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Q8BFP9

- PDK1_MOUSE

UniProt

Q8BFP9 - PDK1_MOUSE

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Protein

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

Gene

Pdk1

Organism
Mus musculus (Mouse)
Status
Reviewed - 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 By similarity.By similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei316 – 3161ATPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi277 – 2848ATPBy similarity
Nucleotide bindingi335 – 3362ATPBy similarity
Nucleotide bindingi352 – 3576ATPBy similarity

GO - Molecular functioni

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

GO - Biological processi

  1. cell proliferation Source: UniProtKB
  2. glucose metabolic process Source: UniProtKB-KW
  3. hypoxia-inducible factor-1alpha signaling pathway Source: UniProtKB
  4. intracellular signal transduction Source: MGI
  5. intrinsic apoptotic signaling pathway in response to oxidative stress Source: UniProtKB
  6. protein phosphorylation Source: GOC
  7. regulation of acetyl-CoA biosynthetic process from pyruvate Source: UniProtKB
  8. regulation of glucose metabolic process Source: UniProtKB
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_226284. Regulation of pyruvate dehydrogenase (PDH) complex.

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 2

Organism-specific databases

MGIiMGI:1926119. Pdk1.

Subcellular locationi

Mitochondrion matrix By similarity

GO - Cellular componenti

  1. mitochondrial pyruvate dehydrogenase complex Source: UniProtKB
  2. mitochondrion Source: MGI
  3. plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2626MitochondrionSequence AnalysisAdd
BLAST
Chaini27 – 434408[Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 1, mitochondrialPRO_0000023438Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei136 – 1361Phosphotyrosine; by FGFR1By similarity
Modified residuei241 – 2411Phosphotyrosine; by FGFR1, ABL1, FLT3 and JAK2By similarity
Modified residuei242 – 2421Phosphotyrosine; by FGFR1By similarity
Modified residuei403 – 4031N6-succinyllysine1 Publication

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-241 and Tyr-242 strongly increases kinase activity, while phosphorylation at Tyr-136 has a lesser effect By similarity.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ8BFP9.
PaxDbiQ8BFP9.
PRIDEiQ8BFP9.

PTM databases

PhosphoSiteiQ8BFP9.

Expressioni

Inductioni

Up-regulated by glucose and palmitate. Up- regulated via the HIF1A signaling pathway in response to hypoxia.2 Publications

Gene expression databases

BgeeiQ8BFP9.
CleanExiMM_PDK1.
ExpressionAtlasiQ8BFP9. baseline and differential.
GenevestigatoriQ8BFP9.

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) By similarity.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ8BFP9.
SMRiQ8BFP9. Positions 41-421.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini161 – 391231Histidine 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.
InParanoidiQ8BFP9.
KOiK12077.
OMAiEDAKTIY.
OrthoDBiEOG71VSSV.
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]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8BFP9-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRLARLLRGG TSVRPLCAVP CASRSLASAS ASGSGPASEL GVPGQVDFYA
60 70 80 90 100
RFSPSPLSMK QFLDFGSVNA CEKTSFMFLR QELPVRLANI MKEISLLPDN
110 120 130 140 150
LLRTPSVQLV QSWYIQSLQE LLDFKDKSAE DAKTIYEFTD TVIRIRNRHN
160 170 180 190 200
DVIPTMAQGV TEYKESFGVD PVTSQNVQYF LDRFYMSRIS IRMLLNQHSL
210 220 230 240 250
LFGGKGSPSH RKHIGSINPN CDVVEVIKDG YENARRLCDL YYVNSPELEL
260 270 280 290 300
EELNAKSPGQ TIQVVYVPSH LYHMVFELFK NAMRATMEHH ADKGVYPPIQ
310 320 330 340 350
VHVTLGEEDL TVKMSDRGGG VPLRKIDRLF NYMYSTAPRP RVETSRAVPL
360 370 380 390 400
AGFGYGLPIS RLYAQYFQGD LKLYSLEGYG TDAVIYIKAL STESVERLPV
410 420 430
YNKAAWKHYK ANHEADDWCV PSREPKDMTT FRSS
Length:434
Mass (Da):48,995
Last modified:July 27, 2011 - v2
Checksum:i8A514C863E751040
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti324 – 3241R → S in BAC32879. (PubMed:16141072)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK046805 mRNA. Translation: BAC32879.1.
AK153649 mRNA. Translation: BAE32134.1.
AL928963 Genomic DNA. Translation: CAM26372.1.
CH466519 Genomic DNA. Translation: EDL27100.1.
CH466519 Genomic DNA. Translation: EDL27102.1.
CH466519 Genomic DNA. Translation: EDL27104.1.
CCDSiCCDS16119.1.
RefSeqiNP_766253.2. NM_172665.5.
UniGeneiMm.34411.

