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1-phosphatidyl-1D-myo-inositol 3,4,5-triphosphate + H2O
1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate + 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 1,2,4,5,6-pentakisphosphate + H2O
1D-myo-inositol 1,2,4,6-tetrakisphosphate + phosphate
-
-
-
-
?
1D-myo-inositol 1,2,4,5-tetrakisphosphate + H2O
1D-myo-inositol 1,2,4-trisphosphate + phosphate
-
-
-
-
?
1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O
1D-myo-inositol 1,3,4-trisphosphate + phosphate
1D-myo-inositol 1,3,4,5-tetrasphosphate + H2O
1D-myo-inositol 1,3,4-trisphosphate + phosphate
-
-
-
-
?
1D-myo-inositol 1,4,5-trisphosphate + H2O
1D-myo-inositol 1,4-bisphosphate + phosphate
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
-
preferred substrate
-
-
?
1D-myo-inositol 4,5,6-trisphosphate + H2O
1D-myo-inositol 4,6-bisphosphate + phosphate
-
-
-
-
?
3-O-methylfluorescein phosphate + H2O
3-O-methylfluorescein + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
7-methyl-6-thioguanosine + H2O
7-methyl-6-thioguanine + ribose 1-phosphate
-
spectrophotometric continuous coupled enzyme assay substrate
-
-
?
7-nitrobenz-2-oxa-1,3-diazole 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O
7-nitrobenz-2-oxa-1,3-diazole 1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate
-
fluorescence-labeled substrate
-
-
?
D(+)-sn-1,2-di-O-hexadecanoylglyceryl 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate + H2O
D(+)-sn-1,2-di-O-hexadecanoylglyceryl 1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate + phosphate
D(+)-sn-1,2-di-O-hexadecanoylglyceryl 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O
D(+)-sn-1,2-di-O-hexadecanoylglyceryl 1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate
D-myo-phosphatidylinositol 3,4,5-trisphosphate
D-myo-phosphatidylinositol 3,4-bisphosphate + phosphate
D-myo-phosphatidylinositol 3,5-bisphosphate
D-myo-phosphatidylinositol 3-phosphate
-
-
-
?
D-myo-phosphatidylinositol 4,5-bisphosphate
D-myo-phosphatidylinositol 4-phosphate + phosphate
inositol 1,3,4,5-tetrakisphosphate + H2O
inositol 1,3,4-trisphosphate + phosphate
myo-inositol 1,4,5-trisphosphate + H2O
inositol 1,4-diphosphate + phosphate
myo-inositol 3,4,5-trisphosphate + H2O
?
-
-
-
-
?
phosphatidyl-myo-inositol 4,5-bisphosphate + H2O
phosphatidylinositol 4-phosphate + phosphate
phosphatidylinositol 3,4,5-trisphosphate + H2O
phosphatidylinositol 3,4-bisphosphate + phosphate
-
-
?
phosphatidylinositol 3,4,5-trisphosphate + H2O
phosphatidylinositol 4,5-bisphosphate + phosphate
-
-
-
?
phosphatidylinositol 3,5-bisphosphate + H2O
phosphatidylinositol 3-phosphate + phosphate
-
-
?
phosphatidylinositol 4,5-bisphosphate + H2O
phosphatidylinositol 4-phosphate + phosphate
phosphatidylinositol-3,4,5-trisphosphate + H2O
phosphatidylinositol-3,4-bisphosphate + phosphate
-
-
-
-
?
phosphatidylinositol-4,5-bisphosphate + H2O
phosphatidylinositol-4-phosphate + phosphate
additional information
?
-
1-phosphatidyl-1D-myo-inositol 3,4,5-triphosphate + H2O
1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate + phosphate
-
-
-
-
?
1-phosphatidyl-1D-myo-inositol 3,4,5-triphosphate + H2O
1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate + 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 3,4,5-trisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate + phosphate
recombinant enzyme
-
-
?
1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate + phosphate
-
-
-
-
?
1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate + 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 3,4,5-trisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate + 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 4,5-bisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate
-
-
-
?
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate
best substrate
-
-
?
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate
the enzyme is involved in regulation of 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate levels in stem
-
-
?
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate
preferred substrate of the recombinant enzyme
-
-
?
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate
-
-
-
-
?
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate
-
-
-
-
?
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate
-
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate is required for formation, polarization, and elongation of spermatid cysts, overview
-
-
?
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate
-
-
-
-
?
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate
-
-
-
?
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate
-
-
-
?
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate
-
-
-
?
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate
-
best substrate
-
-
?
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate
-
preferred substrate
-
-
?
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate
-
synaptojanin-1 regulates of turnover of a 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate pool involved Ca2+ signalling and in clathrin and actin dynamics at the cell surface, SJ-1 attenuates the oscillations of Ca2+ induced by ATP and the catalytic domain of its 5-Pase domain mimicking the effect, overview
-
-
?
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate
-
best substrate for OCRL
-
-
?
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate
the voltage-sensitive phosphoinositide phosphatase Ci-VSP, a membrane-resident PI(4,5) P2-5-phosphatase, removes phosphatidylinositol-4,5-bisphosphate from the plasma membrane
-
-
?
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate
-
-
-
-
?
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate
-
-
-
-
?
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate
-
good substrate
-
-
?
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate
-
-
-
-
?
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate
-
the enzyme is involved in regulation of 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate levels, an important second messenger in signalling pathways, e.g. MAP kinase activation, enzyme regulation by effectors TAX4 and IRS4, overview
-
-
?
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate
-
-
-
-
?
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate
-
the enzyme is involved in regulation of 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate levels, an important second messenger in signalling pathways, e.g. MAP kinase activation, enzyme regulation by effectors TAX4 and IRS4, overview
-
-
?
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate
-
-
-
-
?
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate
-
-
-
-
?
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate
-
-
-
-
?
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate
-
-
-
-
?
1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O
1D-myo-inositol 1,3,4-trisphosphate + phosphate
-
-
-
?
1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O
1D-myo-inositol 1,3,4-trisphosphate + phosphate
-
-
-
-
?
1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O
1D-myo-inositol 1,3,4-trisphosphate + phosphate
-
-
-
?
1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O
1D-myo-inositol 1,3,4-trisphosphate + phosphate
-
good substrate of OCRL, not synaptojanin2
-
-
?
1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O
1D-myo-inositol 1,3,4-trisphosphate + phosphate
-
-
-
-
?
1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O
1D-myo-inositol 1,3,4-trisphosphate + phosphate
-
-
-
-
?
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
1D-myo-inositol 1,4-bisphosphate + phosphate
-
-
-
?
1D-myo-inositol 1,4,5-trisphosphate + H2O
1D-myo-inositol 1,4-bisphosphate + phosphate
-
-
-
?
1D-myo-inositol 1,4,5-trisphosphate + H2O
1D-myo-inositol 1,4-bisphosphate + phosphate
recombinant enzyme
-
-
?
1D-myo-inositol 1,4,5-trisphosphate + H2O
1D-myo-inositol 1,4-bisphosphate + phosphate
-
-
-
-
?
1D-myo-inositol 1,4,5-trisphosphate + H2O
1D-myo-inositol 1,4-bisphosphate + phosphate
-
-
-
-
?
1D-myo-inositol 1,4,5-trisphosphate + H2O
1D-myo-inositol 1,4-bisphosphate + phosphate
-
-
-
-
?
1D-myo-inositol 1,4,5-trisphosphate + H2O
1D-myo-inositol 1,4-bisphosphate + phosphate
-
-
-
-
?
D(+)-sn-1,2-di-O-hexadecanoylglyceryl 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate + H2O
D(+)-sn-1,2-di-O-hexadecanoylglyceryl 1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate + phosphate
-
3-O-phospho-linked
-
-
?
D(+)-sn-1,2-di-O-hexadecanoylglyceryl 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate + H2O
D(+)-sn-1,2-di-O-hexadecanoylglyceryl 1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate + phosphate
-
3-O-phospho-linked, best substrate
-
-
?
D(+)-sn-1,2-di-O-hexadecanoylglyceryl 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate + H2O
D(+)-sn-1,2-di-O-hexadecanoylglyceryl 1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate + phosphate
-
3-O-phospho-linked
-
-
?
D(+)-sn-1,2-di-O-hexadecanoylglyceryl 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O
D(+)-sn-1,2-di-O-hexadecanoylglyceryl 1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate
-
3-O-phospho-linked, best substrate for synaptojanin2
-
-
?
D(+)-sn-1,2-di-O-hexadecanoylglyceryl 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O
D(+)-sn-1,2-di-O-hexadecanoylglyceryl 1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate
-
3-O-phospho-linked, best substrate
-
-
?
D(+)-sn-1,2-di-O-hexadecanoylglyceryl 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O
D(+)-sn-1,2-di-O-hexadecanoylglyceryl 1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate
-
3-O-phospho-linked, best substrate for synaptojanin1
-
-
?
D-myo-phosphatidylinositol 3,4,5-trisphosphate
D-myo-phosphatidylinositol 3,4-bisphosphate + phosphate
-
-
-
-
?
D-myo-phosphatidylinositol 3,4,5-trisphosphate
D-myo-phosphatidylinositol 3,4-bisphosphate + phosphate
-
-
-
-
?
D-myo-phosphatidylinositol 3,4,5-trisphosphate
D-myo-phosphatidylinositol 3,4-bisphosphate + phosphate
-
-
-
-
?
D-myo-phosphatidylinositol 3,4,5-trisphosphate
D-myo-phosphatidylinositol 3,4-bisphosphate + phosphate
-
reaction is not stimulated by phosphatidylserine
-
-
?
D-myo-phosphatidylinositol 3,4,5-trisphosphate
D-myo-phosphatidylinositol 3,4-bisphosphate + phosphate
-
reaction is strongly stimulated by phosphatidylserine
-
-
?
D-myo-phosphatidylinositol 3,4,5-trisphosphate
D-myo-phosphatidylinositol 3,4-bisphosphate + phosphate
-
-
-
-
?
