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1D-myo-inositol 1,3,4-trisphosphate + ATP
1D-myo-inositol 1,3,4,5-tetrakisphosphate + ADP
A1KXK8
key enzyme in the inositol phosphate pathway and a negative regulator of osmotic stress signaling
-
-
?
1D-myo-inositol 1,3,4-trisphosphate + ATP
1D-myo-inositol 1,3,4,6-tetrakisphosphate + ADP
A1KXK8
key enzyme in the inositol phosphate pathway and a negative regulator of osmotic stress signaling
-
-
?
1D-myo-inositol-1,3,4,5,6-pentakisphosphate + ADP
1D-myo-inositol-3,4,5,6-tetrakisphosphate + ATP
-
enzyme catalyzes both forward and reverse reaction
putative regulator of Ca2+-activated chloride channels.
-
r
1D-myo-inositol-1,3,4,5-tetrakisphosphate + ATP
1D-myo-inositol-1,3,4,5,6-pentakisphosphate + ADP
-
-
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r
1D-myo-inositol-1,3,4,5-tetrakisphosphate + ATP
1D-myo-inositol-1,3,4,6-tetrakisphosphate + ATP
enzyme displays isomerase activity
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-
?
1D-myo-inositol-1,3,4,6-tetrakisphosphate + ATP
1D-myo-inositol-1,3,4,5,6-pentakisphosphate + ADP
-
-
-
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r
1D-myo-inositol-1,3,4-trisphosphate + ATP
1D-myo-inositol-1,3,4,5-tetrakisphosphate + ADP
-
-
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-
r
1D-myo-inositol-1,3,4-trisphosphate + ATP
1D-myo-inositol-1,3,4,6-tetrakisphosphate + ADP
1D-myo-inositol-1,4,5,6-tetrakisphosphate + ATP
1D-myo-inositol-1,3,4,6-tetrakisphosphate + ATP
AtITPK4 is more active against 1D-myo-inositol-1,4,5,6-tetrakisphosphate than against 1D-myo-inositol-3,4,5,6-tetrakisphosphate.
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?
1D-myo-inositol-1,4,6-trisphosphate + 1D-myo-inositol-3,4,6-trisphosphate + 2 ATP
2 1D-myo-inositol-1,3,4,6-tetrakisphosphate + 2 ADP
racemic mixture
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?
1D-myo-inositol-3,4,5,6-tetrakisphosphate + ATP
1D-myo-inositol-1,3,4,6-tetrakisphosphate + ATP
enzyme displays isomerase activity
-
-
?
ATP + 1D-myo-inositol 1,3,4-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
ATP + 1D-myo-inositol 1,3,4-trisphosphate
ADP + 1D-myo-inositol 1,3,4,6-tetrakisphosphate
ATP + 1D-myo-inositol 1,4,6-trisphosphate + 1D-myo-inositol 3,4,6-trisphosphate
ADP + inositol tetrakisphosphate
racemic mix of phosphates
-
-
?
ATP + 1D-myo-inositol 3,4,5,6-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-trisphosphate
?
-
-
-
?
ATP + 1D-myo-inositol-1,3,4-trisphosphate
ADP + 1D-myo-inositol-1,3,4,5-tetrakisphosphate
ATP + 1D-myo-inositol-1,3,4-trisphosphate
ADP + 1D-myo-inositol-1,3,4,6-tetrakisphosphate
ATP + ATF-2
ADP + phosphorylated ATF-2
ATP + c-Jun
ADP + phosphorylated c-Jun
ATP + IkappaBalpha
ADP + phosphorylated IkappaBalpha
-
substrate of the free enzyme and the COP9 signalosome complex
-
-
?
ATP + p53
ADP + phosphorylated p53
-
substrate of the free enzyme and the COP9 signalosome complex
-
-
?
additional information
?
-
1D-myo-inositol-1,3,4-trisphosphate + ATP
1D-myo-inositol-1,3,4,6-tetrakisphosphate + ADP
-
-
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?
1D-myo-inositol-1,3,4-trisphosphate + ATP
1D-myo-inositol-1,3,4,6-tetrakisphosphate + ADP
-
-
-
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r
ATP + 1D-myo-inositol 1,3,4-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,3,4-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,3,4-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,3,4-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,3,4-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,3,4-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 1,3,4-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,3,4-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 1,3,4-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,3,4-trisphosphate
ADP + 1D-myo-inositol 1,3,4,6-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,3,4-trisphosphate
ADP + 1D-myo-inositol 1,3,4,6-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,3,4-trisphosphate
ADP + 1D-myo-inositol 1,3,4,6-tetrakisphosphate
-
-
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?
ATP + 1D-myo-inositol 1,3,4-trisphosphate
ADP + 1D-myo-inositol 1,3,4,6-tetrakisphosphate
-
-
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?
ATP + 1D-myo-inositol 1,3,4-trisphosphate
ADP + 1D-myo-inositol 1,3,4,6-tetrakisphosphate
The substrate is converted to InsP4 but not to InsP5
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?
ATP + 1D-myo-inositol 1,3,4-trisphosphate
ADP + 1D-myo-inositol 1,3,4,6-tetrakisphosphate
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-
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?
ATP + 1D-myo-inositol 1,3,4-trisphosphate
ADP + 1D-myo-inositol 1,3,4,6-tetrakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 1,3,4-trisphosphate
ADP + 1D-myo-inositol 1,3,4,6-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,3,4-trisphosphate
ADP + 1D-myo-inositol 1,3,4,6-tetrakisphosphate
-
-
-
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?
ATP + 1D-myo-inositol 1,3,4-trisphosphate
ADP + 1D-myo-inositol 1,3,4,6-tetrakisphosphate
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-
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?
ATP + 1D-myo-inositol 3,4,5,6-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
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?
ATP + 1D-myo-inositol 3,4,5,6-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
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r
ATP + 1D-myo-inositol-1,3,4-trisphosphate
ADP + 1D-myo-inositol-1,3,4,5-tetrakisphosphate
-
recombinant enzyme, 3fold lower activity compared to 1D-myo-inositol-1,3,4,6-tetrakisphosphate formation
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?
