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Information on EC 3.1.3.36 - phosphoinositide 5-phosphatase
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3.1.3.36 phosphoinositide 5-phosphataseIUBMB Comments
These enzymes can also remove the 5-phosphate from Ins(1,4,5)P3 and/or Ins(1,3,4,5)P4. They are a diverse family of enzymes, with differing abilities to catalyse two or more of the four reactions listed. They are thought to use inositol lipids rather than inositol phosphates as substrates in vivo. All of them can use either or both of PtdIns(4,5)P2 and PtdIns(3,4,5)P3 as substrates; this is the main property that distinguishes them from EC 3.1.3.56, inositol-polyphosphate 5-phosphatase.
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Word Map
- 3.1.3.36
-
endocytosis
- phosphatases
- synaptic
- actin
-
domain-containing
- 3-kinase
- pten
-
endocytic
-
x-linked
-
ptdins3,4,5p3
- dynamin
- cataract
- clathrin
-
clathrin-mediated
- cilia
-
endophilins
-
clathrin-coated
-
tensin
- dent
-
voltage-sensing
-
polyphosphoinositide
- amphiphysins
-
joubert
-
ptdins3,4p2
- ciliopathies
- 1,3,4,5-tetrakisphosphate
-
ptdins4p
- grb2
-
tubulopathy
-
tyrosine-based
-
immunoreceptor
-
itims
- ship-1
- 3,4-bisphosphate
-
pleckstrin
-
fcgammariib
-
ciliogenesis
-
4-phosphatase
-
intersectin
-
hypercalciuria
- phosphatidylinositol-3,4,5-trisphosphate
-
microrna-155
-
nephrocalcinosis
- myotubularins
- 3,4,5-triphosphate
- eps15
-
myotubular
-
n-wasp
- phosphoinositol
- inpp4b
- molecular biology
- medicine
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Synonyms
ship2, ship1, ocrl1, synaptojanin, inpp5e, synj1, phosphoinositide phosphatase, inositol polyphosphate 5-phosphatase, ci-vsp, inositol 5-phosphatase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
5PTase
dOCRL
-
orthologue of the human oculocerebrorenal syndrome of Lowe 1, i.e. OCRL1
inositol 5-phosphatase
inositol phosphatase
inositol polyphosphate 5-phosphatase
INP51
INPP5B
INPP5E
IP5P
OCRL
OCRL1
OCRL1a
OCRL1 exists as two slice isoforms that differ by a single exon encoding 8 amino acids. The longer protein, termed isoform a, is the only form in brain, while both isoforms are present in all other tissues
phosphatidylinositol 4,5-bisphosphate phosphatase
Phosphoinositide 5-phosphatase
phosphoinositide phosphatase
PI(4,5)P2 5-phosphatase
PIP2 5-phosphatase
PIP2 phosphatase
PIPP
proline-rich inositol polyphosphate 5-phosphatase
SAC9
SH2-containing inositol 5'-phosphatase 2
SHIP1
SHIP2
SKIP
Synaptojanin
synaptojanin1
type II inositol polyphosphate 5-phosphatase
type II phosphoinositide 5-phosphatase
VSP
additional information
additional information
-
the enzyme belongs to the endonuclease/exonuclease/phosphatase family
additional information
cf. EC 3.1.3.56, inositol polyphosphate 5-phosphatase
additional information
cf. EC 3.1.3.56, inositol polyphosphate 5-phosphatase
additional information
-
cf. EC 3.1.3.56, inositol polyphosphate 5-phosphatase
additional information
-
cf. EC 3.1.3.56, inositol polyphosphate 5-phosphatase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
catalytic and kinetic reaction mechanism, substrate binding, overview
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SYSTEMATIC NAME
IUBMB Comments
phosphatidyl-myo-inositol-4,5-bisphosphate 4-phosphohydrolase
These enzymes can also remove the 5-phosphate from Ins(1,4,5)P3 and/or Ins(1,3,4,5)P4. They are a diverse family of enzymes, with differing abilities to catalyse two or more of the four reactions listed. They are thought to use inositol lipids rather than inositol phosphates as substrates in vivo. All of them can use either or both of PtdIns(4,5)P2 and PtdIns(3,4,5)P3 as substrates; this is the main property that distinguishes them from EC 3.1.3.56, inositol-polyphosphate 5-phosphatase.
