PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
11853552-3	2002	Cross-linking experiments with purified syncollin, and granule content and membrane proteins revealed a direct interaction between syncollin and GP-2, a major glycosylphosphatidylinositol (GPI)-anchored membrane glycoprotein.	Glycosylphosphatidylinositols	159-187	glycoprotein 2	Homo sapiens	145-149	
11853552-3	2002	Cross-linking experiments with purified syncollin, and granule content and membrane proteins revealed a direct interaction between syncollin and GP-2, a major glycosylphosphatidylinositol (GPI)-anchored membrane glycoprotein.	Glycosylphosphatidylinositols	189-192	glycoprotein 2	Homo sapiens	145-149	
11853552-6	2002	Cleavage of the GPI anchor of GP-2 by treatment of granule membranes with phosphatidylinositol-specific phospholipase C had no effect on the membrane attachment of syncollin, indicating that it is not mediated exclusively via an interaction with GP-2.	Glycosylphosphatidylinositols	16-19	glycoprotein 2	Homo sapiens	30-34	
8185160-7	1994	(5) Further alkalinization of acinar lumen pH accelerates the enzymatic cleavage of the glycosyl phosphatidyl-inositol anchor associated with GP2 and thus releases the GP2/proteoglycan matrix from lumenal membranes, a process that appears to be required for vesicular retrieval of granule membranes from the apical plasma membrane and their reuse in the secretory process.	Glycosylphosphatidylinositols	88-118	glycoprotein 2	Homo sapiens	142-145	
7536674-1	1994	The GP2/THP family of glycosyl phosphatidylinositol (GPI)-anchored proteins is targeted to apical secretory compartments in polarized epithelial cells.	Glycosylphosphatidylinositols	22-51	glycoprotein 2	Homo sapiens	4-7	
7536674-1	1994	The GP2/THP family of glycosyl phosphatidylinositol (GPI)-anchored proteins is targeted to apical secretory compartments in polarized epithelial cells.	Glycosylphosphatidylinositols	53-56	glycoprotein 2	Homo sapiens	4-7	
8185160-7	1994	(5) Further alkalinization of acinar lumen pH accelerates the enzymatic cleavage of the glycosyl phosphatidyl-inositol anchor associated with GP2 and thus releases the GP2/proteoglycan matrix from lumenal membranes, a process that appears to be required for vesicular retrieval of granule membranes from the apical plasma membrane and their reuse in the secretory process.	Glycosylphosphatidylinositols	88-118	glycoprotein 2	Homo sapiens	168-171	
8471046-6	1993	These results show that the glycosylphosphatidylinositol-anchored protein GP-2 co-aggregates with zymogens in the acidic environment believed to exist in the pancreatic TGN, and thus suggest that GP-2 would function as a membrane anchor for zymogen aggregates, facilitating their entrapment in budding vesicles directed towards the regulated secretory pathway.	Glycosylphosphatidylinositols	28-56	glycoprotein 2	Homo sapiens	74-78	
8223713-1	1993	GP2, the major zymogen granule membrane (ZGM) protein in the pancreas, is linked to the lumenal leaflet of the lipid bilayer via a glycosyl-phosphatidylinositol (GPI) moiety.	Glycosylphosphatidylinositols	131-160	glycoprotein 2	Homo sapiens	0-3	
8223713-1	1993	GP2, the major zymogen granule membrane (ZGM) protein in the pancreas, is linked to the lumenal leaflet of the lipid bilayer via a glycosyl-phosphatidylinositol (GPI) moiety.	Glycosylphosphatidylinositols	162-165	glycoprotein 2	Homo sapiens	0-3	
8326020-2	1993	GP2, a protein in the exocrine pancreas, is a glycosyl phosphatidylinositol-anchored protein that is cleaved from the zymogen granule membrane and secreted into pancreatic juice.	Glycosylphosphatidylinositols	46-75	glycoprotein 2	Homo sapiens	0-3	
8471046-6	1993	These results show that the glycosylphosphatidylinositol-anchored protein GP-2 co-aggregates with zymogens in the acidic environment believed to exist in the pancreatic TGN, and thus suggest that GP-2 would function as a membrane anchor for zymogen aggregates, facilitating their entrapment in budding vesicles directed towards the regulated secretory pathway.	Glycosylphosphatidylinositols	28-56	glycoprotein 2	Homo sapiens	196-200	
2456764-4	1988	This determinant being a distinctive feature of the glycan moiety of phosphatidyl-inositol anchored membrane proteins, it established the glycosyl-phosphatidyl-inositol nature of the GP-2 membrane anchor.	Glycosylphosphatidylinositols	138-168	glycoprotein 2	Homo sapiens	183-187	
1999417-6	1991	A hydrophobic stretch of amino acids is present at the carboxyl terminus which is likely to serve as a signal for attachment of a glycosyl phosphatidylinositol (GPI) membrane anchor as has been described for GP-2.	Glycosylphosphatidylinositols	130-159	glycoprotein 2	Homo sapiens	208-212	
1999417-6	1991	A hydrophobic stretch of amino acids is present at the carboxyl terminus which is likely to serve as a signal for attachment of a glycosyl phosphatidylinositol (GPI) membrane anchor as has been described for GP-2.	Glycosylphosphatidylinositols	161-164	glycoprotein 2	Homo sapiens	208-212	
30233574-4	2018	Methods: GP2 isoforms were stably expressed as glycosylphosphatidyl - inositol-anchored molecules in the membrane of HEp-2 cells and used as autoantigenic targets in indirect immunofluorescence assay (IFA).	Glycosylphosphatidylinositols	47-78	glycoprotein 2	Homo sapiens	9-12