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Information on EC 3.1.3.36 - phosphoinositide 5-phosphatase and Organism(s) Mus musculus and UniProt Accession Q9JII1
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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
-
domain-containing
- actin
- pten
- 3-kinase
-
endocytic
-
x-linked
-
ptdins3,4,5p3
- cataract
- clathrin
- dynamin
- cilia
-
clathrin-mediated
-
tensin
-
polyphosphoinositide
- dent
-
clathrin-coated
-
endophilins
-
voltage-sensing
-
joubert
- amphiphysins
- ciliopathies
-
ptdins3,4p2
-
ptdins4p
- 1,3,4,5-tetrakisphosphate
-
itims
-
fcgammariib
-
tubulopathy
-
pleckstrin
-
tyrosine-based
-
immunoreceptor
- ship-1
- 3,4-bisphosphate
-
nephrocalcinosis
- eps15
-
ciliogenesis
-
microrna-155
-
arl13b
- phosphatidylinositol-3,4,5-trisphosphate
- 3,4,5-triphosphate
-
4-phosphatase
- myotubularins
-
hypercalciuria
- inpp4b
-
intersectin
-
n-wasp
- phosphatidylinositol-4-phosphate
-
myotubular
- molecular biology
- medicine
The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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, inositol 5-phosphatase, ci-vsp, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
5PTase
-
-
-
-
diphosphoinositide phosphatase
-
-
-
-
inositol triphosphate 5-phosphomonoesterase
-
-
-
-
Lowe's oculocerebrorenal syndrome protein
-
-
-
-
OCRL protein
-
-
-
-
p150
-
-
-
-
phosphatase, triphosphoinositide
-
-
-
-
phosphatidyl 4,5-bisphosphate-specific phosphomonoesterase
-
-
-
-
phosphatidyl bisphosphate phosphatase
-
-
-
-
phosphatidyl-inositol 4,5-bisphosphate 5-phosphatase
-
-
-
-
phosphatidyl-myo-inositol-4,5-bisphosphate phosphatase
-
-
-
-
phosphatidyl-myo-inositol-4,5-bisphosphate phosphohydrolase
-
-
-
-
phosphatidylinositol 4,5-bisphosphate phosphatase
-
-
-
-
phosphatidylinositol-bisphosphatase
-
-
-
-
Phosphoinositide 5-phosphatase
-
-
-
-
PIP2 phosphatase
-
-
-
-
PtdIns(4,5)P2 5-phosphatase
-
-
-
-
SHIP2
Synaptojanin
-
-
-
-
triphosphoinositide phosphatase
-
-
-
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triphosphoinositide phosphomonoesterase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
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.
CAS REGISTRY NUMBER
COMMENTARY
9036-01-5
-
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
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
-
-
-
?
phosphatidylinositol 3,4,5-trisphosphate + H2O
phosphatidylinositol 3,4-bisphosphate + phosphate
-
-
?
phosphatidylinositol 3,5-bisphosphate + H2O
phosphatidylinositol 3-phosphate + 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
1D-myo-inositol 1,3,4-trisphosphate + 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, 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
-
-
?
D-myo-phosphatidylinositol 3,4,5-trisphosphate
D-myo-phosphatidylinositol 3,4-bisphosphate + phosphate
-
-
-
-
?
phosphatidylinositol-3,4,5-trisphosphate + H2O
phosphatidylinositol-3,4-bisphosphate + phosphate
-
-
-
-
?
phosphatidylinositol-4,5-bisphosphate + H2O
phosphatidylinositol-4-phosphate + phosphate
-
-
-
-
?
additional information
?
-
-
substrate specificity, no activity with 1D-myo-inositol 1,5-bisphosphate, overview
-
-
?
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
-
-
-
-
?
phosphatidylinositol-4,5-bisphosphate + H2O
phosphatidylinositol-4-phosphate + phosphate
-
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
in macrophages infected with Legionella pneumophila the localization of endogenous OCRL1 is identified on Legionella-containing vacuoles containing single or several bacteria
-
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
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
malfunction
metabolism
physiological function
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
-
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 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
-
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
metabolism
-
proline-rich inositol polyphosphate 5-phosphatase is one of the signal-modifying enzymes that play pivotal regulatory roles in PI3K signalling pathway
metabolism
-
SKIP controls PIP3 content in an insulin stimulation-dependent manner
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
-
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
-
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
-
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). INP5E_MOUSE
647
0
71915
Swiss-Prot
other Location (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
centrosomal kinase AURKA phosphorylates INPP5E and thereby increases its 5-phosphatase activity
phosphoprotein
-
SHIP1 is localized to the membrane and is tyrosine phosphorylated during cell adhesion
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
additional information
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant GST-tagged catalytic domains from Escherichia coli strain DH5alpha by glutathione affinity chromatography
-
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)
expression of GST-tagged catalytic domain comprising residues A305-A721, in Escherichia coli strain DH5alpha
-
from oocytes and fertilized eggs, recombinant overexpression of FLAG-tagged proline-rich inositol polyphosphate 5-phosphatase in eggs
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
molecular biology
-
SHIP2 lipid phosphatase activity plays an important role in the metabolism of PtdIns(3,4,5)P3 in response to H2O2
medicine
-
inhibition of SHIP2 for the prevention and/or treatment of type 2 diabetes
medicine
-
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kong, A.M.; Speed, C.J.; O'Malley, C.J.; Layton, M.J.; Meehan, T.; Loveland, K.L.; Cheema, S.; Ooms, L.M.; Mitchell, C.A.