ATP + 1D-myo-inositol-1,3,4-trisphosphate
ADP + 1D-myo-inositol-1,3,4,5-tetrakisphosphate
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-
-
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?
ATP + 1D-myo-inositol-1,3,4-trisphosphate
ADP + 1D-myo-inositol-1,3,4,5-tetrakisphosphate
-
5fold lower activity compared to 1D-myo-inositol-1,3,4,6-tetrakisphosphate formation
-
-
?
ATP + 1D-myo-inositol-1,3,4-trisphosphate
ADP + 1D-myo-inositol-1,3,4,5-tetrakisphosphate
-
lower activity compared to 1D-myo-inositol-1,3,4,6-tetrakisphosphate formation
-
-
?
ATP + 1D-myo-inositol-1,3,4-trisphosphate
ADP + 1D-myo-inositol-1,3,4,5-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol-1,3,4-trisphosphate
ADP + 1D-myo-inositol-1,3,4,5-tetrakisphosphate
-
the formation of 1D-myo-inositol-1,3,4,6-tetrakisphosphate is slightly preferred compared to formation of 1D-myo-inositol-1,3,4,5-tetrakisphosphate, ratio 1.5:1
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?
ATP + 1D-myo-inositol-1,3,4-trisphosphate
ADP + 1D-myo-inositol-1,3,4,5-tetrakisphosphate
-
the formation of 1D-myo-inositol-1,3,4,6-tetrakisphosphate is slightly preferred compared to formation of 1D-myo-inositol-1,3,4,5-tetrakisphosphate, ratio 1.5:1
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?
ATP + 1D-myo-inositol-1,3,4-trisphosphate
ADP + 1D-myo-inositol-1,3,4,5-tetrakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol-1,3,4-trisphosphate
ADP + 1D-myo-inositol-1,3,4,5-tetrakisphosphate
-
5fold lower activity compared to 1D-myo-inositol-1,3,4,6-tetrakisphosphate formation
-
-
?
ATP + 1D-myo-inositol-1,3,4-trisphosphate
ADP + 1D-myo-inositol-1,3,4,5-tetrakisphosphate
lower activity compared to 1D-myo-inositol-1,3,4,6-tetrakisphosphate formation
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-
?
ATP + 1D-myo-inositol-1,3,4-trisphosphate
ADP + 1D-myo-inositol-1,3,4,5-tetrakisphosphate
-
substrate of the free enzyme and the COP9 signalosome complex
-
-
?
ATP + 1D-myo-inositol-1,3,4-trisphosphate
ADP + 1D-myo-inositol-1,3,4,5-tetrakisphosphate
-
5fold lower activity compared to 1D-myo-inositol-1,3,4,6-tetrakisphosphate formation
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-
?
ATP + 1D-myo-inositol-1,3,4-trisphosphate
ADP + 1D-myo-inositol-1,3,4,6-tetrakisphosphate
-
recombinant enzyme, 3fold higher activity compared to 1D-myo-inositol-1,3,4,5-tetrakisphosphate formation
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?
ATP + 1D-myo-inositol-1,3,4-trisphosphate
ADP + 1D-myo-inositol-1,3,4,6-tetrakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol-1,3,4-trisphosphate
ADP + 1D-myo-inositol-1,3,4,6-tetrakisphosphate
-
5fold higher activity compared to 1D-myo-inositol-1,3,4,5-tetrakisphosphate formation
-
-
?
ATP + 1D-myo-inositol-1,3,4-trisphosphate
ADP + 1D-myo-inositol-1,3,4,6-tetrakisphosphate
-
higher activity compared to 1D-myo-inositol-1,3,4,5-tetrakisphosphate formation
-
-
?
ATP + 1D-myo-inositol-1,3,4-trisphosphate
ADP + 1D-myo-inositol-1,3,4,6-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol-1,3,4-trisphosphate
ADP + 1D-myo-inositol-1,3,4,6-tetrakisphosphate
-
the formation of 1D-myo-inositol-1,3,4,6-tetrakisphosphate is slightly preferred compared to formation of 1D-myo-inositol-1,3,4,5-tetrakisphosphate, ratio 1.5:1
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?
ATP + 1D-myo-inositol-1,3,4-trisphosphate
ADP + 1D-myo-inositol-1,3,4,6-tetrakisphosphate
-
the formation of 1D-myo-inositol-1,3,4,6-tetrakisphosphate is slightly preferred compared to formation of 1D-myo-inositol-1,3,4,5-tetrakisphosphate, ratio 1.5:1
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?
ATP + 1D-myo-inositol-1,3,4-trisphosphate
ADP + 1D-myo-inositol-1,3,4,6-tetrakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol-1,3,4-trisphosphate
ADP + 1D-myo-inositol-1,3,4,6-tetrakisphosphate
-
5fold higher activity compared to 1D-myo-inositol-1,3,4,5-tetrakisphosphate formation
-
-
?
ATP + 1D-myo-inositol-1,3,4-trisphosphate
ADP + 1D-myo-inositol-1,3,4,6-tetrakisphosphate
higher activity compared to 1D-myo-inositol-1,3,4,5-tetrakisphosphate formation
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-
?
ATP + 1D-myo-inositol-1,3,4-trisphosphate
ADP + 1D-myo-inositol-1,3,4,6-tetrakisphosphate
-
substrate of the free enzyme and the COP9 signalosome complex
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-
?
ATP + 1D-myo-inositol-1,3,4-trisphosphate
ADP + 1D-myo-inositol-1,3,4,6-tetrakisphosphate
-
5fold higher activity compared to 1D-myo-inositol-1,3,4,5-tetrakisphosphate formation
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-
?
ATP + ATF-2
ADP + phosphorylated ATF-2
-
phosphorylation predominantly on serine residues
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?
ATP + ATF-2
ADP + phosphorylated ATF-2
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phosphorylation predominantly on serine residues
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?
ATP + c-Jun
ADP + phosphorylated c-Jun
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?
ATP + c-Jun
ADP + phosphorylated c-Jun
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?
