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Information on EC 3.1.3.86 - phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase
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3.1.3.86 phosphatidylinositol-3,4,5-trisphosphate 5-phosphataseIUBMB Comments
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) . The enzyme is involved in several signal transduction pathways in the immune system leading to an adverse range of effects.
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Word Map
- 3.1.3.86
-
immunoreceptor
-
5'-phosphatase
-
tyrosine-based
-
ship-2
-
ptdins3,4,5p3
-
fcgammariib
-
fcepsilonri
- 3,4-bisphosphate
-
microrna-155
- medicine
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
ship-1, sh2-containing inositol phosphatase, sh2 domain-containing inositol 5-phosphatase, ptdins(3,4,5)p3 5-phosphatase, ptdins(3,4,5)p3 phosphatase, sh2 domain containing inositol 5-phosphatase, phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase 1, sh2 domain-containing inositol 5-phosphatase 2, 75 kda 5-phosphatase, phosphatidylinositol (3,4,5)-trisphosphate 5-phosphatase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase
PtdIns(3,4,5)P3 5-phosphatase
SH2-containing inositol phosphatase
SHIP
SHIP2
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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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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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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
-
-
-
-
?
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
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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 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
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
-
-
-
-
?
additional information
?
-
SHIP2 does not hydrolyze 1-phosphatidyl-1D-myo-inositol 1,3,4,5-tetrakisphosphate in vitro
-
-
-
additional information
?
-
SHIP2 does not hydrolyze 1-phosphatidyl-1D-myo-inositol 1,3,4,5-tetrakisphosphate in vitro
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
synaptojanin accounts for the major part of the active PtdIns(3,4,5)P3 5-phosphatase activity in rat brain
-
-
-
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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 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
-
-
?
additional information
?
-
O15357
SHIP2 does not hydrolyze 1-phosphatidyl-1D-myo-inositol 1,3,4,5-tetrakisphosphate in vitro
-
-
-
additional information
?
-
Q92835
SHIP2 does not hydrolyze 1-phosphatidyl-1D-myo-inositol 1,3,4,5-tetrakisphosphate in vitro
-
-
-
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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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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
phosphatidylinositol 4,5-bisphosphate
-
strong inhibition at low micromolar concentrations
phosphatidylinositol 4-phosphate
-
inhibition at low micromolar concentrations
additional information
-
the enzyme is insensitive to N-ethylmaleimide, InsPh and 2,3-bisphosphoglycerate
-
additional information
-
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
-
additional information
-
vinexin beta does not affect PtdIns(3,4,5)P3 5-phosphatase activity of SHIP2
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Adenocarcinoma
Murine pancreatic adenocarcinoma dampens SHIP-1 expression and alters MDSC homeostasis and function.
Arthritis, Gouty
MicroRNA-155 as a proinflammatory regulator via SHIP-1 down-regulation in acute gouty arthritis.
Asthma
Src homology 2 domain-containing inositol 5-phosphatase 1 deficiency leads to a spontaneous allergic inflammation in the murine lung.
Autoimmune Diseases
SHIP-1 deficiency in the myeloid compartment is insufficient to induce myeloid expansion or chronic inflammation.
Colitis
IL-10/microRNA-155/SHIP-1 signaling pathway is crucial for commensal bacteria induced spontaneous colitis.
Colitis
MicroRNA-155 promotes the pathogenesis of experimental colitis by repressing SHIP-1 expression.
Diabetes Mellitus, Type 2
A high-throughput microfluidic assay for SH2 domain-containing inositol 5-phosphatase 2.
Hematologic Neoplasms
A novel strategy for modulation of MDSC to enhance cancer immunotherapy.
Hypersensitivity
Gene transfer of SHIP-1 inhibits proliferation of juvenile myelomonocytic leukemia cells carrying KRAS2 or PTPN11 mutations.
Ileitis
SHIP-1 deficiency in the myeloid compartment is insufficient to induce myeloid expansion or chronic inflammation.
Infection
Low perforin and elevated SHIP-1 expression is associated with functional anergy of natural killer cells in chronic HIV-1 infection.
Infection
Targeting SHIP-1 in Myeloid Cells Enhances Trained Immunity and Boosts Response to Infection.
Influenza, Human
Distinct macrophage subpopulations characterize acute infection and chronic inflammatory lung disease.
