PMID-sentid	Pub_year	Sent_text	compound_name	comp_offset	prot_official_name	organism	prot_offset
15100098-7	2004	To further establish that the stimulation of sodium transport induced by insulin is related to PIP(3) levels, we transfected A6 cells with human PTEN cDNA and observed a 30% decrease in the natriferic effect of insulin.	pip(3)	95-101	insulin	Homo sapiens	73-80
15282193-9	2004	Notably, in response to insulin, phosphatidylinositol 3,4,5-trisphosphate (PIP(3)) formed in the basolateral membrane, rapidly diffused within the bilayer, and crossed the tight junction to enter the apical membrane.	pip(3)	75-81	insulin	Homo sapiens	24-31
15610010-4	2004	The present study focuses on the PH domain of the general receptor for phosphoinositides, isoform 1 (GRP1), which regulates the actin cytoskeleton in response to PIP(3) signals at the plasma membrane surface.	pip(3)	162-168	cytohesin 3	Homo sapiens	50-99
15610010-4	2004	The present study focuses on the PH domain of the general receptor for phosphoinositides, isoform 1 (GRP1), which regulates the actin cytoskeleton in response to PIP(3) signals at the plasma membrane surface.	pip(3)	162-168	cytohesin 3	Homo sapiens	101-105
15610010-6	2004	Equilibrium binding measurements utilizing protein-to-membrane fluorescence resonance energy transfer (FRET) to detect GRP1-PH domain docking to membrane-bound PIP lipids confirm specific binding to PIP(3).	pip(3)	199-205	cytohesin 3	Homo sapiens	119-123
15610010-7	2004	A novel FRET competitive binding measurement developed to quantitate docking affinity yields a K(D) of 50 +/- 10 nM for GRP1-PH domain binding to membrane-bound PIP(3) in a physiological lipid mixture approximating the composition of the plasma membrane inner leaflet.	pip(3)	161-167	cytohesin 3	Homo sapiens	120-124
15100098-7	2004	To further establish that the stimulation of sodium transport induced by insulin is related to PIP(3) levels, we transfected A6 cells with human PTEN cDNA and observed a 30% decrease in the natriferic effect of insulin.	pip(3)	95-101	phosphatase and tensin homolog	Homo sapiens	145-149
15100098-7	2004	To further establish that the stimulation of sodium transport induced by insulin is related to PIP(3) levels, we transfected A6 cells with human PTEN cDNA and observed a 30% decrease in the natriferic effect of insulin.	pip(3)	95-101	insulin	Homo sapiens	211-218
15100098-8	2004	Similarly, the increase in sodium transport observed by addition of permeant PIP(3) was also reduced by 30% in PTEN-overexpressing cells.	pip(3)	77-83	phosphatase and tensin homolog	Homo sapiens	111-115
14718524-2	2004	This PIP(3) phosphatase activity of PTEN contributes to its tumor suppressor function by inhibition of Akt kinase, a direct target of PIP(3).	pip(3)	5-11	phosphatase and tensin homolog	Homo sapiens	36-40
15001465-4	2004	Since SHIP shares the same substrate (PIP(3)) with Pten, we hypothesized that the former might compensate for Pten haploinsufficiency in the marrow.	pip(3)	38-44	inositol polyphosphate-5-phosphatase D	Mus musculus	6-10
14764529-3	2004	Using a novel fluorescent stain, we show that both populations generate similar levels of a key messenger, phosphatidylinositol 3,4,5 trisphosphate (PIP(3)), in response to SDF-1.	pip(3)	149-155	chemokine (C-X-C motif) ligand 12	Mus musculus	173-178
14718524-2	2004	This PIP(3) phosphatase activity of PTEN contributes to its tumor suppressor function by inhibition of Akt kinase, a direct target of PIP(3).	pip(3)	5-11	AKT serine/threonine kinase 1	Homo sapiens	103-106
14560023-7	2003	This phosphorylation inhibited phosphatidylinositol 3,4,5-trisphosphate (PIP(3)) binding to PKB, thereby preventing activation of the kinase by insulin.	pip(3)	73-79	protein tyrosine kinase 2 beta	Homo sapiens	92-95
14607243-5	2003	Examples for the former are as follows: (i) Phosphatidylinositol 3,4,5-trisphosphate (PIP(3)) inhibits RGS-action, which can be recovered by Ca(2+)/calmodulin.	pip(3)	86-92	paired like homeodomain 2	Homo sapiens	103-106
14560023-7	2003	This phosphorylation inhibited phosphatidylinositol 3,4,5-trisphosphate (PIP(3)) binding to PKB, thereby preventing activation of the kinase by insulin.	pip(3)	73-79	insulin	Homo sapiens	144-151
14560023-8	2003	In contrast, a PKB-PH domain with a T34A mutation retained the ability to bind PIP(3) even in the presence of a ceramide-activated PKCzeta and, as such, expression of PKB T34A mutant in L6 cells was resistant to inhibition by ceramide treatment.	pip(3)	79-85	protein tyrosine kinase 2 beta	Homo sapiens	15-18
14560023-8	2003	In contrast, a PKB-PH domain with a T34A mutation retained the ability to bind PIP(3) even in the presence of a ceramide-activated PKCzeta and, as such, expression of PKB T34A mutant in L6 cells was resistant to inhibition by ceramide treatment.	pip(3)	79-85	protein kinase C zeta	Homo sapiens	131-138
