PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
1650359-1	1991	The phosphorylation sites in the myristoylated alanine-rich C kinase substrate or MARCKS protein consist of four serines contained within a conserved, basic region of 25 amino acids, termed the phosphorylation site domain.	Serine	113-120	myristoylated alanine rich protein kinase C substrate	Homo sapiens	33-78	
1650359-1	1991	The phosphorylation sites in the myristoylated alanine-rich C kinase substrate or MARCKS protein consist of four serines contained within a conserved, basic region of 25 amino acids, termed the phosphorylation site domain.	Serine	113-120	myristoylated alanine rich protein kinase C substrate	Homo sapiens	82-88	
1650359-10	1991	Thus, the phosphorylation site domain peptide of the MARCKS protein is a high affinity substrate for protein kinase C in vitro; the cognate peptide containing no serines is a potent but not completely specific inhibitor of both protein kinase C and its catalytic fragment.	Serine	162-169	myristoylated alanine rich protein kinase C substrate	Homo sapiens	53-59