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CAS REGISTRY NUMBER
COMMENTARY
9036-01-5
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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 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
-
-
-
?
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
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
-
-
-
?
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
-
?
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-3,4,5-trisphosphate + H2O
phosphatidylinositol-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-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
-
-
-
?
D-myo-phosphatidylinositol 3,4,5-trisphosphate
D-myo-phosphatidylinositol 3,4-bisphosphate
-
-
-
?
D-myo-phosphatidylinositol 3,4,5-trisphosphate
D-myo-phosphatidylinositol 3,4-bisphosphate
-
-
-
?
D-myo-phosphatidylinositol 3,4,5-trisphosphate
D-myo-phosphatidylinositol 3,4-bisphosphate
-
reaction is not stimulated by phosphatidylserine
-
?
D-myo-phosphatidylinositol 3,4,5-trisphosphate
D-myo-phosphatidylinositol 3,4-bisphosphate
-
reaction is strongly stimulated by phosphatidylserine
-
?
D-myo-phosphatidylinositol 3,4,5-trisphosphate
D-myo-phosphatidylinositol 3,4-bisphosphate
-
-
-
?
D-myo-phosphatidylinositol 3,4,5-trisphosphate
D-myo-phosphatidylinositol 3,4-bisphosphate
-
-
?
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
?
-
-
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
-
?
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.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
-
-
-
?
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
-
-
?
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
-
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
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
-
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
-
-
-
-
?
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
?
-
-
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
?
-
-
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.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Co2+
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
additional information
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+
-
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
4-amino-5-(4-chlorophenyl)-7(t-butyl)pyrazolo(3,4-d)pyrimidine
-
inhibits translocation of SHIP1 to the plasma membrane and tyrsine phosphorylation
5,5'-dithiobis(2-nitrobenzoate)
-
25-40% inhibition at 0.1 mM, 85-90% inhibition at 5 mM
o-Iodosobenzoate
-
25-40% inhibition at 0.1 mM, 85-90% inhibition at 5 mM
cetyltrimethylammonium bromide
-
reduced activity in presence of both Triton X-100 and cetyltrimethylammonium bromide
cetyltrimethylammonium bromide
-
only activates when added with the substrate and in the presence of Mg2+
Triton X-100
-
reduced activity in presence of both Triton X-100 and cetyltrimethylammonium bromide
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1,2-dioctanoylphosphatidylinositol 4-phosphate
-
hydrolysis of D-myo-phosphatidylinositol 4,5-bisphosphate and D-myo-phosphatidylinositol 3,4,5-trisphosphate is stimulated up to 100fold
IRS4
-
binds and activates the enzyme INP51, acts as a negative regulator for 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate contents, IRS4 contains an EPS15 homology domain, interaction analysis
-
phosphatidylcholine
-
vesicles of phosphatidylcholine only stimulate SHIP2 activity by 2fold. This effect is specific for di-C8 and di-C16 fatty acids of D-myo-phosphatidylinositol 3,4,5-trisphosphate as substrate
phosphatidylserine
-
vesicles of phosphatidylserine (PtdSer) greatly stimulate SHIP2. This effect is specific for di-C8 and di-C16 fatty acids of D-myo-phosphatidylinositol 3,4,5-trisphosphate as substrate
potassium bisperoxo (1,10-phenanthroline) oxovanadate (V)
-
protein phosphatase inhibitor bpV(phen), a cell permeable derivative, enhances the activity of PtdIns3P3 5-phosphatase, particularly SHIP2
Sodium vanadate
-
protein phosphatase inhibitor enhances the activity of PtdIns3P3 5-phosphatase, particularly SHIP2
TAX4
-
binds and activates the enzyme INP51, acts as a negative regulator for 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate contents, TAX4 contains an EPS15 homology domain, interaction analysis
-
additional information
-
