2.7.1.151: inositol-polyphosphate multikinase
This is an abbreviated version!
For detailed information about inositol-polyphosphate multikinase, go to the full flat file.
Word Map on EC 2.7.1.151
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2.7.1.151
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phosphatidylinositol
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phospholipase
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phosphoinositide
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4,5-bisphosphate
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4-phosphate
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5-phosphatase
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1,3,4,5-tetrakisphosphate
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bacteriorhodopsin
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insp3
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pip2
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ptdins4,5p2
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4-kinase
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hexakisphosphate
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pikfyve
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ptdins4p
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pentakisphosphate
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1,3,4-trisphosphate
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3hinositol
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phosphatidylinositol-4-phosphate
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photocycle
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diphosphoinositol
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inositide
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3,4,5-trisphosphate
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5/6-kinase
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polyphosphoinositide
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medicine
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light-driven
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arf6
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agriculture
- 2.7.1.151
- phosphatidylinositol
- phospholipase
- phosphoinositide
- 4,5-bisphosphate
- 4-phosphate
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5-phosphatase
- 1,3,4,5-tetrakisphosphate
-
bacteriorhodopsin
- insp3
- pip2
-
ptdins4,5p2
-
4-kinase
- hexakisphosphate
- pikfyve
-
ptdins4p
- pentakisphosphate
- 1,3,4-trisphosphate
-
3hinositol
- phosphatidylinositol-4-phosphate
-
photocycle
-
diphosphoinositol
-
inositide
- 3,4,5-trisphosphate
-
5/6-kinase
-
polyphosphoinositide
- medicine
-
light-driven
- arf6
- agriculture
Reaction
Synonyms
1,3,4,6-tetrakisphosphate 5-kinase, 5-kinase, Arg82, ArgRIII, ARGSIII, AtIpk2a, AtIpk2b, AtIpk2beta, HsIPMK, Impk, inositol 1,4,5-trisphosphate 3-kinase, inositol phosphate multikinase, inositol phosphate multikinase 2, inositol polyphosphate 6-/3-kinase, inositol polyphosphate kinase, inositol polyphosphate multikinase, Ins(1,4,5)P3 3-kinase, InsP4 5-kinase, IP3 3-kinase, IP3/IP4 6-/3-kinase, IP3K, IPK, Ipk2, Ipk2/Impk/IP3K, Ipk2a, Ipk2beta/IP3K, IPKII, IPMK, ITPK1, Kcs1, Kcs1p, More, phosphoinositol kinase, PI3K, StIPMK
ECTree
2.7.1.151 inositol-polyphosphate multikinaseAdvanced search results
results (
results (Engineering
Engineering on EC 2.7.1.151 - inositol-polyphosphate multikinase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D100A
isozyme IPK2beta, site-directed mutagenesis, inactive mutant
D98A
isozyme IPK2alpha, site-directed mutagenesis, inactive mutant
K117W
mutant exhibits nearly normal 6-kinase function but harbors significantly reduced 3-kinase activity. The mutant complements conditional nutritional growth defects observed in ipmk null yeast and suppresses lethality observed in ipmk null flies
K117W/K121W
mutant exhibits nearly normal 6-kinase function but harbors significantly reduced 3-kinase activity. The mutant complements conditional nutritional growth defects observed in ipmk null yeast and suppresses lethality observed in ipmk null flies
K121W
although no inositol tetrakisphosphate is present with wild-type IPMK, levels of inositol tetrakisphosphate and inositol hexakisphosphate are equivalent in mutant K121W
H388A
site-directed mutagenesis, the mutant shows no Ins(1,4,5)P3 3-kinase activity and reduced Ins(1,3,4,5)P4 6-kinase activity compared to wild-type
K160A
site-directed mutagenesis, the mutant shows no Ins(1,4,5)P3 3-kinase activity and reduced Ins(1,3,4,5)P4 6-kinase activity compared to wild-type
K167A
site-directed mutagenesis, the mutant shows reduced Ins(1,4,5)P3 3-kinase activity and Ins(1,3,4,5)P4 6-kinase activity compared to wild-type
K327Q/K328Q
site-directed mutagenesis, generation of an IPMK mutant with inactivated nuclear localization signal, NLS, whose intracellular distribution is unaffected by inhibition of conventional protein import
Q163A
site-directed mutagenesis, the mutant shows no Ins(1,4,5)P3 3-kinase activity and reduced Ins(1,3,4,5)P4 6-kinase activity compared to wild-type
Q163K
site-directed mutagenesis, the mutant shows reduced Ins(1,4,5)P3 3-kinase activity and increased Ins(1,3,4,5)P4 6-kinase activity compared to wild-type
Q163R
site-directed mutagenesis, the mutant shows reduced Ins(1,4,5)P3 3-kinase activity and increased Ins(1,3,4,5)P4 6-kinase activity compared to wild-type
Q164A
site-directed mutagenesis, the mutant shows reduced Ins(1,4,5)P3 3-kinase activity and Ins(1,3,4,5)P4 6-kinase activity compared to wild-type
Q164K
site-directed mutagenesis, the mutant shows reduced Ins(1,4,5)P3 3-kinase activity and increased Ins(1,3,4,5)P4 6-kinase activity compared to wild-type
Q164R
site-directed mutagenesis, the mutant shows reduced Ins(1,4,5)P3 3-kinase activity and increased Ins(1,3,4,5)P4 6-kinase activity compared to wild-type
Q196A
site-directed mutagenesis, the mutant shows reduced Ins(1,4,5)P3 3-kinase activity and Ins(1,3,4,5)P4 6-kinase activity compared to wild-type
