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Q15119

- PDK2_HUMAN

UniProt

Q15119 - PDK2_HUMAN

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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

Functioni

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
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.
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
Complete GO annotation...

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

BgeeiQ15119.
CleanExiHS_PDK2.
ExpressionAtlasiQ15119. baseline and differential.
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. 6 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 – 238Combined sources
Helixi33 – 375Combined sources
Helixi43 – 6826Combined sources
Helixi73 – 764Combined sources
Helixi79 – 9618Combined sources
Turni97 – 1004Combined sources
Helixi106 – 12217Combined sources
Turni123 – 1253Combined sources
Helixi126 – 14116Combined sources
Helixi145 – 17531Combined sources
Beta strandi177 – 1793Combined sources
Beta strandi191 – 1966Combined sources
Helixi197 – 21620Combined sources
Beta strandi222 – 2309Combined sources
Beta strandi237 – 2404Combined sources
Helixi242 – 26221Combined sources
Turni263 – 2664Combined sources
Beta strandi273 – 2797Combined sources
Beta strandi281 – 29010Combined sources
Helixi297 – 2993Combined sources
Helixi301 – 3044Combined sources
Turni306 – 3094Combined sources
Helixi329 – 33911Combined sources
Beta strandi343 – 3497Combined sources
Turni350 – 3523Combined sources
Beta strandi353 – 36311Combined sources
Turni364 – 3663Combined sources
Helixi376 – 3816Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00550000074574.
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_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. 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

        10         20         30         40         50
MRWVWALLKN ASLAGAPKYI EHFSKFSPSP LSMKQFLDFG SSNACEKTSF
60 70 80 90 100
TFLRQELPVR LANIMKEINL LPDRVLSTPS VQLVQSWYVQ SLLDIMEFLD
110 120 130 140 150
KDPEDHRTLS QFTDALVTIR NRHNDVVPTM AQGVLEYKDT YGDDPVSNQN
160 170 180 190 200
IQYFLDRFYL SRISIRMLIN QHTLIFDGST NPAHPKHIGS IDPNCNVSEV
210 220 230 240 250
VKDAYDMAKL LCDKYYMASP DLEIQEINAA NSKQPIHMVY VPSHLYHMLF
260 270 280 290 300
ELFKNAMRAT VESHESSLIL PPIKVMVALG EEDLSIKMSD RGGGVPLRKI
310 320 330 340 350
ERLFSYMYST APTPQPGTGG TPLAGFGYGL PISRLYAKYF QGDLQLFSME
360 370 380 390 400
GFGTDAVIYL KALSTDSVER LPVYNKSAWR HYQTIQEAGD WCVPSTEPKN

TSTYRVS
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:
EMBLi
GenBanki
DDBJi
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]
ENST00000614357; ENSP00000481915; ENSG00000005882. [Q15119-2]
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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. 6 interactions.
IntActi Q15119. 6 interactions.
MINTi MINT-1379180.
STRINGi 9606.ENSP00000007708.

Chemistry

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 ]
ENST00000614357 ; ENSP00000481915 ; ENSG00000005882 . [Q15119-2 ]
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.
GeneTreei ENSGT00550000074574.
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

Bgeei Q15119.
CleanExi HS_PDK2.
ExpressionAtlasi Q15119. baseline and differential.
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_C.
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

« 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(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: November 26, 2014
This is version 145 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