ATP + c-Jun
ADP + phosphorylated c-Jun
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substrate of the free enzyme and the COP9 signalosome complex, which both show no activity with the 1-79 residue fragment of c-Jun
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?
additional information
?
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the enzyme is involved in photomorphogenesis under red light conditions
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?
additional information
?
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the enzyme performs autophosphorylation, the enzyme is associated with the COP9 signalosome, i.e. CSN
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?
additional information
?
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the enzyme displays inositol 1,4,5,6-tetrakisphosphate and inositol 1,3,4,5-tetrakisphosphate isomerase activity. It lacks the Ins(3,4,5,6)P4 1-kinase
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?
additional information
?
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the enzyme displays inositol 1,4,5,6-tetrakisphosphate and inositol 1,3,4,5-tetrakisphosphate isomerase activity. It lacks the Ins(3,4,5,6)P4 1-kinase
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?
additional information
?
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the enzyme displays inositol 1,4,5,6-tetrakisphosphate and inositol 1,3,4,5-tetrakisphosphate isomerase activity. It lacks the Ins(3,4,5,6)P4 1-kinase
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?
additional information
?
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the enzyme displays inositol 1,4,5,6-tetrakisphosphate and inositol 1,3,4,5-tetrakisphosphate isomerase activity. It lacks the Ins(3,4,5,6)P4 1-kinase
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?
additional information
?
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the enzyme displays inositol 1,4,5,6-tetrakisphosphate and inositol 1,3,4,5-tetrakisphosphate isomerase activity. It lacks the Ins(3,4,5,6)P4 1-kinase
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?
additional information
?
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AtITPK4 differs from other family members in that it not display inositol 3,4,5,6-tetrakisphosphate 1-kinase activity. It displays inositol 1,4,5,6-tetrakisphosphate and inositol-1,3,4,5-tetrakisphosphate isomerase activity. With inositol tetrakisphosphate substrates, ITPK4 displays an isomerase activity (in the absence of inositol pentakisphosphate product) interpreting as phosphatase and kinase activity. AtITPK4 shows isomerase activity against other substrates. Removal of the 1- or 3-phosphate of inositol-1,3,4,6-tetrakisphosphate and subsequent rephosphorylation at the same position generates inositol-1,3,4,6-tetrakisphosphate.
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?
additional information
?
-
AtITPK4 differs from other family members in that it not display inositol 3,4,5,6-tetrakisphosphate 1-kinase activity. It displays inositol 1,4,5,6-tetrakisphosphate and inositol-1,3,4,5-tetrakisphosphate isomerase activity. With inositol tetrakisphosphate substrates, ITPK4 displays an isomerase activity (in the absence of inositol pentakisphosphate product) interpreting as phosphatase and kinase activity. AtITPK4 shows isomerase activity against other substrates. Removal of the 1- or 3-phosphate of inositol-1,3,4,6-tetrakisphosphate and subsequent rephosphorylation at the same position generates inositol-1,3,4,6-tetrakisphosphate.
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?
additional information
?
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AtITPK4 differs from other family members in that it not display inositol 3,4,5,6-tetrakisphosphate 1-kinase activity. It displays inositol 1,4,5,6-tetrakisphosphate and inositol-1,3,4,5-tetrakisphosphate isomerase activity. With inositol tetrakisphosphate substrates, ITPK4 displays an isomerase activity (in the absence of inositol pentakisphosphate product) interpreting as phosphatase and kinase activity. AtITPK4 shows isomerase activity against other substrates. Removal of the 1- or 3-phosphate of inositol-1,3,4,6-tetrakisphosphate and subsequent rephosphorylation at the same position generates inositol-1,3,4,6-tetrakisphosphate.
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?
additional information
?
-
AtITPK4 differs from other family members in that it not display inositol 3,4,5,6-tetrakisphosphate 1-kinase activity. It displays inositol 1,4,5,6-tetrakisphosphate and inositol-1,3,4,5-tetrakisphosphate isomerase activity. With inositol tetrakisphosphate substrates, ITPK4 displays an isomerase activity (in the absence of inositol pentakisphosphate product) interpreting as phosphatase and kinase activity. AtITPK4 shows isomerase activity against other substrates. Removal of the 1- or 3-phosphate of inositol-1,3,4,6-tetrakisphosphate and subsequent rephosphorylation at the same position generates inositol-1,3,4,6-tetrakisphosphate.
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?
additional information
?
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AtITPK4 differs from other family members in that it not display inositol 3,4,5,6-tetrakisphosphate 1-kinase activity. It displays inositol 1,4,5,6-tetrakisphosphate and inositol-1,3,4,5-tetrakisphosphate isomerase activity. With inositol tetrakisphosphate substrates, ITPK4 displays an isomerase activity (in the absence of inositol pentakisphosphate product) interpreting as phosphatase and kinase activity. AtITPK4 shows isomerase activity against other substrates. Removal of the 1- or 3-phosphate of inositol-1,3,4,6-tetrakisphosphate and subsequent rephosphorylation at the same position generates inositol-1,3,4,6-tetrakisphosphate.
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additional information
?
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enzyme displays both kinase and phosphatase activity.
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?
additional information
?
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enzyme displays both kinase and phosphatase activity.
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?
additional information
?
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enzyme displays both kinase and phosphatase activity.
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?
additional information
?
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enzyme displays both kinase and phosphatase activity.
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?
additional information
?
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enzyme displays both kinase and phosphatase activity.
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?
additional information
?
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the enzyme also performs the reaction of EC 2.7.1.134, phosphorylation of position 1 of 1D-myo-inositol 3,4,5,6-tetrakisphosphate
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?
additional information
?
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the enzyme also performs the reaction of EC 2.7.1.134, phosphorylation of position 1 of 1D-myo-inositol 3,4,5,6-tetrakisphosphate
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?
additional information
?
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the enzyme also performs the reaction of EC 2.7.1.134, phosphorylation of position 1 of 1D-myo-inositol 3,4,5,6-tetrakisphosphate
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?
additional information
?
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the enzyme is involved in both the inositol phosphate and the stress response pathways which are linked by the enzyme, overview
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?
additional information
?
