[1]
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NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ENZYME ACTIVITY, AND TISSUE SPECIFICITY.
DOI=10.1006/bbrc.1996.1161; PubMed=8769125 [NCBI, ExPASy, EBI, Israel, Japan]
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).
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[2]
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NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, AND INTERACTION WITH SHC1.
PubMed=8874179 [NCBI, ExPASy, EBI, Israel, Japan]
Ware M.D.,
Rosten P.,
Damen J.E.,
Liu L.,
Humphries R.K.,
Krystal G.;
"Cloning and characterization of human SHIP, the 145-kD inositol 5-phosphatase that associates with SHC after cytokine stimulation.";
Blood 88:2833-2840(1996).
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[3]
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NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE [MRNA] OF 1-1139 (ISOFORM 1), ENZYME ACTIVITY, AND INTERACTION WITH GRB2.
TISSUE=Lung;
DOI=10.1016/S0960-9822(02)00511-0; PubMed=8723348 [NCBI, ExPASy, EBI, Israel, Japan]
Kavanaugh W.M.,
Pot D.A.,
Chin S.M.,
Deuter-Reinhard M.,
Jefferson A.B.,
Norris F.A.,
Masiarz F.R.,
Cousens L.S.,
Majerus P.W.,
Williams L.T.;
"Multiple forms of an inositol polyphosphate 5-phosphatase form signaling complexes with Shc and Grb2.";
Curr. Biol. 6:438-445(1996).
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[4]
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NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
PubMed=9058707 [NCBI, ExPASy, EBI, Israel, Japan]
Geier S.J.,
Algate P.A.,
Carlberg K.,
Flowers D.,
Friedman C.,
Trask B.,
Rohrschneider L.R.;
"The human SHIP gene is differentially expressed in cell lineages of the bone marrow and blood.";
Blood 89:1876-1885(1997).
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[5]
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NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, PHOSPHORYLATION, AND INTERACTION WITH GRB2.
PubMed=9108392 [NCBI, ExPASy, EBI, Israel, Japan]
Odai H.,
Sasaki K.,
Iwamatsu A.,
Nakamoto T.,
Ueno H.,
Yamagata T.,
Mitani K.,
Yazaki Y.,
Hirai H.;
"Purification and molecular cloning of SH2- and SH3-containing inositol polyphosphate-5-phosphatase, which is involved in the signaling pathway of granulocyte-macrophage colony-stimulating factor, erythropoietin, and Bcr-Abl.";
Blood 89:2745-2756(1997).
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[6]
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NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=B-cell, and Lymph;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
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[7]
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INTERACTION WITH SLAMF1.
PubMed=10229804 [NCBI, ExPASy, EBI, Israel, Japan]
Mikhalap S.V.,
Shlapatska L.M.,
Berdova A.G.,
Law C.L.,
Clark E.A.,
Sidorenko S.P.;
"CDw150 associates with src-homology 2-containing inositol phosphatase and modulates CD95-mediated apoptosis.";
J. Immunol. 162:5719-5727(1999).
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[8]
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FUNCTION.
PubMed=12421919 [NCBI, ExPASy, EBI, Israel, Japan]
Freeburn R.W.,
Wright K.L.,
Burgess S.J.,
Astoul E.,
Cantrell D.A.,
Ward S.G.;
"Evidence that SHIP-1 contributes to phosphatidylinositol 3,4,5-trisphosphate metabolism in T lymphocytes and can regulate novel phosphoinositide 3-kinase effectors.";
J. Immunol. 169:5441-5450(2002).
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[9]
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PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-865 AND TYR-1022, AND MASS SPECTROMETRY.
DOI=10.1016/j.cell.2007.11.025; PubMed=18083107 [NCBI, ExPASy, EBI, Israel, Japan]
Rikova K.,
Guo A.,
Zeng Q.,
Possemato A.,
Yu J.,
Haack H.,
Nardone J.,
Lee K.,
Reeves C.,
Li Y.,
Hu Y.,
Tan Z.,
Stokes M.,
Sullivan L.,
Mitchell J.,
Wetzel R.,
Macneill J.,
Ren J.M.,
Yuan J., ![]()
Bakalarski C.E.,
Villen J.,
Kornhauser J.M.,
Smith B.,
Li D.,
Zhou X.,
Gygi S.P.,
Gu T.-L.,
Polakiewicz R.D.,
Rush J.,
Comb M.J.;
"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer.";
Cell 131:1190-1203(2007).
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[10]
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VARIANT GLU-685.
DOI=10.1038/sj.leu.2402725; PubMed=12529653 [NCBI, ExPASy, EBI, Israel, Japan]
Luo J.-M.,
Yoshida H.,
Komura S.,
Ohishi N.,
Pan L.,
Shigeno K.,
Hanamura I.,
Miura K.,
Iida S.,
Ueda R.,
Naoe T.,
Akao Y.,
Ohno R.,
Ohnishi K.;
"Possible dominant-negative mutation of the SHIP gene in acute myeloid leukemia.";
Leukemia 17:1-8(2003).
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[11]
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SUBCELLULAR LOCATION, PHOSPHORYLATION, AND INTERACTION WITH DOK1.
DOI=10.1016/S0898-6568(00)00073-5; PubMed=10822173 [NCBI, ExPASy, EBI, Israel, Japan]
Dunant N.M.,
Wisniewski D.,
Strife A.,
Clarkson B.,
Resh M.D.;
"The phosphatidylinositol polyphosphate 5-phosphatase SHIP1 associates with the dok1 phosphoprotein in bcr-Abl transformed cells.";
Cell. Signal. 12:317-326(2000).
