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Ligand 1D-myo-inositol 1,4,5-trisphosphate

Basic Ligand Information

Molecular Structure

Related pathways

Pathway Source

Pathways

KEGG

Adrenergic signaling in cardiomyocytes, African trypanosomiasis, AGE-RAGE signaling pathway in diabetic complications, Aldosterone synthesis and secretion, Alzheimer disease, Amoebiasis, Apelin signaling pathway, B cell receptor signaling pathway, C-type lectin receptor signaling pathway, Calcium signaling pathway, cAMP signaling pathway, cGMP-PKG signaling pathway, Chagas disease, Chemokine signaling pathway, Cholinergic synapse, Cortisol synthesis and secretion, Cushing syndrome, Dopaminergic synapse, Endocrine and other factor-regulated calcium reabsorption, Epstein-Barr virus infection, ErbB signaling pathway, Estrogen signaling pathway, Fc epsilon RI signaling pathway, Fc gamma R-mediated phagocytosis, Gap junction, Gastric acid secretion, Glioma, Glucagon signaling pathway, Glutamatergic synapse, GnRH secretion, GnRH signaling pathway, Growth hormone synthesis, secretion and action, Hepatocellular carcinoma, HIF-1 signaling pathway, Human cytomegalovirus infection, Human immunodeficiency virus 1 infection, Huntington disease, Inflammatory mediator regulation of TRP channels, Inositol phosphate metabolism, Insulin secretion, Kaposi sarcoma-associated herpesvirus infection, Lipid and atherosclerosis, Long-term depression, Long-term potentiation, MAPK signaling pathway, Melanogenesis, Natural killer cell mediated cytotoxicity, Neurotrophin signaling pathway, Neutrophil extracellular trap formation, NF-kappa B signaling pathway, NOD-like receptor signaling pathway, Non-small cell lung cancer, Oocyte meiosis, Osteoclast differentiation, Oxytocin signaling pathway, Pancreatic secretion, Parathyroid hormone synthesis, secretion and action, Parkinson disease, Pathways in cancer, Pathways of neurodegeneration - multiple diseases, PD-L1 expression and PD-1 checkpoint pathway in cancer, Phosphatidylinositol signaling system, Phospholipase D signaling pathway, Phototransduction - fly, Platelet activation, Ras signaling pathway, Relaxin signaling pathway, Renin secretion, Retrograde endocannabinoid signaling, Salivary secretion, Serotonergic synapse, Shigellosis, Sphingolipid signaling pathway, Spinocerebellar ataxia, T cell receptor signaling pathway, Taste transduction, Th1 and Th2 cell differentiation, Th17 cell differentiation, Thyroid hormone signaling pathway, Thyroid hormone synthesis, Vascular smooth muscle contraction, VEGF signaling pathway, Vibrio cholerae infection, Yersinia infection more

MetaCyc

1D-myo-inositol hexakisphosphate biosynthesis I (from Ins(1,4,5)P3), 1D-myo-inositol hexakisphosphate biosynthesis II (mammalian), 2-arachidonoylglycerol biosynthesis, D-myo-inositol (1,3,4)-trisphosphate biosynthesis, D-myo-inositol (1,4,5)-trisphosphate biosynthesis, D-myo-inositol (1,4,5)-trisphosphate degradation, D-myo-inositol-5-phosphate metabolism, phosphatidate metabolism, as a signaling molecule, phospholipases more

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (9 results)

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Show Natural Substrate (9 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.7.1.127

ATP + 1D-myo-inositol 1,4,5-triphosphate = ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate

687650

-

2.7.1.127

ATP + 1D-myo-inositol 1,4,5-trisphosphate = ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate

