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Information on EC 2.7.1.159 - inositol-1,3,4-trisphosphate 5/6-kinase
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2.7.1.159 inositol-1,3,4-trisphosphate 5/6-kinaseIUBMB Comments
In humans, this enzyme, along with EC 2.7.1.127 (inositol-trisphosphate 3-kinase), EC 2.7.1.140 (inositol-tetrakisphosphate 5-kinase) and EC 2.7.1.158 (inositol pentakisphosphate 2-kinase) is involved in the production of inositol hexakisphosphate (InsP6). InsP6 is involved in many cellular processes, including mRNA export from the nucleus . Yeasts do not have this enzyme, so produce InsP6 from Ins(1,4,5)P3 by the actions of EC 2.7.1.151 (inositol-polyphosphate multikinase) and EC 2.7.1.158 (inositol-pentakisphosphate 2-kinase) . The enzymes from animals and plants also have the activity of EC 2.7.1.134, inositol-tetrakisphosphate 1-kinase.
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Word Map
- 2.7.1.159
-
phytic
- polyphosphate
-
hexakisphosphate
- dehydration
-
itpks
-
2-kinase
- phosphorus
- pentakisphosphate
-
signalosome
-
lipid-independent
-
tnfalpha-induced
- 1,3,4,5,6-pentakisphosphate
-
monophosphatase
-
photomorphogenesis
-
1,4,5-tris-phosphate
- 1,3,4,6-tetrakisphosphate
- phytate
- imp
- ikappabalpha
-
atp-grasp
- agriculture
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
5/6-kinase, gmitpk2, ositl1, atitpk4, 5/6 kinase, at2g43980, inositol 1,3,4-triphosphate 5/6-kinase, inositol 1,3,4 trisphosphate kinase-2, inositol-1,3,4-trisphosphate 5/6-kinase, inositol-1,3,4-trisphosphate kinase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
inositol 1,3,4-triphosphate 5/6-kinase
inositol 1,3,4-trisphosphate 5/6-kinase
Ins(1,3,4)P3 5/6-kinase
ITPK
ITPK1
ITPK2
ITPK3
additional information
additional information
the enzyme belongs to the ATP-grasp family
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + 1D-myo-inositol 1,3,4-trisphosphate = ADP + 1D-myo-inositol 1,3,4,5-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-1,3,4,5-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-1,3,4,5-tetrakisphosphate
determination of substrate binding sites, catalytic reaction mechanism
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-1,3,4,6-tetrakisphosphate
determination of substrate binding sites, catalytic reaction mechanism
ATP + 1D-myo-inositol-1,3,4-trisphosphate = ADP + 1D-myo-inositol-1,3,4,6-tetrakisphosphate
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Phosphorylation
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SYSTEMATIC NAME
IUBMB Comments
ATP:1D-myo-inositol 1,3,4-trisphosphate 5-phosphotransferase
In humans, this enzyme, along with EC 2.7.1.127 (inositol-trisphosphate 3-kinase), EC 2.7.1.140 (inositol-tetrakisphosphate 5-kinase) and EC 2.7.1.158 (inositol pentakisphosphate 2-kinase) is involved in the production of inositol hexakisphosphate (InsP6). InsP6 is involved in many cellular processes, including mRNA export from the nucleus [2]. Yeasts do not have this enzyme, so produce InsP6 from Ins(1,4,5)P3 by the actions of EC 2.7.1.151 (inositol-polyphosphate multikinase) and EC 2.7.1.158 (inositol-pentakisphosphate 2-kinase) [2]. The enzymes from animals and plants also have the activity of EC 2.7.1.134, inositol-tetrakisphosphate 1-kinase.
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CAS REGISTRY NUMBER
COMMENTARY
288307-53-9
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
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-
?
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
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enzyme catalyzes both forward and reverse reaction
putative regulator of Ca2+-activated chloride channels.
