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Information on EC 3.1.3.56 - inositol-polyphosphate 5-phosphatase
for references in articles please use BRENDA:EC3.1.3.56
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EC Tree 3 Hydrolases
3.1 Acting on ester bonds
3.1.3 Phosphoric-monoester hydrolases
3.1.3.56 inositol-polyphosphate 5-phosphatase
IUBMB Comments
One mammalian isoform is known. This enzyme is distinguished from the family of enzymes classified under EC 3.1.3.36, phosphoinositide 5-phosphatase, by its inability to dephosphorylate inositol lipids.
The enzyme appears in viruses and cellular organisms
- 3.1.3.56
- phosphatidylinositol
- 1,4-bisphosphate
- 5ptases
-
oculocerebrorenal
- 3,4,5-trisphosphate
-
ptdins4,5p2
-
3hinositol
- 2,3-bisphosphoglycerate
- inpp5f
-
ptdins3,4,5p3
- medicine
- molecular biology
Reaction Schemes
showSynonyms
inpp5k, ins(1,4,5)p3 5-phosphatase, inositol polyphosphate-5-phosphatase, inpp5a, insp 5-ptase, insp3 5-phosphatase, pip3 phosphatase, at5ptase1, inositol polyphosphatase, 5pt13, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
5PTase
D-myo-inositol 1,4,5-triphosphate 5-phosphatase
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D-myo-inositol 1,4,5-trisphosphate 5-phosphatase
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D-myo-inositol(1,4,5)/(1,3,4,5)-polyphosphate 5-phosphatase
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inosine triphosphatase
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inositol 1,4,5-triphosphate 5-phosphatase
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inositol 1,4,5-trisphosphate 5-monophosphatase
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inositol 1,4,5-trisphosphate 5-phosphatase
inositol 1,4,5-trisphosphate phosphatase
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inositol phosphate 5-phosphomonoesterase
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inositol polyphosphate 5-phosphatase
inositol polyphosphate-5-phosphatase
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inositol trisphosphate phosphomonoesterase
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inositol-1,4,5-trisphosphate/1,3,4,5-tetrakisphosphate 5-phosphatase
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INPP5K
Ins(1,4,5)P3 5-phosphatase
Ins(1,4,5)P3/Ins(1,3,4,5)P4 5-phosphatase
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L-myo-inositol 1,4,5-trisphosphate-monoesterase
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Le5PT1
Le5PT2
myo-inositol-1,4,5-trisphosphate 5-phosphatase
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phosphatase, inosine tri-5PTASE
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protein-tyrosine phosphatase
PTP
SHIP2
Siw14
SKIP
type I inositol-1,4,5-trisphosphate 5-phosphatase
tyrosine-protein phosphatase
additional information
inositol 1,4,5-trisphosphate 5-phosphatase
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Ins(1,4,5)P3 5-phosphatase
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additional information
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the enzyme belongs to the type I 5-phosphatase family, cf. EC 3.1.3.36, phosphoinositide 5-phosphatase
additional information
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cf. EC 3.1.3.36, phosphoinositide 5-phosphatase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O = 1D-myo-inositol 1,3,4-trisphosphate + phosphate
D-myo-inositol 1,4,5-trisphosphate + H2O = myo-inositol 1,4-bisphosphate + phosphate
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1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O = 1D-myo-inositol 1,3,4-trisphosphate + phosphate
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1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O = 1D-myo-inositol 1,3,4-trisphosphate + phosphate
catalytic and kinetic reaction mechanism, substrate binding, overview
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1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O = 1D-myo-inositol 1,3,4-trisphosphate + phosphate
catalytic and kinetic reaction mechanism, substrate binding, overview
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
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PATHWAY SOURCE
PATHWAYS
MetaCyc
1D-myo-inositol hexakisphosphate biosynthesis II (mammalian), D-myo-inositol (1,3,4)-trisphosphate biosynthesis, D-myo-inositol (1,4,5)-trisphosphate degradation
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SYSTEMATIC NAME
IUBMB Comments
1D-myo-inositol-1,4,5-trisphosphate 5-phosphohydrolase
One mammalian isoform is known. This enzyme is distinguished from the family of enzymes classified under EC 3.1.3.36, phosphoinositide 5-phosphatase, by its inability to dephosphorylate inositol lipids.
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CAS REGISTRY NUMBER
COMMENTARY
106283-14-1
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9082-57-9
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1,5-bisdiphosphoinositol 2,3,4,6-tetrakisphosphate + H2O
1-diphosphoinositol 2,3,4,6-tetrakisphosphate + phosphate
1-(3-sn-phosphatidyl)-L-myo-inositol 4,5-bisphosphate + H2O
phosphatidylinositol 4-phosphate + phosphate
1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate + phosphate
1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 3-phosphate + phosphate
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate
1D-myo-inositol 1,2,3,4,5-pentakisphosphate + H2O
1D-myo-inositol 1,2,3,4-tetrakisphosphate + phosphate
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Substrates: preferred substrate
Products: -
Products: -
?
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + H2O
1D-myo-inositol 1,2,4,6-tetrakisphosphate + phosphate
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Substrates: -
Products: -
Products: -
?
1D-myo-inositol 1,2,4,5-tetrakisphosphate + H2O
1D-myo-inositol 1,2,4-trisphosphate + phosphate
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Substrates: -
Products: -
Products: -
?
1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O
1D-myo-inositol 1,3,4-trisphosphate + phosphate
1D-myo-inositol 1,4,5,6-tetrakisphosphate + H2O
1D-myo-inositol 1,4,6-trisphosphate + phosphate
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Substrates: -
Products: -
Products: -
?
1D-myo-inositol 1,4,5-trisphosphate + H2O
1D-myo-inositol 1,4-disphosphate + phosphate
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Substrates: -
Products: -
Products: -
?
1D-myo-inositol 1,4,5-trisphosphate + H2O
myo-inositol 1,4-bisphosphate + phosphate
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Substrates: -
Products: -
Products: -
?
1D-myo-inositol 2,4,5,6-tetrakisphosphate + H2O
1D-myo-inositol 2,4,6-trisphosphate + phosphate
1D-myo-inositol 2,4,5-trisphosphate + H2O
1D-myo-inositol 2,4-bisphosphate + phosphate
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Substrates: preferred substrate
Products: -
Products: -
?
1D-myo-inositol 3,4,5-trisphosphate + H2O
1D-myo-inositol 3,4-bisphosphate + phosphate
Substrates: -
Products: -
Products: -
?
1D-myo-inositol 3,5-bisphosphate + H2O
1D-myo-inositol 3-phosphate + phosphate
Substrates: -
Products: -
Products: -
?
1D-myo-inositol 4,5,6-trisphosphate + H2O
1D-myo-inositol 4,6-bisphosphate + phosphate
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Substrates: -
Products: -
Products: -
?
3-hydroxybenzene 1,2,4-trisphosphate + H2O
2,3-dihydroxybenzene 1,4-bisphosphate + phosphate
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Substrates: this is the first example of its kind to illustrate that an unnatural aromatic polyphosphorylated molecule can be specifically dephosphorylated by type I Ins(1,4,5)P3 5-phosphatase. No reaction with benzene 1,2,4-trisphosphate
Products: -
Products: -
?
3-O-methylfluorescein phosphate + H2O
3-O-methylfluorescein + phosphate
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Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
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Substrates: -
Products: -
Products: -
?
5-diphosphoinositol 1,2,3,4,6-pentakisphosphate + H2O
myo-inositol hexakisphosphate + phosphate
5-diphosphoinositol 1,3,4,6-tetrakisphosphate + H2O
inositol-1,3,4,5,6-pentakisphosphate + phosphate
6-diphosphoinositol 1,2,3,4,5-pentakisphosphate + H2O
?
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Substrates: low activity
Products: -
Products: -
?
7-methyl-6-thioguanosine + H2O
7-methyl-6-thioguanine + ribose 1-phosphate
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Substrates: spectrophotometric continous coupled enzyme assay substrate
Products: -
Products: -
?
D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O
D-myo-inositol 1,3,4-trisphosphate + phosphate
D-myo-inositol 1,4,5,6-tetrakisphosphate + H2O
D-myo-inositol 1,4,6-trisphosphate + phosphate
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Substrates: poor substrate
Products: -
Products: -
?
D-myo-inositol 1,4,5-trisphosphate + H2O
myo-inositol 1,4-bisphosphate + phosphate
Substrates: -
Products: -
Products: -
?
glycerophosphoinositol 4,5-bisphosphate + H2O
glycerophosphoinositol 4-phosphate + phosphate
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Substrates: at 13% of the rate of inositol 1,4,5-trisphosphate hydrolysis
Products: -
Products: -
?
inositol 1,2-cyclic 4,5-trisphosphate + H2O
?
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Substrates: poor substrate
Products: -
Products: -
?
inositol 4,5-bisphosphate + H2O
inositol 4-phosphate + phosphate
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Substrates: -
Products: -
Products: -
?
phosphatidyl-L-myo-inositol 3,4,5-trisphosphate + H2O
phosphatidylinositol 3,4-bisphosphate + phosphate
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Substrates: -
Products: -
Products: -
?
1,5-bisdiphosphoinositol 2,3,4,6-tetrakisphosphate + H2O
1-diphosphoinositol 2,3,4,6-tetrakisphosphate + phosphate
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Substrates: moderate activity
Products: -
Products: -
?
1,5-bisdiphosphoinositol 2,3,4,6-tetrakisphosphate + H2O
1-diphosphoinositol 2,3,4,6-tetrakisphosphate + phosphate
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Substrates: moderate activity
Products: -
Products: -
?
1-(3-sn-phosphatidyl)-L-myo-inositol 4,5-bisphosphate + H2O
phosphatidylinositol 4-phosphate + phosphate
Substrates: -
Products: -
Products: -
?
1-(3-sn-phosphatidyl)-L-myo-inositol 4,5-bisphosphate + H2O
phosphatidylinositol 4-phosphate + phosphate
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Substrates: -
Products: -
Products: -
?
1-(3-sn-phosphatidyl)-L-myo-inositol 4,5-bisphosphate + H2O
phosphatidylinositol 4-phosphate + phosphate
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Substrates: -
Products: -
Products: -
?
1-(3-sn-phosphatidyl)-L-myo-inositol 4,5-bisphosphate + H2O
phosphatidylinositol 4-phosphate + phosphate
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Substrates: regulation of the 1-(3-sn-phosphatidyl)-L-myo-inositol 4,5-bisphosphate level at membrane ruffels
Products: -
Products: -
?
1-(3-sn-phosphatidyl)-L-myo-inositol 4,5-bisphosphate + H2O
phosphatidylinositol 4-phosphate + phosphate
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Substrates: -
Products: -
Products: -
?
1-(3-sn-phosphatidyl)-L-myo-inositol 4,5-bisphosphate + H2O
phosphatidylinositol 4-phosphate + phosphate
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Substrates: -
Products: -
Products: -
?
1-diphosphoinositol 2,3,4,5,6-pentakisphosphate + H2O
?
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Substrates: low activity
Products: -
Products: -
?
1-diphosphoinositol 2,3,4,5,6-pentakisphosphate + H2O
?
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Substrates: low activity
Products: -
Products: -
?
1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate + phosphate
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Substrates: -
Products: -
Products: -
?
1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 3-phosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 3-phosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O
1D-myo-inositol 1,3,4-trisphosphate + phosphate
Substrates: -
Products: -
Products: -
?
1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O
1D-myo-inositol 1,3,4-trisphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O
1D-myo-inositol 1,3,4-trisphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O
1D-myo-inositol 1,3,4-trisphosphate + phosphate
Substrates: -
Products: -
Products: -
?
1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O
1D-myo-inositol 1,3,4-trisphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
1D-myo-inositol 1,4,5-trisphosphate + H2O
1D-myo-inositol 1,4-bisphosphate + phosphate
Substrates: specific for
Products: -
Products: -
?
1D-myo-inositol 1,4,5-trisphosphate + H2O
1D-myo-inositol 1,4-bisphosphate + phosphate
Substrates: absolutely specific for
Products: -
Products: -
?
1D-myo-inositol 1,4,5-trisphosphate + H2O
1D-myo-inositol 1,4-bisphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
1D-myo-inositol 1,4,5-trisphosphate + H2O
1D-myo-inositol 1,4-bisphosphate + phosphate
Substrates: -
Products: -
Products: -
?
1D-myo-inositol 1,4,5-trisphosphate + H2O
1D-myo-inositol 1,4-bisphosphate + phosphate
-
Substrates: 1D-myo-inositol 1,4,5-trisphosphate metabolism, regulation, overview
Products: -
Products: -
?
1D-myo-inositol 1,4,5-trisphosphate + H2O
1D-myo-inositol 1,4-bisphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
1D-myo-inositol 1,4,5-trisphosphate + H2O
1D-myo-inositol 1,4-bisphosphate + phosphate
Substrates: specific for
Products: -
Products: -
?
1D-myo-inositol 1,4,5-trisphosphate + H2O
1D-myo-inositol 1,4-bisphosphate + phosphate
-
Substrates: the enzyme is involved in Ins(1,4,5)P3-mediated Ca2+ signaling associated to PRIP-1, a Ins(1,4,5)P3-binding protein, overview
Products: -
Products: -
?
1D-myo-inositol 1,4,5-trisphosphate + H2O
1D-myo-inositol 1,4-bisphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
1D-myo-inositol 1,4,5-trisphosphate + H2O
1D-myo-inositol 1,4-bisphosphate + phosphate
-
Substrates: the enzyme is involved in the metabolism of polyphosphoinisotide in cellular signalling
Products: -
Products: -
?
1D-myo-inositol 1,4,5-trisphosphate + H2O
1D-myo-inositol 1,4-bisphosphate + phosphate
-
Substrates: recombinant purified enzyme expressed in Escherichia coli
Products: -
Products: -
?