640752, 640758, 640759, 640731, 640732, 640757, 640761, 640747, 640760, 640741, 640755, 640756, 640746, 640736, 640734, 640739, 640753, 640742, 640743, 640749, 640750, 640754, 640735, 640748, 662346, 661488, 661446, 663226, 662827, 676129, 673012, 687650, 699006, 699348, 700975, 699694, 737402, 737593, 737647, 737961, 738022, 738216, 737403, 737400, 738088, 739679, 760741, 762015, 761786, 761191, 760540, 762237

-

2.7.1.151

2 ATP + 1D-myo-inositol 1,4,5-trisphosphate = 2 ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate

686905

-

2.7.1.151

ATP + 1D-myo-inositol 1,4,5-trisphosphate = ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate

662114, 662391, 661446, 686905, 737989, 761469

-

2.7.1.151

ATP + 1D-myo-inositol 1,4,5-trisphosphate = ADP + 1D-myo-inositol 1,4,5,6-tetrakisphosphate

662114, 662391, 661446, 662346, 739703, 739065, 737989

-

2.7.1.151

3 ATP + 2 1D-myo-inositol 1,4,5-trisphosphate = 3 ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate

686905

-

3.1.3.56

1D-myo-inositol 1,4,5-trisphosphate + H2O = 1D-myo-inositol 1,4-bisphosphate + phosphate

666585, 665580, 665810, 666645, 663839

-

3.1.3.56

1D-myo-inositol 1,4,5-trisphosphate + H2O = myo-inositol 1,4-bisphosphate + phosphate

729621

-

3.1.3.56

D-myo-inositol 1,4,5-trisphosphate + H2O = D-myo-inositol 1,4-bisphosphate + phosphate

646372, 646379, 646384, 646380, 646383, 646391, 646378, 646400, 646377, 646382, 646385, 646389, 646392, 646393, 646395, 646396, 646397, 646398, 646403, 646375, 646376, 646381, 646399, 586935, 646373, 646374, 646386, 646387, 646388, 646402, 646404, 646394, 646401

-

2.7.1.127

2 entries

2.7.1.151

4 entries

3.1.3.56

3 entries

In Vivo Product in Enzyme-catalyzed Reactions (5 results)

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Show Natural Product (5 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

3.1.3.62

D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O = D-myo-inositol 1,4,5-trisphosphate + phosphate

646429

-

3.1.4.11

1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-triphosphate + diacylglycerol

-

-

3.1.4.11

1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol

652082, 653348, 650333, 650433, 652651, 649088, 649261, 649330, 652515, -

-

3.1.4.11

phosphatidylinositol 4,5-bisphosphate + H2O = D-myo-inositol 1,4,5-trisphosphate + diacylglycerol

135143

-

3.1.4.11

3 entries

3.1.4.3

phosphatidylinositol-bisphosphate + H2O = inositol 1,4,5-trisphosphate + 1,2-diacylglycerol

135282, 135283, 135284, 135288, 135290, 135291, 135287, 135285

-

Substrate in Enzyme-catalyzed Reactions (23 results)

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Show Substrate (23 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.7.1.127

ATP + 1D-myo-inositol 1,4,5-triphosphate = ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate

687650

-

2.7.1.127

ATP + 1D-myo-inositol 1,4,5-trisphosphate = ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate

640744, 640745, 640752, 640733, 640734, 640751, 640755, 640735, 640736, 640737, 640738, 640739, 640746, 640749, 640753, 640757, 640742, 640743, 640740, 640741, 640754, 640732, 640747, 640759, 640761, 640758, 640756, 640748, 640750, 640731, 640760, 662346, 661488, 661446, 663226, 662827, 660884, 663233, 660978, 661334, 662828, 676129, 673012, 687650, 699006, 699348, 700975, 699694, 737402, 737593, 737647, 737961, 738022, 738216, 737403, 737400, 738088, 739679, 760741, 762015, 761786, 761191, 760540, 762237

-

2.7.1.127

2 entries

2.7.1.140

ATP + myo-inositol 1,4,5-trisphosphate = ADP + myo-inositol-1,3,4,5-tetrakisphosphate

