Proteins > 3-phosphoinositide-dependent protein kinase 1
Page last updated: 2024-08-07 15:23:46

3-phosphoinositide-dependent protein kinase 1

A 3-phosphoinositide-dependent protein kinase 1 that is encoded in the genome of human. [PRO:DNx, UniProtKB:O15530]

Synonyms

hPDK1;
EC 2.7.11.1

Research

Bioassay Publications (35)

TimeframeStudies on this Protein(%)All Drugs %
pre-19900 (0.00)18.7374
1990's0 (0.00)18.2507
2000's11 (31.43)29.6817
2010's23 (65.71)24.3611
2020's1 (2.86)2.80

Compounds (111)

Drugs with Inhibition Measurements

DrugTaxonomyMeasurementAverage (mM)Bioassay(s)Publication(s)
5-fluoroindole-2-carboxylic acidHomo sapiens (human)IC50297.000011
bisindolylmaleimide iHomo sapiens (human)IC509.000011
2-(1-(2-(1-methylpyrrolidino)ethyl)-1h-indol-3-yl)maleimideHomo sapiens (human)IC5014.000011
bisindolylmaleimide iiiHomo sapiens (human)IC503.485717
ro 31-7549Homo sapiens (human)IC501.000011
celecoxibHomo sapiens (human)IC5048.000022
niclosamideHomo sapiens (human)IC5083.900011
1H-indazol-3-amineHomo sapiens (human)IC50311.000011
2,6-diaminopurineHomo sapiens (human)IC5050.800011
staurosporineHomo sapiens (human)IC500.007233
6-methoxypurineHomo sapiens (human)IC50340.000011
7-hydroxystaurosporineHomo sapiens (human)IC500.005522
3-amino-1,2,4-benzotriazineHomo sapiens (human)IC50160.000011
1-oxo-1,2,3,4-tetrahydroisoquinolineHomo sapiens (human)IC50169.000011
ruboxistaurinHomo sapiens (human)IC500.648428
isoxanthohumolHomo sapiens (human)IC5058.700011
xanthohumolHomo sapiens (human)IC506.600011
2-tert-butyl-9-fluoro-3,6-dihydro-7h-benz(h)imidazo(4,5-f)isoquinoline-7-oneHomo sapiens (human)IC500.020011
chir 99021Homo sapiens (human)IC5010.000011
osu 03012Homo sapiens (human)IC505.000011
bx795Homo sapiens (human)IC500.006022
saracatinibHomo sapiens (human)IC5010.000011
meridianin aHomo sapiens (human)IC505.400011
bx 517Homo sapiens (human)IC500.017888
danusertibHomo sapiens (human)IC5010.000011
nvp-aew541Homo sapiens (human)IC508.900011
N-[3-[[5-bromo-4-[2-(1H-imidazol-5-yl)ethylamino]-2-pyrimidinyl]amino]phenyl]-1-pyrrolidinecarboxamideHomo sapiens (human)IC500.012011
pha 848125Homo sapiens (human)IC5010.000011
entrectinibHomo sapiens (human)IC5010.000011
gsk 2334470Homo sapiens (human)IC500.061087
nms-p118Homo sapiens (human)IC5010.000011
4-hydroxyquinazolineHomo sapiens (human)IC50345.000011
1,4-Dihydrothieno[3,2-d]pyrimidin-4-oneHomo sapiens (human)IC50492.000011
7-Methyl-3,4-dihydrothieno[3,2-d]pyrimidin-4-oneHomo sapiens (human)IC50461.000011
debromohymenialdisineHomo sapiens (human)IC508.666117