1D-myo-inositol 1,4,5-trisphosphate + H2O
1D-myo-inositol 1,4-bisphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
1D-myo-inositol 2,4,5,6-tetrakisphosphate + H2O
1D-myo-inositol 2,4,6-trisphosphate + phosphate
-
Substrates: low activity
Products: -
Products: -
?
1D-myo-inositol 2,4,5,6-tetrakisphosphate + H2O
1D-myo-inositol 2,4,6-trisphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
4-diphosphoinositol 1,2,3,5,6-pentakisphosphate + H2O
?
-
Substrates: low activity
Products: -
Products: -
?
4-diphosphoinositol 1,2,3,5,6-pentakisphosphate + H2O
?
-
Substrates: low activity
Products: -
Products: -
?
5-diphosphoinositol 1,2,3,4,6-pentakisphosphate + H2O
myo-inositol hexakisphosphate + phosphate
-
Substrates: best substrate
Products: -
Products: -
?
5-diphosphoinositol 1,2,3,4,6-pentakisphosphate + H2O
myo-inositol hexakisphosphate + phosphate
-
Substrates: best substrate
Products: -
Products: -
?
5-diphosphoinositol 1,3,4,6-tetrakisphosphate + H2O
inositol-1,3,4,5,6-pentakisphosphate + phosphate
-
Substrates: moderate to low activity
Products: -
Products: -
?
5-diphosphoinositol 1,3,4,6-tetrakisphosphate + H2O
inositol-1,3,4,5,6-pentakisphosphate + phosphate
-
Substrates: moderate to low activity
Products: -
Products: -
?
D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O
D-myo-inositol 1,3,4-trisphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O
D-myo-inositol 1,3,4-trisphosphate + phosphate
-
Substrates: substrate for type I but not type II enzyme
Products: -
Products: -
?
D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O
D-myo-inositol 1,3,4-trisphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O
D-myo-inositol 1,3,4-trisphosphate + phosphate
-
Substrates: product is precursor for inositol 1,3,4,5,6-pentiskphosphate via inositol 1,3,4,6-tetraiskphosphate
Products: -
Products: -
?
D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O
D-myo-inositol 1,3,4-trisphosphate + phosphate
Substrates: -
Products: -
Products: -
?
D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O
D-myo-inositol 1,3,4-trisphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O
D-myo-inositol 1,3,4-trisphosphate + phosphate
-
Substrates: very poor substrate
Products: -
Products: -
?
D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O
D-myo-inositol 1,3,4-trisphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O
D-myo-inositol 1,3,4-trisphosphate + phosphate
-
Substrates: product is precursor for inositol 1,3,4,5,6-pentiskphosphate via inositol 1,3,4,6-tetraiskphosphate
Products: -
Products: -
?
D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O
D-myo-inositol 1,3,4-trisphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O
D-myo-inositol 1,3,4-trisphosphate + phosphate
-
Substrates: substrate for type I but not type II enzyme
Products: -
Products: -
?
D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O
D-myo-inositol 1,3,4-trisphosphate + phosphate
-
Substrates: at 8% of the rate of inositol 1,4,5-trisphosphate hydrolysis
Products: -
Products: -
?
D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O
D-myo-inositol 1,3,4-trisphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O
D-myo-inositol 1,3,4-trisphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O
D-myo-inositol 1,3,4-trisphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O
D-myo-inositol 1,3,4-trisphosphate + phosphate
-
Substrates: type I and type II enzyme
Products: -
Products: -
?
D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O
D-myo-inositol 1,3,4-trisphosphate + phosphate
-
Substrates: product is precursor for inositol 1,3,4,5,6-pentiskphosphate via inositol 1,3,4,6-tetraiskphosphate
Products: -
Products: -
?
D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O
D-myo-inositol 1,3,4-trisphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
D-myo-inositol 1,4,5-trisphosphate + H2O
D-myo-inositol 1,4-bisphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
D-myo-inositol 1,4,5-trisphosphate + H2O
D-myo-inositol 1,4-bisphosphate + phosphate
-
Substrates: regulation of intracellular Ca2+ level by degradation of intracellular Ca2+ releasing second messenger D-myo-inositol 1,4,5-trisphosphate
Products: -
Products: -
?
D-myo-inositol 1,4,5-trisphosphate + H2O
D-myo-inositol 1,4-bisphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
D-myo-inositol 1,4,5-trisphosphate + H2O
D-myo-inositol 1,4-bisphosphate + phosphate
-
Substrates: regulation of intracellular Ca2+ level by degradation of intracellular Ca2+ releasing second messenger D-myo-inositol 1,4,5-trisphosphate
Products: -
Products: -
?
D-myo-inositol 1,4,5-trisphosphate + H2O
D-myo-inositol 1,4-bisphosphate + phosphate
Substrates: -
Products: -
Products: -
?
D-myo-inositol 1,4,5-trisphosphate + H2O
D-myo-inositol 1,4-bisphosphate + phosphate
Substrates: regulation of intracellular Ca2+ level by degradation of intracellular Ca2+ releasing second messenger D-myo-inositol 1,4,5-trisphosphate
Products: -
Products: -
?
D-myo-inositol 1,4,5-trisphosphate + H2O
D-myo-inositol 1,4-bisphosphate + phosphate
Frog
-
Substrates: -
Products: -
Products: -
?
D-myo-inositol 1,4,5-trisphosphate + H2O
D-myo-inositol 1,4-bisphosphate + phosphate
Frog
-
Substrates: regulation of intracellular Ca2+ level by degradation of intracellular Ca2+ releasing second messenger D-myo-inositol 1,4,5-trisphosphate
Products: -
Products: -
?
D-myo-inositol 1,4,5-trisphosphate + H2O
D-myo-inositol 1,4-bisphosphate + phosphate
-
646372, 646377, 646379, 646382, 646385, 646389, 646392, 646393, 646395, 646396, 646397, 646398, 646403
Substrates: -
Products: -
Products: -
?
D-myo-inositol 1,4,5-trisphosphate + H2O
D-myo-inositol 1,4-bisphosphate + phosphate
-
Substrates: regulation of intracellular Ca2+ level by degradation of intracellular Ca2+ releasing second messenger D-myo-inositol 1,4,5-trisphosphate
Products: -
Products: -
?
D-myo-inositol 1,4,5-trisphosphate + H2O
D-myo-inositol 1,4-bisphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
D-myo-inositol 1,4,5-trisphosphate + H2O
D-myo-inositol 1,4-bisphosphate + phosphate
-
Substrates: regulation of intracellular Ca2+ level by degradation of intracellular Ca2+ releasing second messenger D-myo-inositol 1,4,5-trisphosphate
Products: -
Products: -
?
D-myo-inositol 1,4,5-trisphosphate + H2O
D-myo-inositol 1,4-bisphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
D-myo-inositol 1,4,5-trisphosphate + H2O
D-myo-inositol 1,4-bisphosphate + phosphate
-
Substrates: involved in regulation of excitation-contraction coupling in skeletal muscle
Products: -
Products: -
?
D-myo-inositol 1,4,5-trisphosphate + H2O
D-myo-inositol 1,4-bisphosphate + phosphate
-
Substrates: regulation of intracellular Ca2+ level by degradation of intracellular Ca2+ releasing second messenger D-myo-inositol 1,4,5-trisphosphate
Products: -
Products: -
?
D-myo-inositol 1,4,5-trisphosphate + H2O
D-myo-inositol 1,4-bisphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
D-myo-inositol 1,4,5-trisphosphate + H2O
D-myo-inositol 1,4-bisphosphate + phosphate
-
Substrates: regulation of intracellular Ca2+ level by degradation of intracellular Ca2+ releasing second messenger D-myo-inositol 1,4,5-trisphosphate
Products: -
Products: -
?
D-myo-inositol 1,4,5-trisphosphate + H2O
D-myo-inositol 1,4-bisphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
D-myo-inositol 1,4,5-trisphosphate + H2O
D-myo-inositol 1,4-bisphosphate + phosphate
-
Substrates: regulation of intracellular Ca2+ level by degradation of intracellular Ca2+ releasing second messenger D-myo-inositol 1,4,5-trisphosphate
Products: -
Products: -
?
D-myo-inositol 1,4,5-trisphosphate + H2O
D-myo-inositol 1,4-bisphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
D-myo-inositol 1,4,5-trisphosphate + H2O
D-myo-inositol 1,4-bisphosphate + phosphate
-
Substrates: regulation of intracellular Ca2+ level by degradation of intracellular Ca2+ releasing second messenger D-myo-inositol 1,4,5-trisphosphate
Products: -
Products: -
?
D-myo-inositol 1,4,5-trisphosphate + H2O
D-myo-inositol 1,4-bisphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
D-myo-inositol 1,4,5-trisphosphate + H2O
D-myo-inositol 1,4-bisphosphate + phosphate
-
Substrates: regulation of intracellular Ca2+ level by degradation of intracellular Ca2+ releasing second messenger D-myo-inositol 1,4,5-trisphosphate
Products: -
Products: -
?
D-myo-inositol 1,4,5-trisphosphate + H2O
D-myo-inositol 1,4-bisphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
D-myo-inositol 1,4,5-trisphosphate + H2O
D-myo-inositol 1,4-bisphosphate + phosphate
-
Substrates: involved in regulation of excitation-contraction coupling in skeletal muscle
Products: -
Products: -
?
D-myo-inositol 1,4,5-trisphosphate + H2O
D-myo-inositol 1,4-bisphosphate + phosphate
-
Substrates: regulation of intracellular Ca2+ level by degradation of intracellular Ca2+ releasing second messenger D-myo-inositol 1,4,5-trisphosphate
Products: -
Products: -
?
D-myo-inositol 1,4,5-trisphosphate + H2O
D-myo-inositol 1,4-bisphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
D-myo-inositol 1,4,5-trisphosphate + H2O
D-myo-inositol 1,4-bisphosphate + phosphate
-
Substrates: regulation of intracellular Ca2+ level by degradation of intracellular Ca2+ releasing second messenger D-myo-inositol 1,4,5-trisphosphate
Products: -
Products: -
?
additional information
?
-
Substrates: substrate specificity, no activity with 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate, 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate, 1D-myo-inositol 1,3,4,5-tetrakisphosphate, 1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate, 1-phosphatidyl-1D-myo-inositol 5-phosphate, 1-phosphatidyl-1D-myo-inositol 4-phosphate, and 1-phosphatidyl-1D-myo-inositol 3-phosphate
Products: -
Products: -
?
additional information
?
-
Substrates: substrate specificity, no activity with 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate, 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate, 1D-myo-inositol 1,3,4,5-tetrakisphosphate, 1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate, 1-phosphatidyl-1D-myo-inositol 5-phosphate, 1-phosphatidyl-1D-myo-inositol 4-phosphate, and 1-phosphatidyl-1D-myo-inositol 3-phosphate
Products: -
Products: -
?
additional information
?
-
-
Substrates: D-6-deoxy-myo-inositol 1,3,4,5-tetrakisphosphate are not hydrolyzed
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme knockout results in decrease in nucleocytoplasmic inositol phosphate 6-/3-kinases Ipk2/Ipk1-dependent inositol hexakisphosphate synthesis, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: glycerophosphoinositol 4-phosphate and inositol 1,4-bisphosphate are not hydrolyzed
Products: -
Products: -
?
additional information
?
-
-
Substrates: glycerophosphoinositol 4,5-bisphosphate is not hydrolyzed
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme has multiple roles in cellular signalling and may regulate distinct pathways
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate specificity, no activity with 1D-myo-inositol 1,4,5-trisphosphate, 1-phosphatidyl-1D-myo-inositol 5-phosphate, 1D-myo-inositol 1,5-bisphosphate, and 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme only binds soluble inositol polyphosphates
Products: -
Products: -
?
additional information
?
-
Substrates: isofom SHIP2 is unable to dephosphorylate 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme binds to PRIP-1, a Ins(1,4,5)P3-binding protein, via the protein's PH-domain, which inhibits the enzyme activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme shows high activity and exquisite specificity for the 5-diphosphate group of inositol diphosphates (5-PP-InsP), substrate-binding pocket structure analysis, overview. No activity with inositol hexakisphosphate, poor activity with 2-diphosphoinositol 1,3,4,5,6-pentakisphosphate and 3-diphosphoinositol 1,2,4,5,6-pentakisphosphate. Enzyme Siw14 also acts as protein tyrosine phosphatase, EC 3.1.3.48
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme has multiple roles in cellular signalling and may regulate distinct pathways
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate specificity, no activity with 1-phosphatidyl-1D-myo-inositol 5-phosphate, 1D-myo-inositol 1,5-bisphosphate, 1D-myo-inositol 1,3,5-trisphosphate, and with alpha-D-glucose 1-phosphate, D-glucose 6-phosphate, and alpha-D,L-glycerophosphate, overview
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1-(3-sn-phosphatidyl)-L-myo-inositol 4,5-bisphosphate + H2O
phosphatidylinositol 4-phosphate + phosphate
1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O
1D-myo-inositol 1,3,4-trisphosphate + phosphate
1D-myo-inositol 1,4,5-trisphosphate + H2O
myo-inositol 1,4-bisphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
1D-myo-inositol 3,4,5-trisphosphate + H2O
1D-myo-inositol 3,4-bisphosphate + phosphate
Substrates: -
Products: -
Products: -
?
1D-myo-inositol 3,5-bisphosphate + H2O
1D-myo-inositol 3-phosphate + phosphate
Substrates: -
Products: -
Products: -
?
D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O
D-myo-inositol 1,3,4-trisphosphate + phosphate
inositol 4,5-bisphosphate + H2O
inositol 4-phosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
1-(3-sn-phosphatidyl)-L-myo-inositol 4,5-bisphosphate + H2O
phosphatidylinositol 4-phosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
1-(3-sn-phosphatidyl)-L-myo-inositol 4,5-bisphosphate + H2O
phosphatidylinositol 4-phosphate + phosphate
-
Substrates: regulation of the 1-(3-sn-phosphatidyl)-L-myo-inositol 4,5-bisphosphate level at membrane ruffels
Products: -
Products: -
?
