- INPP5D
Inositol polyphosphate-5-phosphatase, 145kDa, also known as INPP5D, is a human
gene .cite web | title = Entrez Gene: INPP5D inositol polyphosphate-5-phosphatase, 145kDa| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3635| accessdate = ]PBB_Summary
section_title =
summary_text = This gene is a member of the inositol polyphosphate-5-phosphatase (INPP5) family and encodes a protein with an N-terminal SH2 domain, an inositol phosphatase domain, and two C-terminal protein interaction domains. Expression of this protein is restricted to hematopoietic cells where its movement from the cytosol to the plasma membrane is mediated by tyrosine phosphorylation. At the plasma membrane, the protein hydrolyzes the 5' phosphate from phosphatidylinositol (3,4,5)-trisphosphate and inositol-1,3,4,5-tetrakisphosphate, thereby affecting multiple signaling pathways. Overall, the protein functions as a negative regulator of myeliod cell proliferation and survival. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.cite web | title = Entrez Gene: INPP5D inositol polyphosphate-5-phosphatase, 145kDa| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3635| accessdate = ]References
Further reading
PBB_Further_reading
citations =
*cite journal | author=MacDonald SM, Vonakis BM |title=Association of the Src homology 2 domain-containing inositol 5' phosphatase (SHIP) to releasability in human basophils. |journal=Mol. Immunol. |volume=38 |issue= 16-18 |pages= 1323–7 |year= 2003 |pmid= 12217402 |doi=
*cite journal | author=Damen JE, Liu L, Rosten P, "et al." |title=The 145-kDa protein induced to associate with Shc by multiple cytokines is an inositol tetraphosphate and phosphatidylinositol 3,4,5-triphosphate 5-phosphatase. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 4 |pages= 1689–93 |year= 1996 |pmid= 8643691 |doi=
*cite journal | author=Lioubin MN, Algate PA, Tsai S, "et al." |title=p150Ship, a signal transduction molecule with inositol polyphosphate-5-phosphatase activity. |journal=Genes Dev. |volume=10 |issue= 9 |pages= 1084–95 |year= 1996 |pmid= 8654924 |doi=
*cite journal | author=Kavanaugh WM, Pot DA, Chin SM, "et al." |title=Multiple forms of an inositol polyphosphate 5-phosphatase form signaling complexes with Shc and Grb2. |journal=Curr. Biol. |volume=6 |issue= 4 |pages= 438–45 |year= 1997 |pmid= 8723348 |doi=
*cite journal | author=Drayer AL, Pesesse X, De Smedt F, "et al." |title=Cloning and expression of a human placenta inositol 1,3,4,5-tetrakisphosphate and phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase. |journal=Biochem. Biophys. Res. Commun. |volume=225 |issue= 1 |pages= 243–9 |year= 1996 |pmid= 8769125 |doi= 10.1006/bbrc.1996.1161
*cite journal | author=Ware MD, Rosten P, Damen JE, "et al." |title=Cloning and characterization of human SHIP, the 145-kD inositol 5-phosphatase that associates with SHC after cytokine stimulation. |journal=Blood |volume=88 |issue= 8 |pages= 2833–40 |year= 1996 |pmid= 8874179 |doi=
*cite journal | author=Geier SJ, Algate PA, Carlberg K, "et al." |title=The human SHIP gene is differentially expressed in cell lineages of the bone marrow and blood. |journal=Blood |volume=89 |issue= 6 |pages= 1876–85 |year= 1997 |pmid= 9058707 |doi=
*cite journal | author=Odai H, Sasaki K, Iwamatsu A, "et al." |title=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. |journal=Blood |volume=89 |issue= 8 |pages= 2745–56 |year= 1997 |pmid= 9108392 |doi=