D-myo-phosphatidylinositol 3,4,5-trisphosphate
D-myo-phosphatidylinositol 3,4-bisphosphate + phosphate
-
-
-
?
D-myo-phosphatidylinositol 3,4,5-trisphosphate
D-myo-phosphatidylinositol 3,4-bisphosphate + phosphate
-
-
-
-
?
D-myo-phosphatidylinositol 4,5-bisphosphate
D-myo-phosphatidylinositol 4-phosphate + phosphate
-
-
-
-
?
D-myo-phosphatidylinositol 4,5-bisphosphate
D-myo-phosphatidylinositol 4-phosphate + phosphate
-
D-myo-phosphatidylinositol 4,5-bisphosphate is a much better substrate than D-myo-phosphatidylinositol 3,4,5-trisphosphate
-
-
?
inositol 1,3,4,5-tetrakisphosphate + H2O
inositol 1,3,4-trisphosphate + phosphate
-
-
-
?
inositol 1,3,4,5-tetrakisphosphate + H2O
inositol 1,3,4-trisphosphate + phosphate
-
-
-
-
?
myo-inositol 1,4,5-trisphosphate + H2O
inositol 1,4-diphosphate + phosphate
-
at 17% of the activity with phosphatidyl-myo-inositol 4,5-bisphosphate
-
-
?
myo-inositol 1,4,5-trisphosphate + H2O
inositol 1,4-diphosphate + phosphate
-
at 30% of the activity with phosphatidyl-myo-inositol 4,5-bisphosphate
-
-
?
myo-inositol 1,4,5-trisphosphate + H2O
inositol 1,4-diphosphate + phosphate
-
at 2% of the activity with phosphatidyl-myo-inositol 4,5-bisphosphate
-
-
?
myo-inositol 1,4,5-trisphosphate + H2O
inositol 1,4-diphosphate + phosphate
-
-
-
-
?
myo-inositol 1,4,5-trisphosphate + H2O
inositol 1,4-diphosphate + phosphate
-
-
-
?
myo-inositol 1,4,5-trisphosphate + H2O
inositol 1,4-diphosphate + phosphate
-
-
-
-
?
phosphatidyl-myo-inositol 4,5-bisphosphate + H2O
phosphatidylinositol 4-phosphate + phosphate
-
-
-
-
?
phosphatidyl-myo-inositol 4,5-bisphosphate + H2O
phosphatidylinositol 4-phosphate + phosphate
-
-
-
-
?
phosphatidyl-myo-inositol 4,5-bisphosphate + H2O
phosphatidylinositol 4-phosphate + phosphate
-
-
-
-
?
phosphatidyl-myo-inositol 4,5-bisphosphate + H2O
phosphatidylinositol 4-phosphate + phosphate
-
-
-
-
?
phosphatidyl-myo-inositol 4,5-bisphosphate + H2O
phosphatidylinositol 4-phosphate + phosphate
-
-
-
-
?
phosphatidyl-myo-inositol 4,5-bisphosphate + H2O
phosphatidylinositol 4-phosphate + phosphate
-
-
-
?
phosphatidyl-myo-inositol 4,5-bisphosphate + H2O
phosphatidylinositol 4-phosphate + phosphate
-
-
-
-
?
phosphatidyl-myo-inositol 4,5-bisphosphate + H2O
phosphatidylinositol 4-phosphate + phosphate
-
-
-
?
phosphatidyl-myo-inositol 4,5-bisphosphate + H2O
phosphatidylinositol 4-phosphate + phosphate
-
-
-
-
?
phosphatidyl-myo-inositol 4,5-bisphosphate + H2O
phosphatidylinositol 4-phosphate + phosphate
-
-
-
-
?
phosphatidyl-myo-inositol 4,5-bisphosphate + H2O
phosphatidylinositol 4-phosphate + phosphate
-
-
-
?
phosphatidyl-myo-inositol 4,5-bisphosphate + H2O
phosphatidylinositol 4-phosphate + phosphate
-
-
-
-
?
phosphatidyl-myo-inositol 4,5-bisphosphate + H2O
phosphatidylinositol 4-phosphate + phosphate
-
1-(3-sn-phosphatidyl)-D-myo-inositol 4,5-bisphosphate
-
-
?
phosphatidyl-myo-inositol 4,5-bisphosphate + H2O
phosphatidylinositol 4-phosphate + phosphate
-
-
-
-
?
phosphatidyl-myo-inositol 4,5-bisphosphate + H2O
phosphatidylinositol 4-phosphate + phosphate
-
-
-
-
?
phosphatidyl-myo-inositol 4,5-bisphosphate + H2O
phosphatidylinositol 4-phosphate + phosphate
-
-
-
-
?
phosphatidyl-myo-inositol 4,5-bisphosphate + H2O
phosphatidylinositol 4-phosphate + phosphate
-
1-(3-sn-phosphatidyl)-D-myo-inositol 4,5-bisphosphate
-
-
?
phosphatidyl-myo-inositol 4,5-bisphosphate + H2O
phosphatidylinositol 4-phosphate + phosphate
-
-
-
-
?
phosphatidylinositol 4,5-bisphosphate + H2O
phosphatidylinositol 4-phosphate + phosphate
-
-
-
?
phosphatidylinositol 4,5-bisphosphate + H2O
phosphatidylinositol 4-phosphate + phosphate
-
-
-
-
?
phosphatidylinositol-4,5-bisphosphate + H2O
phosphatidylinositol-4-phosphate + phosphate
-
-
-
-
?
phosphatidylinositol-4,5-bisphosphate + H2O
phosphatidylinositol-4-phosphate + phosphate
-
-
-
-
?
additional information
?
-
the enzyme is essential in secondary cell wall synthesis in fiber cells and xylem vessels, enzyme deficiency causes a high reduction in secondary cell wall thickness and stem stability due to altered actin organization in fiber cells
-
-
?
additional information
?
-
-
the enzyme is essential in secondary cell wall synthesis in fiber cells and xylem vessels, enzyme deficiency causes a high reduction in secondary cell wall thickness and stem stability due to altered actin organization in fiber cells
-
-
?
additional information
?
-
substrate specificity, no activity with 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
-
-
?
additional information
?
-
-
substrate specificity, no activity with 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
-
-
?
additional information
?
-
substrate specificity, no activity with 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
-
-
?
additional information
?
-
-
substrate specificity, no activity with 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
-
-
?
additional information
?
-
-
the enzyme participates in the rearrangement of actin filaments that occurs in growth factor-stimulated cells
-
-
?
additional information
?
-
quantitation of voltage dependent 5- and 3-phosphatase subreactions against endogenous substrates. 3-Phosphatase activity against phosphatidylinositol 3,4,5-trisphosphate, reaction of EC 3.1.3.67, is 55fold slower than 5-phosphatase activity against phosphatidylinositol 4,5-bisphosphate, reaction of EC 3.1.3.36
-
-
?
additional information
?
-
-
no activity with 1-(3-sn-phosphatidyl)-D-myo-inositol 4-phosphate
-
-
?
additional information
?
-
-
the X-chromosome encoded enzyme is deficient in oculocerebrorenal syndrome
-
-
?
additional information
?
-
-
the X-chromosome encoded enzyme is deficient in oculocerebrorenal syndrome
-
-
?
additional information
?
-
-
the X-chromosome encoded enzyme is deficient in oculocerebrorenal syndrome
-
-
?
additional information
?
-
-
the enzyme may function in lysosomal membrane trafficking by regulating the specific pool of phosphatidylinositol 4,5-diphosphate that is associated with lysosomes
-
-
?
additional information
?
-
-
the primary defect in oculocerebrorenal syndrome of Lowe is a deficiency of Golgi phosphatidylinositol 4,5-diphosphate phosphatase. This disorder results from dysregulation of Golgi function and in this way causes developmental defects in the lens and abnormal renal and neurological function
-
-
?
additional information
?
-
-
substrate specificity, no activity with 1D-myo-inositol 1,5-bisphosphate, overview
-
-
?
additional information
?
-
-
enzyme possesses a dual phosphatase activity: 5-phosphatase activity excecuted by the inositol-5-phosphatase domain and a 3- and 4-phosphatase activity executed by the Sac1-like domain harboring a less selective phosphoinositide phosphatase activity
-
-
?
additional information
?
-
-
c-Jun NH2-terminal kinase (JNK)-interacting protein 1 (JIP1) interacts with SHIP2 and thereby positively modulates the MLK3/JIP1-mediated JNK1 activation
-
-
?
additional information
?
-
-
intersectin1 (ITSN1) is identified as a new binding partner of the SH2 domain containing inositol 5-phosphatase 2 (SHIP2)
-
-
?
additional information
?
-
OCRL1 isoform a binds clathrin with higher affinity than isoform b, and is significantly more enriched in clathrin-coated trafficking intermediates
-
-
?
additional information
?
-
-
SHIP2 interacts with RhoA in a GTP-dependent manner
-
-
?
additional information
?
-
-
substrate specificity, no activity with 1D-myo-inositol 1,5-bisphosphate, overview
-
-
?
additional information
?
-
-
acetylcholine increases activity
-
-
?
additional information
?
-
-
the diabetic state does not affect enzyme activity
-
-
?
additional information
?
-
-
substrate specificity, no activity with 1D-myo-inositol 1,5-bisphosphate and 1D-myo-inositol 1,4,5-trisphosphate, overview
-
-
?
additional information
?
-
-
the enzyme has multiple roles in cellular signalling and may regulate distinct pathways
-
-
?
additional information
?
-
-
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
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-
?
additional information
?
-
-
VPA0450 is an inositol polyphosphate 5-phosphatase that hydrolyzed the D5 phosphate from the plasma membrane phospholipid phosphatidylinositol 4,5-bisphosphate
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?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate + phosphate
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate
phosphatidylinositol-3,4,5-trisphosphate + H2O
phosphatidylinositol-3,4-bisphosphate + phosphate
-
-
-
-
?
phosphatidylinositol-4,5-bisphosphate + H2O
phosphatidylinositol-4-phosphate + phosphate
additional information
?
