PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 31836657-10 2020 Inhibition of SHIP1/SHIP2 reduced cellular survival and S6 phosphorylation and enhanced basal calcium levels in human CLL cells. Calcium 94-101 inositol polyphosphate-5-phosphatase D Homo sapiens 14-19 11805146-4 2002 In addition, we show that defects of calcium mobilization and c-Jun NH2-terminal kinase (JNK) activation in Vav3-deficient cells are relieved by deletion of a PIP3 hydrolyzing enzyme, SH2 domain-containing inositol polyphosphate 5"-phosphatase (SHIP). Calcium 37-44 inositol polyphosphate-5-phosphatase D Homo sapiens 184-243 16601135-5 2006 Cas and c-Cbl, known to function in podosomes of osteoclasts, were identified as novel proteins binding to the SHIP SH2 domain by mass spectrometric analysis, and this interaction appeared to be dependent on the Src kinase activity. Calcium 0-3 inositol polyphosphate-5-phosphatase D Homo sapiens 111-115 16236046-0 2005 Calcium antagonists and deep gingival pockets in the population-based SHIP study. Calcium 0-7 inositol polyphosphate-5-phosphatase D Homo sapiens 70-74 10779347-8 2000 However, studies with an Shc-deficient B-cell line indicated that Shc-SHIP complex formation is not required and that other proteins that bind these tyrosines may be important in FcgammaRIIB1/SHIP-mediated calcium inhibition. Calcium 206-213 inositol polyphosphate-5-phosphatase D Homo sapiens 192-196 11709085-0 2001 FcgammaRIIB-mediated inhibition of T-cell receptor signal transduction involves the phosphorylation of SH2-containing inositol 5-phosphatase (SHIP), dephosphorylation of the linker of activated T-cells (LAT) and inhibition of calcium mobilization. Calcium 226-233 inositol polyphosphate-5-phosphatase D Homo sapiens 142-146 11418650-4 2001 SHIP-deficient B cell blasts display efficient FcgammaRIIB-dependent inhibition of calcium mobilization as well as Akt and extracellular signal-related protein kinase phosphorylation. Calcium 83-90 inositol polyphosphate-5-phosphatase D Homo sapiens 0-4 10779347-3 2000 While point mutations of the signature motifs in the inositol phosphatase domain abolish SHIP"s ability to inhibit calcium flux in B cells, little is known about the function of the evolutionarily conserved, putative noncatalytic regions of SHIP in vivo. Calcium 115-122 inositol polyphosphate-5-phosphatase D Homo sapiens 89-93 9597145-6 1998 The regulation of calcium responses involves a network of tyrosine kinases (e.g. lyn, syk), tyrosine or lipid phosphatases (CD45, SHP-1, SHIP), and accessory molecules (CD21/CD19, CD22, FcR gamma 2b). Calcium 18-25 inositol polyphosphate-5-phosphatase D Homo sapiens 137-141 9857188-7 1998 These results suggest that SHIP prevents SF from triggering degranulation of normal BMMCs, and does so by hydrolyzing PIP3, which in turn limits extracellular calcium entry at a step after the release of intracellular calcium. Calcium 159-166 inositol polyphosphate-5-phosphatase D Homo sapiens 27-31 9857188-7 1998 These results suggest that SHIP prevents SF from triggering degranulation of normal BMMCs, and does so by hydrolyzing PIP3, which in turn limits extracellular calcium entry at a step after the release of intracellular calcium. Calcium 218-225 inositol polyphosphate-5-phosphatase D Homo sapiens 27-31 8805703-4 1996 SHIP, by hydrolysing the 5-phosphate of phosphatidylinositol(3,4,5)P3 and inositol(1,3,4,5)P4, suggests a mechanism by which Fc(gamma)RIIB can inhibit calcium influx and downstream responses triggered by immune receptors. Calcium 151-158 inositol polyphosphate-5-phosphatase D Homo sapiens 0-4