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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
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-trisphosphate + phosphate
inositol 1,3,4,5-tetrakisphosphate + H2O
?
additional information
?
-
1-phosphatidyl-1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 1,3,4-trisphosphate + phosphate
-
-
-
-
?
1-phosphatidyl-1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 1,3,4-trisphosphate + 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-tetrakisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 1,3,4-trisphosphate + 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 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
best substrate
-
-
?
1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate + phosphate
preferred substrate
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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-trisphosphate + phosphate
-
-
-
-
?
1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 1,3,4-trisphosphate + phosphate
-
-
-
-
?
inositol 1,3,4,5-tetrakisphosphate + H2O
?
-
-
-
?
inositol 1,3,4,5-tetrakisphosphate + H2O
?
-
in vitro substrate of SHIP2
-
-
?
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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1-phosphatidyl-1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 1,3,4-trisphosphate + 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
additional information
?
-
1-phosphatidyl-1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 1,3,4-trisphosphate + 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 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
preferred substrate
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
?
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(2R)-2-[(S)-hydroxy(2-phenylbenzo[h]quinolin-4-yl)methyl]piperidin-1-ium
-
(2R)-2-[(S)-[5,7-dichloro-3-adamantyl)naphthalen-1-yl](hydroxy)methyl]piperidin-1-ium
-
2,3-bisphosphoglycerate
-
-
2-[1-(2,4-dichlorobenzyl)-2-methyl-5-(methylmercapto)-1H-indol-3-yl] ethanaminium chloride
-
2-[1-(2-chlorobenzyl)-2-methyl-5-(methylmercapto)-1H-indol-3-yl] ethanaminium chloride
-
2-[1-[(2,4-dichlorophenyl)methyl]-2-methyl-5-(methylsulfanyl)-1H-indol-3-yl]ethan-1-aminium
40% inhibition at 0.5 mM
2-[1-[(2-chlorophenyl)methyl]-2-methyl-5-(methylsulfanyl)-1H-indol-3-yl]ethan-1-aminium
-
3-alpha-aminocholestane
selective inhibitor of isoform SHIP-1
3-[(2,4-dichlorophenyl)methoxy]-N-[(2,6-difluorophenyl)methyl]thiophene-2-carboxamide
AS1938909, competitive inhibitor of SHIP2
3-[(4-chlorophenyl)methoxy]-N-[(1S)-1-phenylethyl]thiophene-2-carboxamide
AS1949490, competitive inhibitor of SHIP2
4-hydroxymercuribenzoate
-
-
AQX-1125
Rosiptor, inhibitor of isoform SHIP-1
benzene 1,2,3,4-tetrayl tetrakis(phosphate)
-
benzene 1,2,3,5-tetrayl tetrakis(phosphate)
-
benzene 1,2,4,5-tetrayl tetrakis(phosphate)
-
biphenyl 2,3',4,5',6-pentayl pentakis(phosphate)
-
inositol hexakissulfate
-
inhibitory at high concentrations
N-(4-[[(4-chlorophenyl)methoxy]methyl]pyridin-2-yl)-2-phenylacetamide
-
N-(4-[[(4-chlorophenyl)methoxy]methyl]pyridin-2-yl)-3-phenylpropanamide
-
N-[4-[(4-chlorophenyl)methoxy]pyridin-2-yl]-2-(2,6-difluorophenyl)acetamide
-
N-[4-[(4-chlorophenyl)methoxy]pyridin-2-yl]-2-phenylacetamide
-
N-[4-[(4-chlorophenyl)methoxy]pyridin-2-yl]-3-phenylpropanamide
-
neomycin
-
partial inhibition
phosphatidylinositol 4,5-bisphosphate
-
strong inhibition at low micromolar concentrations
phosphatidylinositol 4-phosphate
-
inhibition at low micromolar concentrations
sodium stibogluconate
inhibitor of isoform SHIP-1
TNO155
inhibitor of isoform SHIP-2
vanadate
-
partial inhibition at millimolar concentrations
NSC13480
development of stereoselctive synthetic route to inhibitor
NSC305787
development of stereoselctive synthetic route to inhibitor
additional information
an amine tethered to the quinoline core is required for SHIP inhibition
-
additional information
not inhibited by 3-alpha-aminocholestane
-
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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0.001 - 0.088
1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate
0.0316 - 0.1
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate
0.082 - 0.126
Inositol 1,3,4,5-tetrakisphosphate
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
0.043
1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate
wild type enzyme, at pH 7.0 and 23°C
0.059
1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate
mutant enzyme R649A, at pH 7.0 and 23°C
0.061
1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate
mutant enzyme F593D/L597D, at pH 7.0 and 23°C
0.088