-
1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate + phosphate
-
-
-
-
?
1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate + 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 3,4,5-trisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate + phosphate
-
-
-
-
?
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate
-
-
-
?
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate
the enzyme is involved in regulation of 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate levels in stem
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-
?
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate
-
-
-
-
?
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate
-
-
-
-
?
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate
-
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate is required for formation, polarization, and elongation of spermatid cysts, overview
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-
?
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate
-
-
-
-
?
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate
-
-
-
?
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate
-
-
-
?
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate
-
-
-
?
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate
-
preferred substrate
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-
?
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate
-
synaptojanin-1 regulates of turnover of a 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate pool involved Ca2+ signalling and in clathrin and actin dynamics at the cell surface, SJ-1 attenuates the oscillations of Ca2+ induced by ATP and the catalytic domain of its 5-Pase domain mimicking the effect, overview
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-
?
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate
the voltage-sensitive phosphoinositide phosphatase Ci-VSP, a membrane-resident PI(4,5) P2-5-phosphatase, removes phosphatidylinositol-4,5-bisphosphate from the plasma membrane
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-
?
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate
-
-
-
-
?
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate
-
-
-
-
?
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate
-
the enzyme is involved in regulation of 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate levels, an important second messenger in signalling pathways, e.g. MAP kinase activation, enzyme regulation by effectors TAX4 and IRS4, overview
-
-
?
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate
-
the enzyme is involved in regulation of 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate levels, an important second messenger in signalling pathways, e.g. MAP kinase activation, enzyme regulation by effectors TAX4 and IRS4, overview
-
-
?
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate
-
-
-
-
?
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate
-
-
-
-
?
phosphatidylinositol-4,5-bisphosphate + H2O
phosphatidylinositol-4-phosphate + phosphate
-
-
-
-
?
phosphatidylinositol-4,5-bisphosphate + H2O
phosphatidylinositol-4-phosphate + phosphate
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-
-
-
?
additional information
?
-
the enzyme is essential in secondary cell wall synthesis in fiber cells and xylem vessels, enzyme deficiency causes a high reduction in secondary cell wall thickness and stem stability due to altered actin organization in fiber cells
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-
?
additional information
?
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-
the enzyme is essential in secondary cell wall synthesis in fiber cells and xylem vessels, enzyme deficiency causes a high reduction in secondary cell wall thickness and stem stability due to altered actin organization in fiber cells
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-
?
additional information
?
-
-
the enzyme participates in the rearrangement of actin filaments that occurs in growth factor-stimulated cells
-
-
?
additional information
?
-
-
the X-chromosome encoded enzyme is deficient in oculocerebrorenal syndrome
-
-
?
additional information
?
-
-
the X-chromosome encoded enzyme is deficient in oculocerebrorenal syndrome
-
-
?
additional information
?
-
-
the X-chromosome encoded enzyme is deficient in oculocerebrorenal syndrome
-
-
?
additional information
?
-
-
the enzyme may function in lysosomal membrane trafficking by regulating the specific pool of phosphatidylinositol 4,5-diphosphate that is associated with lysosomes
-
-
?
additional information
?
-
-
the primary defect in oculocerebrorenal syndrome of Lowe is a deficiency of Golgi phosphatidylinositol 4,5-diphosphate phosphatase. This disorder results from dysregulation of Golgi function and in this way causes developmental defects in the lens and abnormal renal and neurological function
-
-
?
additional information
?
-
-
c-Jun NH2-terminal kinase (JNK)-interacting protein 1 (JIP1) interacts with SHIP2 and thereby positively modulates the MLK3/JIP1-mediated JNK1 activation
-
-
?
additional information
?
-
-
intersectin1 (ITSN1) is identified as a new binding partner of the SH2 domain containing inositol 5-phosphatase 2 (SHIP2)
-
-
?
additional information
?
-
OCRL1 isoform a binds clathrin with higher affinity than isoform b, and is significantly more enriched in clathrin-coated trafficking intermediates
-
-
?
additional information
?
-
-
SHIP2 interacts with RhoA in a GTP-dependent manner
-
-
?
additional information
?
-
-
acetylcholine increases activity
-
-
?
additional information
?
-
-
the diabetic state does not affect enzyme activity
-
-
?
additional information
?
-
-
the enzyme has multiple roles in cellular signalling and may regulate distinct pathways
-
-
?
additional information
?
-
-
VPA0450 is an inositol polyphosphate 5-phosphatase that hydrolyzed the D5 phosphate from the plasma membrane phospholipid phosphatidylinositol 4,5-bisphosphate
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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malfunction
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At5PTase7 mutants show reduced salt tolerance and increased salt stress response, phenotype, overview
malfunction
-
both knockdown of SHIP2 expression and acute production of PI(3,4,5)P3 shorten clathrin-coated pits lifetime by enhancing the rate of pit maturation
malfunction
excess amounts of SHIP2 may be related, at least in part, to brain dysfunction in insulin resistance with type 2 diabetes. A dominant-negative mutant of SHIP2, expressed in cultured neurons, causes insulin signaling augmentation. Inhibition of SHIP2 ameliorates the impairment of hippocampal synaptic plasticity and memory formation in db/db mice
malfunction
-
in absence of dOCRL, several essential components of the cleavage furrow are found to be incorrectly localized on giant cytoplasmic vacuoles rich in PI(4,5)P2 and in endocytic markers
malfunction
-
inducible reduction of negative charge rescues DELTAsopB bacteria-containing Salmonella-containing vacuoles from fusion with lysosomes
malfunction
-
mutant sac9-1 plants have a constitutively stressed phenotype with shorter roots which notably accumulate phosphatidylinositol 4,5-bisphosphate and its hydrolysis product inositol trisphosphate, phenotype with extreme abnormalities of cell wall and membrane structures in sac9-1 primary root cells, regardless of cell type, position within the meristematic area, and plane of section, overview
malfunction
-
no effects by siRNA-mediated OCRL1 knockdown on biosynthetic and postendocytic membrane traffic in renal epithelial cells, overview. Cells depleted of OCRL1 do not have significantly elevated levels of cellular PIP2 but display an increase in actin comet, OCRL1 knockdown results in a significant increase in secretion of the lysosomal hydrolase cathepsin D
malfunction
-
no effects by siRNA-mediated OCRL1 knockdown on biosynthetic and postendocytic membrane traffic in renal epithelial cells, overview. Cells depleted of OCRL1 do not have significantly elevated levels of cellular PIP2 but display an increase in actin comet, OCRL1 knockdown results in a significant increase in secretion of the lysosomal hydrolase cathepsin D
malfunction
-
plasma membrane phosphatidylinositol-4,5-bisphosphate depletion by rapamycin-induced translocation of an inositol lipid 5-phosphatase or by a voltage-sensitive 5-phosphatase suppresses CaV1.2 and CaV1.3 channel currents by about 35% and CaV2.1 and CaV2.2 currents by 29% and 55%, respectively, mechanism, detailed overview. Other CaV channels are less sensitive. Inhibition of CaV channels by Dr-VSP is not simple voltage-dependent inhibition. Phosphatidylinositol-4,5-bisphosphate-dependent modulation of CaV2.2 channels and recovery requiring ATP and phosphatidylinositol-4,5-bisphosphate resynthesis, overview
malfunction
-
reduction of plasma membrane phosphatidylinositol 4,5-bisphosphate by low-level expression of the PIP2 phosphatase SigD or mutation of the PIP2 biosynthetic enzyme Skittles results in dramatic defects in spermatid cysts, which become bipolar and fail to fully elongate
malfunction
-
the phosphatidylinositol-4,5-bisphosphate 5-phosphatase OCRL is mutated in Lowe syndrome patients. Depletion of Rab35 or OCRL inhibits cytokinesis abscission and is associated with local abnormal PtdIns(4;5)P2 and F-actin accumulation in the intercellular bridge, pleiotropic phenotypes associated with Lowe disease, overview
malfunction
-
enzyme knockdown results in increased proliferation and anchorage-independent growth of melanocytes
malfunction
-
knockdown of SKIP results in thick myotubes with a larger number of nuclei than that in control cells and enhances the expression of myogenin mRNA
malfunction
mutations of isoform OCRL are related to Lowes syndrome and Dent disease characterized by renal failure
malfunction
-
depletion of SHIP2 attenuates cell polarization and migration, which is rescued by wild-type SHIP2 but not by a mutant defective in RhoA binding. In addition, the depletion of SHIP2 impairs the proper localization of phosphatidylinositol 3,4,5-trisphosphate, which is not restored by a mutant defective in RhoA binding
malfunction
-
expression of SKIP in C2C12 cells results in a slight decrease in myogenin expression and Akt phosphorylation after 48 h, with a marked decrease in MHC expression after 72 h. Expression of a phosphatase dead mutant in C2C12 cells does not show any effect
malfunction
-
in cells knocked down for OCRL, transfection of enzymatically active EGFP-OCRL-a (but not of a phosphatase-dead enzyme) decreases the levels of intracellular Listeria monocytogenes and of actin associated with invading bacteria
malfunction
-
in SHIP2 siRNA transfected cells, insulin treatment does not lead to alter the PIP3 level in contrast to SKIP or PTEN silenced cells. Results demonstrate that SHIP2 in contrast to SKIP is not involved in the regulation of insulin signaling in C2C12 cells
malfunction
-
in SKIP siRNA transfected cells, insulin treatment show an increase in PIP3 compared with control cells. Significant decrease in PI(3,4)P2 level is observed by the silencing of SKIP compared to control cells. PI(3,4)P2 levels are not altered in siRNA-transfected cells. Silencing of SKIP, increases the insulin-dependent recruitment of GLUT4 vesicles to the plasma membrane
malfunction
-
inactivation of OCRL by siRNA leads to an increase in the internalization levels of Listeria monocytogenes in HeLa cells. OCRL depletion does not increase but rather decreases the surface expression of the receptor Met
