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1D-myo-inositol 1,3,4,5,6-pentakisphosphate + ATP
1D-myo-inositol hexakisphosphate + ADP
intermediate in both lipid-dependent and lipid-independent phytic acid biosynthetic pathways
phytic acid, in higher plants, phytic acid can mediate abscisic acid-induced guard cell closure by inactivating plasma membrane inward K+ conductance. During this process, phytic acid appears to act as an endomembrane calcium-releasing signal.
-
ir
1D-myo-inositol 1,4,6-trisphosphate + ATP
1D-myo-inositol 1,2,4,6-tetrakisphosphate + ADP
relative substrate specificity 93.9%
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
ATP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,6-tetrakisphosphate
?
-
-
-
?
ATP + 1D-myo-inositol 1,4,5,6-tetrakisphosphate
?
-
-
-
?
ATP + 1D-myo-inositol 1,4,5,6-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,4,5,6-tetrakisphosphate + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 1,4,6-trisphosphate
ADP + 1D-myo-inositol 1,4,5,6-tetrakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 3,4,5,6-tetrakisphosphate
?
ATP + 1D-myo-inositol 3,4,5,6-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
-
-
-
?
ATP + myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + myo-inositol hexakisphosphate
-
-
-
?
ATP + myo-inositol 1,4,6-trisphosphate
ADP + inositol 1,2,4,6-tetrakisphosphate
-
-
-
?
additional information
?
-
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
the enzyme may be involved in both inositol hexakisphosphate formation in maturing seeds and ATP resynthesis in germinating seeds
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
it is suggested that the enzyme is necessary for yolk sac development or function. Loss of inositol 1,3,4,5,6-pentakisphosphate 2-kinase is lethal
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
rate-determining step in production of 1D-myo-inositol hexakisphosphate
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
cytoplasmic production of 1D-myo-inositol hexakisphosphate is sufficient for mediating the Gle1-mRNA export pathway
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
the product 1D-myo-inositol hexakisphosphate plays a role in messenger RNA export
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
the predominant activity of StITPK1 is that of an InsP5-ADP phosphotransferase.
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?
ATP + 1D-myo-inositol 1,4,5,6-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 1,4,5,6-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 1,4,5,6-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 3,4,5,6-tetrakisphosphate
?
-
-
-
?
ATP + 1D-myo-inositol 3,4,5,6-tetrakisphosphate
?
-
low activity
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-
?
additional information
?
-
no activity with 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
?
additional information
?
-
phosphotransfer from 2-FAM-InsP5 (2-O-(2-(5-fluoresceinylcarboxy)aminoethyl)-myo-inositol 1,3,4,5,6-pentakisphosphate) to ADP by AtIP5 2-K
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-
-
additional information
?
-
with inositol tris/tetrakisphosphate kinase 1 (ITPK1, EC 2.7.1.134) and inositol pentakisphosphate 2-kinase (IPK1, EC 2.7.1.158) combined at a 1:20 ATP:ADP ratio, InsP6 is converted via Ins(1,3,4,5,6)P5 to Ins(3,4,5,6) P4 and/or Ins(1,4,5,6)P4 with concomitant generation of ATP
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-
-
additional information
?
-
substrate binding structure, overview
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-
-
additional information
?
-
substrate binding structure, overview
-
-
-
additional information
?
-
substrate binding structure, overview
-
-
-
additional information
?
-
substrate binding structure, overview
-
-
-
additional information
?
-
binding sites of ADP and IP6 are observed to be present side by side with few common interacting amino acid residues: R193, K171. The residues that are making interactions with ADP include W130, K171, R193, H197, K201, Q204, and N239, whereas the residues that are making interactions with IP6 include G17, E18, G19, A20, N22, L23, V24, R40, K43, R131, R169, K171, R193, R242, and S373
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-
-
additional information
?
-
binding sites of ADP and IP6 are observed to be present side by side with few common interacting amino acid residues: R193, K171. The residues that are making interactions with ADP include W130, K171, R193, H197, K201, Q204, and N239, whereas the residues that are making interactions with IP6 include G17, E18, G19, A20, N22, L23, V24, R40, K43, R131, R169, K171, R193, R242, and S373
-
-
-
additional information
?
-
-
binding sites of ADP and IP6 are observed to be present side by side with few common interacting amino acid residues: R193, K171. The residues that are making interactions with ADP include W130, K171, R193, H197, K201, Q204, and N239, whereas the residues that are making interactions with IP6 include G17, E18, G19, A20, N22, L23, V24, R40, K43, R131, R169, K171, R193, R242, and S373
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-
-
additional information
?
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-
the enzyme changes its kinase activity towards 1D-myo-inositol hexakisphosphate at a decreasing ATP/ADP ratio to an ADP phosphotransferase activity and dephosphorylate 1D-myo-inositol hexakisphosphate
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-
?
additional information
?
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-
loss of the 2-kinase is lethal
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-
?
additional information
?