Drugs with Activation Measurements

DrugTaxonomyMeasurementAverage (mM)Bioassay(s)Publication(s)
9-xylosyladenineHomo sapiens (human)Kd20.000011
sb 202190Homo sapiens (human)Kd10.000011
imatinibHomo sapiens (human)Kd10.000022
pyrazolanthroneHomo sapiens (human)Kd1.250011
staurosporineHomo sapiens (human)Kd0.001722
gefitinibHomo sapiens (human)Kd10.000022
lestaurtinibHomo sapiens (human)Kd0.003422
vatalanibHomo sapiens (human)Kd10.000022
ruboxistaurinHomo sapiens (human)Kd0.700022
canertinibHomo sapiens (human)Kd10.000022
birb 796Homo sapiens (human)Kd10.000022
cyc 202Homo sapiens (human)Kd10.000011
sb 203580Homo sapiens (human)Kd10.000022
enzastaurinHomo sapiens (human)Kd10.000011
erlotinibHomo sapiens (human)Kd10.000022
lapatinibHomo sapiens (human)Kd10.000022
sorafenibHomo sapiens (human)Kd10.000033
pd 173955Homo sapiens (human)Kd10.000011
s 1033Homo sapiens (human)Kd10.000011
bms 387032Homo sapiens (human)Kd10.000022
tandutinibHomo sapiens (human)Kd10.000033
vx-745Homo sapiens (human)Kd10.000022
dasatinibHomo sapiens (human)Kd10.000022
zd 6474Homo sapiens (human)Kd10.000022
4-(5-benzo(1,3)dioxol-5-yl-4-pyridin-2-yl-1h-imidazol-2-yl)benzamideHomo sapiens (human)Kd10.000011
alvocidibHomo sapiens (human)Kd10.000022
bosutinibHomo sapiens (human)Kd10.000011
su 11248Homo sapiens (human)Kd3.500033
jnj-7706621Homo sapiens (human)Kd3.100011
2-tert-butyl-9-fluoro-3,6-dihydro-7h-benz(h)imidazo(4,5-f)isoquinoline-7-oneHomo sapiens (human)EC500.001011
vx680Homo sapiens (human)Kd10.000022
ekb 569Homo sapiens (human)Kd10.000011
axitinibHomo sapiens (human)Kd10.000011
pd 184352Homo sapiens (human)Kd10.000011
bms345541Homo sapiens (human)Kd10.000011
midostaurinHomo sapiens (human)Kd0.163333
ki 20227Homo sapiens (human)Kd10.000011
cp 724714Homo sapiens (human)Kd10.000011
pi103Homo sapiens (human)Kd10.000022
hki 272Homo sapiens (human)Kd10.000011
tofacitinibHomo sapiens (human)Kd10.000022
n-(6-chloro-7-methoxy-9h-beta-carbolin-8-yl)-2-methylnicotinamideHomo sapiens (human)Kd10.000011
cediranibHomo sapiens (human)Kd10.000011
masitinibHomo sapiens (human)Kd10.000011
bx795Homo sapiens (human)EC500.026011
pazopanibHomo sapiens (human)Kd10.000022
azd 6244Homo sapiens (human)Kd10.000011
su 14813Homo sapiens (human)Kd2.600022
bibw 2992Homo sapiens (human)Kd10.000011
tg100-115Homo sapiens (human)Kd10.000011
pha 665752Homo sapiens (human)Kd10.000011
6-[[5-fluoro-2-(3,4,5-trimethoxyanilino)-4-pyrimidinyl]amino]-2,2-dimethyl-4H-pyrido[3,2-b][1,4]oxazin-3-oneHomo sapiens (human)Kd0.120011
brivanibHomo sapiens (human)Kd10.000011
at 7519Homo sapiens (human)Kd10.000011
bi 2536Homo sapiens (human)Kd10.000011
nvp-ast487Homo sapiens (human)Kd10.000022
kw 2449Homo sapiens (human)Kd0.650011
abt 869Homo sapiens (human)Kd10.000022
gw 2580Homo sapiens (human)Kd10.000022
crizotinibHomo sapiens (human)Kd10.000011
chir-265Homo sapiens (human)Kd10.000022
motesanibHomo sapiens (human)Kd10.000022
mln8054Homo sapiens (human)Kd10.000022
GDC-0879Homo sapiens (human)Kd10.000011
gsk 461364Homo sapiens (human)Kd10.000011
azd 1152-hqpaHomo sapiens (human)Kd10.000022
nvp-tae684Homo sapiens (human)Kd10.000011
fedratinibHomo sapiens (human)Kd10.000011
gsk690693Homo sapiens (human)Kd10.000011
gdc 0941Homo sapiens (human)Kd10.000011
plx 4720Homo sapiens (human)Kd10.000011
sgx 523Homo sapiens (human)Kd10.000011
quizartinibHomo sapiens (human)Kd10.000022
incb-018424Homo sapiens (human)Kd10.000011
gsk 1838705aHomo sapiens (human)Kd10.000011
gsk 1363089Homo sapiens (human)Kd10.000011
1-[(3,4-difluorophenyl)methyl]-2-oxo-N-[(1R)-2-[(2-oxo-1,3-dihydrobenzimidazol-5-yl)oxy]-1-phenylethyl]-3-pyridinecarboxamideHomo sapiens (human)EC500.001011
chir 258Homo sapiens (human)Kd10.000022
nintedanibHomo sapiens (human)Kd2.800011
pp242Homo sapiens (human)Kd10.000011

Enables

This protein enables 7 target(s):