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the enzyme is part of the COP9 signalosome complex consisting of 8 proteins
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?
additional information
?
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the enzyme also preferably performs the phosphoinositol trisphosphate 3-kinase reaction with 1D-myo-inositol-1,4,5-trisphosphate as substrate, EC 2.7.1.127, no activity with 1D-myo-inositol-1,4-bisphosphate
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?
additional information
?
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the enzyme shows multiple activities
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additional information
?
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the enzyme also preferably performs the phosphoinositol trisphosphate 3-kinase reaction with 1D-myo-inositol-1,4,5-trisphosphate as substrate, EC 2.7.1.127, no activity with 1D-myo-inositol-1,4-bisphosphate
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?
additional information
?
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ITPK can also interconvert Ins (3,4,5,6)P4 and Ins (1,3,4,5,6)P5 within a substrate cycle to regulate the concentration of Ins (3,4,5,6)P4
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additional information
?
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regulation of enzymes involved in the inositol phosphate metabolism in human cells, overview
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?
additional information
?
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the enzyme inhibits tumor necrosis factor alpha-induced apoptosis involving the activation of PARP, BID, caspase-3 and caspase-8, but protects not against etoposide- or cycloheximide-induced apotosis, mechanism
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?
additional information
?
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the enzyme associates with the COP9 signalosome, an complex of 8 proteins, by binding to CSN1
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?
additional information
?
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the enzyme is part of the COP9 signalosome complex consisting of 8 proteins
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?
additional information
?
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integration of inositol phosphate signaling pathways via human ITPK1
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?
additional information
?
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enzyme has both phosphatase and kinase activity
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?
additional information
?
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The enzyme can phosphorylate both 1D-myo-inositol-1,3,4-trisphosphate at the 5 or 6 positions and 1D-myo-inositol-3,4,5,6-tetrakisphosphate at the 1 position and can also dephosphorylate 1D-myo-inositol-1,3,4,5,6-pentaakisphosphate to 1D-myo-inositol-3,4,5,6-tetrakisphosphate
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?
additional information
?
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The phenomenon of intersubstrate transfer is only found in the human enzyme, which can use 1D-myo-inositol 1,3,4-trisphosphate to regulate increased cellular concentrations of 1D-myo-inositol-3,4,5,6-tetrakisphosphate
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?
additional information
?
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the various enzyme activities manifested by ITPK1 provide a molecular mechanism that allows the receptor-activated changes in phospholipase C activity and consequent increases in the concentration of 1D-myo-inositol 1,3,4-trisphosphate to regulate the abundance of 1D-myo-inositol-3,4,5,6-tetrakisphosphate
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-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1D-myo-inositol 1,3,4-trisphosphate + ATP
1D-myo-inositol 1,3,4,5-tetrakisphosphate + ADP
A1KXK8
key enzyme in the inositol phosphate pathway and a negative regulator of osmotic stress signaling
-
-
?
1D-myo-inositol 1,3,4-trisphosphate + ATP
1D-myo-inositol 1,3,4,6-tetrakisphosphate + ADP
A1KXK8
key enzyme in the inositol phosphate pathway and a negative regulator of osmotic stress signaling
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-
?
1D-myo-inositol-1,3,4,5,6-pentakisphosphate + ADP
1D-myo-inositol-3,4,5,6-tetrakisphosphate + ATP
-
enzyme catalyzes both forward and reverse reaction
putative regulator of Ca2+-activated chloride channels.
-
r
1D-myo-inositol-1,3,4,5-tetrakisphosphate + ATP
1D-myo-inositol-1,3,4,5,6-pentakisphosphate + ADP
-
-
-
-
r
1D-myo-inositol-1,3,4,5-tetrakisphosphate + ATP
1D-myo-inositol-1,3,4,6-tetrakisphosphate + ATP
enzyme displays isomerase activity
-
-
?
1D-myo-inositol-1,3,4,6-tetrakisphosphate + ATP
1D-myo-inositol-1,3,4,5,6-pentakisphosphate + ADP
-
-
-
-
r
1D-myo-inositol-1,3,4-trisphosphate + ATP
1D-myo-inositol-1,3,4,5-tetrakisphosphate + ADP
-
-
-
-
r
1D-myo-inositol-1,3,4-trisphosphate + ATP
1D-myo-inositol-1,3,4,6-tetrakisphosphate + ADP
1D-myo-inositol-1,4,6-trisphosphate + 1D-myo-inositol-3,4,6-trisphosphate + 2 ATP
2 1D-myo-inositol-1,3,4,6-tetrakisphosphate + 2 ADP
racemic mixture
-
-
?
1D-myo-inositol-3,4,5,6-tetrakisphosphate + ATP
1D-myo-inositol-1,3,4,6-tetrakisphosphate + ATP
enzyme displays isomerase activity
-
-
?
ATP + 1D-myo-inositol 1,3,4-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
ATP + 1D-myo-inositol 1,3,4-trisphosphate
ADP + 1D-myo-inositol 1,3,4,6-tetrakisphosphate
ATP + 1D-myo-inositol 1,4,6-trisphosphate + 1D-myo-inositol 3,4,6-trisphosphate
ADP + inositol tetrakisphosphate
racemic mix of phosphates
-
-
?
ATP + 1D-myo-inositol 3,4,5,6-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
-
-
-
?
ATP + 1D-myo-inositol-1,3,4-trisphosphate
ADP + 1D-myo-inositol-1,3,4,5-tetrakisphosphate
ATP + 1D-myo-inositol-1,3,4-trisphosphate
ADP + 1D-myo-inositol-1,3,4,6-tetrakisphosphate
additional information
?
-
1D-myo-inositol-1,3,4-trisphosphate + ATP
1D-myo-inositol-1,3,4,6-tetrakisphosphate + ADP
-
-
-
?
