PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
22777911-1	2012	TAPP1 and TAPP2 (where TAPP is tandem PH domain containing protein) are dual PH domain adaptors that selectively bind PI(3,4)P2 (phosphatidylinositol (3,4)-bisphosphate).	phosphoinositide-3,4-bisphosphate	118-127	pleckstrin homology domain containing, family A (phosphoinositide binding specific) member 1	Mus musculus	0-5	
27859053-3	2017	TAPP KI mice bearing PH domain-inactivating mutations in both TAPP1 and TAPP2 genes, uncoupling them from PI(3,4)P2, exhibit increased BCR-induced activation of the kinase Akt and develop lupus-like characteristics including anti-DNA antibodies and deposition of immune complexes in kidneys.	phosphoinositide-3,4-bisphosphate	106-115	pleckstrin homology domain containing, family A (phosphoinositide binding specific) member 1	Mus musculus	62-67	
21204784-9	2011	These observations provide the first genetic evidence to support the notion that binding of TAPP1 and TAPP2 adap-tors to PtdIns(3,4)P(2) function as negative regulators of the insulin and PI3K signalling pathways.	phosphoinositide-3,4-bisphosphate	121-133	pleckstrin homology domain containing, family A (phosphoinositide binding specific) member 1	Mus musculus	92-97	
12605860-8	2003	The versatility and general utility of this approach were demonstrated by exchanging the GRP1 PH domain for that of TAPP1 (which binds PtdIns(3,4)P(2) and not PtdIns(3,4,5)P(3)).	phosphoinositide-3,4-bisphosphate	135-147	pleckstrin homology domain containing, family A (phosphoinositide binding specific) member 1	Mus musculus	116-121