PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
9328837-7	1997	These findings are consistent with our earlier model that SHIP and Grb2 compete for binding to phospho-Shc and support the notion that, in addition to the hydrolysis of inositol phosphates and phospholipids, SHIP contributes to anti-proliferative biochemistry by blocking protein-protein interactions.	Inositol Phosphates	169-188	inositol polyphosphate-5-phosphatase D	Homo sapiens	58-62	
21864674-3	2012	In addition, SHIP1 converts Ins(1,3,4,5)P(4) to Ins(1,3,4)P(3) thereby regulating inositol phosphate metabolism.	Inositol Phosphates	82-100	inositol polyphosphate-5-phosphatase D	Homo sapiens	13-18	
21864674-11	2012	Our data indicate that SHIP1 is partly localized in the nucleus and suggest that SHIP1 plays a role for nuclear phosphoinositide and/or nuclear inositol phosphate signaling.	Inositol Phosphates	144-162	inositol polyphosphate-5-phosphatase D	Homo sapiens	23-28	
21864674-11	2012	Our data indicate that SHIP1 is partly localized in the nucleus and suggest that SHIP1 plays a role for nuclear phosphoinositide and/or nuclear inositol phosphate signaling.	Inositol Phosphates	144-162	inositol polyphosphate-5-phosphatase D	Homo sapiens	81-86	
32005521-4	2020	In this study, we identified new inositol phosphate (InsP) substrates of SHIP1 by metal dye detection high-performance liquid chromatography and compared the substrate profiles of SHIP1 and SHIP2.	Inositol Phosphates	33-51	inositol polyphosphate-5-phosphatase D	Homo sapiens	73-78