640974

-

2.7.1.151

2 ATP + 1D-myo-inositol 1,4,5-trisphosphate = 2 ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate

660946, 686905

-

2.7.1.151

ATP + 1D-myo-inositol 1,4,5-trisphosphate = ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate

662114, 662391, 661446, 660926, 660946, 640974, 686905, 737989, 761469

-

2.7.1.151

ATP + 1D-myo-inositol 1,4,5-trisphosphate = ADP + 1D-myo-inositol 1,3,4,6-tetrakisphosphate

640974

-

2.7.1.151

ATP + 1D-myo-inositol 1,4,5-trisphosphate = ADP + 1D-myo-inositol 1,4,5,6-tetrakisphosphate

662114, 662391, 661446, 662346, 660946, 662119, 722781, 739703, 739065, 737989

-

2.7.1.151

3 ATP + 2 1D-myo-inositol 1,4,5-trisphosphate = 3 ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate

686905

-

2.7.1.151

inositol (1,4,5)-triphosphate + ATP = inositol (1,3,4,5)-tetrakisphosphate + ADP

393223

-

2.7.1.151

inositol (1,4,5)-triphosphate + ATP = inositol (1,3,4,5)-tetrakisphosphate + inositol (1,4,5,6)-tetrakisphosphate + ADP

393222

-

2.7.1.151

ATP + inositol 1,4,5-trisphosphate = ADP + inositol (1,3,4,5)-tetrakisphosphate

660926

-

2.7.1.151

8 entries

2.7.1.158

ATP + 1D-myo-inositol 1,4,5-trisphosphate = ADP + 1D-myo-inositol 1,4,5,6-tetrakisphosphate + 1D-myo-inositol 1,3,4,5-tetrakisphosphate

660942

-

3.1.3.2

inositol 1,4,5-triphosphate + H2O = ?

134783

-

3.1.3.36

1D-myo-inositol 1,4,5-trisphosphate + H2O = 1D-myo-inositol 1,4-bisphosphate + phosphate

665575, 664945, 666576, 666585, 678188, 682328, 691787

-

3.1.3.36

myo-inositol 1,4,5-trisphosphate + H2O = inositol 1,4-diphosphate + phosphate

134819, 134810, 134820, 134823, 134811

-

3.1.3.56

1D-myo-inositol 1,4,5-trisphosphate + H2O = 1D-myo-inositol 1,4-bisphosphate + phosphate

666585, 665580, 665810, 666645, 663839, 665575, 694699, 772168

-

3.1.3.56

1D-myo-inositol 1,4,5-trisphosphate + H2O = 1D-myo-inositol 1,4-disphosphate + phosphate

679206, 682680

-

3.1.3.56

1D-myo-inositol 1,4,5-trisphosphate + H2O = myo-inositol 1,4-bisphosphate + phosphate

729621

-

3.1.3.56

D-myo-inositol 1,4,5-trisphosphate + H2O = D-myo-inositol 1,4-bisphosphate + phosphate

646400, 646372, 646377, 646379, 646382, 646385, 646389, 646392, 646393, 646395, 646396, 646397, 646398, 646403, 646375, 646376, 646381, 646399, 646384, 646391, 586935, 646373, 646374, 646380, 646383, 646386, 646387, 646388, 646378, 646402, 646404, 646394, 646401

-

3.1.3.56

D-myo-inositol 1,4,5-trisphosphate + H2O = myo-inositol 1,4-bisphosphate + phosphate

772168

-

3.1.3.36

2 entries

3.1.3.56

5 entries

3.1.3.57

inositol 1,4,5-trisphosphate + H2O = ? + phosphate

702183

-

3.1.3.7

D-myo-inositol-1,4,5-trisphosphate + H2O = ?

