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