14560023-8	2003	In contrast, a PKB-PH domain with a T34A mutation retained the ability to bind PIP(3) even in the presence of a ceramide-activated PKCzeta and, as such, expression of PKB T34A mutant in L6 cells was resistant to inhibition by ceramide treatment.	pip(3)	79-85	protein tyrosine kinase 2 beta	Homo sapiens	167-170
19003108-4	2002	The recombinant S3a protein bound specifically to PIP(3).	pip(3)	50-56	ribosomal protein S3A	Homo sapiens	16-19
12606772-5	2003	PIP(3) production peaks 30 s after shear begins and is initiated by von Willebrand factor (VWF) binding to the glycoprotein (Gp) Ib-IX-V complex.	pip(3)	0-6	von Willebrand factor	Homo sapiens	68-89
12606772-5	2003	PIP(3) production peaks 30 s after shear begins and is initiated by von Willebrand factor (VWF) binding to the glycoprotein (Gp) Ib-IX-V complex.	pip(3)	0-6	von Willebrand factor	Homo sapiens	91-94
12606772-9	2003	Inhibiting Syk activation with piceatannol results in the inhibition of PIP(3) production and aggregation.	pip(3)	72-78	spleen associated tyrosine kinase	Homo sapiens	11-14
12761192-3	2003	The major activation pathway of PKCzeta depends on phosphatidylinositol (PI)-3,4,5-trisphosphate (PIP(3)), which is mainly produced by PI-3 kinase.	pip(3)	98-104	protein kinase C zeta	Homo sapiens	32-39
12761192-4	2003	3"-PI-dependent protein kinase 1, which binds with high affinity to PIP(3), phosphorylates and activates PKCzeta.	pip(3)	68-74	protein kinase C zeta	Homo sapiens	105-112
12887923-7	2003	Although ligand-induced production of PIP(3) is not required for activation of this pathway, PIP(3) appears to localize the activation of Cdc42 by the pathway.	pip(3)	93-99	cell division cycle 42	Homo sapiens	138-143
11897055-3	2002	Mutations in the Btk PH domain result in changes in its affinity for PIP(3), with higher binding leading to cell transformation in vitro and lower binding leading to antibody deficiencies in both humans and mice.	pip(3)	69-75	Bruton tyrosine kinase	Homo sapiens	17-20
12123595-0	2002	Rac activation: P-Rex1 - a convergence point for PIP(3) and Gbetagamma?	pip(3)	49-55	AKT serine/threonine kinase 1	Homo sapiens	0-3
12123595-0	2002	Rac activation: P-Rex1 - a convergence point for PIP(3) and Gbetagamma?	pip(3)	49-55	phosphatidylinositol-3,4,5-trisphosphate dependent Rac exchange factor 1	Homo sapiens	16-22
12123595-2	2002	P-Rex1 is synergistically activated by PIP(3) and Gbetagamma and may act as a coincidence detector for these signaling molecules.	pip(3)	39-45	phosphatidylinositol-3,4,5-trisphosphate dependent Rac exchange factor 1	Homo sapiens	0-6
11882383-4	2002	PI-3K generates phosphatidylinositol-3,4,5-trisphosphate (PIP(3)), a lipid second messenger essential for the translocation of PKB/Akt to the plasma membrane where it is phosphorylated and activated by phosphoinositide-dependent kinase-1 (PDK-1) and possibly other kinases.	pip(3)	58-64	AKT serine/threonine kinase 1	Homo sapiens	127-130
11882383-4	2002	PI-3K generates phosphatidylinositol-3,4,5-trisphosphate (PIP(3)), a lipid second messenger essential for the translocation of PKB/Akt to the plasma membrane where it is phosphorylated and activated by phosphoinositide-dependent kinase-1 (PDK-1) and possibly other kinases.	pip(3)	58-64	AKT serine/threonine kinase 1	Homo sapiens	131-134
11882383-4	2002	PI-3K generates phosphatidylinositol-3,4,5-trisphosphate (PIP(3)), a lipid second messenger essential for the translocation of PKB/Akt to the plasma membrane where it is phosphorylated and activated by phosphoinositide-dependent kinase-1 (PDK-1) and possibly other kinases.	pip(3)	58-64	pyruvate dehydrogenase kinase 1	Homo sapiens	202-237
11882383-4	2002	PI-3K generates phosphatidylinositol-3,4,5-trisphosphate (PIP(3)), a lipid second messenger essential for the translocation of PKB/Akt to the plasma membrane where it is phosphorylated and activated by phosphoinositide-dependent kinase-1 (PDK-1) and possibly other kinases.	pip(3)	58-64	pyruvate dehydrogenase kinase 1	Homo sapiens	239-244
11141077-5	2001	Activating effects of insulin and/or PIP(3) on enzyme activity were completely abolished in T410A-PKC-zeta, partially compromised in T560A-PKC-zeta, T410E/T560A-PKC-zeta, and T410A/T560E-PKC-zeta, and largely intact in T410E-PKC-zeta, T560E-PKC-zeta, and T410E/T560E-PKC-zeta.	pip(3)	37-43	protein kinase C zeta	Homo sapiens	98-106
11222379-7	2001	These results suggest that the C-terminus plays a critical role in enabling SHIP to hydrolyze PIP(3) and inhibit BMMC degranulation.	pip(3)	94-100	inositol polyphosphate-5-phosphatase D	Mus musculus	76-80