in contrast to phosphatidylserine SH2 domain containing inositol 5-phosphatase 2 (SHIP2) no stimulation by phosphatidylserine (PtdSer)
-
additional information
the voltage-sensitive phosphoinositide phosphatase Ci-VSP, a membrane-resident PI(4,5) P2-5-phosphatase, is rapidly and reversibly activated by strong depolarization of the membrane potential
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.088
1-phosphatidyl-1D-myo-inositol 3,4,5-triphosphate
-
wild-type, pH not specified in the publication, temperature not specified in the publication
0.0316
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate
-
mutant D360A/N362A, pH not specified in the publication, temperature not specified in the publication
0.0738
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate
-
wild-type, pH not specified in the publication, temperature not specified in the publication
additional information
additional information
-
kinetics, substrate specificity, overview
-
additional information
additional information
-
with soluble diC8 D-myo-phosphatidylinositol 4,5-bisphosphate as a substrate, sigmoidal kinetics are observed, suggesting the presence of allosteric activation sites
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
57.5
1-phosphatidyl-1D-myo-inositol 3,4,5-triphosphate
-
wild-type, pH not specified in the publication, temperature not specified in the publication
28.2
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate
-
mutant D360A/N362A, pH not specified in the publication, temperature not specified in the publication
140.5
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate
-
wild-type, pH not specified in the publication, temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
653
1-phosphatidyl-1D-myo-inositol 3,4,5-triphosphate
-
wild-type, pH not specified in the publication, temperature not specified in the publication
892
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate
-
mutant D360A/N362A, pH not specified in the publication, temperature not specified in the publication
1900
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate
-
wild-type, pH not specified in the publication, temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
the adaptor protein APS, which specifically interacts with SHIP2, increases the PtdIns(3,4,5)P3 5-phosphatase activity of SHIP2 (76.7% at 3 microM APS and by 111.3% at 6 microM APS)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.1 - 8.1
-
pH 6.1: about 30% of maximal activity, pH 8.1: about 20% of maximal activity
6.5 - 8.3
-
pH 6.5: about 60% of maximal activity, pH 8.3: about 50% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
by cDNA microarray analysis it is shown that (PI[4,5]P2) phosphatase mRNAas are up-regulated in hepatocytes cultured on a basement membrane matrix, Engelbreth-Holm-Swarm (EHS) gel, which led to the finding that the PI(4,5)P2 levels of hepatocytes decreased on EHS gel
brenda
-
highly expressed in neurons of the arcuate and lateral nuclei of the hypothalamus. Treatment with a phosphorthioate-modified antisense oligonucleotide for 5ptase IV reduces the hypothalamic expression of 5ptase IV by approximately 80%
brenda
additional information
72-5ptase is expressed in differentiated 3T3-L1 adipocytes
brenda
-
embryonic and myelinated brain, the specific activity increases with myelination
brenda
widely expressed in adult mouse brain. SHIP2 mRNA and protein expression levels are significantly increased in the brain of type 2 diabetic db/db mice, semiquantitative RT-PCR expression analysis
brenda
-
widely expressed in adult mouse brain. SHIP2 mRNA and protein expression levels are significantly increased in the brain of type 2 diabetic db/db mice, semiquantitative RT-PCR expression analysis
brenda
-
the enzyme is more active in the kidney cortex than in the medulla
brenda
-
cell lines from kidney proximal tubules of a patient with Lowe syndrome and a normal individual
brenda
-
fibroblast cell line from patients with oculocerebrorenal syndrome of Lowe
brenda
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growth kinetics of wild-type and sac9 mutant primary roots, phenotype and tissue organization, overview
brenda
-
growth kinetics of wild-type and sac9 mutant primary roots, phenotype and tissue organization, overview
brenda
additional information
expression of 5PTase13 is suppressed by blue light irradiation. Expression level of 5PTase13 is significantly enhanced in phototropin1 single or phototropin1 phototropin2 double mutants under blue light