malfunction
-
SHIP1-/- neutrophils are extremely adherent, which results in impaired cell migration. Reduction in cell adhesion can rescue the defect in cell migration in SHIP1-/- neutrophils. Cell adhesion results in excessive Akt activation in SHIP1-/- cells
malfunction
-
silencing of SKIP increases IGF-II transcription and myoblast differentiation. Knockdown of SKIP results in thick myotubes with a larger number of nuclei than in control C2C12 cells
malfunction
-
enzyme depletion exclusively impairs apical secretory transport in intestinal epithelia. Enzyme loss leads to increased phosphatidylinositol 4,5-bisphosphate levels and overaccumulation of actin structures as well as intracellular accumulation of ARF-6 and UNC-16
malfunction
-
excess amounts of SHIP2 may be related, at least in part, to brain dysfunction in insulin resistance with type 2 diabetes. A dominant-negative mutant of SHIP2, expressed in cultured neurons, causes insulin signaling augmentation. Inhibition of SHIP2 ameliorates the impairment of hippocampal synaptic plasticity and memory formation in db/db mice
-
malfunction
-
mutant sac9-1 plants have a constitutively stressed phenotype with shorter roots which notably accumulate phosphatidylinositol 4,5-bisphosphate and its hydrolysis product inositol trisphosphate, phenotype with extreme abnormalities of cell wall and membrane structures in sac9-1 primary root cells, regardless of cell type, position within the meristematic area, and plane of section, overview
-
metabolism
-
proline-rich inositol polyphosphate 5-phosphatase is one of the signal-modifying enzymes that play pivotal regulatory roles in PI3K signalling pathway
metabolism
-
the enzyme negatively regulates myogenesis through inhibition of insulin-like growth factor-II production and attenuation of the insulin-like growth factor-II-Akt-mTOR signaling pathway
metabolism
-
SKIP controls PIP3 content in an insulin stimulation-dependent manner
metabolism
-
the interaction of the enzyme with ARF-6 curbs ARF-6 activity by limiting the access of ARF-6(GDP) to its guanine nucleotide exchange factor, BRIS-1
metabolism
-
proline-rich inositol polyphosphate 5-phosphatase is one of the signal-modifying enzymes that play pivotal regulatory roles in PI3K signalling pathway
-
physiological function
-
dOCRL is essential for cytokinesis and cell division, it dephosphorylates phosphatidylinositol-4,5-bisphosphate on internal membranes to restrict this phosphoinositide at the plasma membrane and thereby regulates cleavage furrow formation and ingression. dOCRL is required for proper furrowing of the contractile ring and proper assembly
physiological function
-
inositol 5-phosphatase SHIP2 is a negative regulator of PI(3,4,5)P3-dependent signaling, and it also negatively regulates PI(4,5)P2 levels and is concentrated at endocytic clathrin-coated pits via interactions with the scaffold protein intersectin. SHIP2 is recruited early at the pits and dissociates before fission, positive role of both SHIP2 substrates, PI(4,5)P2 and PI(3,4,5)P3, on coat assembly, overview
physiological function
no relevance of phosphatidylinositol-4,5-bisphosphate for the regulation of the specific ion channel type, termed TASK, and no requirement for the enzyme, overview
physiological function
-
nonredundant function of At5PTase7 in salt stress response by regulating ROS production and gene expression, involvement of the At5PTases in Arabidopsis salt tolerance, overview
physiological function
-
role for enzyme OCRL1 in membrane trafficking between the trans-Golgi network and endosomes, but OCRL1 does not directly modulate endocytosis or postendocytic membrane traffic
physiological function
-
role for enzyme OCRL1 in membrane trafficking between the trans-Golgi network and endosomes, but OCRL1 does not directly modulate endocytosis or postendocytic membrane traffic
physiological function
-
role of proline-rich inositol polyphosphate 5-phosphatase in early development of fertilized mouse eggs, via inhibition of Akt activity through inhibition of Akt phosphorylation at Ser473 and subsequent downstream signalling events
physiological function
SH2-containing inositol 5'-phosphatase 2, i.e. SHIP2, is a negative regulator of phosphatidylinositol 3,4,5-trisphosphate-mediated signals and shows physiological significance in neurons
physiological function
-
the bacterial phosphoinositide phosphatase SopB is a phosphoinositide phosphatase that, by dephosphorylation of phosphatidylinositol-4,5-bisphosphate at the plasma membrane, contributes to invasion and nascent Salmonella-containing vacuole biogenesis, and controls membrane surface charge of nascent Salmonella-containing vacuoles by reducing levels of negatively charged lipids phosphatidylinositol-4,5-bisphosphate and phosphatidylserine. This SopB activity results in dissociation of a number of hostcell endocytic trafficking proteins from this compartment and inhibits Salmonella-containing vacuole-lysosome fusion, mechanism, overview. SopB is required for efficient sealing of the Salmonella-containing vacuole membrane during invasion. SopB alters Rab protein recruitment to phagosomes
physiological function
-
the phosphatidylinositol-4,5-bisphosphate 5-phosphatase OCRL is a downstream effector of the Rab35 GTPase in cytokinesis abscission. PtdIns(4;5)P2 hydrolysis is important for normal cytokinesis abscission to locally remodel the F-actin cytoskeleton in the intercellular bridge, role for the phosphatase OCRL in cell division
physiological function
-
VPA0450 disrupts cytoskeletal binding sites on the inner surface of membranes of human cells and causes plasma membrane blebbing, which compromised membrane integrity and probably contributed to cell death by facilitating lysis. The effector VPA0450 causes cell rounding faster than the parental POR3 strain or the complemented strain during infection of HeLa cells
physiological function
-
the enzyme plays a tumor suppressive role in human melanoma. Enzyme overexpression blocks Akt activation, inhibits proliferation and undermines survival of melanoma cells in vitro, and retards melanoma growth in a xenograft model
physiological function
-
the enzyme regulates MyoD-mediated muscle differentiation
physiological function
-
by reducing the levels of PI(4,5)P2 and PI(3,4,5)P3 at the plasma membrane, OCRL restricts infection through modulation of actin dynamics at bacterial internalization sites
physiological function
-
during cell migration SHIP1 acts a negative regulator of PtdIns(3,4,5)P3 formation at the cell-substratum interface, preventing the formation of top-down PtdIns(3,4,5) P3 polarity and facilitating proper cell attachment and detachment during chemotaxis
physiological function
-
SHIP2 restricts PI(3,4,5)P3 localization at the leading edge in migrating cells to thereby control the cell polarity downstream of RhoA
physiological function
-
SKIP negatively regulates insulin signaling and glucose uptake by inhibiting GLUT4 docking and/or fusion to the plasma membrane
physiological function
-
SKIP negatively regulates myogenesis through inhibition of IGF-II production and attenuation of the IGF-II-Akt-mTOR signaling pathway. SKIP as a key regulator of muscle cell differentiation
physiological function
isoform INPP5E directly interacts with AURKA, a centrosomal kinase that regulates mitosis and ciliary disassembly. The interaction is important for the stability of primary cilia. AURKA phosphorylates INPP5E and thereby increases its 5-phosphatase activity, which in turn promotes transcriptional downregulation of AURKA, partly through an AKT-dependent mechanism
physiological function
-
nuclear phosphatidylinositol 5-phosphatase (PIP5Pase) interacts with repressor activator protein RAP1 in a multiprotein complex and functions in the control of variant surface glycoprotein allelic exclusion. RAP1 binds PIP5Pase substrate phosphatidylinositol 3,4,5-trisphosphate and catalytic mutation of PIP5Pase results in simultaneous transcription of variant surface glycoproteins from all telomeric expression sites and from silent subtelomeric variant surface glycoprotein arrays. PIP5Pase and RAP1 bind to telomeric expression sites, especially at 70-bp repeats and telomeres, and their binding is altered by PIP5Pase inactivation or knockdown
physiological function
-
SH2-containing inositol 5'-phosphatase 2, i.e. SHIP2, is a negative regulator of phosphatidylinositol 3,4,5-trisphosphate-mediated signals and shows physiological significance in neurons
-
physiological function
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role of proline-rich inositol polyphosphate 5-phosphatase in early development of fertilized mouse eggs, via inhibition of Akt activity through inhibition of Akt phosphorylation at Ser473 and subsequent downstream signalling events
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additional information
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GTP-bound, active Rab35 directly interacts with OCRL and controls its localization at the intercellular bridge
additional information
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Salmonella typhimurium uses a membrane-charge based mechanism to control Salmonella-containing vacuole maturation
additional information
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VPA0450 contains five of the six catalytic motifs found in the active site for the family of inositol polyphosphate 5-phosphatases, enzymes that specifically dephosphorylate the D5 phosphate on an inositol ring
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DELTA1-465
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the production of mutant DELTA466-787 containing the catalytic 5-phosphatase domain in DDd5P4 suppresses the growth of wild-type Legionella pneumophila, while the production of DELTA1-465 lacking the catalytic 5-phosphatase domain in Dd5P4-deficient host cells does not affect intracellular growth of the bacteria, indicating that catalytic activity of Dd5P4 is required to attenuate intracellular replication of Legionella pneumophila
DELTARhoGAPDd5P4
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transfection of dd5p4-null cells with a truncated Dd5P4 lacking the C-terminal RhoGAP domain does not restore endocytic defects, suggesting that the C-terminal RhoGAP domain is essential
C383S
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mutant with an almost entirely eliminated 3-phosphatase and 4-phosphatase activity, but a maintained 5-phosphatase activity also fails to rescue the endocytic defects in synj1-/- neurons
C392S
site-directed mutagenesis, inactivating mutation in the conserved CX5R(T/S) motif of the Sac domain
C641A
site-directed mutagenesis, the mutation removes the prenylation site of the enzyme
C910A
mutation of the C-terminal cysteine (C910A), which abolishes prenylation of INPP5B does not affect cellular targeting of INPP5B
D192A
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to assess the role of catalytic activity of SKIP on its suppressive effect, a phosphatase-negative mutant D192A is generated: 5-phosphatase activity is not required for the suppressive effect
D193/E195A
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binding activity is much lower compared to wild-type fragment consisting of amino acids 124-314. Binding activity for active RhoA is dramatically reduced compared to wild-type
D223/K224A
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binding activity is much lower compared to wild-type fragment consisting of amino acids 124-314