11141077-5	2001	Activating effects of insulin and/or PIP(3) on enzyme activity were completely abolished in T410A-PKC-zeta, partially compromised in T560A-PKC-zeta, T410E/T560A-PKC-zeta, and T410A/T560E-PKC-zeta, and largely intact in T410E-PKC-zeta, T560E-PKC-zeta, and T410E/T560E-PKC-zeta.	pip(3)	37-43	protein kinase C zeta	Homo sapiens	139-147
11141077-5	2001	Activating effects of insulin and/or PIP(3) on enzyme activity were completely abolished in T410A-PKC-zeta, partially compromised in T560A-PKC-zeta, T410E/T560A-PKC-zeta, and T410A/T560E-PKC-zeta, and largely intact in T410E-PKC-zeta, T560E-PKC-zeta, and T410E/T560E-PKC-zeta.	pip(3)	37-43	protein kinase C zeta	Homo sapiens	139-147
11141077-5	2001	Activating effects of insulin and/or PIP(3) on enzyme activity were completely abolished in T410A-PKC-zeta, partially compromised in T560A-PKC-zeta, T410E/T560A-PKC-zeta, and T410A/T560E-PKC-zeta, and largely intact in T410E-PKC-zeta, T560E-PKC-zeta, and T410E/T560E-PKC-zeta.	pip(3)	37-43	protein kinase C zeta	Homo sapiens	139-147
11141077-5	2001	Activating effects of insulin and/or PIP(3) on enzyme activity were completely abolished in T410A-PKC-zeta, partially compromised in T560A-PKC-zeta, T410E/T560A-PKC-zeta, and T410A/T560E-PKC-zeta, and largely intact in T410E-PKC-zeta, T560E-PKC-zeta, and T410E/T560E-PKC-zeta.	pip(3)	37-43	protein kinase C zeta	Homo sapiens	139-147
11141077-5	2001	Activating effects of insulin and/or PIP(3) on enzyme activity were completely abolished in T410A-PKC-zeta, partially compromised in T560A-PKC-zeta, T410E/T560A-PKC-zeta, and T410A/T560E-PKC-zeta, and largely intact in T410E-PKC-zeta, T560E-PKC-zeta, and T410E/T560E-PKC-zeta.	pip(3)	37-43	protein kinase C zeta	Homo sapiens	139-147
11141077-5	2001	Activating effects of insulin and/or PIP(3) on enzyme activity were completely abolished in T410A-PKC-zeta, partially compromised in T560A-PKC-zeta, T410E/T560A-PKC-zeta, and T410A/T560E-PKC-zeta, and largely intact in T410E-PKC-zeta, T560E-PKC-zeta, and T410E/T560E-PKC-zeta.	pip(3)	37-43	protein kinase C zeta	Homo sapiens	139-147
11141077-8	2001	Insulin, but not PIP(3), activated truncated, pseudosubstrate-lacking forms of PKC-zeta and PKC-lambda by a wortmannin-sensitive mechanism, apparently involving PI 3-kinase/PDK-1-dependent phosphorylations but independent of PIP(3)-dependent conformational activation.	pip(3)	225-231	insulin	Homo sapiens	0-7
11141077-9	2001	Our findings suggest that insulin, via PIP(3), provokes increases in PKC-zeta enzyme activity through (a) PDK-1-dependent T410 loop phosphorylation, (b) T560 autophosphorylation, and (c) phosphorylation-independent/conformational-dependent relief of pseudosubstrate autoinhibition.	pip(3)	39-45	insulin	Homo sapiens	26-33
11141077-9	2001	Our findings suggest that insulin, via PIP(3), provokes increases in PKC-zeta enzyme activity through (a) PDK-1-dependent T410 loop phosphorylation, (b) T560 autophosphorylation, and (c) phosphorylation-independent/conformational-dependent relief of pseudosubstrate autoinhibition.	pip(3)	39-45	protein kinase C zeta	Homo sapiens	69-77
11141077-9	2001	Our findings suggest that insulin, via PIP(3), provokes increases in PKC-zeta enzyme activity through (a) PDK-1-dependent T410 loop phosphorylation, (b) T560 autophosphorylation, and (c) phosphorylation-independent/conformational-dependent relief of pseudosubstrate autoinhibition.	pip(3)	39-45	3-phosphoinositide dependent protein kinase 1	Homo sapiens	106-111
20826681-9	2010	Using the green fluorescent protein-plekstrin homology domain of Akt, which targets to PI3K-generated phosphatidylinositol-3,4,5-triphosphate (PIP(3)), we report localized microdomains of PIP(3) accumulation that form in synchrony with F-actin patches and that NGF promotes the formation of microdomains of PIP(3) and patches.	pip(3)	143-149	nerve growth factor	Gallus gallus	261-264
10464256-5	1999	Also, insulin in situ and PIP(3) in vitro activated and stimulated autophosphorylation of a PKC-zeta mutant, in which threonine 410 is replaced by glutamate (but not by an inactivating alanine) and cannot be activated by PDK-1.	pip(3)	26-32	pyruvate dehydrogenase kinase 1	Rattus norvegicus	221-226
10464256-6	1999	Surprisingly, insulin activated a truncated PKC-zeta that lacks the regulatory (presumably PIP(3)-binding) domain; this may reflect PIP(3) effects on PDK-1 or transphosphorylation by endogenous full-length PKC-zeta.	pip(3)	132-138	pyruvate dehydrogenase kinase 1	Rattus norvegicus	150-155
10464256-7	1999	Our findings suggest that insulin activates both PKC-zeta and PKC-lambda in plasma membranes, microsomes, and GLUT4 vesicles by a mechanism requiring increases in PIP(3), PDK-1-dependent phosphorylation of activation loop sites in PKC-zeta and lambda, and subsequent autophosphorylation and/or transphosphorylation.	pip(3)	163-169	protein kinase C, zeta	Rattus norvegicus	49-52