-
mIP5 2-K active site and substrate recognition, overview. The adenine is strongly recognized through polar and hydrophobic interactions with both protein lobes and the hinge connecting them. In particular, it forms polar interactions with His14 and the backbones of Pro116 and Leu118. The ribose OHs interact with the C-lobe residues Glu136 and Arg209. The triphosphate moiety is tightly bound to the N-lobe of the enzyme through polar interactions and to the C-lobe through two magnesium ions. In particular, phosphate interaction with residue Arg-33, with a flexible loop (G-loop, residues Gly15-Ser20) and with an acidic residue (Asp437) through the magnesium ions, is conserved throughout the PK superfamily and is essential for nucleotide binding and kinase activity
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-
-
additional information
?
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-
mIP5 2-K active site and substrate recognition, overview. The adenine is strongly recognized through polar and hydrophobic interactions with both protein lobes and the hinge connecting them. In particular, it forms polar interactions with His14 and the backbones of Pro116 and Leu118. The ribose OHs interact with the C-lobe residues Glu136 and Arg209. The triphosphate moiety is tightly bound to the N-lobe of the enzyme through polar interactions and to the C-lobe through two magnesium ions. In particular, phosphate interaction with residue Arg-33, with a flexible loop (G-loop, residues Gly15-Ser20) and with an acidic residue (Asp437) through the magnesium ions, is conserved throughout the PK superfamily and is essential for nucleotide binding and kinase activity
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-
-
additional information
?
-
-
the enzyme changes its kinase activity towards 1D-myo-inositol hexakisphosphate at a decreasing ATP/ADP ratio to an ADP phosphotransferase activity and dephosphorylate 1D-myo-inositol hexakisphosphate
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-
?
additional information
?
-
StITPK1 displays inositol 3,4,5,6-tetrakisphosphate 1-kinase activity. The enzyme displays inositol 1,3,4,5,6-pentakisphosphate 1-phosphatase activity in the absence of a nucleotide acceptor and inositol 1,3,4,5,6-pentakisphosphate-ADP phosphotransferase activity in presence of physiological concentrations of ADP. Additionally, StITPK1 shows inositol phosphate-inositol phosphate phosphotransferase activity.
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-
?
additional information
?
-
-
StITPK1 displays inositol 3,4,5,6-tetrakisphosphate 1-kinase activity. The enzyme displays inositol 1,3,4,5,6-pentakisphosphate 1-phosphatase activity in the absence of a nucleotide acceptor and inositol 1,3,4,5,6-pentakisphosphate-ADP phosphotransferase activity in presence of physiological concentrations of ADP. Additionally, StITPK1 shows inositol phosphate-inositol phosphate phosphotransferase activity.
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-
?
additional information
?
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-
capable to catalyze the phosphorylation of myo-inositol 1,4,5,6-tetrakisphosphate (relative substrate specificity 76.8%), and myo-inositol 3,4,5,6-tetrakisphosphate (relative substrate specificity 32.6%)
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-
?
additional information
?
-
capable to catalyze the phosphorylation of myo-inositol 1,4,5,6-tetrakisphosphate (relative substrate specificity 76.8%), and myo-inositol 3,4,5,6-tetrakisphosphate (relative substrate specificity 32.6%)
-
-
?
additional information
?
-
capable to catalyze the phosphorylation of myo-inositol 1,4,5,6-tetrakisphosphate (relative substrate specificity 76.8%), and myo-inositol 3,4,5,6-tetrakisphosphate (relative substrate specificity 32.6%)
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1D-myo-inositol 1,3,4,5,6-pentakisphosphate + ATP
1D-myo-inositol hexakisphosphate + ADP
intermediate in both lipid-dependent and lipid-independent phytic acid biosynthetic pathways
phytic acid, in higher plants, phytic acid can mediate abscisic acid-induced guard cell closure by inactivating plasma membrane inward K+ conductance. During this process, phytic acid appears to act as an endomembrane calcium-releasing signal.
-
ir
1D-myo-inositol 1,4,6-trisphosphate + ATP
1D-myo-inositol 1,2,4,6-tetrakisphosphate + ADP
relative substrate specificity 93.9%
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
additional information
?
-
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
the enzyme may be involved in both inositol hexakisphosphate formation in maturing seeds and ATP resynthesis in germinating seeds
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
it is suggested that the enzyme is necessary for yolk sac development or function. Loss of inositol 1,3,4,5,6-pentakisphosphate 2-kinase is lethal
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
rate-determining step in production of 1D-myo-inositol hexakisphosphate
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
cytoplasmic production of 1D-myo-inositol hexakisphosphate is sufficient for mediating the Gle1-mRNA export pathway
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
the product 1D-myo-inositol hexakisphosphate plays a role in messenger RNA export
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
the predominant activity of StITPK1 is that of an InsP5-ADP phosphotransferase.
-
-
?
additional information
?
-
-
loss of the 2-kinase is lethal
-
-
?
additional information
?
-
StITPK1 displays inositol 3,4,5,6-tetrakisphosphate 1-kinase activity. The enzyme displays inositol 1,3,4,5,6-pentakisphosphate 1-phosphatase activity in the absence of a nucleotide acceptor and inositol 1,3,4,5,6-pentakisphosphate-ADP phosphotransferase activity in presence of physiological concentrations of ADP. Additionally, StITPK1 shows inositol phosphate-inositol phosphate phosphotransferase activity.
-
-
?
additional information
?
