PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
19403696-3	2009	Here, we show that potential phospholipid translocases in the Drs2/Dnf family (type IV P-type ATPases [P4-ATPases]) are downstream targets of Kes1p repression.	Phospholipids	29-41	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	142-147	
15617515-5	2005	Recent studies have determined that Kes1p and ORP1S both bind phospholipids as ligands.	Phospholipids	62-75	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	36-41	
16136145-7	2005	The structure of Osh4 in the absence of ligand exposes potential phospholipid-binding sites that are positioned for membrane docking and sterol exchange.	Phospholipids	65-77	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	17-21	
15617515-9	2005	The results determined that the phospholipid binding domain per se was insufficient for inhibition of vesicular transport by ORP1S, and that transport of carboxypeptidase Y and invertase from the Golgi may be regulated differentially by specific regions of ORP1S/Kes1p.	Phospholipids	32-44	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	263-268