23051731-6	2012	p110alpha was activated at mitosis entry and regulated early mitotic events, such as PIP(3) generation, prometaphase progression, and spindle orientation.	pip(3)	85-91	phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit alpha	Homo sapiens	0-9
22279049-7	2012	At the same time, stabilization of the PTEN mRNA by IGF2BP1 enhances PTEN expression and antagonizes PIP(3)-directed signaling.	pip(3)	101-107	phosphatase and tensin homolog	Homo sapiens	39-43
22279049-7	2012	At the same time, stabilization of the PTEN mRNA by IGF2BP1 enhances PTEN expression and antagonizes PIP(3)-directed signaling.	pip(3)	101-107	insulin like growth factor 2 mRNA binding protein 1	Homo sapiens	52-59
21828076-1	2011	The PTEN (phosphatase and tensin homolog) phosphatase is unique in mammals in terms of its tumor suppressor activity, exerted by dephosphorylation of the lipid second messenger PIP(3) (phosphatidylinositol 3,4,5-trisphosphate), which activates the phosphoinositide 3-kinase/Akt/mTOR (mammalian target of rapamycin) oncogenic pathway.	pip(3)	177-183	phosphatase and tensin homolog	Homo sapiens	4-8
21828076-1	2011	The PTEN (phosphatase and tensin homolog) phosphatase is unique in mammals in terms of its tumor suppressor activity, exerted by dephosphorylation of the lipid second messenger PIP(3) (phosphatidylinositol 3,4,5-trisphosphate), which activates the phosphoinositide 3-kinase/Akt/mTOR (mammalian target of rapamycin) oncogenic pathway.	pip(3)	177-183	AKT serine/threonine kinase 1	Homo sapiens	274-277
21828076-1	2011	The PTEN (phosphatase and tensin homolog) phosphatase is unique in mammals in terms of its tumor suppressor activity, exerted by dephosphorylation of the lipid second messenger PIP(3) (phosphatidylinositol 3,4,5-trisphosphate), which activates the phosphoinositide 3-kinase/Akt/mTOR (mammalian target of rapamycin) oncogenic pathway.	pip(3)	177-183	mechanistic target of rapamycin kinase	Homo sapiens	278-282
21828076-1	2011	The PTEN (phosphatase and tensin homolog) phosphatase is unique in mammals in terms of its tumor suppressor activity, exerted by dephosphorylation of the lipid second messenger PIP(3) (phosphatidylinositol 3,4,5-trisphosphate), which activates the phosphoinositide 3-kinase/Akt/mTOR (mammalian target of rapamycin) oncogenic pathway.	pip(3)	177-183	mechanistic target of rapamycin kinase	Homo sapiens	284-313
21474070-4	2011	Anchored PKA activates PDE3B to enhance cAMP degradation and phosphorylates p110gamma to inhibit PIP(3) production.	pip(3)	97-103	phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit gamma	Homo sapiens	76-85
21097842-5	2011	We find that oxidative inactivation of the lipid phosphatase PTEN by As(2)O(3) enhances cardiac calcium currents in the therapeutic concentration range via a PI3Kalpha-dependent increase in phosphatidylinositol 3,4,5-triphosphate (PIP(3)) production.	pip(3)	231-237	phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN	Cavia porcellus	61-65
21097842-6	2011	In guinea pig ventricular myocytes, even a modest reduction in PTEN activity is sufficient to increase cellular PIP(3) levels.	pip(3)	112-118	phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN	Cavia porcellus	63-67
21097842-7	2011	Under control conditions, PIP(3) levels are kept low by PTEN and do not affect calcium current amplitudes.	pip(3)	26-32	phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN	Cavia porcellus	56-60
21220345-1	2011	The second messenger phosphatidylinositol (3,4,5)-trisphosphate (PIP(3)), formed by the p110 family of PI3-kinases, promotes cellular growth, proliferation, and survival, in large part by activating the protein kinase Akt/PKB.	pip(3)	65-71	AKT serine/threonine kinase 1	Homo sapiens	218-225
21220345-2	2011	We show that inositol polyphosphate multikinase (IPMK) physiologically generates PIP(3) as well as water soluble inositol phosphates.	pip(3)	81-87	inositol polyphosphate multikinase	Homo sapiens	13-47
21184743-3	2011	After stimulation with insulin-like growth factor I (IGF-I), MYH9 colocalized with PIP(3) in lamellipodia at the leading edge of cells.	pip(3)	83-89	insulin like growth factor 1	Homo sapiens	23-51
21184743-3	2011	After stimulation with insulin-like growth factor I (IGF-I), MYH9 colocalized with PIP(3) in lamellipodia at the leading edge of cells.	pip(3)	83-89	insulin like growth factor 1	Homo sapiens	53-58
21184743-3	2011	After stimulation with insulin-like growth factor I (IGF-I), MYH9 colocalized with PIP(3) in lamellipodia at the leading edge of cells.	pip(3)	83-89	myosin heavy chain 9	Homo sapiens	61-65
21556061-1	2011	PTEN dephosphorylates the 3-position phosphate of phosphatidylinositol 3,4,5 triphosphate (PIP(3)), thereby inhibiting AKT activation.	pip(3)	91-97	phosphatase and tensin homolog	Homo sapiens	0-4
