Names & Taxonomy
- Uniprot ID:
- Q15119
- Entry Name:
- PDK2_HUMAN
- Status:
- reviewed
- Protein Names:
- [Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 2, mitochondrial (EC 2.7.11.2) (Pyruvate dehydrogenase kinase isoform 2) (PDH kinase 2) (PDKII)
- Gene Names:
- PDK2 PDHK2
- Gene Names Primary:
- PDK2
- Organism:
- Homo sapiens (Human)
Structure
- Length:
- 407
- Sequence:
- MRWVWALLKNASLAGAPKYIEHFSKFSPSPLSMKQFLDFGSSNACEKTSFTFLRQELPVRLANIMKEINLLPDRVLSTPSVQLVQSWYVQSLLDIMEFLDKDPEDHRTLSQFTDALVTIRNRHNDVVPTMAQGVLEYKDTYGDDPVSNQNIQYFLDRFYLSRISIRMLINQHTLIFDGSTNPAHPKHIGSIDPNCNVSEVVKDAYDMAKLLCDKYYMASPDLEIQEINAANSKQPIHMVYVPSHLYHMLFELFKNAMRATVESHESSLILPPIKVMVALGEEDLSIKMSDRGGGVPLRKIERLFSYMYSTAPTPQPGTGGTPLAGFGYGLPISRLYAKYFQGDLQLFSMEGFGTDAVIYLKALSTDSVERLPVYNKSAWRHYQTIQEAGDWCVPSTEPKNTSTYRVS
- Proteomes:
- UP000005640
Subcellular location
- Subcellular Location:
- Mitochondrion matrix.
Function
- Function:
- 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.
- Catalytic Activity:
- ATP + = ADP + phosphate.
- Enzyme Regulation:
- ENZYME REGULATION: 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.
- Gene Ontology Go:
- cytoplasm
mitochondrial matrix
mitochondrial pyruvate dehydrogenase complex
mitochondrion
nucleoplasm
ATP binding
protein homodimerization activity
protein kinase activity
pyruvate dehydrogenase (acetyl-transferring) kinase activity
cellular metabolic process
cellular response to nutrient
cellular response to reactive oxygen species
glucose homeostasis
glucose metabolic process
insulin receptor signaling pathway
intrinsic apoptotic signaling pathway by p53 class mediator
protein phosphorylation
pyruvate metabolic process
regulation of acetyl-CoA biosynthetic process from pyruvate
regulation of cellular ketone metabolic process
regulation of gluconeogenesis
regulation of glucose metabolic process
regulation of pH
small molecule metabolic process - Gene Ontology Biological Process:
- cellular metabolic process
cellular response to nutrient
cellular response to reactive oxygen species
glucose homeostasis
glucose metabolic process
insulin receptor signaling pathway
intrinsic apoptotic signaling pathway by p53 class mediator
protein phosphorylation
pyruvate metabolic process
regulation of acetyl-CoA biosynthetic process from pyruvate
regulation of cellular ketone metabolic process
regulation of gluconeogenesis
regulation of glucose metabolic process
regulation of pH
small molecule metabolic process - Gene Ontology Molecular Function:
- ATP binding
protein homodimerization activity
protein kinase activity
pyruvate dehydrogenase (acetyl-transferring) kinase activity - Gene Ontology Cellular Component:
- cytoplasm
mitochondrial matrix
mitochondrial pyruvate dehydrogenase complex
mitochondrion
nucleoplasm - Keywords:
- 3D-structure
ATP-binding
Alternative splicing
Carbohydrate metabolism
Complete proteome
Glucose metabolism
Kinase
Mitochondrion
Nucleotide-binding
Polymorphism
Reference proteome
Transferase
Transit peptide