PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
2295617-2	1990	The acidic phospholipids such as phosphatidylserine (PS), phosphatidic acid, phosphatidyl-glycerol, and cardiolipin, which are activators of PKC in the assay of protein phosphorylation, could differentially inactivate PKC I, II, and III during preincubation in the absence of divalent cation.	Phosphatidylserines	33-51	protein kinase C iota	Homo sapiens	141-144	
2295617-2	1990	The acidic phospholipids such as phosphatidylserine (PS), phosphatidic acid, phosphatidyl-glycerol, and cardiolipin, which are activators of PKC in the assay of protein phosphorylation, could differentially inactivate PKC I, II, and III during preincubation in the absence of divalent cation.	Phosphatidylserines	33-51	protein kinase C iota	Homo sapiens	218-236	
2295617-2	1990	The acidic phospholipids such as phosphatidylserine (PS), phosphatidic acid, phosphatidyl-glycerol, and cardiolipin, which are activators of PKC in the assay of protein phosphorylation, could differentially inactivate PKC I, II, and III during preincubation in the absence of divalent cation.	Phosphatidylserines	53-55	protein kinase C iota	Homo sapiens	141-144	
2295617-12	1990	In the presence of divalent cations, PS interacted preferentially with the regulatory domain of PKC and resulted in the activation of the kinase.	Phosphatidylserines	37-39	protein kinase C iota	Homo sapiens	96-99