Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
ATP + 1D-myo-inositol 1,4,5-triphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
-
r
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
ATP + 1D-myo-inositol 2,4,5-trisphosphate
ADP + 1D-myo-inositol 2,4,5,6-tetrakisphosphate
-
recombinant, catalytically active fragment of isoform C, in the presence of Ins(1,3,4,5)P4, authentic side activity of isoform C
-
?
ATP + D-2-deoxy-myo-inositol 1,4,5-trisphosphate
ADP + D-2-deoxy-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
-
-
?
additional information
?
-
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
reducing the influx of calcium released from endoplasmic reticulum via IP3 receptor signaling
-
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
multiple regulation mechanisms of enzyme isoform A and B
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
domain structure of IP3K-C
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
regulatory mechanism of isoenzyme B involving phosphorylation by both protein kinase C and CaM kinase II
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
regulation mechanism of isoenzyme A involving CaM kinase II-mediated phosphorylation
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
environment of the active site, proposed binding site model for Ins(1,4,5)P3
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
also phosphorylates the 1,2-cyclic form of myo-inositol 1,4,5-trisphosphate
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
specific for phosphorylation of the 3-position
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
specific for phosphorylation of the 3-position
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
enzyme is specific for phosphorylating the position 3 of the myo-inositol ring and requires vicinal phosphates in the 4 and 5 positions
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
isoform A: N-terminal 66-amino acid F-actin-binding region
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
differential expression and regulation of the two enzyme isoforms A and B provides multiple mechanisms for regulating the cytosolic level of inositol 1,4,5-trisphosphate in cells, regulation mechanisms
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
inositol 1,4,5-trisphosphate and inositol 1,3,4,5-tetrakisphosphate have separate second messenger roles, perhaps both relating to Ca2+-signaling events
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
inositol 1,4,5-trisphosphate is a second messenger
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
inositol 1,4,5-trisphosphate is a second messenger
-
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
inositol 1,4,5-trisphosphate is a second messenger
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
inositol 1,4,5-trisphosphate is a second messenger
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
inositol 1,4,5-trisphosphate is a second messenger
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
inositol 1,4,5-trisphosphate is a second messenger
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
phosphorylation of IP3 in dentritic spines to produce IP4 is important for modulating the compartmentalization of calcium at synapses, control of calcium signals, the rapid, localized synthesis of IP4 may have complex effects on cytosolic calcium and on the molecular mechanisms that control learning and memory
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
IP3K regulates the intracellular level of the 2 second messengers Ins(1,4,5)P3 and Ins(1,3,4,5)P4
-
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
regulation mechanism of isoenzyme A in brain involving CaM kinase II-mediated phosphorylation, role of Ins(1,4,5)P3 3-kinase in brain
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
IP3K isoform C: nucleocytoplasmic shuttling, particular role in nuclear inositol trisphosphate phosphorylation and cellular growth, enzyme seems to function during the intervalls between signaling events, keeps the resting Ins(1,4,5)P3 very low and provides a basal Ins(1,3,4,5)P4 production in the absence of stimulatory signals from the exterior
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
enzyme occupies a central position in inositol phosphate metabolism by terminating the Ca2+ mobilizing of InsP3 and by generating InsP4
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
inositol tris/tetrakisphosphate pathway
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
isoform B may play a significant role in the regulation of Ins(1,4,5)P3 levels, and consequently in Ca2+ responses following stimulation of cells with Ins(1,4,5)P3-elevating agonists
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
inositol 1,4,5-trisphosphate mobilizes Ca2+ from the intracellular stores of permeabilized cells, enzyme is Ca2+-regulated
-
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
important regulatory role in inositol phosphate signaling by promoting the formation of additional inositol polyphosphate isomers
-
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
inositol phosphate metabolism
-
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
inositol phosphate metabolism
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
inositol phosphate metabolism
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
inositol phosphate metabolism
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
involved in inositol polyphosphate metabolism
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
involved in inositol polyphosphate metabolism
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
involved in inositol polyphosphate metabolism
-
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
the enzyme plays a key role in maintaining Ca2+ homeostasis by regulating the concentrations of 1D-myo-inositol 1,4,5-trisphosphate and 1D-myo-inositol 1,3,4,5-tetrakisphosphate, the enzyme has an important regulatory function in the inositol phosphate metabolism which is important for several cellular functions and signaling, overview
-
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
inositol phosphate 3-kinase reaction of the inositol polyphosphate multikinase, EC 2.7.1.151
-
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
InsP3K activity is a determinant of the extent of basal Ras activation in mast cells and of the Ras activation that follows antigenic crosslinking of the FcepsilonRI
-
-
?
additional information
?
-
-
not: GTP, 5'-guanylylimidodiphosphate
-
-
?
additional information
?
-
-
the enzyme might be involved in brain development, memory, and learning
-
-
?
additional information
?
