SH2-domain containing Phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase 2 is an enzyme that in humans is encoded by the INPPL1gene.[1][2]
INPPL1 encodes inositol polyphosphate-5 phosphatase-like 1, a protein that in addition to the phosphatase domain contains an SH2 (src-homology domain 2) motif.[2]
↑Wisniewski D, Strife A, Swendeman S, Erdjument-Bromage H, Geromanos S, Kavanaugh WM, Tempst P, Clarkson B (April 1999). "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 (8): 2707–20. PMID10194451.
↑Pesesse X, Dewaste V, De Smedt F, Laffargue M, Giuriato S, Moreau C, Payrastre B, Erneux C (July 2001). "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 (30): 28348–55. doi:10.1074/jbc.M103537200. PMID11349134.
↑Habib T, Hejna JA, Moses RE, Decker SJ (July 1998). "Growth factors and insulin stimulate tyrosine phosphorylation of the 51C/SHIP2 protein". J. Biol. Chem. 273 (29): 18605–9. doi:10.1074/jbc.273.29.18605. PMID9660833.
↑Vandenbroere I, Paternotte N, Dumont JE, Erneux C, Pirson I (January 2003). "The c-Cbl-associated protein and c-Cbl are two new partners of the SH2-containing inositol polyphosphate 5-phosphatase SHIP2". Biochem. Biophys. Res. Commun. 300 (2): 494–500. doi:10.1016/s0006-291x(02)02894-2. PMID12504111.
Further reading
Pesesse X, Deleu S, De Smedt F, Drayer L, Erneux C (1997). "Identification of a second SH2-domain-containing protein closely related to the phosphatidylinositol polyphosphate 5-phosphatase SHIP". Biochem. Biophys. Res. Commun. 239 (3): 697–700. doi:10.1006/bbrc.1997.7538. PMID9367831.
Habib T, Hejna JA, Moses RE, Decker SJ (1998). "Growth factors and insulin stimulate tyrosine phosphorylation of the 51C/SHIP2 protein". J. Biol. Chem. 273 (29): 18605–9. doi:10.1074/jbc.273.29.18605. PMID9660833.
Pesesse X, Moreau C, Drayer AL, Woscholski R, Parker P, Erneux C (1998). "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 (3): 301–3. doi:10.1016/S0014-5793(98)01255-1. PMID9824312.
Wisniewski D, Strife A, Swendeman S, Erdjument-Bromage H, Geromanos S, Kavanaugh WM, Tempst P, Clarkson B (1999). "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 (8): 2707–20. PMID10194451.
Bruyns C, Pesesse X, Moreau C, Blero D, Erneux C (1999). "The two SH2-domain-containing inositol 5-phosphatases SHIP1 and SHIP2 are coexpressed in human T lymphocytes". Biol. Chem. 380 (7–8): 969–74. doi:10.1515/BC.1999.120. PMID10494849.
Schurmans S, Carrió R, Behrends J, Pouillon V, Merino J, Clément S (2000). "The mouse SHIP2 (Inppl1) gene: complementary DNA, genomic structure, promoter analysis, and gene expression in the embryo and adult mouse". Genomics. 62 (2): 260–71. doi:10.1006/geno.1999.5995. PMID10610720.
Muraille E, Bruhns P, Pesesse X, Daëron M, Erneux C (2000). "The SH2 domain containing inositol 5-phosphatase SHIP2 associates to the immunoreceptor tyrosine-based inhibition motif of Fc gammaRIIB in B cells under negative signaling". Immunol. Lett. 72 (1): 7–15. doi:10.1016/S0165-2478(00)00162-0. PMID10789675.
Marion E, Kaisaki PJ, Pouillon V, Gueydan C, Levy JC, Bodson A, Krzentowski G, Daubresse JC, Mockel J, Behrends J, Servais G, Szpirer C, Kruys V, Gauguier D, Schurmans S (2002). "The gene INPPL1, encoding the lipid phosphatase SHIP2, is a candidate for type 2 diabetes in rat and man". Diabetes. 51 (7): 2012–7. doi:10.2337/diabetes.51.7.2012. PMID12086927.
Prasad N, Topping RS, Decker SJ (2003). "Src family tyrosine kinases regulate adhesion-dependent tyrosine phosphorylation of 5'-inositol phosphatase SHIP2 during cell attachment and spreading on collagen I.". J. Cell Sci. 115 (Pt 19): 3807–15. doi:10.1242/jcs.00070. PMID12235291.
Tridandapani S, Wang Y, Marsh CB, Anderson CL (2002). "Src homology 2 domain-containing inositol polyphosphate phosphatase regulates NF-kappa B-mediated gene transcription by phagocytic Fc gamma Rs in human myeloid cells". J. Immunol. 169 (8): 4370–8. doi:10.4049/jimmunol.169.8.4370. PMID12370370.
Vandenbroere I, Paternotte N, Dumont JE, Erneux C, Pirson I (2003). "The c-Cbl-associated protein and c-Cbl are two new partners of the SH2-containing inositol polyphosphate 5-phosphatase SHIP2". Biochem. Biophys. Res. Commun. 300 (2): 494–500. doi:10.1016/S0006-291X(02)02894-2. PMID12504111.
Pengal RA, Ganesan LP, Fang H, Marsh CB, Anderson CL, Tridandapani S (2003). "SHIP-2 inositol phosphatase is inducibly expressed in human monocytes and serves to regulate Fcgamma receptor-mediated signaling". J. Biol. Chem. 278 (25): 22657–63. doi:10.1074/jbc.M302907200. PMID12690104.
Kaisaki PJ, Delépine M, Woon PY, Sebag-Montefiore L, Wilder SP, Menzel S, Vionnet N, Marion E, Riveline JP, Charpentier G, Schurmans S, Levy JC, Lathrop M, Farrall M, Gauguier D (2004). "Polymorphisms in type II SH2 domain-containing inositol 5-phosphatase (INPPL1, SHIP2) are associated with physiological abnormalities of the metabolic syndrome". Diabetes. 53 (7): 1900–4. doi:10.2337/diabetes.53.7.1900. PMID15220217.