1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate
-
wild type enzyme, at pH 7.5 and 25°C
0.0316
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate
-
mutant enzyme D360A/N362A, at pH 7.5 and 25°C
0.0738
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate
-
wild type enzyme, at pH 7.5 and 25°C
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
0.082
Inositol 1,3,4,5-tetrakisphosphate
mutant enzyme F593D/L597D, at pH 7.0 and 23°C
0.098
Inositol 1,3,4,5-tetrakisphosphate
wild type enzyme, at pH 7.0 and 23°C
0.126
Inositol 1,3,4,5-tetrakisphosphate
mutant enzyme R649A, at pH 7.0 and 23°C
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metabolism
-
the enzyme participates in the insulin signalling pathway in vivo
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
malfunction
apoptosis in MDA-MB-231 cells is increased in SHIP2-depleted cells as compared to control cells
malfunction
disruption of the enzyme-Mena interaction in cancer cells leads to attenuated capacity for extracellular matrix degradation and invasion in vitro, as well as reduced metastasis in vivo
malfunction
enzyme deficiency leads to myeloproliferation and B-cell lymphoma in mice
malfunction
enzyme depletion inhibits cell migration of glioblastoma cells
malfunction
enzyme mutations are associated with opsismodysplasia. Mice expressing a germline catalytically inactive SHIP2 mutant protein are viable, but have defects in the development of muscle, adipose tissue and the female genital tract, as well as in somatic growth
malfunction
isoform SHIP2 inhibition or knockdown inhibits cell migration and reduces phosphorylated protein kinase B levels, resulting in sensitivity to chemotherapeutics
physiological function
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
-
SHIP is involved in platelet activation evoked by thrombin
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
-
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
physiological function
high glucose induces SHIP2 mRNA and protein levels in HepG2 cells. Overexpression of a dominant negative mutant SHIP2 ameliorates high glucose-induced de novo lipogenesis and secretion of apoB containing lipoprotein in HepG2 cells. Overexpression of the SHIP2 dominant negative mutant decreases high glucose-induced apoB containing lipoproteins secretion via reduction in reactive oxygen species generation, JNK phosphorylation and Akt activation. AMPK/mTOR/SREBP1 is the signaling pathway that mediates the effects of SHIP2 modulation on hepatic de novo lipogenesis
physiological function
isoform SHIP1 inhibits haematopoietic cell proliferation, inhibits Akt signalling and regulates immune cell function in vitro and in vivo
physiological function
isoform SHIP2 functions as oncogene in colorectal cancer by regulating protein kinase B activation
physiological function
isoform SHIP2 regulates Akt signalling in metabolic tissues
physiological function
overexpression of the wild-ype SHIP2 gene leads to a higher total lipid content (28%) compared to control, whereas overexpression of the dominant negative SHIP2 gene reduces total lipid content in oleate treated cells by 40%. Overexpression of SHIP2 wild-type also leads to a significant increase in both secretion of apoB100 containing lipoproteins and de novo lipogenesis. Overexpression of the SHIP2 dominant negative gene prevents oleate-induced de novo lipogenesis and secretion of apoB100 containing lipoproteins in HepG2 cells
physiological function
the enzyme acts as a negative regulator of immune response and haematopoietic progenitor cell proliferation/survival, and as an inducer of cellular apoptosis. Isoform SHIP-1 is also implicated both as a haematopoietic tumour suppressor and activator
physiological function
the enzyme acts as a negative regulator of immune response and haematopoietic progenitor cell proliferation/survival, and as an inducer of cellular apoptosis. Isoform SHIP-2 is a negative regulator of glucose homeostasis and is involved in the maturation and activation of mast cells as well as in phagocytosis directed by Fc receptors for immunoglobulin G, thus regulating allergic reactions and antibacterial defense
physiological function
the enzyme is involved in insulin signalling
physiological function
the enzyme SHIP2 recruits Mena, but not vasodilator-stimulated phosphoprotein, to invadopodia
physiological function
-
the enzyme's activity controls 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate binding by RAP1 and, thus, transcriptional silencing of variant surface glycoprotein genes
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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
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