-
the enzyme binds to F-actin in the cellular actin cytoskeleton with its F-actin domain at the N-terminus, the C-terminal fragment cannot bind to F-actin
-
-
?
additional information
?
-
-
the enzyme contains a catalytic domain and a 4-helix substrate binding domain, both are in an open conformation with respect to each other, thus substrate recognition and catalysis involve a dynamic conformational cycle
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
ATP + 1D-myo-inositol 1,4,5-triphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
-
r
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
additional information
?
-
-
the enzyme might be involved in brain development, memory, and learning
-
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
reducing the influx of calcium released from endoplasmic reticulum via IP3 receptor signaling
-
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
regulatory mechanism of isoenzyme B involving phosphorylation by both protein kinase C and CaM kinase II
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
differential expression and regulation of the two enzyme isoforms A and B provides multiple mechanisms for regulating the cytosolic level of inositol 1,4,5-trisphosphate in cells, regulation mechanisms
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
inositol 1,4,5-trisphosphate and inositol 1,3,4,5-tetrakisphosphate have separate second messenger roles, perhaps both relating to Ca2+-signaling events
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
inositol 1,4,5-trisphosphate is a second messenger
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
inositol 1,4,5-trisphosphate is a second messenger
-
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
inositol 1,4,5-trisphosphate is a second messenger
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
inositol 1,4,5-trisphosphate is a second messenger
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
inositol 1,4,5-trisphosphate is a second messenger
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
inositol 1,4,5-trisphosphate is a second messenger
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
phosphorylation of IP3 in dentritic spines to produce IP4 is important for modulating the compartmentalization of calcium at synapses, control of calcium signals, the rapid, localized synthesis of IP4 may have complex effects on cytosolic calcium and on the molecular mechanisms that control learning and memory
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
IP3K regulates the intracellular level of the 2 second messengers Ins(1,4,5)P3 and Ins(1,3,4,5)P4
-
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
regulation mechanism of isoenzyme A in brain involving CaM kinase II-mediated phosphorylation, role of Ins(1,4,5)P3 3-kinase in brain
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
IP3K isoform C: nucleocytoplasmic shuttling, particular role in nuclear inositol trisphosphate phosphorylation and cellular growth, enzyme seems to function during the intervalls between signaling events, keeps the resting Ins(1,4,5)P3 very low and provides a basal Ins(1,3,4,5)P4 production in the absence of stimulatory signals from the exterior
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
enzyme occupies a central position in inositol phosphate metabolism by terminating the Ca2+ mobilizing of InsP3 and by generating InsP4
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
inositol tris/tetrakisphosphate pathway
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
isoform B may play a significant role in the regulation of Ins(1,4,5)P3 levels, and consequently in Ca2+ responses following stimulation of cells with Ins(1,4,5)P3-elevating agonists
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
inositol 1,4,5-trisphosphate mobilizes Ca2+ from the intracellular stores of permeabilized cells, enzyme is Ca2+-regulated
-
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
important regulatory role in inositol phosphate signaling by promoting the formation of additional inositol polyphosphate isomers
-
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
inositol phosphate metabolism
-
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
inositol phosphate metabolism
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
inositol phosphate metabolism
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
inositol phosphate metabolism
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
involved in inositol polyphosphate metabolism
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
involved in inositol polyphosphate metabolism
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
involved in inositol polyphosphate metabolism
-
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
the enzyme plays a key role in maintaining Ca2+ homeostasis by regulating the concentrations of 1D-myo-inositol 1,4,5-trisphosphate and 1D-myo-inositol 1,3,4,5-tetrakisphosphate, the enzyme has an important regulatory function in the inositol phosphate metabolism which is important for several cellular functions and signaling, overview
-
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
InsP3K activity is a determinant of the extent of basal Ras activation in mast cells and of the Ras activation that follows antigenic crosslinking of the FcepsilonRI
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(2'S)-1D-1,2-O-[(2'-phosphoryloxy)propane-1',3'-diyl]-myo-inositol 4,5-bisphosphate
-
synthetic bicyclic inositol trisphosphate S epimer, IC50 is 0.156 mM
1D-myo-inositol 1,3,4,5-tetrakisphosphate
1D-myo-inositol 1,4,5-trisphosphate
-
recombinant, catalytically active fragment of isoform C, substrate inhibition by high concentrations
3',4',7,8-tetrahydroxyflavone
