PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 19955438-4 2009 We have previously shown that phosphorylation of PLC-gamma1 by Itk requires a direct, phosphotyrosine-independent interaction between the Src homology 2 (SH2) domain of PLC-gamma1 and the kinase domain of Itk. Phosphotyrosine 86-101 phospholipase C gamma 1 Homo sapiens 49-59 25916191-4 2015 The SLP-76 phosphotyrosine-containing sequence, pY(173)IDR, does not conform to the canonical recognition motif for an SH2 domain yet binds with significant affinity to the C-terminal SH2 domain of PLCgamma1 (SH2C). Phosphotyrosine 11-26 phospholipase C gamma 1 Homo sapiens 198-207 19955438-4 2009 We have previously shown that phosphorylation of PLC-gamma1 by Itk requires a direct, phosphotyrosine-independent interaction between the Src homology 2 (SH2) domain of PLC-gamma1 and the kinase domain of Itk. Phosphotyrosine 86-101 phospholipase C gamma 1 Homo sapiens 169-179 19955438-6 2009 The binding surface on PLCgamma1 that mediates recognition by Itk highlights a nonclassical binding activity of the well-studied SH2 domain providing further evidence that SH2 domains participate in important signaling interactions beyond recognition of phosphotyrosine. Phosphotyrosine 254-269 phospholipase C gamma 1 Homo sapiens 23-32 31871542-8 2019 These phosphotyrosines provide docking sites for signalling molecules which, in turn, activate Ras/MAPK, PI3K/Akt, and PLC-gamma1/PKC intracellular cascades. Phosphotyrosine 6-22 phospholipase C gamma 1 Homo sapiens 119-129 17620338-4 2007 Here, we demonstrate that endogenous Cbl is essential for ligand-induced ubiquitinylation and degradation of PDGFRbeta; this involves the Cbl TKB domain binding to PDGFRbeta phosphotyrosine 1021, a known phospholipase C (PLC) gamma1 SH2 domain-binding site. Phosphotyrosine 174-189 phospholipase C gamma 1 Homo sapiens 204-232 15169852-2 2004 In this study, we used a phospholipase C gamma 1 (PLCgamma1) binding, cell-penetrating peptide to sequester PLCgamma1 away from its target, the phosphotyrosine residues within the activated growth factor receptor. Phosphotyrosine 144-159 phospholipase C gamma 1 Homo sapiens 25-48 17250586-5 2007 Immunoblotting with phosphotyrosine-specific antibodies identified Zeta-associated protein of 70,000 molecular weight (ZAP-70), linker for the activation of T cells (LAT), and phospholipase-C-gamma1 (PLCgamma1) to be among the proteins that become phosphorylated upon CXCR3 activation. Phosphotyrosine 20-35 phospholipase C gamma 1 Homo sapiens 176-198 17250586-5 2007 Immunoblotting with phosphotyrosine-specific antibodies identified Zeta-associated protein of 70,000 molecular weight (ZAP-70), linker for the activation of T cells (LAT), and phospholipase-C-gamma1 (PLCgamma1) to be among the proteins that become phosphorylated upon CXCR3 activation. Phosphotyrosine 20-35 phospholipase C gamma 1 Homo sapiens 200-209 15641795-1 2005 The signal transduction protein phospholipase C-gamma1 (PLC-gamma1) is activated when its C-terminal SH2 domain (PLCC) binds the phosphorylated Tyr-1021 site (pTyr-1021) in the beta-platelet-derived growth factor receptor (PDGFR). Phosphotyrosine 159-163 phospholipase C gamma 1 Homo sapiens 56-66 15169852-2 2004 In this study, we used a phospholipase C gamma 1 (PLCgamma1) binding, cell-penetrating peptide to sequester PLCgamma1 away from its target, the phosphotyrosine residues within the activated growth factor receptor. Phosphotyrosine 144-159 phospholipase C gamma 1 Homo sapiens 50-59 15169852-2 2004 In this study, we used a phospholipase C gamma 1 (PLCgamma1) binding, cell-penetrating peptide to sequester PLCgamma1 away from its target, the phosphotyrosine residues within the activated growth factor receptor. Phosphotyrosine 144-159 phospholipase C gamma 1 Homo sapiens 108-117 7773170-2 1995 Specific phosphotyrosine (pTyr)-modified EGFR fragment peptides can inhibit this intermolecular binding between activated EGFR and a tandem amino- and carboxy-terminal (N/C) SH2 protein construct derived from PLC gamma-1. Phosphotyrosine 9-24 phospholipase