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2 ATP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate + 1D-myo-inositol 1,4,5,6-tetrakisphosphate
2 ADP + 2 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
2 ATP + 1D-myo-inositol 1,4,5-trisphosphate
2 ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
2 ATP + 1D-myo-inositol 4,5-bisphosphate
2 ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
-
-
?
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
ATP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate
ATP + 1D-myo-inositol 1,2,3,4,5,6-hexakisphosphate
ADP + diphosphoinositol pentakisphosphate
-
isozyme Kcs1
-
-
?
ATP + 1D-myo-inositol 1,2,3,4,6-pentakisphosphate
ADP + 1D-myo-inositol 1,2,3,4,5,6-hexakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,2,3,4,6-pentakisphosphate
ADP + inositol hexakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + diphosphoinositol tetrakisphosphate
-
isozyme Kcs1
-
-
?
ATP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ATP + 1D-myo-inositol 1,3,4,6-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ATP + 1D-myo-inositol 1,3,4,6-tetrakisphosphate
ADP + ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
-
-
-
-
r
ATP + 1D-myo-inositol 1,4,5,6-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
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 1,3,4,6-tetrakisphosphate
-
2fold less active compared to 1D-myo-inositol 1,3,4,6-tetrakisphosphate
-
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,4,5,6-tetrakisphosphate
ATP + 1D-myo-inositol 4,5-bisphosphate
ADP + 1D-myo-inositol 3,4,5-trisphosphate
ATP + inositol 1,3,4,5-tetrakisphosphate
ADP + inositol (1,3,4,5,6)-pentakisphosphate
-
substrate preference for inositol 1,3,4,6-tetrakisphosphate over inositol 1,4,5-trisphosphate and inositol 1,3,4,5-tetrakisphosphate
-
-
?
ATP + inositol 1,4,5,6-tetrakisphosphate
ADP + inositol (1,3,4,5,6)-pentakisphosphate
ATP + inositol 1,4,5-trisphosphate
ADP + inositol (1,3,4,5)-tetrakisphosphate
-
substrate preference for inositol 1,3,4,6-tetrakisphosphate over inositol 1,4,5-trisphosphate and inositol 1,3,4,5-tetrakisphosphate
-
-
?
ATP + phosphatidylinositol 4,5-bisphosphate
ADP + phosphatidylinositol (3,4,5)-trisphosphate
-
-
-
-
?
ATP + phosphatidylinositol 4,5-bisphosphate
ADP + phosphatidylinositol 3,4,5-trisphosphate
-
in rats
-
-
?
inositol (1,3,4,5)-tetrakisphosphate + ATP
inositol (1,3,4,5,6)-pentakisphosphate + ADP
-
no inositol (1,2,4,5,6) pentakisphosphate is formed
-
?
inositol (1,3,4,5)-tetrakisphosphate + ATP
inositol pentakisphosphate + ADP
-
-
?
inositol (1,3,4,6)-tetrakisphosphate + ATP
ADP + inositol (1,3,4,5,6)-pentakisphosphate
-
substrate preference for inositol 1,3,4,6-tetrakisphosphate over inositol 1,4,5-trisphosphate and inositol 1,3,4,5-tetrakisphosphate
-
-
?
inositol (1,4,5)-triphosphate + ATP
inositol (1,3,4,5)-tetrakisphosphate + ADP
-
-
?
inositol (1,4,5)-triphosphate + ATP
inositol (1,3,4,5)-tetrakisphosphate + inositol (1,4,5,6)-tetrakisphosphate + ADP
-
-
-
?
inositol (1,4,5,6)-tetrakisphosphate + ATP
inositol (1,3,4,5,6)-pentakisphosphate + ADP
inositol (3,4,5,6)-tetrakisphosphate + ATP
inositol (1,3,4,5,6)-pentakisphosphate + ADP
-
hITPK1 has more than 13000fold preference for inositol (3,4,5,6)-tetrakisphosphate over its enantiomer inositol (1,4,5,6)-tetrakisphosphate
-
-
?
inositol (4,5)-bisphosphate + ATP
inositol (1,4,5)-trisphosphate + ADP
-
-
?
inositol bisphosphate + ATP
inositol trisphosphate + ADP
-
-
-
?
inositol monophosphate + ATP
inositol diphosphate + ADP
-
-
-
?
inositol pentakisphosphate + ATP
diphosphoinositol tetrakisphosphate + ADP
-
-
?
inositol pentakisphosphate + ATP
inositol hexakisphosphate + ADP
inositol tetrakisphosphate + ATP
inositol pentakisphosphate + ADP
-
-
-
?
myo-inositol tetrakisphosphate + ATP
myo-inositol pentakisphosphate + ADP
myo-inositol triphosphate + ATP
myo-inositol tetrakisphosphate + ADP
additional information
?
-
2 ATP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate + 1D-myo-inositol 1,4,5,6-tetrakisphosphate
2 ADP + 2 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
-
-
-
-
?
2 ATP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate + 1D-myo-inositol 1,4,5,6-tetrakisphosphate
2 ADP + 2 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
-
-
-
-
?
2 ATP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate + 1D-myo-inositol 1,4,5,6-tetrakisphosphate
2 ADP + 2 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
-
in rats and humans
-
-
?
2 ATP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate + 1D-myo-inositol 1,4,5,6-tetrakisphosphate
2 ADP + 2 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
-
in rats and humans
-
-
?
2 ATP + 1D-myo-inositol 1,4,5-trisphosphate
2 ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
-
-
-
-
r
2 ATP + 1D-myo-inositol 1,4,5-trisphosphate
2 ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
in rats and humans
-
-
?
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
-
in rats and humans
-
-
?
ATP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate
-
-
-
-
?
ATP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
-
low activity
-
-
?
ATP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
-
43fold less active compared to 1D-myo-inositol 1,3,4,6-tetrakisphosphate
-
-
?