*cite journal | author=Liu L, Damen JE, Ware MD, Krystal G |title=Interleukin-3 induces the association of the inositol 5-phosphatase SHIP with SHP2. |journal=J. Biol. Chem. |volume=272 |issue= 17 |pages= 10998–1001 |year= 1997 |pmid= 9110989 |doi=
*cite journal | author=Giuriato S, Payrastre B, Drayer AL, "et al." |title=Tyrosine phosphorylation and relocation of SHIP are integrin-mediated in thrombin-stimulated human blood platelets. |journal=J. Biol. Chem. |volume=272 |issue= 43 |pages= 26857–63 |year= 1997 |pmid= 9341117 |doi=
*cite journal | author=Kuroiwa A, Yamashita Y, Inui M, "et al." |title=Association of tyrosine phosphatases SHP-1 and SHP-2, inositol 5-phosphatase SHIP with gp49B1, and chromosomal assignment of the gene. |journal=J. Biol. Chem. |volume=273 |issue= 2 |pages= 1070–4 |year= 1998 |pmid= 9422771 |doi=
*cite journal | author=Liu Q, Shalaby F, Jones J, "et al." |title=The SH2-containing inositol polyphosphate 5-phosphatase, ship, is expressed during hematopoiesis and spermatogenesis. |journal=Blood |volume=91 |issue= 8 |pages= 2753–9 |year= 1998 |pmid= 9531585 |doi=
*cite journal | author=Zhang S, Broxmeyer HE |title=p85 subunit of PI3 kinase does not bind to human Flt3 receptor, but associates with SHP2, SHIP, and a tyrosine-phosphorylated 100-kDa protein in Flt3 ligand-stimulated hematopoietic cells. |journal=Biochem. Biophys. Res. Commun. |volume=254 |issue= 2 |pages= 440–5 |year= 1999 |pmid= 9918857 |doi= 10.1006/bbrc.1998.9959
*cite journal | author=Mikhalap SV, Shlapatska LM, Berdova AG, "et al." |title=CDw150 associates with src-homology 2-containing inositol phosphatase and modulates CD95-mediated apoptosis. |journal=J. Immunol. |volume=162 |issue= 10 |pages= 5719–27 |year= 1999 |pmid= 10229804 |doi=
*cite journal | author=Pumphrey NJ, Taylor V, Freeman S, "et al." |title=Differential association of cytoplasmic signalling molecules SHP-1, SHP-2, SHIP and phospholipase C-gamma1 with PECAM-1/CD31. |journal=FEBS Lett. |volume=450 |issue= 1-2 |pages= 77–83 |year= 1999 |pmid= 10350061 |doi=
*cite journal | author=Mason JM, Beattie BK, Liu Q, "et al." |title=The SH2 inositol 5-phosphatase Ship1 is recruited in an SH2-dependent manner to the erythropoietin receptor. |journal=J. Biol. Chem. |volume=275 |issue= 6 |pages= 4398–406 |year= 2000 |pmid= 10660611 |doi=
*cite journal | author=Bone H, Welham MJ |title=Shc associates with the IL-3 receptor beta subunit, SHIP and Gab2 following IL-3 stimulation. Contribution of Shc PTB and SH2 domains. |journal=Cell. Signal. |volume=12 |issue= 3 |pages= 183–94 |year= 2000 |pmid= 10704825 |doi=
*cite journal | author=Lemay S, Davidson D, Latour S, Veillette A |title=Dok-3, a novel adapter molecule involved in the negative regulation of immunoreceptor signaling. |journal=Mol. Cell. Biol. |volume=20 |issue= 8 |pages= 2743–54 |year= 2000 |pmid= 10733577 |doi=
*cite journal | author=Poe JC, Fujimoto M, Jansen PJ, "et al." |title=CD22 forms a quaternary complex with SHIP, Grb2, and Shc. A pathway for regulation of B lymphocyte antigen receptor-induced calcium flux. |journal=J. Biol. Chem. |volume=275 |issue= 23 |pages= 17420–7 |year= 2000 |pmid= 10748054 |doi= 10.1074/jbc.M001892200
*cite journal | author=Dunant NM, Wisniewski D, Strife A, "et al." |title=The phosphatidylinositol polyphosphate 5-phosphatase SHIP1 associates with the dok1 phosphoprotein in bcr-Abl transformed cells. |journal=Cell. Signal. |volume=12 |issue= 5 |pages= 317–26 |year= 2000 |pmid= 10822173 |doi=PBB_Controls
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