PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 29852247-8 2018 Furthermore, we identified serine and tyrosine phosphorylation as a molecular mechanism for the regulation of nucleocytoplasmic shuttling of SHIP1 where tyrosine phosphorylation of distinct residues i.e. Y864, Y914, Y1021 reduces nuclear localization, whereas serine phosphorylation at S933 enhances nuclear localization of SHIP1. Tyrosine 38-46 inositol polyphosphate-5-phosphatase D Homo sapiens 324-329 31308061-5 2019 LYN kinase and phosphatases INPP5D (SHIP1) and PTPN6 (SHP1) displayed greatest levels of tyrosine phosphorylation when DOCK4 expression levels were reduced using DOCK4-specific siRNA. Tyrosine 89-97 inositol polyphosphate-5-phosphatase D Homo sapiens 28-34 31308061-5 2019 LYN kinase and phosphatases INPP5D (SHIP1) and PTPN6 (SHP1) displayed greatest levels of tyrosine phosphorylation when DOCK4 expression levels were reduced using DOCK4-specific siRNA. Tyrosine 89-97 inositol polyphosphate-5-phosphatase D Homo sapiens 36-41 10822173-4 2000 Expression of Bcr-Abl induced tyrosine phosphorylation of both Dok1 and SHIP1 and the formation of a Dok1/SHIP1 complex. Tyrosine 30-38 inositol polyphosphate-5-phosphatase D Homo sapiens 72-77 10822173-5 2000 Tyr(P) SHIP1 was also bound to Shc in Bcr-Abl expressing cells. Tyrosine 0-3 inositol polyphosphate-5-phosphatase D Homo sapiens 7-12 29852247-8 2018 Furthermore, we identified serine and tyrosine phosphorylation as a molecular mechanism for the regulation of nucleocytoplasmic shuttling of SHIP1 where tyrosine phosphorylation of distinct residues i.e. Y864, Y914, Y1021 reduces nuclear localization, whereas serine phosphorylation at S933 enhances nuclear localization of SHIP1. Tyrosine 38-46 inositol polyphosphate-5-phosphatase D Homo sapiens 141-146 29852247-8 2018 Furthermore, we identified serine and tyrosine phosphorylation as a molecular mechanism for the regulation of nucleocytoplasmic shuttling of SHIP1 where tyrosine phosphorylation of distinct residues i.e. Y864, Y914, Y1021 reduces nuclear localization, whereas serine phosphorylation at S933 enhances nuclear localization of SHIP1. Tyrosine 153-161 inositol polyphosphate-5-phosphatase D Homo sapiens 141-146 29852247-8 2018 Furthermore, we identified serine and tyrosine phosphorylation as a molecular mechanism for the regulation of nucleocytoplasmic shuttling of SHIP1 where tyrosine phosphorylation of distinct residues i.e. Y864, Y914, Y1021 reduces nuclear localization, whereas serine phosphorylation at S933 enhances nuclear localization of SHIP1. Tyrosine 153-161 inositol polyphosphate-5-phosphatase D Homo sapiens 324-329 27206658-5 2016 In this line, Lyn has been demonstrated to tyrosine-phosphorylate and activate SHIP1, thereby constituting a negative feedback control of PI3K-mediated signals. Tyrosine 43-51 inositol polyphosphate-5-phosphatase D Homo sapiens 79-84 27550373-2 2016 SHIP function is thought to require the dual engagement of the BCR and negative regulatory coreceptors as only the latter appear capable of recruiting SHIP from the cytosol to the plasma membrane by the virtue of phosphorylated immunoreceptor tyrosine-based inhibitory motifs. Tyrosine 243-251 inositol polyphosphate-5-phosphatase D Homo sapiens 0-4 27456487-8 2016 BCR-induced association of SHIP with binding partner Shc1 is dependent on Syk, as is tyrosine phosphorylation of both partners. Tyrosine 85-93 inositol polyphosphate-5-phosphatase D Homo sapiens 27-31 27206658-7 2016 RESULTS: Lyn-/- BMMCs, which show a suppressed degranulation response, were found to exhibit abrogated tyrosine phosphorylation of SHIP1 as well. Tyrosine 103-111 inositol polyphosphate-5-phosphatase D Homo sapiens 131-136 25312647-6 2015 SLAMF7-mediated inhibition in NK cells lacking EAT-2 was mediated by SH2 domain-containing inositol phosphatase 1 (SHIP-1), which was recruited via tyrosine 261 of SLAMF7. Tyrosine 148-156 inositol polyphosphate-5-phosphatase D Homo sapiens 69-113 26304991-9 2015 The interaction with SHIP1 is of particular importance because it binds to the critical tyrosine residues at the C terminus of PSTPIP2, which is known to be crucial for its PEST-phosphatase-independent inhibitory effects in different cellular systems. Tyrosine 88-96 inositol polyphosphate-5-phosphatase D Homo sapiens 21-26 25312647-6 2015 SLAMF7-mediated inhibition in NK cells lacking EAT-2 was mediated by SH2 domain-containing inositol phosphatase 1 (SHIP-1), which was recruited via tyrosine 261 of SLAMF7. Tyrosine 148-156 inositol polyphosphate-5-phosphatase D Homo sapiens 115-121 22641604-4 2012 Tyrosine phosphorylation of SHIP1/2 has been considered to be the determining regulatory modification. Tyrosine 0-8 inositol polyphosphate-5-phosphatase D Homo sapiens 28-35 24405601-8 2014 CONCLUSION: This study provides evidence for the decreased FcgammaRIIb1 translocation to lipid rafts as well as for the reduced tyrosine-phosphorylated FcgammaRIIb1 and SHIP recruitment to FcgammaRIIb1 in lipid rafts of B lymphocytes from SLE patients after stimulated with IgG anti-mu. Tyrosine 