brenda
additional information
-
expression of 5PTase13 is suppressed by blue light irradiation. Expression level of 5PTase13 is significantly enhanced in phototropin1 single or phototropin1 phototropin2 double mutants under blue light
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
multicolor total internal reflection fluorescence microscopy (TIRFM) is used to visualize the spatial-temporal recruitment of SJ1, and its binding partner endophilin to clathrin-coated-pits. Differential temporal recruitment of the two major SJ1 splice variants to clathrin-coated-pits is observed. SJ1-145 is rapidly recruited as a burst, together with its binding partner endophilin, at a late stage of clathrin-coated-pit formation
brenda
-
multicolor total internal reflection fluorescence microscopy (TIRFM) is used to visualize the spatialtemporal recruitment of SJ1, and its binding partner endophilin to clathrin-coated-pits. Differential temporal recruitment of the two major SJ1 splice variants to clathrin-coated-pits is observed. SJ1-170 is present at all stages of CCP formation
brenda
-
SHIP2 is predominately cytosolic but translocates to the cell periphery in response to bpV(phen)
brenda
-
preferential localization of the Mg2+-dependent enzyme in cytosol
brenda
subcellular localisation found in Golgi apparatus and ER-to-Golgi intermediate compartment (ERGIC). INPP5B binds to specific RAB proteins within the secretory pathway, and mutational analysis indicates that RAB binding is required for efficient Golgi targeting of INPP5B
brenda
-
dOCRL dephosphorylates PI(4,5)P2 on internal membranes
brenda
-
upon insulin stimulation, the adaptor protein APS and SHIP2 are recruited to cell membranes as seen by immunofluorescence studies
brenda
voltage-sensitive phosphoinositide phosphatase Ci-VSP
brenda
-
in HuH-7 cells overexpressing SKIP and infected with hepatitis B virus (HBV), SKIP localizes to nucleus in addition to endoplasmic reticulum and suppresses HBV gene expression and replication. SKIP loses its nuclear localization and suppressive effect during replication of a core-negative HBV mutant
brenda
both isoforms a and b predominantly localize to the perinuclear region
-
brenda
-
CD32a cross-linking induces translocation to the plasma membrane
brenda
-
localization of SHIP2 at clathrin-coated pits is mediated by its proline-rich region. When the targeting signal present in this domain is missing, another targeting signal that directs the protein to focal adhesion predominates, overview
brenda
-
SHIP1 is localized to the membrane during cell adhesion
brenda
-
Dd5P4 accumulates on Legionella-containing vacuoles in wild-type Legionella pneumophilia infected Dictyostelium discoideum
brenda
-
OCRL1 accumulates on Legionella-containing vacuoles in wild-type Legionella pneumophilia infected Dictyostelium discoideum
brenda
-
in macrophages infected with Legionella pneumophila the localization of endogenous OCRL1 is identified on Legionella-containing vacuoles containing single or several bacteria
brenda
additional information
OCRL1a is significantly more abundant in the cytoplasmic puncta, and there is less diffuse cytosolic staining compared to isoform b in NRK- and HeLa cells
-
brenda
additional information
-
77% of the activity is localized in the particulate fraction
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
additional information
malfunction
-
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
-
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
additional information
-
GTP-bound, active Rab35 directly interacts with OCRL and controls its localization at the intercellular bridge
additional information
-
Salmonella typhimurium uses a membrane-charge based mechanism to control Salmonella-containing vacuole maturation
additional information
-
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
Show AA Sequence and Transmembrane Helices (3809 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Schizosaccharomyces pombe (strain 972 / ATCC 24843)
Schizosaccharomyces pombe (strain 972 / ATCC 24843)
Schizosaccharomyces pombe (strain 972 / ATCC 24843)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
57000
-
x * 57000, formation of larger aggregates in the absence of salt, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
?