D524A
mutation of the aspartic acid within the conserved sequence PAWCDRIL in the 5-phosphatase domain which renders INPP5B catalytically inactive, has no effect on the targeting of INPP5B to the Golgi apparatus, ERGIC or endosomes
D556A
site-directed mutagenesis, inactivating point mutation of the conserved DRVL motif of INPP5E
D730A
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mutant with a deficient 5-phosphatase activity fails to rescue the endocytic defects in synj1-/- neurons
DELTA1-885/1186-1258
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the effects of SHIP2 on c-Jun NH2-terminal kinase (JNK) activity and JIP1 (JNK-interacting protein 1) tyrosine phosphorylation are independent of the SHIP2 phosphoinositide 5-phosphatase activity, as similar results are obtained when using a SHIP2 catalytic inactive mutant instead of wild-type SHIP2
DELTA237-893
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the N-terminal domain of OCRL1 is localized throughout the host cytoplasm and it binds Legionella pneumophila LpnE, a Sel1-like repeat protein involved in Legionella-containing vacuoles formation, which localizes to Legionella-containing vacuoles and selectively binds PtdIns(3)P
DELTA73-77
deletion of this LIDIA sequence motif within the N-terminal region of OCRL1 reveals that this sequence motif functions as a second clathrin binding domain in both isoforms
DELTAPIP2
expression of OCRL1 isoform a, but not isoform b, lacking the 5-phosphatase domain impairs transferrin endocytosis
G664D
G664D mutation shows little effect on binding to clathrin, alpha-adaptin, Rac1 or APPL1, while binding to Rabs 5 and 6 is almost completely abolished. The effects of G664D mutation are the same for both OCRL1 isoforms
P105E
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Glu in SHIP1 SH2 domain, faster association kinetics for binding to immobilized peptide VApYSYL
P686A/D690A/R691A
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catalytically inactive dominant-negative mutant inhibits proliferation of preadipocytes more potently than wild-type SHIP2. Phospho-Akt, phospho-ERK1/2, and PDGF receptor (PDGFR) levels are reduced in mutant-expressing preadipocytes. The inhibition of PDGF-activated mitogenic pathways by SHIP2 mutant is consistent with a decrease in PDGFR phosphorylation caused by a drop in receptor levels in SHIP2 mutant-expressing cells. SHIP2 mutant promotes ubiquitination of the PDGFR and its degradation via the lysosomal pathway independently of the association between the E3 ubiquitin ligase c-Cbl and PDGFR
P88S
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Ser in SHIP1 SH2 domain, faster association kinetics for binding to immobilized peptide VApYSYL
D480N
catalytically inactive 75-5ptase
P687A/D691A/R692G
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liver-specific expression of a dominant-negative SHIP2 mutant in hyperglycemic and hyperinsulinemic KKAy mice increases basal and insulin-stimulated Akt phosphorylation. Protein levels of glucose-6-phosphatase and phosphoenolpyruvate carboxykinase are reduced, and liver produces less glucose through gluconeogenesis. SHIP2 inhibition improves hepatic glycogen metabolism by modulating the phosphorylation states of glycogen phosphorylase and glycogen synthase, which increases hepatic glycogen content. Enhanced glucokinase and reduced pyruvate dehydrogenase kinase 4 expression, together with increased plasma triglycerides, indicate improved glycolysis. Liver-specific inhibition of SHIP2 improves glucose tolerance and markedly reduces prandial blood glucose levels in KKAy mice
E597Q
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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
D360A/N362A
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significant decrease in catalytic activity
D319A
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catalytically inactive mutant
D319A
-
inactive mutant bearing a mutation in 5-phosphatase catalytic domain. This mutant is not able to restore dd5p4-null cells
additional information
construction of catalytically inactive fra3 missense mutants with an amino acid substitution in the conserved motif II of the catalytic domain, FRA3 overexpressing transgenic plants do not show a phenotype
additional information
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construction of catalytically inactive fra3 missense mutants with an amino acid substitution in the conserved motif II of the catalytic domain, FRA3 overexpressing transgenic plants do not show a phenotype
additional information
disruption of the gene 5PTase13 results in shortened hypocotyls and expanded cotyledons. Suppression of 5PTase13 expression rescues the elongated hypocotyls in the phototropin1 or phototropin1 phototropin2 mutants. Further analysis shows that the blue light-induced elevation of cytosolic Ca2+ is inhibited in the phot1 mutant but enhanced in the 5pt13 mutant, suggesting that 5PTase13 antagonizes phototropin1-mediated effects on calcium signaling under blue light
additional information
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disruption of the gene 5PTase13 results in shortened hypocotyls and expanded cotyledons. Suppression of 5PTase13 expression rescues the elongated hypocotyls in the phototropin1 or phototropin1 phototropin2 mutants. Further analysis shows that the blue light-induced elevation of cytosolic Ca2+ is inhibited in the phot1 mutant but enhanced in the 5pt13 mutant, suggesting that 5PTase13 antagonizes phototropin1-mediated effects on calcium signaling under blue light
additional information
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random mutagensis and identification of mutant At5ptase7, that shows increased sensitivity, which is improved by overexpression. At5ptase7 mutants demonstrate reduced production of reactive oxygen species, phenotype, overview. Supplementation of mutants with exogenous PtdIns dephosphorylated at the D5' position restores ROS production, while PtdIns(4,5)P2, PtdIns(3,5)P2, or PtdIns(3,4,5)P3 are ineffective
additional information
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siRNA-mediated knockdown of oculocerebrorenal syndrome of Lowe, i.e. OCRL1 in epithelial cells, phenotype, overview
additional information
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direct interaction of SHIP2 with insulin receptor and filamin are evidenced in COS-7 cells
additional information
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in CHO cells, SHIP2 is found to form a complex with Cbl and Cbl-associated protein (CAP), two proteins potentially involved in insulin-induced glucose uptake
additional information
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expression of the human homolog OCRL (oculocerebrorenal syndrome of Lowe) in Dictyostelium discoideum dd5p4-null cells shows that expression of OCRL largely restores phagocytosis, growth and developmental defects of dd5p4-null cells, indicating that human OCRL can functionally replace Dictyostelium Dd5P4
additional information
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ectopically expressed Dd5P4 localizes to Legionella-containing vacuoles in Dictyostelium discoideum via an N-terminal domain. Dd5P4 is catalytically active on Legionella-containing vacuoles. Legionella pneumophilia replication and Legionella-containing vacuoles (LCV) formation occurres more efficiently in Dictyostelium discoideum amoebae lacking the Dd5P4, implicated in retrograde endosome to Golgi trafficking. The phenotype is complemented by Dd5P4 but not the catalytically inactive 5-phosphatase
additional information
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identification of mutants leading to Lowe oculocerebrorenal syndrome, MIM 309000
additional information
a deletion construct containing the N-terminus and 5-phosphatase domain (amino acids 1-564) of INPP5B is cytosolic, whereas a construct comprising the region downstream of the catalytic domain, including the RHO GAP-like domain and linker region connecting this to the catalytic domain (residues 564-913), is targeted to the Golgi to the wild-type protein. Further truncations of this C-terminal region abolishes membrane targeting, suggesting that both the linker and RHO GAP-like domains are required for correct cellular targeting
additional information
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a minimal catalytic construct D421-T730 is also sensitive to stimulation by phosphatidylserine
additional information
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cortical cultures are generated from 1-day-old Synj1 knockout and wild-type mice. Neurons are transfected with an synapto-pHluorin (spH) expression plasmid alone or cotransfected with spH and Flag- or HA-tagged human synaptojanin1 plasmid. Synaptojanin1 is required for normal vesicle endocytosis. Defects in both endocytosis and postendocytic vesicle reavailability can be fully restored upon reintroduction of synaptojanin1
additional information
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it is shown hat SHIP2 interacts with the adaptor protein APS in 3T3-L1 adipocytes and in transfected CHO-IR cells (Chinese hamster ovary cells stably transfected with the insulin receptor). SHIP2 negatively regulates APS insulin-induced tyrosine phosphorylation and consequently inhibits APS association with c-Cbl. Co-transfection of SHIP2 and APS in CHO-IR cells further increases the inhibitory effect of SHIP2 on Akt insulin-induced phosphorylation
additional information
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using the translocatable 5-phosphatase method, it is shown that upon addition of rapamycin, which causes a rapid depletion of D-myo-phosphatidylinositol 4,5-bisphosphate, Cx43 gap junctional communication is closed
additional information
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a rapamycin-inducible PI(4,5)P2 5-phosphatase is used to deplete PI(4,5)P2 in TRPV6-expressing cells. This technique is based on the translocation of the phosphatase domain of the PI(4,5)P2 5-phosphatase to the plasma membrane induced by rapamycin, which is shown to cause depletion of PI(4,5)P2. Rapamycin (100 nM) inhibits the whole-cell monovalent currents through TRPV6 channels expressing the rapamycin-inducible PI(4,5)P2 5-phosphatase constructs and has no effect in parallel controls
additional information
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ectopically expressed OCRL1 localizes to Legionella-containing vacuoles in Dictyostelium discoideum via an N-terminal domain
additional information
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hepatitis B virus core protein interacts with SKIP, both in vivo and in vitro. The minimal sequence required for interaction is the amino acid region from 116 to 149 for the core protein and the SKIP carboxyl homology (SKICH) domain for SKIP. When hepatitis B virus replicates in HuH-7 cells, overexpressed SKIP localizes to nucleus in addition to endoplasmic reticulum and suppresses heptitis B virus gene expression and replication. SKIP loses its nuclear localization and suppressive effect during replication of a core-negative HBV mutant
additional information
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in hepatitis B virus infected HuH-7 cells, HBV gene expression is enhanced significantly when endogenous SKIP expression is knocked down by a SKIP-specific siRNA
additional information
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mutation analysis show that the suppression domain of SKIP localises to amino acids 199-226