128-136 inositol polyphosphate-5-phosphatase D Homo sapiens 169-173 22820502-7 2012 In agreement with this model, we found that the SHIP1 mutant F28L located in the FLVR motif of the SH2 domain was incapable of binding tyrosine-phosphorylated proteins including the GM-CSF receptor and that the SHIP1 mutant Q1076X lost its ability to bind to the C-terminal SH3 domain of the adapter protein Grb2. Tyrosine 135-143 inositol polyphosphate-5-phosphatase D Homo sapiens 48-53 22820502-9 2012 In summary, our data indicate that SHIP1 mutations detected in human leukemia patients impair the negative regulatory function of SHIP1 on PI3K/AKT signaling in leukemia cells either directly by reduced enzymatic activity or indirectly by disturbed protein interaction with tyrosine-phosphorylated membrane receptors or adapter proteins. Tyrosine 274-282 inositol polyphosphate-5-phosphatase D Homo sapiens 35-40 22820502-9 2012 In summary, our data indicate that SHIP1 mutations detected in human leukemia patients impair the negative regulatory function of SHIP1 on PI3K/AKT signaling in leukemia cells either directly by reduced enzymatic activity or indirectly by disturbed protein interaction with tyrosine-phosphorylated membrane receptors or adapter proteins. Tyrosine 274-282 inositol polyphosphate-5-phosphatase D Homo sapiens 130-135 19682241-9 2009 The novel platelet adapter Dok-3 and the structurally related Dok-1 are tyrosine phosphorylated in an Src kinase-independent manner downstream of alphaIIbbeta3 in human platelets, leading to an interaction with Grb2 and SHIP-1. Tyrosine 72-80 inositol polyphosphate-5-phosphatase D Homo sapiens 220-226 22078222-3 2011 In studies reported here, Src homology-2 (SH2)-containing inositol 5-phosphatase SHIP-1 and its adaptor Dok-1 were found to be constitutively phosphorylated in anergic B cells, and activation of this inhibitory circuit was dependent on Src-family kinase activity and consequent to biased BCR immunoreceptor tyrosine-based activation motif (ITAM) monophosphorylation. Tyrosine 307-315 inositol polyphosphate-5-phosphatase D Homo sapiens 81-87 22182704-7 2012 Interestingly, whereas the SHIP1 SH2-domain can be pulled-down with phospho-peptides corresponding to the immunoreceptor tyrosine-based activation motif (ITAM) of Ig-alpha from detergent lysates, no interaction between full-length SHIP1 and the phosphorylated Ig-alpha ITAM can be observed. Tyrosine 121-129 inositol polyphosphate-5-phosphatase D Homo sapiens 27-32 22182704-7 2012 Interestingly, whereas the SHIP1 SH2-domain can be pulled-down with phospho-peptides corresponding to the immunoreceptor tyrosine-based activation motif (ITAM) of Ig-alpha from detergent lysates, no interaction between full-length SHIP1 and the phosphorylated Ig-alpha ITAM can be observed. Tyrosine 121-129 inositol polyphosphate-5-phosphatase D Homo sapiens 231-236 20308635-7 2010 Lyn B also showed increased binding of tyrosine-phosphorylated proteins, which included the negative regulatory lipid phosphatase SHIP-1. Tyrosine 39-47 inositol polyphosphate-5-phosphatase D Homo sapiens 130-136 18424727-5 2008 This effect derives from Kit-mediated tyrosine phosphorylation of CD300a and recruitment of the SHIP-1 but not of SH2-containing protein phosphatase 1. Tyrosine 38-46 inositol polyphosphate-5-phosphatase D Homo sapiens 96-102 16682172-7 2006 CD32a cross-linking also induced the tyrosine phosphorylation of SHIP1, its translocation to the plasma membrane and its co-immunoprecipitation with CD32a. Tyrosine 37-45 inositol polyphosphate-5-phosphatase D Homo sapiens 65-70 16682172-9 2006 PP2, a Src kinase inhibitor, inhibited the tyrosine phosphorylation of SHIP1 as well as its translocation to the plasma membrane. Tyrosine 43-51 inositol polyphosphate-5-phosphatase D Homo sapiens 71-76 18322174-4 2008 We show here that two of these tyrosines provide two binding sites for SHIP1, that LAT recruits SHIP1 in vivo, and that SHIP1 recruitment is enhanced in NTAL-deficient cells. Tyrosine 31-40 inositol polyphosphate-5-phosphatase D Homo sapiens 71-76 18322174-4 2008 We show here that two of these tyrosines provide two binding sites for SHIP1, that LAT recruits SHIP1 in vivo, and that SHIP1 recruitment is enhanced in NTAL-deficient cells. Tyrosine 31-40 inositol polyphosphate-5-phosphatase D Homo sapiens 96-101 18322174-4 2008 We show here that two of these tyrosines provide two binding sites for SHIP1, that LAT recruits SHIP1 in vivo, and that SHIP1 recruitment is enhanced in NTAL-deficient cells. Tyrosine 31-40 inositol polyphosphate-5-phosphatase D Homo sapiens 96-101 18253061-6 2008 Of interest to note is that tyrosine-phosphorylated neogenin and uncoordinated 5 H2 (Unc5H2) not only bind to the Src homology 2 (SH2) domains of Fyn and SHP2, but also interact with the SH2 domain of SHIP1, suggesting a differential signaling between DCC and neogenin/Unc5H2. Tyrosine 28-36 inositol polyphosphate-5-phosphatase D Homo sapiens 201-206 17046573-5 2006 We also found that Ins/IGF-1 stimulates the tyrosine phosphorylation of SHIP1 and, in keeping