NP_002601.1
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NCBI GenBank Nucleotide #
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UniProt Secondary Accession #
UniProt Related Accession #
Molecular Weight
51,623 Da
NCBI Official Full Name
[Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 1, mitochondrial isoform 2
NCBI Official Synonym Full Names
pyruvate dehydrogenase kinase 1
NCBI Protein Information
[Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 1, mitochondrial
UniProt Protein Name
[Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 1, mitochondrial
UniProt Synonym Protein Names
Pyruvate dehydrogenase kinase isoform 1; PDH kinase 1
UniProt Synonym Gene Names
UniProt Entry Name
PDK1_HUMAN
NCBI Summary for PDK1
Pyruvate dehydrogenase (PDH) is a mitochondrial multienzyme complex that catalyzes the oxidative decarboxylation of pyruvate and is one of the major enzymes responsible for the regulation of homeostasis of carbohydrate fuels in mammals. The enzymatic activity is regulated by a phosphorylation/dephosphorylation cycle. Phosphorylation of PDH by a specific pyruvate dehydrogenase kinase (PDK) results in inactivation. Multiple alternatively spliced transcript variants have been found for this gene. [provided by RefSeq, Jun 2013]
UniProt Comments for PDK1
PDHK1: an ubiquitously expressed, atypical protein kinase associated with the mitochondrial matrix. The PDHKs play crucial roles in switching metabolic flux from oxidative phosphorylation towards glycolysis. PDHK1 is detected in heart, pancreatic islets, and skeletal muscles. Contains a HATPase_c catalytic domain, found in several ATP-binding proteins including protein histidine kinases (PHKs), PHDKs, DNA gyrase B, topoisomerases, heat shock proteins, and DNA mismatch repair proteins. PDHK regulates glucose oxidation through inhibitory phosphorylation of the E1 alpha subunit of the mitochondrial pyruvate dehydrogenase complex (PDHC) at any one of 3 inhibitory serine residues. Inhibitory sites 1, 2, and 3 correspond to S293, S300, and S232 in human PDHA1, respectively. Four PDHK isoenzymes have been described, each with different site specificity: all four phosphorylate sites 1 and 2 but at different rates; for site 1 PDHK2 >PDHK4 >PDHK1 >PDHK3; for site 2, PDHK3> PDHK4 > PDHK2 > PDHK1. Only PDHK1 phosphorylates site 3. PDHKs are recruited to the PDHC by binding to a lipoyl group covalently attached to the inner lipoyl domain of the E2 component. PDHA1 deficiency is the most common enzyme defect in patients with primary lactic acidosis. PDHK1 is a direct HIF-1 target gene. Suppression of PDH by PDHK inhibits the conversion of pyruvate to acetyl-CoA, attenuates mitochondrial respiration, and may contribute to the increased lactate production observed in many tumors. The PDH pathway is repressed in a majority of non-small cell lung carcinomas. Inhibited by AZD7545, dichloroacetate (DCA) and radicicol. Radicicol inhibits kinase activity by binding directly to the ATP-binding pocket of PDHK, similar to HSP90 from the same ATPase/kinase superfamily.
Protein type: Mitochondrial; EC 2.7.11.2; Kinase, protein; Protein kinase, atypical; ATYPICAL group; PDHK family
Chromosomal Location of Human Ortholog: 2q31.1
Cellular Component: mitochondrial matrix; mitochondrial pyruvate dehydrogenase complex; mitochondrion
Molecular Function: ATP binding; protein binding; protein kinase activity; pyruvate dehydrogenase (acetyl-transferring) kinase activity
Biological Process: cell proliferation; glucose metabolic process; induction of apoptosis by oxidative stress; protein amino acid phosphorylation; regulation of acetyl-CoA biosynthetic process from pyruvate
Research Articles on PDK1
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Products associated with anti-PDK1 antibody
Pathways associated with anti-PDK1 antibody
Diseases associated with anti-PDK1 antibody
Organs/Tissues associated with anti-PDK1 antibody
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