1D-myo-inositol-1,3,4-trisphosphate + ATP
1D-myo-inositol-1,3,4,6-tetrakisphosphate + ADP
-
-
-
-
r
ATP + 1D-myo-inositol 1,3,4-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,3,4-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,3,4-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,3,4-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,3,4-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,3,4-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 1,3,4-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,3,4-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 1,3,4-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,3,4-trisphosphate
ADP + 1D-myo-inositol 1,3,4,6-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,3,4-trisphosphate
ADP + 1D-myo-inositol 1,3,4,6-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,3,4-trisphosphate
ADP + 1D-myo-inositol 1,3,4,6-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,3,4-trisphosphate
ADP + 1D-myo-inositol 1,3,4,6-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,3,4-trisphosphate
ADP + 1D-myo-inositol 1,3,4,6-tetrakisphosphate
The substrate is converted to InsP4 but not to InsP5
-
-
?
ATP + 1D-myo-inositol 1,3,4-trisphosphate
ADP + 1D-myo-inositol 1,3,4,6-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,3,4-trisphosphate
ADP + 1D-myo-inositol 1,3,4,6-tetrakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 1,3,4-trisphosphate
ADP + 1D-myo-inositol 1,3,4,6-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,3,4-trisphosphate
ADP + 1D-myo-inositol 1,3,4,6-tetrakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 1,3,4-trisphosphate
ADP + 1D-myo-inositol 1,3,4,6-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol-1,3,4-trisphosphate
ADP + 1D-myo-inositol-1,3,4,5-tetrakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol-1,3,4-trisphosphate
ADP + 1D-myo-inositol-1,3,4,5-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol-1,3,4-trisphosphate
ADP + 1D-myo-inositol-1,3,4,5-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol-1,3,4-trisphosphate
ADP + 1D-myo-inositol-1,3,4,6-tetrakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol-1,3,4-trisphosphate
ADP + 1D-myo-inositol-1,3,4,6-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol-1,3,4-trisphosphate
ADP + 1D-myo-inositol-1,3,4,6-tetrakisphosphate
-
-
-
?
additional information
?
-
the enzyme is involved in photomorphogenesis under red light conditions
-
-
?
additional information
?
-
AtITPK4 differs from other family members in that it not display inositol 3,4,5,6-tetrakisphosphate 1-kinase activity. It displays inositol 1,4,5,6-tetrakisphosphate and inositol-1,3,4,5-tetrakisphosphate isomerase activity. With inositol tetrakisphosphate substrates, ITPK4 displays an isomerase activity (in the absence of inositol pentakisphosphate product) interpreting as phosphatase and kinase activity. AtITPK4 shows isomerase activity against other substrates. Removal of the 1- or 3-phosphate of inositol-1,3,4,6-tetrakisphosphate and subsequent rephosphorylation at the same position generates inositol-1,3,4,6-tetrakisphosphate.
-
-
?
additional information
?
-
AtITPK4 differs from other family members in that it not display inositol 3,4,5,6-tetrakisphosphate 1-kinase activity. It displays inositol 1,4,5,6-tetrakisphosphate and inositol-1,3,4,5-tetrakisphosphate isomerase activity. With inositol tetrakisphosphate substrates, ITPK4 displays an isomerase activity (in the absence of inositol pentakisphosphate product) interpreting as phosphatase and kinase activity. AtITPK4 shows isomerase activity against other substrates. Removal of the 1- or 3-phosphate of inositol-1,3,4,6-tetrakisphosphate and subsequent rephosphorylation at the same position generates inositol-1,3,4,6-tetrakisphosphate.
-
-
?
additional information
?
-
AtITPK4 differs from other family members in that it not display inositol 3,4,5,6-tetrakisphosphate 1-kinase activity. It displays inositol 1,4,5,6-tetrakisphosphate and inositol-1,3,4,5-tetrakisphosphate isomerase activity. With inositol tetrakisphosphate substrates, ITPK4 displays an isomerase activity (in the absence of inositol pentakisphosphate product) interpreting as phosphatase and kinase activity. AtITPK4 shows isomerase activity against other substrates. Removal of the 1- or 3-phosphate of inositol-1,3,4,6-tetrakisphosphate and subsequent rephosphorylation at the same position generates inositol-1,3,4,6-tetrakisphosphate.
-
-
?
additional information
?
-
AtITPK4 differs from other family members in that it not display inositol 3,4,5,6-tetrakisphosphate 1-kinase activity. It displays inositol 1,4,5,6-tetrakisphosphate and inositol-1,3,4,5-tetrakisphosphate isomerase activity. With inositol tetrakisphosphate substrates, ITPK4 displays an isomerase activity (in the absence of inositol pentakisphosphate product) interpreting as phosphatase and kinase activity. AtITPK4 shows isomerase activity against other substrates. Removal of the 1- or 3-phosphate of inositol-1,3,4,6-tetrakisphosphate and subsequent rephosphorylation at the same position generates inositol-1,3,4,6-tetrakisphosphate.
-
-
?
additional information
?
-
-
AtITPK4 differs from other family members in that it not display inositol 3,4,5,6-tetrakisphosphate 1-kinase activity. It displays inositol 1,4,5,6-tetrakisphosphate and inositol-1,3,4,5-tetrakisphosphate isomerase activity. With inositol tetrakisphosphate substrates, ITPK4 displays an isomerase activity (in the absence of inositol pentakisphosphate product) interpreting as phosphatase and kinase activity. AtITPK4 shows isomerase activity against other substrates. Removal of the 1- or 3-phosphate of inositol-1,3,4,6-tetrakisphosphate and subsequent rephosphorylation at the same position generates inositol-1,3,4,6-tetrakisphosphate.
-
-
?
additional information
?
-
enzyme displays both kinase and phosphatase activity.
-
-
?
additional information
?
-
enzyme displays both kinase and phosphatase activity.
-
-
?
additional information
?
-
enzyme displays both kinase and phosphatase activity.
-
-
?
additional information
?
-
enzyme displays both kinase and phosphatase activity.
-
-
?
additional information
?
-
-
enzyme displays both kinase and phosphatase activity.
-
-
?
additional information
?
-
-
the enzyme is involved in both the inositol phosphate and the stress response pathways which are linked by the enzyme, overview
-
-
?
additional information
?
-
-
regulation of enzymes involved in the inositol phosphate metabolism in human cells, overview
-
-
?
additional information
?
