PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
25699547-5	2015	In addition to the expected activation of Btk by membranes containing phosphatidylinositol triphosphate (PIP3), we found that inositol hexakisphosphate (IP6), a soluble signaling molecule found in both animal and plant cells, also activates Btk.	Phytic Acid	126-151	Bruton tyrosine kinase	Homo sapiens	241-244	
31189594-4	2019	Here, we find that inositol hexakisphosphate (InsP6) acts as a physiological regulator of Btk in BCR signaling.	Phytic Acid	19-44	Bruton tyrosine kinase	Homo sapiens	90-93	
25699547-5	2015	In addition to the expected activation of Btk by membranes containing phosphatidylinositol triphosphate (PIP3), we found that inositol hexakisphosphate (IP6), a soluble signaling molecule found in both animal and plant cells, also activates Btk.	Phytic Acid	153-156	Bruton tyrosine kinase	Homo sapiens	241-244	
25699547-7	2015	Sequence comparisons with other Tec-family kinases suggest that activation by IP6 is unique to Btk.	Phytic Acid	78-81	Bruton tyrosine kinase	Homo sapiens	95-98	
9240435-0	1997	Characterization of the pleckstrin homology domain of Btk as an inositol polyphosphate and phosphoinositide binding domain.	Phytic Acid	64-86	Bruton tyrosine kinase	Homo sapiens	54-57	
8939985-5	1996	In contrast, a gain-of-function mutant called Btk*, which carries a E41K mutation in the PH domain, binds IP6 with two times higher affinity than the wild type.	Phytic Acid	106-109	Bruton tyrosine kinase	Homo sapiens	46-49