D-2-deoxyinositol 1,3,4,5-tetrakisphosphate
-
strong inhibition of isozyme A, IC50 is 0.0054 mM
D-2-deoxyinositol 1,4,5-trisphosphate
-
strong inhibition of isozyme A, IC50 is 0.0017 mM
D-3-deoxyinositol 1,4,6-trisphosphate
-
strong inhibition of isozyme A, IC50 is 0.0014 mM
D-6-deoxyinositol 1,3,4,5-tetrakisphosphate
-
strong inhibition of isozyme A, IC50 is 0.0051 mM
D-myo-inositol 1,4,5-trisphosphate
-
strong inhibition, purified recombinant enzyme, IC50 value is 0.003 mM in absence of Ca2+
D-myo-inositol 2,4,5-trisphosphate
-
IC50 is 0.117 mM
D-scyllo-inositol 1,2,3,4-tetrakisphosphate
-
purified recombinant enzyme, IC50 value is above 0.1 mM in absence of Ca2+
D-scyllo-inositol 1,2,4-trisphosphate
-
purified recombinant enzyme, IC50 value is 0.044 mM in absence of Ca2+
EGTA
-
Ca2+/calmodulin-activated enzyme
epigallocatechin-3-gallate
inositol phosphate
-
inhibitory effects of all possible 38 regioisomers of synthetic inositol phosphates, only inositol trisphosphates and tetrakisphosphates inhibit, not or very weak: inositol monophosphates, bisphosphates and pentakisphosphates, the recognition of myo-inositol phosphate regioisomers is highly structure-selective
L-scyllo-inositol 1,2,3,4-tetrakisphosphate
-
purified recombinant enzyme, IC50 value is above 0.1 mM in absence of Ca2+
L-scyllo-inositol 1,2,4-trisphosphate
-
purified recombinant enzyme, IC50 value is 0.006 mM in absence of Ca2+
N-(6-Aminohexyl)-5-chloro-1-naphthalenesulfonamide
-
i.e. W-7, calmodulin-antagonist
protein kinase A
-
isoforms A and B are differentially regulated via phosphorylation by the cAMP-dependent protein kinase, isoform A: stimulation in the presence or absence of Ca2+/calmodulin, isoform B: no effect on activity in the absence of Ca2+/calmodulin, 45% inhibition in the presence of Ca2+/calmodulin
-
scyllo-inositol 1,2,3,5-tetrakisphosphate
-
weak inhibition, purified recombinant enzyme, IC50 value is 0.028 mM in absence of Ca2+
scyllo-inositol 1,2,3-trisphosphate
-
purified recombinant enzyme, IC50 value is 0.027 mM in absence of Ca2+
scyllo-inositol 1,2,4,5-tetrakisphosphate
-
weak inhibition, purified recombinant enzyme, IC50 value is 0.039 mM in absence of Ca2+
scyllo-inositol 1,3,5-trisphosphate
-
purified recombinant enzyme, IC50 value is 0.090 mM in absence of Ca2+
TSH
-
thyroid-stimulating hormone, inhibits at a physiological concentration, inhibition is mimicked by dibuturyl cyclic AMP and forskolin, mechanism
1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
marked product inhibition, isoforms A and B
1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
product inhibition, IC50 is 0.013 mM
3',4',7,8-tetrahydroxyflavone
-
3',4',7,8-tetrahydroxyflavone
-
mixed-type versus ATP, noncompetitive versus 1D-myo-inositol 1,4,5-trisphosphate
aurintricarboxylic acid
-
aurintricarboxylic acid
-
strong inhibition, mixed-type versus ATP, noncompetitive versus 1D-myo-inositol 1,4,5-trisphosphate
Ca2+
-
-
Ca2+
-
isoforms A and B, above 0.01 mM
epicatechin-3-gallate
-
epicatechin-3-gallate
-
mixed-type versus ATP, noncompetitive versus 1D-myo-inositol 1,4,5-triphosphate
epigallocatechin-3-gallate
-
epigallocatechin-3-gallate
-
mixed-type versus ATP, noncompetitive versus 1D-myo-inositol 1,4,5-triphosphate
gossypol
-
gossypol
-
mixed-type versus ATP, noncompetitive versus 1D-myo-inositol 1,4,5-trisphosphate
hypericin
-
hypericin
-
mixed-type versus ATP, noncompetitive versus 1D-myo-inositol 1,4,5-triphosphate
KN-62
-
calmodulin-dependent protein kinase II inhibitor
KN-62
-
prevents the carbachol- or UTP-mediated activation
KN-93
-
calmodulin-dependent protein kinase II inhibitor
KN-93
-
prevents the carbachol- or UTP-mediated activation
myricetin
-
myricetin
-
mixed-type versus ATP, noncompetitive versus 1D-myo-inositol 1,4,5-trisphosphate
Protein kinase C
-
protein kinase C alone, without CaM kinase II, inhibits in the presence of Ca2+ and calmodulin
-
Protein kinase C
-
isoforms A and B are differentially regulated via phosphorylation by protein kinase C, isoform A: phosphorylated to the extent of 2 mol/mol, 72% inhibition in the absence of Ca2+/calmodulin, isoform B: phosphorylated to the extent of 2.7 mol/mol, no effect on activity in the absence of Ca2+/calmodulin, both isoforms are inhibited by 70% in the presence of Ca2+/calmodulin
-
Protein kinase C
-
negative regulatory function, phosphorylates the enzyme at Ser175, simultaneous phosphorylation at Ser109 and Ser175 also inactivates the enzyme
-
quercetin
-
quercetin
-
mixed-type versus ATP, noncompetitive versus 1D-myo-inositol 1,4,5-trisphosphate
additional information
-
not inhibited by GTP or 5'-guanylylimidodiphosphate
-
additional information
-
enzyme contains several motifs susceptible to a variety of proteases
-
additional information
-
IC50 values, overiew, no inhibition by chlorogenic acid, poor inhibition by rose bengal, and ellagic acid
-
additional information
-
inhibitor binding structures and mechanism, scyllo-inositol pentakisphosphate, scyllo-inositol hexakisphosphate, scyllo-inositol monophosphate, and scyllo-inositol S-bisphosphates are poor inhibitors
-
additional information
-
poor inhibition by adenophostin analogues xylo-furanophostin and furanophostin, by L-myo-inositol 2,4,5-trisphosphate, synthetic bicyclic inositol trisphosphate R epimer, and by epi-1D-myo-inositol 1,3,6-trisphosphate
-
additional information
All inhibitors display a mixed-type inhibition with respect to ATP and a noncompetitive inhibition with respect to 1D-myo-inositol 1,4,5-triphosphate. Mutagenesis studies reveal that both the calmodulin binding and the ATP binding domains in IP3K are involved in inhibitor binding. Most discovered potent IP3K inhibitors exert antiproliferative effects on cultured cells in vitro or in animal experiments and tumor treatment studies in vivo.
