PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
33348649-10	2020	Suppression of RASSF1A and subsequent downregulation of DAB2IP enhances GTP loading onto RAS, thus increasing RAS mitogenic signaling in both mutant- and wildtype-RAS cells.	Guanosine Triphosphate	72-75	Ras association domain family member 1	Homo sapiens	15-22	
23294242-1	2013	The Ras association domain family (Rassf) is one of the Ras effectors, which can bind to several GTP-charged Ras-like GTPases.	Guanosine Triphosphate	97-100	Ras association domain family member 1	Homo sapiens	35-40	
26825171-3	2016	Direct interaction between the C-terminal amino acids (256-277) of RASSF1A and active GTP-RhoA was critical for this antagonism.	Guanosine Triphosphate	86-89	Ras association domain family member 1	Homo sapiens	67-74	
26825171-4	2016	In addition, interaction between the N-terminal amino acids (69-82) of RASSF1A and the ubiquitin E3 ligase Smad ubiquitination regulatory factor 1 (Smurf1) disrupted GTPase activity by facilitating Smurf1-mediated ubiquitination of GTP-RhoA.	Guanosine Triphosphate	166-169	Ras association domain family member 1	Homo sapiens	71-78	
19091744-1	2009	The Rassf1-6 polypeptides each contain a Ras/Rap association domain, which enables binding to several GTP-charged Ras-like GTPases, at least in vitro or when overexpressed.	Guanosine Triphosphate	102-105	Ras association domain family member 1	Homo sapiens	4-12	
10998413-6	2000	We now show that RASSF1 binds Ras in a GTP-dependent manner, both in vivo and directly in vitro.	Guanosine Triphosphate	39-42	Ras association domain family member 1	Homo sapiens	17-23