-
x * 57000, formation of larger aggregates in the absence of salt, SDS-PAGE
additional information
the enzyme contains a WD-repeat domain and a 5PTase catalytic domain, domain organization
additional information
-
the enzyme contains a WD-repeat domain and a 5PTase catalytic domain, domain organization
additional information
the enzyme is composed of two domains, an N-terminal WD-repeat domain and a C-terminal catalytic domain
additional information
-
the enzyme is composed of two domains, an N-terminal WD-repeat domain and a C-terminal catalytic domain
additional information
-
three-dimensional structure analysis of enzyme with active site-bound substrate, analysis of crystal structure
additional information
-
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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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
phosphoprotein
-
phosphorylation site: NPXY motif C-terminal to the active site and tyrosine residue 1162 which is also located toward the C-terminus. Epidermal growth factor receptor-stimulates tyrosine phosphorylation of SHIP2 which correlates with increased SHIP2 5-phosphatase activity. This effect is demonstrated in HeLa cells
phosphoprotein
-
SHIP1 is localized to the membrane and is tyrosine phosphorylated during cell adhesion
phosphoprotein
centrosomal kinase AURKA phosphorylates INPP5E and thereby increases its 5-phosphatase activity
phosphoprotein
-
upon intracerebroventricular treatment with insulin, 5ptase IV undergoes a time-dependent tyrosine phosphorylation. Treatment with a phosphorthioate-modified antisense oligonucleotide for 5ptase IV shows a 70% reduction of insulin induced tyrosine phosphorylation of 5ptase IV and an increase in basal accumulation of phosphorylated inositols in the hypothalamus
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with biphenyl 3,3',4,4',5,5'-hexakisphosphate, to 2.89 A resolution. One inhibitor pole locates in the phospholipid headgroup binding site and the second solvent-exposed ring binds to the His-Tag of another INPP5B molecule, while a molecule of inorganic phosphate is also present in the active site. In complex with benzene 1,2,4,5-tetrakisphosphate, to 2.9 A resolution. Conserved residues among the 5-phosphatase family mediate interactions with the inhibitors similar to those with the polar groups present in positions 1, 4, 5, and 6 on the inositol ring of the substrate. 5-Phosphatase specificity most likely resides in the variable zone located close to the 2- and 3-positions of the inositol ring
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D319A
DELTA1-465
-
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
-
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
-
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
-
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
-
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
-
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
-
mutant with a deficient 5-phosphatase activity fails to rescue the endocytic defects in synj1-/- neurons
DELTA1-885/1186-1258
-
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
-
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
-
Glu in SHIP1 SH2 domain, faster association kinetics for binding to immobilized peptide VApYSYL
P686A/D690A/R691A
-
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
-
Ser in SHIP1 SH2 domain, faster association kinetics for binding to immobilized peptide VApYSYL
P687A/D691A/R692G
-
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
-
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
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
-
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
-
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
-
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
-
siRNA-mediated knockdown of oculocerebrorenal syndrome of Lowe, i.e. OCRL1 in epithelial cells, phenotype, overview
additional information
-
direct interaction of SHIP2 with insulin receptor and filamin are evidenced in COS-7 cells
additional information
-
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
-
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
-
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
-
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
-
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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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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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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
purification by gel filtration chromatography on Sephacryl S-100 followed by cation exchange chromatography on SP-Sepharose
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recombinant GST-tagged catalytic domains from Escherichia coli strain DH5alpha by glutathione affinity chromatography
recombinant GST-tagged catalytic domains of synaptojanin2 and OCRL from Escherichia coli strain DH5alpha by glutathione affinity chromatography
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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
