PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
14674748-11	2003	It is suggested that Ser phosphorylation allows protein-protein association by electrostatic stabilization: an obvious negative binding region of Vpu was recognizable by positive residues (Arg and Lys) of the WD domain of beta-TrCP.	Arginine	189-192	beta-transducin repeat containing E3 ubiquitin protein ligase	Homo sapiens	222-231	
28004927-8	2017	Four other arginines, Arg285, Arg410, Arg431, and Arg521, were found essential in the stabilization of p100 on the beta-TrCP surface.	Arginine	11-20	beta-transducin repeat containing E3 ubiquitin protein ligase	Homo sapiens	115-124	
28004927-9	2017	Importantly, the requirement for these five arginine residues of beta-TrCP for the interaction with p100 was further confirmed in vivo, thereby validating the docking model through a biological approach.	Arginine	44-52	beta-transducin repeat containing E3 ubiquitin protein ligase	Homo sapiens	65-74