with this, Ins/IGF-1-induced PKB phosphorylation is higher in SHIP1-/- BMMCs and is inhibited in SHIP+/+ as well as SHIP1-/- BMMCs with inhibitors of phosphatidylinositol-3-kinase (PI3K). Tyrosine 44-52 inositol polyphosphate-5-phosphatase D Homo sapiens 72-77 15486046-12 2005 In summary, 1) SHIP-WT and SHIPDeltaIP expression inhibit insulin and PDGF stimulated Ras, MAPK kinase, and MAPK activities; 2) SHIP associates with tyrosine phosphorylated Shc, and the proline-rich sequences in SHIP associate with Grb2 and titrate out SOS to form Shc*Grb2*SHIP complexes; and 3) dissociation of SOS from the Shc*Grb2 complex inhibits Ras GTP loading, leading to decreased signaling through the MAPK pathway. Tyrosine 149-157 inositol polyphosphate-5-phosphatase D Homo sapiens 27-31 16876851-0 2006 SHIP1/2 interaction with tyrosine phosphorylated peptides mimicking an immunoreceptor signalling motif. Tyrosine 25-33 inositol polyphosphate-5-phosphatase D Homo sapiens 0-7 17046573-5 2006 We also found that Ins/IGF-1 stimulates the tyrosine phosphorylation of SHIP1 and, in keeping with this, Ins/IGF-1-induced PKB phosphorylation is higher in SHIP1-/- BMMCs and is inhibited in SHIP+/+ as well as SHIP1-/- BMMCs with inhibitors of phosphatidylinositol-3-kinase (PI3K). Tyrosine 44-52 inositol polyphosphate-5-phosphatase D Homo sapiens 72-76 16360206-1 2006 Proteins that bear immunoreceptor tyrosine based inhibitory motifs (ITIM) are believed to participate in the repression of cell activation via phosphatases such as SHP-1, SHP-2 and/or SHIP-1. Tyrosine 34-42 inositol polyphosphate-5-phosphatase D Homo sapiens 184-190 16115887-3 2005 Inhibition is mediated by the recruitment of the inositol phosphatase, SHIP, to the Fc gammaRIIB1 phosphorylated tyrosine-based inhibitory motif (ITIM). Tyrosine 113-121 inositol polyphosphate-5-phosphatase D Homo sapiens 71-75 15735664-0 2005 The SH2-domian-containing inositol 5-phosphatase (SHIP)-2 binds to c-Met directly via tyrosine residue 1356 and involves hepatocyte growth factor (HGF)-induced lamellipodium formation, cell scattering and cell spreading. Tyrosine 86-94 inositol polyphosphate-5-phosphatase D Homo sapiens 50-54 15486046-3 2005 Insulin and PDGF both stimulated tyrosine phosphorylation of SHIP-WT and of SHIPDeltaIP, and tyrosine phosphorylation of SHIP-associated proteins increased after ligand stimulation. Tyrosine 33-41 inositol polyphosphate-5-phosphatase D Homo sapiens 61-65 15486046-4 2005 Tyrosine-phosphorylated PDGFR, IR, and insulin receptor substrate-1 all immunoprecipitated with SHIP. Tyrosine 0-8 inositol polyphosphate-5-phosphatase D Homo sapiens 96-100 15486046-8 2005 This association was primarily between the SHIP-SH2 domain and the phosphorylated tyrosine residues of Shc because no association was observed when the 3YF-Shc mutant was coexpressed with SHIP. Tyrosine 82-90 inositol polyphosphate-5-phosphatase D Homo sapiens 43-47 15486046-12 2005 In summary, 1) SHIP-WT and SHIPDeltaIP expression inhibit insulin and PDGF stimulated Ras, MAPK kinase, and MAPK activities; 2) SHIP associates with tyrosine phosphorylated Shc, and the proline-rich sequences in SHIP associate with Grb2 and titrate out SOS to form Shc*Grb2*SHIP complexes; and 3) dissociation of SOS from the Shc*Grb2 complex inhibits Ras GTP loading, leading to decreased signaling through the MAPK pathway. Tyrosine 149-157 inositol polyphosphate-5-phosphatase D Homo sapiens 15-19 15169881-5 2004 Our studies showed that engagement of 2B4 on NK cells triggered a tyrosine phosphorylation signal implicating 2B4, Vav-1, and, to a lesser extent, SHIP-1 and c-Cbl. Tyrosine 66-74 inositol polyphosphate-5-phosphatase D Homo sapiens 147-153 15486046-12 2005 In summary, 1) SHIP-WT and SHIPDeltaIP expression inhibit insulin and PDGF stimulated Ras, MAPK kinase, and MAPK activities; 2) SHIP associates with tyrosine phosphorylated Shc, and the proline-rich sequences in SHIP associate with Grb2 and titrate out SOS to form Shc*Grb2*SHIP complexes; and 3) dissociation of SOS from the Shc*Grb2 complex inhibits Ras GTP loading, leading to decreased signaling through the MAPK pathway. Tyrosine 149-157 inositol polyphosphate-5-phosphatase D Homo sapiens 27-31 15456754-0 2004 Two distinct tyrosine-based motifs enable the inhibitory receptor FcgammaRIIB to cooperatively recruit the inositol phosphatases SHIP1/2 and the adapters Grb2/Grap. Tyrosine 13-21 inositol polyphosphate-5-phosphatase D Homo sapiens 129-136 15456754-4 2004 We show here that a second tyrosine-containing motif in the intracytoplasmic domain of FcgammaRIIB is required for SHIP1/2 to be coprecipitated with the receptor. Tyrosine 27-35 inositol polyphosphate-5-phosphatase D Homo sapiens 115-122 15363123-1 2004 The SH2 domain containing inositol 5"-phosphatase (SHIP) was initially described as a 145 kD protein phosphorylated on tyrosines upon growth factor and cytokine stimulation. Tyrosine 119-128 inositol polyphosphate-5-phosphatase D Homo sapiens 4-49 15363123-1 2004 The SH2 domain containing inositol 5"-phosphatase (SHIP) was initially described