Insulin Resistance
Association of SH2-containing inositol phosphatase 2 with the insulin resistance of diabetic db/db mice.
Insulin Resistance
Polymorphisms in type II SH2 domain-containing inositol 5-phosphatase (INPPL1, SHIP2) are associated with physiological abnormalities of the metabolic syndrome.
Insulin Resistance
SH2 domain-containing inositol 5-phosphatase (SHIP2) inhibition ameliorates high glucose-induced de-novo lipogenesis and VLDL production through regulating AMPK/mTOR/SREBP1 pathway and ROS production in HepG2 cells.
Leukemia
Gene transfer of SHIP-1 inhibits proliferation of juvenile myelomonocytic leukemia cells carrying KRAS2 or PTPN11 mutations.
Leukemia
The inositol 5'-phosphatase SHIP-2 negatively regulates IgE-induced mast cell degranulation and cytokine production.
Leukemia
[Effect of SHIP-1 on Invasion, Migration and PI3K-AKT Signaling Pathway of Leukemic Cells].
Leukemia, Erythroblastic, Acute
The inositol phosphatase SHIP-1 is negatively regulated by Fli-1 and its loss accelerates leukemogenesis.
Leukemia, Myelomonocytic, Juvenile
Gene transfer of SHIP-1 inhibits proliferation of juvenile myelomonocytic leukemia cells carrying KRAS2 or PTPN11 mutations.
Leukemia-Lymphoma, Adult T-Cell
Alteration of phosphatidylinositol 3-kinase cascade in the multilobulated nuclear formation of adult T cell leukemia/lymphoma (ATLL).
Leukemia-Lymphoma, Adult T-Cell
Human T-cell leukemia virus type I tax down-regulates the expression of phosphatidylinositol 3,4,5-trisphosphate inositol phosphatases via the NF-kappaB pathway.
Lung Diseases
Distinct macrophage subpopulations characterize acute infection and chronic inflammatory lung disease.
Lung Diseases
Genetic segregation of inflammatory lung disease and autoimmune disease severity in SHIP-1-/- mice.
Lung Diseases
SHIP-1 deficiency in the myeloid compartment is insufficient to induce myeloid expansion or chronic inflammation.
Lymphoma
B-cell receptor signalling and its crosstalk with other pathways in normal and malignant cells.
Lymphoma
Phosphoinositide phosphatase SHIP-1 regulates apoptosis induced by edelfosine, Fas ligation and DNA damage in mouse lymphoma cells.
Lymphoma
Quantification of change in phosphorylation of BCR-ABL kinase and its substrates in response to Imatinib treatment in human chronic myelogenous leukemia cells.
Lymphoma, B-Cell
SHIP-1 inhibits CD95/APO-1/Fas-induced apoptosis in primary T lymphocytes and T leukemic cells by promoting CD95 glycosylation independently of its phosphatase activity.
Metabolic Syndrome
Polymorphisms in type II SH2 domain-containing inositol 5-phosphatase (INPPL1, SHIP2) are associated with physiological abnormalities of the metabolic syndrome.
Multiple Myeloma
Immune cell inhibition by SLAMF7 is mediated by a mechanism requiring src kinases, CD45, and SHIP-1 that is defective in multiple myeloma cells.
Myelodysplastic Syndromes
Loss of SHIP-1 protein expression in high-risk myelodysplastic syndromes is associated with miR-210 and miR-155.
Myeloproliferative Disorders
The duplicitous nature of the Lyn tyrosine kinase in growth factor signaling.
Neoplasms
Alteration of phosphatidylinositol 3-kinase cascade in the multilobulated nuclear formation of adult T cell leukemia/lymphoma (ATLL).
Neoplasms
Enzymatic and non-enzymatic activities of SHIP-1 in signal transduction and cancer.
Neoplasms
Histamine-releasing factor/translationally controlled tumor protein (HRF/TCTP)-induced histamine release is enhanced with SHIP-1 knockdown in cultured human mast cell and basophil models.
Neoplasms
Human T-cell leukemia virus type I tax down-regulates the expression of phosphatidylinositol 3,4,5-trisphosphate inositol phosphatases via the NF-kappaB pathway.
Neoplasms
Murine pancreatic adenocarcinoma dampens SHIP-1 expression and alters MDSC homeostasis and function.