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[12]
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PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-915, AND MASS SPECTROMETRY.
DOI=10.1038/nbt1046; PubMed=15592455 [NCBI, ExPASy, EBI, Israel, Japan]
Rush J.,
Moritz A.,
Lee K.A.,
Guo A.,
Goss V.L.,
Spek E.J.,
Zhang H.,
Zha X.-M.,
Polakiewicz R.D.,
Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
Nat. Biotechnol. 23:94-101(2005).
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[13]
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FUNCTION.
DOI=10.1016/j.cellsig.2006.03.012; PubMed=16682172 [NCBI, ExPASy, EBI, Israel, Japan]
Vaillancourt M.,
Levasseur S.,
Tremblay M.-L.,
Marois L.,
Rollet-Labelle E.,
Naccache P.H.;
"The Src homology 2-containing inositol 5-phosphatase 1 (SHIP1) is involved in CD32a signaling in human neutrophils.";
Cell. Signal. 18:2022-2032(2006).
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- FUNCTION: Phosphatidylinositol (PtdIns) phosphatase that specifically hydrolyzes the 5-phosphate of phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3) to produce PtdIns(3,4)P2, thereby negatively regulating the PI3K (phosphoinositide 3-kinase) pathways. Acts as a negative regulator of B-cell antigen receptor signaling. Mediates signaling from the FC-gamma-RIIB receptor (FCGR2B), playing a central role in terminating signal transduction from activating immune/hematopoietic cell receptor systems. Acts as a negative regulator of myeloid cell proliferation/survival and chemotaxis, mast cell degranulation, immune cells homeostasis, integrin alpha-IIb/beta-3 signaling in platelets and JNK signaling in B-cells. Regulates proliferation of osteoclast precursors, macrophage programming, phagocytosis and activation and is required for endotoxin tolerance. Involved in the control of cell-cell junctions, CD32a signaling in neutrophils and modulation of EGF-induced phospholipase C activity. Key regulator of neutrophil migration, by governing the formation of the leading edge and polarization required for chemotaxis. Modulates FCGR3/CD16-mediated cytotoxicity in NK cells. Mediates the activin/TGF-beta-induced apoptosis through its Smad-dependent expression. May also hydrolyze PtdIns(1,3,4,5)P4, and could thus affect the levels of the higher inositol polyphosphates like InsP6.
- CATALYTIC ACTIVITY: Phosphatidylinositol 3,4,5-trisphosphate + H2O = phosphatidylinositol 3,4-bisphosphate + phosphate.
- ENZYME REGULATION: Activated upon translocation to the sites of synthesis of PtdIns(3,4,5)P3 in the membrane (By similarity).
- SUBUNIT: Interacts with tyrosine phosphorylated forms of SHC1, DOK1, DOK3, PTPN11/SHP-2, SLAMF1/CD150. Interacts with PTPN11 in response to IL-3. Interacts with receptors EPOR, MS4A2/FCER1B and FCER1G, FCGR2A, FCGR2B and FCGR3. Interacts with GRB2 and PLCG1. Interacts with tyrosine kinases SRC and TEC. Interacts with FCGR2A, leading to regulate gene expression during the phagocytic process. Interacts with c-Met/MET (By similarity).
- INTERACTION:
P08631:HCK; NbExp=1; IntAct=EBI-1380477, EBI-346340;
- SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane protein. Note=Translocates to the plasma membrane when activated, translocation is probably due to different mechanisms depending on the stimulus and cell type. Partly translocated via its SH2 domain which mediates interaction with tyrosine phosphorylated receptors such as the FC-gamma-RIIB receptor (FCGR2B) or CD16/FCGR3. Tyrosine phosphorylation may also participate to membrane localization (By similarity).
- ALTERNATIVE PRODUCTS:
3 named isoforms [FASTA] produced by alternative splicing.
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| Name | 2 |
| Isoform ID | Q92835-2 |
| Features which should be applied to build the isoform sequence: VSP_027978. |
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- TISSUE SPECIFICITY: Specifically expressed in immune and hematopoietic cells. Expressed in bone marrow and blood cells. Levels vary considerably within this compartment. Present in at least 74% of immature CD34+ cells, whereas within the more mature population of CD33+ cells, it is present in only 10% of cells. Present in the majority of T-cells, while it is present in a minority of B-cells (at protein level).
- DOMAIN: The SH2 domain interacts with tyrosine phosphorylated forms of proteins such as SHC1 or PTPN11/SHP-2. It competes with that of GRB2 for binding to phosphorylated SHC1 to inhibit the Ras pathway. It is also required for tyrosine phosphorylation (By similarity).
- DOMAIN: The NPXY sequence motif found in many tyrosine-phosphorylated proteins is required for the specific binding of the PID domain (By similarity).
- PTM: Tyrosine phosphorylated by the members of the SRC family after exposure to a diverse array of extracellular stimuli such as cytokines, growth factors, antibodies, chemokines, integrin ligands and hypertonic and oxidative stress. Phosphorylated upon IgG receptor FCGR2B-binding.
- SIMILARITY: Belongs to the inositol-1,4,5-trisphosphate 5-phosphatase family.
- SIMILARITY: Contains 1 SH2 domain.
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