677696

-

3.1.3.78

inositol 1,4,5-trisphosphate + H2O = inositol 1,5-bisphosphate + phosphate

697606

-

Product in Enzyme-catalyzed Reactions (12 results)

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Show Product (12 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.7.1.151

inositol (4,5)-bisphosphate + ATP = inositol (1,4,5)-trisphosphate + ADP

393223

-

2.7.1.151

inositol bisphosphate + ATP = inositol trisphosphate + ADP

393219

-

2.7.1.151

2 entries

3.1.3.62

D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O = D-myo-inositol 1,4,5-trisphosphate + phosphate

646428, 646436, 646381, 646431, 646432, 646435, 646438, 646384, 646429, 646434, 646437, -

-

3.1.3.67

inositol 1,3,4,5-tetrakisphosphate + H2O = inositol 1,4,5-trisphosphate + phosphate

650767, 651881

-

3.1.4.11

1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-triphosphate + diacylglycerol

-

-

3.1.4.11

phosphatidylinositol 4,5-bisphosphate + H2O = diacylglycerol + 1D-myo-inositol 1,4,5-triphosphate

-

-

3.1.4.11

1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol

653442, 649261, 652208, 650986, 653195, 652651, 653241, 650433, 651282, 649330, 652515, 649762, 650333, 650786, 653348, 649088, 652082, 649997, -

-

3.1.4.11

1D-myo-inositol 1,4,5-trisphosphate fluorescent derivative WH-15 + H2O = 1D-myo-inositol 1,4,5-trisphosphate + quinomethide + 6-aminoquinoline + ?

-

-

3.1.4.11

phosphatidylinositol 4,5-bisphosphate + H2O = D-myo-inositol 1,4,5-trisphosphate + diacylglycerol

135130, 135120, 135121, 135143, 135136, 135123, -

-

3.1.4.11

phosphatidylinositol 4,5-bisphosphate = inositol 1,4,5-trisphosphate

-

-

3.1.4.11

1-stearoyl-2-arachidonoyl-phosphatidylinositol 4,5-bisphosphate + H2O = myo-inositol 1,4,5-trisphosphate + 1-stearoyl-2-arachidonoyl-glycerol

-

-

3.1.4.11

7 entries

3.1.4.3

phosphatidylinositol-bisphosphate + H2O = inositol 1,4,5-trisphosphate + 1,2-diacylglycerol

135282, 135283, 135284, 135288, 135290, 135291, 135287, 649812, 135285

-

Activator in Enzyme-catalyzed Reactions (1 result)

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Show Activating Compound (1 entry)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

3.4.24.56

activates, maximal 30.6fold activation

755263

-

Inhibitor in Enzyme-catalyzed Reactions (10 results)

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Show Inhibitors (10 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

2.7.1.127

recombinant, catalytically active fragment of isoform C, substrate inhibition by high concentrations

640761

-

2.7.1.127

substrate inhibition of the catalytic domain

662827

-

2.7.1.127

strong inhibition, purified recombinant enzyme, IC50 value is 0.003 mM in absence of Ca2+

661334

-

2.7.1.134

0.1 mM, more than 80% inhibition

640818

-

2.7.1.134

competitive inhibition

640817

-

2.7.1.127

3 entries

2.7.1.134

2 entries

2.7.1.151

IC50: 0.1 mM

673651

-

2.7.4.21

IC50 for ATP synthase activity is 0.253 mM

642551

-

3.1.3.62

0.05 mM, about 50% inhibition

646381

-

3.1.3.62

product inhibition kinetics

646429, 646432

-

3.1.3.62

2 entries

4.6.1.2

-

34826

-

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (1 result)

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Show Turnover Number (1 entry)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

3.1.3.56

340

-

37°C

646386

K_M Value (58 results)

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Show KM Value (58 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

2.7.1.127

0.0002

-

pH 7.5, 30°C, recombinant, catalytically active fragment of isoform C

640761

2.7.1.127

0.0002

-

recombinant catalytic/CaM binding domain, pH 7.5, 30°C

662346

2.7.1.127

0.0002

-

recombinant enzyme IP3K-C fragment comprising calmodulin binding domain and catalytic domain