Neoplasms
Regulation of hematopoietic cell signaling by SHIP-1 inositol phosphatase: growth factors and beyond.
Neoplasms
The duplicitous nature of the Lyn tyrosine kinase in growth factor signaling.
Osteoarthritis
MicroRNA-155 as a proinflammatory regulator in clinical and experimental arthritis.
Pancreatic Neoplasms
Murine pancreatic adenocarcinoma dampens SHIP-1 expression and alters MDSC homeostasis and function.
phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase deficiency
Distinct macrophage subpopulations characterize acute infection and chronic inflammatory lung disease.
phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase deficiency
SHIP-1 deficiency in the myeloid compartment is insufficient to induce myeloid expansion or chronic inflammation.
phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase deficiency
SHIP-1 increases early oxidative burst and regulates phagosome maturation in macrophages.
phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase deficiency
SHIP-1 inhibits CD95/APO-1/Fas-induced apoptosis in primary T lymphocytes and T leukemic cells by promoting CD95 glycosylation independently of its phosphatase activity.
Pneumonia
Genetic segregation of inflammatory lung disease and autoimmune disease severity in SHIP-1-/- mice.
Pneumonia
SHIP-1 deficiency in the myeloid compartment is insufficient to induce myeloid expansion or chronic inflammation.
Pulmonary Disease, Chronic Obstructive
SHIP-1 deficiency in the myeloid compartment is insufficient to induce myeloid expansion or chronic inflammation.
Stroke
Phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase 1: a meaningful and independent marker to predict stroke in the chinese population.
Vaccinia
SH2-containing inositol phosphatase (SHIP-1) transiently translocates to raft domains and modulates CD16-mediated cytotoxicity in human NK cells.
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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
-
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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
subline R10- cell; subline R10- cell; subline R10+ cell; subline R10+ cell
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
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
-
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
-
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
-
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
-
SHIP is involved in platelet activation evoked by thrombin
physiological function
-
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
-
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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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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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
-
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
-
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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Jackson, S.P.; Schoenwaelder, S.M.; Matzaris, M.; Brown, S.; Mitchell, C.A.
Phosphatidylinositol 3,4,5-trisphosphate is a substrate for the 75 kDa inositol polyphosphate 5-phosphatase and a novel 5-phosphatase which forms a complex with the p85/p110 form of phosphoinositide 3-kinase
EMBO J.
14
4490-4500
1995
Homo sapiens
brenda
Vandeput, F.; Backers, K.; Villeret, V.; Pesesse, X.; Erneux, C.
The influence of anionic lipids on SHIP2 phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase activity
Cell. Signal.
18
2193-2199
2006
Homo sapiens
brenda
Drayer, A.L.; Pesesse, X.; De Smedt, F.; Woscholski, R.; Parker, P.; Erneux, C.
Cloning and expression of a human placenta inositol 1,3,4,5-tetrakisphosphate and phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase
Biochem. Biophys. Res. Commun.
225
243-249
1996
Homo sapiens
brenda
Drayer, A.; Pesesse, X.; De Smedt, F.; Communi, D.; Moreau, C.; Erneux, C.
The family of inositol and phosphatidylinositol polyphosphate 5-phosphatases
Biochem. Soc. Trans.
24
1001-1005
1996
Homo sapiens, Rattus norvegicus
brenda
Wisniewski, D.; Strife, A.; Swendeman, S.; Erdjument-Bromage, H.; Geromanos, S.; Kavanaugh, W.M.; Tempst, P.; Clarkson, B.
A novel SH2-containing phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase (SHIP2) is constitutively tyrosine phosphorylated and associated with src homologous and collagen gene (SHC) in chronic myelogenous leukemia progenitor cells
Blood
93
2707-2720
1999
Homo sapiens (O15357), Homo sapiens (Q92835)
brenda
Zwaenepoel, K.; Goris, J.; Erneux, C.; Parker, P.J.; Janssens, V.
Protein phosphatase 2A PR130/Balpha1 subunit binds to the SH2 domain-containing inositol polyphosphate 5-phosphatase 2 and prevents epidermal growth factor (EGF)-induced EGF receptor degradation sustaining EGF-mediated signaling
FASEB J.