-
-
the enzyme inhibits tumor necrosis factor alpha-induced apoptosis involving the activation of PARP, BID, caspase-3 and caspase-8, but protects not against etoposide- or cycloheximide-induced apotosis, mechanism
-
-
?
additional information
?
-
-
integration of inositol phosphate signaling pathways via human ITPK1
-
-
?
additional information
?
-
-
enzyme has both phosphatase and kinase activity
-
-
?
additional information
?
-
-
The enzyme can phosphorylate both 1D-myo-inositol-1,3,4-trisphosphate at the 5 or 6 positions and 1D-myo-inositol-3,4,5,6-tetrakisphosphate at the 1 position and can also dephosphorylate 1D-myo-inositol-1,3,4,5,6-pentaakisphosphate to 1D-myo-inositol-3,4,5,6-tetrakisphosphate
-
-
?
additional information
?
-
-
The phenomenon of intersubstrate transfer is only found in the human enzyme, which can use 1D-myo-inositol 1,3,4-trisphosphate to regulate increased cellular concentrations of 1D-myo-inositol-3,4,5,6-tetrakisphosphate
-
-
?
additional information
?
-
-
the various enzyme activities manifested by ITPK1 provide a molecular mechanism that allows the receptor-activated changes in phospholipase C activity and consequent increases in the concentration of 1D-myo-inositol 1,3,4-trisphosphate to regulate the abundance of 1D-myo-inositol-3,4,5,6-tetrakisphosphate
-
-
?
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evolution
OsITPK6 belongs to subgroup III, with 12 exons and 11 introns, of the OsITPK gene family. ITPK6 is a unique gene in the ITPK gene family
evolution
phylogenetic tree showing the evolutionary relatedness of GmITPK2 with ITPKs of monocot and dicot species using Entamoeba histolytica (EhITPK) as an outgroup member
malfunction
-
required for proper development of the neural tube and axial mesoderm
malfunction
loss of this gene in itpk3-1 does neither affect phytate seed levels, nor seed Zn, Fe, and Mn but the micronutrient bioavailability is strongly reduced by seed phytate that forms complexes with seed cations. Low seed zinc is primarily caused by plant growth in Zn-deficient soil
malfunction
the epidermis structure of seed coat is irregularly formed in seeds of itpk2-1 mutant, resulting in the increased permeability of seed coat to tetrazolium salts. The cell wall shows a dramatic decrease in composition of suberin and cutin, which relate to the permeability of seed coat and the formation of which is accompanied with seed coat development. ITPK2 deficiency results in the distorted seed coat and crumpled columellas. Seed coat of itpk2-1 mutant presents high permeability to 2,3,5-triphenyltetrazolium and has less mucilage
malfunction
although both ipk1-1 and itpk1 mutants exhibit decreased levels of InsP6 (phytate) and diphosphoinositol pentakisphosphate (PP-InsP5, InsP7), disruption of another ITPK family enzyme, ITPK4, which correspondingly causes depletion of InsP6 and InsP7, does not display similar phosphate-related phenotypes, which precludes these InsP species from being effectors. Notably, the level of D/L-Ins(3,4,5,6)P4 is concurrently elevated in both ipk1-1 and itpk1 mutants, which demonstrates a specific correlation with the misregulated phosphate phenotypes. The level of D/L-Ins(3,4,5,6)P4 is not responsive to phosphate starvation that instead manifests a shoot-specific increase in the InsP7 level. ITPK1 overexpression significantly decreases phosphate uptake activity, in contrast to the elevated uptake activity shown by itpk1 mutants. In addition, several PSR genes are downregulated in ITPK1-overexpressing lines compared with the wild-type (e.g. PHT1:2, SPX1, AT4, IPS1 and PAP17)
malfunction
mutation of OsITPK6 not only significantly reduces the accumulation of IP6 in rice grains but also impairs plant growth and tolerance to abiotic stress. Nucleotide substitutions of gene OsITPK6 can significantly lower the phytic acid content in rice grains. Impact of ositpk6 mutations on plant growth and seed germination, panicle phenotype of mutant OsITPK6 and wild-type plants, overview. There is no significant difference in the number of leaves and roots with or without stress treatment between ositpk6_1 and wild-type
malfunction
-
loss of this gene in itpk3-1 does neither affect phytate seed levels, nor seed Zn, Fe, and Mn but the micronutrient bioavailability is strongly reduced by seed phytate that forms complexes with seed cations. Low seed zinc is primarily caused by plant growth in Zn-deficient soil
-
malfunction
-
required for proper development of the neural tube and axial mesoderm
-
metabolism
measurement of Fe, Zn, and Mn concentrations in seeds of Arabidopsis thaliana accessions grown in Zn-deficient and Zn-amended conditions, overview. Inositol 1,3,4-trisphosphate 5/6-kinase 3 gene (ITPK3), located close to a significant nucleotide polymorphism associated with relative Zn seed concentrations, is dispensable for seed micronutrients accumulation in ecotype Col-0
metabolism
following the formation of myo-inositol-3-phosphate, sequential phosphorylation reactions via action of various inositol phosphate kinases-myo-inositol kinase (Mik), inositol 1,3,4-trisphosphate kinase (Itpk), inositol 1,4,5-trisphosphate 3/6 kinase (Ipk2), and inositol 1,3,4,5,6-pentakisphosphate kinase (Ipk1) lead to phytic acid (PA, myo-inositol 1,2,3,4,5,6-hexakisphosphate) synthesis via the lipid-independent pathway and fine-tune the phosphorous flux towards PA accumulation
metabolism
-