-
-
StITPK1 displays inositol 3,4,5,6-tetrakisphosphate 1-kinase activity. The enzyme displays inositol 1,3,4,5,6-pentakisphosphate 1-phosphatase activity in the absence of a nucleotide acceptor and inositol 1,3,4,5,6-pentakisphosphate-ADP phosphotransferase activity in presence of physiological concentrations of ADP. Additionally, StITPK1 shows inositol phosphate-inositol phosphate phosphotransferase activity.
-
-
?
additional information
?
-
-
capable to catalyze the phosphorylation of myo-inositol 1,4,5,6-tetrakisphosphate (relative substrate specificity 76.8%), and myo-inositol 3,4,5,6-tetrakisphosphate (relative substrate specificity 32.6%)
-
-
?
additional information
?
-
capable to catalyze the phosphorylation of myo-inositol 1,4,5,6-tetrakisphosphate (relative substrate specificity 76.8%), and myo-inositol 3,4,5,6-tetrakisphosphate (relative substrate specificity 32.6%)
-
-
?
additional information
?
-
capable to catalyze the phosphorylation of myo-inositol 1,4,5,6-tetrakisphosphate (relative substrate specificity 76.8%), and myo-inositol 3,4,5,6-tetrakisphosphate (relative substrate specificity 32.6%)
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0004 - 0.176
1D-myo-inositol 1,3,4,5,6-pentakisphosphate
0.06681
1D-myo-inositol 1,3,4,6-tetrakisphosphate
wild type enzyme, at pH 7.5 and 25°C
0.05599
1D-myo-inositol 1,4,5,6-tetrakisphosphate
wild type enzyme, at pH 7.5 and 25°C
0.00055
1D-myo-inositol 1,4,5-triphosphate
-
about, cosubstrate: ATP
0.04754 - 0.07917
1D-myo-inositol 3,4,5,6-tetrakisphosphate
0.119
myo-inositol 1,3,4,5,6-pentakisphosphate
-
0.0004
1D-myo-inositol 1,3,4,5,6-pentakisphosphate
-
-
0.000644
1D-myo-inositol 1,3,4,5,6-pentakisphosphate
-
-
0.0023
1D-myo-inositol 1,3,4,5,6-pentakisphosphate
-
-
0.022
1D-myo-inositol 1,3,4,5,6-pentakisphosphate
-
30°C, pH 7.5
0.022
1D-myo-inositol 1,3,4,5,6-pentakisphosphate
-
at 0.4 mM ATP
0.03372
1D-myo-inositol 1,3,4,5,6-pentakisphosphate
mutant enzyme N238A, at pH 7.5 and 25°C
0.03979
1D-myo-inositol 1,3,4,5,6-pentakisphosphate
mutant enzyme K200A, at pH 7.5 and 25°C
0.04348
1D-myo-inositol 1,3,4,5,6-pentakisphosphate
mutant enzyme H196A, at pH 7.5 and 25°C
0.04453
1D-myo-inositol 1,3,4,5,6-pentakisphosphate
-
mutant enzyme E82C/S142C, at pH 7.5 and 25°C
0.0548
1D-myo-inositol 1,3,4,5,6-pentakisphosphate
mutant enzyme R45A, at pH 7.5 and 25°C
0.05935
1D-myo-inositol 1,3,4,5,6-pentakisphosphate
mutant enzyme R192A, at pH 7.5 and 25°C
0.06227
1D-myo-inositol 1,3,4,5,6-pentakisphosphate
mutant enzyme R415A, at pH 7.5 and 25°C
0.0628
1D-myo-inositol 1,3,4,5,6-pentakisphosphate
-
0.06305
1D-myo-inositol 1,3,4,5,6-pentakisphosphate
-
wild type enzyme, at pH 7.5 and 25°C
0.06305
1D-myo-inositol 1,3,4,5,6-pentakisphosphate
wild type enzyme, at pH 7.5 and 25°C
0.07686
1D-myo-inositol 1,3,4,5,6-pentakisphosphate
mutant enzyme Y419A, at pH 7.5 and 25°C
0.0833
1D-myo-inositol 1,3,4,5,6-pentakisphosphate
mutant enzyme N239A, at pH 7.5 and 25°C
0.119
1D-myo-inositol 1,3,4,5,6-pentakisphosphate
-
0.119
1D-myo-inositol 1,3,4,5,6-pentakisphosphate
400 microM of substrate ATP is used
0.176
1D-myo-inositol 1,3,4,5,6-pentakisphosphate
-
at 0.0004 mM ATP
0.04754
1D-myo-inositol 3,4,5,6-tetrakisphosphate
-
wild type enzyme, at pH 7.5 and 25°C
0.04754
1D-myo-inositol 3,4,5,6-tetrakisphosphate
wild type enzyme, at pH 7.5 and 25°C
0.07917
1D-myo-inositol 3,4,5,6-tetrakisphosphate
-
mutant enzyme E82C/S142C, at pH 7.5 and 25°C
0.0084
ATP
-
-
0.07
ATP
-
about, cosubstrate: 1D-myo-inositol 1,4,5-triphosphate
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0.246 - 0.736
1D-myo-inositol 1,3,4,5,6-pentakisphosphate
0.4581
1D-myo-inositol 1,3,4,6-tetrakisphosphate
wild type enzyme, at pH 7.5 and 25°C
0.11
1D-myo-inositol 1,4,5,6-tetrakisphosphate
wild type enzyme, at pH 7.5 and 25°C
0.105 - 0.549
1D-myo-inositol 3,4,5,6-tetrakisphosphate
0.246
1D-myo-inositol 1,3,4,5,6-pentakisphosphate
mutant enzyme N238A, at pH 7.5 and 25°C
0.265
1D-myo-inositol 1,3,4,5,6-pentakisphosphate
mutant enzyme N239A, at pH 7.5 and 25°C
0.279
1D-myo-inositol 1,3,4,5,6-pentakisphosphate
mutant enzyme K200A, at pH 7.5 and 25°C
0.367
1D-myo-inositol 1,3,4,5,6-pentakisphosphate
