PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 34499159-6 2021 The binding of the TOS motif to Mip1 is dependent on Mip1 Tyr-533, whose equivalent in RAPTOR is known to interact with the TOS motif in their co-crystals. tos 19-22 regulatory associated protein of MTOR complex 1 Homo sapiens 87-93 34499159-6 2021 The binding of the TOS motif to Mip1 is dependent on Mip1 Tyr-533, whose equivalent in RAPTOR is known to interact with the TOS motif in their co-crystals. tos 124-127 regulatory associated protein of MTOR complex 1 Homo sapiens 87-93 14684181-3 2004 Raptor appears to serve as an mTOR scaffold protein, the binding of which to the TOS motif of mTOR substrates is necessary for effective mTOR-catalyzed phosphorylation. tos 81-84 regulatory associated protein of MTOR complex 1 Homo sapiens 0-6 29236692-7 2017 We also present crystal structures of RAPTOR-TOS motif complexes that define the determinants of TOS recognition, of an mTOR FKBP12-rapamycin-binding (FRB) domain-substrate complex that establishes a second substrate-recruitment mechanism, and of a truncated mTOR-PRAS40 complex that reveals PRAS40 inhibits both substrate-recruitment sites. tos 45-48 regulatory associated protein of MTOR complex 1 Homo sapiens 38-44 12747827-4 2003 RESULTS: Here, we show that a functional TOS motif is required for 4E-BP1 to bind to raptor (a recently identified mTOR-interacting protein), for 4E-BP1 to be efficiently phosphorylated in vitro by the mTOR/raptor complex, and for 4E-BP1 to be phosphorylated in vivo at all identified mTOR-regulated sites. tos 41-44 regulatory associated protein of MTOR complex 1 Homo sapiens 85-91 12747827-4 2003 RESULTS: Here, we show that a functional TOS motif is required for 4E-BP1 to bind to raptor (a recently identified mTOR-interacting protein), for 4E-BP1 to be efficiently phosphorylated in vitro by the mTOR/raptor complex, and for 4E-BP1 to be phosphorylated in vivo at all identified mTOR-regulated sites. tos 41-44 regulatory associated protein of MTOR complex 1 Homo sapiens 207-213 12747827-7 2003 CONCLUSIONS: Our data demonstrate that the TOS motif functions as a docking site for the mTOR/raptor complex, which is required for multisite phosphorylation of 4E-BP1, eIF4E release from 4E-BP1, and cell growth. tos 43-46 regulatory associated protein of MTOR complex 1 Homo sapiens 94-100 12604610-4 2003 A point mutation of the TOS motif also eliminates all in vitro mTOR-catalyzed 4E-BP1 phosphorylation and abolishes the raptor-dependent component of mTOR-catalyzed p70S6k phosphorylation in vitro. tos 24-27 regulatory associated protein of MTOR complex 1 Homo sapiens 119-125 12604610-5 2003 Raptor appears to serve as an mTOR scaffold protein, the binding of which to the TOS motif of mTOR substrates is necessary for effective mTOR-catalyzed phosphorylation in vivo and perhaps for conferring their sensitivity to rapamycin and amino acid sufficiency. tos 81-84 regulatory associated protein of MTOR complex 1 Homo sapiens 0-6