PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
20179103-5	2010	However, only active Mek2 could bind Pin1, acting as a scaffold to bridge Pin1 and BPGAP1 in a manner that involves the release of an autoinhibited proline-rich motif, 186-PPLP-189, proximal to the RhoGAP domain.	Proline	148-155	peptidylprolyl cis/trans isomerase, NIMA-interacting 1	Homo sapiens	37-41	
20179103-6	2010	This allows the non-canonical 186-PPLP-189 and 256-DDYGD-260 motifs of the proline-rich region and RhoGAP domain of BPGAP1 to become accessible to concerted binding by the WW and PPI domains of Pin1, respectively.	Proline	75-82	peptidylprolyl cis/trans isomerase, NIMA-interacting 1	Homo sapiens	194-198