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r
1D-myo-inositol-1,3,4,5-tetrakisphosphate + ATP
1D-myo-inositol-1,3,4,5,6-pentakisphosphate + ADP
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-
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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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-
-
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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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-
-
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r
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
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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 1,4,6-trisphosphate + 1D-myo-inositol 3,4,6-trisphosphate
ADP + inositol tetrakisphosphate
racemic mix of phosphates
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-
?
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
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-
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?
ATP + 1D-myo-inositol-1,3,4-trisphosphate
?
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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
ATP + 1D-myo-inositol-1,3,4-trisphosphate
ADP + 1D-myo-inositol-1,3,4,6-tetrakisphosphate
ATP + IkappaBalpha
ADP + phosphorylated IkappaBalpha
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substrate of the free enzyme and the COP9 signalosome complex
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-
?
ATP + p53
ADP + phosphorylated p53
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substrate of the free enzyme and the COP9 signalosome complex
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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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-
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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
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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
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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
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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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-
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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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-
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r
ATP + 1D-myo-inositol-1,3,4-trisphosphate
ADP + 1D-myo-inositol-1,3,4,5-tetrakisphosphate
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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
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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
-
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
-
-
-
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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
-
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
-
-
?
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
-
-
?
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
-
?
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
-
?
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
-
substrate of the free enzyme and the COP9 signalosome complex
-
-
?
ATP + 1D-myo-inositol-1,3,4-trisphosphate
ADP + 1D-myo-inositol-1,3,4,6-tetrakisphosphate
-
5fold higher activity compared to 1D-myo-inositol-1,3,4,5-tetrakisphosphate formation
-
-
?
ATP + ATF-2
ADP + phosphorylated ATF-2
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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
-
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
?
-
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
?
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
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.
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-
?
additional information
?
-
enzyme displays both kinase and phosphatase activity.
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-
?
additional information
?
-
enzyme displays both kinase and phosphatase activity.
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-
?
additional information
?
-
enzyme displays both kinase and phosphatase activity.
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-
?
additional information
?
-
enzyme displays both kinase and phosphatase activity.
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-
?
additional information
?
-
-
enzyme displays both kinase and phosphatase activity.
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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
-
-
?
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
?
-
-
the enzyme is part of the COP9 signalosome complex consisting of 8 proteins
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
the enzyme shows multiple activities
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
-
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
?
-
-
the enzyme associates with the COP9 signalosome, an complex of 8 proteins, by binding to CSN1
-
-
?
additional information
?
-
-
the enzyme is part of the COP9 signalosome complex consisting of 8 proteins
-
-
?
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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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
-
-
-
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-1,4,6-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 1,3,4,6-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
-
-
-
?
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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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mn2+
-
activates the protein phopshorylation, but inhibits the inositol-1,3,4-trisphosphate 5/6-kinase reaction
NaCl
A1KXK8
Induced gene expression in rice by 200 mM. Level of relative germination in the two T3 transgenic tobacco lines overexpressing the OsITL1 gene is approximately 20-30% lower than that in the wild-type lines in the presence of 100 mM NaCl. In presence of 150 or 200 mM NaCl, seedling development is more significantly inhibited in transgenic tobacco plants than in wild-type plants. Transgenic plants that overexpress OsITL1 are more sensitive to NaCl stress during seed germination and early seedling development. The leaves of the transgenic seedlings show complete bleaching or extensive chlorosis after 7 days of exposure to 200 Mm NaCl
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1D-myo-inositol-3,4,5,6-tetrakisphosphate
-
inhibits the 5/6-kinase activities, but not the phosphorylation of ATF-2
curcumin
-
inhibits both the free enzyme and the COP9 signalosome complex-associated kinase
Mn2+
-
activates the protein phopshorylation, but inhibits the inositol-1,3,4-trisphosphate 5/6-kinase reaction
protein kinase A
-
slight inhibition of enzyme activity with ATF-2 as substrate
-
additional information
-
enzyme activity is unaffected by protein kinase C, protein kinase A, and Ca2+/calmodulin
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
CSN1
-
the enzyme associates with the COP9 signalosome, an complex of 8 proteins, by binding to CSN1, activates
-
additional information
enzyme expression is slightly induced by heat shock
-
additional information
-
enzyme activity is unaffected by protein kinase C, protein kinase A, and Ca2+/calmodulin
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Dehydration
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.