1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O
1D-myo-inositol 1,3,4-trisphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O
1D-myo-inositol 1,3,4-trisphosphate + phosphate
Substrates: -
Products: -
Products: -
?
1D-myo-inositol 1,4,5-trisphosphate + H2O
1D-myo-inositol 1,4-bisphosphate + phosphate
Substrates: specific for
Products: -
Products: -
?
1D-myo-inositol 1,4,5-trisphosphate + H2O
1D-myo-inositol 1,4-bisphosphate + phosphate
-
Substrates: 1D-myo-inositol 1,4,5-trisphosphate metabolism, regulation, overview
Products: -
Products: -
?
1D-myo-inositol 1,4,5-trisphosphate + H2O
1D-myo-inositol 1,4-bisphosphate + phosphate
Substrates: specific for
Products: -
Products: -
?
1D-myo-inositol 1,4,5-trisphosphate + H2O
1D-myo-inositol 1,4-bisphosphate + phosphate
-
Substrates: the enzyme is involved in Ins(1,4,5)P3-mediated Ca2+ signaling associated to PRIP-1, a Ins(1,4,5)P3-binding protein, overview
Products: -
Products: -
?
1D-myo-inositol 1,4,5-trisphosphate + H2O
1D-myo-inositol 1,4-bisphosphate + phosphate
-
Substrates: the enzyme is involved in the metabolism of polyphosphoinisotide in cellular signalling
Products: -
Products: -
?
D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O
D-myo-inositol 1,3,4-trisphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O
D-myo-inositol 1,3,4-trisphosphate + phosphate
-
Substrates: product is precursor for inositol 1,3,4,5,6-pentiskphosphate via inositol 1,3,4,6-tetraiskphosphate
Products: -
Products: -
?
D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O
D-myo-inositol 1,3,4-trisphosphate + phosphate
Substrates: -
Products: -
Products: -
?
D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O
D-myo-inositol 1,3,4-trisphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O
D-myo-inositol 1,3,4-trisphosphate + phosphate
-
Substrates: product is precursor for inositol 1,3,4,5,6-pentiskphosphate via inositol 1,3,4,6-tetraiskphosphate
Products: -
Products: -
?
D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O
D-myo-inositol 1,3,4-trisphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O
D-myo-inositol 1,3,4-trisphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O
D-myo-inositol 1,3,4-trisphosphate + phosphate
-
Substrates: product is precursor for inositol 1,3,4,5,6-pentiskphosphate via inositol 1,3,4,6-tetraiskphosphate
Products: -
Products: -
?
D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O
D-myo-inositol 1,3,4-trisphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
D-myo-inositol 1,4,5-trisphosphate + H2O
D-myo-inositol 1,4-bisphosphate + phosphate
-
Substrates: regulation of intracellular Ca2+ level by degradation of intracellular Ca2+ releasing second messenger D-myo-inositol 1,4,5-trisphosphate
Products: -
Products: -
?
D-myo-inositol 1,4,5-trisphosphate + H2O
D-myo-inositol 1,4-bisphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
D-myo-inositol 1,4,5-trisphosphate + H2O
D-myo-inositol 1,4-bisphosphate + phosphate
-
Substrates: regulation of intracellular Ca2+ level by degradation of intracellular Ca2+ releasing second messenger D-myo-inositol 1,4,5-trisphosphate
Products: -
Products: -
?
D-myo-inositol 1,4,5-trisphosphate + H2O
D-myo-inositol 1,4-bisphosphate + phosphate
Substrates: regulation of intracellular Ca2+ level by degradation of intracellular Ca2+ releasing second messenger D-myo-inositol 1,4,5-trisphosphate
Products: -
Products: -
?
D-myo-inositol 1,4,5-trisphosphate + H2O
D-myo-inositol 1,4-bisphosphate + phosphate
Frog
-
Substrates: regulation of intracellular Ca2+ level by degradation of intracellular Ca2+ releasing second messenger D-myo-inositol 1,4,5-trisphosphate
Products: -
Products: -
?
D-myo-inositol 1,4,5-trisphosphate + H2O
D-myo-inositol 1,4-bisphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
D-myo-inositol 1,4,5-trisphosphate + H2O
D-myo-inositol 1,4-bisphosphate + phosphate
-
Substrates: regulation of intracellular Ca2+ level by degradation of intracellular Ca2+ releasing second messenger D-myo-inositol 1,4,5-trisphosphate
Products: -
Products: -
?
D-myo-inositol 1,4,5-trisphosphate + H2O
D-myo-inositol 1,4-bisphosphate + phosphate
-
Substrates: regulation of intracellular Ca2+ level by degradation of intracellular Ca2+ releasing second messenger D-myo-inositol 1,4,5-trisphosphate
Products: -
Products: -
?
D-myo-inositol 1,4,5-trisphosphate + H2O
D-myo-inositol 1,4-bisphosphate + phosphate
-
Substrates: involved in regulation of excitation-contraction coupling in skeletal muscle
Products: -
Products: -
?
D-myo-inositol 1,4,5-trisphosphate + H2O
D-myo-inositol 1,4-bisphosphate + phosphate
-
Substrates: regulation of intracellular Ca2+ level by degradation of intracellular Ca2+ releasing second messenger D-myo-inositol 1,4,5-trisphosphate
Products: -
Products: -
?
D-myo-inositol 1,4,5-trisphosphate + H2O
D-myo-inositol 1,4-bisphosphate + phosphate
-
Substrates: regulation of intracellular Ca2+ level by degradation of intracellular Ca2+ releasing second messenger D-myo-inositol 1,4,5-trisphosphate
Products: -
Products: -
?
D-myo-inositol 1,4,5-trisphosphate + H2O
D-myo-inositol 1,4-bisphosphate + phosphate
-
Substrates: regulation of intracellular Ca2+ level by degradation of intracellular Ca2+ releasing second messenger D-myo-inositol 1,4,5-trisphosphate
Products: -
Products: -
?
D-myo-inositol 1,4,5-trisphosphate + H2O
D-myo-inositol 1,4-bisphosphate + phosphate
-
Substrates: regulation of intracellular Ca2+ level by degradation of intracellular Ca2+ releasing second messenger D-myo-inositol 1,4,5-trisphosphate
Products: -
Products: -
?
D-myo-inositol 1,4,5-trisphosphate + H2O
D-myo-inositol 1,4-bisphosphate + phosphate
-
Substrates: regulation of intracellular Ca2+ level by degradation of intracellular Ca2+ releasing second messenger D-myo-inositol 1,4,5-trisphosphate
Products: -
Products: -
?
D-myo-inositol 1,4,5-trisphosphate + H2O
D-myo-inositol 1,4-bisphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
D-myo-inositol 1,4,5-trisphosphate + H2O
D-myo-inositol 1,4-bisphosphate + phosphate
-
Substrates: involved in regulation of excitation-contraction coupling in skeletal muscle
Products: -
Products: -
?
D-myo-inositol 1,4,5-trisphosphate + H2O
D-myo-inositol 1,4-bisphosphate + phosphate
-
Substrates: regulation of intracellular Ca2+ level by degradation of intracellular Ca2+ releasing second messenger D-myo-inositol 1,4,5-trisphosphate
Products: -
Products: -
?
D-myo-inositol 1,4,5-trisphosphate + H2O
D-myo-inositol 1,4-bisphosphate + phosphate
-
Substrates: regulation of intracellular Ca2+ level by degradation of intracellular Ca2+ releasing second messenger D-myo-inositol 1,4,5-trisphosphate
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme knockout results in decrease in nucleocytoplasmic inositol phosphate 6-/3-kinases Ipk2/Ipk1-dependent inositol hexakisphosphate synthesis, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme has multiple roles in cellular signalling and may regulate distinct pathways
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme only binds soluble inositol polyphosphates
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme has multiple roles in cellular signalling and may regulate distinct pathways
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Co2+
-
activates, competitive binding to other metal ions, KM 0.0145 mM and turnover number 7.28 s-1 at pH 7.0, 30°C, recombinant enzyme
Mg2+
Mn2+
Ni2+
-
activates, competitive binding to other metal ions, KM 0.0064 mM and turnover number 5.48 s-1 at pH 7.0, 30°C, recombinant enzyme
Mg2+
-
required, optimal at 2 mM, existence of a second inhibitory metal binding site, competitive binding to other metal ions, KM 0.53 mM and turnover number 9.64 s-1 at pH 7.0, 30°C, recombinant enzyme
Mn2+
-
activates, competitive binding to other metal ions, KM 0.012 mM and turnover number 7.48 s-1 at pH 7.0, 30°C, recombinant enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Glycerophosphoinositol 4,5-bisphosphate
-
competitive with D-myo-inositol 1,4,5-trisphosphate
Phenylglyoxal
-
Arg-343 and Arg-350 were found to be covalently modified; irreversible, substrates and 2,3-bisphosphoglycerate protect against inactivation
protein PRIP-1
-
binding to PRIP-1, a Ins(1,4,5)P3-binding protein, inhibits the enzyme in vitro, in vivo binding of Ins(1,4,5)P3 to PRIP-1 prevents it from being hydrolyzed by the enzyme, PRIP-1 has a domain organization similar to phospholipase C-delta1, interaction analysis, overview
-
additional information
-
inositol 1,4-bisphosphate does not inhibit enzyme activity
-
Inositol 1,3,4,5-tetrakisphosphate
-
competitive with D-myo-inositol 1,4,5-trisphosphate
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
wounding and abscisic acid induce the enzyme
-
additional information
wounding and abscisic acid induce the enzyme
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Alzheimer Disease
INPP5D rs35349669 polymorphism with late-onset Alzheimer's disease: A replication study and meta-analysis.
Astrocytoma
Identification of novel genetic alterations in samples of malignant glioma patients.
Ataxia
INPP5K and SIL1 associated pathologies with overlapping clinical phenotypes converge through dysregulation of PHGDH.
Breast Neoplasms
Polyphenolic extract of InsP 5-ptase expressing tomato plants reduce the proliferation of MCF-7 breast cancer cells.
Carcinoma
A distinct and replicable variant of the squamous cell carcinoma gene inositol polyphosphate-5-phosphatase modifies the susceptibility of arsenic-associated skin lesions in Bangladesh.
Carcinoma
Frequent loss of inositol polyphosphate-5-phosphatase in oropharyngeal squamous cell carcinoma.
Carcinoma
Prognostic Value of Inositol Polyphosphate-5-Phosphatase Expression in Recurrent and Metastatic Cutaneous Squamous Cell Carcinoma.
Carcinoma
Random DNA fragmentation allows detection of single-copy, single-exon alterations of copy number by oligonucleotide array CGH in clinical FFPE samples.
Carcinoma, Squamous Cell
A distinct and replicable variant of the squamous cell carcinoma gene inositol polyphosphate-5-phosphatase modifies the susceptibility of arsenic-associated skin lesions in Bangladesh.
Carcinoma, Squamous Cell
Prognostic Value of Inositol Polyphosphate-5-Phosphatase Expression in Recurrent and Metastatic Cutaneous Squamous Cell Carcinoma.
Carcinoma, Squamous Cell
Random DNA fragmentation allows detection of single-copy, single-exon alterations of copy number by oligonucleotide array CGH in clinical FFPE samples.
Cardiomegaly
Inpp5f Is a Polyphosphoinositide Phosphatase That Regulates Cardiac Hypertrophic Responsiveness.
Cataract
A Recurrent Pathogenic Variant of INPP5K Underlies Autosomal Recessive Congenital Muscular Dystrophy With Cataracts and Intellectual Disability: Evidence for a Founder Effect in Southern Italy.
Cataract
INPP5K and SIL1 associated pathologies with overlapping clinical phenotypes converge through dysregulation of PHGDH.
Cataract
INPP5K variant causes autosomal recessive congenital cataract in a Pakistani family.
Cataract
Mutations in INPP5K Cause a Form of Congenital Muscular Dystrophy Overlapping Marinesco-Sjögren Syndrome and Dystroglycanopathy.
Cataract
Mutations in INPP5K, Encoding a Phosphoinositide 5-Phosphatase, Cause Congenital Muscular Dystrophy with Cataracts and Mild Cognitive Impairment.
Cataract
The phosphoinositide 5-phosphatase INPP5K: From gene structure to in vivo functions.
Ciliopathies
Mutations in INPP5E, encoding inositol polyphosphate-5-phosphatase E, link phosphatidyl inositol signaling to the ciliopathies.
Dehydration
Inositol polyphosphate 5-phosphatase-controlled Ins(1,4,5)P3/Ca2+ is crucial for maintaining pollen dormancy and regulating early germination of pollen.
Glioblastoma
Identification of novel genetic alterations in samples of malignant glioma patients.
Glioma
Identification of novel genetic alterations in samples of malignant glioma patients.
Glioma
Inositol Polyphosphate-5-Phosphatase F (INPP5F) inhibits STAT3 activity and suppresses gliomas tumorigenicity.
inositol-polyphosphate 5-phosphatase deficiency
Inositol 1,4,5-trisphosphate phosphatase deficiency and malignant hyperpyrexia in swine.
Insulin Resistance
Phosphatidylinositol 3,4,5-Trisphosphate Phosphatase SKIP Links Endoplasmic Reticulum Stress in Skeletal Muscle to Insulin Resistance.
Intellectual Disability
A Recurrent Pathogenic Variant of INPP5K Underlies Autosomal Recessive Congenital Muscular Dystrophy With Cataracts and Intellectual Disability: Evidence for a Founder Effect in Southern Italy.
Intellectual Disability
INPP5K variant causes autosomal recessive congenital cataract in a Pakistani family.