Q196K
site-directed mutagenesis, the mutant shows reduced Ins(1,4,5)P3 3-kinase activity and increased Ins(1,3,4,5)P4 6-kinase activity compared to wild-type
Q196R
site-directed mutagenesis, the mutant shows reduced Ins(1,4,5)P3 3-kinase activity and increased Ins(1,3,4,5)P4 6-kinase activity compared to wild-type
Q78A
site-directed mutagenesis, the mutant shows no Ins(1,4,5)P3 3-kinase activity and reduced Ins(1,3,4,5)P4 6-kinase activity compared to wild-type
R82A
site-directed mutagenesis, the mutant shows no Ins(1,4,5)P3 3-kinase activity and reduced Ins(1,3,4,5)P4 6-kinase activity compared to wild-type
L794A/L801A
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site-directed mutagenesis, expression in the knockout mutant strain results in activity similar to the wild-type enzyme, phenotype overview
L794A/L801A/L857A/L864A
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site-directed mutagenesis, expression in the knockout mutant strain results in activity similar to the wild-type enzyme, the mutant strain shows compromised cell wall integrity, phenotype overview
L857A/L864A
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site-directed mutagenesis, expression in the knockout mutant strain results in activity similar to the wild-type enzyme, phenotype overview
S887A/L888A/L889A
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site-directed mutagenesis, expression in the knockout mutant strain results in activity similar to the wild-type enzyme, the mutant strain shows compromised cell wall integrity, phenotype overview
additional information
additional information
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construction of an N-terminal deletion mutant comprising residues 266-371, the mutant enzyme is inhibited by aurintricarboxylic acid, gossypol, 3',4',7,8-tetrahydroxyflavone, epigallocatechin-3-gallate, chlorogenic acid, and rose bengal, but not by quercetin, epicatechin-3-gallate, ellagic acid, hypericin, and myricetin in contrary to the wild-type
additional information
genetic or RNA interference-mediated, and shRNA-mediated knockdown of enzyme IPMK
additional information
overexpression of catalytically inactive IPMK mutants is sufficient to reduce RAD51 foci formation
additional information
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overexpression of catalytically inactive IPMK mutants is sufficient to reduce RAD51 foci formation
additional information
generation of the core catalytic domain of the enzyme that contains residues 50 to 416, from which an internal domain comprising residues 263 to 377 is deleted. The deletion is necessary to obtain crystals, it is replaced with a simple Gly-Gly-Ser-Gly-Gly linker. This deletion does not compromise catalytic activity, it is a non-catalytic region of the protein. It contains a nuclear localization sequence, flanked by residues that host protein kinase phosphorylation sites that regulate nuclear localization sequence functionality. Gln residues at positions 163, 164, and 196 are mutated each to Arg and Lys, both of which have side chains that are larger and also positively charged at physiological pH. The results are quite dramatic: in each case, the rate of Ins(1,4,5)P3 3-kinase activity declines, but in contrast, the rate of Ins(1,3,4,5)P4 6-kinase activity is not impaired, three of these mutants show increased 6-kinase activity, analysis of the structural basis, overview
additional information
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generation of the core catalytic domain of the enzyme that contains residues 50 to 416, from which an internal domain comprising residues 263 to 377 is deleted. The deletion is necessary to obtain crystals, it is replaced with a simple Gly-Gly-Ser-Gly-Gly linker. This deletion does not compromise catalytic activity, it is a non-catalytic region of the protein. It contains a nuclear localization sequence, flanked by residues that host protein kinase phosphorylation sites that regulate nuclear localization sequence functionality. Gln residues at positions 163, 164, and 196 are mutated each to Arg and Lys, both of which have side chains that are larger and also positively charged at physiological pH. The results are quite dramatic: in each case, the rate of Ins(1,4,5)P3 3-kinase activity declines, but in contrast, the rate of Ins(1,3,4,5)P4 6-kinase activity is not impaired, three of these mutants show increased 6-kinase activity, analysis of the structural basis, overview
additional information
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construction of mutants by disrution of gene ipk2, the resulting enzyme-deficient Ipk2 null mice die around embryonic day 9.5 with multiple morphological defects, including abnormal folding of the neural tube, overview
additional information
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an enzyme-deficient mutant strain is resistant to inhibition by wortmannin, while transformation with the wild-type enzyme reverses the effect, the enzyme-deficient mutant shows increased phosphatidylinositol 4,5-bisphosphate levels
additional information
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construction of a knockout mutant strain from strain BY4709, the mutant cells contain a fragmented vacuolar compartment, cell growth and cell wall integrity are perturbed, and response to sal stress is altered, a metabolic block in arg82DELTA cells results in the same phenotype, overexpression of the enzyme can partially bypass the metabolic block, overview, expression of full length enzyme and enzyme mutants in the knockout strain, phenotypes overview
additional information
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growth of an enzyme-deficient strain can be rescued by expression of either 1D-myo-inositol 1,4,5-trisphosphate 3-kinase or 6-kinase at high temperatures, but only 1D-myo-inositol 1,4,5-trisphosphate 6-kinase expression enables the strain to grow on ornithine