as a 145 kD protein phosphorylated on tyrosines upon growth factor and cytokine stimulation. Tyrosine 119-128 inositol polyphosphate-5-phosphatase D Homo sapiens 51-55 12882960-4 2003 In the human monocytic cell line, THP-1, SHIP-1 became tyrosine-phosphorylated following M-CSF activation in a Src family kinase-dependent manner. Tyrosine 55-63 inositol polyphosphate-5-phosphatase D Homo sapiens 41-47 14993273-4 2004 Our biochemical analyses showed that the Dok-3-SHIP-1 complex acts by selectively inhibiting the B-cell receptor (BCR)-evoked activation of the Jun N-terminal protein kinase (JNK) cascade without affecting overall protein tyrosine phosphorylation or activation of previously described SHIP-1 targets like Btk and Akt/PKB. Tyrosine 222-230 inositol polyphosphate-5-phosphatase D Homo sapiens 47-53 12506011-4 2003 We show that phosphoinositide 3 (PI 3)-kinase associates with 4 tyrosine-phosphorylated proteins in primary human erythroid progenitors, namely insulin receptor substrate-2 (IRS2), Src homology 2 domain-containing inositol 5"-phosphatase (SHIP), Grb2-associated binder-1 (Gab1), and the Epo receptor (EpoR). Tyrosine 64-72 inositol polyphosphate-5-phosphatase D Homo sapiens 181-237 12370370-3 2002 Recent studies have established that clustering FcgammaR on human myeloid cells causes tyrosine phosphorylation of Src homology 2 domain-containing inositol polyphosphate phosphatase (SHIP). Tyrosine 87-95 inositol polyphosphate-5-phosphatase D Homo sapiens 115-182 12393695-4 2002 Moreover, CD16 stimulation on human primary natural killer (NK) cells induces the rapid and transient translocation of SHIP-1 in the lipid-enriched plasma membrane microdomains, termed rafts, where it associates with tyrosine-phosphorylated zeta chain and shc adaptor protein. Tyrosine 217-225 inositol polyphosphate-5-phosphatase D Homo sapiens 119-125 12370370-3 2002 Recent studies have established that clustering FcgammaR on human myeloid cells causes tyrosine phosphorylation of Src homology 2 domain-containing inositol polyphosphate phosphatase (SHIP). Tyrosine 87-95 inositol polyphosphate-5-phosphatase D Homo sapiens 184-188 12370370-4 2002 However, it is not known how these immunoreceptor tyrosine-based activation motif (ITAM)-bearing phagocytic FcgammaR activate SHIP, or whether the activation of SHIP by ITAMs has any functional relevance. Tyrosine 50-58 inositol polyphosphate-5-phosphatase D Homo sapiens 126-130 11567986-5 2001 In embryonic stem cells, s-SHIP partners with the adapter protein Grb2 without tyrosine phosphorylation and is present constitutively at the cell membrane. Tyrosine 79-87 inositol polyphosphate-5-phosphatase D Homo sapiens 27-31 11453982-4 2001 As a model compound, we synthesized a bisphosphopeptide, combining the sequences of p-ITIM and the N-terminal tyrosine phosphorylated motif of SHIP with a flexible spacer. Tyrosine 110-118 inositol polyphosphate-5-phosphatase D Homo sapiens 143-147 10875931-1 2000 The SH2-containing inositol 5"-phosphatase (SHIP) is tyrosine-phosphorylated in response to cytokines such as interleukin (IL)-3, granulocyte-macrophage colony-stimulating factor, and macrophage colony-stimulating factor. Tyrosine 53-61 inositol polyphosphate-5-phosphatase D Homo sapiens 4-42 11035084-2 2000 Previous studies concluded that inhibitory signal transduction by FcgammaRIIB is mediated solely by its immunoreceptor tyrosine-based inhibition motif (ITIM) that, when phosphorylated, recruits the SH2-containing inositol 5"- phosphatase SHIP and the SH2-containing tyrosine phosphatases SHP-1 and SHP-2. Tyrosine 119-127 inositol polyphosphate-5-phosphatase D Homo sapiens 238-242 11035084-4 2000 Although the ITIM appears to contain all the structural information required for receptor-mediated tyrosine phosphorylation of SHIP, phosphorylation is enhanced when the C-terminal sequence is present. Tyrosine 99-107 inositol polyphosphate-5-phosphatase D Homo sapiens 127-131 10875931-1 2000 The SH2-containing inositol 5"-phosphatase (SHIP) is tyrosine-phosphorylated in response to cytokines such as interleukin (IL)-3, granulocyte-macrophage colony-stimulating factor, and macrophage colony-stimulating factor. Tyrosine 53-61 inositol polyphosphate-5-phosphatase D Homo sapiens 44-48 10875931-3 2000 It has been recently shown that IL-4 induces tyrosine phosphorylation of SHIP, implicating the phosphatase in IL-4 processes. Tyrosine 45-53 inositol polyphosphate-5-phosphatase D Homo sapiens 73-77 10875931-4 2000 Tyrosine kinases, Jak1 and Jak3, involved in IL-4 signaling can associate with SHIP, yet only Jak1 can tyrosine-phosphorylate SHIP when co-expressed. Tyrosine 103-111 inositol polyphosphate-5-phosphatase D Homo sapiens 126-130 10794720-1 2000 SH2-containing inositol-5-phosphatase 1 (SHIP1) was originally identified as a 145 kDa protein that became tyrosine-phosphorylated in response to multiple cytokines. Tyrosine 107-115 inositol polyphosphate-5-phosphatase D Homo sapiens 0-39 10794720-1 2000 SH2-containing inositol-5-phosphatase 1 (SHIP1) was originally identified as a 145 kDa