mutant enzyme R192A, at pH 7.5 and 25°C
0.453
1D-myo-inositol 1,3,4,5,6-pentakisphosphate
mutant enzyme R45A, at pH 7.5 and 25°C
0.569
1D-myo-inositol 1,3,4,5,6-pentakisphosphate
mutant enzyme H196A, at pH 7.5 and 25°C
0.645
1D-myo-inositol 1,3,4,5,6-pentakisphosphate
mutant enzyme R415A, at pH 7.5 and 25°C
0.694
1D-myo-inositol 1,3,4,5,6-pentakisphosphate
mutant enzyme Y419A, at pH 7.5 and 25°C
0.734
1D-myo-inositol 1,3,4,5,6-pentakisphosphate
-
wild type enzyme, at pH 7.5 and 25°C
0.734
1D-myo-inositol 1,3,4,5,6-pentakisphosphate
wild type enzyme, at pH 7.5 and 25°C
0.736
1D-myo-inositol 1,3,4,5,6-pentakisphosphate
-
mutant enzyme E82C/S142C, at pH 7.5 and 25°C
0.105
1D-myo-inositol 3,4,5,6-tetrakisphosphate
-
wild type enzyme, at pH 7.5 and 25°C
0.105
1D-myo-inositol 3,4,5,6-tetrakisphosphate
wild type enzyme, at pH 7.5 and 25°C
0.549
1D-myo-inositol 3,4,5,6-tetrakisphosphate
-
mutant enzyme E82C/S142C, at pH 7.5 and 25°C
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evolution
differential spatial and temporal expression profiling of gene GmIpk1 and its two homologues Glyma06g03310 and Glyma04g03310 in Glycine max
evolution
most residues involved in substrate binding and catalysis are conserved between mammal and plant IP5 2-Ks, but some differences in the inositide P1 and P3 coordination are observed. InmIP5 2-K, additional interactions with P1 are produced through the side chain of Lys173, a residue non-conserved with the plant IP5 2-Ks but absolutely conserved in mammal enzymes, whereas conservative substitutions can be observed in other vertebrates
evolution
the amino acid sequence of GmIPK1 shows much similarity with that of Phaseolus vulgaris and Cicer arietinum. It also shows the presence of the characteristic Ins_P5_2-kinase domain required for catalytic activity
malfunction
-
a functional Asp1 kinase domain abolishes invasive growth which is monopolar
malfunction
a loss-of-function mutant exhibits disturbed phosphate homeostasis and overaccumulated phosphate as a consequence of increased phosphate uptake activity and root-to-shoot phosphate translocation. The mutant also shows a phosphate deficiency-like root system architecture with reduced primary root and enhanced lateral root growth
malfunction
a mutant of inositol pentakisphosphate 2-kinase displays hypersensitivity to arsenate stress and less arsenate uptake when compared to the wild type enzyme
malfunction
cells lacking the enzyme display defects in dynein-dependent trafficking pathways including endosomal sorting, vesicle movement and Golgi maintenance
malfunction
disruption of inositol pentakisphosphate 2-kinase profoundly influences cellular processes
malfunction
in contrast to wild-type IPK1, which is able to restore the phosphate content of the ipk1-1 mutant to wild-type level, both kinase-inactive IPK1 forms fail to complement excessive phosphate accumulation and PSR gene activation in ipk1-1. 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. Misregulation of phosphate homeostasis in ipk1-1 is not caused by defective InsP6-mediated mRNA export. Neither of the kinase-inactive IPK1 mutants K168A and D368A complement the PSR-like RSA phenotypes (i.e. reduced primary root and enhanced lateral root growth) of ipk1-1 mutant. In addition to the decreased InsP6 level, levels of InsP7 and InsP8 are also reduced in ipk1-1 mutants
malfunction
urine inositol pentakisphosphate 2-kinase and changes in kidney structure in early diabetic kidney disease in type 1 diabetes. A higher prevalence of detectable urinary inositol 1,3,4,5,6-pentakisphosphate 2-kinase (IPP2K) in type 1 diabetes correlates with early renal function decline. Proximal tubule cells from people with type 1 diabetes and diabetic kidney disease (DKD) express more IPP2K compared with controls. Demographics and clinical characteristics by tertile of baseline urine inositol 1,3,4,5,6-pentakisphosphate 2-kinase/creatinine (IPP2K/Cr), overview
malfunction
-
cells lacking the enzyme display defects in dynein-dependent trafficking pathways including endosomal sorting, vesicle movement and Golgi maintenance
-
metabolism
genetic dissection of the roles for InsP and PP-InsP biosynthesis enzymes in regulation of phosphate homeostasis, overview