Dehydration
OsITL1 gene encoding an inositol 1,3,4-trisphosphate 5/6-kinase is a negative regulator of osmotic stress signaling.
Dehydration
PI signal transduction and ubiquitination respond to dehydration stress in the red seaweed Gloiopeltis furcata under successive tidal cycles.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.042
1D-myo-inositol 1,3,4,6-tetrakisphosphate
-
additional information
additional information
-
kinetics, recombinant enzyme with CSN1
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5
1D-myo-inositol-1,3,4-trisphosphate
-
pH 7.6, 37°C, in absence of CSN1, first order rate constant
20
1D-myo-inositol-1,3,4-trisphosphate
-
pH 7.6, 37°C, in presence of CSN1, first order rate constant
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.003 - 0.004
1D-myo-inositol-1,3,4,5-tetrakisphosphate
-
pH 7.2, 37°C, versus 1D-myo-inositol-1,3,4-trisphosphate
0.002 - 0.003
1D-myo-inositol-1,3,4,6-tetrakisphosphate
-
pH 7.2, 37°C, versus 1D-myo-inositol-1,3,4-trisphosphate
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
372
500
-
purified recombinant enzyme from Sf21 cells, with substrate 1D-myo-inositol-1,3,4-trisphosphate
additional information
additional information
not detected in mature flowers, but expression of trancript is confirmed by mRNA in situ analysis
additional information
not detected in mature flowers, but expression of trancript is confirmed by mRNA in situ analysis
additional information
not detected in mature flowers, but expression of trancript is confirmed by mRNA in situ analysis
additional information
not detected in mature flowers, but expression of trancript is confirmed by mRNA in situ analysis
additional information
-
not detected in mature flowers, but expression of trancript is confirmed by mRNA in situ analysis
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.2
7.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
cv. Pusa-16, grown in the fields of Division of Genetics, I.A.R.I, New Delhi
UniProt
brenda
AtITPK4 protein is distinguished from the other proteins by an extended N-terminal sequence (39 residues longer than that of AtITPK2). A blast search with amino acids 1-80 of AtITPK4 as query fails to identify significant homology to any proteins of other known functional annotation. In alignment, AtITPK4 has an extra 121 amino acids N-terminal to the start of the Entamoeba enzyme. AtITPK4 shows 14.9% identity and 25.7% similarity to the Entamoeba enzyme in a pairwise alignment.
SwissProt
brenda
enzyme belongs to a larger family of ATP-grasp fold proteins
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
young, AtITPK4 transcript is expressed throughout early flower development which culminates in the opening of the flower bud
brenda
additional information
expressed in male and female organs of young and mature flowers
brenda
spatio-temporal transcript profiling signified GmItpk2 to be seed-specific, with higher transcript levels in the early stage of seed development, GmItpk2 expression profiling overview
brenda
weak expression, revealed expression in the seed and pod wall
brenda
additional information
ubiquitous enzyme expression in tissues
brenda
additional information
expression pattern of isozyme ITPK2, no or very poor expression in stem
brenda
additional information
-
expression pattern of gene ITPK as a drought-related hub gene
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
cytosolic localization of GmITPK2 protein is predicted by CELLO tool with a reliability index of 2.976
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
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
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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
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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
Show AA Sequence and Transmembrane Helices (1415 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
48000
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x * 36000-38000, proteolytically C-terminally truncated enzyme, SDS-PAGE, x * 48000, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
?