protein that became tyrosine-phosphorylated in response to multiple cytokines. Tyrosine 107-115 inositol polyphosphate-5-phosphatase D Homo sapiens 41-46 10794720-3 2000 We found recently that SHIP1 was present in human blood platelets as an Ins(1,3,4, 5)P(4)-phosphatase and a PtdIns(3,4,5)P(3)-5-phosphatase that became tyrosine-phosphorylated and was relocated to the cytoskeleton in an integrin-dependent manner. Tyrosine 152-160 inositol polyphosphate-5-phosphatase D Homo sapiens 23-28 10794720-4 2000 Here we report biochemical and pharmacological evidence that the tyrosine kinase pp60(c-src) is constitutively associated with SHIP1 and is involved in its tyrosine phosphorylation downstream of integrin engagement in thrombin-activated human platelets. Tyrosine 65-73 inositol polyphosphate-5-phosphatase D Homo sapiens 127-132 10794720-6 2000 Moreover, the integrin-dependent relocation of SHIP1 to the cytoskeleton did not require its tyrosine phosphorylation. Tyrosine 93-101 inositol polyphosphate-5-phosphatase D Homo sapiens 47-52 10794720-7 2000 These results suggest that SHIP1 is first recruited to the integrin-linked signalling complexes and then becomes tyrosine-phosphorylated through a Src-kinase-dependent mechanism but independently of the actin cytoskeleton reorganization. Tyrosine 113-121 inositol polyphosphate-5-phosphatase D Homo sapiens 27-32 10597315-4 1999 When stably expressed in K562 cells, SHIP was found to be constitutively tyrosine phosphorylated and associated with endogenous Shc and Grb-2. Tyrosine 73-81 inositol polyphosphate-5-phosphatase D Homo sapiens 37-41 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. Tyrosine 149-158 inositol polyphosphate-5-phosphatase D Homo sapiens 192-196 10755621-4 2000 These effects require the recruitment and tyrosine phosphorylation of the phosphatidylinositol 5-phosphatase SHIP, which further recruits p62dok via the latter"s phosphotyrosine-binding domain. Tyrosine 42-50 inositol polyphosphate-5-phosphatase D Homo sapiens 109-113 10660611-1 2000 Ship1 (SH2 inositol 5-phosphatase 1) has been shown to be a target of tyrosine phosphorylation downstream of cytokine and immunoregulatory receptors. Tyrosine 70-78 inositol polyphosphate-5-phosphatase D Homo sapiens 0-5 10660611-1 2000 Ship1 (SH2 inositol 5-phosphatase 1) has been shown to be a target of tyrosine phosphorylation downstream of cytokine and immunoregulatory receptors. Tyrosine 70-78 inositol polyphosphate-5-phosphatase D Homo sapiens 7-35 10660611-5 2000 EPO activates the tyrosine phosphorylation of Ship1, resulting in the interdependent recruitment of Shc and Grb2. Tyrosine 18-26 inositol polyphosphate-5-phosphatase D Homo sapiens 46-51 10660611-7 2000 Utilizing a panel of EPO-R deletion and tyrosine mutants, we have discovered remarkable redundancy in Ship1 recruitment. Tyrosine 40-48 inositol polyphosphate-5-phosphatase D Homo sapiens 102-107 10660611-8 2000 EPO-R Tyr(401) appears to be a major site of Ship1 binding; however, Tyr(429) and Tyr(431) can also serve to recruit Ship1. Tyrosine 6-9 inositol polyphosphate-5-phosphatase D Homo sapiens 45-50 10623804-2 2000 In vitro peptide binding experiments using phosphotyrosine-containing sequences derived from the immunoreceptor tyrosine-based inhibitory motif (ITIM) known to mediate Fc gamma RIIB1 effects suggest that the receptor uses SH2-containing inositol phosphatase (SHIP) and SH2-containing phosphotyrosine phosphatase (SHP)-1, as well as SHP-2 as effectors. Tyrosine 50-58 inositol polyphosphate-5-phosphatase D Homo sapiens 222-257 10623804-2 2000 In vitro peptide binding experiments using phosphotyrosine-containing sequences derived from the immunoreceptor tyrosine-based inhibitory motif (ITIM) known to mediate Fc gamma RIIB1 effects suggest that the receptor uses SH2-containing inositol phosphatase (SHIP) and SH2-containing phosphotyrosine phosphatase (SHP)-1, as well as SHP-2 as effectors. Tyrosine 50-58 inositol polyphosphate-5-phosphatase D Homo sapiens 259-263 10499514-0 1999 Role of the Src homology 2 (SH2) domain and C-terminus tyrosine phosphorylation sites of SH2-containing inositol phosphatase (SHIP) in the regulation of insulin-induced mitogenesis. Tyrosine 55-63 inositol polyphosphate-5-phosphatase D Homo sapiens 89-124 10499514-0 1999 Role of the Src homology 2 (SH2) domain and C-terminus tyrosine phosphorylation sites of SH2-containing inositol phosphatase (SHIP) in the regulation of insulin-induced mitogenesis. Tyrosine 55-63 inositol polyphosphate-5-phosphatase D Homo sapiens 126-130 10499514-4 1999 Although SHIP can bind via its 917/1020-Tyr residues and SH2 domain to Shc PTB domain and 317-Tyr residue, respectively, insulin-induced SHIP association with Shc was more greatly decreased in 2F-SHIP cells than that in deltaSH2-SHIP cells. Tyrosine 40-43 inositol polyphosphate-5-phosphatase D Homo sapiens 9-13 10499514-4 1999 Although SHIP can bind via its 917/1020-Tyr residues and SH2 domain to Shc PTB domain and 317-Tyr residue, respectively, insulin-induced SHIP association with Shc was more greatly decreased