-
additional information
The flavonoids myricetin, 3',4',7,8-tetrahydroxyflavone, and epigallocatechin-3-gallate have a markedly stronger effect on isoforms A and C than on isoform B
-
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0.156
(2'S)-1D-1,2-O-[(2'-phosphoryloxy)propane-1',3'-diyl]-myo-inositol 4,5-bisphosphate
Rattus norvegicus
-
synthetic bicyclic inositol trisphosphate S epimer, IC50 is 0.156 mM
0.013
1D-myo-inositol 1,3,4,5-tetrakisphosphate
Rattus norvegicus
-
product inhibition, IC50 is 0.013 mM
0.00019 - 0.00061
3',4',7,8-tetrahydroxyflavone
0.000062
aurintricarboxylic acid
Rattus norvegicus
IP3K-C, maximal inhibition 100%
0.0054
D-2-deoxyinositol 1,3,4,5-tetrakisphosphate
Rattus norvegicus
-
strong inhibition of isozyme A, IC50 is 0.0054 mM
0.0017
D-2-deoxyinositol 1,4,5-trisphosphate
Rattus norvegicus
-
strong inhibition of isozyme A, IC50 is 0.0017 mM
0.0014
D-3-deoxyinositol 1,4,6-trisphosphate
Rattus norvegicus
-
strong inhibition of isozyme A, IC50 is 0.0014 mM
0.0051
D-6-deoxyinositol 1,3,4,5-tetrakisphosphate
Rattus norvegicus
-
strong inhibition of isozyme A, IC50 is 0.0051 mM
0.003
D-myo-inositol 1,4,5-trisphosphate
Rattus norvegicus
-
strong inhibition, purified recombinant enzyme, IC50 value is 0.003 mM in absence of Ca2+
0.117
D-myo-inositol 2,4,5-trisphosphate
Rattus norvegicus
-
IC50 is 0.117 mM
0.1
D-scyllo-inositol 1,2,3,4-tetrakisphosphate
Rattus norvegicus
-
purified recombinant enzyme, IC50 value is above 0.1 mM in absence of Ca2+
0.044
D-scyllo-inositol 1,2,4-trisphosphate
Rattus norvegicus
-
purified recombinant enzyme, IC50 value is 0.044 mM in absence of Ca2+
0.00069
ellagic acid
Rattus norvegicus
IP3K-C, maximal inhibition 85%
0.000385
epicatechin-3-gallate
Rattus norvegicus
IP3K-C, maximal inhibition 100%
0.00021
epigallocatechin-3-gallate
Rattus norvegicus
IP3K-C, maximal inhibition 100%
0.000175
gossypol
Rattus norvegicus
IP3K-C, maximal inhibition 100%
0.00017
hypericin
Rattus norvegicus
IP3K-C, maximal inhibition 100%
0.1
L-scyllo-inositol 1,2,3,4-tetrakisphosphate
Rattus norvegicus
-
purified recombinant enzyme, IC50 value is above 0.1 mM in absence of Ca2+
0.006
L-scyllo-inositol 1,2,4-trisphosphate
Rattus norvegicus
-
purified recombinant enzyme, IC50 value is 0.006 mM in absence of Ca2+
0.00029
myricetin
Rattus norvegicus
IP3K-C, maximal inhibition 62%
0.00039
quercetin
Rattus norvegicus
IP3K-C, maximal inhibition 71%
0.00017
Rose bengal
Rattus norvegicus
IP3K-C, maximal inhibition 100%
0.028
scyllo-inositol 1,2,3,5-tetrakisphosphate
Rattus norvegicus
-
weak inhibition, purified recombinant enzyme, IC50 value is 0.028 mM in absence of Ca2+
0.027
scyllo-inositol 1,2,3-trisphosphate
Rattus norvegicus
-
purified recombinant enzyme, IC50 value is 0.027 mM in absence of Ca2+
0.039
scyllo-inositol 1,2,4,5-tetrakisphosphate
Rattus norvegicus
-
weak inhibition, purified recombinant enzyme, IC50 value is 0.039 mM in absence of Ca2+
0.09
scyllo-inositol 1,3,5-trisphosphate
Rattus norvegicus
-
purified recombinant enzyme, IC50 value is 0.090 mM in absence of Ca2+
additional information
chlorogenic acid
0.00019
3',4',7,8-tetrahydroxyflavone
Rattus norvegicus
IP3K-C, maximal inhibition 75%
0.00019
3',4',7,8-tetrahydroxyflavone
Rattus norvegicus
recombinant enzyme IP3K-C fragment comprising calmodulin binding and catalytic domain
0.00061
3',4',7,8-tetrahydroxyflavone
Rattus norvegicus
recombinant enzyme IP3K-C fragment comprising catalytic domain
additional information
chlorogenic acid
Rattus norvegicus
IP3K-C, IC > 0.1
additional information
additional information
Rattus norvegicus
RnIP3K-C including the calmodulin binding and the catalytic domain shows a 3-fold lower IC50 value for 3',4',7,8-tetrahydroxyflavone than RnIP3K including only the calmodulin binding domain. The maximum degree of inhibition is unchanged. Together with the finding that Ca2+-calmodulin partly reverses IP3K inhibition indicates a facilitating but not essential involvement of the calmodulin binding domain in inhibitor binding.