C gamma 1 Homo sapiens 209-220 10652211-7 2000 Although direct tyrosine phosphorylation of PLCgamma1 was not detectable, the amount of PLCgamma1 coprecipitable with anti-phosphotyrosine was increased after IL-4 stimulation. Phosphotyrosine 123-138 phospholipase C gamma 1 Homo sapiens 88-97 9716455-2 1998 To study the roles of Tyr-783 phosphorylation in vivo, we developed a polyclonal antibody that recognizes PLCgamma1 containing phosphotyrosine 783 (alpha-PLCgamma1 PY). Phosphotyrosine 127-142 phospholipase C gamma 1 Homo sapiens 106-115 7773170-2 1995 Specific phosphotyrosine (pTyr)-modified EGFR fragment peptides can inhibit this intermolecular binding between activated EGFR and a tandem amino- and carboxy-terminal (N/C) SH2 protein construct derived from PLC gamma-1. Phosphotyrosine 26-30 phospholipase C gamma 1 Homo sapiens 209-220 7989748-4 1994 Anti-phosphotyrosine immunoprecipitates from lysates of PAF-stimulated cells, when fractionated by SDS-PAGE and analyzed by Western blotting with anti-PLC-gamma 1, showed that maximal tyrosine phosphorylation of this enzyme occurred within 2 min of stimulation. Phosphotyrosine 5-20 phospholipase C gamma 1 Homo sapiens 151-162 1643644-4 1992 Immunoblot analysis reveals low levels of phosphotyrosine in PLC-gamma 1 and EGF receptors in unstimulated MDA-468 cells and greatly increased phosphotyrosine levels in these proteins as a result of EGF stimulation of the cells. Phosphotyrosine 42-57 phospholipase C gamma 1 Homo sapiens 61-72 8321198-11 1993 Although phosphotyrosine 766 is sufficient for interaction of PLC gamma 1 and other SH2 substrates with the FGF-R kinase, phosphorylation and presumably activation of substrates require the kinase homodimer and phosphorylation of Tyr-653. Phosphotyrosine 9-24 phospholipase C gamma 1 Homo sapiens 62-73 8391259-6 1993 Furthermore, tyrphostin treatment clearly decreased the PLC gamma 1 and p85 contents in such an anti-phosphotyrosine immunoprecipitate. Phosphotyrosine 101-116 phospholipase C gamma 1 Homo sapiens 56-67 1550550-6 1992 Immunoprecipitation with antibodies against PLC-gamma 1 or PLC-gamma 2 and subsequent Western blotting with anti-phosphotyrosine antibodies revealed that both PLC-gamma 1 and PLC-gamma 2 are tyrosine phosphorylated in stimulated but not in resting B cells. Phosphotyrosine 113-128 phospholipase C gamma 1 Homo sapiens 159-170 1370476-11 1992 Furthermore, in the absence of PMA, activation of PKC by diacylglycerol provides a negative feedback signal responsible for reducing the phosphotyrosine contents of PLC-gamma 1. Phosphotyrosine 137-152 phospholipase C gamma 1 Homo sapiens 165-176 1683701-5 1991 In 18 of 21 carcinomas that contained high levels of PLC-gamma 1, the presence of phosphotyrosine on PLC-gamma 1 could also be detected. Phosphotyrosine 82-97 phospholipase C gamma 1 Homo sapiens 53-64 1395933-3 1992 Growth factors elicit increases in both the phosphoserine and the phosphotyrosine content of the PLC-gamma 1 isozyme. Phosphotyrosine 66-81 phospholipase C gamma 1 Homo sapiens 97-108 1683701-5 1991 In 18 of 21 carcinomas that contained high levels of PLC-gamma 1, the presence of phosphotyrosine on PLC-gamma 1 could also be detected. Phosphotyrosine 82-97 phospholipase C gamma 1 Homo sapiens 101-112 2472218-1 1989 Binding of EGF to cells expressing human EGF receptor stimulated rapid tyrosine phosphorylation of phospholipase C-II (PLC-II), as revealed by immunoblotting analysis with phosphotyrosine-specific antibodies. Phosphotyrosine 172-187 phospholipase C gamma 1 Homo sapiens 99-117 1712101-5 1991 Nearly all of the PLC activity recovered in eluates from anti-phosphotyrosine immunoprecipitates was depleted by anti-PLC-gamma 1 antibodies. Phosphotyrosine 62-77 phospholipase C gamma 1 Homo sapiens 118-129 2472218-1 1989 Binding of EGF to cells expressing human EGF receptor stimulated rapid tyrosine phosphorylation of phospholipase C-II (PLC-II), as revealed by immunoblotting analysis with phosphotyrosine-specific antibodies. Phosphotyrosine 172-187 phospholipase C gamma 1 Homo sapiens 119-125