PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
12101225-3	2002	Interestingly, the pSer/Thr-Pro motifs in proteins exist in two completely distinct cis and trans conformations, whose conversion is catalyzed specifically by the essential prolyl isomerase Pin1.	Phosphoserine	19-23	peptidyl-prolyl cis/trans isomerase, NIMA-interacting 1	Mus musculus	190-194	
33717117-1	2021	Pin1 is the only known peptidyl-prolyl cis-trans isomerase (PPIase) that can specifically recognize and isomerize the phosphorylated Serine/Threonine-Proline (pSer/Thr-Pro) motif, change the conformation of proteins through protein phosphorylation, thus regulate various cellular processes in the body.	Phosphoserine	159-163	peptidyl-prolyl cis/trans isomerase, NIMA-interacting 1	Mus musculus	0-4	
25187260-1	2015	Pin1 is a peptidyl prolyl cis-trans isomerase that specifically binds to the phosphoserine-proline or phosphothreonine-proline motifs of numerous proteins.	Phosphoserine	77-90	peptidyl-prolyl cis/trans isomerase, NIMA-interacting 1	Mus musculus	0-4	
27475846-1	2016	Pin1 is a peptidylprolyl cis/trans isomerase and it has a unique enzymatic activity of catalyzing isomerization of the peptide bond between phospho-serine/threonine and proline.	Phosphoserine	140-154	peptidyl-prolyl cis/trans isomerase, NIMA-interacting 1	Mus musculus	0-4	
26991250-4	2016	Pin1, a peptidyl-prolyl cis/trans isomerase (PPIase) that recognizes and binds to phosphorylated serine/threonine residues preceded by a proline (pSer/Thr-Pro) is also expressed in the developing brain.	Phosphoserine	146-150	peptidyl-prolyl cis/trans isomerase, NIMA-interacting 1	Mus musculus	0-4	
27073025-3	2016	Pin1 recognizes phosphoserine/phosphothreonine-proline motifs in target proteins and catalyzes prolyl isomerization at the peptide bond.	Phosphoserine	16-29	peptidyl-prolyl cis/trans isomerase, NIMA-interacting 1	Mus musculus	0-4