-
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evolution
inositol(1,4,5)trisphosphate 3-kinases (Itpks) occur in three isoenzyme forms, Itpka/b and c, in human, rat and mouse. They share a catalytic domain relatively well conserved at the C-terminal end and a quite isoenzyme specific regulatory domain at the N-terminal end of the protein
malfunction
neurite length is significantly decreased in cells overexpressing isozymes Itpka and Itpkb but not Itpkc or IPMK. This result does not depend on the overexpression level of any of the kinases. PC12 cells overexpressing GFP-tagged kinase-dead mutants Itpka/b have shorter neurites than GFP control cells
metabolism
1D-myo-inositol 1,3,4,5-tetrakisphosphate, Ins(1,3,4,5)P4 can interact with a relatively specific Ins(1,3,4,5)P4 binding protein Rasa3, alternatively, Ins(1,3,4,5)P4 can also compete with phosphoinositides to the binding of PH domain containing proteins such as Akt, protein kinase B. In neutrophils and hematopoietic progenitors, elevated levels of Ins(1,3,4,5)P4 inhibit the recruitment of Akt at the plasma membrane, and its activation, acting as a competitor of PtdIns(3,4,5)P3 binding to its PH domain
evolution
inositol(1,4,5)trisphosphate 3-kinases (Itpks) occur in three isoenzyme forms, Itpka/b and c, in human, rat and mouse. They share a catalytic domain relatively well conserved at the C-terminal end and a quite isoenzyme specific regulatory domain at the N-terminal end of the protein
malfunction
neurite length is significantly decreased in cells overexpressing isozymes Itpka and Itpkb but not Itpkc or IPMK. This result does not depend on the overexpression level of any of the kinases. PC-12 cells overexpressing GFP-tagged kinase-dead mutants Itpka/b have shorter neurites than GFP control cells
metabolism
1D-myo-inositol 1,3,4,5-tetrakisphosphate, Ins(1,3,4,5)P4 can interact with a relatively specific Ins(1,3,4,5)P4 binding protein Rasa3, alternatively, Ins(1,3,4,5)P4 can also compete with phosphoinositides to the binding of PH domain containing proteins such as Akt, protein kinase B. In neutrophils and hematopoietic progenitors, elevated levels of Ins(1,3,4,5)P4 inhibit the recruitment of Akt at the plasma membrane, and its activation, acting as a competitor of PtdIns(3,4,5)P3 binding to its PH domain
physiological function
on neural activation, inositol 1,4,5-trisphosphate 3-kinase A binds directly to activated Rac1 and recruits it to the actin cytoskeleton in the postsynaptic area, enzyme is critical for the spatial and temporal regulation of spine actin remodeling, synaptic plasticity, and learning and memory via an activity-dependent Rac scaffolding mechanism, inositol 1,4,5-trisphosphate 3-kinase A catalytic activity regulates calcium levels by modulating the metabolism of 1D-myo-inositol 1,4,5-trisphosphate
physiological function
isozyme Itpka contains an F-actin binding site at the N-terminal part that confers to Itpka the properties of an F-actin bundling protein with two major consequences: it can reorganize the cytoskeletal network, particularly in dendritic spines, and it can provide an opportunity for Ins(1,3,4,5)P4 to act very locally as second messenger. Isozyme Itpka is an F-actin bundling protein regulating dendritic spines structural plasticity and a scaffold protein for synaptic rac signaling, Itpka overexpression induces cytoskeletal reorganization, high expression of Itpka in cancer cells increases invasion and migration in vitro. Itpka and Itpkb isoforms inhibit neurite outgrowth in PC12 cells, while isozyme Itpkc does not
physiological function
isozyme Itpka inhibits neurite outgrowth through both F-actin binding
physiological function
in natural killer (NK) cells, isozyme Itpkb promotes NK-cell terminal maturation but limits NK-cell effector functions. Itpka and Itpkb isoforms inhibit neurite outgrowth in PC12 cells, while isozyme Itpkc does not