in 2F-SHIP cells than that in deltaSH2-SHIP cells. Tyrosine 94-97 inositol polyphosphate-5-phosphatase D Homo sapiens 9-13 10499514-3 1999 Insulin-stimulated tyrosine phosphorylation of WT-SHIP and deltaSH2-SHIP, whereas tyrosine phosphorylation of 2F-SHIP was not detectable, indicating that 917/1020-Tyr are key phosphorylation sites on SHIP. Tyrosine 19-27 inositol polyphosphate-5-phosphatase D Homo sapiens 50-54 10352260-0 1999 The SH2-containing 5"-inositol phosphatase (SHIP) is tyrosine phosphorylated after Fc gamma receptor clustering in monocytes. Tyrosine 53-61 inositol polyphosphate-5-phosphatase D Homo sapiens 4-42 10457218-4 1999 Following aggregation of FcgammaRI, SHIP is rapidly and transiently tyrosine phosphorylated and becomes associated with the adapter molecule Shc. Tyrosine 68-76 inositol polyphosphate-5-phosphatase D Homo sapiens 36-40 10457218-5 1999 Shc also becomes tyrosine phosphorylated and translocates from the cytoplasm to the membrane fraction concomitant with the association between Shc and SHIP. Tyrosine 17-25 inositol polyphosphate-5-phosphatase D Homo sapiens 151-155 10457220-4 1999 Using BIACORE(R)2000 analysis, we determined that both SHP1 and SHP2 bound to the tyrosine-phosphorylated cytoplasmic tail of Ly49A with affinities in the nanomolar range, whilst SHIP showed no binding. Tyrosine 82-90 inositol polyphosphate-5-phosphatase D Homo sapiens 179-183 10494849-1 1999 The activation of many hematopoietic cells via cytokine receptors, as well as B and T cell receptors, leads to the tyrosine phosphorylation of Shc and its association with both Grb2-Sos1 complexes and with a 145 kDa protein referred to as the SH2 containing inositol 5-phosphatase (SHIP1). Tyrosine 115-123 inositol polyphosphate-5-phosphatase D Homo sapiens 282-287 10494849-6 1999 SHIP1 was tyrosine phosphorylated in resting naive T cells. Tyrosine 10-18 inositol polyphosphate-5-phosphatase D Homo sapiens 0-5 10382761-6 1999 Moreover, P-ITIM-bound SHP-2 dephosphorylates synthetic peptides corresponding to the sites of tyrosine phosphorylation on SHIP and Shc, indicating that these proteins are its potential substrates. Tyrosine 95-103 inositol polyphosphate-5-phosphatase D Homo sapiens 123-127 10352260-5 1999 We find that clustering of either Fc gamma RIIa or Fc gamma RI is effective in inducing SHIP phosphorylation, that SHIP binds in vitro to a phosphorylated immunoreceptor tyrosine-based activation motif, peptide from the cytoplasmic domain of Fc gamma RIIa in activation-independent fashion, although SHIP binding increases upon cell activation, and that Fc gamma RIIb and Fc gamma RIIc are not responsible for the observed SHIP phosphorylation. Tyrosine 170-178 inositol polyphosphate-5-phosphatase D Homo sapiens 115-119 10352260-6 1999 These findings prompt us to propose that SHIP inhibits Fc gamma R-mediated signal transduction by engaging immunoreceptor tyrosine-based activation motif-containing cytoplasmic domains of Fc gamma RIIa and Fc gamma RI-associated gamma-chain. Tyrosine 122-130 inositol polyphosphate-5-phosphatase D Homo sapiens 41-45 10352260-0 1999 The SH2-containing 5"-inositol phosphatase (SHIP) is tyrosine phosphorylated after Fc gamma receptor clustering in monocytes. Tyrosine 53-61 inositol polyphosphate-5-phosphatase D Homo sapiens 44-48 10352260-3 1999 Continuing to assess systematically the molecules participating in the cascade, we have found that the SH2-containing 5"-inositol phosphatase (SHIP) is phosphorylated on tyrosine early and transiently after Fc gamma R clustering. Tyrosine 170-178 inositol polyphosphate-5-phosphatase D Homo sapiens 103-141 10352260-3 1999 Continuing to assess systematically the molecules participating in the cascade, we have found that the SH2-containing 5"-inositol phosphatase (SHIP) is phosphorylated on tyrosine early and transiently after Fc gamma R clustering. Tyrosine 170-178 inositol polyphosphate-5-phosphatase D Homo sapiens 143-147 10352260-5 1999 We find that clustering of either Fc gamma RIIa or Fc gamma RI is effective in inducing SHIP phosphorylation, that SHIP binds in vitro to a phosphorylated immunoreceptor tyrosine-based activation motif, peptide from the cytoplasmic domain of Fc gamma RIIa in activation-independent fashion, although SHIP binding increases upon cell activation, and that Fc gamma RIIb and Fc gamma RIIc are not responsible for the observed SHIP phosphorylation. Tyrosine 170-178 inositol polyphosphate-5-phosphatase D Homo sapiens 88-92 10352260-5 1999 We find that clustering of either Fc gamma RIIa or Fc gamma RI is effective in inducing SHIP phosphorylation, that SHIP binds in vitro to a phosphorylated immunoreceptor tyrosine-based activation motif, peptide from the cytoplasmic domain of Fc gamma RIIa in activation-independent fashion, although SHIP binding increases upon cell activation, and that Fc gamma RIIb and Fc gamma RIIc are not responsible for the observed SHIP phosphorylation. Tyrosine 170-178 inositol polyphosphate-5-phosphatase D Homo sapiens 115-119 10352260-5 1999 We find that clustering of either Fc