21556061-1	2011	PTEN dephosphorylates the 3-position phosphate of phosphatidylinositol 3,4,5 triphosphate (PIP(3)), thereby inhibiting AKT activation.	pip(3)	91-97	AKT serine/threonine kinase 1	Homo sapiens	119-122
21779440-6	2010	As PTEN exerts enzymatic activity as a phosphatidylinositol-3,4,5-trisphosphate (PIP(3)) phosphatase, thus opposing the activity of PI3K, the concerted actions to increase the availability of PIP(3) in cancer cells, relying either on other phosphoinositide enzymes or on the intrinsic regulation of PTEN activity by other molecules, will be discussed.	pip(3)	81-87	phosphatase and tensin homolog	Homo sapiens	3-7
21779440-6	2010	As PTEN exerts enzymatic activity as a phosphatidylinositol-3,4,5-trisphosphate (PIP(3)) phosphatase, thus opposing the activity of PI3K, the concerted actions to increase the availability of PIP(3) in cancer cells, relying either on other phosphoinositide enzymes or on the intrinsic regulation of PTEN activity by other molecules, will be discussed.	pip(3)	81-87	phosphatase and tensin homolog	Homo sapiens	299-303
10747990-4	2000	Amino acid substitutions in helix 5 within the RGS domain of RGS4 reduce binding affinity and inhibition by PIP(3) but do not affect inhibition of GAP activity by palmitoylation.	pip(3)	108-114	regulator of G protein signaling 4	Homo sapiens	61-65
10747990-5	2000	Conversely, the GAP activity of a palmitoylation-resistant mutant RGS4 is inhibited by PIP(3).	pip(3)	87-93	regulator of G protein signaling 4	Homo sapiens	66-70
10747990-8	2000	Ca(2+)/calmodulin reverses PIP(3)-mediated but not palmitoylation-mediated inhibition of GAP activity.	pip(3)	27-33	calmodulin 1	Homo sapiens	7-17
22729222-5	2012	Affected dermal fibroblasts showed enhanced basal and epidermal growth factor (EGF)-stimulated phosphatidylinositol 3,4,5-trisphosphate (PIP(3)) generation and concomitant activation of downstream signaling relative to their unaffected counterparts.	pip(3)	137-143	epidermal growth factor	Homo sapiens	54-77
22729222-5	2012	Affected dermal fibroblasts showed enhanced basal and epidermal growth factor (EGF)-stimulated phosphatidylinositol 3,4,5-trisphosphate (PIP(3)) generation and concomitant activation of downstream signaling relative to their unaffected counterparts.	pip(3)	137-143	epidermal growth factor	Homo sapiens	79-82
23028816-1	2012	Binding of the membrane phospholipid phosphatidylinositol 3,4,5-trisphosphate (PIP(3)) to the Pleckstrin Homology (PH) domain of the Tec family protein tyrosine kinase, Inducible T cell Kinase (ITK), is critical for the recruitment of the kinase to the plasma membrane and its co-localization with the TCR-CD3 molecular complex.	pip(3)	79-85	IL2 inducible T cell kinase	Homo sapiens	169-192
23028816-1	2012	Binding of the membrane phospholipid phosphatidylinositol 3,4,5-trisphosphate (PIP(3)) to the Pleckstrin Homology (PH) domain of the Tec family protein tyrosine kinase, Inducible T cell Kinase (ITK), is critical for the recruitment of the kinase to the plasma membrane and its co-localization with the TCR-CD3 molecular complex.	pip(3)	79-85	IL2 inducible T cell kinase	Homo sapiens	194-197
23028816-5	2012	We found that FYF triple mutation inhibits the TCR-induced production of IL-4 by impairing ITK binding to PIP(3), reducing ITK membrane recruitment, inducing conformational changes at the T cell-APC contact site, and compromising phosphorylation of ITK and subsequent phosphorylation of PLCgamma(1).	pip(3)	106-112	interleukin 4	Homo sapiens	73-77
23028816-5	2012	We found that FYF triple mutation inhibits the TCR-induced production of IL-4 by impairing ITK binding to PIP(3), reducing ITK membrane recruitment, inducing conformational changes at the T cell-APC contact site, and compromising phosphorylation of ITK and subsequent phosphorylation of PLCgamma(1).	pip(3)	106-112	IL2 inducible T cell kinase	Homo sapiens	91-94
23028816-7	2012	Thus, the FYF mutation uncouples PIP(3)-mediated ITK membrane recruitment from the interactions of the kinase with key components of the TCR signalosome and abrogates ITK function in T cells.	pip(3)	33-39	IL2 inducible T cell kinase	Homo sapiens	49-52
23028816-7	2012	Thus, the FYF mutation uncouples PIP(3)-mediated ITK membrane recruitment from the interactions of the kinase with key components of the TCR signalosome and abrogates ITK function in T cells.	pip(3)	33-39	IL2 inducible T cell kinase	Homo sapiens	167-170
22848683-8	2012	Using this assay, we performed a detailed pharmacological analysis of PIP(3) production induced by IGF1, insulin and insulin analogues in living breast cancer-derived MCF-7 and MDA-MB231 cells.	pip(3)	70-76	insulin like growth factor 1	Homo sapiens	99-103
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