physiological function
isozyme Itpkb inhibits neurite outgrowth through both F-actin binding
physiological function
isozyme Itpkc does not influence neurite length and neuron growth or F-actin binding
physiological function
Itpka and Itpkb isoforms inhibit neurite outgrowth in PC12 cells, while isozyme Itpkc does not
additional information
an F-actin binding site is located in the N-terminal part of isozyme Itpka. The catalytic activity is located at the C-terminal end, N-terminal deletion mutants are fully active
additional information
an F-actin binding site is located in the N-terminal part of isozyme Itpka. The catalytic activity is located at the C-terminal end, N-terminal deletion mutants are fully active
additional information
an F-actin binding site is located in the N-terminal part of isozyme Itpka. The catalytic activity is located at the C-terminal end, N-terminal deletion mutants are fully active
additional information
an F-actin binding site is located in the N-terminal part of isozyme Itpkb. The catalytic activity is located at the C-terminal end, N-terminal deletion mutants are fully active
additional information
an F-actin binding site is located in the N-terminal part of isozyme Itpkb. The catalytic activity is located at the C-terminal end, N-terminal deletion mutants are fully active
additional information
an F-actin binding site is located in the N-terminal part of isozyme Itpkb. The catalytic activity is located at the C-terminal end, N-terminal deletion mutants are fully active
additional information
isozyme Itpkb contains an F-actin binding site at the N-terminal part
additional information
isozyme Itpkb contains an F-actin binding site at the N-terminal part
additional information
isozyme Itpkb contains an F-actin binding site at the N-terminal part
additional information
neurite length is significantly decreased in cells overexpressing isozymes Itpka and Itpkb but not Itpkc or IPMK. This result does not depend on the overexpression level of any of the kinases
additional information
neurite length is significantly decreased in cells overexpressing isozymes Itpka and Itpkb but not Itpkc or IPMK. This result does not depend on the overexpression level of any of the kinases
additional information
neurite length is significantly decreased in cells overexpressing isozymes Itpka and Itpkb but not Itpkc or IPMK. This result does not depend on the overexpression level of any of the kinases
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Hansen, C.A.; Mah, S.; Williamson, J.R.
Formation and metabolism of inositol 1,3,4,5-tetrakisphosphate in liver
J. Biol. Chem.
261
8100-8103
1986
Rattus norvegicus
brenda
Irvine, R.F.; Letcher, A.J.; Heslop, J.P.; Berridge, M.J.
The inositol tris/tetrakisphosphate pathway--demonstration of Ins(1,4,5)P3 3-kinase activity in animal tissues
Nature
320
631-634
1986
Rattus norvegicus, Xenopus sp.
brenda
Johanson, R.A.; Hansen, C.A.; Williamson, J.R.
Purification of D-myo-inositol 1,4,5-trisphosphate 3-kinase from rat brain
J. Biol. Chem.
263
7465-7471
1988
Rattus norvegicus
brenda
Lee, S.Y.; Sim, S.S.; Kim, J.W.; Moon, K.H.; Kim, J.H.; Rhee, S.G.
Purification and properties of D-myo-inositol 1,4,5-trisphosphate 3-kinase from rat brain. Susceptibility to calpain
J. Biol. Chem.
265
9434-9440
1990
Rattus norvegicus
brenda
Takazawa, K.; Lemos, M.; Delvaux, A.; Lejeune, C.; Dumont, J.E.; Erneux, C.
Rat brain inositol 1,4,5-trisphosphate 3-kinase. Ca2(+)-sensitivity, purification and antibody production
Biochem. J.
268
213-217
1990
Rattus norvegicus
brenda
Takazawa, K.; Passareiro, H.; Dumont, J.E.; Erneux, C.
Ca2+/calmodulin-sensitive inositol 1,4,5-trisphosphate 3-kinase in rat and bovine brain tissues
Biochem. Biophys. Res. Commun.
153
632-641
1988
Bos taurus, Rattus norvegicus
brenda
Biden, T.J.; Comte, M.; Cox, J.A.; Wollheim, C.B.