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x * 36000-38000, proteolytically C-terminally truncated enzyme, SDS-PAGE, x * 48000, SDS-PAGE
additional information
the predicted three-dimensional model confirms 12 alpha-helices and 14 beta-barrel sheets with ATP-binding site close to beta-sheet present towards the C-terminus of the protein molecule. Secondary structure prediction of GmITPK2 using PDBSum tool
additional information
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the predicted three-dimensional model confirms 12 alpha-helices and 14 beta-barrel sheets with ATP-binding site close to beta-sheet present towards the C-terminus of the protein molecule. Secondary structure prediction of GmITPK2 using PDBSum tool
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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isoform ITPK1 can be acetylated by the acetyltransferases CREB-binding protein, CBP, and p300 both in vivo and in vitro and can be deacetylated by mammalian silent information regulator 2, SIRT1. Acetylation of ITPK1 decreases its enzyme activity and protein stability, and inhibits the synthesis of higher phosphorylated forms of inositol polyphosphates in the inositol signaling pathway. The acetylation sites are lysine residues 340, 383, and 410, which are all located on the surface of the protein
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme free or in complex with ATP analogue AMP-PCP and substrate inositol-1,3,4-trisphosphate in presence of Mg2+, 30 mg/ml protein in 25 mM Tris-HCl, pH 8.0, 150 mM NaCl, and 10 mM DTT, mixed with a solution containing 20% PEG 3000, 0.1 M Tris-HCl, pH 7.5, and 0.1 M Ca(OAc)2, several months, crystals are seeded into sitting drops of 15 mg/ml protein, 25% PEG 3350, 5% PEG 400, 0.1 M Bis-Tris, pH 5.5, 10 mM DTT, and 10 mM L-cysteine, with or without ligands added as 10 mM AMP-PCP, 10 mM MgCl2, and 5 mM inositol-1,3,4-trisphosphate, direct X-ray diffraction analysis after this step or further seeding adding ADP and other ligands, overview, X-ray diffraction structure determination and analysis at 1.2-2.0 A resolution
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
P522L
ositpk6 mutant, the line with the P522L amino acid substitution has agronomic performance (seed weight, germination, and seedling growth) similar to that of its wild-type parent
additional information
additional information
construction of an enzyme-deficient mutant line, phenotype with reduced hypocotyl
additional information
construction of the homogenous At4g08170 mutant (SALK_120653C, NASCcode N653925) carrying a T-DNA insertion in the intron in wild-type line Col-0
additional information
functional analysis of itpk2-1 mutant (SAIL_25_H09), phenotype, overview
additional information
generation of itpk1-1 mutants, phenotype, overview. Genetic interaction analysis of bifunctional ITPK1 (EC 2.7.1.159/EC 2.7.1.134) and IPK1 (EC 2.7.1.158) with a genetic cross between ipk1-1 and itpk1 mutants. The ipk1-1 itpk1 double mutants exhibit more severe growth defects than single mutants and those that proceeded to the reproductive stage bore aborted seeds. Common elevation of D/L-Ins(3,4,5,6)P4 in itpk1 and ipk1-1 mutants
additional information
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construction of the homogenous At4g08170 mutant (SALK_120653C, NASCcode N653925) carrying a T-DNA insertion in the intron in wild-type line Col-0
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additional information
construction of diverse mutants and analysis of the function of the residues in catalysis and substrate binding, overview
additional information