metabolism
inositol 1,3,4,5,6-pentakisphosphate 2-kinase catalyzes the terminal step in the phytic acid biosynthetic pathway
metabolism
inositol tris/tetrakisphosphate kinase 1 (ITPK1, EC 2.7.1.134) and inositol pentakisphosphate 2-kinase (IPK1, EC 2.7.1.158) comprise a reversible metabolic cassette converting Ins(3,4,5,6)P4 into 5-InsP7 and back in a nucleotide-dependent manner. Ability of Arabidopsis inositol tris/tetrakisphosphate kinase 1 to discriminate between symmetric and enantiomeric substrates in the production of diverse symmetric and asymmetric myo-inositol phosphate and diphospho-myo-inositol phosphate (inositol diphosphate) products
metabolism
IPK1 is the terminal enzyme in phytic acid biosynthesis
metabolism
nositol 1,3,4,5,6-pentakisphosphate 2-kinase catalyzes the terminal step in the phytic acid biosynthetic pathway
physiological function
knock-out mutant cells are defective in nuclear mRNA export, cell morphology, polarized growth, and cell separation
physiological function
-
Asp1 kinase activity regulates cell-cell adhesion and increases resistance towards thiabendazole. The Asp1 kinase activity encoded by the N-terminal part of the protein is regulated negatively by the C-terminal domain of Asp1. Asp1 is a key regulator of the morphological switch via the cAMP protein kinase A
physiological function
the enzyme activity is required for cytoplasmic dynein transport
physiological function
the enzyme has important roles in growth and phosphate homeostasis
physiological function
association of urine inositol 1,3,4,5,6-pentakisphosphate 2-kinase (IPP2K) with the presence and progression of diabetic kidney disease (DKD) lesions. Inositol 6-phosphate is a key intracellular signaling molecule with roles in mRNA editing and chromatin remodeling
physiological function
GmIPK1 plays a significant role in phytate synthesis
physiological function
inositol 1,3,4,5,6-pentakisphosphate 2-kinase (IP5 2-K) phosphorylates inositol pentakisphosphate (IP5) to produce inositol 1,2,3,4,5,6-hexakisphosphate (IP6), from ATP
physiological function
inositol pentakisphosphate 2-kinase catalyzes the phosphorylation of the axial 2-OH of myo-inositol 1,3,4,5,6-pentakisphosphate for de novo synthesis of myo-inositol hexakisphosphate
physiological function
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. In addition to regulating the phosphate content, the kinase activity of IPK1 is also required for root system architecture
physiological function
-
the enzyme activity is required for cytoplasmic dynein transport
-
additional information
molecular docking study
additional information
molecular docking study
additional information
-
molecular docking study
additional information
overall structure analysis of enzyme CnIpk1, conformational state and changes, overview
additional information
three-dimensional homolgy modelling, GmIPK1 protein model (PMD ID PM0079931), using Arabidopsis thaliana enzyme structure (PDB ID 4AQK) as template, structure-function relationship of GmIPK1, molecular dynamics simulations and molecular docking study, overview
additional information
three-dimensional homolgy modelling, GmIPK1 protein model (PMD ID PM0079931), using Arabidopsis thaliana enzyme structure (PDB ID 4AQK) as template, structure-function relationship of GmIPK1, molecular dynamics simulations and molecular docking study, overview
additional information
-
three-dimensional homolgy modelling, GmIPK1 protein model (PMD ID PM0079931), using Arabidopsis thaliana enzyme structure (PDB ID 4AQK) as template, structure-function relationship of GmIPK1, molecular dynamics simulations and molecular docking study, overview
additional information
-
overall structure analysis of enzyme CnIpk1, conformational state and changes, overview
-
additional information
-
overall structure analysis of enzyme CnIpk1, conformational state and changes, overview
-
additional information
-
overall structure analysis of enzyme CnIpk1, conformational state and changes, overview
-
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?
-
x * 52000, SDS-PAGE
?
x * 51132, sequence calculation
?
