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Protein

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

Gene

PDK3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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 kinase activity Source: UniProtKB
  3. protein serine/threonine kinase activity Source: UniProtKB
  4. pyruvate dehydrogenase (acetyl-transferring) kinase activity Source: UniProtKB

GO - Biological processi

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

Keywords - Molecular functioni

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.
REACT_267785. Signaling by Retinoic Acid.

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 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:8811. PDK3.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial matrix Source: Reactome
  2. mitochondrion Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Charcot-Marie-Tooth disease, X-linked dominant, 6 (CMTX6)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA 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.

See also OMIM:300905
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. 11 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 – 218Combined sources
Helixi29 – 3810Combined sources
Helixi42 – 6423Combined sources
Helixi69 – 724Combined sources
Helixi75 – 9218Combined sources
Helixi93 – 964Combined sources
Beta strandi99 – 1013Combined sources
Helixi102 – 11817Combined sources
Helixi119 – 1213Combined sources
Helixi122 – 13716Combined sources
Helixi141 – 17232Combined sources
Beta strandi179 – 1846Combined sources
Beta strandi187 – 1926Combined sources
Helixi193 – 21220Combined sources
Beta strandi218 – 2247Combined sources
Beta strandi233 – 2364Combined sources
Helixi238 – 26023Combined sources
Beta strandi262 – 2654Combined sources
Beta strandi270 – 2767Combined sources
Beta strandi278 – 28710Combined sources
Helixi294 – 2974Combined sources
Helixi298 – 3014Combined sources
Turni303 – 3053Combined sources
Beta strandi323 – 3253Combined sources
Helixi327 – 33711Combined sources
Beta strandi341 – 3477Combined sources
Turni348 – 3503Combined sources
Beta strandi351 – 36010Combined sources
Helixi362 – 3643Combined sources
Helixi374 – 3807Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00550000074574.
HOGENOMiHOG000164315.
HOVERGENiHBG000511.
InParanoidiQ15120.
KOiK00898.
OMAiYYMLFEL.
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_C.
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. AlignAdd to basket

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

        10         20         30         40         50
MRLFRWLLKQ PVPKQIERYS RFSPSPLSIK QFLDFGRDNA CEKTSYMFLR
60 70 80 90 100
KELPVRLANT MREVNLLPDN LLNRPSVGLV QSWYMQSFLE LLEYENKSPE
110 120 130 140 150
DPQVLDNFLQ VLIKVRNRHN DVVPTMAQGV IEYKEKFGFD PFISTNIQYF
160 170 180 190 200
LDRFYTNRIS FRMLINQHTL LFGGDTNPVH PKHIGSIDPT CNVADVVKDA
210 220 230 240 250
YETAKMLCEQ YYLVAPELEV EEFNAKAPDK PIQVVYVPSH LFHMLFELFK
260 270 280 290 300
NSMRATVELY EDRKEGYPAV KTLVTLGKED LSIKISDLGG GVPLRKIDRL
310 320 330 340 350
FNYMYSTAPR PSLEPTRAAP LAGFGYGLPI SRLYARYFQG DLKLYSMEGV
360 370 380 390 400
GTDAVIYLKA LSSESFERLP VFNKSAWRHY KTTPEADDWS NPSSEPRDAS

KYKAKQ
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

BioGridi111191. 11 interactions.
DIPiDIP-29498N.
IntActiQ15120. 2 interactions.
STRINGi9606.ENSP00000387536.

Chemistry

ChEMBLiCHEMBL2096665.

PTM databases

PhosphoSiteiQ15120.

Polymorphism databases

DMDMi3183119.

Proteomic databases

MaxQBiQ15120.
PaxDbiQ15120.
PRIDEiQ15120.

Protocols and materials databases

DNASUi5165.
Structural Biology KnowledgebaseSearch...

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]

Organism-specific databases

CTDi5165.
GeneCardsiGC0XP024393.
HGNCiHGNC:8811. PDK3.
HPAiHPA046583.
MIMi300905. phenotype.
300906. gene.
neXtProtiNX_Q15120.
Orphaneti352675. X-linked Charcot-Marie-Tooth disease type 6.
PharmGKBiPA33156.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0642.
GeneTreeiENSGT00550000074574.
HOGENOMiHOG000164315.
HOVERGENiHBG000511.
InParanoidiQ15120.
KOiK00898.
OMAiYYMLFEL.
OrthoDBiEOG71VSSV.
PhylomeDBiQ15120.
TreeFamiTF314918.

Enzyme and pathway databases

ReactomeiREACT_12528. Regulation of pyruvate dehydrogenase (PDH) complex.
REACT_267785. Signaling by Retinoic Acid.

Miscellaneous databases

ChiTaRSiPDK3. human.
EvolutionaryTraceiQ15120.
GeneWikiiPDK3.
GenomeRNAii5165.
NextBioi19982.
PROiQ15120.
SOURCEiSearch...

Gene expression databases

BgeeiQ15120.
CleanExiHS_PDK3.
GenevestigatoriQ15120.

Family and domain databases

Gene3Di1.20.140.20. 1 hit.
3.30.565.10. 1 hit.
InterProiIPR018955. BCDHK/PDK_N.
IPR003594. HATPase_C.
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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1994) [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(2003) [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(2003) [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(1999) [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(2000) [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(2001) [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(2005) [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(2006) [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(2007) [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(2010) [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(2010) [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(2011) [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(2004) [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(2006) [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(2006) [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(2006) [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(2012) [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: April 1, 2015
This is version 154 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.