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Protein

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

Gene

PDK1

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

Functioni

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

  • ATP binding Source: UniProtKB-KW
  • protein kinase activity Source: UniProtKB
  • pyruvate dehydrogenase (acetyl-transferring) kinase activity Source: UniProtKB

GO - Biological processi

  • activation of mitophagy in response to mitochondrial depolarization Source: ParkinsonsUK-UCL
  • cell proliferation Source: UniProtKB
  • cellular metabolic process Source: Reactome
  • glucose metabolic process Source: ProtInc
  • hypoxia-inducible factor-1alpha signaling pathway Source: UniProtKB
  • intrinsic apoptotic signaling pathway in response to oxidative stress Source: UniProtKB
  • protein phosphorylation Source: GOC
  • pyruvate metabolic process Source: Reactome
  • regulation of acetyl-CoA biosynthetic process from pyruvate Source: Reactome
  • regulation of glucose metabolic process Source: UniProtKB
  • 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

BRENDAi2.7.11.2. 2681.
ReactomeiREACT_12528. Regulation of pyruvate dehydrogenase (PDH) complex.
REACT_267785. Signaling by Retinoic Acid.
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 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:8809. PDK1.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial matrix Source: Reactome
  • mitochondrial pyruvate dehydrogenase complex Source: Ensembl
  • mitochondrion Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33154.

Polymorphism and mutation databases

DMDMi3183117.

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

BgeeiQ15118.
CleanExiHS_PDK1.
ExpressionAtlasiQ15118. baseline and differential.
GenevisibleiQ15118. HS.

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. 28 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 – 509Combined sources
Helixi59 – 679Combined sources
Helixi72 – 9423Combined sources
Helixi99 – 1024Combined sources
Helixi105 – 12218Combined sources
Beta strandi125 – 1273Combined sources
Helixi132 – 14817Combined sources
Turni149 – 1513Combined sources
Helixi152 – 16615Combined sources
Helixi171 – 20232Combined sources
Beta strandi219 – 2246Combined sources
Helixi225 – 24420Combined sources
Beta strandi250 – 25910Combined sources
Beta strandi265 – 2684Combined sources
Helixi270 – 29122Combined sources
Turni293 – 2953Combined sources
Beta strandi301 – 3077Combined sources
Beta strandi309 – 31810Combined sources
Helixi325 – 3284Combined sources
Helixi329 – 3324Combined sources
Turni334 – 3374Combined sources
Beta strandi352 – 3543Combined sources
Helixi358 – 36811Combined sources
Beta strandi372 – 3787Combined sources
Turni379 – 3813Combined sources
Beta strandi382 – 39211Combined sources
Turni393 – 3953Combined sources
Helixi405 – 4117Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00550000074574.
HOGENOMiHOG000164315.
HOVERGENiHBG000511.
InParanoidiQ15118.
KOiK12077.
OMAiEDAKTIY.
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_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: 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

        10         20         30         40         50
MRLARLLRGA ALAGPGPGLR AAGFSRSFSS DSGSSPASER GVPGQVDFYA
60 70 80 90 100
RFSPSPLSMK QFLDFGSVNA CEKTSFMFLR QELPVRLANI MKEISLLPDN
110 120 130 140 150
LLRTPSVQLV QSWYIQSLQE LLDFKDKSAE DAKAIYDFTD TVIRIRNRHN
160 170 180 190 200
DVIPTMAQGV IEYKESFGVD PVTSQNVQYF LDRFYMSRIS IRMLLNQHSL
210 220 230 240 250
LFGGKGKGSP SHRKHIGSIN PNCNVLEVIK DGYENARRLC DLYYINSPEL
260 270 280 290 300
ELEELNAKSP GQPIQVVYVP SHLYHMVFEL FKNAMRATME HHANRGVYPP
310 320 330 340 350
IQVHVTLGNE DLTVKMSDRG GGVPLRKIDR LFNYMYSTAP RPRVETSRAV
360 370 380 390 400
PLAGFGYGLP ISRLYAQYFQ GDLKLYSLEG YGTDAVIYIK ALSTDSIERL
410 420 430
PVYNKAAWKH YNTNHEADDW CVPSREPKDM TTFRSA
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 (Ref. 2) Curated
Sequence conflicti96 – 961L → R in BAH14173 (PubMed:14702039).Curated
Sequence conflicti363 – 3631R → C in ABB29979 (Ref. 2) Curated

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:
EMBLi
GenBanki
DDBJi
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. [Q15118-2]
NP_002601.1. NM_002610.4. [Q15118-1]
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]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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. [Q15118-2]
NP_002601.1. NM_002610.4. [Q15118-1]
UniGeneiHs.470633.
Hs.733780.

3D structure databases

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

Protein-protein interaction databases

BioGridi111189. 28 interactions.
DIPiDIP-29497N.
IntActiQ15118. 6 interactions.
MINTiMINT-2881420.
STRINGi9606.ENSP00000282077.

Chemistry

BindingDBiQ15118.
ChEMBLiCHEMBL4766.

PTM databases

PhosphoSiteiQ15118.

Polymorphism and mutation databases

DMDMi3183117.

Proteomic databases

MaxQBiQ15118.
PaxDbiQ15118.
PRIDEiQ15118.

Protocols and materials databases

DNASUi5163.
Structural Biology KnowledgebaseSearch...

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]

Organism-specific databases

CTDi5163.
GeneCardsiGC02P173420.
HGNCiHGNC:8809. PDK1.
HPAiCAB017554.
HPA027376.
MIMi602524. gene.
neXtProtiNX_Q15118.
PharmGKBiPA33154.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0642.
GeneTreeiENSGT00550000074574.
HOGENOMiHOG000164315.
HOVERGENiHBG000511.
InParanoidiQ15118.
KOiK12077.
OMAiEDAKTIY.
OrthoDBiEOG71VSSV.
PhylomeDBiQ15118.
TreeFamiTF314918.

Enzyme and pathway databases

BRENDAi2.7.11.2. 2681.
ReactomeiREACT_12528. Regulation of pyruvate dehydrogenase (PDH) complex.
REACT_267785. Signaling by Retinoic Acid.
SignaLinkiQ15118.

Miscellaneous databases

EvolutionaryTraceiQ15118.
GeneWikiiPyruvate_dehydrogenase_lipoamide_kinase_isozyme_1.
GenomeRNAii5163.
NextBioi19974.
PROiQ15118.
SOURCEiSearch...

Gene expression databases

BgeeiQ15118.
CleanExiHS_PDK1.
ExpressionAtlasiQ15118. baseline and differential.
GenevisibleiQ15118. HS.

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(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: June 24, 2015
This is version 144 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

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.