PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
10786691-9	2000	RXRalpha was found to contain two proline, glutamate/aspartate, serine, and threonine (PEST) motifs, which confer rapid turnover of many short-lived regulatory proteins that are degraded by the ubiquitin/proteasome pathway.	Aspartic Acid	53-62	retinoid X receptor alpha	Homo sapiens	0-8	
25294873-4	2014	After confirming its type III activity generating only omega-N(G)-monomethylarginine and its distinct substrate specificity for RXR motifs surrounded by basic residues, we performed site-directed mutagenesis studies on this enzyme, revealing that two acidic residues within the double E loop, Asp-147 and Glu-149, modulate the substrate preference.	Aspartic Acid	293-296	retinoid X receptor alpha	Homo sapiens	128-131