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enzyme overexpression in HEK-293 cells inhibits TNFalpha-induced activation of caspases-8, -3, and -9, siRNA gene silencing of the enzyme in HeLa cells results in higher susceptibility of the cells to TNFalpha-induced apoptosis
additional information
-
enzyme silencing in HeLa cells decreases the levels of inositol pentakisphosphate and inositol hexakisphosphate, while overexpression in HEK-293 cells increases the levels of InsP4, InsP5, and InsP6, overview
additional information
OsITPK6 mutants are generated by CRISPR/Cas9-mediated mutagenesis, generation of 23 hygromycin phosphotransferase (HPT)-positive T0 plants transformed with the CRISPR/Cas9 vector pH-itpk6. Genotyping of gene ITPK6, the ositpk6_1 (a 6-nt in-frame deletion) mutation results in the loss of two amino acids at positions 91 to 92. In contrast, all the other three mutations, i.e. ositpk6_2 (a 1-nt insertion), ositpk6_3 (a 5-nt deletion), and ositpk6_4 (a 2-nt deletion), generate a premature stop codon almost right after the mutation site and, hence, significantly shorten the encoded proteins. Consequently, the ositpk6_2, _3 and _4 mutant alleles are predicted to produce proteins of only 105, 103, and 104 amino acids, respectively. The two amino acids missing in the ositpk6_1 mutant are located in a highly conserved segment, suggesting the mutation of ositpk6_1 might have a potential functional consequence. Plant growth of mutants ositpk6_2, _3, and _4 is significantly impaired. Their panicles are significantly shorter (30.1%, 28.8%, and 29.1%, respectively) compared to wild-type parental cultivar Xidao 1, phenotypes, overview. Numbers and lengths of root from mutant plants are reduced under salt stress compared to wild-type
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
12900fold from brain by ion exchange chromatography, and heparin/inositol hexakisphosphate affinity chromatography
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26171fold from liver by polyethylene glycol precipitation, ion exchange chromatography and heparin and inositol hexakisphosphate affinity chromatograpies
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Cells are pelleted and resuspended in buffer, sonicated, centrifuged and the supernatant of the lysate is retained. Ni2+-nitrilotriacetate resin prewashed in NiSO4 is added to the lysate and incubated. The resin is washed twice with 10 ml of 50 mM NaH2PO4, 300 mM NaCl and 20 mM imidazole (pH 8) to elute non-specifically bound proteins, and washed with of NaH2PO4, 300 mM NaCl and 250 mM imidazole to elute AtIPK1 protein. Bacterial lysates and protein fractions from the purification are analysed by SDS-PAGE. Protein concentration is determined by the Bradford assay.
Cells are pelleted and resuspended in buffer, sonicated, centrifuged and the supernatant of the lysate is retained. Ni2+-nitrilotriacetate resin prewashed in NiSO4 is added to the lysate and incubated. The resin is washed twice with 10 ml of 50 mM NaH2PO4, 300 mM NaCl and 20 mM imidazole (pH 8) to elute non-specifically bound proteins, and washed with of NaH2PO4, 300 mM NaCl and 250 mM imidazole to elute AtIPK1 protein. Bacterial lysates and protein fractions from the purification are analysed by SDS-PAGE. Protein concentration is determined by the Bradford method.
Cells are pelleted and resuspended in buffer, sonicated, centrifuged and the supernatant of the lysate is retained. Ni2+-nitrilotriacetate resin prewashed in NiSO4 is added to the lysate and incubated. The resin is washed twice with 10 ml of 50 mM NaH2PO4, 300 mM NaCl and 20 mM imidazole (pH 8) to elute non-specifically bound proteins, and washed with of NaH2PO4, 300 mM NaCl and 250 mM imidazole to elute AtIPK1 protein. Bacterial lysates and protein fractions from the purification are analysed by SDS/PAGE. Protein concentration is determined by Bradford assay.
