PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 18355321-8 2008 We have identified a previously unknown mechanism in which phosphotyrosine-binding domain-containing adaptors, by means of relocating Ret receptor complexes to lipid rafts, segregate diverse signaling and cellular functions mediated by Ret. Phosphotyrosine 59-74 ret proto-oncogene Homo sapiens 134-137 18355321-8 2008 We have identified a previously unknown mechanism in which phosphotyrosine-binding domain-containing adaptors, by means of relocating Ret receptor complexes to lipid rafts, segregate diverse signaling and cellular functions mediated by Ret. Phosphotyrosine 59-74 ret proto-oncogene Homo sapiens 236-239 14607833-0 2004 Structural basis for the specific recognition of RET by the Dok1 phosphotyrosine binding domain. Phosphotyrosine 65-80 ret proto-oncogene Homo sapiens 49-52 16847065-0 2006 Engineering the recruitment of phosphotyrosine binding domain-containing adaptor proteins reveals distinct roles for RET receptor-mediated cell survival. Phosphotyrosine 31-46 ret proto-oncogene Homo sapiens 117-120 16847065-2 2006 The recruitment at the phosphorylated Tyr(1062) site in RET of a number of different phosphotyrosine binding (PTB) domain-containing adaptor proteins, including Shc and Frs2, plays a dominant role for the multiple different biological functions of the RET receptor during development, including stimulation of cell survival. Phosphotyrosine 85-100 ret proto-oncogene Homo sapiens 56-59 16847065-2 2006 The recruitment at the phosphorylated Tyr(1062) site in RET of a number of different phosphotyrosine binding (PTB) domain-containing adaptor proteins, including Shc and Frs2, plays a dominant role for the multiple different biological functions of the RET receptor during development, including stimulation of cell survival. Phosphotyrosine 85-100 ret proto-oncogene Homo sapiens 252-255 14711813-2 2004 Some studies have revealed a few possible autophosphorylation sites of RET by [(32)P]phosphopeptide mapping or by using specific anti-phosphotyrosine antibodies. Phosphotyrosine 134-149 ret proto-oncogene Homo sapiens 71-74 10728700-6 2000 They showed RET transcript, protein amounts as well as Ret-associated phosphotyrosine levels similar to those measured in MEN-2A-associated pheochromocytomas. Phosphotyrosine 70-85 ret proto-oncogene Homo sapiens 55-58 11390647-4 2001 Complex formation between RET and FRS2 is mediated by binding of the phosphotyrosine-binding domain of FRS2 to pY1062, a residue in RET that also functions as a binding site for Shc. Phosphotyrosine 69-84 ret proto-oncogene Homo sapiens 26-29 11390647-4 2001 Complex formation between RET and FRS2 is mediated by binding of the phosphotyrosine-binding domain of FRS2 to pY1062, a residue in RET that also functions as a binding site for Shc. Phosphotyrosine 69-84 ret proto-oncogene Homo sapiens 132-135 10465268-0 1999 The role of amino acids surrounding tyrosine 1062 in ret in specific binding of the shc phosphotyrosine-binding domain. Phosphotyrosine 88-103 ret proto-oncogene Homo sapiens 53-56 10465268-1 1999 We investigated the role of the I-E-N-K-L (amino acids 1057-1061) sequence amino-terminal to Tyr1062 in Ret for binding of the Shc phosphotyrosine-binding (PTB) domain. Phosphotyrosine 131-146 ret proto-oncogene Homo sapiens 104-107 10070972-8 1999 Furthermore, we show that Ret is able to associate with the SH2 domain of Src in a phosphotyrosine-dependent fashion. Phosphotyrosine 83-98 ret proto-oncogene Homo sapiens 26-29 9764818-7 1998 This possibility is supported by the evidence that the mutant Ret/ptc2Y620F long isoform displays a weak coimmunoprecipitation with Grb2 and that this mutant, lacking the docking site for Grb2 but owing all the others