2.7.1.127: inositol-trisphosphate 3-kinase
This is an abbreviated version!
For detailed information about inositol-trisphosphate 3-kinase, go to the full flat file.
Word Map on EC 2.7.1.127
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2.7.1.127
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1,3,4,5-tetrakisphosphate
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kawasaki
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vasculitis
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5-phosphatase
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tetrakisphosphate
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diagnostics
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medicine
- 2.7.1.127
- 1,3,4,5-tetrakisphosphate
- kawasaki
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vasculitis
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5-phosphatase
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tetrakisphosphate
- diagnostics
- medicine
Reaction
Synonyms
1D-myo-inositol-trisphosphate 3-kinase, Arg82, ArgRIII, D-myo-inositol 1,4,5-trisphosphate 3-kinase, GsIP3K-A, HsIP3K-A, inositol (1,4,5) trisphosphate 3 kinase B, inositol (1,4,5) trisphosphate 3-kinase, inositol 1,4,5-trisphosphate 3-kinase, inositol 1,4,5-trisphosphate 3-kinase A, inositol 1,4,5-trisphosphate 3-kinase B, inositol 1,4,5-trisphosphate 3-kinase C, inositol 1,4,5-trisphosphate 3-kinases, inositol 1,4,5-trisphosphate kinase, inositol 1,4,5-trisphosphate kinase 2, inositol 1,4,5-trisphosphate-3-kinase-A, inositol polyphosphate multikinase, inositol trisphosphate 3-kinase B, inositol(1,4,5)P3 3-kinase, inositol(1,4,5)trisphosphate 3-kinase, inositol(1,4,5)trisphosphate 3-kinases, inositol-1,4,5-trisphosphate 3-kinase, inositol-1,4,5-trisphosphate 3-kinase A, inositol-1,4,5-trisphosphate 3-kinase-A, inositol-1,4,5-trisphosphate-3-kinase, inositol-1,4,5-trisphosphate-3-kinase A, inositol-1,4,5-trisphosphate-3-kinase-A, inositol-trisphosphate 3-kinase B, Ins(1,4,5)P(3) 3-kinase B, Ins(1,4,5)P3 3-kinase, Ins(1,4,5)P3 3-kinase isoform B, Ins(1,4,5)P3 kinase, InsP3 3-kinase, InsP3 3-kinase A, InsP3 3-kinase B, InsP3 3-kinase C, InsP3K, InsP3KB, InsP3Kinase, IP3 3-kinase, IP3 3-kinase 2, IP3-3K, IP3K, IP3K-A, IP3K-B, IP3K-C, IP3K1, IP3K2, IP3KA, IP3KB, IP3KC, IP3kin, Ipk2, IPMK, ITPKA, Itpkb, Itpkc, kinase (phosphorylating), inositol 1,4,5-trisphosphate 3-, More, RnIP3K-C, wavy
ECTree
2.7.1.127 inositol-trisphosphate 3-kinaseAdvanced search results
results (
results (Activating Compound
Activating Compound on EC 2.7.1.127 - inositol-trisphosphate 3-kinase
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ACTIVATING COMPOUND 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
1-(2,5-dimethoxy-4-iodophenyl)-2-aminopropane
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5-HT2 agonist DOI, 3fold activation
1D-myo-inositol 1,3,4,5-tetrakisphosphate
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recombinant, catalytically active fragment of isoform C, allosteric product activation in the absence of Ca2+/calmodulin, which per se activates enzyme and abolishes the allosteric effect
Ca2+/calmodulin
for enzyme activation, Ca2+/calmodulin, 2.15 microg/ml calmodulin and 10-20 microM free CaCl2 is added to the assay mixture
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serotonin
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potentiates enzyme activity mediated through the activation of 5-HT2 receptors, enzyme up-regulation occurs through activation of PLC-coupled serotoninergic receptors and requires the phosphorylation of the enzyme by the ubiquitous multimeric protein kinase CaMKII
Triton X-100
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Antagonizing the effect of all inhibitors identified with GgIP3K-A. When 0.2% Triton X-100 is added to assays containing the respective inhibitors at IC50, the previous inhibition of GgIP3K-A is immediately reversed by an extent between 49 and 100%
Ca2+/CaM-dependent kinase II
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i.e. CaMKII, activates the enzyme by phosphorylation of Thr311
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Ca2+/CaM-dependent kinase II
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i.e. CaMKII, activates the enzyme by phosphorylation of threonine residue
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Ca2+/CaM-dependent kinase II
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i.e. CaMKII, activates the enzyme by phosphorylation at a Thr residue
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Calmodulin
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2-3fold activation of isozyme IP33K-A and 7-8fold of isozyme IP33K-B, in a Ca2+-dependent manner, the binding site contains amphiphilic alpha-helices with cluster of positively charged and hydrophobic amino acids
Calmodulin
the enzyme is activated by Ca2+/calmodulin. The human isozyme IP3-3K A contains a CaM binding domain at residues 158-183, binding structure and identification all of the key residues involved in the interaction, overview
Calmodulin
the enzyme is activated by Ca2+/calmodulin. The isozyme contains a CaM binding domain
Calmodulin
the enzyme is highly activated by Ca2+/calmodulin, ten to twentyfold increase in activity in human platelets. The isozyme contains a CaM binding domain
Calmodulin
the enzyme is activated by Ca2+/calmodulin. The isozyme contains a CaM binding domain
Calmodulin
the enzyme is highly activated by Ca2+/calmodulin. The isozyme contains a CaM binding domain
Calmodulin
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isozyme IP33K-A: 3-6fold activation in a Ca2+-dependent manner, the binding site contains amphiphilic alpha-helices with cluster of positively charged and hydrophobic amino acids, residues Ser156-Leu189 and Trp165 are required
Calmodulin
the enzyme is activated by Ca2+/calmodulin. The isozyme contains a CaM binding domain
Calmodulin
the enzyme is highly activated by Ca2+/calmodulin, two or threefold in rat brain. The isozyme contains a CaM binding domain
