PDK1 Serine/threonine kinase which acts as a master kinase, phosphorylating and activating a subgroup of the AGC family of protein kinases. Its targets include: protein kinase B (PKB/AKT1, PKB/AKT2, PKB/AKT3), p70 ribosomal protein S6 kinase (RPS6KB1), p90 ribosomal protein S6 kinase (RPS6KA1, RPS6KA2 and RPS6KA3), cyclic AMP-dependent protein kinase (PRKACA), protein kinase C (PRKCD and PRKCZ), serum and glucocorticoid-inducible kinase (SGK1, SGK2 and SGK3), p21-activated kinase-1 (PAK1), protein kinase PKN (PKN1 and PKN2). Plays a central role in the transduction of signals from insulin by providing the activating phosphorylation to PKB/AKT1, thus propagating the signal to downstream targets controlling cell proliferation and survival, as well as glucose and amino acid uptake and storage. Negatively regulates the TGF-beta-induced signaling by: modulating the association of SMAD3 and SMAD7 with TGF-beta receptor, phosphorylating SMAD2, SMAD3, SMAD4 and SMAD7, preventing the nuclear translocation of SMAD3 and SMAD4 and the translocation of SMAD7 from the nucleus to the cytoplasm in response to TGF-beta. Activates PPARG transcriptional activity and promotes adipocyte differentiation. Activates the NF-kappa-B pathway via phosphorylation of IKKB. The tyrosine phosphorylated form is crucial for the regulation of focal adhesions by angiotensin II. Controls proliferation, survival, and growth of developing pancreatic cells. Participates in the regulation of Ca(2+) entry and Ca(2+)-activated K(+) channels of mast cells. Essential for the motility of vascular endothelial cells (ECs) and is involved in the regulation of their chemotaxis. Plays a critical role in cardiac homeostasis by serving as a dual effector for cell survival and beta-adrenergic response. Plays an important role during thymocyte development by regulating the expression of key nutrient receptors on the surface of pre-T cells and mediating Notch-induced cell growth and proliferative responses. Provides negative feedback inhibition to toll-like receptor-mediated NF-kappa-B activation in macrophages. Isoform 3 is catalytically inactive. Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. PDPK1 subfamily. Appears to be expressed ubiquitously. The Tyr-9 phosphorylated form is markedly increased in diseased tissue compared with normal tissue from lung, liver, colon and breast. 5 alternatively spliced human isoforms have been reported. Note: This description may include information from UniProtKB.
Protein type: AGC group; EC; Kinase, protein; Nuclear receptor co-regulator; PKB family; Protein kinase, AGC; Protein kinase, Ser/Thr (non-receptor)
Chromosomal Location of Human Ortholog: 10q12
Cellular Component:  cell projection; cytoplasm; cytoplasmic vesicle; cytosol; focal adhesion; nucleus; perikaryon; plasma membrane; postsynaptic density
Molecular Function:  3-phosphoinositide-dependent protein kinase activity; ATP binding; insulin receptor binding; phospholipase activator activity; phospholipase binding; protein kinase binding; protein serine/threonine kinase activity
Biological Process:  activation of protein kinase B activity; calcium-mediated signaling; cell migration; cellular response to brain-derived neurotrophic factor stimulus; cellular response to epidermal growth factor stimulus; cellular response to insulin stimulus; epidermal growth factor receptor signaling pathway; extrinsic apoptotic signaling pathway; focal adhesion assembly; hyperosmotic response; intracellular signal transduction; negative regulation of cardiac muscle cell apoptotic process; negative regulation of endothelial cell apoptotic process; negative regulation of neuron apoptotic process; negative regulation of protein kinase activity; negative regulation of toll-like receptor signaling pathway; negative regulation of transforming growth factor beta receptor signaling pathway; peptidyl-serine phosphorylation; peptidyl-threonine phosphorylation; positive regulation of angiogenesis; positive regulation of blood vessel endothelial cell migration; positive regulation of phospholipase activity; positive regulation of protein localization to plasma membrane; positive regulation of release of sequestered calcium ion into cytosol; positive regulation of sprouting angiogenesis; positive regulation of vascular endothelial cell proliferation; protein phosphorylation; regulation of endothelial cell migration; regulation of I-kappaB kinase/NF-kappaB signaling; regulation of mast cell degranulation; type B pancreatic cell development
Reference #:  O55173 (UniProtKB)
Alt. Names/Synonyms: 3-phosphoinositide dependent protein kinase-1; 3-phosphoinositide-dependent protein kinase 1; Pdk1; Pdpk1; PkB kinase; Protein kinase B kinase
Gene Symbols: Pdpk1
Molecular weight: 63,593 Da
Basal Isoelectric point: 6.72  Predict pI for various phosphorylation states
CST Pathways:  Inhibition of Apoptosis  |  Insulin Receptor Signaling  |  mTOR Signaling  |  NF-kB Signaling  |  PI3K/Akt Signaling  |  Protein Kinase C Signaling  |  T Cell Receptor Signaling  |  Translation: eIF4E and p70S6K
Protein-Specific Antibodies, siRNAs or Recombinant Proteins from Cell Signaling Technology® Total Proteins
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Cross-references to other databases:  STRING  |  Reactome  |  BioGPS  |  Pfam  |  ENZYME  |  Phospho.ELM  |  NetworKIN  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene  |  NURSA