PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
21775285-2	2011	Akt is activated during growth factor stimulation through a process that requires binding of Akt to phosphatidylinositol 3,4,5-trisphosphate (PIP(3)), which promotes membrane localization and phosphorylation of Akt by the upstream kinase PDK1 (phosphoinositide-dependent protein kinase 1).	pip(3)	142-148	thymoma viral proto-oncogene 1	Mus musculus	0-3	
21775285-4	2011	Acetylation blocked binding of Akt and PDK1 to PIP(3), thereby preventing membrane localization and phosphorylation of Akt.	pip(3)	47-53	thymoma viral proto-oncogene 1	Mus musculus	119-122	
21775285-5	2011	Deacetylation by SIRT1 enhanced binding of Akt and PDK1 to PIP(3) and promoted their activation.	pip(3)	59-65	thymoma viral proto-oncogene 1	Mus musculus	43-46	
21775285-2	2011	Akt is activated during growth factor stimulation through a process that requires binding of Akt to phosphatidylinositol 3,4,5-trisphosphate (PIP(3)), which promotes membrane localization and phosphorylation of Akt by the upstream kinase PDK1 (phosphoinositide-dependent protein kinase 1).	pip(3)	142-148	thymoma viral proto-oncogene 1	Mus musculus	93-96	
21775285-2	2011	Akt is activated during growth factor stimulation through a process that requires binding of Akt to phosphatidylinositol 3,4,5-trisphosphate (PIP(3)), which promotes membrane localization and phosphorylation of Akt by the upstream kinase PDK1 (phosphoinositide-dependent protein kinase 1).	pip(3)	142-148	thymoma viral proto-oncogene 1	Mus musculus	93-96	
21775285-3	2011	We show that Akt and PDK1 are acetylated at lysine residues in their pleckstrin homology domains, which mediate PIP(3) binding.	pip(3)	112-118	thymoma viral proto-oncogene 1	Mus musculus	13-16	
21775285-4	2011	Acetylation blocked binding of Akt and PDK1 to PIP(3), thereby preventing membrane localization and phosphorylation of Akt.	pip(3)	47-53	thymoma viral proto-oncogene 1	Mus musculus	31-34	
16243036-3	2005	Here, we characterized P-Rex1, a Gbetagamma and PIP(3)-regulated guanine nucleotide exchange factor that was initially identified as a Rac activator in response to chemoattractants, for its roles in the regulation of Rac activity and neutrophil functions.	pip(3)	48-54	thymoma viral proto-oncogene 1	Mus musculus	135-138	
16243036-3	2005	Here, we characterized P-Rex1, a Gbetagamma and PIP(3)-regulated guanine nucleotide exchange factor that was initially identified as a Rac activator in response to chemoattractants, for its roles in the regulation of Rac activity and neutrophil functions.	pip(3)	48-54	thymoma viral proto-oncogene 1	Mus musculus	217-220