additional information
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downregulation of the enzyme in HeLa cells by RNAi
additional information
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siRNA-mediated knockdown of oculocerebrorenal syndrome of Lowe, i.e. OCRL1 in epithelial cells, phenotype, overview
additional information
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using different fragments of SHIP2 it is shown that the SHIP2-NDELTASH2-4 fragment (124-314 amino acids) is sufficient to bind to RhoA. These results indicate that active RhoA directly interacts with SHIP2 at the N-terminal region between the SH2 and catalytic domains
additional information
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by genetic inactivation Src homology 2 (SH2) domain-containing inositol-5-phosphatase 1 (SHIP1) it is shown that it is a key regulator of neutrophil migration and that genetic inactivation of SHIP1 leads to severe defects in neutrophil polarization and motility
additional information
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in SHIP2 deficient mouse embryonic fibroblasts (MEFs) stimulated by H2O2 at 15 min, PtdIns(3,4,5)P3 is increased as compared to +/+ cells. No significant increase in PtdIns(3,4)P2 can be detected at 15 or 120 min incubation of the cells with H2O2 (0.6 mM). PKB activity is also upregulated in SHIP2 -/- cells as compared to +/+ cells in response to H2O2
additional information
in the absence of insulin stimulation and phosphatidylinositol 3,4,5-triphosphate generation, wild type, but not catalytically inactive D480N mutant, promotes GLUT4 translocation and insertion into the plasma membrane but not glucose uptake
additional information
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liver-specific overexpresion of wild-type SHIP2 or a dominant-negative mutant in mice by adenoviral vector injection leads to inhibition of insulin-induced Akt activation, glucose metabolism and hepatic gene expression using wild-type SHIP2 while the dominant negative mutant fails to do so
additional information
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overexpression of SHIP2 in L6 myotubes and B lymphocytes results in inhibition of both Akt-dependent and ERK1/2-dependent pathways stimulated by insulin. Expression of a dominant negative SHIP2 mutant in 3T3-L1 adipocytes results in inactivation of insulin signaling through the PI-3 kinase/Akt pathway. However, when SHIP2 is knocked down by RNA silencing in 3T3-L1 adipocytes, no effects are observed, suggesting that loss of SHIP2 function has no impact on insulin singnaling in 3T3-L1 adipocytes
additional information
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SHIP-2 gene is knockdown in bone marrow-derived mast cells (BMMCs) by using the lentiviral-based RNA interference technique. Elimination results in both increased mast cell degranulation and cytokine (IL-4 and IL-13) gene expression upon FcepsilonRI stimulation. Absence of SHIP-2 results in increased activation of the small GTPase Rac-1 and in enhanced microtubule polymerization upon FcepsilonRI engagement
additional information
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SHIP2 knock out mice (deletion of the first 18 exons of the SHIP2 gene) exhibit enhanced PtdIns 3-kinase-dependent signalling, alteration in lipid metabolism and energy expenditure. SHIP2 knock-out mice fed with a high-fat diet are resistant to weight gain and do not become hyperglycemic or insulin resistant
additional information
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overexpression of FLAG-tagged proline-rich inositol polyphosphate 5-phosphatase in eggs affects localization of phosphorylated Akt at Ser473, egg cell division, MPF activity, and dephosphorylation of cdc2 at Tyr15
additional information
transgenic mice overexpressing SHIP2 show increased amounts of SHIP2 inducing the disruption of insulin/IGF-I signaling through Akt. Neuroprotective effects of insulin and IGF-I are significantly attenuated in cultured cerebellar granule neurons from SHIP2 transgenic mice, the number of apoptosis-positive cells is increased in cerebral cortex of the transgenic mice at an elderly age, phenotype, overview
additional information
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transgenic mice overexpressing SHIP2 show increased amounts of SHIP2 inducing the disruption of insulin/IGF-I signaling through Akt. Neuroprotective effects of insulin and IGF-I are significantly attenuated in cultured cerebellar granule neurons from SHIP2 transgenic mice, the number of apoptosis-positive cells is increased in cerebral cortex of the transgenic mice at an elderly age, phenotype, overview
additional information
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transgenic mice overexpressing SHIP2 show increased amounts of SHIP2 inducing the disruption of insulin/IGF-I signaling through Akt. Neuroprotective effects of insulin and IGF-I are significantly attenuated in cultured cerebellar granule neurons from SHIP2 transgenic mice, the number of apoptosis-positive cells is increased in cerebral cortex of the transgenic mice at an elderly age, phenotype, overview
-
additional information
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overexpression of FLAG-tagged proline-rich inositol polyphosphate 5-phosphatase in eggs affects localization of phosphorylated Akt at Ser473, egg cell division, MPF activity, and dephosphorylation of cdc2 at Tyr15
-
additional information
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whole body insulin sensitivity is examined in vivo by insulin tolerance tests before and after the intraperitoneal application of an SHIP2-antisense oligonucleotide. Treatment with a SHIP2-antisense oligonucleotide can rapidly improve muscle insulin sensitivity in dietary insulin resistance
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Matzaris, M.; Jackson, S.P.; Laxminarayan, K.M.; Speed, C.J.; Mitchell, C.A.
Identification and characterization of the phosphatidylinositol-(4,5)-bisphosphate 5-phosphatase in human platelets
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Homo sapiens
brenda
Dawson, R.M.C.; Thompson, W.
The triphosphoinositide phosphomonoesterase of brain tissue
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Bos taurus
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Evidence for a specific phosphatidylinositol 4-phosphate phosphatase in human erythrocyte membranes
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1984
Canis lupus familiaris, Homo sapiens, Oryctolagus cuniculus, Ovis aries, Platyrrhini, Rattus norvegicus
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Mack, S.E.; Palmer, F.B.St.C.
Soluble and membrane-bound polyphosphoinositide phosphohydrolases in mammalian erythrocytes
Biochem. Cell Biol.
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1988
Oryctolagus cuniculus, Ovis aries, Homo sapiens, Rattus norvegicus, Sus scrofa
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Koutouzov, S.; Marche, P.
The Mg2+-activated phosphatidylinositol 4,5-bisphosphate-specific phosphomonoesterase of erythrocyte membrane
FEBS Lett.
144
16-20
1982
Rattus norvegicus
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Roach, P.D.; Palmer, F.B.St.C.
Human erythrocyte cytosol phosphatidyl-inositol-bisphosphate phosphatase
Biochim. Biophys. Acta
661
323-333
1981
Homo sapiens
brenda
Palmer, F.B.St.C.
The phosphatidyl-myo-inositol-4,5-biphosphate phosphatase from Crithidia fasciculata
Can. J. Biochem.
59
469-476
1981
Crithidia fasciculata
brenda
Akhtar, R.A.; Abdel-Latif, A.A.
Studies on the properties of triphosphoinositide phosphomonoesterase and phosphodiesterase of rabbit iris smooth muscle
Biochim. Biophys. Acta
527
159-170
1978
Oryctolagus cuniculus
brenda
Whiting, P.H.; Palmano, K.P.; Hawthorne, J.N.
Enzymes of myo-inositol and inositol lipid metabolism in rats with streptozotocin-induced diabetes
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Rattus norvegicus
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Sheltawy, A.; Brammer, M.; Borrill, D.
The subcellular distribution of triphosphoinositide phosphomonoesterase in guinea-pig brain
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Cavia porcellus
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Cooper, P.H.; Hawthorne, J.N.
Phosphomonoesterase hydrolysis of polyphosphoinositides in rat kidney: Properties and subcellular localization of the enzyme system
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150
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Rattus norvegicus
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Lefebvre, Y.A.; White, D.A.; Hawthorne, J.N.
Diphosphoinositide metabolism in bovine adrenal medulla
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Bos taurus
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Abdel-Latif, A.; Akhtar, R.A.; Hawthorne, J.
Acetylcholine increases breakdown of triphosphoinositide of rabbit iris muscle prelabelled with phosphate
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Oryctolagus cuniculus
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Phosphatidylinositol 4,5-bisphosphate phosphatase regulates the rearrangement of actin filaments
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17
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Bos taurus
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Zhang, X.; Jefferson, A.B.; Auethavekiat, V.; Majerus, P.W.
The protein deficient in Lowe syndrome is a phosphatidylinositol-4,5-bisphosphate 5-phosphatase
Proc. Natl. Acad. Sci. USA
92
4853-4856
1995
Homo sapiens
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Zhang, X.; Hartz, P.A.; Philip, E.; Racusen, L.C.; Majerus, P.W.
Cell lines from kidney proximal tubules of a patient with Lowe syndrome lack OCRL inositol polyphosphate 5-phosphatase and accumulate phosphatidylinositol 4,5-bisphosphate
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273
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Homo sapiens
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Lowe syndrome, a deficiency of a phosphatidyl-inositol 4,5-bisphosphate 5-phosphatase in the Golgi apparatus
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Homo sapiens
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Palmer, F.B.S.C.
Enzymes that degrade phosphatidylinositol 4-phosphate and phosphatidylinositol 4,5-bisphosphate have different developmental profiles in chick brain
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Gallus gallus
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Palmer, F.B.S.C.; Theolis, R.; Cook, H.W.; Byers, D.M.
Purification of two immunologically related phosphatidylinositol-(4,5)-bisphosphate phosphatases from bovine brain cytosol
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Kong, A.M.; Speed, C.J.; O'Malley, C.J.; Layton, M.J.; Meehan, T.; Loveland, K.L.; Cheema, S.; Ooms, L.M.; Mitchell, C.A.
Cloning and characterization of a 72-kDa inositol-polyphosphate 5-phosphatase localized to the Golgi network
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Roschinger, W.; Muntau, A.C.; Rudolph, G.; Roscher, A.A.; Kammerer, S.
Carrier assessment in families with Lowe oculocerebrorenal syndrome: Novel mutations in the OCRL1 gene and correlation of direct DNA diagnosis with ocular examination
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Johenning, F.W.; Wenk, M.R.; Uhlen, P.; Degray, B.; Lee, E.; De Camilli, P.; Ehrlich, B.E.