24
538-547
2010
Homo sapiens
brenda
Paternotte, N.; Zhang, J.; Vandenbroere, I.; Backers, K.; Blero, D.; Kioka, N.; Vanderwinden, J.M.; Pirson, I.; Erneux, C.
SHIP2 interaction with the cytoskeletal protein Vinexin
FEBS J.
272
6052-6066
2005
Mus musculus
brenda
Pesesse, X.; Moreau, C.; Drayer, A.L.; Woscholski, R.; Parker, P.; Erneux, C.
The SH2 domain containing inositol 5-phosphatase SHIP2 displays phosphatidylinositol 3,4,5-trisphosphate and inositol 1,3,4,5-tetrakisphosphate 5-phosphatase activity
FEBS Lett.
437
301-303
1998
Homo sapiens
brenda
Lioubin, M.N.; Algate, P.A.; Tsai, S.; Carlberg, K.; Aebersold, A.; Rohrschneider, L.R.
p150Ship, a signal transduction molecule with inositol polyphosphate-5-phosphatase activity
Genes Dev.
10
1084-95
1996
Homo sapiens
brenda
Woscholski, R.; Waterfield, M.D.; Parker, P.J.
Purification and biochemical characterization of a mammalian phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase
J. Biol. Chem.
270
31001-31007
1995
Rattus norvegicus
brenda
Giuriato, S.; Payrastre, B.; Drayer, A.L.; Plantavid, M.; Woscholski, R.; Parker, P.; Erneux, C.; Chap, H.
Tyrosine phosphorylation and relocation of SHIP are integrin-mediated in thrombin-stimulated human blood platelets
J. Biol. Chem.
272
26857-26863
1997
Homo sapiens
brenda
Woscholski, R.; Finan, P.M.; Radley, E.; Totty, N.F.; Sterling, A.E.; Hsuan, J.J.; Waterfield, M.D.; Parker, P.J.
Synaptojanin is the major constitutively active phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase in rodent brain
J. Biol. Chem.
272
9625-9628
1997
Rattus norvegicus
brenda
Pesesse, X.; Dewaste, V.; De Smedt, F.; Laffargue, M.; Giuriato, S.; Moreau, C.; Payrastre, B.; Erneux, C.
The Src homology 2 domain containing inositol 5-phosphatase SHIP2 is recruited to the epidermal growth factor (EGF) receptor and dephosphorylates phosphatidylinositol 3,4,5-trisphosphate in EGF-stimulated COS-7 cells
J. Biol. Chem.
276
28348-28355
2001
Homo sapiens
brenda
Ooms, L.M.; Dyson, J.M.; Kong, A.M.; Mitchell, C.A.
Analysis of phosphatidylinositol 3,4,5 trisphosphate 5-phosphatase activity by in vitro and in vivo assays
Methods Mol. Biol.
462
223-239
2009
Chlorocebus aethiops
brenda
Damen, J.E.; Liu, L.; Rosten, P.; Humphries, R.K.; Jefferson, A.B.; Majerus, P.W.; Krystal, G.
The 145-kDa protein induced to associate with Shc by multiple cytokines is an inositol tetraphosphate and phosphatidylinositol 3,4,5-triphosphate 5-phosphatase
Proc. Natl. Acad. Sci. USA
93
1689-1693
1996
Mus musculus
brenda
Kuehbacher, A.; Dambournet, D.; Echard, A.; Cossart, P.; Pizarro-Cerda, J.
Phosphatidylinositol 5-phosphatase oculocerebrorenal syndrome of Lowe protein (OCRL) controls actin dynamics during early steps of Listeria monocytogenes infection
J. Biol. Chem.
287
13128-13136
2012
Danio rerio
brenda
Ijuin, T.; Takenawa, T.
Regulation of insulin signaling and glucose transporter 4 (GLUT4) exocytosis by phosphatidylinositol 3,4,5-trisphosphate (PIP3) phosphatase, skeletal muscle, and kidney enriched inositol polyphosphate phosphatase (SKIP)
J. Biol. Chem.
287
6991-6999
2012
Mus musculus
brenda
Tu, W.J.; Liu, X.Y.; Dong, H.; Yu, Y.; Wang, Y.; Chen, H.
Phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase 1: a meaningful and independent marker to predict stroke in the Chinese population
J. Mol. Neurosci.
52
507-514
2014
Homo sapiens
brenda
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