21775285-2	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
21775285-2	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	pyruvate dehydrogenase kinase, isoenzyme 1	Mus musculus	238-242
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	pyruvate dehydrogenase kinase, isoenzyme 1	Mus musculus	244-287
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
21775285-3	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	pyruvate dehydrogenase kinase, isoenzyme 1	Mus musculus	21-25
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
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	pyruvate dehydrogenase kinase, isoenzyme 1	Mus musculus	39-43
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	sirtuin 1	Mus musculus	17-22
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
21775285-5	2011	Deacetylation by SIRT1 enhanced binding of Akt and PDK1 to PIP(3) and promoted their activation.	pip(3)	59-65	pyruvate dehydrogenase kinase, isoenzyme 1	Mus musculus	51-55
21402045-3	2011	On activation of the pathway, PDK1 and AKT1/2 translocate to the membrane and bind to phosphatidylinositol-(3,4,5)-trisphosphate (PIP(3)) through interaction with their pleckstrin-homology domains.	pip(3)	130-136	pyruvate dehydrogenase (acetyl-transferring) kinase isozyme 1, mitochondrial	Cricetulus griseus	30-34
21402045-3	2011	On activation of the pathway, PDK1 and AKT1/2 translocate to the membrane and bind to phosphatidylinositol-(3,4,5)-trisphosphate (PIP(3)) through interaction with their pleckstrin-homology domains.	pip(3)	130-136	RAC-alpha serine/threonine-protein kinase	Cricetulus griseus	39-45
21402788-1	2011	Akt activation relies on the binding of Akt to phosphatidylinositol-3,4,5-trisphosphate (PIP(3)) in the membrane.	pip(3)	89-95	AKT serine/threonine kinase 1	Homo sapiens	0-3
21402788-1	2011	Akt activation relies on the binding of Akt to phosphatidylinositol-3,4,5-trisphosphate (PIP(3)) in the membrane.	pip(3)	89-95	AKT serine/threonine kinase 1	Homo sapiens	40-43
21402788-2	2011	Here, we demonstrate that Akt activation requires not only PIP(3) but also membrane phosphatidylserine (PS).	pip(3)	59-65	AKT serine/threonine kinase 1	Homo sapiens	26-29
21402788-4	2011	PS promotes Akt-PIP(3) binding, participates in PIP(3)-induced Akt interdomain conformational changes for T308 phosphorylation, and causes an open conformation that allows for S473 phosphorylation by mTORC2.	pip(3)	16-22	AKT serine/threonine kinase 1	Homo sapiens	12-15
21402788-4	2011	PS promotes Akt-PIP(3) binding, participates in PIP(3)-induced Akt interdomain conformational changes for T308 phosphorylation, and causes an open conformation that allows for S473 phosphorylation by mTORC2.	pip(3)	48-54	AKT serine/threonine kinase 1	Homo sapiens	63-66
21402788-4	2011	PS promotes Akt-PIP(3) binding, participates in PIP(3)-induced Akt interdomain conformational changes for T308 phosphorylation, and causes an open conformation that allows for S473 phosphorylation by mTORC2.	pip(3)	48-54	CREB regulated transcription coactivator 2	Mus musculus	200-206
21402788-7	2011	These data identify a critical function of PS for Akt activation and cell survival, particularly in conditions with limited PIP(3) availability.	pip(3)	124-130	AKT serine/threonine kinase 1	Homo sapiens	50-53
21220345-2	2011	We show that inositol polyphosphate multikinase (IPMK) physiologically generates PIP(3) as well as water soluble inositol phosphates.	pip(3)	81-87	inositol polyphosphate multikinase	Homo sapiens	49-53
21220345-5	2011	Thus, growth factor stimulation of Akt signaling involves PIP(3) generation through the sequential activations of the p110 PI3-kinases and IPMK.	pip(3)	58-64	AKT serine/threonine kinase 1	Homo sapiens	35-38
21220345-5	2011	Thus, growth factor stimulation of Akt signaling involves PIP(3) generation through the sequential activations of the p110 PI3-kinases and IPMK.	pip(3)	58-64	inositol polyphosphate multikinase	Homo sapiens	139-143
21172654-2	2010	Here, we identify the PIP(3)-Gbetagamma-dependent Rac-GEF P-Rex1 as an essential mediator of Rac1 activation, motility, cell growth, and tumorigenesis driven by ErbB receptors in breast cancer cells.	pip(3)	22-28	phosphatidylinositol-3,4,5-trisphosphate dependent Rac exchange factor 1	Homo sapiens	58-64
21172654-2	2010	Here, we identify the PIP(3)-Gbetagamma-dependent Rac-GEF P-Rex1 as an essential mediator of Rac1 activation, motility, cell growth, and tumorigenesis driven by ErbB receptors in breast cancer cells.	pip(3)	22-28	Rac family small GTPase 1	Homo sapiens	93-97
21172654-2	2010	Here, we identify the PIP(3)-Gbetagamma-dependent Rac-GEF P-Rex1 as an essential mediator of Rac1 activation, motility, cell growth, and tumorigenesis driven by ErbB receptors in breast cancer cells.	pip(3)	22-28	epidermal growth factor receptor	Homo sapiens	161-165