TargetCategoryDefinition
protein serine/threonine kinase activitymolecular functionCatalysis of the reactions: ATP + protein serine = ADP + protein serine phosphate, and ATP + protein threonine = ADP + protein threonine phosphate. [GOC:bf, MetaCyc:PROTEIN-KINASE-RXN, PMID:2956925]
3-phosphoinositide-dependent protein kinase activitymolecular functionPhosphatidylinositol-3-phosphate-dependent catalysis of the reaction: ATP + a protein = ADP + a phosphoprotein. [GOC:mah]
protein bindingmolecular functionBinding to a protein. [GOC:go_curators]
ATP bindingmolecular functionBinding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. [ISBN:0198506732]
phospholipase activator activitymolecular functionBinds to and increases the activity of a phospholipase, an enzyme that catalyzes of the hydrolysis of a glycerophospholipid. [GOC:ai]
phospholipase bindingmolecular functionBinding to a phospholipase. [GOC:jl]
protein serine kinase activitymolecular functionCatalysis of the reactions: ATP + protein serine = ADP + protein serine phosphate. [RHEA:17989]

Located In

This protein is located in 8 target(s):

TargetCategoryDefinition
nucleuscellular componentA membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent. [GOC:go_curators]
cytoplasmcellular componentThe contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. [ISBN:0198547684]
cytosolcellular componentThe part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. [GOC:hjd, GOC:jl]
plasma membranecellular componentThe membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. [ISBN:0716731363]
focal adhesioncellular componentA cell-substrate junction that anchors the cell to the extracellular matrix and that forms a point of termination of actin filaments. In insects focal adhesion has also been referred to as hemi-adherens junction (HAJ). [GOC:aruk, GOC:bc, ISBN:0124325653, ISBN:0815316208, PMID:10419689, PMID:12191915, PMID:15246682, PMID:1643657, PMID:16805308, PMID:19197329, PMID:23033047, PMID:26923917, PMID:28796323, PMID:8314002]
postsynaptic densitycellular componentAn electron dense network of proteins within and adjacent to the postsynaptic membrane of an asymmetric, neuron-neuron synapse. Its major components include neurotransmitter receptors and the proteins that spatially and functionally organize them such as anchoring and scaffolding molecules, signaling enzymes and cytoskeletal components. [GOC:BHF, GOC:dos, GOC:ef, GOC:jid, GOC:pr, GOC:sjp, http://molneuro.kaist.ac.kr/psd, PMID:14532281, Wikipedia:Postsynaptic_density]
cytoplasmic vesiclecellular componentA vesicle found in the cytoplasm of a cell. [GOC:ai, GOC:mah, GOC:vesicles]
cell projectioncellular componentA prolongation or process extending from a cell, e.g. a flagellum or axon. [GOC:jl, http://www.cogsci.princeton.edu/~wn/]

Involved In

This protein is involved in 33 target(s):