gamma RIIa or Fc gamma RI is effective in inducing SHIP phosphorylation, that SHIP binds in vitro to a phosphorylated immunoreceptor tyrosine-based activation motif, peptide from the cytoplasmic domain of Fc gamma RIIa in activation-independent fashion, although SHIP binding increases upon cell activation, and that Fc gamma RIIb and Fc gamma RIIc are not responsible for the observed SHIP phosphorylation. Tyrosine 170-178 inositol polyphosphate-5-phosphatase D Homo sapiens 115-119 10397152-3 1999 After being phosphorylated by BCR-activated tyrosine kinases, the immunoreceptor tyrosine-based inhibitory motif (P-ITIM) of Fc gamma RIIb recruits SH2 domain containing protein tyrosine phosphatase(s) (PTPs) and polyphosphoinositol 5-phosphatase (SHIP) to the vicinity of BCR, which in turn dephosphorylate their specific substrates. Tyrosine 44-52 inositol polyphosphate-5-phosphatase D Homo sapiens 248-252 10229804-6 1999 Both Fgr and SHIP interact with phosphorylated tyrosines in CDw150"s cytoplasmic tail. Tyrosine 47-56 inositol polyphosphate-5-phosphatase D Homo sapiens 13-17 10229804-9 1999 The ability of CDw150 to regulate cell death does not correlate with serine phosphorylation of the Akt kinase, but does correlate with SHIP tyrosine dephosphorylation. Tyrosine 140-148 inositol polyphosphate-5-phosphatase D Homo sapiens 135-139 10207047-2 1999 We and others have reported that SHIP is rapidly tyrosine phosphorylated upon B cell antigen receptor (BCR) cross-linking and forms a complex with the adapter protein Shc. Tyrosine 49-57 inositol polyphosphate-5-phosphatase D Homo sapiens 33-37 10350061-6 1999 These results suggest that overlapping immunoreceptor tyrosine-based inhibition motif/immunoreceptor tyrosine-based activation motif-like motifs within platelet endothelial cell adhesion molecule 1 mediate differential interactions between the Src homology 2 containing signalling proteins SHP-1, SHP-2, SHIP and PLC-gamma1. Tyrosine 54-62 inositol polyphosphate-5-phosphatase D Homo sapiens 304-308 10194451-12 1999 These observations suggest (1) that SHIP1 and SHIP2 may have a different hierarchy of binding SH3 containing proteins and therefore may modulate different signaling pathways and/or localize to different cellular compartments and (2) that they may be substrates for tyrosine phosphorylation by different tyrosine kinases. Tyrosine 265-273 inositol polyphosphate-5-phosphatase D Homo sapiens 36-41 10194451-13 1999 Because recent evidence has clearly implicated both PI(3,4, 5)P3 and PI(3,4)P2 in growth factor-mediated signaling, our finding that both SHIP1 and SHIP2 are constitutively tyrosine phosphorylated in CML primary hematopoietic progenitor cells may thus have important implications in p210(bcr/abl)-mediated myeloid expansion. Tyrosine 173-181 inositol polyphosphate-5-phosphatase D Homo sapiens 138-143 10194437-0 1999 Erythropoietin induces the tyrosine phosphorylation of GAB1 and its association with SHC, SHP2, SHIP, and phosphatidylinositol 3-kinase. Tyrosine 27-35 inositol polyphosphate-5-phosphatase D Homo sapiens 96-100 9295037-7 1997 In addition, we show that point mutation of the amino acid residue in position tyrosine-2 of Fc gammaRIIB and KIR ITIM abolihes their binding to SHP-1 and SHP-2, but leaves intact the association of SHIP with Fc gammaRIIB ITIM. Tyrosine 79-87 inositol polyphosphate-5-phosphatase D Homo sapiens 199-203 10066815-6 1999 This interaction is mediated by the binding of the SH2 domains of the p85 subunit of PI3K to a tyrosine-based motif in the C-terminal region of SHIP. Tyrosine 95-103 inositol polyphosphate-5-phosphatase D Homo sapiens 144-148 9393882-5 1997 Both phosphatases in the complex were tyrosine phosphorylated, and the amount of SHIP coprecipitating with SHP-2 was inversely related to the amount of SHIP coprecipitating with SHC. Tyrosine 38-46 inositol polyphosphate-5-phosphatase D Homo sapiens 152-156 10080542-10 1999 SHIP is also tyrosine-phosphorylated and associates with Shc after FL simulation. Tyrosine 13-21 inositol polyphosphate-5-phosphatase D Homo sapiens 0-4 9918857-8 1999 In THP-1 cells, p85 associates inducibly with tyrosine phosphorylated SHIP, p100 and p120. Tyrosine 46-54 inositol polyphosphate-5-phosphatase D Homo sapiens 70-74 9852043-7 1998 Using mutants of FcgammaRIIB1 and SHIP-deficient B cells, we demonstrate that inhibition of Akt activity is mediated by the immune cell tyrosine-based inhibitory motif within FcgammaRIIB1 as well as SHIP. Tyrosine 136-144 inositol polyphosphate-5-phosphatase D Homo sapiens 34-38 9857188-6 1998 Although PI-3-kinase inhibitors blocked the release of intracellular calcium, implicating PIP3, and PLCgamma-2 was slightly more tyrosine phosphorylated in SHIP-/- cells, the increase in inositol-1,4,5-trisphosphate (IP3) and intracellular calcium levels were identical in SHIP-/- and SHIP+/+ BMMCs. Tyrosine 129-137 inositol polyphosphate-5-phosphatase D Homo sapiens 156-160 10395202-1 1998 Previous studies by our lab and others established that co-crosslinking sIg and IgG receptor FcgammaRIIb in B cells in