687650

2.7.1.127

0.00021

-

pH 7.1, 30°C, addition of Ca2+/calmodulin increases the Km 2fold

640735

2.7.1.127

0.0004

-

pH 7.2, 37°C

640742

2.7.1.127

0.0004

-

recombinant enzyme fragment comprising calmodulin binding domain

687650

2.7.1.127

0.0004

-

recombinant wild-type catalytic/CaM binding domain, pH 7.5, 30°C

662346

2.7.1.127

0.00047

-

recombinant mutant K268E catalytic/CaM binding domain, pH 7.5, 30°C

662346

2.7.1.127

0.00054

-

IP3K-A K336Q mutant

687650

2.7.1.127

0.00054

-

recombinant mutant K272D catalytic/CaM binding domain, pH 7.5, 30°C

662346

2.7.1.127

0.00056

-

pH 7.2, 37°C, in presence or absence of 50 nM calmodulin

640750

2.7.1.127

0.0006

-

brain enzyme

640732

2.7.1.127

0.00076

-

pH 7.4, 37°C

640734

2.7.1.127

0.001

0.002

pH 7.5, 37°C

640741

2.7.1.127

0.0015

-

isoform B

640758

2.7.1.127

0.0016

-

25°C

640747

2.7.1.127

0.0017

-

recombinant catalytic binding domain, pH 7.5, 30°C

662346

2.7.1.127

0.0017

-

recombinant enzyme IP3K-C fragment comprising catalytic domain

687650

2.7.1.127

0.002

-

pH 7.4, 37°C, platelet enzyme

640733

2.7.1.127

0.002

0.005

pH 7.5, 37°C, recombinant isoenzymes A and B

640759

2.7.1.127

0.0021

-

recombinant IP3K, in absence of Ca2+/calmodulin, 37°C

640749

2.7.1.127

0.004

-

37°C, isoform A

640756

2.7.1.127

0.004

-

pH 7.4

640756

2.7.1.127

0.004

-

pH 7.5

640756

2.7.1.127

0.011

-

pH 7.5, 37°C, in absence of 2,3-bisphosphoglycerate

640737

2.7.1.127

25 entries

2.7.1.140

0.00011

-

pH 7.2, 37°C

640974

2.7.1.151

0.00011

-

recombinant enzyme, pH 7.2, 37°C

660926, 640974

2.7.1.151

0.000112

-

37°C, pH 7.2

660926

2.7.1.151

0.00028

-

pH 7.8, 30°C, 0.5 mM ATP, recombinant enzyme

660946

2.7.1.151

0.00035

-

recombinant wild-type enzyme, pH 7.5, 30°C

662346

2.7.1.151

0.0004

-

recombinant deletion mutant enzyme, pH 7.5, 30°C

662346

2.7.1.151

0.015

-

pH 7.5, 37°C, recombinant isozyme Ipk2alpha

662119

2.7.1.151

0.05

-

mutant K121W, pH 6.6, 30°C

722781

2.7.1.151

0.162

-

wild-type, pH 6.6, 30°C

722781

2.7.1.151

8 entries

2.7.1.158

0.00055

-

about, cosubstrate: ATP

660942

3.1.3.36

0.123

-

-

134820

3.1.3.36

0.421

-

-

678188

3.1.3.56

0.001

-

pH 7.4, 37°C

646373

3.1.3.56

0.003

-

type I enzyme, pH 7.1, 30°C

646376

3.1.3.56

0.006

-

pH 6.5, 37°C

646377

3.1.3.56

0.0089

-

type I enzyme, pH 7.5, 37°C

646391

3.1.3.56

0.0105

-

37°C

646386

3.1.3.56

0.014

-

membrane associated enzyme, pH 7.2, 37°C

646392

3.1.3.56

0.016

0.019

-

646379

3.1.3.56

0.016

0.019

membrane bound enzyme, pH 7.2, 30°C

646378

3.1.3.56

0.018

-

particulate enzyme

646387

3.1.3.56

0.018

-

type II enzyme, pH 7.1, 30°C

646376

3.1.3.56

0.019

-

soluble enzyme

646387

3.1.3.56

0.021

-

native enzyme

646396

3.1.3.56

0.022

-

membrane associated enzyme, pH 7.2, 37°C