TargetCategoryDefinition
type B pancreatic cell developmentbiological processThe process whose specific outcome is the progression of a type B pancreatic cell over time, from its formation to the mature structure. A type B pancreatic cell is a cell located towards center of the islets of Langerhans that secretes insulin. [CL:0000169, GOC:dph]
protein phosphorylationbiological processThe process of introducing a phosphate group on to a protein. [GOC:hb]
negative regulation of protein kinase activitybiological processAny process that stops, prevents, or reduces the frequency, rate or extent of protein kinase activity. [GOC:go_curators]
hyperosmotic responsebiological processAny process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of detection of, or exposure to, a hyperosmotic environment, i.e. an environment with a higher concentration of solutes than the organism or cell. [GOC:jl, PMID:12142009]
epidermal growth factor receptor signaling pathwaybiological processThe series of molecular signals initiated by binding of a ligand to the tyrosine kinase receptor EGFR (ERBB1) on the surface of a cell. The pathway ends with regulation of a downstream cellular process, e.g. transcription. [GOC:ceb]
insulin receptor signaling pathwaybiological processThe series of molecular signals generated as a consequence of the insulin receptor binding to insulin. [GOC:ceb]
positive regulation of phospholipase activitybiological processAny process that increases the frequency, rate or extent of phospholipase activity, the hydrolysis of a phospholipid. [GOC:BHF, GOC:dph, GOC:tb]
negative regulation of cardiac muscle cell apoptotic processbiological processAny process that decreases the rate or extent of cardiac cell apoptotic process, a form of programmed cell death induced by external or internal signals that trigger the activity of proteolytic caspases whose actions dismantle a cardiac muscle cell and result in its death. [GOC:BHF, GOC:dph, GOC:mtg_apoptosis, GOC:rl, GOC:tb]
cell migrationbiological processThe controlled self-propelled movement of a cell from one site to a destination guided by molecular cues. [GOC:cjm, GOC:dph, GOC:ems, GOC:pf, Wikipedia:Cell_migration]
peptidyl-threonine phosphorylationbiological processThe phosphorylation of peptidyl-threonine to form peptidyl-O-phospho-L-threonine. [RESID:AA0038]
calcium-mediated signalingbiological processAny intracellular signal transduction in which the signal is passed on within the cell via calcium ions. [GOC:signaling]
actin cytoskeleton organizationbiological processA process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of cytoskeletal structures comprising actin filaments and their associated proteins. [GOC:dph, GOC:jl, GOC:mah]
negative regulation of transforming growth factor beta receptor signaling pathwaybiological processAny process that stops, prevents, or reduces the frequency, rate or extent of any TGF-beta receptor signaling pathway. [GOC:mah]
T cell costimulationbiological processThe process of providing, via surface-bound receptor-ligand pairs, a second, antigen-independent, signal in addition to that provided by the T cell receptor to augment T cell activation. [ISBN:0781735149]
activation of protein kinase B activitybiological processAny process that initiates the activity of the inactive enzyme protein kinase B. [GOC:pg]
cellular response to insulin stimulusbiological processAny process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an insulin stimulus. Insulin is a polypeptide hormone produced by the islets of Langerhans of the pancreas in mammals, and by the homologous organs of other organisms. [GOC:mah, ISBN:0198506732]
negative regulation of toll-like receptor signaling pathwaybiological processAny process that stops, prevents, or reduces the frequency, rate, or extent of toll-like receptor signaling pathway. [GOC:add, PMID:16551253, PMID:17328678]
regulation of canonical NF-kappaB signal transductionbiological processAny process that modulates the canonical NF-kappaB signaling cascade. [GOC:jl, PMID:12773372]
regulation of mast cell degranulationbiological processAny process that modulates the frequency, rate, or extent of mast cell degranulation. [ISBN:0781735149]
positive regulation of blood vessel endothelial cell migrationbiological processAny process that activates or increases the frequency, rate or extent of the migration of the endothelial cells of blood vessels. [GOC:go_curators]
positive regulation of angiogenesisbiological processAny process that activates or increases angiogenesis. [GOC:go_curators]
protein autophosphorylationbiological processThe phosphorylation by a protein of one or more of its own amino acid residues (cis-autophosphorylation), or residues on an identical protein (trans-autophosphorylation). [ISBN:0198506732]
insulin-like growth factor receptor signaling pathwaybiological processThe series of molecular signals initiated by a ligand binding to an insulin-like growth factor receptor on the surface of a target cell, and ending with the regulation of a downstream cellular process, e.g. transcription. [GOC:ceb]
positive regulation of release of sequestered calcium ion into cytosolbiological processAny process that activates or increases the frequency, rate or extent of the release into the cytosolic compartment of calcium ions sequestered in the endoplasmic reticulum or mitochondria. [GOC:ai]
positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transductionbiological processAny process that activates or increases the frequency, rate or extent of phosphatidylinositol 3-kinase/protein kinase B signal transduction. [GOC:ai]
cellular response to epidermal growth factor stimulusbiological processAny process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an epidermal growth factor stimulus. [GOC:mah]
extrinsic apoptotic signaling pathwaybiological processThe series of molecular signals in which a signal is conveyed from the cell surface to trigger the apoptotic death of a cell. The pathway starts with either a ligand binding to a cell surface receptor, or a ligand being withdrawn from a cell surface receptor (e.g. in the case of signaling by dependence receptors), and ends when the execution phase of apoptosis is triggered. [GOC:mtg_apoptosis, GOC:yaf, PMID:17340152]
positive regulation of protein localization to plasma membranebiological processAny process that activates or increases the frequency, rate or extent of protein localization to plasma membrane. [GO_REF:0000058, GOC:BHF, GOC:rl, GOC:TermGenie, PMID:11602640]
positive regulation of sprouting angiogenesisbiological processAny process that activates or increases the frequency, rate or extent of sprouting angiogenesis. [GO_REF:0000058, GOC:TermGenie, PMID:16756958]
positive regulation of vascular endothelial cell proliferationbiological processAny process that activates or increases the frequency, rate or extent of vascular endothelial cell proliferation. [GO_REF:0000058, GOC:BHF, GOC:BHF_telomere, GOC:nc, GOC:TermGenie, PMID:23201774]
negative regulation of endothelial cell apoptotic processbiological processAny process that stops, prevents or reduces the frequency, rate or extent of endothelial cell apoptotic process. [GOC:BHF, GOC:mah, GOC:mtg_apoptosis]
peptidyl-serine phosphorylationbiological processThe phosphorylation of peptidyl-serine to form peptidyl-O-phospho-L-serine. [RESID:AA0037]
intracellular signal transductionbiological processThe process in which a signal is passed on to downstream components within the cell, which become activated themselves to further propagate the signal and finally trigger a change in the function or state of the cell. [GOC:bf, GOC:jl, GOC:signaling, ISBN:3527303782]