Calcium-calmodulin stimulates inositol 1,4,5-trisphosphate kinase activity from insulin-secreting RINm5F cells
J. Biol. Chem.
262
9437-9440
1987
Rattus norvegicus
brenda
Collin, T.
Serotonin induces an increase in D-myo-inositol (1,4,5)-trisphosphate 3-kinase activity in rat brainstem slices
Neurosci. Lett.
255
67-70
1998
Rattus norvegicus
brenda
Choi, G.; Chang, Y.T.; Chung, S.K.; Choi, K.Y.
Molecular interactions of all possible regioisomers of synthetic myo-inositol phosphates with inositol 1,4,5-trisphosphate 3-kinase
Bioorg. Med. Chem. Lett.
7
2709-2714
1997
Rattus norvegicus
-
brenda
Shin, Y.S.; Choi, G.; Choi, K.Y.
Overexpression, purification and characterization of inositol 1,4,5-triphosphate 3-kinase from rat brain
Mol. Cells
5
348-353
1995
Rattus norvegicus
-
brenda
Vanweyenberg, V.; Communi, D.; D'Santos, C.S.; Erneux, C.
Tissue- and cell-specific expression of Ins(1,4,5)P3 3-kinase isoenzymes
Biochem. J.
306
429-435
1995
Homo sapiens, Rattus norvegicus
brenda
Takazawa, K.; Go, M.; Endo, T.; Erneux, C.; Onaya, T.
Inositol 1,4,5-trisphosphate 3-kinase activity in FRTL-5 cells: regulation of the enzyme activity by TSH
J. Endocrinol.
144
527-532
1995
Rattus norvegicus
brenda
Communi, D.; Vanweyenberg, V.; Erneux, C.
D-myo-inositol 1,4,5-trisphosphate 3-kinase A is activated by receptor activation through a calcium:calmodulin-dependent protein kinase II phosphorylation mechanism
EMBO J.
16
1943-1952
1997
Homo sapiens, Rattus norvegicus
brenda
Millard, T.H.; Cullen, P.J.; Banting, G.
Effects of elevated expression of inositol 1,4,5-trisphosphate 3-kinase B on Ca2+ homoeostasis in HeLa cells
Biochem. J.
352
709-715
2000
Rattus norvegicus
brenda
Communi, D.; Dewaste, V.; Erneux, C.
Calcium-calmodulin-dependent protein kinase II and protein kinase C-mediated phosphorylation and activation of D-myo-inositol 1,4, 5-trisphosphate 3-kinase B in astrocytes
J. Biol. Chem.
274
14734-14742
1999
Homo sapiens, Rattus norvegicus
brenda
Woodring, P.J.; Garrison, J.C.
Expression, purification, and regulation of two isoforms of the inositol 1,4,5-trisphosphate 3-kinase
J. Biol. Chem.
272
30447-30454
1997
Rattus norvegicus
brenda
Schell, M.J.; Erneux, C.; Irvine, R.F.
Inositol 1,4,5-trisphosphate 3-kinase A associates with F-actin and dendritic spines via its N terminus
J. Biol. Chem.
276
37537-37546
2001
Rattus norvegicus
brenda
Nalaskowski, M.M.; Bertsch, U.; Fanick, W.; Stockebrand, M.C.; Schmale, H.; Mayr, G.W.
Rat inositol 1,4,5-trisphosphate 3-kinase C is enzymatically specialized for basal cellular inositol trisphosphate phosphorylation and shuttles actively between nucleus and cytoplasm
J. Biol. Chem.
278
19765-19776
2003
Rattus norvegicus
brenda
Brehm, M.A.; Schreiber, I.; Bertsch, U.; Wegner, A.; Mayr, G.W.
Identification of the actin-binding domain of Ins(1,4,5)P3 3-kinase isoform B (IP3K-B)
Biochem. J.
382
353-362
2004
Homo sapiens, Rattus norvegicus (P42335)
brenda
Kwon, Y.U.; Im, J.; Choi, G.; Kim, Y.S.; Choi, K.Y.; Chung, S.K.
Synthesis of three enantiomeric pairs of scyllo-inositol phosphate and molecular interactions between all possible regioisomers of scyllo-inositol phosphate and inositol 1,4,5-trisphosphate 3-kinase
Bioorg. Med. Chem. Lett.
13
2981-2984
2003
Rattus norvegicus
brenda
Xia, H.J.; Yang, G.
Inositol 1,4,5-trisphosphate 3-kinases: functions and regulations
Cell Res.
15
83-91
2005
Drosophila melanogaster, Homo sapiens, Rattus norvegicus, Sus scrofa
brenda
Poinas, A.; Backers, K.; Riley, A.M.; Mills, S.J.; Moreau, C.; Potter, B.V.; Erneux, C.
Interaction of the catalytic domain of inositol 1,4,5-trisphosphate 3-kinase A with inositol phosphate analogues
Chembiochem
6
1449-1457
2005
Rattus norvegicus
brenda
Mayr, G.W.; Windhorst, S.; Hillemeier, K.