646392

3.1.3.56

0.024

-

soluble enzyme, pH 7.2, 30°C

646378

3.1.3.56

0.025

-

pH 7.0, 37°C

646372

3.1.3.56

0.028

-

recombinant enzyme from E. coli

646374

3.1.3.56

0.029

-

pH 7.4, 37°C

586935

3.1.3.56

0.032

-

-

646402

3.1.3.56

0.0714

-

type II enzyme, pH 7.5, 37°C

646391

3.1.3.56

0.205

-

R343A mutant

646396

3.1.3.56

0.32

-

R350A mutant

646396

3.1.3.36

2 entries

3.1.3.56

21 entries

K_i Value (3 results)

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Show KI Value (3 entries)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

2.7.1.134

0.048

-

pH 7.2, 37°C

640817

2.7.1.151

0.002

-

-

673651

3.1.3.62

0.002

-

pH 7.4, 37°C

646429

IC₅₀ Value (2 results)

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Show IC50 Value (2 entries)

EC NUMBER

IC50 VALUE

IC50 VALUE MAXIMUM

COMMENTARY

LITERATURE

2.7.1.127

0.003

-

strong inhibition, purified recombinant enzyme, IC50 value is 0.003 mM in absence of Ca2+

661334

2.7.1.151

0.1

-

IC50: 0.1 mM

673651

References & Links

Literature References (194)

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Show Reference (194 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

34826

2892490

A magnesium-dependent guanylate cyclase in cell-free preparations of Dictyostelium discoideum

1988

Janssens, P.M.V.; de Jong, C.C.C.

Biochem. Biophys. Res. Commun.

150

405-411

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Song, E.S.; Jang, H.; Guo, H.F.; Juliano, M.A.; Juliano, L.; Morris, A.J.; Galperin, E.; Rodgers, D.W.; Hersh, L.B.

Proc. Natl. Acad. Sci. USA

114

E2826-E2835

760540

28377279

Inositol-1,4,5-trisphosphate 3-kinase-A (ITPKA) is frequently over-expressed and functions as an oncogene in several tumor types

2017

Windhorst, S.; Song, K.; Gazdar, A.F.

Biochem. Pharmacol.

137

1-9

760540

28377279

Inositol-1,4,5-trisphosphate 3-kinase-A (ITPKA) is frequently over-expressed and functions as an oncogene in several tumor types

2017

Windhorst, S.; Song, K.; Gazdar, A.F.

Biochem. Pharmacol.

137

1-9

760741

27582507

miR-140-5p attenuates chemotherapeutic drug-induced cell death by regulating autophagy through inositol 1,4,5-trisphosphate kinase 2 (IP3k2) in human osteosarcoma cells

2016

Wei, R.; Cao, G.; Deng, Z.; Su, J.; Cai, L.

Biosci. Rep.

36

art:e00392

760741

27582507

miR-140-5p attenuates chemotherapeutic drug-induced cell death by regulating autophagy through inositol 1,4,5-trisphosphate kinase 2 (IP3k2) in human osteosarcoma cells

2016

Wei, R.; Cao, G.; Deng, Z.; Su, J.; Cai, L.

Biosci. Rep.

36

art:e00392

761191

26613949

The wavy mutation maps to the inositol 1,4,5-Trisphosphate 3-Kinase 2 (IP3K2) gene of drosophila and interacts with IP3R to affect wing development

2016

Dean, D.; Maroja, L.; Cottrill, S.; Bomkamp, B.; Westervelt, K.; Deitcher, D.

