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Enzyme Nomenclature
Information on EC 3.1.3.86 - phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase
for references in articles please use BRENDA:EC3.1.3.86
Word Map on EC 3.1.3.86
- 3.1.3.86
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immunoreceptor
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5'-phosphatase
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ship-2
-
tyrosine-based
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ptdins3,4,5p3
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fcgammariib
- 3,4-bisphosphate
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fcepsilonri
-
microrna-155
- 1,3,4,5-tetrakisphosphate
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socs-1
-
ptdins3,4p2
- medicine
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
3.1.3.86
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RECOMMENDED NAME
GeneOntology No.
phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate + H2O = 1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate + phosphate
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
1-phosphatidyl-1D-myo-inositol-3,4,5-trisphosphate 5-phosphohydrolase
This enzyme hydroylses 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3) to produce PtdIns(3,4)P2, thereby negatively regulating the PI3K (phosphoinositide 3-kinase) pathways. The enzyme also shows activity toward (PtdIns(1,3,4,5)P4) [5]. The enzyme is involved in several signal transduction pathways in the immune system leading to an adverse range of effects.
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
malfunction
-
cell adhesion to collagen-I-coated dishes is decreased in SHIP2-deicient MEF cells compared with wild type cells
malfunction
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depletion of SHIP 5'-phosphatases increases neutrophil wound attraction and random motility through a PI3K-dependent pathway. Ectopic expression of the SHIP1 phosphatase domain impairs neutrophil migration
physiological function
isoforms SHIP2 and SHIP1 have a different hierarchy of binding SH3-domain containing proteins; isoforms SHIP2 and SHIP1 have a different hierarchy of binding SH3-domain containing proteins
physiological function
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PR130/Balpha1 and SHIP2 partially colocalize in untreated HeLa cells, and both translocate to the cell membrane on epidermal growth factor stimulation. Protein phosphatase 2A PR130/Balpha1 subunit binds to the SH2 domain-containing inositol polyphosphate 5-phosphatase 2 and prevents epidermal growth factor-induced epidermal growth factor receptor degradation sustaining epidermal growth factor-mediated signaling
physiological function
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SHIP2 interaction with vinexin alpha promotes the localization of SHIP2 at the periphery of the cells leaving its catalytic site intact. SHIP2 is active both as a PtdIns(3,4,5)P3 5-phosphatase and as a modulator of focal contact formation
physiological function
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SHIP is involved in platelet activation evoked by thrombin
physiological function
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the Src homology 2 domain containing inositol 5-phosphatase SHIP2 is recruited to the epidermal growth factor receptor and dephosphorylates phosphatidylinositol 3,4,5-trisphosphate in epidermal growth factor-stimulated COS-7 cells
physiological function
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SHIP phosphatases serve as a brake that limit neutrophil motility and inflammation, at least in part through their effects on PI3K signaling
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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 1,3,4,5-tetrakisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 1,3,4-triphosphate + phosphate
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-
-
-
?
1-phosphatidyl-1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 1,3,4-trisphosphate + phosphate
substrate of isoform SHIP1 in vitro
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-
?
1-phosphatidyl-1D-myo-inositol 1,3,4,5-tetraphosphate + H2O
1-phosphatidyl-1D-myo-inositol 1,3,4-triphosphate + 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
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-
-
-
?
1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 1,3,4-triphosphate + phosphate
1-phosphatidyl-1D-myo-inositol 1,3,4,5-tetraphosphate + H2O
1-phosphatidyl-1D-myo-inositol 1,3,4-triphosphate + phosphate
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-
-
-
?
1-phosphatidyl-1D-myo-inositol 1,3,4,5-tetraphosphate + H2O
1-phosphatidyl-1D-myo-inositol 1,3,4-triphosphate + phosphate
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-
-
-
?
1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate + phosphate
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-
-
-
?
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
-
in vivo substrate of SHIP2
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-
?
1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate + phosphate
substrate of isoforms SHIP2 and SHIP1 in vitro
-
-
?
1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate + phosphate
-
in vitro substrate of SHIP2
-
-
?
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
-
-
-
-
?
1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 1,3,4-triphosphate + phosphate
-
-
-
-
?
1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 1,3,4-triphosphate + phosphate
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-
-
-
?
additional information
?
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SHIP2 does not hydrolyze 1-phosphatidyl-1D-myo-inositol 1,3,4,5-tetrakisphosphate in vitro
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-
-
additional information
?