ATP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
-
-
-
-
ir
ATP + 1D-myo-inositol 1,3,4,6-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,6-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,6-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
-
preferred substrate
-
-
?
ATP + 1D-myo-inositol 1,4,5,6-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,4,5,6-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,4,5,6-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 1,4,5,6-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,4,5,6-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
-
recombinant enzyme in yeast mutant cells
-
-
?
ATP + 1D-myo-inositol 1,4,5,6-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
-
-
-
-
ir
ATP + 1D-myo-inositol 1,4,5,6-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
-
preferred substrate of isozyme Ipk2
-
-
?
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
-
-
-
ir
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
2fold less active compared to 1D-myo-inositol 1,3,4,6-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
-
-
-
-
ir
ATP + 1D-myo-inositol 1,4,5-trisphosphate
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
-
the enzyme initiates a inositol polyphosphate pathway, isozyme Kcs1 is also involved, inositol metabolism, overview
-
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
isozyme Ipk2 and isozyme Kcs1
-
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,4,5,6-tetrakisphosphate
-
-
-
-
ir
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,4,5,6-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,4,5,6-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,4,5,6-tetrakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,4,5,6-tetrakisphosphate
-
-
-
-
ir
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,4,5,6-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,4,5,6-tetrakisphosphate
-
-
-
ir
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,4,5,6-tetrakisphosphate
-
-
-
-
ir
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,4,5,6-tetrakisphosphate
-
preferred substrate of isozyme Ipk2
-
-
?
ATP + 1D-myo-inositol 4,5-bisphosphate
ADP + 1D-myo-inositol 3,4,5-trisphosphate
-
-
-
?
ATP + 1D-myo-inositol 4,5-bisphosphate
ADP + 1D-myo-inositol 3,4,5-trisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 4,5-bisphosphate
ADP + 1D-myo-inositol 3,4,5-trisphosphate
-
the enzyme is specific for 1D-myo-inositol 4,5-bisphosphate
product identification
-
?
ATP + 1D-myo-inositol 4,5-bisphosphate
ADP + 1D-myo-inositol 3,4,5-trisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 4,5-bisphosphate
ADP + 1D-myo-inositol 3,4,5-trisphosphate
-
the enzyme is specific for 1D-myo-inositol 4,5-bisphosphate
product identification
-
?
ATP + 1D-myo-inositol 4,5-bisphosphate
ADP + 1D-myo-inositol 3,4,5-trisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 4,5-bisphosphate
ADP + 1D-myo-inositol 3,4,5-trisphosphate
-
the enzyme is specific for 1D-myo-inositol 4,5-bisphosphate
product identification
-
?
ATP + inositol 1,4,5,6-tetrakisphosphate
ADP + inositol (1,3,4,5,6)-pentakisphosphate
-
-
-
-
?
ATP + inositol 1,4,5,6-tetrakisphosphate
ADP + inositol (1,3,4,5,6)-pentakisphosphate
-
stable over-expression of the human protein in HEK-293 cells abrogates the in vivo elevation of inositol 1,4,5,6-tetrakisphosphate from the Salmonella dublin SopB protein. The enzyme may play a role in regulation of the level of inositol 1,4,5,6-tetrakisphosphate in human cells
-
-
?
inositol (1,4,5,6)-tetrakisphosphate + ATP
inositol (1,3,4,5,6)-pentakisphosphate + ADP
-
hITPK1 has more than 13000fold preference for inositol (3,4,5,6)-tetrakisphosphate over its enantiomer inositol (1,4,5,6)-tetrakisphosphate
-
-
?
inositol (1,4,5,6)-tetrakisphosphate + ATP
inositol (1,3,4,5,6)-pentakisphosphate + ADP
-
inositol polyphosphate multikinase is a key mediators in the production of inositol (1,3,4,5,6)-pentakisphosphate
-
-
?
inositol (1,4,5,6)-tetrakisphosphate + ATP
inositol (1,3,4,5,6)-pentakisphosphate + ADP
-
no inositol (1,2,4,5,6) pentakisphosphate is formed
-
?
inositol pentakisphosphate + ATP
inositol hexakisphosphate + ADP
-
-
-
?
inositol pentakisphosphate + ATP
inositol hexakisphosphate + ADP
-
-
-
?
myo-inositol tetrakisphosphate + ATP
myo-inositol pentakisphosphate + ADP
-
-
-
?
myo-inositol tetrakisphosphate + ATP
myo-inositol pentakisphosphate + ADP
-
-
-
?
myo-inositol tetrakisphosphate + ATP
myo-inositol pentakisphosphate + ADP
-
-
-
?
myo-inositol triphosphate + ATP
myo-inositol tetrakisphosphate + ADP
-
it appears that the enzyme utilizes inositol triphosphate as the initial substrate for the synthesis of higher myo-inositol polyphosphates
-
?
myo-inositol triphosphate + ATP
myo-inositol tetrakisphosphate + ADP
-
-
-
?
myo-inositol triphosphate + ATP
myo-inositol tetrakisphosphate + ADP
-
-
-
?
additional information
?
-
-
the enzyme is involved in the inositol phosphate metabolism which is important for several cellular functions and signaling, metabolism overview
-
-
?
additional information
?
-
substrate specificity, no formation of 1D-myo-inositol 1,3,4,5,6-pentakisphosphate from 1D-myo-inositol 1,4,5-trisphosphate
-
-
?
additional information
?
-
substrate specificity, no formation of 1D-myo-inositol 1,3,4,5,6-pentakisphosphate from 1D-myo-inositol 1,4,5-trisphosphate
-
-
?
additional information
?
-
-
substrate specificity, no formation of 1D-myo-inositol 1,3,4,5,6-pentakisphosphate from 1D-myo-inositol 1,4,5-trisphosphate
-
-
?
additional information
?
