: EAX11174.1 .
    BC039158 mRNA. Translation: AAH39158.1 .
    CCDSi CCDS2250.1. [Q15118-1 ]
    CCDS63059.1. [Q15118-2 ]
    PIRi I55465.
    RefSeqi NP_001265478.1. NM_001278549.1.
    NP_002601.1. NM_002610.4.
    UniGenei Hs.470633.
    Hs.733780.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2Q8F X-ray 2.03 A 30-436 [» ]
    2Q8G X-ray 1.90 A 30-436 [» ]
    2Q8H X-ray 2.00 A 30-436 [» ]
    ProteinModelPortali Q15118.
    SMRi Q15118. Positions 41-423.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111189. 17 interactions.
    DIPi DIP-29497N.
    IntActi Q15118. 6 interactions.
    MINTi MINT-2881420.
    STRINGi 9606.ENSP00000282077.

    Chemistry

    BindingDBi Q15118.
    ChEMBLi CHEMBL4766.

    PTM databases

    PhosphoSitei Q15118.

    Polymorphism databases

    DMDMi 3183117.

    Proteomic databases

    MaxQBi Q15118.
    PaxDbi Q15118.
    PRIDEi Q15118.

    Protocols and materials databases

    DNASUi 5163.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000282077 ; ENSP00000282077 ; ENSG00000152256 . [Q15118-1 ]
    ENST00000392571 ; ENSP00000376352 ; ENSG00000152256 . [Q15118-2 ]
    ENST00000410055 ; ENSP00000386985 ; ENSG00000152256 . [Q15118-1 ]
    GeneIDi 5163.
    KEGGi hsa:5163.
    UCSCi uc002uhs.3. human. [Q15118-1 ]

    Organism-specific databases

    CTDi 5163.
    GeneCardsi GC02P173384.
    HGNCi HGNC:8809. PDK1.
    HPAi CAB017554.
    HPA027376.
    MIMi 602524. gene.
    neXtProti NX_Q15118.
    PharmGKBi PA33154.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0642.
    HOGENOMi HOG000164315.
    HOVERGENi HBG000511.
    KOi K12077.
    OrthoDBi EOG71VSSV.
    PhylomeDBi Q15118.
    TreeFami TF314918.

    Enzyme and pathway databases

    Reactomei REACT_12528. Regulation of pyruvate dehydrogenase (PDH) complex.
    SignaLinki Q15118.

    Miscellaneous databases

    ChiTaRSi Pdk1. human.
    EvolutionaryTracei Q15118.
    GeneWikii Pyruvate_dehydrogenase_lipoamide_kinase_isozyme_1.
    GenomeRNAii 5163.
    NextBioi 19974.
    PROi Q15118.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q15118.
    Bgeei Q15118.
    CleanExi HS_PDK1.
    Genevestigatori Q15118.

    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. Li H., Nong W., Zhou G., Ke R., Shen C., Zhong G., Zheng Z., Liang M., Tang Z., Huang B., Lin L., Yang S.
      Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    3. "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).
    4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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.
    7. "Pyruvate dehydrogenase complex activity controls metabolic and malignant phenotype in cancer cells."
      McFate T., Mohyeldin A., Lu H., Thakar J., Henriques J., Halim N.D., Wu H., Schell M.J., Tsang T.M., Teahan O., Zhou S., Califano J.A., Jeoung N.H., Harris R.A., Verma A.
      J. Biol. Chem. 283:22700-22708(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. "Overexpression of pyruvate dehydrogenase kinase 3 increases drug resistance and early recurrence in colon cancer."
      Lu C.W., Lin S.C., Chien C.W., Lin S.C., Lee C.T., Lin B.W., Lee J.C., Tsai S.J.
      Am. J. Pathol. 179:1405-1414(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION BY HYPOXIA.
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "Tyrosine phosphorylation of mitochondrial pyruvate dehydrogenase kinase 1 is important for cancer metabolism."
      Hitosugi T., Fan J., Chung T.W., Lythgoe K., Wang X., Xie J., Ge Q., Gu T.L., Polakiewicz R.D., Roesel J.L., Chen G.Z., Boggon T.J., Lonial S., Fu H., Khuri F.R., Kang S., Chen J.
      Mol. Cell 44:864-877(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYR-136; TYR-243 AND TYR-244.
    11. "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 (1.9 ANGSTROMS) OF 30-436 IN COMPLEX WITH THE INHIBITORS AZD7545 AND DICHLOROACETATE, FUNCTION, SUBUNIT, CATALYTIC ACTIVITY, ENZYME REGULATION.
    12. "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] THR-412.

    Entry informationi

    Entry nameiPDK1_HUMAN
    AccessioniPrimary (citable) accession number: Q15118
    Secondary accession number(s): B2R6T1
    , B7Z937, D3DPD8, E9PD65, Q308M4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 136 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 2
      Human chromosome 2: 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