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