Intellectual Disability
Mutations in INPP5K Cause a Form of Congenital Muscular Dystrophy Overlapping Marinesco-Sjögren Syndrome and Dystroglycanopathy.
Intellectual Disability
Mutations in INPP5K, Encoding a Phosphoinositide 5-Phosphatase, Cause Congenital Muscular Dystrophy with Cataracts and Mild Cognitive Impairment.
Intellectual Disability
The phosphoinositide 5-phosphatase INPP5K: From gene structure to in vivo functions.
Keratosis, Actinic
Loss of inositol polyphosphate 5-phosphatase is an early event in development of cutaneous squamous cell carcinoma.
Keratosis, Actinic
Prognostic Value of Inositol Polyphosphate-5-Phosphatase Expression in Recurrent and Metastatic Cutaneous Squamous Cell Carcinoma.
Keratosis, Actinic
The prognostic value of inositol polyphosphate 5-phosphatase in cutaneous squamous cell carcinoma.
Liver Neoplasms
The Prediction and Prognostic Significance of INPP5K Expression in Patients with Liver Cancer.
Microcephaly
Mutations in INPP5K Cause a Form of Congenital Muscular Dystrophy Overlapping Marinesco-Sjögren Syndrome and Dystroglycanopathy.
Microphthalmos
Mutations in INPP5K Cause a Form of Congenital Muscular Dystrophy Overlapping Marinesco-Sjögren Syndrome and Dystroglycanopathy.
Muscular Diseases
INPP5K and SIL1 associated pathologies with overlapping clinical phenotypes converge through dysregulation of PHGDH.
Muscular Dystrophies
A Recurrent Pathogenic Variant of INPP5K Underlies Autosomal Recessive Congenital Muscular Dystrophy With Cataracts and Intellectual Disability: Evidence for a Founder Effect in Southern Italy.
Muscular Dystrophies
Bidirectional interconversion between PtdIns4P and PtdIns(4,5)P2 is required for autophagic lysosome reformation and protection from skeletal muscle disease.
Muscular Dystrophies
Defective lysosome reformation during autophagy causes skeletal muscle disease.
Muscular Dystrophies
INPP5K variant causes autosomal recessive congenital cataract in a Pakistani family.
Muscular Dystrophies
Mutations in INPP5K Cause a Form of Congenital Muscular Dystrophy Overlapping Marinesco-Sjögren Syndrome and Dystroglycanopathy.
Muscular Dystrophies
Mutations in INPP5K, Encoding a Phosphoinositide 5-Phosphatase, Cause Congenital Muscular Dystrophy with Cataracts and Mild Cognitive Impairment.
Muscular Dystrophies
The phosphoinositide 5-phosphatase INPP5K: From gene structure to in vivo functions.
Neoplasm Metastasis
A new gene panel as a marker for ESCC poor prognosis; INPP5A, TWIST1, MMP2, and EGFR.
Neoplasm Metastasis
The prognostic value of inositol polyphosphate 5-phosphatase in cutaneous squamous cell carcinoma.
Neoplasms
A new gene panel as a marker for ESCC poor prognosis; INPP5A, TWIST1, MMP2, and EGFR.
Neoplasms
Analysis of an independent tumor suppressor locus telomeric to Tp53 suggested Inpp5k and Myo1c as novel tumor suppressor gene candidates in this region.
Neoplasms
Canine Mammary Tumours Are Affected by Frequent Copy Number Aberrations, including Amplification of MYC and Loss of PTEN.
Neoplasms
Loss of inositol polyphosphate 5-phosphatase is an early event in development of cutaneous squamous cell carcinoma.
Neoplasms
MiR-181a-5p Promotes Proliferation and Invasion, and Inhibits Apoptosis of Cervical Cancer Cells via Regulating Inositol Polyphosphate-5-Phosphatase A (INPP5A).
Neoplasms
MiR-661 contributed to cell proliferation of human ovarian cancer cells by repressing INPP5J expression.
Neoplasms
Phosphorylation-mediated PTEN conformational closure and deactivation revealed with protein semisynthesis.
Neoplasms
Prognostic Value of Inositol Polyphosphate-5-Phosphatase Expression in Recurrent and Metastatic Cutaneous Squamous Cell Carcinoma.
Neoplasms
Random DNA fragmentation allows detection of single-copy, single-exon alterations of copy number by oligonucleotide array CGH in clinical FFPE samples.
Neoplasms
SEREX identification of new tumour-associated antigens in cutaneous T-cell lymphoma.
Neoplasms
The phosphoinositide 5-phosphatase INPP5K: From gene structure to in vivo functions.
Neoplasms
The Prediction and Prognostic Significance of INPP5K Expression in Patients with Liver Cancer.
Neoplasms
The Prognostic Value of DNA Methylation, Post-Translational Modifications and Correlated with Immune Infiltrates in Gynecologic Cancers.
Neoplasms
The prognostic value of inositol polyphosphate 5-phosphatase in cutaneous squamous cell carcinoma.
Neural Tube Defects
Relationship Between INPP5E Gene Expression and Embryonic Neural Development in a Mouse Model of Neural Tube Defect.
Oculocerebrorenal Syndrome
A novel OCRL1 gene mutation in a Turkish child with Lowe syndrome.
Oculocerebrorenal Syndrome
A Novel OCRL1 Mutation in a Patient with the Mild Phenotype of Lowe Syndrome.
Oculocerebrorenal Syndrome
Decreased urinary excretion of the ectodomain form of megalin (A-megalin) in children with OCRL gene mutations.
Oculocerebrorenal Syndrome
The Lowe's oculocerebrorenal syndrome gene encodes a protein highly homologous to inositol polyphosphate-5-phosphatase.
Ovarian Neoplasms
MiR-661 contributed to cell proliferation of human ovarian cancer cells by repressing INPP5J expression.
Parkinson Disease
Association analysis of NUCKS1 and INPP5K polymorphism with Parkinson's disease.
Parkinson Disease
Parkinson's Disease Risk Variant rs1109303 Regulates the Expression of INPP5K and CRK in Human Brain.
phosphoinositide 5-phosphatase deficiency
The role of Arabidopsis 5PTase13 in root gravitropism through modulation of vesicle trafficking.
Spinocerebellar Ataxias
Cerebellum-enriched protein INPP5A contributes to selective neuropathology in mouse model of spinocerebellar ataxias type 17.
Squamous Cell Carcinoma of Head and Neck
Frequent loss of inositol polyphosphate-5-phosphatase in oropharyngeal squamous cell carcinoma.
Thymoma
Hdac2 regulates the cardiac hypertrophic response by modulating Gsk3 beta activity.
Uterine Cervical Neoplasms
MiR-181a-5p Promotes Proliferation and Invasion, and Inhibits Apoptosis of Cervical Cancer Cells via Regulating Inositol Polyphosphate-5-Phosphatase A (INPP5A).
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0101
1,5-bisdiphosphoinositol 2,3,4,6-tetrakisphosphate
-
pH 7.2, 30°C, wild-type enzyme Siw14
0.0568
5-diphosphoinositol 1,3,4,6-tetrakisphosphate
-
pH 7.2, 30°C, recombinant wild-type enzyme Siw14
0.007
5-diphosphoinositol 1,2,3,4,6-pentakisphosphate
-
pH 7.2, 30°C, Siw14 mutant N215A
0.0102
5-diphosphoinositol 1,2,3,4,6-pentakisphosphate
-
pH 7.2, 30°C, Siw14 mutant N183A
0.0104
5-diphosphoinositol 1,2,3,4,6-pentakisphosphate
-
pH 7.2, 30°C, wild-type enzyme Siw14
0.0116
5-diphosphoinositol 1,2,3,4,6-pentakisphosphate
-
pH 7.2, 30°C, recombinant truncated enzyme Siw14(116-281)
0.0122
5-diphosphoinositol 1,2,3,4,6-pentakisphosphate
-
pH 7.2, 30°C, Siw14 mutant E185A
0.0145
5-diphosphoinositol 1,2,3,4,6-pentakisphosphate
-
pH 7.2, 30°C, Siw14 mutant R216A
0.017
5-diphosphoinositol 1,2,3,4,6-pentakisphosphate
-
pH 7.2, 30°C, Siw14 mutant H219A
0.0286
5-diphosphoinositol 1,2,3,4,6-pentakisphosphate
-
pH 7.2, 30°C, Siw14 mutant K218A
0.0326
5-diphosphoinositol 1,2,3,4,6-pentakisphosphate
-
pH 7.2, 30°C, Siw14 mutant K250A
0.0471
5-diphosphoinositol 1,2,3,4,6-pentakisphosphate
-
pH 7.2, 30°C, Siw14 mutant K184A
0.0481
5-diphosphoinositol 1,2,3,4,6-pentakisphosphate
-
pH 7.2, 30°C, Siw14 mutant R252A
0.0008
D-myo-Inositol 1,3,4,5-tetrakisphosphate
-
type I enzyme, pH 7.1, 30°C
0.003
D-myo-Inositol 1,3,4,5-tetrakisphosphate
recombinant enzyme from E. coli
0.014
D-myo-inositol 1,4,5-trisphosphate
-
membrane associated enzyme, pH 7.2, 37°C
0.016 - 0.019
D-myo-inositol 1,4,5-trisphosphate
-
membrane bound enzyme, pH 7.2, 30°C
0.022
D-myo-inositol 1,4,5-trisphosphate
-
membrane associated enzyme, pH 7.2, 37°C
0.024
D-myo-inositol 1,4,5-trisphosphate
-
soluble enzyme, pH 7.2, 30°C
0.028
D-myo-inositol 1,4,5-trisphosphate
recombinant enzyme from E. coli
additional information
additional information
-
kinetics, substrate specificity, overview
-
additional information
additional information
-
kinetics, substrate specificity, overview
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.63
1,5-bisdiphosphoinositol 2,3,4,6-tetrakisphosphate
-
pH 7.2, 30°C, wild-type enzyme Siw14
0.77
5-diphosphoinositol 1,3,4,6-tetrakisphosphate
-
pH 7.2, 30°C, recombinant wild-type enzyme Siw14
0.21
5-diphosphoinositol 1,2,3,4,6-pentakisphosphate
-
pH 7.2, 30°C, Siw14 mutant K250A
0.29
5-diphosphoinositol 1,2,3,4,6-pentakisphosphate
-
pH 7.2, 30°C, Siw14 mutant N215A
0.35
5-diphosphoinositol 1,2,3,4,6-pentakisphosphate
-
pH 7.2, 30°C, Siw14 mutant R252A
0.38
5-diphosphoinositol 1,2,3,4,6-pentakisphosphate
-
pH 7.2, 30°C, Siw14 mutant H219A
0.46
5-diphosphoinositol 1,2,3,4,6-pentakisphosphate
-
pH 7.2, 30°C, Siw14 mutant K184A
0.48
5-diphosphoinositol 1,2,3,4,6-pentakisphosphate
-
pH 7.2, 30°C, Siw14 mutant K218A
0.57
5-diphosphoinositol 1,2,3,4,6-pentakisphosphate
-
pH 7.2, 30°C, Siw14 mutant N183A
0.8
5-diphosphoinositol 1,2,3,4,6-pentakisphosphate
-
pH 7.2, 30°C, Siw14 mutant E185A
1.26
5-diphosphoinositol 1,2,3,4,6-pentakisphosphate
-
pH 7.2, 30°C, Siw14 mutant R216A
1.31
5-diphosphoinositol 1,2,3,4,6-pentakisphosphate
-
pH 7.2, 30°C, wild-type enzyme Siw14
1.32
5-diphosphoinositol 1,2,3,4,6-pentakisphosphate
-
pH 7.2, 30°C, recombinant truncated enzyme Siw14(116-281)
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
62.38
1,5-bisdiphosphoinositol 2,3,4,6-tetrakisphosphate
-
pH 7.2, 30°C, wild-type enzyme Siw14
13.56
5-diphosphoinositol 1,3,4,6-tetrakisphosphate
-
pH 7.2, 30°C, recombinant wild-type enzyme Siw14
6.44
5-diphosphoinositol 1,2,3,4,6-pentakisphosphate
-
pH 7.2, 30°C, Siw14 mutant K250A
7.28
5-diphosphoinositol 1,2,3,4,6-pentakisphosphate
-
pH 7.2, 30°C, Siw14 mutant R252A
9.77
5-diphosphoinositol 1,2,3,4,6-pentakisphosphate
-
pH 7.2, 30°C, Siw14 mutant K184A
16.78
5-diphosphoinositol 1,2,3,4,6-pentakisphosphate
-
pH 7.2, 30°C, Siw14 mutant K218A
22.36
5-diphosphoinositol 1,2,3,4,6-pentakisphosphate
-
pH 7.2, 30°C, Siw14 mutant H219A
41.43
5-diphosphoinositol 1,2,3,4,6-pentakisphosphate
-
pH 7.2, 30°C, Siw14 mutant N215A
55.88
5-diphosphoinositol 1,2,3,4,6-pentakisphosphate
-
pH 7.2, 30°C, Siw14 mutant N183A
65.57
5-diphosphoinositol 1,2,3,4,6-pentakisphosphate
-
pH 7.2, 30°C, Siw14 mutant E185A
86.9
5-diphosphoinositol 1,2,3,4,6-pentakisphosphate
-
pH 7.2, 30°C, Siw14 mutant R216A
113.79
5-diphosphoinositol 1,2,3,4,6-pentakisphosphate
-
pH 7.2, 30°C, recombinant truncated enzyme Siw14(116-281)
125.96
5-diphosphoinositol 1,2,3,4,6-pentakisphosphate
-
pH 7.2, 30°C, wild-type enzyme Siw14
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.02
Inositol 1,3,4,5,6-pentakisphosphate
-
with inositol 1,4,5-trisphosphate as substrate
0.035
Inositol 1,3,4,5,6-pentakisphosphate
-
with inositol 1,3,4,5-tetrakisphosphate as substrate
0.015
Inositol hexakisphosphate
-
with inositol 1,3,4,5-tetrakisphosphate as substrate
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.021
2,3-dihydroxybenzene 1,4-bisphosphate
Homo sapiens
-
in the presence of 1 mM Ins-(1,4,5)P3 as substrate
0.068
3-benzyloxybenzene 1,2,4-trisphosphate
Homo sapiens
-
IC50 value is obtained in the presence of 1 microM D-myo-inositol 1,4,5-trisphosphate as substrate
0.021
3-hydroxybenzene 1,2,4-trisphosphate
Homo sapiens
-
IC50 value is obtained in the presence of 1 microM D-myo-inositol 1,4,5-trisphosphate as substrate
0.098
benzene 1,2,3,4-tetrakisphosphate
Homo sapiens
-
IC50 value is obtained in the presence of 1 microM D-myo-inositol 1,4,5-trisphosphate as substrate 6
0.078
benzene 1,2,3,5-tetrakisphosphate
Homo sapiens
-
IC50 value is obtained in the presence of 1 microM D-myo-inositol 1,4,5-trisphosphate as substrate 6
0.086
benzene 1,2,3-trisphosphate
Homo sapiens
-
IC50 value is obtained in the presence of 1 microM D-myo-inositol 1,4,5-trisphosphate as substrate
0.004
benzene 1,2,4,5-tetrakisphosphate
Homo sapiens
-
IC50 value is obtained in the presence of 1 microM D-myo-inositol 1,4,5-trisphosphate as substrate
0.016
benzene 1,3,5-trisphosphate
Homo sapiens
-
IC50 value is obtained in the presence of 1 microM D-myo-inositol 1,4,5-trisphosphate as substrate
0.001
biphenyl 2,3',4,5',6-pentakisphosphate
Homo sapiens
-
IC50 value is obtained in the presence of 1 microM D-myo-inositol 1,4,5-trisphosphate as substrate
additional information
benzene 1,2-bisphosphate
Homo sapiens
-
IC value is higher than 0.2 mM, IC50 value is obtained in the presence of 1 microM D-myo-inositol 1,4,5-trisphosphate as substrate
0.014
benzene 1,2,4-trisphosphate
Homo sapiens
-
in the presence of 1 mM Ins-(1,4,5)P3 as substrate
0.014
benzene 1,2,4-trisphosphate
Homo sapiens
-
potential mimic of D-myo-inositol 1,4,5-trisphosphate, IC50 value is obtained in the presence of 1 microM D-myo-inositol 1,4,5-trisphosphate as substrate
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
additional information
additional information
inositol 1,4,5-trisphosphate levels in transgenic Arabidopsis thaliana seedlings, roots and hypocotyls, expressing the recombinant enzyme
additional information
-
inositol 1,4,5-trisphosphate levels in transgenic Arabidopsis thaliana seedlings, roots and hypocotyls, expressing the recombinant enzyme
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 7.4
7.2
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 9
6.25 - 8.25
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
brenda
syncytia induced by nematode Heterodera schachtii