-
AtIpk2b Is an auxin-inducible gene and is important for the auxin signaling pathway
-
-
?
additional information
?
-
IP3K is involved in axillary shoot branching via Auxin signaling
-
-
?
additional information
?
-
-
Genome-wide RNA interference screen in cultured Drosophila melanogaster haemocyte-like cells identifies as a regulator of the Janus tyrosine kinase/signal transducer and activator of transcription.
-
-
?
additional information
?
-
-
the enzyme is involved in the inositol phosphate metabolism which is important for several cellular functions and signaling, metabolism overview
-
-
?
additional information
?
-
-
the enzyme might be involved in regulation of cell growth
-
-
?
additional information
?
-
-
the enzyme regulates inositol 1,4,5,6-tetrakisphosphate
-
-
?
additional information
?
-
-
substrate specificity model, the enzyme shows inositol phosphate 5-kinase activity, overview
-
-
?
additional information
?
-
-
substrate specificity, product identification
-
-
?
additional information
?
-
-
inositol (1,4,5,6)-tetrakisphosphate is not a physiological substrate
-
-
?
additional information
?
-
-
enzyme has a preferred 5-kinase activity over 3-kinase and 6-kinase activities
-
-
?
additional information
?
-
-
role in chromatin remodelling
-
-
?
additional information
?
-
-
Studies in the rat cells and mice suggest that Ins(1,4,5)P3 3-kinases likely contribute little to the synthesis of inositol pentakisphosphate and inositol hexakisphosphate
-
-
?
additional information
?
-
-
The 3-step pathway to InsP6 mediated by phospholipase C, IPMK and inositol kinase (Ipk1) in yeast contrasts with an alternative description of a 5-step pathway in human cells.
-
-
?
additional information
?
-
-
inositol polyphosphate multikinase is a multifunctional enzyme with PI3-kinase, IP3-kinase and catalytically independent activities. IPMK is a PI3-kinase which phosphorylates PIP2 into PIP3, serving as a physiologic activator of Akt/PKB. It also possesses IP3-kinase activity, converting IP3 into IP4 (1,3,4,5) or IP4 (1,4,5,6). Whether the phosphorylation of IP3 at the 3-position or the 6-position is physiologically regulated
-
-
?
additional information
?
-
inositol polyphosphate multikinase is an enzyme that displays soluble inositol phosphate kinase activity, lipid kinase activity, and various noncatalytic interactions
-
-
?
additional information
?
-
-
inositol polyphosphate multikinase is an enzyme that displays soluble inositol phosphate kinase activity, lipid kinase activity, and various noncatalytic interactions
-
-
?
additional information
?
-
IPMK is a broad-specificity enzyme that converts inositol 1,4,5-trisphosphate into inositol 1,4,5,6-tetrakisphosphate (IP4) and subsequently inositol 1,3,4,5,6-pentakisphosphate
-
-
?
additional information
?
-
recombinant HsIMPK uses 3-kinase activity to phosphorylate Ins(1,4,5)P3 to Ins(1,3,4,5)P4, and then phosphorylates the latter with a 6-kinase activity that yields Ins(1,3,4,5,6)P5. It also shows PtdIns(4,5)P2 3-kinase activity. Substrate binding structures, overview
-
-
-
additional information
?
-
-
recombinant HsIMPK uses 3-kinase activity to phosphorylate Ins(1,4,5)P3 to Ins(1,3,4,5)P4, and then phosphorylates the latter with a 6-kinase activity that yields Ins(1,3,4,5,6)P5. It also shows PtdIns(4,5)P2 3-kinase activity. Substrate binding structures, overview
-
-
-
additional information
?
-
-
the enzyme plays an essential role in mouse embryogenesis and second messenger production
-
-
?
additional information
?
-
-
the enzyme exhibits 3-,5-, and 6-kinase activity on inositol tris- and tetrakisphosphate substrates, e.g. 1D-myo-inositol 1,4,5-trisphosphate
-
-
?
additional information
?
-
the absence of expression of the three isoenzymes of the inositol 1,4,5-trisphosphate 3-kinase does not prevent the formation of inositol pentakisphosphate and hexakisphosphate
-
-
?
additional information
?
-
-
the absence of expression of the three isoenzymes of the inositol 1,4,5-trisphosphate 3-kinase does not prevent the formation of inositol pentakisphosphate and hexakisphosphate
-
-
?
additional information
?
-
-
the enzyme also performs the inositol phosphate 3-kinase reaction, EC 2.7.1.127
-
-
?
additional information
?
-
-
role in chromatin remodelling
-
-
?
additional information
?
-
-
Studies in the rat cells and mice suggest that Ins(1,4,5)P3 3-kinases likely contribute little to the synthesis of InsP5 and InsP6
-
-
?
additional information
?
-
-
The 3-step pathway to InsP6 mediated by phospholipase C, IPMK and inositol kinase (Ipk1) in yeast contrasts with an alternative description of a 5-step pathway in human cells.
-
-
?
additional information
?
-
-
the enzyme is involved in regulation of telomere length and cell death, overview
-
-
?
additional information
?
-
-
the enzyme is involved in the inositol phosphate metabolism which is important for several cellular functions and signaling, metabolism overview
-
-
?
additional information
?
-
-
the enzyme is involved inregulation of arginine-sensitive ArgR-Mcm1 transcriptional complex, overview
-
-
?
additional information
?
-
-
the enzyme is required for resistance to salt stress, cell wall integrity, and vascuolar morphogenesis
-
-
?
additional information
?
-
-
the enzyme performs also the inositol phosphate 3-kinase reaction, EC 2.7.1.127
-
-
?
additional information
?
-
-
the enzyme is involved inregulation of arginine-sensitive ArgR-Mcm1 transcriptional complex, overview
-
-
?
additional information
?