pathways enriched analysis indicates that the ubiquitin-mediated proteolysis pathway (UPP) and phosphatidylinositol (PI) signaling system are crucial for a successful transcriptional response in Gloiopeltis furcata to simulated natural tidal changes with twoconsecutive dehydration-rehydration cycles, overview. Genes encoding ubiquitin-protein ligase E3 (E3-1), SUMO-activating enzyme sub-unit 2 (SAE2), calmodulin (CaM), and inositol-1,3,4-trisphosphate 5/6-kinase (ITPK) are the hub genes which respond positively to two successive dehydration treatments. Network-based interactions with hub genes indicate that transcription factor (e.g. TFIID), RNA modification (e.g. DEAH) and osmotic adjustment (e.g. MIP, ABC1, Bam1) are related to these two pathways. The PI signal connected with Ca2+/CaM pathway responds to dehydration, and the role of CaM and ITPK in signal transduction
metabolism
the kinase activity of inositol pentakisphosphate 2-kinase (IPK1) is required for phytate (inositol hexakisphosphate, InsP6) synthesis, and is indispensable for maintaining phosphate homeostasis under phosphate-replete conditions. Inositol 1,3,4-trisphosphate 5/6-kinase 1 (ITPK1) plays an equivalent role. Genetic dissection of the roles for InsP and PP-InsP biosynthesis enzymes in regulation of phosphate homeostasis, overview
metabolism
-
measurement of Fe, Zn, and Mn concentrations in seeds of Arabidopsis thaliana accessions grown in Zn-deficient and Zn-amended conditions, overview. Inositol 1,3,4-trisphosphate 5/6-kinase 3 gene (ITPK3), located close to a significant nucleotide polymorphism associated with relative Zn seed concentrations, is dispensable for seed micronutrients accumulation in ecotype Col-0
-
physiological function
T-DNA insertion in a gene encoding a putative inositol 1,3,4-trisphosphate 5/6-kinase, i.e. ITPK2, dsm3, leads to a drought- and salt-hypersensitive mutant. Under drought stress conditions, the mutant has significantly less accumulation of osmolytes such as proline and soluble sugar and shows significantly reduced root volume, spikelet fertility, biomass, and grain yield with concomittant increase in malondialdehyde level Overexpression of DSM3 in rice results in drought- and salt-hypersensitive phenotypes and physiological changes similar to those in the mutant. Inositol trisphosphate level is decreased in the overexpressors under normal condition and drought stress
physiological function
enzyme ITPK2 plays an essential role in seed coat development and lipid polyester barrier formation
physiological function
-
enzyme ITPK is the key regulatory enzyme at the branch point for the synthesis of InsP4 isomers [e.g. Ins(1,3,4,5)P4, Ins(1,3,4,6)P4 and Ins(3,4,5,6)P4], inositol pentakisphosphate (InsP5) and inositol hexaphosphate (InsP6). Ins (3,4,5,6)P4 can act as second messenger and play important roles in signal transduction
physiological function
inositol 1,3,4, trisphosphate 5/6 kinase (ITPK), a polyphosphate kinase that converts inositol 1,3,4-trisphosphate to inositol 1,3,4,5/6-tetraphosphate, averting the inositol phosphate pool towards phytic acid (PA) biosynthesis, is a key regulator that exists in four different isoforms in soybean. Role of inositol 1,3,4-trisphosphate 5/6 kinase-2 (GmITPK2) as a dehydration and salinity stress regulator in Glycine max. The significantly higher expression of GmITPK2 under drought and salinity stress suggests its role in providing tolerance mechanism against abiotic stress
physiological function
inositol 1,3,4-trisphosphate kinase-2 (GmItpk2), catalyzing the ATP-dependent phosphorylation of inositol 1,3,4-trisphosphate (IP3) to inositol 1,3,4,5-tetraphosphate or inositol 1,3,4,6-tetraphosphate, is a key enzyme diverting the flux of inositol phosphate pool towards phytate biosynthesis
physiological function
the enzyme is required for phytate (inositol hexakisphosphate, InsP6) synthesis and involved in maintaining phosphate homeostasis under phosphate-replete conditions
additional information
enzyme homology-based modeling and structure comparisons, overview. Active site mapping and molecular docking with ATP
additional information
-
enzyme homology-based modeling and structure comparisons, overview. Active site mapping and molecular docking with ATP
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Wilson, M.P.; Majerus, P.W.
Isolation of inositol 1,3,4-trisphosphate 5/6-kinase, cDNA cloning, and expression of the recombinant enzyme
J. Biol. Chem.
271
11904-11910
1996
Bos taurus, Homo sapiens (Q13572)
brenda
Verbsky, J.W.; Chang, S.C.; Wilson, M.P.; Mochizuki, Y.; Majerus, P.W.
The pathway for the production of inositol hexakisphosphate in human cells
J. Biol. Chem.
280
1911-1920
2005
Homo sapiens
brenda
Wilson, M.P.; Majerus, P.W.
Characterization of a cDNA encoding Arabidopsis thaliana inositol 1,3,4-trisphosphate 5/6-kinase
Biochem. Biophys. Res. Commun.
232
678-681
1997
Arabidopsis thaliana
brenda
Abdullah, M.; Hughes, P.J.; Craxton, A.; Gigg, R.; Desai, T.; Marecek, J.F.; Prestwich, G.D.; Shears, S.B.
Purification and characterization of inositol-1,3,4-trisphosphate 5/6-kinase from rat liver using an inositol hexakisphosphate affinity column
J. Biol. Chem.
267
22340-22345
1992
Rattus norvegicus
brenda
Wilson, M.P.; Sun, Y.; Cao, L.; Majerus, P.W.
Inositol 1,3,4-trisphosphate 5/6-kinase is a protein kinase that phosphorylates the transcription factors c-Jun and ATF-2
J. Biol. Chem.
276
40998-41004
2001
Bos taurus, Homo sapiens
brenda
Sun, Y.; Wilson, M.P.; Majerus, P.W.
Inositol 1,3,4-trisphosphate 5/6-kinase associates with the COP9 signalosome by binding to CSN1
J. Biol. Chem.
277
45759-45764
2002
Homo sapiens
brenda
Sun, Y.; Mochizuki, Y.; Majerus, P.W.
Inositol 1,3,4-trisphosphate 5/6-kinase inhibits tumor necrosis factor-induced apoptosis
J. Biol. Chem.
278
43645-43653
2003
Homo sapiens
brenda
Field, J.; Wilson, M.P.; Mai, Z.; Majerus, P.W.; Samuelson, J.