Cells are pelleted and resuspended in buffer, sonicated, centrifuged and the supernatant of the lysate is retained. Ni2+-nitrilotriacetate resin prewashed in NiSO4 is added to the lysate and incubated. The resin is washed twice with 10 ml of 50 mM NaH2PO4, 300 mM NaCl and 20 mM imidazole (pH 8) to elute non-specifically bound proteins, and washed with of NaH2PO4, 300 mM NaCl and 250 mM imidazole to elute AtIPK1 protein. Bacterial lysates and protein fractions from the purification are analysed by SDS/PAGE. Protein concentration is determined by the Bradford method.
recombinant enzyme from insect Sf21 cells, recombinant enzyme partially from 293 cells by ion exchange chromatography
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recombinant GST-tagged enzyme from Escherichia coli by glutathione affinity chromatography and gel filtration
recombinant GST-tagged enzyme, the GST-tag is cleaved off by treatment with GST-3Cpro
recombinant His-tagged enzyme from Escherichia coli by adsorption and calmodulin affinity chromatography
recombinant His5-tagged GmITPK2 from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
Cloning and transformation of tobacco plants (Nicotiana tabacum L. cv. K326)
A1KXK8
DNA and amino acid sequence determination and analysis, expression as GST-tagged enzyme in bacteria
DNA and amino acid sequence determination and analysis, expression as tagged enzyme in Escherichia coli
-
DNA and N-terminal amino acid sequence determination and analysis, expression as His-tagged enzyme in Escherichia coli
expression in 293 cells, expression in Spodoptera frugiperda Sf21 cells using the baculovirus infection system
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expression of GST-tagged wild-type enzyme and of mutant enzymes in Escherichia coli
expression of the enzyme tagged with 6 repeats of Myc at the N-terminus in Spodoptera frugiperda Sf21 cells using the baculovirus infection system, expression of His6-tagged and of FLAG-tagged enzyme in Escherichia coli strain BL21(DE3), co-overexpression of the enzyme with CSN1 in HeLa cells
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gene ITPK2, expression analysis of wild-type and mutant enzymes by quantitative real-time PCR analysis
gene Itpk2, genetic organization and gene structure, isozyme sequence comparisons, in-silico analysis of the promoter region of ITPKs, the promoter region of GmITPK2 shows the presence of two MYB binding elements for drought inducibility and one for abscisic acid response, quantitative RT-PCR enzyme expression analysis. The His5-tagged GmITPK2-expressing recombinant Escherichia coli strain BL21(DE3) cells show tolerance to drought and salinity and thus demonstrate the functional redundancy of the gene across taxa
gene itpk3-1, genotyping, 108 different accessions, the Arabidopsis accessions differ in their response to Zn deficiency, quantitative real-time PCR enzyme expression anaysis, overview
in Escherichia coli Rosetta, transformed with pET28a and pET28c containing 3 kinase cDNAs. Vector-encoded hexa-histidine (His) tags are added to all proteins.
single copy Itpk2 gene, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, recombinant expression of His-tagged GmITPK2 in Escherichia coli strain BL21(DE3)
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
developmental expression
expression profiling of the GmITPK transcripts under different experimental conditions of drought and salinity stress. Plants treated with 200 mM NaCl, the transcript expression of GmITPK2 is maximal 1 h after treatment i.e. 7.09fold and gradually reduced to 2.82fold 8 h after treatment. A steady upregulation is observed in plants treated with 0.1 mM abscisic acid as the transcript accumulation increased gradually with time ranging from 1.0 to 14fold. In PEG-induced drought stress the transcript accumulation is maximal (6.6fold) 1 h after treatment and steadily decreases to 3.4 8 h after treatment. The transcript profiles show a higher fold change in the expression GmITPK2 alone, compared to remaining members of GmITPK gene family
GmITPK2 is an early dehydration responsive gene which is also induced by dehydration and exogenous treatment with abscisic acid
successive dehydration treatment induces the enzyme expression in red sea weed
-
there is no significant difference in the number of leaves and roots with or without stress treatment between ositpk6_1 and wild-type
transcript level is induced about tenfold by drought and salt treatments and about 29fold induced by by abscisic acid, but only slightly induced by heat shock
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
OsITPK6 can be a desirable target of mutagenesis for breeding yield-competitive lpa rice
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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.
1
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
106
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.
77
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)
45
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.
7
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
8
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.
19
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
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