PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
15305021-2	2004	Recently we cloned pyroglutamyl aminopeptidase I (PAP-I) which is known for specifically removing a L-pyroglutamate (L-pGlu) residue from the amino terminus of proteins and peptides including TRH.	Pyrrolidonecarboxylic Acid	100-115	pyroglutamyl-peptidase I	Rattus norvegicus	19-48	
15305021-2	2004	Recently we cloned pyroglutamyl aminopeptidase I (PAP-I) which is known for specifically removing a L-pyroglutamate (L-pGlu) residue from the amino terminus of proteins and peptides including TRH.	Pyrrolidonecarboxylic Acid	100-115	pyroglutamyl-peptidase I	Rattus norvegicus	50-55	
14600395-1	2003	Pyroglutamyl aminopeptidase I (PAP-I) is a cytosolic cysteine peptidase, which hydrolytically removes the L-pyroglutamate residue from the amino terminus of endogenous proteins and peptides.	Pyrrolidonecarboxylic Acid	106-121	pyroglutamyl-peptidase I	Rattus norvegicus	0-29	
14709911-1	2004	Pyroglutamyl aminopeptidase I (PAP-I) is known for specifically removing the L-pyroglutamate (L-pGlu) residue from the amino terminus of L-pGlu proteins and peptides.	Pyrrolidonecarboxylic Acid	77-92	pyroglutamyl-peptidase I	Rattus norvegicus	0-29	
14709911-1	2004	Pyroglutamyl aminopeptidase I (PAP-I) is known for specifically removing the L-pyroglutamate (L-pGlu) residue from the amino terminus of L-pGlu proteins and peptides.	Pyrrolidonecarboxylic Acid	77-92	pyroglutamyl-peptidase I	Rattus norvegicus	31-36	
14709911-2	2004	In general, substrate recognition of PAP-I as to L-pGlu moiety is tightly regulated.	Pyrrolidonecarboxylic Acid	51-55	pyroglutamyl-peptidase I	Rattus norvegicus	37-42	
14600395-1	2003	Pyroglutamyl aminopeptidase I (PAP-I) is a cytosolic cysteine peptidase, which hydrolytically removes the L-pyroglutamate residue from the amino terminus of endogenous proteins and peptides.	Pyrrolidonecarboxylic Acid	106-121	pyroglutamyl-peptidase I	Rattus norvegicus	31-36	
7494810-8	1995	Conversion studies showed that pGlu-L-Dopa-Pro was degraded by pyroglutamyl aminopeptidase I, an enzyme releasing the N-terminal pyroglutamic acid, with Vmax and Km of 0.6 mumole/min/g protein and 21 mM, respectively, and that L-Dopa-Pro was degraded by prolidase with Vmax and Km of 44 mumole/min/g protein and 0.48 mM, respectively.	Pyrrolidonecarboxylic Acid	129-146	pyroglutamyl-peptidase I	Rattus norvegicus	63-92	
12450739-3	2002	PAP I cleaves the pGlu-amino acid bond of neuropeptides such as thyroliberin, luliberin, neurotensin, and bombesin.	Pyrrolidonecarboxylic Acid	18-22	pyroglutamyl-peptidase I	Rattus norvegicus	0-5