PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
24070605-1	2013	The phosphoinositide 5-kinase PIKfyve and 5-phosphatase Sac3 are scaffolded by ArPIKfyve in the PIKfyve-ArPIKfyve-Sac3 (PAS) regulatory complex to trigger a unique loop of PtdIns3P-PtdIns(3,5)P2 synthesis and turnover.	Aminosalicylic Acid	120-123	VAC14 component of PIKFYVE complex	Homo sapiens	79-88	
24070605-1	2013	The phosphoinositide 5-kinase PIKfyve and 5-phosphatase Sac3 are scaffolded by ArPIKfyve in the PIKfyve-ArPIKfyve-Sac3 (PAS) regulatory complex to trigger a unique loop of PtdIns3P-PtdIns(3,5)P2 synthesis and turnover.	Aminosalicylic Acid	120-123	VAC14 component of PIKFYVE complex	Homo sapiens	104-113	
18950639-3	2008	However, whether the three proteins suffice for the organization/maintenance of this complex [referred to as the PAS (PIKfyve-ArPIKfyve-Sac3) complex], how they interact with one another, and what the functional relevance of this ternary association would be remained unresolved.	Aminosalicylic Acid	113-116	VAC14 component of PIKFYVE complex	Homo sapiens	126-135	
19840946-2	2009	We previously established that PIKfyve is activated within the triple PIKfyve-ArPIKfyve-Sac3 (PAS) core.	Aminosalicylic Acid	94-97	VAC14 component of PIKFYVE complex	Homo sapiens	78-87	
18950639-5	2008	ArPIKfyve is the principal organizer interacting with both Sac3 and PIKfyve, whereas Sac3 is permissive for maximal PIKfyve-ArPIKfyve association in the PAS complex.	Aminosalicylic Acid	153-156	VAC14 component of PIKFYVE complex	Homo sapiens	0-9	
18950639-5	2008	ArPIKfyve is the principal organizer interacting with both Sac3 and PIKfyve, whereas Sac3 is permissive for maximal PIKfyve-ArPIKfyve association in the PAS complex.	Aminosalicylic Acid	153-156	VAC14 component of PIKFYVE complex	Homo sapiens	124-133	
18950639-6	2008	We further identified that ArPIKfyve scaffolds the PAS complex through homomeric interactions, mediated via its conserved C-terminal domain.	Aminosalicylic Acid	51-54	VAC14 component of PIKFYVE complex	Homo sapiens	27-36	
18950639-7	2008	Introduction of the C-terminal peptide fragment of the ArPIKfyve-ArPIKfyve contact sites effectively disassembled the PAS complex and reduced the in vitro PIKfyve lipid kinase activity.	Aminosalicylic Acid	118-121	VAC14 component of PIKFYVE complex	Homo sapiens	55-64	
18950639-7	2008	Introduction of the C-terminal peptide fragment of the ArPIKfyve-ArPIKfyve contact sites effectively disassembled the PAS complex and reduced the in vitro PIKfyve lipid kinase activity.	Aminosalicylic Acid	118-121	VAC14 component of PIKFYVE complex	Homo sapiens	65-74	
18950639-9	2008	Our data indicate that the PAS complex is organized to provide optimal PIKfyve functionality and is maintained via ArPIKfyve homomeric and heteromeric interactions.	Aminosalicylic Acid	27-30	VAC14 component of PIKFYVE complex	Homo sapiens	115-124