-
x * 78033, calculated from amino acid sequence
monomer
1 * 41000, there are four monomers in the asymmetric unit, but size-exclusion chromatographic analysis indicates that an estimated molecular weight of CnIpk1 corresponds to 41 kDa, which is equivalent to a monomer. The four monomers in the asymmetric unit do not form any noticeable oligomeric conformation in a symmetric manner, which indicated that CnIpk1 is a monomeric enzyme
monomer
-
1 * 41000, there are four monomers in the asymmetric unit, but size-exclusion chromatographic analysis indicates that an estimated molecular weight of CnIpk1 corresponds to 41 kDa, which is equivalent to a monomer. The four monomers in the asymmetric unit do not form any noticeable oligomeric conformation in a symmetric manner, which indicated that CnIpk1 is a monomeric enzyme
-
monomer
-
1 * 41000, there are four monomers in the asymmetric unit, but size-exclusion chromatographic analysis indicates that an estimated molecular weight of CnIpk1 corresponds to 41 kDa, which is equivalent to a monomer. The four monomers in the asymmetric unit do not form any noticeable oligomeric conformation in a symmetric manner, which indicated that CnIpk1 is a monomeric enzyme
-
monomer
-
1 * 41000, there are four monomers in the asymmetric unit, but size-exclusion chromatographic analysis indicates that an estimated molecular weight of CnIpk1 corresponds to 41 kDa, which is equivalent to a monomer. The four monomers in the asymmetric unit do not form any noticeable oligomeric conformation in a symmetric manner, which indicated that CnIpk1 is a monomeric enzyme
-
additional information
enzyme CnIpk1 exhibits two structural lobes: the N-terminal lobe (N-lobe, residues Met1-Glu134) and the C-terminal lobe (C-lobe, residues Ile146-Arg415) with an 11-residue loop between the lobes. Specifically, the N-lobe forms an alpha/beta fold with five antiparallel beta-strands in an 1-2-3-5-4 order and surrounding alpha-helices, structure overview
additional information
-
enzyme CnIpk1 exhibits two structural lobes: the N-terminal lobe (N-lobe, residues Met1-Glu134) and the C-terminal lobe (C-lobe, residues Ile146-Arg415) with an 11-residue loop between the lobes. Specifically, the N-lobe forms an alpha/beta fold with five antiparallel beta-strands in an 1-2-3-5-4 order and surrounding alpha-helices, structure overview
-
additional information
-
enzyme CnIpk1 exhibits two structural lobes: the N-terminal lobe (N-lobe, residues Met1-Glu134) and the C-terminal lobe (C-lobe, residues Ile146-Arg415) with an 11-residue loop between the lobes. Specifically, the N-lobe forms an alpha/beta fold with five antiparallel beta-strands in an 1-2-3-5-4 order and surrounding alpha-helices, structure overview
-
additional information
-
enzyme CnIpk1 exhibits two structural lobes: the N-terminal lobe (N-lobe, residues Met1-Glu134) and the C-terminal lobe (C-lobe, residues Ile146-Arg415) with an 11-residue loop between the lobes. Specifically, the N-lobe forms an alpha/beta fold with five antiparallel beta-strands in an 1-2-3-5-4 order and surrounding alpha-helices, structure overview
-
additional information
enzyme domain analysis from sequence, sequence comparisons
additional information
secondary structure prediction revealing that 74.46% of amino acids are in alpha-helix, whereas 57.64% of residues in beta-sheets and 12.19% in coil conformations, structure modeling, overview
additional information
secondary structure prediction revealing that 74.46% of amino acids are in alpha-helix, whereas 57.64% of residues in beta-sheets and 12.19% in coil conformations, structure modeling, overview
additional information
-
secondary structure prediction revealing that 74.46% of amino acids are in alpha-helix, whereas 57.64% of residues in beta-sheets and 12.19% in coil conformations, structure modeling, overview
additional information
peptide mapping, quantitative LC-selective reaction monitoring-MS (LC-SRM-MS) analysis
additional information
-
peptide mapping, quantitative LC-selective reaction monitoring-MS (LC-SRM-MS) analysis
additional information
mouse IP5 2-K folds in two lobes, N- and C-terminal lobes, connected by a hinge, thereby conserving the general fold scheme of PKs and IPKs, and in a similar way, both lobes coordinate the nucleotide between them. The N-lobe core forms a beta-sheet from five antiparallel beta-strands (beta1-beta5) showing two helical segments. The first helical segment (N-I) harbors alpha1, equivalent to the helix alphaC characterized in all protein kinases, whereas the second one (N-II) is a specific insertion different in every IPK subfamily. Structure comparisons
additional information
-
mouse IP5 2-K folds in two lobes, N- and C-terminal lobes, connected by a hinge, thereby conserving the general fold scheme of PKs and IPKs, and in a similar way, both lobes coordinate the nucleotide between them. The N-lobe core forms a beta-sheet from five antiparallel beta-strands (beta1-beta5) showing two helical segments. The first helical segment (N-I) harbors alpha1, equivalent to the helix alphaC characterized in all protein kinases, whereas the second one (N-II) is a specific insertion different in every IPK subfamily. Structure comparisons
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York, J.D.; Odom, A.R.; Murphy, R.; Ives, E.B.; Wente, S.R.
A phospholipase C-dependent inositol polyphosphate kinase pathway required for efficient messenger RNA export
Science
285
96-100
1999
Saccharomyces cerevisiae
brenda
Ongusaga, P.P.; Hughes, P.J.; Davey, J.; Michell, R.H.
Inositol hexakisphosphate in Schizosaccharomyces pombe: synthesis from Ins(1,4,5)P3 and osmotic regulation
Biochem. J.
335
671-679
1998
Schizosaccharomyces pombe
-
brenda
Sweetman, D.; Johnson, S.; Caddick, S.E.; Hanke, D.E.; Brearley, C.A.
Characterization of an Arabidopsis inositol 1,3,4,5,6-pentakisphosphate 2-kinase (AtIPK1)
Biochem. J.