20010819-5	2010	PIP(3) downregulation impaired PSD-95 accumulation in spines.	pip(3)	0-6	discs large MAGUK scaffold protein 4	Rattus norvegicus	31-37
20197055-3	2010	Thus, deletion of p110alpha in liver results in markedly blunted insulin signaling with decreased generation of PIP(3) and loss of insulin activation of Akt, defects that could not be rescued by overexpression of p110beta.	pip(3)	112-118	phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit alpha	Mus musculus	18-27
20498366-7	2010	However, the amplitude of the PIP(3) response after PKA inhibition was restored by a specific agonist to the cAMP-dependent guanine nucleotide exchange factor Epac.	pip(3)	30-36	Rap guanine nucleotide exchange factor (GEF) 3	Mus musculus	159-163
20498366-8	2010	Suppression of cAMP formation with adenylyl cyclase inhibitors reduced already established PIP(3) oscillations in glucose-stimulated cells, and this effect was almost completely counteracted by the Epac agonist.	pip(3)	91-97	Rap guanine nucleotide exchange factor (GEF) 3	Mus musculus	198-202
20200318-9	2010	These changes were independent of impaired proliferation of muscle progenitor or satellite cells but were principally related to increased expression of PTEN, which reduced PIP(3) in muscle.	pip(3)	173-179	phosphatase and tensin homolog	Mus musculus	153-157
19897731-9	2009	The activity of immunoprecipitated phosphatidylinositol 3-kinase gamma (PI3Kgamma), responsible for chemoattractant-induced synthesis of PIP(3) and Akt phosphorylation, is unperturbed in p55(-/-) neutrophils.	pip(3)	137-143	phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit gamma	Mus musculus	35-70
19897731-9	2009	The activity of immunoprecipitated phosphatidylinositol 3-kinase gamma (PI3Kgamma), responsible for chemoattractant-induced synthesis of PIP(3) and Akt phosphorylation, is unperturbed in p55(-/-) neutrophils.	pip(3)	137-143	phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit gamma	Mus musculus	72-81
19897731-10	2009	Although the total amount of PIP(3) is normal in p55(-/-) neutrophils, PIP(3) is diffusely localized and forms punctate aggregates in activated p55(-/-) neutrophils, as compared to its accumulation at the leading edge membrane in the wild type neutrophils.	pip(3)	71-77	membrane protein, palmitoylated	Mus musculus	144-147
19602588-3	2009	PIP(3) recruits PDK1 and AKT to the cell membrane through interactions with their pleckstrin homology domains, allowing PDK1 to activate AKT by phosphorylating it at residue threonine-308.	pip(3)	0-6	pyruvate dehydrogenase kinase 1	Homo sapiens	16-20
20157769-6	2009	Using phosphoinositide-specific biosensors we confirmed that E-cadherin-based cell-cell contacts are enriched in PIP(3), the principal product of PI3-kinase.	pip(3)	113-119	cadherin 1	Homo sapiens	61-71
19602588-3	2009	PIP(3) recruits PDK1 and AKT to the cell membrane through interactions with their pleckstrin homology domains, allowing PDK1 to activate AKT by phosphorylating it at residue threonine-308.	pip(3)	0-6	AKT serine/threonine kinase 1	Homo sapiens	25-28
19602588-3	2009	PIP(3) recruits PDK1 and AKT to the cell membrane through interactions with their pleckstrin homology domains, allowing PDK1 to activate AKT by phosphorylating it at residue threonine-308.	pip(3)	0-6	pyruvate dehydrogenase kinase 1	Homo sapiens	120-124
19602588-3	2009	PIP(3) recruits PDK1 and AKT to the cell membrane through interactions with their pleckstrin homology domains, allowing PDK1 to activate AKT by phosphorylating it at residue threonine-308.	pip(3)	0-6	AKT serine/threonine kinase 1	Homo sapiens	137-140
18759931-4	2008	By limiting the amount of PIP(3) available within the cell, PTEN directly opposes PI3K activity and influences the selection of developing thymocytes as well as the activation requirements of mature T cells.	pip(3)	26-32	phosphatase and tensin homolog	Homo sapiens	60-64
19574958-7	2009	MyD88 is not essential for PI3K activation and Akt phosphorylation; however, cooperates with Mal for PIP(3) formation and accumulation at the leading edge.	pip(3)	101-107	MYD88 innate immune signal transduction adaptor	Homo sapiens	0-5
19295169-11	2009	These results suggest that, in Jurkat T cells, PIP(2), PIP(3), and SDF-1alpha reduce Kv1.3 channel activity and that the reduction by SDF-1alpha may be mediated by the enhancement of PIP(3) production.	pip(3)	55-61	potassium voltage-gated channel subfamily A member 3	Homo sapiens	85-90
19295169-11	2009	These results suggest that, in Jurkat T cells, PIP(2), PIP(3), and SDF-1alpha reduce Kv1.3 channel activity and that the reduction by SDF-1alpha may be mediated by the enhancement of PIP(3) production.	pip(3)	183-189	potassium voltage-gated channel subfamily A member 3	Homo sapiens	85-90