SwissProt
brenda
-
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
expression pattern, no expression in root
brenda
additional information
expression pattern, no expression in root
brenda
additional information
expression of At5pTase1 is weaker than At5Ptase2
brenda
additional information
expression of At5pTase1 is weaker than At5Ptase2
brenda
additional information
-
expression of At5pTase1 is weaker than At5Ptase2
brenda
additional information
expression of At5pTase2 is generally stronger than At5Ptase1
brenda
additional information
expression of At5pTase2 is generally stronger than At5Ptase1
brenda
additional information
-
expression of At5pTase2 is generally stronger than At5Ptase1
brenda
additional information
-
PIPP enzyme not expressed in spleen, thymus, skeletal muscle, testis and skin
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
mostly concentrated in the endoplasmic reticulum
brenda
-
using a GFP-fusion construct it is shown that in most cells, the GFP fluorescence retracts from the cell wall, and is most concentrated in a ring, consistent with a cell surface or plasma membrane location
brenda
-
85-90% of total activity, can be solubilized by cholate or to lesser extent by 2 M KCl
brenda
-
membrane associated enzyme has lower specific activity than soluble enzyme
brenda
-
two isoforms postulated one of which is membrane associated
brenda
-
sarcotubular membrane, 60-65% of total activity
brenda
-
two isoforms postulated one of which is membrane associated
brenda
-
two different soluble enzymes, type I and type II
-
brenda
-
two soluble forms, together both forms represent 26% of total activity
-
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
-
enzyme Siw14 is a member of the protein tyrosine-phosphatase (PTP) superfamily. Siw14 has a cysteine-based, class I CX5R(S/T) motif that defines the family of protein-tyrosine phosphatases (PTPs). Bioinformatic studies lead to Siw14 being classified as belonging within a specialist subgroup of PTPs, the dual specific protein-tyrosine phosphatases (DUSPs). The DUSPs themselves include a distinct class of proteins that appears not to have substantial activity against phosphoproteins. These are usually described as nonprotein-specific or atypical phosphatases. The inclusion of Siw14 in this category is supported by biochemical analysis, the enzyme's catalytic activity against 5-diphosphoinositol 1,2,3,4,6-pentakisphosphate (5-InsP7) is several orders of magnitude greater than that against 4-nitrophenyl phosphate, a generic protein phosphatase substrate. Other members of this atypical DUSP subgroup preferentially hydrolyze either phosphorylated carbohydrates, inositol lipids, or triphosphate groups in mRNA. Thus, this DUSP subfamily exhibits catalytic site diversity that is not observed for classical PTPs
evolution
-
phylogenetic analyses are performed to delineate the evolutionary history of the polyphosphate 5-phosphatase family in major angiosperm lineages
evolution
-
phylogenetic analyses are performed to delineate the evolutionary history of the polyphosphate 5-phosphatase family in major angiosperm lineages
evolution
-
phylogenetic analyses are performed to delineate the evolutionary history of the polyphosphate 5-phosphatase family in major angiosperm lineages
evolution
-
phylogenetic analyses are performed to delineate the evolutionary history of the polyphosphate 5-phosphatase family in major angiosperm lineages
evolution
-
phylogenetic analyses are performed to delineate the evolutionary history of the polyphosphate 5-phosphatase family in major angiosperm lineages
evolution
-
phylogenetic analyses are performed to delineate the evolutionary history of the polyphosphate 5-phosphatase family in major angiosperm lineages
evolution
-
phylogenetic analyses are performed to delineate the evolutionary history of the polyphosphate 5-phosphatase family in major angiosperm lineages
evolution
-
phylogenetic analyses are performed to delineate the evolutionary history of the polyphosphate 5-phosphatase family in major angiosperm lineages
evolution
-
phylogenetic analyses are performed to delineate the evolutionary history of the polyphosphate 5-phosphatase family in major angiosperm lineages
evolution
-
phylogenetic analyses are performed to delineate the evolutionary history of the polyphosphate 5-phosphatase family in major angiosperm lineages
evolution
-
phylogenetic analyses are performed to delineate the evolutionary history of the polyphosphate 5-phosphatase family in major angiosperm lineages
evolution
-
phylogenetic analyses are performed to delineate the evolutionary history of the polyphosphate 5-phosphatase family in major angiosperm lineages
evolution
-
phylogenetic analyses are performed to delineate the evolutionary history of the polyphosphate 5-phosphatase family in major angiosperm lineages
evolution
-
phylogenetic analyses are performed to delineate the evolutionary history of the polyphosphate 5-phosphatase family in major angiosperm lineages
evolution
-
phylogenetic analyses are performed to delineate the evolutionary history of the polyphosphate 5-phosphatase family in major angiosperm lineages
evolution
-
phylogenetic analyses are performed to delineate the evolutionary history of the polyphosphate 5-phosphatase family in major angiosperm lineages
evolution
-
phylogenetic analyses are performed to delineate the evolutionary history of the polyphosphate 5-phosphatase family in major angiosperm lineages
evolution
-
phylogenetic analyses are performed to delineate the evolutionary history of the polyphosphate 5-phosphatase family in major angiosperm lineages
evolution
-
phylogenetic analyses are performed to delineate the evolutionary history of the polyphosphate 5-phosphatase family in major angiosperm lineages
evolution
-
phylogenetic analyses are performed to delineate the evolutionary history of the polyphosphate 5-phosphatase family in major angiosperm lineages
evolution
-
phylogenetic analyses are performed to delineate the evolutionary history of the polyphosphate 5-phosphatase family in major angiosperm lineages
evolution
-
phylogenetic analyses are performed to delineate the evolutionary history of the polyphosphate 5-phosphatase family in major angiosperm lineages
evolution
-
enzyme Siw14 is a member of the protein tyrosine-phosphatase (PTP) superfamily. Siw14 has a cysteine-based, class I CX5R(S/T) motif that defines the family of protein-tyrosine phosphatases (PTPs). Bioinformatic studies lead to Siw14 being classified as belonging within a specialist subgroup of PTPs, the dual specific protein-tyrosine phosphatases (DUSPs). The DUSPs themselves include a distinct class of proteins that appears not to have substantial activity against phosphoproteins. These are usually described as nonprotein-specific or atypical phosphatases. The inclusion of Siw14 in this category is supported by biochemical analysis, the enzyme's catalytic activity against 5-diphosphoinositol 1,2,3,4,6-pentakisphosphate (5-InsP7) is several orders of magnitude greater than that against 4-nitrophenyl phosphate, a generic protein phosphatase substrate. Other members of this atypical DUSP subgroup preferentially hydrolyze either phosphorylated carbohydrates, inositol lipids, or triphosphate groups in mRNA. Thus, this DUSP subfamily exhibits catalytic site diversity that is not observed for classical PTPs
-
malfunction
-
the increase in the levels of 1D-myo-inositol 1,4,5-trisphosphate/Ca2+ caused by deficiency of inositol polyphosphate 5-phosphatases is sufficient to break pollen dormancy and to trigger early germination
malfunction
transgenic tobacco plants overexpressing Le5PT1 exhibit reduced growth in height, leaf area, and dry weight compared to wild type plants. The transgenic plants have lower water use efficiency than wild type and the downregulation of the drought-responsive gene, NtERD10B
malfunction
-
mutations in INPP5K have been detected in patients with a rare form of autosomal recessive congenital muscular dystrophy with cataract, short stature and intellectual disability
malfunction
Solanum lycopersicum Ohio 8245
-
transgenic tobacco plants overexpressing Le5PT1 exhibit reduced growth in height, leaf area, and dry weight compared to wild type plants. The transgenic plants have lower water use efficiency than wild type and the downregulation of the drought-responsive gene, NtERD10B
-
metabolism
-
inositol pyrophosphate metabolism in Saccharomyces cerevisiae involving enzyme Siw14, overview
metabolism
-
inositol pyrophosphate metabolism in Saccharomyces cerevisiae involving enzyme Siw14, overview
-
physiological function
-
the enzyme is crucial for maintaining pollen dormancy
physiological function
SHIP2 plays a role in negative regulation of insulin signaling and as a potential drug target for obesity and type 2 diabetes
physiological function
-
mutations of the isoform SHIP2 result in defects in insulin signaling and obesity
physiological function
downregulation of INPP5K disrupts muscle fiber morphology and results in abnormal eye development
physiological function
-
the enzyme links endoplasmic reticulum stress to insulin resistance in skeletal muscle
physiological function
the enzyme is involved in plant growth and abiotic stress responses. Le5PT1 may have a negative role in response to water deficit through the repression of drought-inducible genes that in turn affects plant growth and development
physiological function
-
INPP5K functions extend from control of insulin signaling, endoplasmic reticulum stress response and structural integrity, myoblast differentiation, cytoskeleton organization, cell adhesion and migration, renal osmoregulation, to cancer
physiological function
-
the enzyme has essential functions in growth, development, and stress responses in plants, yeasts, and animals
physiological function
-
divergent functions of polyphosphate 5-phosphatase genes, allowing the angiosperms to successfully adapt to a great number of ecological niches
physiological function
-
Gs5PTase8 plays a positive role in salt tolerance and might be a candidate gene for improving soybean adaptation to salt stress. Ectopic expression of Gs5PTase8 enhances salt tolerance in plants
physiological function
-
the enzyme has essential functions in growth, development, and stress responses in plants, yeasts, and animals
physiological function
-
divergent functions of polyphosphate 5-phosphatase genes, allowing the angiosperms to successfully adapt to a great number of ecological niches
physiological function
-
the enzyme has essential functions in growth, development, and stress responses in plants, yeasts, and animals
physiological function
-
divergent functions of polyphosphate 5-phosphatase genes, allowing the angiosperms to successfully adapt to a great number of ecological niches
physiological function
-
the enzyme has essential functions in growth, development, and stress responses in plants, yeasts, and animals
physiological function
-
divergent functions of polyphosphate 5-phosphatase genes, allowing the angiosperms to successfully adapt to a great number of ecological niches
physiological function
-
the enzyme has essential functions in growth, development, and stress responses in plants, yeasts, and animals
physiological function
-
divergent functions of polyphosphate 5-phosphatase genes, allowing the angiosperms to successfully adapt to a great number of ecological niches
physiological function
-
the enzyme has essential functions in growth, development, and stress responses in plants, yeasts, and animals
physiological function
-
divergent functions of polyphosphate 5-phosphatase genes, allowing the angiosperms to successfully adapt to a great number of ecological niches
physiological function
-
the enzyme has essential functions in growth, development, and stress responses in plants, yeasts, and animals
physiological function
-
divergent functions of polyphosphate 5-phosphatase genes, allowing the angiosperms to successfully adapt to a great number of ecological niches
physiological function
-
the enzyme has essential functions in growth, development, and stress responses in plants, yeasts, and animals
physiological function
-
divergent functions of polyphosphate 5-phosphatase genes, allowing the angiosperms to successfully adapt to a great number of ecological niches
physiological function
-
the enzyme has essential functions in growth, development, and stress responses in plants, yeasts, and animals
physiological function
-
divergent functions of polyphosphate 5-phosphatase genes, allowing the angiosperms to successfully adapt to a great number of ecological niches
physiological function
-
the enzyme has essential functions in growth, development, and stress responses in plants, yeasts, and animals
physiological function
-
divergent functions of polyphosphate 5-phosphatase genes, allowing the angiosperms to successfully adapt to a great number of ecological niches
physiological function
-
the enzyme has essential functions in growth, development, and stress responses in plants, yeasts, and animals
physiological function
-
divergent functions of polyphosphate 5-phosphatase genes, allowing the angiosperms to successfully adapt to a great number of ecological niches
physiological function
-
the enzyme has essential functions in growth, development, and stress responses in plants, yeasts, and animals