An Entamoeba histolytica inositol 1,3,4-trisphosphate 5/6-kinase has a novel 3-kinase activity
Mol. Biochem. Parasitol.
108
119-123
2000
Entamoeba histolytica (Q9XYQ1), Entamoeba histolytica HM-1 (Q9XYQ1)
brenda
Miller, G.J.; Wilson, M.P.; Majerus, P.W.; Hurley, J.H.
Specificity determinants in inositol polyphosphate synthesis: crystal structure of inositol 1,3,4-trisphosphate 5/6-kinase
Mol. Cell
18
201-212
2005
Entamoeba histolytica (Q9XYQ1)
brenda
Qin, Z.X.; Chen, Q.J.; Tong, Z.; Wang, X.C.
The Arabidopsis inositol 1,3,4-trisphosphate 5/6 kinase, AtItpk-1, is involved in plant photomorphogenesis under red light conditions, possibly via interaction with COP9 signalosome
Plant Physiol. Biochem.
43
947-954
2005
Arabidopsis thaliana (Q9SUG3)
brenda
Sweetman, D.; Stavridou, I.; Johnson, S.; Green, P.; Caddick, S.E.; Brearley, C.A.
Arabidopsis thaliana inositol 1,3,4-trisphosphate 5/6-kinase 4 (AtITPK4) is an outlier to a family of ATP-grasp fold proteins from Arabidopsis
FEBS Lett.
581
4165-4171
2007
Arabidopsis thaliana (O80568), Arabidopsis thaliana (O81893), Arabidopsis thaliana (Q9SBA5), Arabidopsis thaliana (Q9SUG3), Arabidopsis thaliana
brenda
Chamberlain, P.P.; Qian, X.; Stiles, A.R.; Cho, J.; Jones, D.H.; Lesley, S.A.; Grabau, E.A.; Shears, S.B.; Spraggon, G.
Integration of inositol phosphate signaling pathways via human ITPK1
J. Biol. Chem.
282
28117-28125
2007
Homo sapiens
brenda
Niu, X.; Chen, Q.; Wang, X.
OsITL1 gene encoding an inositol 1,3,4-trisphosphate 5/6-kinase is a negative regulator of osmotic stress signaling
Biotechnol. Lett.
30
1687-1692
2008
Oryza sativa (A1KXK8)
brenda
Saiardi, A.; Cockcroft, S.
Human ITPK1: a reversible inositol phosphate kinase/phosphatase that links receptor-dependent phospholipase C to Ca2+-activated chloride channels
Sci. Signal.
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1-3
2008
Homo sapiens
brenda
Wilson, M.P.; Hugge, C.; Bielinska, M.; Nicholas, P.; Majerus, P.W.; Wilson, D.B.
Neural tube defects in mice with reduced levels of inositol 1,3,4-trisphosphate 5/6-kinase
Proc. Natl. Acad. Sci. USA
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9831-9835
2009
Mus musculus
brenda
Du, H.; Liu, L.; You, L.; Yang, M.; He, Y.; Li, X.; Xiong, L.
Characterization of an inositol 1,3,4-trisphosphate 5/6-kinase gene that is essential for drought and salt stress responses in rice
Plant Mol. Biol.
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547-563
2011
Oryza sativa (Q10PL5)
brenda
Zhang, C.; Majerus, P.W.; Wilson, M.P.
Regulation of inositol 1,3,4-trisphosphate 5/6-kinase (ITPK1) by reversible lysine acetylation
Proc. Natl. Acad. Sci. USA
109
2290-2295
2012
Homo sapiens
brenda
Tang, Y.; Tan, S.; Xue, H.
Arabidopsis inositol 1,3,4-trisphosphate 5/6 kinase 2 is required for seed coat development
Acta Biochim. Biophys. Sin. (Shanghai)
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549-560
2013
Arabidopsis thaliana (O81893)
brenda
Chen, X.; Yuan, L.; Ludewig, U.
Natural genetic variation of seed micronutrients of Arabidopsis thaliana grown in zinc-deficient and zinc-amended soil
Front. Plant Sci.
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1070
2016
Arabidopsis thaliana (Q9SUG3), Arabidopsis thaliana Col-0 (Q9SUG3)
brenda
Marathe, A.; Krishnan, V.; Mahajan, M.M.; Thimmegowda, V.; Dahuja, A.; Jolly, M.; Praveen, S.; Sachdev, A.
Characterization and molecular modeling of inositol 1,3,4 tris phosphate 5/6 kinase-2 from Glycine max (L) Merr. comprehending its evolutionary conservancy at functional level
3 Biotech
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50
2018
Glycine max (A7X665), Glycine max
brenda
Liu, S.; Hu, Z.; Zhang, Q.; Yang, X.; Critchley, A.; Duan, D.
PI signal transduction and ubiquitination respond to dehydration stress in the red seaweed Gloiopeltis furcata under successive tidal cycles
BMC Plant Biol.
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516
2019
Gloiopeltis furcata
brenda
Kuo, H.; Hsu, Y.; Lin, W.; Chen, K.; Munnik, T.; Brearley, C.; Chiou, T.
Arabidopsis inositol phosphate kinases IPK1 and ITPK1 constitute a metabolic pathway in maintaining phosphate homeostasis
Plant J.
95
613-630
2018
Arabidopsis thaliana (Q9SBA5)
brenda
Marathe, A.; Krishnan, V.; Vinutha, T.; Dahuja, A.; Jolly, M.; Sachdev, A.
Exploring the role of inositol 1,3,4-trisphosphate 5/6 kinase-2 (GmITPK2) as a dehydration and salinity stress regulator in Glycine max (L.) Merr. through heterologous expression in E. coli
Plant Physiol. Biochem.
123
331-341
2018
Glycine max (A7X665), Glycine max
brenda
Jiang, M.; Liu, Y.; Liu, Y.; Tan, Y.; Huang, J.; Shu, Q.
Mutation of inositol 1,3,4-trisphosphate 5/6-kinase6 impairs plant growth and phytic acid synthesis in rice
Plants (Basel)
8
114
2019
Oryza sativa Japonica Group (Q0J0B2)
brenda