a feedback suppression model (negative signaling) promoted tyrosine phosphorylation of the inositol 5-phosphatase SHIP and its interaction with Shc and that these events were associated with inhibition of the Ras pathway. Tyrosine 178-186 inositol polyphosphate-5-phosphatase D Homo sapiens 233-237 9341117-6 1997 Thrombin stimulation induced a tyrosine phosphorylation of SHIP, this effect being prevented if platelets were not shaken or if RGD-containing peptides were present, indicating an aggregation-dependent, integrin-mediated event. Tyrosine 31-39 inositol polyphosphate-5-phosphatase D Homo sapiens 59-63 9341117-7 1997 Moreover, although the intrinsic phosphatase activity of SHIP did not appear to be significantly increased, tyrosine-phosphorylated SHIP was relocated to the actin cytoskeleton upon activation in an aggregation- and integrin engagement-dependent manner. Tyrosine 108-116 inositol polyphosphate-5-phosphatase D Homo sapiens 132-136 9341117-8 1997 Finally, the striking correlation observed between phosphatidylinositol 3,4-bisphosphate production and the tyrosine phosphorylation of SHIP, as well as its relocation to the cytoskeleton upon thrombin stimulation, suggest a role for SHIP in the aggregation-dependent and GpIIb-IIIa-mediated accumulation of this important phosphoinositide. Tyrosine 108-116 inositol polyphosphate-5-phosphatase D Homo sapiens 136-140 9328837-1 1997 SHIP is a SH2 domain-containing inositol polyphosphatase that is selectively tyrosine phosphorylated and associated with the adapter protein Shc in B lymphocytes upon co-crosslinking surface immunoglobulin and Fc gamma RIIB1. Tyrosine 77-85 inositol polyphosphate-5-phosphatase D Homo sapiens 0-4 9058707-3 1997 SHIP also contains several potential SH3 domain-binding sites, an SH2 domain for binding other tyrosine phosphorylated proteins, and an enzymatic activity that removes the phosphate from the 5 position of phosphatidylinositol 3,4,5-phosphate or from inositol 1,3,4,5-phosphate. Tyrosine 95-103 inositol polyphosphate-5-phosphatase D Homo sapiens 0-4 9099679-5 1997 During T cell receptor signaling, tyrosine phosphorylation of SHIP and its association with Shc occurred only upon activation. Tyrosine 34-42 inositol polyphosphate-5-phosphatase D Homo sapiens 62-66 9099679-6 1997 We demonstrate that the phosphotyrosine binding domain of Shc is necessary and sufficient for its association with tyrosine-phosphorylated SHIP. Tyrosine 31-39 inositol polyphosphate-5-phosphatase D Homo sapiens 139-143 9099679-7 1997 Through site-directed mutagenesis, we have identified two tyrosines on SHIP, Tyr-917, and Tyr-1020, as the principal contact sites for the Shc-phosphotyrosine binding domain. Tyrosine 58-67 inositol polyphosphate-5-phosphatase D Homo sapiens 71-75 9099679-7 1997 Through site-directed mutagenesis, we have identified two tyrosines on SHIP, Tyr-917, and Tyr-1020, as the principal contact sites for the Shc-phosphotyrosine binding domain. Tyrosine 77-80 inositol polyphosphate-5-phosphatase D Homo sapiens 71-75 9203414-2 1997 Recent studies have shown that this motif, when phosphorylated on tyrosine, forms a docking site for the Src homology 2 recognition domains of the protein tyrosine phosphatase SHP-1 and the inositol 5-phosphatase SHIP. Tyrosine 66-74 inositol polyphosphate-5-phosphatase D Homo sapiens 213-217 9232445-7 1997 Among the P-ITIM associated tyr phosphorylated components, the 145 kDa one was identified as the inositol polyphosphate 5-phosphatase, SHIP and the 72 kDa protein as the protein tyrosine phosphatase (PTP) SHP2, whereas SHP1 was not detected. Tyrosine 28-31 inositol polyphosphate-5-phosphatase D Homo sapiens 135-139 9052858-0 1996 The SHIP phosphatase becomes associated with Fc gammaRIIB1 and is tyrosine phosphorylated during "negative" signaling. Tyrosine 66-74 inositol polyphosphate-5-phosphatase D Homo sapiens 4-8 8805618-0 1996 Negative signaling in B lymphocytes induces tyrosine phosphorylation of the 145-kDa inositol polyphosphate 5-phosphatase, SHIP. Tyrosine 44-52 inositol polyphosphate-5-phosphatase D Homo sapiens 122-126 8805618-4 1996 Since co-clustering of the BCR and Fc gamma RII also down-regulates proliferation induced by Ag receptor stimulation, we hypothesize that tyrosine phosphorylation of SHIP and its association with Shc contribute to negative signaling through effects on inositol and phosphatidylinositol metabolism. Tyrosine 138-146 inositol polyphosphate-5-phosphatase D Homo sapiens 166-170 9052858-5 1996 SHIP is inducibly tyrosine phosphorylated following BCR-FcgammaRIIB1 co-ligation. Tyrosine 18-26 inositol polyphosphate-5-phosphatase D Homo sapiens 0-4 9052858-6 1996 Further, we observe SHIP association with tyrosine phosphorylated FcgammaRIIB1 in intact cells following BCR-FcgammaRIIB1 co-ligation. Tyrosine 42-50 inositol polyphosphate-5-phosphatase D Homo sapiens 20-24 9052858-7 1996 To a much lesser but significant degree, tyrosine phosphorylation of SHIP is also observed upon BCR ligation. Tyrosine 41-49 inositol polyphosphate-5-phosphatase D Homo sapiens 69-73