PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
28247964-7	2017	Overexpression of the TAPP1 PH domain, which binds to PI(3,4)P2 , and knockdown of Lpd, a downstream effector of PI(3,4)P2 , resulted in similar phenotypes to those induced by SHIP2 knockdown.	phosphoinositide-3,4-bisphosphate	54-63	pleckstrin homology domain containing A1	Homo sapiens	22-27	
29103771-1	2017	Tandem pH domain-containing proteins TAPP1 and TAPP2 are adaptor proteins that specifically bind to phosphatidylinositol-3,4-bisphosphate, or PI(3,4)P2, a product of phosphoinositide 3-kinases (PI3K).	phosphoinositide-3,4-bisphosphate	142-151	pleckstrin homology domain containing A1	Homo sapiens	37-42	
26022180-6	2015	A number of signaling proteins that specifically bind to PI(3,4)P2 have been characterized, including the tandem PH domain-containing proteins (TAPP1 and TAPP2) and lamellipodin/RAPH1.	phosphoinositide-3,4-bisphosphate	57-66	pleckstrin homology domain containing A1	Homo sapiens	144-149	
11513726-4	2001	Recently, a new PH-domain-containing protein, termed tandem PH-domain-containing protein (TAPP) 1, was described which is the first protein reported to bind PtdIns(3,4)P(2) specifically.	phosphoinositide-3,4-bisphosphate	157-169	pleckstrin homology domain containing A1	Homo sapiens	60-97	
23460911-2	2013	Tandem PH domain-containing proteins TAPP1 and TAPP2 are adaptor proteins that specifically bind to phosphatidylinositol-3,4-bisphosphate, or PI(3,4)P2, a product of phosphoinositide 3-kinases (PI3K).	phosphoinositide-3,4-bisphosphate	142-151	pleckstrin homology domain containing A1	Homo sapiens	37-42	
24038012-9	2014	In addition, visualization of PI(3,4)P2 with the fluorescent protein fused with the TAPP1-derived pleckstrin homology (PH) domain suggested that Gg-VSP influenced the distribution of PI(3,4)P2 .	phosphoinositide-3,4-bisphosphate	30-39	pleckstrin homology domain containing A1	Homo sapiens	84-89	
24038012-9	2014	In addition, visualization of PI(3,4)P2 with the fluorescent protein fused with the TAPP1-derived pleckstrin homology (PH) domain suggested that Gg-VSP influenced the distribution of PI(3,4)P2 .	phosphoinositide-3,4-bisphosphate	183-192	pleckstrin homology domain containing A1	Homo sapiens	84-89	
21263009-4	2011	A secondary purification of these proteins, optimized using tandem pleckstrin homology domain containing protein-1 (TAPP-1), an established PtdIns(3,4)P(2) selective ligand, yields a fraction enriched in proteins of potentially similar lipid binding character that are identified by liquid chromatography-tandem MS. Thirdly, this approach is coupled to stable isotope labeling with amino acids in cell culture using differential isotope labeling of cells stimulated in the absence and presence of the PI 3-kinase inhibitor wortmannin.	phosphoinositide-3,4-bisphosphate	140-152	pleckstrin homology domain containing A1	Homo sapiens	116-122	
11513726-8	2001	We show that mutation of this glycine to alanine in DAPP1 converts DAPP1 into a TAPP1-like PH domain that only interacts with PtdIns(3,4)P(2), whereas the alanine to glycine mutation in TAPP1 permits the TAPP1 PH domain to interact with PtdIns(3,4,5)P(3).	phosphoinositide-3,4-bisphosphate	126-138	pleckstrin homology domain containing A1	Homo sapiens	80-85