G3 (Bethesda)

6

299-310

761191

26613949

The wavy mutation maps to the inositol 1,4,5-Trisphosphate 3-Kinase 2 (IP3K2) gene of drosophila and interacts with IP3R to affect wing development

2016

Dean, D.; Maroja, L.; Cottrill, S.; Bomkamp, B.; Westervelt, K.; Deitcher, D.

G3 (Bethesda)

6

299-310

761469

28882892

Structural features of human inositol phosphate multikinase rationalize its inositol phosphate kinase and phosphoinositide 3-kinase activities

2017

Wang, H.; Shears, S.B.

J. Biol. Chem.

292

18192-18202

761469

28882892

Structural features of human inositol phosphate multikinase rationalize its inositol phosphate kinase and phosphoinositide 3-kinase activities

2017

Wang, H.; Shears, S.B.

J. Biol. Chem.

292

18192-18202

760540

2 entries

760741

2 entries

761191

2 entries

761469

2 entries

761786

27018448

Computational biology analysis of platelet signaling reveals roles of feedbacks through phospholipase C and inositol 1,4,5-trisphosphate 3-kinase in controlling amplitude and duration of calcium oscillations

2016

Balabin, F.A.; Sveshnikova, A.N.

Mathr. Biosci.

276

67-74

762015

32593773

Physiological relevance of the neuronal isoform of inositol-1,4,5-trisphosphate 3-kinases in mice

2020

Blechner, C.; Becker, L.; Fuchs, H.; Rathkolb, B.; Prehn, C.; Adler, T.; Calzada-Wack, J.; Garrett, L.; Gailus-Durner, V.; Morellini, F.; Conrad, S.; Hoelter, S.M.; Wolf, E.; Klopstock, T.; Adamski, J.; Busch, D.; de Angelis, M.H.; Schmeisser, M.J.; Windhorst, S.

Neurosci. Lett.

735

135206

762015

32593773

Physiological relevance of the neuronal isoform of inositol-1,4,5-trisphosphate 3-kinases in mice

2020

Blechner, C.; Becker, L.; Fuchs, H.; Rathkolb, B.; Prehn, C.; Adler, T.; Calzada-Wack, J.; Garrett, L.; Gailus-Durner, V.; Morellini, F.; Conrad, S.; Hoelter, S.M.; Wolf, E.; Klopstock, T.; Adamski, J.; Busch, D.; de Angelis, M.H.; Schmeisser, M.J.; Windhorst, S.

Neurosci. Lett.

735

135206

762237

29617377

Inositol 1,4,5-trisphosphate 3-kinase A overexpressed in mouse forebrain modulates synaptic transmission and mGluR-LTD of CA1 pyramidal neurons

2018

Choi, B.; Lee, H.W.; Mo, S.; Kim, J.Y.; Kim, H.W.; Rhyu, I.J.; Hong, E.; Lee, Y.K.; Choi, J.S.; Kim, C.H.; Kim, H.

PLoS ONE

13

e0193859

762237

29617377

Inositol 1,4,5-trisphosphate 3-kinase A overexpressed in mouse forebrain modulates synaptic transmission and mGluR-LTD of CA1 pyramidal neurons

2018

Choi, B.; Lee, H.W.; Mo, S.; Kim, J.Y.; Kim, H.W.; Rhyu, I.J.; Hong, E.; Lee, Y.K.; Choi, J.S.; Kim, C.H.; Kim, H.

PLoS ONE

13

e0193859

762015

2 entries

762237

2 entries

772168

31426386

The function of inositol phosphatases in plant tolerance to abiotic stress

2019

Jia, Q.; Kong, D.; Li, Q.; Sun, S.; Song, J.; Zhu, Y.; Liang, K.; Ke, Q.; Lin, W.; Huang, J.

Int. J. Mol. Sci.

20

3999

Links to other databases for 1D-myo-inositol 1,4,5-trisphosphate

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