Genome annotation databases

EnsembliENSMUST00000006669; ENSMUSP00000006669; ENSMUSG00000006494.
GeneIDi228026.
KEGGimmu:228026.
UCSCiuc008kbh.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK046805 mRNA. Translation: BAC32879.1 .
AK153649 mRNA. Translation: BAE32134.1 .
AL928963 Genomic DNA. Translation: CAM26372.1 .
CH466519 Genomic DNA. Translation: EDL27100.1 .
CH466519 Genomic DNA. Translation: EDL27102.1 .
CH466519 Genomic DNA. Translation: EDL27104.1 .
CCDSi CCDS16119.1.
RefSeqi NP_766253.2. NM_172665.5.
UniGenei Mm.34411.

3D structure databases

ProteinModelPortali Q8BFP9.
SMRi Q8BFP9. Positions 41-421.
ModBasei Search...
MobiDBi Search...

PTM databases

PhosphoSitei Q8BFP9.

Proteomic databases

MaxQBi Q8BFP9.
PaxDbi Q8BFP9.
PRIDEi Q8BFP9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000006669 ; ENSMUSP00000006669 ; ENSMUSG00000006494 .
GeneIDi 228026.
KEGGi mmu:228026.
UCSCi uc008kbh.1. mouse.

Organism-specific databases

CTDi 5163.
MGIi MGI:1926119. Pdk1.

Phylogenomic databases

eggNOGi COG0642.
GeneTreei ENSGT00550000074574.
HOGENOMi HOG000164315.
HOVERGENi HBG000511.
InParanoidi Q8BFP9.
KOi K12077.
OMAi EDAKTIY.
OrthoDBi EOG71VSSV.
TreeFami TF314918.

Enzyme and pathway databases

Reactomei REACT_226284. Regulation of pyruvate dehydrogenase (PDH) complex.

Miscellaneous databases

ChiTaRSi Pdk1. mouse.
NextBioi 378903.
PROi Q8BFP9.
SOURCEi Search...

Gene expression databases

Bgeei Q8BFP9.
CleanExi MM_PDK1.
ExpressionAtlasi Q8BFP9. baseline and differential.
Genevestigatori Q8BFP9.

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. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Medulla oblongata and Thymus.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "Regulation of PDK mRNA by high fatty acid and glucose in pancreatic islets."
    Xu J., Han J., Epstein P.N., Liu Y.Q.
    Biochem. Biophys. Res. Commun. 344:827-833(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY PALMITATE AND GLUCOSE.
  5. "HIF-1 mediates adaptation to hypoxia by actively downregulating mitochondrial oxygen consumption."
    Papandreou I., Cairns R.A., Fontana L., Lim A.L., Denko N.C.
    Cell Metab. 3:187-197(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY HYPOXIA, FUNCTION.
  6. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-403, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiPDK1_MOUSE
AccessioniPrimary (citable) accession number: Q8BFP9
Secondary accession number(s): Q3U5E5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: July 27, 2011
Last modified: October 29, 2014
This is version 95 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3