Cloning and characterization of a 72-kDa inositol-polyphosphate 5-phosphatase localized to the Golgi network
J. Biol. Chem.
275
24052-24064
2000
Mus musculus (Q9JII1)
Schmid, A.C.; Wise, H.M.; Mitchell, C.A.; Nussbaum, R.; Woscholski, R.
Type II phosphoinositide 5-phosphatases have unique sensitivities towards fatty acid composition and head group phosphorylation
FEBS Lett.
576
9-13
2004
Homo sapiens, Mus musculus, Rattus norvegicus
Vinciguerra, M.; Foti, M.
PTEN and SHIP2 phosphoinositide phosphatases as negative regulators of insulin signalling
Arch. Physiol. Biochem.
112
89-104
2006
Chlorocebus aethiops, Cricetulus griseus, Mus musculus
Batty, I.H.; van der Kaay, J.; Gray, A.; Telfer, J.F.; Dixon, M.J.; Downes, C.P.
The control of phosphatidylinositol 3,4-bisphosphate concentrations by activation of the Src homology 2 domain containing inositol polyphosphate 5-phosphatase 2, SHIP2
Biochem. J.
407
255-266
2007
Homo sapiens, Mus musculus (Q9JII1)
Zhang, J.; Liu, Z.; Rasschaert, J.; Blero, D.; Deneubourg, L.; Schurmans, S.; Erneux, C.; Pesesse, X.
SHIP2 controls PtdIns(3,4,5)P(3) levels and PKB activity in response to oxidative stress
Cell. Signal.
19
2194-2200
2007
Mus musculus
Grempler, R.; Zibrova, D.; Schoelch, C.; van Marle, A.; Rippmann, J.F.; Redemann, N.
Normalization of prandial blood glucose and improvement of glucose tolerance by liver-specific inhibition of SH2 domain containing inositol phosphatase 2 (SHIP2) in diabetic KKAy mice: SHIP2 inhibition causes insulin-mimetic effects on glycogen metabolism
Diabetes
56
2235-2241
2007
Mus musculus
Leung, W.H.; Bolland, S.
The inositol 5-phosphatase SHIP-2 negatively regulates IgE-induced mast cell degranulation and cytokine production
J. Immunol.
179
95-102
2007
Mus musculus
Nishio, M.; Watanabe, K.; Sasaki, J.; Taya, C.; Takasuga, S.; Iizuka, R.; Balla, T.; Yamazaki, M.; Watanabe, H.; Itoh, R.; Kuroda, S.; Horie, Y.; Foerster, I.; Mak, T.W.; Yonekawa, H.; Penninger, J.M.; Kanaho, Y.; Suzuki, A.; Sasaki, T.
Control of cell polarity and motility by the PtdIns(3,4,5)P3 phosphatase SHIP1
Nat. Cell Biol.
9
36-44
2007
Mus musculus
Weber, S.S.; Ragaz, C.; Hilbi, H.
The inositol polyphosphate 5-phosphatase OCRL1 restricts intracellular growth of Legionella, localizes to the replicative vacuole and binds to the bacterial effector LpnE
Cell. Microbiol.
11
442-460
2008
Dictyostelium discoideum, Homo sapiens, Mus musculus
Deng, X.; Feng, C.; Wang, E.H.; Zhu, Y.Q.; Cui, C.; Zong, Z.H.; Li, G.S.; Liu, C.; Meng, J.; Yu, B.Z.
Influence of proline-rich inositol polyphosphate 5-phosphatase, on early development of fertilized mouse eggs, via inhibition of phosphorylation of Akt
Cell Prolif.
44
156-165
2011
Mus musculus, Mus musculus Kunming
Nakatsu, F.; Perera, R.; Lucast, L.; Zoncu, R.; Domin, J.; Gertler, F.; Toomre, D.; De Camilli, P.
The inositol 5-phosphatase SHIP2 regulates endocytic clathrin-coated pit dynamics
J. Cell Biol.
190
307-315
2010
Mus musculus
Soeda, Y.; Tsuneki, H.; Muranaka, H.; Mori, N.; Hosoh, S.; Ichihara, Y.; Kagawa, S.; Wang, X.; Toyooka, N.; Takamura, Y.; Uwano, T.; Nishijo, H.; Wada, T.; Sasaoka, T.
The inositol phosphatase SHIP2 negatively regulates insulin/IGF-I actions implicated in neuroprotection and memory function in mouse brain
Mol. Endocrinol.
24
1965-1977
2010
Mus musculus (Q6P549), Mus musculus, Mus musculus C57/BL6J (Q6P549)
Ijuin, T.; Takenawa, T.
Role of phosphatidylinositol 3,4,5-trisphosphate (PIP3) 5-phosphatase skeletal muscle- and kidney-enriched inositol polyphosphate phosphatase (SKIP) in myoblast differentiation
J. Biol. Chem.
287
31330-31341
2012
Homo sapiens, Mus musculus
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
Mondal, S.; Subramanian, K.K.; Sakai, J.; Bajrami, B.; Luo, H.R.
Phosphoinositide lipid phosphatase SHIP1 and PTEN coordinate to regulate cell migration and adhesion
Mol. Biol. Cell
23
1219-1230
2012
Mus musculus
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