InsP3-mediated intracellular calcium signalling is altered by expression of synaptojanin-1
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Type II phosphoinositide 5-phosphatases have unique sensitivities towards fatty acid composition and head group phosphorylation
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Morales-Johansson, H.; Jenoe, P.; Cooke, F.T.; Hall, M.N.
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Comparative mechanistic and substrate specificity study of inositol polyphosphate 5-phosphatase Schizosaccharomyces pombe Synaptojanin and SHIP2
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Zhong, R.; Burk, D.H.; Morrison, W.H., 3rd; Ye, Z.H.
FRAGILE FIBER3, an Arabidopsis gene encoding a type II inositol polyphosphate 5-phosphatase, is required for secondary wall synthesis and actin organization in fiber cells
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Arabidopsis thaliana (Q84W55), Arabidopsis thaliana
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Zhong, R.; Ye, Z.H.
Molecular and biochemical characterization of three WD-repeat-domain-containing inositol polyphosphate 5-phosphatases in Arabidopsis thaliana
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Arabidopsis thaliana (Q9SKB7), Arabidopsis thaliana
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Buettner, R.; Ottinger, I.; Gerhardt-Salbert, C.; Wrede, C.E.; Schoelmerich, J.; Bollheimer, L.C.
Antisense oligonucleotides against the lipid phosphatase SHIP2 improve muscle insulin sensitivity in a dietary rat model of the metabolic syndrome
Am. J. Physiol. Endocrinol. Metab.
292
E1871-E1878
2007
Rattus norvegicus
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Vinciguerra, M.; Foti, M.
PTEN and SHIP2 phosphoinositide phosphatases as negative regulators of insulin signalling
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2006
Chlorocebus aethiops, Cricetulus griseus, Mus musculus
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Batty, I.H.; van der Kaay, J.; Gray, A.; Telfer, J.F.; Dixon, M.J.; Downes, C.P.
The control of phosphatidylinositol 3,4-bisphosphate concentrations by activation of the Src homology 2 domain containing inositol polyphosphate 5-phosphatase 2, SHIP2
Biochem. J.
407
255-266
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Homo sapiens, Mus musculus (Q9JII1)
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Andersen, J.F.; Ribeiro, J.M.
A secreted salivary inositol polyphosphate 5-phosphatase from a blood-feeding insect: allosteric activation by soluble phosphoinositides and phosphatidylserine
Biochemistry
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2006
Rhodnius prolixus
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Vaillancourt, M.; Levasseur, S.; Tremblay, M.L.; Marois, L.; Rollet-Labelle, E.; Naccache, P.H.
The Src homology 2-containing inositol 5-phosphatase 1 (SHIP1) is involved in CD32a signaling in human neutrophils
Cell. Signal.
18
2022-2032
2006
Homo sapiens
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Vandeput, F.; Backers, K.; Villeret, V.; Pesesse, X.; Erneux, C.
The influence of anionic lipids on SHIP2 phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase activity
Cell. Signal.
18
2193-2199
2006
Homo sapiens
brenda
Zhang, J.; Liu, Z.; Rasschaert, J.; Blero, D.; Deneubourg, L.; Schurmans, S.; Erneux, C.; Pesesse, X.
SHIP2 controls PtdIns(3,4,5)P(3) levels and PKB activity in response to oxidative stress
Cell. Signal.
19
2194-2200
2007
Mus musculus
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Grempler, R.; Zibrova, D.; Schoelch, C.; van Marle, A.; Rippmann, J.F.; Redemann, N.
Normalization of prandial blood glucose and improvement of glucose tolerance by liver-specific inhibition of SH2 domain containing inositol phosphatase 2 (SHIP2) in diabetic KKAy mice: SHIP2 inhibition causes insulin-mimetic effects on glycogen metabolism
Diabetes
56
2235-2241
2007
Mus musculus
brenda
Bertelli, D.F.; Araujo, E.P.; Cesquini, M.; Stoppa, G.R.; Gasparotto-Contessotto, M.; Toyama, M.H.; Felix, J.V.; Carvalheira, J.B.; Michelini, L.C.; Chiavegatto, S.; Boschero, A.C.; Saad, M.J.; Lopes-Cendes, I.; Velloso, L.A.
Phosphoinositide-specific inositol polyphosphate 5-phosphatase IV inhibits inositide trisphosphate accumulation in hypothalamus and regulates food intake and body weight
Endocrinology
147
5385-5399
2006
Rattus norvegicus
brenda
Kimata, T.; Nagaki, M.; Ogiso, T.; Naiki, T.; Kato, T.; Moriwaki, H.
Actin organization and hepatocyte differentiation are regulated by extracellular matrix via PI-4,5-bisphosphate in the rat
Hepatology
44
140-151
2006
Rattus norvegicus
brenda
van Zeijl, L.; Ponsioen, B.; Giepmans, B.N.; Ariaens, A.; Postma, F.R.; Varnai, P.; Balla, T.; Divecha, N.; Jalink, K.; Moolenaar, W.H.
Regulation of connexin43 gap junctional communication by phosphatidylinositol 4,5-bisphosphate
J. Cell Biol.
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881-891
2007
Homo sapiens
brenda
Williams, C.; Choudhury, R.; McKenzie, E.; Lowe, M.
Targeting of the type II inositol polyphosphate 5-phosphatase INPP5B to the early secretory pathway
J. Cell Sci.
120
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2007
Homo sapiens (P32019)
brenda
Onnockx, S.; De Schutter, J.; Blockmans, M.; Xie, J.; Jacobs, C.; Vanderwinden, J.M.; Erneux, C.; Pirson, I.
The association between the SH2-containing inositol polyphosphate 5-Phosphatase 2 (SHIP2) and the adaptor protein APS has an impact on biochemical properties of both partners
J. Cell. Physiol.
214
260-272
2008
Homo sapiens
brenda
Leung, W.H.; Bolland, S.
The inositol 5-phosphatase SHIP-2 negatively regulates IgE-induced mast cell degranulation and cytokine production
J. Immunol.
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95-102
2007
Mus musculus
brenda
Nishio, M.; Watanabe, K.; Sasaki, J.; Taya, C.; Takasuga, S.; Iizuka, R.; Balla, T.; Yamazaki, M.; Watanabe, H.; Itoh, R.; Kuroda, S.; Horie, Y.; Foerster, I.; Mak, T.W.; Yonekawa, H.; Penninger, J.M.; Kanaho, Y.; Suzuki, A.; Sasaki, T.
Control of cell polarity and motility by the PtdIns(3,4,5)P3 phosphatase SHIP1
Nat. Cell Biol.
9
36-44
2007
Mus musculus
brenda
Mani, M.; Lee, S.Y.; Lucast, L.; Cremona, O.; Di Paolo, G.; De Camilli, P.; Ryan, T.A.
The dual phosphatase activity of synaptojanin1 is required for both efficient synaptic vesicle endocytosis and reavailability at nerve terminals
Neuron
56
1004-1018
2007
Homo sapiens
brenda
Chen, X.; Lin, W.H.; Wang, Y.; Luan, S.; Xue, H.W.
An inositol polyphosphate 5-phosphatase functions in PHOTOTROPIN1 signaling in Arabidopis by altering cytosolic Ca2+
Plant Cell
20
353-366
2008
Arabidopsis thaliana (Q9SYK4), Arabidopsis thaliana
brenda
Perera, R.M.; Zoncu, R.; Lucast, L.; De Camilli, P.; Toomre, D.
Two synaptojanin 1 isoforms are recruited to clathrin-coated pits at different stages
Proc. Natl. Acad. Sci. USA
103
19332-19337
2006
Homo sapiens
brenda
Loovers, H.M.; Kortholt, A.; de Groote, H.; Whitty, L.; Nussbaum, R.L.; van Haastert, P.J.
Regulation of phagocytosis in Dictyostelium by the inositol 5-phosphatase OCRL homolog Dd5P4
Traffic
8
618-628
2007
Dictyostelium discoideum
brenda
Hung, C.S.; Lin, Y.L.; Wu, C.I.; Huang, C.J.; Ting, L.P.
Suppression of hepatitis B viral gene expression by phosphoinositide 5-phosphatase SKIP
Cell. Microbiol.
11
37-50
2009
Homo sapiens
brenda
Weber, S.S.; Ragaz, C.; Hilbi, H.
The inositol polyphosphate 5-phosphatase OCRL1 restricts intracellular growth of Legionella, localizes to the replicative vacuole and binds to the bacterial effector LpnE
Cell. Microbiol.
11
442-460
2008
Dictyostelium discoideum, Homo sapiens, Mus musculus
brenda
Xie, J.; Onnockx, S.; Vandenbroere, I.; Degraef, C.; Erneux, C.; Pirson, I.
The docking properties of SHIP2 influence both JIP1 tyrosine phosphorylation and JNK activity
Cell. Signal.
20
1432-1441
2008
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
Xie, J.; Vandenbroere, I.; Pirson, I.
SHIP2 associates with intersectin and recruits it to the plasma membrane in response to EGF
FEBS Lett.
582
3011-3017
2008
Homo sapiens
brenda
Thyagarajan, B.; Lukacs, V.; Rohacs, T.
Hydrolysis of phosphatidylinositol 4,5-bisphosphate mediates calcium-induced inactivation of TRPV6 channels
J. Biol. Chem.
283
14980-14987
2008
Homo sapiens
brenda
Choudhury, R.; Noakes, C.J.; McKenzie, E.; Kox, C.; Lowe, M.
Differential clathrin binding and subcellular localization of OCRL1 splice isoforms
J. Biol. Chem.
284
9965-9973
2009
Homo sapiens (Q01968)
brenda
Artemenko, Y.; Gagnon, A.; Sorisky, A.
Catalytically inactive SHIP2 inhibits proliferation by attenuating PDGF signaling in 3T3-L1 preadipocytes
J. Cell. Physiol.
218
228-236
2009
Homo sapiens
brenda
Zhang, Y.; Wavreille, A.S.; Kunys, A.R.; Pei, D.