-
-
the enzyme performs also the inositol phosphate 3-kinase reaction, EC 2.7.1.127
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2 ATP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate + 1D-myo-inositol 1,4,5,6-tetrakisphosphate
2 ADP + 2 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
2 ATP + 1D-myo-inositol 1,4,5-trisphosphate
2 ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
-
-
-
-
r
2 ATP + 1D-myo-inositol 4,5-bisphosphate
2 ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
-
-
?
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
ATP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate
ATP + 1D-myo-inositol 1,2,3,4,5,6-hexakisphosphate
ADP + diphosphoinositol pentakisphosphate
-
isozyme Kcs1
-
-
?
ATP + 1D-myo-inositol 1,2,3,4,6-pentakisphosphate
ADP + inositol hexakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + diphosphoinositol tetrakisphosphate
-
isozyme Kcs1
-
-
?
ATP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ATP + 1D-myo-inositol 1,3,4,6-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,6-tetrakisphosphate
ADP + ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
-
-
-
-
r
ATP + 1D-myo-inositol 1,4,5,6-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
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 1,4,5,6-tetrakisphosphate
ATP + 1D-myo-inositol 4,5-bisphosphate
ADP + 1D-myo-inositol 3,4,5-trisphosphate
ATP + inositol 1,4,5,6-tetrakisphosphate
ADP + inositol (1,3,4,5,6)-pentakisphosphate
-
stable over-expression of the human protein in HEK-293 cells abrogates the in vivo elevation of inositol 1,4,5,6-tetrakisphosphate from the Salmonella dublin SopB protein. The enzyme may play a role in regulation of the level of inositol 1,4,5,6-tetrakisphosphate in human cells
-
-
?
ATP + phosphatidylinositol 4,5-bisphosphate
ADP + phosphatidylinositol (3,4,5)-trisphosphate
-
-
-
-
?
ATP + phosphatidylinositol 4,5-bisphosphate
ADP + phosphatidylinositol 3,4,5-trisphosphate
-
in rats
-
-
?
inositol (1,4,5,6)-tetrakisphosphate + ATP
inositol (1,3,4,5,6)-pentakisphosphate + ADP
-
inositol polyphosphate multikinase is a key mediators in the production of inositol (1,3,4,5,6)-pentakisphosphate
-
-
?
myo-inositol triphosphate + ATP
myo-inositol tetrakisphosphate + ADP
-
it appears that the enzyme utilizes inositol triphosphate as the initial substrate for the synthesis of higher myo-inositol polyphosphates
-
?
additional information
?
-
2 ATP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate + 1D-myo-inositol 1,4,5,6-tetrakisphosphate
2 ADP + 2 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
-
-
-
-
?
2 ATP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate + 1D-myo-inositol 1,4,5,6-tetrakisphosphate
2 ADP + 2 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
-
-
-
-
?
2 ATP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate + 1D-myo-inositol 1,4,5,6-tetrakisphosphate
2 ADP + 2 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
-
in rats and humans
-
-
?
2 ATP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate + 1D-myo-inositol 1,4,5,6-tetrakisphosphate
2 ADP + 2 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
-
in rats and humans
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
in rats and humans
-
-
?
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
-
in rats and humans
-
-
?
ATP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate
-
-
-
-
?
ATP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
-
-
-
-
ir
ATP + 1D-myo-inositol 1,4,5,6-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 1,4,5,6-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,4,5,6-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
-
recombinant enzyme in yeast mutant cells
-
-
?
ATP + 1D-myo-inositol 1,4,5,6-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
-
-
-
-
ir
ATP + 1D-myo-inositol 1,4,5,6-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
-
preferred substrate of isozyme Ipk2
-
-
?
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
-
-
-
-
ir
ATP + 1D-myo-inositol 1,4,5-trisphosphate
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
-
the enzyme initiates a inositol polyphosphate pathway, isozyme Kcs1 is also involved, inositol metabolism, overview
-
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,4,5,6-tetrakisphosphate
-
-
-
-
ir
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,4,5,6-tetrakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,4,5,6-tetrakisphosphate
-
-
-
-
ir
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,4,5,6-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,4,5,6-tetrakisphosphate
-
-
-
-
ir
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,4,5,6-tetrakisphosphate
-
preferred substrate of isozyme Ipk2
-
-
?
ATP + 1D-myo-inositol 4,5-bisphosphate
ADP + 1D-myo-inositol 3,4,5-trisphosphate
-
-
-
?
ATP + 1D-myo-inositol 4,5-bisphosphate
ADP + 1D-myo-inositol 3,4,5-trisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 4,5-bisphosphate
ADP + 1D-myo-inositol 3,4,5-trisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 4,5-bisphosphate
ADP + 1D-myo-inositol 3,4,5-trisphosphate
-
-
-
-
?
additional information
?
-
-
the enzyme is involved in the inositol phosphate metabolism which is important for several cellular functions and signaling, metabolism overview
-
-
?
additional information
?
-
AtIpk2b Is an auxin-inducible gene and is important for the auxin signaling pathway
-
-
?
additional information
?
-
IP3K is involved in axillary shoot branching via Auxin signaling
-
-
?
additional information
?
-
-
Genome-wide RNA interference screen in cultured Drosophila melanogaster haemocyte-like cells identifies as a regulator of the Janus tyrosine kinase/signal transducer and activator of transcription.
-
-
?
additional information
?
-
-
the enzyme is involved in the inositol phosphate metabolism which is important for several cellular functions and signaling, metabolism overview
-
-
?
additional information
?
-
-
the enzyme might be involved in regulation of cell growth
-
-
?
additional information
?
-
-
the enzyme regulates inositol 1,4,5,6-tetrakisphosphate
-
-
?
additional information
?
-
-
inositol (1,4,5,6)-tetrakisphosphate is not a physiological substrate
-
-
?
additional information
?
-
-
role in chromatin remodelling
-
-
?
additional information
?