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SHIP2 does not hydrolyze 1-phosphatidyl-1D-myo-inositol 1,3,4,5-tetrakisphosphate in vitro
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-
-
additional information
?
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cytosolic Ptdlns(3,4,5)P3 5-phosphatase which associates with phosphoinositide 3-kinase does not metabolize phosphatidylinositol 4,5-bisphosphate, inositol 1,4,5-trisphosphate or inositol 1,3,4,5-tetraphosphate
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-
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additional information
?
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synaptojanin accounts for the major part of the active PtdIns(3,4,5)P3 5-phosphatase activity in rat brain
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-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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 1,3,4,5-tetrakisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 1,3,4-trisphosphate + phosphate
O15357, Q92835
substrate of isoform SHIP1 in vitro
-
-
?
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
-
in vivo substrate of SHIP2
-
-
?
1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate + phosphate
O15357, Q92835
substrate of isoforms SHIP2 and SHIP1 in vitro
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-
?
additional information
?
-
O15357
SHIP2 does not hydrolyze 1-phosphatidyl-1D-myo-inositol 1,3,4,5-tetrakisphosphate in vitro
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-
-
additional information
?
-
Q92835
SHIP2 does not hydrolyze 1-phosphatidyl-1D-myo-inositol 1,3,4,5-tetrakisphosphate in vitro
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-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
additional information
-
Zn2+, Ca2+ and Mn2+ do not support enzyme activity
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
phosphatidylinositol 4,5-bisphosphate
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strong inhibition at low micromolar concentrations
phosphatidylinositol 4-phosphate
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inhibition at low micromolar concentrations
additional information
-
the enzyme is insensitive to N-ethylmaleimide, InsPh and 2,3-bisphosphoglycerate
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additional information
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N-ethylmaleimide, orthophosphate, 4-nitrophenylphosphate, glycerolbisphosphate, inositol hexakisphosphate and (1R,2R,4R)-cyclohexane-1,2,4-trismethylenesulfonate are without significant effect on the enzyme activity
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
SHIP2 enzyme activity with phosphatidylinositol 3,4,5-trisphosphate is 11fold stimulated in the presence of 0.02 mM vesicles of phosphatidylserine. 0.2 mM vesicles of phosphatidylcholine stimulate 2fold phosphatidylinositol 3,4,5-trisphosphate phosphatase activity of SHIP2
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additional information
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vinexin beta does not affect PtdIns(3,4,5)P3 5-phosphatase activity of SHIP2
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.001
1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate
-
in the presence of 5 mM MgCl2, 0.5 mM EGTA, 50 mM Tris, pH 7.4, temperature not specified in the publication
0.1
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate
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in the presence of 5 mM MgCl2, 0.5 mM EGTA, 50 mM Tris, pH 7.4, temperature not specified in the publication
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
subline R10- cell; subline R10- cell; subline R10+ cell; subline R10+ cell
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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PDB
SCOP
CATH
ORGANISM
UNIPROT
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
145000
150000
155000
isoform SHIP2, gel filtration; isoform SHIP2, gel filtration
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
phosphoprotein
isoforms SHIP2 and SHIP1 are constitutively tyrosine phosphorylated in chronic myelogenous leukemia progenitor cells; isoforms SHIP2 and SHIP1 are constitutively tyrosine phosphorylated in chronic myelogenous leukemia progenitor cells. Stimulation of human hematopoietic growth factor responsive cell lines with stem cell factor, interleukin-3, and granulocyte-macrophage colony-stimulating factor leads to rapid tyrosine phosphorylation of SHIP2 and its resulting association with src homologous and collagen gene
phosphoprotein
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thrombin stimulation induces a tyrosine phosphorylation of SHIP
phosphoprotein
-
in COS-7 cells, SHIP2 is tyrosine-phosphorylated at least at two separated tyrosine phosphorylation sites in response to epidermal growth factor
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
HiTrap S column chromatography, phosphocellulose column chromatography, heparin-HiTrap column chromatography, Q-HiTrap column chromatography, and S-300 gel filtration
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the enzyme is co-purified with the p85/pll0 form of PI 3-kinase, by Q-Sepharose column chromatography, S-Sepharose column chromatography, hydroxyapatite column chromatography and Mono S column chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in COS-7 cells
expressed in Escherichia coli BL21(DE3) cells
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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LINKS TO OTHER DATABASES (specific for EC-Number 3.1.3.86)
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