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Protein

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

Gene

Pdk3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 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 (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 sitei287 – 2871ATPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi247 – 2548ATPBy similarity
Nucleotide bindingi306 – 3072ATPBy similarity
Nucleotide bindingi323 – 3286ATPBy similarity

GO - Molecular functioni

GO - Biological processi

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

ReactomeiR-MMU-204174. Regulation of pyruvate dehydrogenase (PDH) complex.
R-MMU-5362517. 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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome X

Organism-specific databases

MGIiMGI:2384308. Pdk3.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial matrix Source: UniProtKB-SubCell
  • mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 415[Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 3, mitochondrialPRO_0000023444
Transit peptidei1 – ?MitochondrionSequence analysis

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei211 – 2111PhosphotyrosineBy similarity
Modified residuei212 – 2121PhosphotyrosineBy similarity
Modified residuei278 – 2781N6-succinyllysineCombined sources
Modified residuei374 – 3741N6-succinyllysineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ922H2.
MaxQBiQ922H2.
PaxDbiQ922H2.
PRIDEiQ922H2.

PTM databases

PhosphoSiteiQ922H2.

Expressioni

Gene expression databases

BgeeiQ922H2.
CleanExiMM_PDK3.
ExpressionAtlasiQ922H2. baseline and differential.
GenevisibleiQ922H2. MM.

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) (By similarity).By similarity

Protein-protein interaction databases

IntActiQ922H2. 2 interactions.
STRINGi10090.ENSMUSP00000036604.

Structurei

3D structure databases

ProteinModelPortaliQ922H2.
SMRiQ922H2. Positions 12-401.
ModBaseiSearch...
MobiDBiSearch...

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

eggNOGiKOG0787. Eukaryota.
COG0642. LUCA.
GeneTreeiENSGT00550000074574.
HOGENOMiHOG000164315.
HOVERGENiHBG000511.
InParanoidiQ922H2.
KOiK00898.
OMAiDPHVLDD.
OrthoDBiEOG71VSSV.
PhylomeDBiQ922H2.
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. His_kinase_dom.
[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.

Q922H2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRLFYRLLKQ PVPKQIERYS RFSPSPLSIK QFLDFGRDNA CEKTSYMFLR
60 70 80 90 100
KELPVRLANT MREVNLLPDN LLNRPSVGLV QSWYMQSFLE LLEYENKSPE
110 120 130 140 150
DPRVLDNFLN VLINIRNRHN DVVPTMAQGV IEYKEKFGFD PFISSNIQYF
160 170 180 190 200
LDRFYTNRIS FRMLINQHTL LFGGDTNPAH PKHIGSIDPT CNVADVVKDA
210 220 230 240 250
YETAKMLCEQ YYLVAPELEV EEFNAKAPNK PIQVVYVPSH LFHMLFELFK
260 270 280 290 300
NSMRATVELH EDKKEGYPAV KTLVTLGKED LSIKISDLGG GVPLRKIDRL
310 320 330 340 350
FNYMYSTAPR PSLEPTRAAP LAGFGYGLPI SRLYARYFQG DLKLYSMEGV
360 370 380 390 400
GTDAVIYLKA LSSESFERLP VFNKSAWRHY KTTPEADDWS NPSSEPRDAS
410
KYKAKQDKIK SNRTF
Length:415
Mass (Da):47,923
Last modified:December 1, 2001 - v1
Checksum:i566497E0F8842822
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti21 – 211R → C in BAC40379 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK075879 mRNA. Translation: BAC36024.1.
AK075985 mRNA. Translation: BAC36097.1.
AK088478 mRNA. Translation: BAC40379.1.
BC008126 mRNA. Translation: AAH08126.1.
CCDSiCCDS30275.1.
RefSeqiNP_663605.1. NM_145630.2.
UniGeneiMm.12775.

Genome annotation databases

EnsembliENSMUST00000045748; ENSMUSP00000036604; ENSMUSG00000035232.
GeneIDi236900.
KEGGimmu:236900.
UCSCiuc009tsx.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK075879 mRNA. Translation: BAC36024.1.
AK075985 mRNA. Translation: BAC36097.1.
AK088478 mRNA. Translation: BAC40379.1.
BC008126 mRNA. Translation: AAH08126.1.
CCDSiCCDS30275.1.
RefSeqiNP_663605.1. NM_145630.2.
UniGeneiMm.12775.

3D structure databases

ProteinModelPortaliQ922H2.
SMRiQ922H2. Positions 12-401.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ922H2. 2 interactions.
STRINGi10090.ENSMUSP00000036604.

PTM databases

PhosphoSiteiQ922H2.

Proteomic databases

EPDiQ922H2.
MaxQBiQ922H2.
PaxDbiQ922H2.
PRIDEiQ922H2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000045748; ENSMUSP00000036604; ENSMUSG00000035232.
GeneIDi236900.
KEGGimmu:236900.
UCSCiuc009tsx.1. mouse.

Organism-specific databases

CTDi5165.
MGIiMGI:2384308. Pdk3.

Phylogenomic databases

eggNOGiKOG0787. Eukaryota.
COG0642. LUCA.
GeneTreeiENSGT00550000074574.
HOGENOMiHOG000164315.
HOVERGENiHBG000511.
InParanoidiQ922H2.
KOiK00898.
OMAiDPHVLDD.
OrthoDBiEOG71VSSV.
PhylomeDBiQ922H2.
TreeFamiTF314918.

Enzyme and pathway databases

ReactomeiR-MMU-204174. Regulation of pyruvate dehydrogenase (PDH) complex.
R-MMU-5362517. Signaling by Retinoic Acid.

Miscellaneous databases

PROiQ922H2.
SOURCEiSearch...

Gene expression databases

BgeeiQ922H2.
CleanExiMM_PDK3.
ExpressionAtlasiQ922H2. baseline and differential.
GenevisibleiQ922H2. MM.

Family and domain databases

Gene3Di1.20.140.20. 1 hit.
3.30.565.10. 1 hit.
InterProiIPR018955. BCDHK/PDK_N.
IPR003594. HATPase_C.
IPR005467. His_kinase_dom.
[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

  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: Tongue.
  2. "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].
    Strain: FVB/N.
    Tissue: Mammary tumor.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Kidney, Lung, Pancreas, Spleen and Testis.
  4. "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-278, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiPDK3_MOUSE
AccessioniPrimary (citable) accession number: Q922H2
Secondary accession number(s): Q8BTX1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: December 1, 2001
Last modified: July 6, 2016
This is version 116 of the entry and version 1 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

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 one 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.