-
-
Studies in the rat cells and mice suggest that Ins(1,4,5)P3 3-kinases likely contribute little to the synthesis of inositol pentakisphosphate and inositol hexakisphosphate
-
-
?
additional information
?
-
-
The 3-step pathway to InsP6 mediated by phospholipase C, IPMK and inositol kinase (Ipk1) in yeast contrasts with an alternative description of a 5-step pathway in human cells.
-
-
?
additional information
?
-
-
inositol polyphosphate multikinase is a multifunctional enzyme with PI3-kinase, IP3-kinase and catalytically independent activities. IPMK is a PI3-kinase which phosphorylates PIP2 into PIP3, serving as a physiologic activator of Akt/PKB. It also possesses IP3-kinase activity, converting IP3 into IP4 (1,3,4,5) or IP4 (1,4,5,6). Whether the phosphorylation of IP3 at the 3-position or the 6-position is physiologically regulated
-
-
?
additional information
?
-
inositol polyphosphate multikinase is an enzyme that displays soluble inositol phosphate kinase activity, lipid kinase activity, and various noncatalytic interactions
-
-
?
additional information
?
-
-
inositol polyphosphate multikinase is an enzyme that displays soluble inositol phosphate kinase activity, lipid kinase activity, and various noncatalytic interactions
-
-
?
additional information
?
-
IPMK is a broad-specificity enzyme that converts inositol 1,4,5-trisphosphate into inositol 1,4,5,6-tetrakisphosphate (IP4) and subsequently inositol 1,3,4,5,6-pentakisphosphate
-
-
?
additional information
?
-
-
the enzyme plays an essential role in mouse embryogenesis and second messenger production
-
-
?
additional information
?
-
the absence of expression of the three isoenzymes of the inositol 1,4,5-trisphosphate 3-kinase does not prevent the formation of inositol pentakisphosphate and hexakisphosphate
-
-
?
additional information
?
-
-
the absence of expression of the three isoenzymes of the inositol 1,4,5-trisphosphate 3-kinase does not prevent the formation of inositol pentakisphosphate and hexakisphosphate
-
-
?
additional information
?
-
-
role in chromatin remodelling
-
-
?
additional information
?
-
-
Studies in the rat cells and mice suggest that Ins(1,4,5)P3 3-kinases likely contribute little to the synthesis of InsP5 and InsP6
-
-
?
additional information
?
-
-
The 3-step pathway to InsP6 mediated by phospholipase C, IPMK and inositol kinase (Ipk1) in yeast contrasts with an alternative description of a 5-step pathway in human cells.
-
-
?
additional information
?
-
-
the enzyme is involved in regulation of telomere length and cell death, overview
-
-
?
additional information
?
-
-
the enzyme is involved in the inositol phosphate metabolism which is important for several cellular functions and signaling, metabolism overview
-
-
?
additional information
?
-
-
the enzyme is involved inregulation of arginine-sensitive ArgR-Mcm1 transcriptional complex, overview
-
-
?
additional information
?
-
-
the enzyme is required for resistance to salt stress, cell wall integrity, and vascuolar morphogenesis
-
-
?
additional information
?
-
-
the enzyme is involved inregulation of arginine-sensitive ArgR-Mcm1 transcriptional complex, overview
-
-
?
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D100A
isozyme IPK2beta, site-directed mutagenesis, inactive mutant
D98A
isozyme IPK2alpha, site-directed mutagenesis, inactive mutant
K117W
mutant exhibits nearly normal 6-kinase function but harbors significantly reduced 3-kinase activity. The mutant complements conditional nutritional growth defects observed in ipmk null yeast and suppresses lethality observed in ipmk null flies
K117W/K121W
mutant exhibits nearly normal 6-kinase function but harbors significantly reduced 3-kinase activity. The mutant complements conditional nutritional growth defects observed in ipmk null yeast and suppresses lethality observed in ipmk null flies
K121W
although no inositol tetrakisphosphate is present with wild-type IPMK, levels of inositol tetrakisphosphate and inositol hexakisphosphate are equivalent in mutant K121W
D144N
site-directed mutagenesis
D144N/K146A
site-directed mutagenesis
H388A
site-directed mutagenesis, the mutant shows no Ins(1,4,5)P3 3-kinase activity and reduced Ins(1,3,4,5)P4 6-kinase activity compared to wild-type
K129A/S235A
catalytically inactive mutant
K146A
site-directed mutagenesis
K160A
site-directed mutagenesis, the mutant shows no Ins(1,4,5)P3 3-kinase activity and reduced Ins(1,3,4,5)P4 6-kinase activity compared to wild-type
K167A
site-directed mutagenesis, the mutant shows reduced Ins(1,4,5)P3 3-kinase activity and Ins(1,3,4,5)P4 6-kinase activity compared to wild-type
K327Q/K328Q
site-directed mutagenesis, generation of an IPMK mutant with inactivated nuclear localization signal, NLS, whose intracellular distribution is unaffected by inhibition of conventional protein import
Q163A
site-directed mutagenesis, the mutant shows no Ins(1,4,5)P3 3-kinase activity and reduced Ins(1,3,4,5)P4 6-kinase activity compared to wild-type
Q163K
site-directed mutagenesis, the mutant shows reduced Ins(1,4,5)P3 3-kinase activity and increased Ins(1,3,4,5)P4 6-kinase activity compared to wild-type
Q163R
site-directed mutagenesis, the mutant shows reduced Ins(1,4,5)P3 3-kinase activity and increased Ins(1,3,4,5)P4 6-kinase activity compared to wild-type
Q164A
site-directed mutagenesis, the mutant shows reduced Ins(1,4,5)P3 3-kinase activity and Ins(1,3,4,5)P4 6-kinase activity compared to wild-type
Q164K
site-directed mutagenesis, the mutant shows reduced Ins(1,4,5)P3 3-kinase activity and increased Ins(1,3,4,5)P4 6-kinase activity compared to wild-type
Q164R
site-directed mutagenesis, the mutant shows reduced Ins(1,4,5)P3 3-kinase activity and increased Ins(1,3,4,5)P4 6-kinase activity compared to wild-type
Q196A