physiological function
-
divergent functions of polyphosphate 5-phosphatase genes, allowing the angiosperms to successfully adapt to a great number of ecological niches
physiological function
-
the enzyme has essential functions in growth, development, and stress responses in plants, yeasts, and animals
physiological function
-
divergent functions of polyphosphate 5-phosphatase genes, allowing the angiosperms to successfully adapt to a great number of ecological niches
physiological function
-
the enzyme has essential functions in growth, development, and stress responses in plants, yeasts, and animals
physiological function
-
divergent functions of polyphosphate 5-phosphatase genes, allowing the angiosperms to successfully adapt to a great number of ecological niches
physiological function
-
the enzyme has essential functions in growth, development, and stress responses in plants, yeasts, and animals
physiological function
-
divergent functions of polyphosphate 5-phosphatase genes, allowing the angiosperms to successfully adapt to a great number of ecological niches
physiological function
-
the enzyme has essential functions in growth, development, and stress responses in plants, yeasts, and animals
physiological function
-
divergent functions of polyphosphate 5-phosphatase genes, allowing the angiosperms to successfully adapt to a great number of ecological niches
physiological function
-
the enzyme has essential functions in growth, development, and stress responses in plants, yeasts, and animals
physiological function
-
divergent functions of polyphosphate 5-phosphatase genes, allowing the angiosperms to successfully adapt to a great number of ecological niches
physiological function
-
the enzyme has essential functions in growth, development, and stress responses in plants, yeasts, and animals
physiological function
-
divergent functions of polyphosphate 5-phosphatase genes, allowing the angiosperms to successfully adapt to a great number of ecological niches
physiological function
-
the enzyme has essential functions in growth, development, and stress responses in plants, yeasts, and animals
physiological function
-
divergent functions of polyphosphate 5-phosphatase genes, allowing the angiosperms to successfully adapt to a great number of ecological niches
physiological function
-
the enzyme has essential functions in growth, development, and stress responses in plants, yeasts, and animals
physiological function
-
divergent functions of polyphosphate 5-phosphatase genes, allowing the angiosperms to successfully adapt to a great number of ecological niches
physiological function
-
the enzyme has essential functions in growth, development, and stress responses in plants, yeasts, and animals
physiological function
-
divergent functions of polyphosphate 5-phosphatase genes, allowing the angiosperms to successfully adapt to a great number of ecological niches
physiological function
-
the enzyme has essential functions in growth, development, and stress responses in plants, yeasts, and animals
physiological function
-
divergent functions of polyphosphate 5-phosphatase genes, allowing the angiosperms to successfully adapt to a great number of ecological niches
physiological function
alters abscisic acid and light signaling, stomatal opening, seedling development
physiological function
pollen dormancy and germination
physiological function
cotyledon vein development, alters auxin, abscisic acid, sugar and PHOTOTROPIN1 signaling, root gravitropism, vesicle trafficking
physiological function
alters abscisic acid signaling, seedling development
physiological function
Solanum lycopersicum Ohio 8245
-
the enzyme is involved in plant growth and abiotic stress responses. Le5PT1 may have a negative role in response to water deficit through the repression of drought-inducible genes that in turn affects plant growth and development
-
additional information
-
active site architecture and substrate binding pocket structure, overview. The core catalytic domain of Siw14 is formed by residues 116-281. The three structural elements that demarcate a 9.2-A-deep substrate-binding pocket each have spatial equivalents in PTPs, but these are specialized for Siw14 to bind and hydrolyze the intensely negatively charged diphosphoinositol phosphates. A loop between the alpha5 and alpha6 helices, corresponding to the Q-loop in PTPs, contains a lysine and an arginine that extend into the catalytic pocket due to displacement of the alpha5 helix orientation through intramolecular crowding caused by three bulky, hydrophobic residues. The general-acid loop in PTPs is replaced in Siw14 with a flexible loop that does not use an aspartate or glutamate as a general acid
additional information
-
active site architecture and substrate binding pocket structure, overview. The core catalytic domain of Siw14 is formed by residues 116-281. The three structural elements that demarcate a 9.2-A-deep substrate-binding pocket each have spatial equivalents in PTPs, but these are specialized for Siw14 to bind and hydrolyze the intensely negatively charged diphosphoinositol phosphates. A loop between the alpha5 and alpha6 helices, corresponding to the Q-loop in PTPs, contains a lysine and an arginine that extend into the catalytic pocket due to displacement of the alpha5 helix orientation through intramolecular crowding caused by three bulky, hydrophobic residues. The general-acid loop in PTPs is replaced in Siw14 with a flexible loop that does not use an aspartate or glutamate as a general acid
-
Show AA Sequence and Transmembrane Helices (4075 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
107000
-
calculated molecular mass, found to be slightly larger in SDS-PAGE
115000
37000
43000
48000
90100
-
SDS-PAGE, maltose binding protein MBP-Type I ins(1,4,5)P3 5-phosphatase fusion protein
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
additional information
monomer
-
1 * 60000, gel filtration, SDS-PAGE, type I, 1 * 160000, gel filtration, SDS-PAGE, type II
additional information
the enzyme contains a WD-repeat domain and a 5PTase catalytic domain
additional information
the enzyme contains a WD-repeat domain and a 5PTase catalytic domain
additional information
-
three-dimensional structure analysis of enzyme with active site-bound substrate, analysis of crystal structure
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
side-chain modification
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant catalytic core of Siw14 (residues 116-281), hanging drop vapor diffusion, mixing of 0.002 ml of 15 mg/ml protein in 150 mM NaCl, and 20 mM Tris-HCl, pH 7.5, with 0.002 ml of well solution containing 0.7 M sodium citrate, and 50 mM 2-mercaptoethanol, 25°C, X-ray diffraction structure determination and analysis at 2.35-2.38 A resolution, model building
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C409S
C939S
-
eliminates isoprenylation of enzyme which reduces activity towards phosphatidylinositol 4,5-bisphosphate
D232A
C214S
-
site-directed mutagenesis, mutation in the P-loop, the mutant shows altered substrate specificities and activities compared to the wild-type enzyme, overview
E185A
-
site-directed mutagenesis, mutation in the Flex-loop, the mutant shows altered substrate specificities and activities compared to the wild-type enzyme, overview
F246A
-
site-directed mutagenesis, mutation in the bulky and hydrophobic loop, inactive mutant
H219A
-
site-directed mutagenesis, mutation in the P-loop/alpha-helix4, the mutant shows altered substrate specificities and activities compared to the wild-type enzyme, overview
K184A
-
site-directed mutagenesis, mutation in the Flex-loop, the mutant shows altered substrate specificities and activities compared to the wild-type enzyme, overview
K218A
-
site-directed mutagenesis, mutation in the P-loop, the mutant shows altered substrate specificities and activities compared to the wild-type enzyme, overview
K250A
-
site-directed mutagenesis, mutation in the alpha4-alpha5-loop, the mutant shows altered substrate specificities and activities compared to the wild-type enzyme, overview
N183A
-
site-directed mutagenesis, mutation in the Flex-loop, the mutant shows altered substrate specificities and activities compared to the wild-type enzyme, overview
N215A
-
site-directed mutagenesis, mutation in the P-loop, the mutant shows altered substrate specificities and activities compared to the wild-type enzyme, overview
R216A
-
site-directed mutagenesis, mutation in the P-loop, the mutant shows altered substrate specificities and activities compared to the wild-type enzyme, overview
R220A
-
site-directed mutagenesis, mutation in the P-loop/alpha4-helix, the mutant shows altered substrate specificities and activities compared to the wild-type enzyme, overview
R252A
-
site-directed mutagenesis, mutation in the alpha4-alpha5-loop, the mutant shows altered substrate specificities and activities compared to the wild-type enzyme, overview
W234A
-
site-directed mutagenesis, mutation in the bulky and hydrophobic loop, the mutant is only active with 5-diphosphoinositol 1,2,3,4,6-pentakisphosphate
W281A
-
site-directed mutagenesis, mutation in the bulky and hydrophobic loop, inactive mutant
C214S
-
site-directed mutagenesis, mutation in the P-loop, the mutant shows altered substrate specificities and activities compared to the wild-type enzyme, overview
-
E185A
-
site-directed mutagenesis, mutation in the Flex-loop, the mutant shows altered substrate specificities and activities compared to the wild-type enzyme, overview
-
K184A
-
site-directed mutagenesis, mutation in the Flex-loop, the mutant shows altered substrate specificities and activities compared to the wild-type enzyme, overview
-
N183A
-
site-directed mutagenesis, mutation in the Flex-loop, the mutant shows altered substrate specificities and activities compared to the wild-type enzyme, overview
-
N215A
-
site-directed mutagenesis, mutation in the P-loop, the mutant shows altered substrate specificities and activities compared to the wild-type enzyme, overview
-
E597Q
-
site-directed mutagenesis, the mutant enzyme shows an over 140fold increased catalytic efficiency and a 2.4fold reduced affinity for Mg2+ compared to the wild-type enzyme
additional information
additional information
T-DNA insertional mutants for 5PTase1 (5ptase1-1 and 5ptase1-2, containing a T-DNA insertion within the fifth and fourth introns) and 5PTase2 (5ptase2-1 which contains a T-DNA insertion in the seventh intron) are identified and characterized and a At5PTase1-1/At5PTase2-1 double mutant is produced: grown in dark, seeds from mutants germinate faster than wild-type seeds and the mutant seedlings have longer hypocotyls than wild-type seedlings. Seeds from these mutant lines demonstrate an increase in sensitivity to abscisic acid. These changes in early seedling growth are accompanied by mass increases in Ins(1,4,5)P3, but not by changes in endogenous ABA content. By labeling the endogenous myoinositol pool in 5ptase1 and 5ptase2 mutants, an increases in Ins(1,4,5)P3 and a decrease in PtdIns, PtdIns(4)P, and phosphatidylinositol (4,5)bisphosphate is detected
additional information
T-DNA insertional mutants for 5PTase1 (5ptase1-1 and 5ptase1-2, containing a T-DNA insertion within the fifth and fourth introns) and 5PTase2 (5ptase2-1 which contains a T-DNA insertion in the seventh intron) are identified and characterized and a At5PTase1-1/At5PTase2-1 double mutant is produced: grown in dark, seeds from mutants germinate faster than wild-type seeds and the mutant seedlings have longer hypocotyls than wild-type seedlings. Seeds from these mutant lines demonstrate an increase in sensitivity to abscisic acid. These changes in early seedling growth are accompanied by mass increases in Ins(1,4,5)P3, but not by changes in endogenous ABA content. By labeling the endogenous myoinositol pool in 5ptase1 and 5ptase2 mutants, an increases in Ins(1,4,5)P3 and a decrease in PtdIns, PtdIns(4)P, and phosphatidylinositol (4,5)bisphosphate is detected
additional information
-
T-DNA insertional mutants for 5PTase1 (5ptase1-1 and 5ptase1-2, containing a T-DNA insertion within the fifth and fourth introns) and 5PTase2 (5ptase2-1 which contains a T-DNA insertion in the seventh intron) are identified and characterized and a At5PTase1-1/At5PTase2-1 double mutant is produced: grown in dark, seeds from mutants germinate faster than wild-type seeds and the mutant seedlings have longer hypocotyls than wild-type seedlings. Seeds from these mutant lines demonstrate an increase in sensitivity to abscisic acid. These changes in early seedling growth are accompanied by mass increases in Ins(1,4,5)P3, but not by changes in endogenous ABA content. By labeling the endogenous myoinositol pool in 5ptase1 and 5ptase2 mutants, an increases in Ins(1,4,5)P3 and a decrease in PtdIns, PtdIns(4)P, and phosphatidylinositol (4,5)bisphosphate is detected
additional information
T-DNA insertional mutants for 5PTase1 (5ptase1-1 and 5ptase1-2, containing a T-DNA insertion within the fifth and fourth introns) and 5PTase2 (5ptase2-1 which contains a T-DNA insertion in the seventh intron) are identified and characterized and a At5PTase1-1/At5PTase2-1 double mutant is produced: grown in dark, seeds from mutants germinate faster than wildtype seeds and the mutant seedlings have longer hypocotyls than wild-type seedlings. Seeds from these mutant lines demonstrate an increase in sensitivity to abscisic acid. These changes in early seedling growth are accompanied by mass increases in Ins(1,4,5)P3, but not by changes in endogenous ABA content. By labeling the endogenous myoinositol pool in 5ptase1 and 5ptase2 mutants, an increases in Ins(1,4,5)P3 and a decrease in PtdIns, PtdIns(4)P, and phosphatidylinositol (4,5)bisphosphate is detected