Antiproliferative plant and synthetic polyphenolics are specific inhibitors of vertebrate inositol-1,4,5-trisphosphate 3-kinases and inositol polyphosphate multikinase
J. Biol. Chem.
280
13229-13240
2005
Gallus gallus, Homo sapiens, Rattus norvegicus
brenda
Miller, G.J.; Hurley, J.H.
Crystal structure of the catalytic core of inositol 1,4,5-trisphosphate 3-kinase
Mol. Cell
15
703-711
2004
Rattus norvegicus
brenda
Resnick, A.C.; Snowman, A.M.; Kang, B.N.; Hurt, K.J.; Snyder, S.H.; Saiardi, A.
Inositol polyphosphate multikinase is a nuclear PI3-kinase with transcriptional regulatory activity
Proc. Natl. Acad. Sci. USA
102
12783-12788
2005
Rattus norvegicus, Saccharomyces cerevisiae, Saccharomyces cerevisiae BY4741
brenda
Nalaskowski, M.M.; Windhorst, S.; Stockebrand, M.C.; Mayr, G.W.
Subcellular localisation of human inositol 1,4,5-trisphosphate 3-kinase C: species-specific use of alternative export sites for nucleo-cytoplasmic shuttling indicates divergent roles of the catalytic and N-terminal domains
Biol. Chem.
387
583-593
2006
Homo sapiens, Rattus norvegicus
brenda
Stokes, A.J.; Shimoda, L.M.; Lee, J.W.; Rillero, C.; Chang, Y.; Turner, H.
FceRI control of Ras via inositol (1,4,5) trisphosphate 3-kinase and inositol tetrakisphosphate
Cell. Signal.
18
640-651
2006
Rattus norvegicus
brenda
Lloyd-Burton, S.M.; Yu, J.C.; Irvine, R.F.; Schell, M.J.
Regulation of inositol 1,4,5-trisphosphate 3-kinases by calcium and localization in cells
J. Biol. Chem.
282
9526-9535
2007
Rattus norvegicus
brenda
Sun, W.; Kang, Y.; Kim, I.H.; Kim, E.H.; Rhyu, I.J.; Kim, H.; Kim, H.
Inhibition of rat brain inositol 1,4,5-trisphosphate 3-kinase A expression by kainic acid
Neurosci. Lett.
392
181-186
2006
Rattus norvegicus
brenda
Mayr, G.W.; Windhorst, S.; Hillemeier, K.
Antiproliferative plant and synthetic polyphenolics are specific inhibitors of vertebrate inositol-1,4,5-trisphosphate 3-kinases and inositol polyphosphate multikinase. [Erratum to document cited in CA143:003106]
J. Biol. Chem.
282
35424
2007
Gallus gallus, Homo sapiens (P23677), Homo sapiens (P27987), Rattus norvegicus (Q80ZG2)
-
brenda
Kim, I.H.; Park, S.K.; Hong, S.T.; Jo, Y.S.; Kim, E.J.; Park, E.H.; Han, S.B.; Shin, H.S.; Sun, W.; Kim, H.T.; Soderling, S.H.; Kim, H.
Inositol 1,4,5-trisphosphate 3-kinase a functions as a scaffold for synaptic Rac signaling
J. Neurosci.
29
14039-14049
2009
Mus musculus, Rattus norvegicus (P17105)
brenda
Lee, D.; Lee, H.W.; Hong, S.; Choi, B.I.; Kim, H.W.; Han, S.B.; Kim, I.H.; Bae, J.Y.; Bae, Y.C.; Rhyu, I.J.; Sun, W.; Kim, H.
Inositol 1,4,5-trisphosphate 3-kinase A is a novel microtubule-associated protein: PKA-dependent phosphoregulation of microtubule binding affinity
J. Biol. Chem.
287
15981-15995
2012
Rattus norvegicus (P17105)
brenda
Erneux, C.; Ghosh, S.; Koenig, S.
Inositol(1,4,5)P3 3-kinase isoenzymes: catalytic properties and importance of targeting to F-actin to understand function
Adv. Biol. Regul.
60
135-143
2016
Homo sapiens (P23677), Homo sapiens (P27987), Homo sapiens (Q96DU7), Homo sapiens, Mus musculus (B2RXC2), Mus musculus (Q7TS72), Mus musculus (Q8R071), Mus musculus, Rattus norvegicus (P17105), Rattus norvegicus (P42335), Rattus norvegicus (Q80ZG2)
brenda
Koenig, S.; Moreau, C.; Dupont, G.; Scoumanne, A.; Erneux, C.
Regulation of NGF-driven neurite outgrowth by Ins(1,4,5)P3 kinase is specifically associated with the two isoenzymes Itpka and Itpkb in a model of PC12 cells
FEBS J.
282
2553-2569
2015
Rattus norvegicus (P17105), Rattus norvegicus (P42335), Rattus norvegicus (Q80ZG2)
brenda