site-directed mutagenesis, the mutant shows reduced Ins(1,4,5)P3 3-kinase activity and Ins(1,3,4,5)P4 6-kinase activity compared to wild-type
Q196K
site-directed mutagenesis, the mutant shows reduced Ins(1,4,5)P3 3-kinase activity and increased Ins(1,3,4,5)P4 6-kinase activity compared to wild-type
Q196R
site-directed mutagenesis, the mutant shows reduced Ins(1,4,5)P3 3-kinase activity and increased Ins(1,3,4,5)P4 6-kinase activity compared to wild-type
Q78A
site-directed mutagenesis, the mutant shows no Ins(1,4,5)P3 3-kinase activity and reduced Ins(1,3,4,5)P4 6-kinase activity compared to wild-type
R82A
site-directed mutagenesis, the mutant shows no Ins(1,4,5)P3 3-kinase activity and reduced Ins(1,3,4,5)P4 6-kinase activity compared to wild-type
L794A/L801A
-
site-directed mutagenesis, expression in the knockout mutant strain results in activity similar to the wild-type enzyme, phenotype overview
L794A/L801A/L857A/L864A
-
site-directed mutagenesis, expression in the knockout mutant strain results in activity similar to the wild-type enzyme, the mutant strain shows compromised cell wall integrity, phenotype overview
L857A/L864A
-
site-directed mutagenesis, expression in the knockout mutant strain results in activity similar to the wild-type enzyme, phenotype overview
S887A/L888A/L889A
-
site-directed mutagenesis, expression in the knockout mutant strain results in activity similar to the wild-type enzyme, the mutant strain shows compromised cell wall integrity, phenotype overview
additional information
-
construction of an N-terminal deletion mutant comprising residues 266-371, the mutant enzyme is inhibited by aurintricarboxylic acid, gossypol, 3',4',7,8-tetrahydroxyflavone, epigallocatechin-3-gallate, chlorogenic acid, and rose bengal, but not by quercetin, epicatechin-3-gallate, ellagic acid, hypericin, and myricetin in contrary to the wild-type
additional information
genetic or RNA interference-mediated, and shRNA-mediated knockdown of enzyme IPMK
additional information
overexpression of catalytically inactive IPMK mutants is sufficient to reduce RAD51 foci formation
additional information
-
overexpression of catalytically inactive IPMK mutants is sufficient to reduce RAD51 foci formation
additional information
generation of the core catalytic domain of the enzyme that contains residues 50 to 416, from which an internal domain comprising residues 263 to 377 is deleted. The deletion is necessary to obtain crystals, it is replaced with a simple Gly-Gly-Ser-Gly-Gly linker. This deletion does not compromise catalytic activity, it is a non-catalytic region of the protein. It contains a nuclear localization sequence, flanked by residues that host protein kinase phosphorylation sites that regulate nuclear localization sequence functionality. Gln residues at positions 163, 164, and 196 are mutated each to Arg and Lys, both of which have side chains that are larger and also positively charged at physiological pH. The results are quite dramatic: in each case, the rate of Ins(1,4,5)P3 3-kinase activity declines, but in contrast, the rate of Ins(1,3,4,5)P4 6-kinase activity is not impaired, three of these mutants show increased 6-kinase activity, analysis of the structural basis, overview
additional information
-
generation of the core catalytic domain of the enzyme that contains residues 50 to 416, from which an internal domain comprising residues 263 to 377 is deleted. The deletion is necessary to obtain crystals, it is replaced with a simple Gly-Gly-Ser-Gly-Gly linker. This deletion does not compromise catalytic activity, it is a non-catalytic region of the protein. It contains a nuclear localization sequence, flanked by residues that host protein kinase phosphorylation sites that regulate nuclear localization sequence functionality. Gln residues at positions 163, 164, and 196 are mutated each to Arg and Lys, both of which have side chains that are larger and also positively charged at physiological pH. The results are quite dramatic: in each case, the rate of Ins(1,4,5)P3 3-kinase activity declines, but in contrast, the rate of Ins(1,3,4,5)P4 6-kinase activity is not impaired, three of these mutants show increased 6-kinase activity, analysis of the structural basis, overview
additional information
-
construction of mutants by disrution of gene ipk2, the resulting enzyme-deficient Ipk2 null mice die around embryonic day 9.5 with multiple morphological defects, including abnormal folding of the neural tube, overview
additional information
-
an enzyme-deficient mutant strain is resistant to inhibition by wortmannin, while transformation with the wild-type enzyme reverses the effect, the enzyme-deficient mutant shows increased phosphatidylinositol 4,5-bisphosphate levels
additional information
-
construction of a knockout mutant strain from strain BY4709, the mutant cells contain a fragmented vacuolar compartment, cell growth and cell wall integrity are perturbed, and response to sal stress is altered, a metabolic block in arg82DELTA cells results in the same phenotype, overexpression of the enzyme can partially bypass the metabolic block, overview, expression of full length enzyme and enzyme mutants in the knockout strain, phenotypes overview
additional information
-
growth of an enzyme-deficient strain can be rescued by expression of either 1D-myo-inositol 1,4,5-trisphosphate 3-kinase or 6-kinase at high temperatures, but only 1D-myo-inositol 1,4,5-trisphosphate 6-kinase expression enables the strain to grow on ornithine
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Chakrabarti, S.; Biswas, B.B.
Metabolism of inositol phosphates. Part XIV. Evidence for the existence of a phosphoinositol kinase in chicken erythrocytes
Indian J. Biochem. Biophys.
18
398-401
1981
Gallus gallus
brenda
Yotsushima, K.; Mitsui, T.; Hayakawa, T.