additional information
T-DNA insertional mutants for 5PTase1 (5ptase1-1 and 5ptase1-2, containing a T-DNA insertion within the fifth and fourth introns) and 5PTase2 (5ptase2-1 which contains a T-DNA insertion in the seventh intron) are identified and characterized and a At5PTase1-1/At5PTase2-1 double mutant is produced: grown in dark, seeds from mutants germinate faster than wildtype seeds and the mutant seedlings have longer hypocotyls than wild-type seedlings. Seeds from these mutant lines demonstrate an increase in sensitivity to abscisic acid. These changes in early seedling growth are accompanied by mass increases in Ins(1,4,5)P3, but not by changes in endogenous ABA content. By labeling the endogenous myoinositol pool in 5ptase1 and 5ptase2 mutants, an increases in Ins(1,4,5)P3 and a decrease in PtdIns, PtdIns(4)P, and phosphatidylinositol (4,5)bisphosphate is detected
additional information
-
T-DNA insertional mutants for 5PTase1 (5ptase1-1 and 5ptase1-2, containing a T-DNA insertion within the fifth and fourth introns) and 5PTase2 (5ptase2-1 which contains a T-DNA insertion in the seventh intron) are identified and characterized and a At5PTase1-1/At5PTase2-1 double mutant is produced: grown in dark, seeds from mutants germinate faster than wildtype seeds and the mutant seedlings have longer hypocotyls than wild-type seedlings. Seeds from these mutant lines demonstrate an increase in sensitivity to abscisic acid. These changes in early seedling growth are accompanied by mass increases in Ins(1,4,5)P3, but not by changes in endogenous ABA content. By labeling the endogenous myoinositol pool in 5ptase1 and 5ptase2 mutants, an increases in Ins(1,4,5)P3 and a decrease in PtdIns, PtdIns(4)P, and phosphatidylinositol (4,5)bisphosphate is detected
additional information
construction of transgenic Arabidopsis thaliana plants expressing the human enzyme, the transgenic plants show no altered growth and life cycle phenotype although the basal level of inositol 1,4,5-trisphosphate is reduced by 90% compared to wild-type plants, but the plants are insensitive to gravitropic stimulation and show no increased InsP3 levels in inflorescence stem under gravistimulation in contrast to wild-type plants, bending responses, overview
additional information
-
construction of transgenic Arabidopsis thaliana plants expressing the human enzyme, the transgenic plants show no altered growth and life cycle phenotype although the basal level of inositol 1,4,5-trisphosphate is reduced by 90% compared to wild-type plants, but the plants are insensitive to gravitropic stimulation and show no increased InsP3 levels in inflorescence stem under gravistimulation in contrast to wild-type plants, bending responses, overview
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
His-tag fusion protein expressed in Escherichia coli
membrane associated enzyme
purification by a dual tag strategy: cDNA encoding human Type I Ins(1,4,5)P3 5-phosphatase is subcloned into a modified pMAL expression vector. This plasmid produces a recombinant protein in fusion with affinity tags located at its N-terminus, consisting in a maltose binding protein (MPB) and an octa-histidine stretch. The construction is transformed into Escherichia coli BL21 (DE3) expression strain. Yield: 18 mg of pure and stable enzyme starting from a 2 L
-
recombinant His-tagged catalytic domain from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, the tag is cleaved off
-
recombinant His-tagged enzyme from yeast by nickel affinity chromatography
recombinant His-tagged full length enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
recombinant His6-MBP-tagged wild-type and mutant enzymes from Escherichia coli by nickel affinity and heparin affinity chromatography, tag cleavage with TEV protease, and gel filtration
-
type I enzyme
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Saccharomyces cerevisiae inp51,52,53, lacking inositol 1,4,5-trisphosphate 5-phosphatase activity, rescue of cell viability in cloned cells, His-tag fusion protein expressed in Escherichia coli BL21
-
expression of His-tagged full length enzyme in Escherichia coli strain BL21(DE3)
-
expression of His-tagged isolated catalytic domain in Escherichia coli strain BL21(DE3)
-
functional expression of the enzyme in transgenic Arabidopsis thaliana plants using the Agrobacterium tumefaciens transfection system
gene 5PTase12, expression of His-tagged full length enzyme in yeast
gene 5PTase13, expression of His-tagged full length enzyme in yeast
gene siw14, recombinant expression of His6-MBP-tagged wild-type and mutant enzymes in Escherichia coli
-
His-tag fusion protein expressed in Escherichia coli
overexpressed in host strain, expressed in Drosophila melanogaster S2 cells
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme expression is increased due to endoplasmic reticulum stress and is higher in the skeletal muscle isolated from high-fat-diet-fed mice and db/db mice than in that from wild type mice. Enzyme protein expression is increased by the expression of transcription factors ATF6alpha and XBP1
-
expression of Le5PT1 is downregulated soon after initiation of dehydration and salt stress as well as exposure to polyethylene glycol and NaCl, but not by exogenous abscisic acid treatment
isoform 5PT12 is preferentially expressed in leaf and mature pollen grains at floral stages 12-14
-
the expression of Le5PT2 gradually increases with time after initiation of dehydration, salt stress, exposure to polyethylene glycol and NaCl, and exogenous abscisic acid treatment
expression of Le5PT1 is downregulated soon after initiation of dehydration and salt stress as well as exposure to polyethylene glycol and NaCl, but not by exogenous abscisic acid treatment
expression of Le5PT1 is downregulated soon after initiation of dehydration and salt stress as well as exposure to polyethylene glycol and NaCl, but not by exogenous abscisic acid treatment
Solanum lycopersicum Ohio 8245
-
-
the expression of Le5PT2 gradually increases with time after initiation of dehydration, salt stress, exposure to polyethylene glycol and NaCl, and exogenous abscisic acid treatment
the expression of Le5PT2 gradually increases with time after initiation of dehydration, salt stress, exposure to polyethylene glycol and NaCl, and exogenous abscisic acid treatment
Solanum lycopersicum Ohio 8245
-
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
molecular biology
At5PTase1 and At5PTase2 genes have nonredundant roles in hydrolyzing inositol second-messenger substrates and regulation of Ins(1,4,5)P3 levels is important during germination and early seedling development
medicine
in individuals exhibiting congenital muscular dystrophy, early-onset cataracts, and mild intellectual disability but normal cranial magnetic resonance imaging, bi-allelic mutations in isoform INPP5K are found. Mutations impair phosphatase activity toward phosphatidylinositol (4,5)-bisphosphate or alter the subcellular localization of INPP5K
medicine
genetic variation in INPP5A appears to have a role in susceptibility to arsenic toxicity. A single nucleotide polymorphism in the INPP5A gene (rs1133400) shows a significant gene-environment interaction with water arsenic on skin lesion risk
medicine
depletion of the inositol polyphosphate 5-phosphatase PIPP (INPP5J) increases breast cancer cell transformation, but reduces cell migration and invasion. PIPP ablation accelerates oncogene-driven breast cancer tumor growth in vivo, but reduces metastasis by regulating AKT1-dependent tumor cell migration. PIPP mRNA expression is reduced in human ER-negative breast cancers associated with reduced long-term outcome
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wang, X.L.; Akhtar, R.A.; Abdel-Latif, A.A.
Studies on the properties of myo-inositol-1,4,5-trisphosphate 5-phosphatase and myo-inositol monophosphatase in bovine iris sphincter smooth muscle: effects of okadaic acid and protein phosphorylation
Biochim. Biophys. Acta
1222
27-36
1994
Bos taurus
brenda
Downes, C.P.; Mussat, M.C.; Michell, R.H.
The inositol trisphosphate phosphomonoesterase of the human erythrocyte membrane
Biochem. J.
203
169-177
1982
Homo sapiens
brenda
Erneux, C.; Lemos, M.; Verjans, B.; Vanderhaeghen, P.; Delvaux, A.; Dumont, J.E.
Soluble and particulate Ins(1,4,5)P3/Ins(1,3,4,5)P4 5-phosphatase in bovine brain
Eur. J. Biochem.
181
317-322
1989
Bos taurus
brenda
Verjans B.; De Smedt, F.; Lecocq, R.; Vanweyenberg, V.; Moreau, C.; Erneux, C.
Cloning and expression in E. coli of dog thyroid cDNA encoding a novel inositol 1,4,5-trisphosphate 5-phosphatase
Biochem. J.
300
85-90
1994
Bos taurus, Canis lupus familiaris (Q29467)
-
brenda
Kirk, C.J.; Michell, R.H.; Parry, J.B.; Shears, S.B.
Inositol trisphosphate and tetrakisphosphate phosphomonoesterases of rat liver
Biochem. Soc. Trans.
15
28-32
1987
Rattus norvegicus
brenda
Hansen, C.A.; Johanson, R.A.; Williamson, M.T.; Williamson, J.R.
Purification and characterization of two types of soluble inositol phosphate 5-phosphomonoesterases from rat brain
J. Biol. Chem.
262
17319-17326
1987
Rattus norvegicus
brenda
Connolly, T.M.; Bansal, V.S.; Bross, T.E.; Irvine, R.F.; Majerus, P.W.
The metabolism of tris- and tetraphosphates of inositol by 5-phosphomonoesterase and 3-kinase enzymes
J. Biol. Chem.
262
2146-2149
1987
Homo sapiens
brenda
Milani, D.; Volpe, P.; Pozzan, T.
D-myo-Inositol 1,4,5-trisphosphate phosphatase in skeletal muscle
Biochem. J.
254
525-529
1988
Oryctolagus cuniculus, Frog
brenda
Mitchell, C.A.; Connolly, T.M.; Majerus, P.W.
Identification and isolation of a 75-kDa inositol polyphosphate-5-phosphatase from human platelets
J. Biol. Chem.
264
8873-8877
1989
Homo sapiens
brenda
Lemos, M.; Dumont, J.E.; Erneux, C.
Identification of the bovine brain Ins(1,4,5)P3 5-phosphatase after SDS-polyacrylamide gel electrophoresis
FEBS Lett.
249
321-323
1989
Bos taurus
brenda
Hughes, P.J.; Shears, S.B.
Inositol 1,3,4,5,6-pentakisphosphate and inositol hexakisphosphate inhibit inositol-1,3,4,5-tetrakisphosphate 3-phosphatase in rat parotid glands
J. Biol. Chem.
265
9869-9875
1990
Rattus norvegicus
brenda
Fowler, C.J.; Brnnstrm, G.
Kinetic and inhibitor profiles of soluble and particulate inositol 1,4-5-trisphosphate 5-phosphatase from GH3 and IMR-32 cells
Biochem. J.
271
735-742
1990
Homo sapiens, Rattus norvegicus
brenda
Hollande, F.; Verjans, B.; Erneux, C.
Regeneration of soluble and particulate inositol 1,4,5-trisphosphate 5-phosphatase after SDS/polyacrylamide gel electrophoresis
Biochem. J.
277
293-294
1991
Bos taurus
brenda
Her, A.; Oberdisse, E.
Inositol 1,3,4,5,6-pentakisphosphate and inositol hexakisphosphate are inhibitors of the soluble inositol 1,3,4,5-tetrakisphosphate 3-phosphatase and the inositol 1,4,5-trisphosphate/1,3,4,5-tetrakisphosphate 5-phosphatase from pig brain
Biochem. J.
278
219-224
1991
Sus scrofa
brenda
Hodgkin, M.; Parry, J.B.; Michell, R.H.; Kirk, C.J.
Generation of plasma membrane domains in polarized epithelial cells: role of cell-cell contacts and assembly of the membrane cytoskeleton
Biochem. Soc. Trans.
19
1055
1991
Homo sapiens, Bos taurus, Sus scrofa, Ovis aries
brenda
Verjans, B.; Lecocq, R.; Moreau, C.; Erneux, C.
Purification of bovine brain inositol-1,4,5-trisphosphate 5-phosphatase
Eur. J. Biochem.
204
1083-1087
1992
Bos taurus
brenda
Lynch, B.J.; Challiss, R.A.J.; Chilvers, E.R.
Characterisation and Ca(2+)-dependency of the soluble and particulate Ins(1,4,5)P3 5-phosphatase in bovine tracheal smooth muscle
Biochem. Soc. Trans.
22
314S
1994
Bos taurus
brenda
Van Dijken, P.; Lammers, A.A.; Ozaki, S.; Potter, B.V.L.; Erneux, C.; Van Haastert, P.J.M.
Phosphorylation of inositol 1,4,5-trisphosphate analogues by 3-kinase and dephosphorylation of inositol 1,3,4,5-tetrakisphosphate analogues by 5-phosphatase
Eur. J. Biochem.
226
561-566
1994
Bos taurus
brenda
Safrany, S.T.; Mills, S.J.; Liu, C.; Lampe, D.; Noble, N.J.; Nahorski, S.R.; Potter, B.V.L.
Design of potent and selective inhibitors of myo-inositol 1,4,5-trisphosphate 5-phosphatase
Biochemistry
33
10763-10769
1994
Homo sapiens, Rattus norvegicus
brenda
Hansbro, P.M.; Foster, P.S.; Hogan, S.P.; Ozaki, S.; Denborough, M.A.
Purification and characterization of D-myo-inositol (1,4,5)/(1,3,4,5)-polyphosphate 5-phosphatase from skeletal muscle
Arch. Biochem. Biophys.
311
47-54
1994
Sus scrofa
brenda
Hodgkin, M.; Craxton, A.; Parry, J.B.; Hughes, P.J.; Potter, B.V.L.; Michell, R.H.; Kirk, C.J.
Bovine testis and human erythrocytes contain different subtypes of membrane-associated Ins(1,4,5)P3/Ins(1,3,4,5)P4 5-phosphomonoesterases
Biochem. J.
297
637-645
1994
Homo sapiens, Bos taurus
brenda
Jefferson, A.B.; Majerus, P.W.
Properties of type II inositol polyphosphate 5-phosphatase
J. Biol. Chem.
270
9370-9377
1995
Homo sapiens
brenda
Carrasco, M.A.; Figueroa, S.
Inositol 1,4,5-triphosphate 3-kinase activity in frog skeletal muscle
Comp. Biochem. Physiol. B
110B
747-753
1995
Frog
-
brenda
De Smedt, F.; Boom, A.; Pesesse, X.; Schiffmann, S.N.; Erneux, C.