394
95-103
2006
Arabidopsis thaliana
brenda
Phillippy, B.Q.; Ullah, A.H.J.; Ehrlich, K.C.
Purification and some properties of inositol 1,3,4,5,6-pentakis phosphate 2-kinase from immature soybean seeds
J. Biol. Chem.
269
28393-28399
1994
Glycine max
brenda
Ives, E.B.; Nichols, J.; Wente, S.R.; York, J.D.
Biochemical and functional characterization of inositol 1,3,4,5,6-pentakisphosphate 2-kinases
J. Biol. Chem.
275
36575-36583
2000
Saccharomyces cerevisiae, Schizosaccharomyces pombe (Q9USK0), Schizosaccharomyces pombe
brenda
Verbsky, J.W.; Wilson, M.P.; Kisseleva, M.V.; Majerus, P.W.; Wente, S.R.
The synthesis of inositol hexakisphosphate. Characterization of human inositol 1,3,4,5,6-pentakisphosphate 2-kinase
J. Biol. Chem.
277
31857-31862
2002
Homo sapiens
brenda
Miller, A.L.; Suntharalingam, N.; et al.
Cytoplasmic inositol hexakisphosphate production is sufficient for mediating the Gle1-mRNA export pathway
J. Biol. Chem.
279
51022-51032
2004
Saccharomyces cerevisiae
brenda
Fujii, M.; York, J.D.
A role for rat inositol polyphosphate kinases rIPK2 and rIPK1 in inositol pentakisphosphate and inositol hexakisphosphate production in rat-1 cells
J. Biol. Chem.
280
1156-1164
2005
Rattus norvegicus, Rattus norvegicus (Q5PXE9)
brenda
Verbsky, J.; Lavine, K.; Majerus, P.W.
Disruption of the mouse inositol 1,3,4,5,6-pentakisphosphate 2-kinase gene, associated lethality, and tissue distribution of 2-kinase expression
Proc. Natl. Acad. Sci. USA
102
8448-8453
2005
Mus musculus
brenda
Brehm, M.A.; Schenk, T.M.; Zhou, X.; Fanick, W.; Lin, H.; Windhorst, S.; Nalaskowski, M.M.; Kobras, M.; Shears, S.B.; Mayr, G.W.
Intracellular localization of human inositol 1,3,4,5,6-pentakisphosphate 2-kinase
Biochem. J.
408
335-345
2007
Homo sapiens
brenda
Sun, Y.; Thompson, M.; Lin, G.; Butler, H.; Gao, Z.; Thornburgh, S.; Yau, K.; Smith, D.A.; Shukla, V.K.
Inositol 1,3,4,5,6-pentakisphosphate 2-kinase from maize: molecular and biochemical characterization
Plant Physiol.
144
1278-1291
2007
Zea mays, Zea mays (A4GWX8), Zea mays (A6YH13)
brenda
Caddick, S.E.; Harrison, C.J.; Stavridou, I.; Mitchell, J.L.; Hemmings, A.M.; Brearley, C.A.
A Solanum tuberosum inositol phosphate kinase (StITPK1) displaying inositol phosphate-inositol phosphate and inositol phosphate-ADP phosphotransferase activities
FEBS Lett.
582
1731-1737
2008
Solanum tuberosum (A4H2J0), Solanum tuberosum
brenda
Sarmah, B.; Wente, S.R.
Dual functions for the Schizosaccharomyces pombe inositol kinase Ipk1 in nuclear mRNA export and polarized cell growth
Eukaryot. Cell
8
134-146
2009
Schizosaccharomyces pombe (Q9USK0), Schizosaccharomyces pombe
brenda
Poehlmann, J.; Fleig, U.
Asp1, a conserved 1/3 inositol polyphosphate kinase, regulates the dimorphic switch in Schizosaccharomyces pombe
Mol. Cell. Biol.
30
4535-4547
2010
Schizosaccharomyces pombe
brenda
Wundenberg, T.; Grabinski, N.; Lin, H.; Mayr, G.W.
Discovery of InsP6-kinases as InsP6-dephosphorylating enzymes provides a new mechanism of cytosolic InsP6 degradation driven by the cellular ATP/ADP ratio
Biochem. J.
462
173-184
2014
Homo sapiens, Rattus norvegicus
brenda
Chanduri, M.; Rai, A.; Malla, A.B.; Wu, M.; Fiedler, D.; Mallik, R.; Bhandari, R.
Inositol hexakisphosphate kinase 1 (IP6K1) activity is required for cytoplasmic dynein-driven transport
Biochem. J.
473
3031-3047
2016
Mus musculus (Q6PD10)
brenda
Wang, H.; Godage, H.Y.; Riley, A.M.; Weaver, J.D.; Shears, S.B.; Potter, B.V.
Synthetic inositol phosphate analogs reveal that PPIP5K2 has a surface-mounted substrate capture site that is a target for drug discovery
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21
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2014
Homo sapiens
brenda
Gosein, V.; Miller, G.J.
Roles of phosphate recognition in inositol 1,3,4,5,6-pentakisphosphate 2-kinase (IPK1) substrate binding and activation
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288
26908-26913
2013
Arabidopsis thaliana (Q93YN9)
brenda
Gosein, V.; Miller, G.J.
