PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 10860857-1 2000 In rat liver derived HTC cells transfected with and expressing human insulin receptors, there are multiple p60-70 proteins that are tyrosine phosphorylated following insulin treatment of cells. Tyrosine 132-140 sequestosome 1 Homo sapiens 107-110 14562045-4 2003 In 11 out of 14 GM-CSF-independent mutants analysed, a constitutively tyrosine-phosphorylated protein of 60 kDa was detected, which was subsequently identified as p60(c-Src). Tyrosine 70-78 sequestosome 1 Homo sapiens 163-166 12408982-4 2002 Tyrosine phosphorylation of either EC MLCK (Y(464), Y(471)) or cortactin (Y(421), Y(466), and Y(482)) by p60(src) significantly increased this direct association. Tyrosine 0-8 sequestosome 1 Homo sapiens 105-108 11113114-6 2001 The sites of tyrosine phosphorylation catalyzed by p60(Src) are Tyr(464) and Tyr(471) within the 69-residue stretch deleted in the MLCK-2 splice variant. Tyrosine 13-21 sequestosome 1 Homo sapiens 51-54 11113114-6 2001 The sites of tyrosine phosphorylation catalyzed by p60(Src) are Tyr(464) and Tyr(471) within the 69-residue stretch deleted in the MLCK-2 splice variant. Tyrosine 64-67 sequestosome 1 Homo sapiens 51-54 11113114-6 2001 The sites of tyrosine phosphorylation catalyzed by p60(Src) are Tyr(464) and Tyr(471) within the 69-residue stretch deleted in the MLCK-2 splice variant. Tyrosine 77-80 sequestosome 1 Homo sapiens 51-54 11113114-7 2001 These results demonstrate for the first time that p60(Src)-mediated tyrosine phosphorylation represents an important mechanism for splice variant-specific regulation of nonmuscle MLCK and vascular cell function. Tyrosine 68-76 sequestosome 1 Homo sapiens 50-53 10860857-2 2000 Employing antibodies to insulin receptor substrate 3 (alpha-IRS-3), we found that IRS-3 is a major p60 phosphoprotein that is tyrosine phosphorylated following insulin treatment of cells and interacts with phosphatidylinositol-3-kinase (PI3K). Tyrosine 126-134 sequestosome 1 Homo sapiens 99-102 10860857-6 2000 In summary, IRS-3 is the major p60 protein that is tyrosine phosphorylated and interacts with PI3K in HTC rat liver derived cells following insulin treatment of cells. Tyrosine 51-59 sequestosome 1 Homo sapiens 31-34 10362724-8 1999 These studies indicate that DPV activates the endothelial contractile apparatus in a Rho GTPase-dependent fashion and suggests that p60(src)-induced tyrosine phosphorylation of MLCK and cortactin may be important features of contractile complex assembly. Tyrosine 149-157 sequestosome 1 Homo sapiens 132-135 10777553-8 2000 CCh also induced tyrosine phosphorylation of p60(src) and association of p60(src) with both PYK-2 and the EGFR. Tyrosine 17-25 sequestosome 1 Homo sapiens 45-48 10444401-10 1999 Protein kinase C downregulation by phorbol 12-myristate 13-acetate and/or inhibitors to protein kinase C, p60(src) kinase, and MAPK kinase inhibited BK-induced MAPK tyrosine phosphorylation. Tyrosine 165-173 sequestosome 1 Homo sapiens 106-109 10412792-9 1999 The nonreceptor tyrosine kinase, c-Src p60, was also strongly tyrosine phosphorylated in the macrophages, and this was not enhanced by the stimulation of HD-LDL. Tyrosine 16-24 sequestosome 1 Homo sapiens 39-42 9237663-0 1997 Inhibition of protein tyrosine phosphatases causes phosphorylation of tyrosine-331 in the p60 TNF receptor and inactivates the receptor-associated kinase. Tyrosine 22-30 sequestosome 1 Homo sapiens 90-93 9736341-3 1998 Using