Post-translational modification of human brain type I inositol-1,4,5-trisphosphate 5-phosphatase by farnesylation
J. Biol. Chem.
271
10419-10424
1996
Homo sapiens, Rattus norvegicus
brenda
Communi, D.; Lecocq, R.; Erneux, C.
Arginine 343 and 350 are two active site residues involved in substrate binding by human type I D-myo-inositol 1,4,5-trisphosphate 5-phosphatase
J. Biol. Chem.
271
11676-11683
1996
Homo sapiens
brenda
De Smedt, F.; Missiaen, L.; Parys, J.B.; Vanweyenberg, V.; De Smedt, H.; Erneux, C.
Isoprenylated human brain type I inositol 1,4,5-trisphosphate 5-phosphatase controls Ca2+ oscillations induced by ATP in Chinese hamster ovary cells
J. Biol. Chem.
272
17367-17375
1997
Homo sapiens
brenda
Erneux, C.; Govaerts, C.; Communi, D.; Pesesse, X.
The diversity and possible functions of the inositol polyphosphate 5-phosphatases
Biochim. Biophys. Acta
1436
185-199
1998
Homo sapiens
brenda
Mochizuki, Y.; Takenawa, T.
Novel inositol polyphosphate 5-phosphatase localizes at membrane ruffles
J. Biol. Chem.
274
36790-36795
1999
Rattus norvegicus
brenda
Whisstock, J.C.; Romero, S.; Gurung, R.; Nandurkar, H.; Ooms, L.M.; Bottomley, S.P.; Mitchell, C.A.
The inositol polyphosphate 5-phosphatases and the apurinic/apyrimidinic base excision repair endonucleases share a common mechanism for catalysis
J. Biol. Chem.
275
37055-37061
2000
Mus musculus, Saccharomyces cerevisiae
brenda
DePass, A.L.; Crain, R.C.; Hepler, P.K.
Inositol 1,4,5 trisphosphate is inactivated by a 5-phosphatase in stamen hair cells of Tradescantia
Planta
213
518-524
2001
Tradescantia virginiana
brenda
Tsujishita, Y.; Guo, S.; Stolz, L.E.; York, J.D.; Hurley, J.H.
Specificity determinants in phosphoinositide dephosphorylation: crystal structure of an archetypal inositol polyphosphate 5-phosphatase
Cell
105
379-389
2001
Schizosaccharomyces pombe
brenda
Whisstock, J.C.; Wiradjaja, F.; Waters, J.E.; Gurung, R.
The structure and function of catalytic domains within inositol polyphosphate 5-phosphatases
IUBMB Life
53
15-23
2002
Homo sapiens
brenda
Burnette, R.N.; Gunesekera, B.M.; Gillaspy, G.E.
An Arabidopsis inositol 5-phosphatase gain-of-function alters abscisic acid signaling
Plant Physiol.
132
1011-1019
2003
Arabidopsis sp.
brenda
Horne, G.; Maechling, C.; Fleig, A.; Hirata, M.; Penner, R.; Spiess, B.; Potter, B.V.
D-6-Deoxy-myo-inositol 1,3,4,5-tetrakisphosphate, a mimic of D-myo-inositol 1,3,4,5-tetrakisphosphate: biological activity and pH-dependent conformational properties
Biochem. Biophys. Res. Commun.
320
1262-1270
2004
Rattus norvegicus
brenda
Chi, Y.; Zhou, B.; Wang, W.Q.; Chung, S.K.; Kwon, Y.U.; Ahn, Y.H.; Chang, Y.T.; Tsujishita, Y.; Hurley, J.H.; Zhang, Z.Y.
Comparative mechanistic and substrate specificity study of inositol polyphosphate 5-phosphatase Schizosaccharomyces pombe Synaptojanin and SHIP2
J. Biol. Chem.
279
44987-44995
2004
Homo sapiens, Schizosaccharomyces pombe
brenda
Seeds, A.M.; Sandquist, J.C.; Spana, E.P.; York, J.D.
A molecular basis for inositol polyphosphate synthesis in Drosophila melanogaster
J. Biol. Chem.
279
47222-47232
2004
Drosophila melanogaster
brenda
Harada, K.; Takeuchi, H.; Oike, M.; Matsuda, M.; Kanematsu, T.; Yagisawa, H.; Nakayama, K.I.; Maeda, K.; Erneux, C.; Hirata, M.
Role of PRIP-1, a novel Ins(1,4,5)P3 binding protein, in Ins(1,4,5)P3-mediated Ca2+ signaling
J. Cell. Physiol.
202
422-433
2005
Mus musculus
brenda
Zhong, R.; Ye, Z.H.
Molecular and biochemical characterization of three WD-repeat-domain-containing inositol polyphosphate 5-phosphatases in Arabidopsis thaliana
Plant Cell Physiol.
45
1720-1728
2004
Arabidopsis thaliana (O80560), Arabidopsis thaliana (Q9SYK4)
brenda
Perera, I.Y.; Hung, C.Y.; Brady, S.; Muday, G.K.; Boss, W.F.
A universal role for inositol 1,4,5-trisphosphate-mediated signaling in plant gravitropism
Plant Physiol.
140
746-760
2006
Homo sapiens (Q14642), Homo sapiens
brenda
Mills, S.J.; Dozol, H.; Vandeput, F.; Backers, K.; Woodman, T.; Erneux, C.; Spiess, B.; Potter, B.V.
3-hydroxybenzene 1,2,4-trisphosphate, a novel second messenger mimic and unusual substrate for type-I myo-inositol 1,4,5-trisphosphate 5-phosphatase: Synthesis and physicochemistry
Chembiochem
7
1696-1706
2006
Homo sapiens
brenda
Gunesekera, B.; Torabinejad, J.; Robinson, J.; Gillaspy, G.E.
Inositol polyphosphate 5-phosphatases 1 and 2 are required for regulating seedling growth
Plant Physiol.
143
1408-1417
2007
Arabidopsis thaliana (Q84MA2), Arabidopsis thaliana (Q9FUR2), Arabidopsis thaliana
brenda
Wohlkoenig, A.; Senechal, M.; Dewitte, F.; Backers, K.; Erneux, C.; Villeret, V.
Expression and purification in high yield of a functionally active recombinant human Type I inositol(1,4,5)P3 5-phosphatase
Protein Expr. Purif.
55
69-74
2007
Homo sapiens
brenda
Mills, S.J.; Vandeput, F.; Trusselle, M.N.; Safrany, S.T.; Erneux, C.; Potter, B.V.
Benzene polyphosphates as tools for cell signalling: inhibition of inositol 1,4,5-trisphosphate 5-phosphatase and interaction with the pH domain of protein kinase Balpha
ChemBioChem
9
1757-1766
2008
Homo sapiens
brenda
Ercetin, M.E.; Ananieva, E.A.; Safaee, N.M.; Torabinejad, J.; Robinson, J.Y.; Gillaspy, G.E.
A phosphatidylinositol phosphate-specific myo-inositol polyphosphate 5-phosphatase required for seedling growth
Plant Mol. Biol.
67
375-388
2008
Arabidopsis thaliana
brenda
Siddique, S.; Endres, S.; Atkins, J.M.; Szakasits, D.; Wieczorek, K.; Hofmann, J.; Blaukopf, C.; Urwin, P.E.; Tenhaken, R.; Grundler, F.M.; Kreil, D.P.; Bohlmann, H.
Myo-inositol oxygenase genes are involved in the development of syncytia induced by Heterodera schachtii in Arabidopsis roots
New Phytol.
184
457-472
2009
Arabidopsis thaliana (Q84MA2), Arabidopsis thaliana (Q9FUR2)
brenda
Khodakovskaya, M.; Sword, C.; Wu, Q.; Perera, I.Y.; Boss, W.F.; Brown, C.S.; Winter Sederoff, H.
Increasing inositol (1,4,5)-trisphosphate metabolism affects drought tolerance, carbohydrate metabolism and phosphate-sensitive biomass increases in tomato
Plant Biotechnol. J.
8
170-183
2010
Homo sapiens
brenda
Wang, Y.; Chu, Y.J.; Xue, H.W.
Inositol polyphosphate 5-phosphatase-controlled Ins(1,4,5)P3/Ca2+ is crucial for maintaining pollen dormancy and regulating early germination of pollen
Development
139
2221-2233
2012
Arabidopsis thaliana
brenda
Braun, W.; Schein, C.
Membrane interaction and functional plasticity of inositol polyphosphate 5-phosphatases
Structure
22
664-666
2014
Homo sapiens
brenda
Tresaugues, L.; Silvander, C.; Flodin, S.; Welin, M.; Nyman, T.; Graeslund, S.; Hammarstroem, M.; Berglund, H.; Nordlund, P.
Structural basis for phosphoinositide substrate recognition, catalysis, and membrane interactions in human inositol polyphosphate 5-phosphatases
Structure
22
744-755
2014
Homo sapiens (O15357)
brenda
Wiessner, M.; Roos, A.; Munn, C.J.; Viswanathan, R.; Whyte, T.; Cox, D.; Schoser, B.; Sewry, C.; Roper, H.; Phadke, R.; Marini Bettolo, C.; Barresi, R.; Charlton, R.; Boennemann, C.G.; Abath Neto, O.; Reed, U.C.; Zanoteli, E.; Araujo Martins Moreno, C.; Ertl-Wagner, B.; Stucka, R.; De Goede, C.; Borges de Silva, T.
Mutations in INPP5K, encoding a phosphoinositide 5-phosphatase, cause congenital muscular dystrophy with cataracts and mild cognitive impairment
Am. J. Hum. Genet.
100
523-536
2017
Homo sapiens (Q9BT40), Danio rerio (A0A2R8QKI3), Danio rerio
brenda
Seow, W.J.; Pan, W.C.; Kile, M.L.; Tong, L.; Baccarelli, A.A.; Quamruzzaman, Q.; Rahman, M.; Mostofa, G.; Rakibuz-Zaman, M.; Kibriya, M.; Ahsan, H.; Lin, X.; Christiani, D.C.
A distinct and replicable variant of the squamous cell carcinoma gene inositol polyphosphate-5-phosphatase modifies the susceptibility of arsenic-associated skin lesions in Bangladesh
Cancer
121
2222-2229
2015
Homo sapiens (Q14642)
brenda
Ooms, L.M.; Binge, L.C.; Davies, E.M.; Rahman, P.; Conway, J.R.; Gurung, R.; Ferguson, D.T.; Papa, A.; Fedele, C.G.; Vieusseux, J.L.; Chai, R.C.; Koentgen, F.; Price, J.T.; Tiganis, T.; Timpson, P.; McLean, C.A.; Mitchell, C.A.
The inositol polyphosphate 5-phosphatase PIPP regulates AKT1-dependent breast cancer growth and metastasis
Cancer Cell
28
155-169
2015
Homo sapiens (Q15735)
brenda
Wang, H.; Gu, C.; Rolfes, R.J.; Jessen, H.J.; Shears, S.B.
Structural and biochemical characterization of Siw14 a protein-tyrosine phosphatase fold that metabolizes inositol pyrophosphates
J. Biol. Chem.
293
6905-6914
2018
Saccharomyces cerevisiae, Saccharomyces cerevisiae ATCC 204508
brenda
Ijuin, T.; Hosooka, T.; Takenawa, T.
Phosphatidylinositol 3,4,5-trisphosphate phosphatase SKIP links endoplasmic reticulum stress in skeletal muscle to insulin resistance
Mol. Cell. Biol.
36
108-118
2016
Mus musculus
brenda
Na, J.K.; Metzger, J.D.
A putative tomato inositol polyphosphate 5-phosphatase, Le5PT1, is involved in plant growth and abiotic stress responses
3 Biotech
10
28
2020
Solanum lycopersicum (A8IDV8), Solanum lycopersicum (A8IDW2), Solanum lycopersicum Ohio 8245 (A8IDV8), Solanum lycopersicum Ohio 8245 (A8IDW2)
brenda
Schurmans, S.; Vande Catsyne, C.A.; Desmet, C.; Moes, B.
The phosphoinositide 5-phosphatase INPP5K From gene structure to in vivo functions
Adv. Biol. Regul.
79
100760
2021
Homo sapiens
brenda
Zhang, Z.; Li, Y.; Luo, Z.; Kong, S.; Zhao, Y.; Zhang, C.; Zhang, W.; Yuan, H.; Cheng, L.
Expansion and functional divergence of inositol polyphosphate 5-phosphatases in angiosperms
Genes (Basel)
10
393
2019
Acorus calamus, Amborella trichopoda, Arabidopsis thaliana, Caenorhabditis elegans, Capsella grandiflora, Capsella rubella, Carica papaya, Chlamydomonas reinhardtii, Danio rerio, Eutrema salsugineum, Ginkgo biloba, Glycine max, Homo sapiens, Lotus japonicus, Medicago truncatula, Mus musculus, Oryza sativa, Physcomitrium patens, Populus trichocarpa, Saccharomyces cerevisiae, Xenopus tropicalis, Zea mays
brenda
Jia, Q.; Kong, D.; Li, Q.; Sun, S.; Song, J.; Zhu, Y.; Liang, K.; Ke, Q.; Lin, W.; Huang, J.
The function of inositol phosphatases in plant tolerance to abiotic stress
Int. J. Mol. Sci.
20
3999
2019
Arabidopsis thaliana (O80560), Arabidopsis thaliana (Q9SYK4), Arabidopsis thaliana (Q84MA2), Arabidopsis thaliana (Q9FUR2)
brenda
Jia, Q.; Sun, S.; Kong, D.; Song, J.; Wu, L.; Yan, Z.; Zuo, L.; Yang, Y.; Liang, K.; Lin, W.; Huang, J.
Ectopic expression of Gs5PTase8, a soybean inositol polyphosphate 5-phosphatase, enhances salt tolerance in plants
Int. J. Mol. Sci.
21
1023
2020
Glycine soja
brenda
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