PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
10563791-2	1999	Peptidylglycine monooxygenase (PHM) carries out the hydroxylation of the alpha-C atom of glycine-extended propeptides, the first step in the amidation of peptide hormones by the bifunctional enzyme peptidyl-alpha-amidating monooxygenase (PAM).	propeptides	106-117	peptidylglycine alpha-amidating monooxygenase	Homo sapiens	31-34	
10563791-2	1999	Peptidylglycine monooxygenase (PHM) carries out the hydroxylation of the alpha-C atom of glycine-extended propeptides, the first step in the amidation of peptide hormones by the bifunctional enzyme peptidyl-alpha-amidating monooxygenase (PAM).	propeptides	106-117	peptidylglycine alpha-amidating monooxygenase	Homo sapiens	198-236	
10563791-2	1999	Peptidylglycine monooxygenase (PHM) carries out the hydroxylation of the alpha-C atom of glycine-extended propeptides, the first step in the amidation of peptide hormones by the bifunctional enzyme peptidyl-alpha-amidating monooxygenase (PAM).	propeptides	106-117	peptidylglycine alpha-amidating monooxygenase	Homo sapiens	238-241	
7760848-1	1995	A highly conserved ten amino acid proregion separates the peptidylglycine alpha-hydroxylating monooxygenase (PHM) domain of the bifunctional peptidylglycine alpha-amidating monooxygenase (PAM) protein from the NH2-terminal signal peptide; propeptides with amino acid sequences similar to the PAM proregion have been identified in other secreted proteins.	propeptides	239-250	peptidylglycine alpha-amidating monooxygenase	Homo sapiens	58-107	
7760848-1	1995	A highly conserved ten amino acid proregion separates the peptidylglycine alpha-hydroxylating monooxygenase (PHM) domain of the bifunctional peptidylglycine alpha-amidating monooxygenase (PAM) protein from the NH2-terminal signal peptide; propeptides with amino acid sequences similar to the PAM proregion have been identified in other secreted proteins.	propeptides	239-250	peptidylglycine alpha-amidating monooxygenase	Homo sapiens	141-186	
7760848-1	1995	A highly conserved ten amino acid proregion separates the peptidylglycine alpha-hydroxylating monooxygenase (PHM) domain of the bifunctional peptidylglycine alpha-amidating monooxygenase (PAM) protein from the NH2-terminal signal peptide; propeptides with amino acid sequences similar to the PAM proregion have been identified in other secreted proteins.	propeptides	239-250	peptidylglycine alpha-amidating monooxygenase	Homo sapiens	188-191	
7760848-1	1995	A highly conserved ten amino acid proregion separates the peptidylglycine alpha-hydroxylating monooxygenase (PHM) domain of the bifunctional peptidylglycine alpha-amidating monooxygenase (PAM) protein from the NH2-terminal signal peptide; propeptides with amino acid sequences similar to the PAM proregion have been identified in other secreted proteins.	propeptides	239-250	peptidylglycine alpha-amidating monooxygenase	Homo sapiens	292-295