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recombinant GST-tagged catalytic domains from Escherichia coli strain DH5alpha by glutathione affinity chromatography
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recombinant GST-tagged catalytic domains from Escherichia coli strain DH5alpha by glutathione affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
72-5ptase is expressed as a hemagglutinin (HA) tagged fusion protein in 3T3-L1 cells. Overexpression in adipocytes generates phosphatidylinositol 3-phosphate at the plasma membrane of unstimulated 3T3-L1 adipocytes (conditions under which phosphatidylinositol 3,4,5-triphosphate is not synthesized)
DNA and amino acid sequence detremination and analysis, expression of GFP-tagged synaptojanin-1 in CHO cells
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expressed as a HIS-tagged fusion protein in 3T3-L1 adipocytes and in CHO-IR cells (Chinese hamster ovary cells stably transfected with the insulin receptor)
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expressed in Escherichia coli as a GST-fusion protein and as a Flag-tagged fusion protein in human hepatoma HuH-7 cells
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expression of GST-tagged catalytic domain comprising residues A305-A721, in Escherichia coli strain DH5alpha
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expression of GST-tagged catalytic domain comprising residues S470-R962, in Escherichia coli strain DH5alpha
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expression of GST-tagged catalytic domains, comprising residues D474-R959 of synaptojanin2 and residues V202-E618 of OCRL, in Escherichia coli strain DH5alpha
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expression of His-tagged full length enzyme in Escherichia coli strain BL21(DE3)
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from oocytes and fertilized eggs, recombinant overexpression of FLAG-tagged proline-rich inositol polyphosphate 5-phosphatase in eggs
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full-length 5PTase13-encoding sequence is N-terminally fused to a polyhistidinetag and a T7-tag and expressed in Escherichia coli cells
full-length human INPP5B cDNA is cloned into pEGFP-C3 with an N-terminal FLAG tag for in vivo expression. INPP5B cDNA is cloned into pGBKT7 for yeast two-hybrid experiments and pBAC2 for expression of recombinant protein in insect cells. DNA encoding the N-terminal 229 amino acids of INPP5B is cloned into pET41EK-LIC for expression of GST-tagged protein in Escherichia coli
gene 5PTase14, DNA and amino acid sequence determination and analysis, genetic organization, expression of His-tagged full length enzyme in yeast
gene fra3, expression pattern, DNA and amino acid sequence determination and analysis, complementation of an enzyme-deficient mutant
IPPRp is cloned into the pET17b expression vector and moved into Escherichia coli strain BL21(DE3)pLys S for protein production
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SH2 domain, a maltose-binding protein fusion protein and a His-tagged version expressed in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
isoform INPP5E is overexpressed in cervical cancer, non-Hodgkin’s lymphoma, and uterine leiomyosarcoma
SHIP2 mRNA and protein expression levels are significantly increased in the brain of type 2 diabetic db/db mice
SKIP expression is markedly elevated during differentiation and is controlled by MyoD in C2C12 cells
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SHIP2 mRNA and protein expression levels are significantly increased in the brain of type 2 diabetic db/db mice
SHIP2 mRNA and protein expression levels are significantly increased in the brain of type 2 diabetic db/db mice
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
molecular biology
medicine
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examination of patients with Lowe oculocerebrorenal syndrome, MIM 309000, and their families for mutations in enzyme gene
medicine
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a SHIP2-antisense oligonucleotide therapy can improve the decrease in insulin-induced glucose disposal observed after high-fat feeding. This effect can be retraced on a molecular level by an improvement in insulin-induced Akt phosphorylation
medicine
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inhibition of hypothalamic 5ptase IV expression by this antisense approach results in reduced daily food intake and body weight loss. 5ptase IV is a powerful regulator of signaling through PI3-kinase in hypothalamus and may become an interesting target for therapeutics of obesity and related disorders
medicine
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inhibition of SHIP2 for the prevention and/or treatment of type 2 diabetes
medicine
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organization of the actin cytoskeleton via D-myo-phosphatidylinositol 4,5-bisphosphate is involved in the regulation of hepatocyte differentiation by the extracellular matrix
medicine