Calmodulin
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up to 20fold activation in a Ca2+-dependent manner, the binding site contains amphiphilic alpha-helices with cluster of positively charged and hydrophobic amino acids
CaM kinase II
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phosphorylation of isoenzyme B by calmodulin kinase II and protein kinase C added together results in a maximal 60-70fold activation, no effect on the sensitivity to the Ca2+/calmodulin complex, CaM kinase II alone activates 35-40fold in the presence of Ca2+ and calmodulin
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CaM kinase II
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phosphorylation of Thr-311 results in 8-10fold enzyme activation in the presence of 0.01 mM free Ca2+ and 0.002 mM calmodulin and in a 25fold increase in sensitivity to the Ca2+/calmodulin complex
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CaM kinase II
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phosphorylation of isoenzyme B by calmodulin kinase II and protein kinase C added together results in a maximal 60-70fold activation, no effect on the sensitivity to the Ca2+/calmodulin complex, CaM kinase II alone activates 35-40fold in the presence of Ca2+ and calmodulin
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cAMP-dependent protein kinase
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i.e. PKA, activates the enzyme by phosphorylation at a serine residue
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cAMP-dependent protein kinase
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i.e. PKA, activates the enzyme by phosphorylation at Ser109, simultaneous phosphorylation at SEr109 and Ser175 inactivates the enzyme
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cAMP-dependent protein kinase
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i.e. PKA, activates the enzyme by phosphorylation at a Ser residue
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Carbachol
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6-8fold okadaic acid-sensitive activation, maximal at 0.01 mM, isoform B, carbachol-activated isoenzyme B shows a redistribution of enzyme from soluble to particulate fraction
Carbachol
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3-5fold activation, maximal at 0.01-0.05 mM, isoenzyme A, increases the phosphorylation of enzyme
Carbachol
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6-8fold okadaic acid-sensitive activation, maximal at 0.01 mM, isoform B, carbachol-activated isoenzyme B shows a redistribution of enzyme from soluble to particulate fraction
Carbachol
activates the enzyme up to 7fold in rat brain cortical slices
protein kinase A
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isoforms A and B are differentially regulated via phosphorylation by the cAMP-dependent protein kinase, isoform A: phosphorylated to the extent of 0.9 mol/mol, 2.5fold stimulation in the absence of Ca2+/calmodulin, 1.5fold stimulation in the presence of Ca2+/calmodulin, isoform B: phosphorylated to the extent of 1 mol/mol, no effect on activity in the absence of Ca2+/calmodulin, 45% inhibition in the presence of Ca2+/calmodulin
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Protein kinase C
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phosphorylation of isoenzyme B by calmodulin kinase II and protein kinase C added together results in a maximal 60-70fold activation, but protein kinase C alone inhibits in the presence of Ca2+ and calmodulin, no effect on the sensitivity to the Ca2+/calmodulin complex
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Protein kinase C
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phosphorylation of isoenzyme B by calmodulin kinase II and protein kinase C added together results in a maximal 60-70fold activation, but protein kinase C alone inhibits in the presence of Ca2+ and calmodulin, no effect on the sensitivity to the Ca2+/calmodulin complex
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UTP
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6-8fold okadaic acid-sensitive activation, maximal at 0.01 mM, isoform B, calphostin C, KN-93 or KN-62 partially prevents activation, UTP-activated isoenzyme B shows a redistribution of enzyme from soluble to particulate fraction
additional information
the enzyme is stimulated by purinergic agonists in human astrocytoma cells
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additional information
the enzyme is stimulated by purinergic agonists in human astrocytoma cells
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additional information
the enzyme is stimulated by purinergic agonists in human astrocytoma cells
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additional information
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the enzyme is stimulated by purinergic agonists in human astrocytoma cells
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additional information
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enhanced inositol 1,4,5-trisphosphate 3-kinase A in the synaptic field by long-term potentiation induction in rat hippocampal neurons
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additional information
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isoenzymes A and B are not activated by protein kinase A
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additional information
enhanced IP3K-A IR in the synaptic field by long-term potentiation induction in rat hippocampal neurons
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additional information
phosphorylation activates the activity of isozyme Itpka
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additional information
phosphorylation activates the activity of isozyme Itpka
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additional information
phosphorylation activates the activity of isozyme Itpka
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