The SH2 domains of inositol polyphosphate 5-phosphatases SHIP1 and SHIP2 have similar ligand specificity but different binding kinetics
Biochemistry
48
11075-11083
2009
Homo sapiens
brenda
Cui, S.; Guerriero, C.; Szalinski, C.; Kinlough, C.; Hughey, R.; Weisz, O.
OCRL1 function in renal epithelial membrane traffic
Am. J. Physiol. Renal Physiol.
298
F335-F345
2010
Canis lupus familiaris, Homo sapiens
brenda
Bakowski, M.A.; Braun, V.; Lam, G.Y.; Yeung, T.; Heo, W.D.; Meyer, T.; Finlay, B.B.; Grinstein, S.; Brumell, J.H.
The phosphoinositide phosphatase SopB manipulates membrane surface charge and trafficking of the Salmonella-containing vacuole
Cell Host Microbe
7
453-462
2010
Salmonella enterica
brenda
Deng, X.; Feng, C.; Wang, E.H.; Zhu, Y.Q.; Cui, C.; Zong, Z.H.; Li, G.S.; Liu, C.; Meng, J.; Yu, B.Z.
Influence of proline-rich inositol polyphosphate 5-phosphatase, on early development of fertilized mouse eggs, via inhibition of phosphorylation of Akt
Cell Prolif.
44
156-165
2011
Mus musculus, Mus musculus Kunming
brenda
Ben El Kadhi, K.; Roubinet, C.; Solinet, S.; Emery, G.; Carreno, S.
The inositol 5-phosphatase dOCRL controls PI(4,5)P2 homeostasis and is necessary for cytokinesis
Curr. Biol.
21
1074-1079
2011
Drosophila melanogaster
brenda
Nakatsu, F.; Perera, R.; Lucast, L.; Zoncu, R.; Domin, J.; Gertler, F.; Toomre, D.; De Camilli, P.
The inositol 5-phosphatase SHIP2 regulates endocytic clathrin-coated pit dynamics
J. Cell Biol.
190
307-315
2010
Mus musculus
brenda
Lindner, M.; Leitner, M.G.; Halaszovich, C.R.; Hammond, G.R.; Oliver, D.
Probing the regulation of TASK potassium channels by PI(4,5)P2 with switchable phosphoinositide phosphatases
J. Physiol.
589
3149-3162
2011
Homo sapiens (Q9NRR6)
brenda
Fabian, L.; Wei, H.; Rollins, J.; Noguchi, T.; Blankenship, J.; Bellamkonda, K.; Polevoy, G.; Gervais, L.; Guichet, A.; Fuller, M.; Brill, J.
Phosphatidylinositol 4,5-bisphosphate directs spermatid cell polarity and exocyst localization in Drosophila
Mol. Biol. Cell
21
1546-1555
2010
Drosophila melanogaster
brenda
Soeda, Y.; Tsuneki, H.; Muranaka, H.; Mori, N.; Hosoh, S.; Ichihara, Y.; Kagawa, S.; Wang, X.; Toyooka, N.; Takamura, Y.; Uwano, T.; Nishijo, H.; Wada, T.; Sasaoka, T.
The inositol phosphatase SHIP2 negatively regulates insulin/IGF-I actions implicated in neuroprotection and memory function in mouse brain
Mol. Endocrinol.
24
1965-1977
2010
Mus musculus (Q6P549), Mus musculus, Mus musculus C57/BL6J (Q6P549)
brenda
Dambournet, D.; MacHicoane, M.; Chesneau, L.; Sachse, M.; Rocancourt, M.; El Marjou, A.; Formstecher, E.; Salomon, R.; Goud, B.; Echard, A.
Rab35 GTPase and OCRL phosphatase remodel lipids and F-actin for successful cytokinesis
Nat. Cell Biol.
13
981-988
2011
Homo sapiens
brenda
Suh, B.; Leal, K.; Hille, B.
Modulation of high-voltage activated Ca2+ channels by membrane phosphatidylinositol 4,5-bisphosphate
Neuron
67
224-238
2010
Danio rerio
brenda
Kaye, Y.; Golani, Y.; Singer, Y.; Leshem, Y.; Cohen, G.; Ercetin, M.; Gillaspy, G.; Levine, A.
Inositol polyphosphate 5-phosphatase7 regulates the production of reactive oxygen species and salt tolerance in Arabidopsis
Plant Physiol.
157
229-241
2011
Arabidopsis thaliana
brenda
Vollmer, A.H.; Youssef, N.N.; Dewald, D.B.
Unique cell wall abnormalities in the putative phosphoinositide phosphatase mutant AtSAC9
Planta
234
993-1005
2011
Arabidopsis thaliana, Arabidopsis thaliana CS1092
brenda
Broberg, C.; Zhang, L.; Gonzalez, H.; Laskowski-Arce, M.; Orth, K.
A Vibrio effector protein is an inositol phosphatase and disrupts host cell membrane integrity
Science
329
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2010
Vibrio parahaemolyticus
brenda
Miyazawa, K.
Phosphoinositide 5-phosphatases: How do they affect tumourigenesis?
J. Biochem.
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1-3
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Homo sapiens (Q9NRR6)
brenda
Ijuin, T.; Takenawa, T.
Role of phosphatidylinositol 3,4,5-trisphosphate (PIP3) 5-phosphatase skeletal muscle- and kidney-enriched inositol polyphosphate phosphatase (SKIP) in myoblast differentiation
J. Biol. Chem.
287
31330-31341
2012
Homo sapiens, Mus musculus
brenda
Ye, Y.; Jin, L.; Wilmott, J.S.; Hu, W.L.; Yosufi, B.; Thorne, R.F.; Liu, T.; Rizos, H.; Yan, X.G.; Dong, L.; Tay, K.H.; Tseng, H.Y.; Guo, S.T.; de Bock, C.E.; Jiang, C.C.; Wang, C.Y.; Wu, M.; Zhang, L.J.; Hersey, P.; Scolyer, R.A.; Zhang, X.D.
PI(4,5)P2 5-phosphatase A regulates PI3K/Akt signalling and has a tumour suppressive role in human melanoma
Nat. Commun.
4
1508
2013
Homo sapiens
brenda
Braun, W.; Schein, C.
Membrane interaction and functional plasticity of inositol polyphosphate 5-phosphatases
Structure
22
664-666
2014
Homo sapiens, Homo sapiens (P32019)
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 (P32019), Homo sapiens (Q01968), Homo sapiens
brenda
Kuehbacher, A.; Dambournet, D.; Echard, A.; Cossart, P.; Pizarro-Cerda, J.
Phosphatidylinositol 5-phosphatase oculocerebrorenal syndrome of Lowe protein (OCRL) controls actin dynamics during early steps of Listeria monocytogenes infection
J. Biol. Chem.
287
13128-13136
2012
Listeria monocytogenes
brenda
Ijuin, T.; Takenawa, T.
Regulation of insulin signaling and glucose transporter 4 (GLUT4) exocytosis by phosphatidylinositol 3,4,5-trisphosphate (PIP3) phosphatase, skeletal muscle, and kidney enriched inositol polyphosphate phosphatase (SKIP)
J. Biol. Chem.
287
6991-6999
2012
Mus musculus
brenda
Mondal, S.; Subramanian, K.K.; Sakai, J.; Bajrami, B.; Luo, H.R.
Phosphoinositide lipid phosphatase SHIP1 and PTEN coordinate to regulate cell migration and adhesion
Mol. Biol. Cell
23
1219-1230
2012
Mus musculus
brenda
Kato, K.; Yazawa, T.; Taki, K.; Mori, K.; Wang, S.; Nishioka, T.; Hamaguchi, T.; Itoh, T.; Takenawa, T.; Kataoka, C.; Matsuura, Y.; Amano, M.; Murohara, T.; Kaibuchi, K.
The inositol 5-phosphatase SHIP2 is an effector of RhoA and is involved in cell polarity and migration
Mol. Biol. Cell
23
2593-2604
2012
Homo sapiens
brenda
Mills, S.J.; Silvander, C.; Cozier, G.; Tresaugues, L.; Nordlund, P.; Potter, B.V.
Crystal Structures of type-II inositol polyphosphate 5-phosphatase INPP5B with synthetic inositol polyphosphate surrogates reveal new mechanistic insights for the inositol 5-phosphatase family
Biochemistry
55
1384-1397
2016
Homo sapiens (P32019)
brenda
Kume, A.; Kawase, K.; Komenoi, S.; Usuki, T.; Takeshita, E.; Sakai, H.; Sakane, F.
The pleckstrin homology domain of diacylglycerol kinase eta strongly and selectively binds to phosphatidylinositol 4,5-bisphosphate
J. Biol. Chem.
291
8150-8161
2016
Homo sapiens
brenda
Chen, D.; Yang, C.; Liu, S.; Hang, W.; Wang, X.; Chen, J.; Shi, A.
SAC-1 ensures epithelial endocytic recycling by restricting ARF-6 activity
J. Cell Biol.
217
2121-2139
2018
Caenorhabditis elegans
brenda
Plotnikova, O.; Seo, S.; Cottle, D.; Conduit, S.; Hakim, S.; Dyson, J.; Mitchell, C.; Smyth, I.
INPP5E interacts with AURKA, linking phosphoinositide signaling to primary cilium stability
J. Cell Sci.
128
364-372
2015
Mus musculus (Q9JII1)
brenda
Cestari, I.; McLeland-Wieser, H.; Stuart, K.
Nuclear phosphatidylinositol 5-phosphatase is essential for allelic exclusion of variant surface glycoprotein genes in trypanosomes
Mol. Cell. Biol.
39
e00395-18
2019
Trypanosoma brucei
brenda
Keum, D.; Kruse, M.; Kim, D.I.; Hille, B.; Suh, B.C.
Phosphoinositide 5- and 3-phosphatase activities of a voltage-sensing phosphatase in living cells show identical voltage dependence
Proc. Natl. Acad. Sci. USA
113
E3686-E3695
2016
Danio rerio (B3IUN7)
brenda