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SHIP2 plays an important role in insulin-dependent signaling pathways controlling glucose and lipid, metabolsim in vivo. A fine tuning of SHIP2 expression/activation in target organs is likely to be beneficial to correct metabolic dysfunctions in pathological conditions such as insulin resistance diabetes melitus and obesity
molecular biology
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results raise the possibility that dynamic phosphoinositide metabolism may occur throughout the lifetime of a clathrin-coated pit
molecular biology
results suggest a role for INPP5B in retrograde ER-to-Golgi intermediate compartment (ERGIC) transport
molecular biology
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SHIP2 lipid phosphatase activity plays an important role in the metabolism of PtdIns(3,4,5)P3 in response to H2O2
molecular biology
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the interaction between adaptor protein APS and SHIP2 provides to both proteins potential negative regulatory mechanisms to act on the insulin cascade
molecular biology
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translocatable phosphatase: method is based on the rapamycin-induced heterodimerization of FRB (fragment of mammalian target of rapamycin that binds FKB12) and FKB12 (FK506 binding protein 12). A mutant version of 5-ptase with a defective membrane targeting domain (CAAX box) is fused to FKB12 and tagged with monomeric red fluorescent protein, whereas its binding partner FRB (fused to CFP) is tethered to the plasma membrane through palmitoylation. In the absence of rapamycin, 5-ptase resides in the cytosol and leaves D-myo-phosphatidylinositol 4,5-bisphosphate levels at the plasma membrane unaltered. Upon addition of 100 nM rapamycin, FKB12 and FRB undergo heterodimerization and the 5-ptase is recruited to the plasma membrane
molecular biology
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c-Jun NH2-terminal kinase (JNK)-interacting protein 1 (JIP1) interacts with SHIP2 and thereby positively modulates the MLK3/JIP1-mediated JNK1 activation. Furthermore, SHIP2 positively regulates the tyrosine phosphorylation of JIP1. By its interacting properties, SHIP2 can modulate JIP1-mediated JNK pathway signaling
molecular biology
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catalytically inactive SHIP2 mutant P686A/D690A/R691A reduces preadipocyte proliferation by attenuating PDGFR signaling
molecular biology
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hydrolysis of phosphatidylinositol 4,5-bisphosphate by PI(4,5)P2 5-phosphatase mediates calcium-induced inactivation of TRPV6 channels
molecular biology
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intersectin1 (ITSN1) is identified as a binding partner of the SH2 domain containing inositol 5-phosphatase 2 (SHIP2). In response to epidermal growth factor, SHIP2 expression is able to recruit the ITSN1 short form (ITSN1-S) to the cell membrane, while SHIP2 overexpression does not modulate the ITSN-mediated extracellular signal-regulated kinase1/2 and c-Jun NH2-terminal kinase activation
molecular biology
OCRL1 exists as two functional pools, one participating in clathrin-mediated trafficking events such as endocytosis, and another that is much less or not involved in this process
molecular biology
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SKIP is translocated from endoplasmic reticulum into nucleus through its interaction with hepatitis B virus core protein and suppresses HBV gene expression via a novel suppression domain
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
J. Biol. Chem.
269
3397-33402
1994
Homo sapiens
brenda
Dawson, R.M.C.; Thompson, W.
The triphosphoinositide phosphomonoesterase of brain tissue
Biochem. J.
91
244-250
1964
Bos taurus
brenda
Mack, S.E.; Palmer, F.B.St.C.
Evidence for a specific phosphatidylinositol 4-phosphate phosphatase in human erythrocyte membranes
J. Lipid Res.
25
75-85
1984
Canis lupus familiaris, Oryctolagus cuniculus, Ovis aries, Homo sapiens, Platyrrhini, Rattus norvegicus
brenda
Mack, S.E.; Palmer, F.B.St.C.
Soluble and membrane-bound polyphosphoinositide phosphohydrolases in mammalian erythrocytes
Biochem. Cell Biol.
66
199-207
1988
Oryctolagus cuniculus, Ovis aries, Homo sapiens, Rattus norvegicus, Sus scrofa
brenda
Koutouzov, S.; Marche, P.
The Mg2+-activated phosphatidylinositol 4,5-bisphosphate-specific phosphomonoesterase of erythrocyte membrane
FEBS Lett.
144
16-20
1982
Rattus norvegicus
brenda
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
Biochem. J.
179
549-553
1979
Rattus norvegicus
brenda
Sheltawy, A.; Brammer, M.; Borrill, D.
The subcellular distribution of triphosphoinositide phosphomonoesterase in guinea-pig brain
Biochem. J.
128
579-586
1972
Cavia porcellus
brenda
Cooper, P.H.; Hawthorne, J.N.
Phosphomonoesterase hydrolysis of polyphosphoinositides in rat kidney: Properties and subcellular localization of the enzyme system
Biochem. J.
150
537-551
1975
Rattus norvegicus
brenda
Lefebvre, Y.A.; White, D.A.; Hawthorne, J.N.
Diphosphoinositide metabolism in bovine adrenal medulla
Can. J. Biochem.
54
746-753
1976
Bos taurus
brenda
Abdel-Latif, A.; Akhtar, R.A.; Hawthorne, J.
Acetylcholine increases breakdown of triphosphoinositide of rabbit iris muscle prelabelled with phosphate
Biochem. J.