Purification of phosphoinositol kinase from suspension-cultured cells of rice (Oryza sativa L.)
Biosci. Biotechnol. Biochem.
59
1953-1955
1995
Oryza sativa
-
brenda
Saiardi, A.; Erdjument-Bromage, H.; Snowman, A.M.; Tempst, P.; Snyder, S.H.
Synthesis of diphosphoinositol pentakisphosphate by a newly identified family of higher inositol polyphosphate kinases
Curr. Biol.
9
1323-1326
1999
Saccharomyces cerevisiae
brenda
York, J.D.; Odom, A.R.; Murphy, R.; Ives, E.B.; Wente, S.R.
A phospholipase C-dependent inositol polyphosphate kinase pathway required for efficient messenger RNA export
Science
285
96-100
1999
Saccharomyces cerevisiae
brenda
Saiardi, A.; Caffrey, J.J.; Snyder, S.H.; Shears, S.B.
Corrigendum to: activation of interstitial collagenase, MMP-1, by staphylococcus aureus cells having surface-bound plasmin: a novel role of plasminogen receptors of bacteria
FEBS Lett.
469
213
2000
Saccharomyces cerevisiae
brenda
Saiardi, A.; Nagata, E.; Luo, H.R.; Sawa, A.; Luo, X.; Snowman, A.M.; Snyder, S.H.
Mammalian inositol polyphosphate multikinase synthesizes inositol 1,4,5-trisphosphate and an inositol pyrophosphate
Proc. Natl. Acad. Sci. USA
98
2306-2311
2001
Rattus norvegicus (Q99NI4)
brenda
Chang, S.C.; Miller, A.L.; Feng, Y.; Wente, S.R.; Majerus, P.W.
The human homolog of the rat inositol phosphate multikinase is an inositol 1,3,4,6-tetrakisphosphate 5-kinase
J. Biol. Chem.
277
43836-43843
2002
Homo sapiens
brenda
Chang, S.C.; Majerus, P.W.
Inositol polyphosphate multikinase regulates inositol 1,4,5,6-tetrakisphosphate
Biochem. Biophys. Res. Commun.
339
209-216
2006
Homo sapiens
brenda
Nalaskowski, M.M.; Deschermeier, C.; Fanick, W.; Mayr, G.W.
The human homologue of yeast ArgRIII protein is an inositol phosphate multikinase with predominantly nuclear localization
Biochem. J.
366
549-556
2002
Homo sapiens (Q8NFU5), Homo sapiens
brenda
Xia, H.J.; Yang, G.
Inositol 1,4,5-trisphosphate 3-kinases: functions and regulations
Cell Res.
15
83-91
2005
Arabidopsis thaliana, Saccharomyces cerevisiae, Homo sapiens
brenda
Dubois, E.; Scherens, B.; Vierendeels, F.; Ho, M.M.W.; Messenguy, F.; Shears, S.B.
In Saccharomyces cerevisiae, the inositol polyphosphate kinase activity of Kcs1p is required for resistance to salt stress, cell wall integrity, and vacuolar morphogenesis
J. Biol. Chem.
277
23755-23763
2002
Saccharomyces cerevisiae
brenda
Stevenson-Paulik, J.; Odom, A.R.; York, J.D.
Molecular and biochemical characterization of two plant inositol polyphosphate 6-/3-/5-kinases
J. Biol. Chem.
277
42711-42718
2002
Arabidopsis thaliana (Q9FLT2), Arabidopsis thaliana (Q9LY23), Arabidopsis thaliana
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
Homo sapiens
brenda
Seeds, A.M.; Bastidas, R.J.; York, J.D.
Molecular definition of a novel inositol polyphosphate metabolic pathway initiated by inositol 1,4,5-trisphosphate 3-kinase activity in Saccharomyces cerevisiae
J. Biol. Chem.
280
27654-27661
2005
Saccharomyces cerevisiae
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
brenda
Saiardi, A.; Resnick, A.C.; Snowman, A.M.; Wendland, B.; Snyder, S.H.
Inositol pyrophosphates regulate cell death and telomere length through phosphoinositide 3-kinase-related protein kinases
Proc. Natl. Acad. Sci. USA
102
1911-1914
2005
Saccharomyces cerevisiae
brenda
Frederick, J.P.; Mattiske, D.; Wofford, J.A.; Megosh, L.C.; Drake, L.Y.; Chiou, S.T.; Hogan, B.L.; York, J.D.
An essential role for an inositol polyphosphate multikinase, Ipk2, in mouse embryogenesis and second messenger production
Proc. Natl. Acad. Sci. USA
102
8454-8459
2005
Mus musculus
brenda
Caddick, S.E.; Harrison, C.J.; Stavridou, I.; Johnson, S.; Brearley, C.A.
A lysine accumulation phenotype of ScIpk2Delta mutant yeast is rescued by Solanum tuberosum inositol phosphate multikinase
Biochem. J.
403
381-389
2007
Solanum tuberosum (A4H2J1), Solanum tuberosum
brenda
Leyman, A.; Pouillon, V.; Bostan, A.; Schurmans, S.; Erneux, C.; Pesesse, X.
The absence of expression of the three isoenzymes of the inositol 1,4,5-trisphosphate 3-kinase does not prevent the formation of inositol pentakisphosphate and hexakisphosphate in mouse embryonic fibroblasts
Cell. Signal.
19
1497-1504
2007
Mus musculus (Q7TT16), Mus musculus
brenda
Riley, A.M.; Deleu, S.; Qian, X.; Mitchell, J.; Chung, S.; Adelt, S.; Vogel, G.; Potter, B.V.; Shears, S.B.
On the contribution of stereochemistry to human ITPK1 specificity: Ins(1,4,5,6)P4 is not a physiologic substrate
FEBS Lett.