Conformational stability of inositol 1,3,4,5,6-pentakisphosphate 2-kinase (IPK1) dictates its substrate selectivity
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288
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2013
Arabidopsis thaliana
brenda
Brehm, M.; Wundenberg, T.; Williams, J.; Mayr, G.; Shears, S.
A non-catalytic role for inositol 1,3,4,5,6-pentakisphosphate 2-kinase in the synthesis of ribosomal RNA
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126
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2013
Homo sapiens
-
brenda
Sun, Y.Y.; Xu, W.Z.; Wu, L.; Wang, R.Z.; He, Z.Y.; Ma, M.
An Arabidopsis mutant of inositol pentakisphosphate 2-kinase AtIPK1 displays reduced arsenate tolerance
Plant Cell Environ.
39
416-426
2016
Arabidopsis thaliana (Q93YN9), Arabidopsis thaliana
brenda
Kuo, H.F.; Chang, T.Y.; Chiang, S.F.; Wang, W.D.; Charng, Y.Y.; Chiou, T.J.
Arabidopsis inositol pentakisphosphate 2-kinase, AtIPK1, is required for growth and modulates phosphate homeostasis at the transcriptional level
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80
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2014
Arabidopsis thaliana (Q93YN9)
brenda
Yu, J.; Saiardi, A.; Greenwood, J.S.; Bewley, J.D.
Molecular and biochemical identification of inositol 1,3,4,5,6-pentakisphosphate 2-kinase encoding mRNA variants in castor bean (Ricinus communis L.) seeds
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239
965-977
2014
Ricinus communis
brenda
Basak, N.; Krishnan, V.; Pandey, V.; Punjabi, M.; Hada, A.; Marathe, A.; Jolly, M.; Palaka, B.K.; Ampasala, D.R.; Sachdev, A.
Expression profiling and in silico homology modeling of inositol pentakisphosphate 2-kinase, a potential candidate gene for low phytate trait in soybean
3 Biotech
10
268
2020
Glycine max (I1JT87), Glycine max (U5TRK1), Glycine max
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Looker, H.C.; Merchant, M.L.; Rane, M.J.; Nelson, R.G.; Kimmel, P.L.; Rovin, B.H.; Klein, J.B.; Mauer, M.; Mauer, M.
Urine inositol pentakisphosphate 2-kinase and changes in kidney structure in early diabetic kidney disease in type 1 diabetes
Am. J. Physiol. Renal Physiol.
315
F1484-F1492
2018
Homo sapiens (Q9H8X2), Homo sapiens
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Whitfield, H.; White, G.; Sprigg, C.; Riley, A.M.; Potter, B.V.L.; Hemmings, A.M.; Brearley, C.A.
An ATP-responsive metabolic cassette comprised of inositol tris/tetrakisphosphate kinase 1 (ITPK1) and inositol pentakisphosphate 2-kinase (IPK1) buffers diphosphosphoinositol phosphate levels
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477
2621-2638
2020
Arabidopsis thaliana (Q93YN9)
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Basak, N.; Krishnan, V.; Pandey, V.; Punjabi, M.; Hada, A.; Marathe, A.; Jolly, M.; Sachdev, A.
Molecular characterization of inositol pentakisphosphate 2-kinase (GmlPk1) from soybean and its expression pattern in the developing seeds
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77
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2017
Glycine max (U5TRK1)
-
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Franco-Echevarria, E.; Sanz-Aparicio, J.; Brearley, C.A.; Gonzalez-Rubio, J.M.; Gonzalez, B.
The crystal structure of mammalian inositol 1,3,4,5,6-pentakisphosphate 2-kinase reveals a new zinc-binding site and key features for protein function
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292
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Mus musculus (Q6P1C1), Mus musculus
brenda
Whitfield, H.; Gilmartin, M.; Baker, K.; Riley, A.M.; Godage, H.Y.; Potter, B.V.L.; Hemmings, A.M.; Brearley, C.A.
A fluorescent probe identifies active site ligands of inositol pentakisphosphate 2-kinase
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61
8838-8846
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Arabidopsis thaliana (Q93YN9)
brenda
Oh, J.; Lee, D.G.; Bahn, Y.S.; Rhee, S.
Crystal structure of inositol 1,3,4,5,6-pentakisphosphate 2-kinase from Cryptococcus neoformans
J. Struct. Biol.
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118-123
2017
Cryptococcus neoformans var. grubii (J9VKS8), Cryptococcus neoformans var. grubii FGSC 9487 (J9VKS8), Cryptococcus neoformans var. grubii ATCC 208821 (J9VKS8), Cryptococcus neoformans var. grubii CBS 10515 (J9VKS8)
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.
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2018
Arabidopsis thaliana (Q93YN9), Arabidopsis thaliana
brenda
Franco-Echevarria, E.; Sanz-Aparicio, J.; Troffer-Charlier, N.; Poterszman, A.; Gonzalez, B.
Crystallization and preliminary X-ray diffraction analysis of a mammal inositol 1,3,4,5,6-pentakisphosphate 2-kinase
Protein J.
36
240-248
2017
Mus musculus (Q6P1C1), Mus musculus
brenda