phosphotyrosines, surprisingly displays a reduced transforming activity compared to that of the two WTs oncogenes. Phosphotyrosine 218-234 ret proto-oncogene Homo sapiens 62-65 9047384-6 1997 In fact, here we show that both the phosphotyrosine binding domains of Shc, PTB and SH2, interact with Ret/ptc2 in vitro. Phosphotyrosine 36-51 ret proto-oncogene Homo sapiens 103-106 9325171-4 1997 In addition, in neuronal cells, but not in astrocytes, Tat increased the phosphotyrosine content of Shc, a protein involved in signal transduction downstream of receptor tyrosine kinase activation. Phosphotyrosine 73-88 ret proto-oncogene Homo sapiens 161-185 32816064-5 2020 Intracellular tyrosine phosphorylation in RET and recruitment of adaptor proteins to phosphotyrosines are essential for various biological functions. Phosphotyrosine 85-101 ret proto-oncogene Homo sapiens 42-45 31100409-4 2019 Activated RTK recruits Shc, via its phosphotyrosine binding (PTB) domain (ShcPTB), precipitating the release of Erk to engage in a signalling response. Phosphotyrosine 36-51 ret proto-oncogene Homo sapiens 10-13 29514104-2 2018 We applied comprehensive phosphoproteomics to unravel differential regulators of receptor tyrosine kinase (RTK)-initiated signaling networks upon activation by Pdgf-betabeta, Fgf-2, or Igf-1 and identified more than 40,000 phosphorylation sites, including many phosphotyrosine sites without additional enrichment. Phosphotyrosine 261-276 ret proto-oncogene Homo sapiens 81-105 29514104-2 2018 We applied comprehensive phosphoproteomics to unravel differential regulators of receptor tyrosine kinase (RTK)-initiated signaling networks upon activation by Pdgf-betabeta, Fgf-2, or Igf-1 and identified more than 40,000 phosphorylation sites, including many phosphotyrosine sites without additional enrichment. Phosphotyrosine 261-276 ret proto-oncogene Homo sapiens 107-110 28092043-2 2017 Their ability to distinguish binding to over thousands of potential phosphotyrosine (pTyr) ligands within the cell is critical for the fidelity of receptor tyrosine kinase (RTK) signaling. Phosphotyrosine 68-83 ret proto-oncogene Homo sapiens 147-171 28092043-2 2017 Their ability to distinguish binding to over thousands of potential phosphotyrosine (pTyr) ligands within the cell is critical for the fidelity of receptor tyrosine kinase (RTK) signaling. Phosphotyrosine 68-83 ret proto-oncogene Homo sapiens 173-176 28092043-2 2017 Their ability to distinguish binding to over thousands of potential phosphotyrosine (pTyr) ligands within the cell is critical for the fidelity of receptor tyrosine kinase (RTK) signaling. Phosphotyrosine 85-89 ret proto-oncogene Homo sapiens 147-171 28092043-2 2017 Their ability to distinguish binding to over thousands of potential phosphotyrosine (pTyr) ligands within the cell is critical for the fidelity of receptor tyrosine kinase (RTK) signaling. Phosphotyrosine 85-89 ret proto-oncogene Homo sapiens 173-176 22355350-0 2012 RET PLCgamma phosphotyrosine binding domain regulates Ca2+ signaling and neocortical neuronal migration. Phosphotyrosine 13-28 ret proto-oncogene Homo sapiens 0-3 19900702-10 2009 We also showed the downregulation of phosphorylation on RET phosphotyrosine residue 905 in BeWo cells with phosphorylation specific antibodies and immunocytochemistry. Phosphotyrosine 60-75 ret proto-oncogene Homo sapiens 56-59 20210798-9 2010 The binding affinity of the DOK-6 phosphotyrosine-binding (PTB) domain to RET was much lower than that of the DOK-1, DOK-4, and SHC PTB domains to RET. Phosphotyrosine 34-49 ret proto-oncogene Homo sapiens 74-77 19223551-4 2009 In addition, RET/PTC physically interacts with beta-catenin and increases its phosphotyrosine content. Phosphotyrosine 78-93 ret proto-oncogene Homo sapiens 13-16