580
324-330
2006
Homo sapiens
brenda
Holmes, W.; Jogl, G.
Crystal structure of inositol phosphate multikinase 2 and implications for substrate specificity
J. Biol. Chem.
281
38109-38116
2006
Saccharomyces cerevisiae
brenda
Gao, Y.; Wang, H.Y.
Inositol pentakisphosphate mediates Wnt/beta-catenin signaling
J. Biol. Chem.
282
26490-26502
2007
Mus musculus
brenda
Resnick, A.C.; Saiardi, A.
Inositol polyphosphate multikinase: metabolic architect of nuclear inositides
Front. Biosci.
13
856-866
2008
Arabidopsis thaliana, Saccharomyces cerevisiae, Drosophila melanogaster, Homo sapiens, Rattus norvegicus, Solanum tuberosum
brenda
Yang, L.; Tang, R.; Zhu, J.; Liu, H.; Mueller-Roeber, B.; Xia, H.; Zhang, H.
Enhancement of stress tolerance in transgenic tobacco plants constitutively expressing AtIpk2beta, an inositol polyphosphate 6-/3-kinase from Arabidopsis thaliana
Plant Mol. Biol.
66
329-343
2008
Arabidopsis thaliana
brenda
Zhang, Z.B.; Yang, G.; Arana, F.; Chen, Z.; Li, Y.; Xia, H.J.
Arabidopsis inositol polyphosphate 6-/3-kinase (AtIpk2beta) is involved in axillary shoot branching via auxin signaling
Plant Physiol.
144
942-951
2007
Arabidopsis thaliana (Q9LY23)
brenda
Zhang, Y.; Liu, H.; Li, B.; Zhang, J.T.; Li, Y.; Zhang, H.
Generation of selectable marker-free transgenic tomato resistant to drought, cold and oxidative stress using the Cre/loxP DNA excision system
Transgenic Res.
18
607-619
2009
Arabidopsis thaliana (Q9FLT2), Arabidopsis thaliana
brenda
Kim, S.; Kim, S.F.; Maag, D.; Maxwell, M.J.; Resnick, A.C.; Juluri, K.R.; Chakraborty, A.; Koldobskiy, M.A.; Cha, S.H.; Barrow, R.; Snowman, A.M.; Snyder, S.H.
Amino acid signaling to mTOR mediated by inositol polyphosphate multikinase
Cell Metab.
13
215-221
2011
Mus musculus
brenda
Endo-Streeter, S.; Tsui, M.K.; Odom, A.R.; Block, J.; York, J.D.
Structural studies and protein engineering of inositol phosphate multikinase
J. Biol. Chem.
287
35360-35369
2012
Arabidopsis thaliana (Q9LY23), Arabidopsis thaliana
brenda
Maag, D.; Maxwell, M.J.; Hardesty, D.A.; Boucher, K.L.; Choudhari, N.; Hanno, A.G.; Ma, J.F.; Snowman, A.S.; Pietropaoli, J.W.; Xu, R.; Storm, P.B.; Saiardi, A.; Snyder, S.H.; Resnick, A.C.
Inositol polyphosphate multikinase is a physiologic PI3-kinase that activates Akt/PKB
Proc. Natl. Acad. Sci. USA
108
1391-1396
2011
Mus musculus
brenda
Bang, S.; Kim, S.; Dailey, M.J.; Chen, Y.; Moran, T.H.; Snyder, S.H.; Kim, S.F.
AMP-activated protein kinase is physiologically regulated by inositol polyphosphate multikinase
Proc. Natl. Acad. Sci. USA
109
616-620
2012
Mus musculus
brenda
Xu, R.; Snyder, S.
Gene transcription by p53 requires inositol polyphosphate multikinase as a co-activator
Cell Cycle
12
1819-1820
2013
Homo sapiens
brenda
Wickramasinghe, V.O.; Savill, J.M.; Chavali, S.; Jonsdottir, A.B.; Rajendra, E.; Gruener, T.; Laskey, R.A.; Babu, M.M.; Venkitaraman, A.R.
Human inositol polyphosphate multikinase regulates transcript-selective nuclear mRNA export to preserve genome integrity
Mol. Cell
51
737-750
2013
Homo sapiens (Q8NFU5), Homo sapiens
brenda
Xu, R.; Paul, B.D.; Smith, D.R.; Tyagi, R.; Rao, F.; Khan, A.B.; Blech, D.J.; Vandiver, M.S.; Harraz, M.M.; Guha, P.; Ahmed, I.; Sen, N.; Gallagher, M.; Snyder, S.H.
Inositol polyphosphate multikinase is a transcriptional coactivator required for immediate early gene induction
Proc. Natl. Acad. Sci. USA
110
16181-16186
2013
Mus musculus (Q7TT16)
brenda
Ahmed, I.; Sbodio, J.I.; Harraz, M.M.; Tyagi, R.; Grima, J.C.; Albacarys, L.K.; Hubbi, M.E.; Xu, R.; Kim, S.; Paul, B.D.; Snyder, S.H.
Huntingtons disease: neural dysfunction linked to inositol polyphosphate multikinase
Proc. Natl. Acad. Sci. USA
112
9751-9756
2015
Homo sapiens (Q8NFU5), Homo sapiens
brenda
Xu, R.; Sen, N.; Paul, B.D.; Snowman, A.M.; Rao, F.; Vandiver, M.S.; Xu, J.; Snyder, S.H.
Inositol polyphosphate multikinase is a coactivator of p53-mediated transcription and cell death
Sci. Signal.
6
ra22
2013
Homo sapiens (Q8NFU5)
brenda
Wang, H.; Shears, S.B.
Structural features of human inositol phosphate multikinase rationalize its inositol phosphate kinase and phosphoinositide 3-kinase activities
J. Biol. Chem.
292
18192-18202
2017
Homo sapiens (Q8NFU5), Homo sapiens
brenda