anti-Csk antibodies and recombinant fusion proteins we detected a single tyrosine-phosphorylated protein of 60 kD (herein referred to as "p60") that associates with the SH2 domain of Csk after stimulation of the FcepsilonRI. Tyrosine 79-87 sequestosome 1 Homo sapiens 144-147 9237663-3 1997 In this report, we show that this inhibition, when induced by pervanadate, caused the tyrosine phosphorylation of the cytoplasmic domain (CD) of the p60 receptor, as revealed by phosphoamino acid analysis. Tyrosine 86-94 sequestosome 1 Homo sapiens 149-152 7545165-4 1995 In addition, the activation of protein kinase C alpha inhibited the in situ ligand-stimulated increase in tyrosine phosphorylation of the GTPase-activating protein-associated p60 protein as well as Shc mediated by these receptors. Tyrosine 106-114 sequestosome 1 Homo sapiens 175-178 8940353-0 1996 Role of the juxtamembrane tyrosine in insulin receptor-mediated tyrosine phosphorylation of p60 endogenous substrates. Tyrosine 26-34 sequestosome 1 Homo sapiens 92-95 8940353-0 1996 Role of the juxtamembrane tyrosine in insulin receptor-mediated tyrosine phosphorylation of p60 endogenous substrates. Tyrosine 64-72 sequestosome 1 Homo sapiens 92-95 8621646-4 1996 In both Jurkat and normal T cells, the Src homology 2 (SH2) domain of Csk bound constitutively to a tyrosine-phosphorylated protein of 60 kDa (p60). Tyrosine 100-108 sequestosome 1 Homo sapiens 143-146 7545165-6 1995 Although the in situ phosphorylation of insulin-receptor substrate-1 and p60 by this receptor was inhibited by prior stimulation of protein kinase C alpha, the in vitro tyrosine phosphorylation of these two substrates by this receptor was not decreased by prior stimulation of the protein kinase C alpha in the cells that served as a source of the substrates. Tyrosine 169-177 sequestosome 1 Homo sapiens 73-76 6311433-2 1983 Cells infected with mutants whose p60srcs lack the major site of either serine or tyrosine phosphorylation were morphologically transformed and formed colonies in soft agar. Tyrosine 82-90 sequestosome 1 Homo sapiens 34-37 3480286-5 1987 p60 and p93 are phosphorylated exclusively on tyrosine residues and can use poly(Glu,Tyr)4:1, histone H1 and vasoactive intestinal peptide as substrates. Tyrosine 46-54 sequestosome 1 Homo sapiens 0-3 7539611-11 1995 Binding of p60 to p85 is similar to the interaction between p85 and IRS-1 in that a tyrosine-phosphorylated peptide containing the YVXM motif can inhibit the association. Tyrosine 84-92 sequestosome 1 Homo sapiens 11-14 2582236-5 1985 Phosphorylation at tyrosine 416 of p60 itself was also extremely low in overproduced p60c-src and high in p60s of transforming mutant viruses. Tyrosine 19-27 sequestosome 1 Homo sapiens 35-38 2582236-5 1985 Phosphorylation at tyrosine 416 of p60 itself was also extremely low in overproduced p60c-src and high in p60s of transforming mutant viruses. Tyrosine 19-27 sequestosome 1 Homo sapiens 85-88 31931029-4 2020 Here we found that EGFR-stimulated phosphorylation of SQSTM1 at tyrosine 433 induces dimerization of its UBA domain, which disturbs the sequestration function of SQSTM1 and causes autophagic flux blocking. Tyrosine 64-72 sequestosome 1 Homo sapiens 54-60 31931029-4 2020 Here we found that EGFR-stimulated phosphorylation of SQSTM1 at tyrosine 433 induces dimerization of its UBA domain, which disturbs the sequestration function of SQSTM1 and causes autophagic flux blocking. Tyrosine 64-72 sequestosome 1 Homo sapiens 162-168