19357636-6	2009	The model predicts and experiments confirm that insulin-induced amplification of mitogenic signaling is abolished by disrupting PIP(3)-mediated positive feedback via GAB1 and IRS.	pip(3)	128-134	insulin	Homo sapiens	48-55
19357636-6	2009	The model predicts and experiments confirm that insulin-induced amplification of mitogenic signaling is abolished by disrupting PIP(3)-mediated positive feedback via GAB1 and IRS.	pip(3)	128-134	GRB2 associated binding protein 1	Homo sapiens	166-170
18794886-3	2008	PI3K-mediated PIP(3) production leads to the activation of the canonical AKT-mTORC1 pathway.	pip(3)	14-20	AKT serine/threonine kinase 1	Homo sapiens	73-76
18794886-3	2008	PI3K-mediated PIP(3) production leads to the activation of the canonical AKT-mTORC1 pathway.	pip(3)	14-20	CREB regulated transcription coactivator 1	Mus musculus	77-83
19759305-5	2009	This unexpected finding coincides with POMC-cell-specific, Stat3-mediated upregulation of SOCS3 expression inhibiting both leptin and insulin signaling as insulin-stimulated PIP(3) (phosphatidylinositol-3,4,5 triphosphate) formation and protein kinase B (AKT) activation in POMC neurons as well as with the fact that insulin"s ability to hyperpolarize POMC neurons is largely reduced in POMC cells of Stat3-C(POMC) mice.	pip(3)	174-180	pro-opiomelanocortin-alpha	Mus musculus	39-43
19759305-5	2009	This unexpected finding coincides with POMC-cell-specific, Stat3-mediated upregulation of SOCS3 expression inhibiting both leptin and insulin signaling as insulin-stimulated PIP(3) (phosphatidylinositol-3,4,5 triphosphate) formation and protein kinase B (AKT) activation in POMC neurons as well as with the fact that insulin"s ability to hyperpolarize POMC neurons is largely reduced in POMC cells of Stat3-C(POMC) mice.	pip(3)	174-180	signal transducer and activator of transcription 3	Mus musculus	59-64
19759305-5	2009	This unexpected finding coincides with POMC-cell-specific, Stat3-mediated upregulation of SOCS3 expression inhibiting both leptin and insulin signaling as insulin-stimulated PIP(3) (phosphatidylinositol-3,4,5 triphosphate) formation and protein kinase B (AKT) activation in POMC neurons as well as with the fact that insulin"s ability to hyperpolarize POMC neurons is largely reduced in POMC cells of Stat3-C(POMC) mice.	pip(3)	174-180	suppressor of cytokine signaling 3	Mus musculus	90-95
19680438-7	2009	Both chico and lnk mutant larvae display a similar reduction in IIS activity as judged by the localization of a PIP(3) reporter and the phosphorylation of protein kinase B (PKB).	pip(3)	112-118	Lnk	Drosophila melanogaster	15-18
19574958-7	2009	MyD88 is not essential for PI3K activation and Akt phosphorylation; however, cooperates with Mal for PIP(3) formation and accumulation at the leading edge.	pip(3)	101-107	mal, T cell differentiation protein	Homo sapiens	93-96
19574958-9	2009	Hence, Mal specifically connects TLR2/6 to PI3K activation, PIP(3) generation and macrophage polarization.	pip(3)	60-66	mal, T cell differentiation protein	Homo sapiens	7-10
19574958-9	2009	Hence, Mal specifically connects TLR2/6 to PI3K activation, PIP(3) generation and macrophage polarization.	pip(3)	60-66	toll like receptor 2	Homo sapiens	33-37
19179444-9	2009	Collectively, nelfinavir uncovers a postreceptor mechanism for insulin resistance, caused by interference with the sensing of PIP(3) by PKB/Akt, leading to impaired GLUT4 translocation and membrane fusion.	pip(3)	126-132	insulin	Homo sapiens	63-70
19179444-9	2009	Collectively, nelfinavir uncovers a postreceptor mechanism for insulin resistance, caused by interference with the sensing of PIP(3) by PKB/Akt, leading to impaired GLUT4 translocation and membrane fusion.	pip(3)	126-132	solute carrier family 2 member 4	Homo sapiens	165-170
19454716-2	2009	PIP(3) is produced by PI3K and regulated by PTEN (phosphatase and tensin homolog deleted on chromosome 10) and SHIP lipid phosphatases.	pip(3)	0-6	phosphatase and tensin homolog	Mus musculus	44-48
19360094-5	2009	Their F1 parents, like weaker age-1 mutants, are far less robust-implying that maternally contributed trace amounts of PI3K activity or of PIP(3) block the extreme age-1 phenotypes.	pip(3)	139-145	Phosphatidylinositol 3-kinase age-1	Caenorhabditis elegans	164-169
18936099-7	2008	The deficits in PIP(3) dynamics correlated with a significant inhibition of growth factor-induced membrane recruitment of endogenous Akt and Rac activation in PKA-inhibited cells.	pip(3)	16-22	AKT serine/threonine kinase 1	Homo sapiens	141-144
18728784-8	2008	Thus, the increase in PIP(3) concentration at the leading edge is generated by positive feedback with an AND gate logic with a PI3K-Rac-actin polymerization pathway as a first input and a PI3K initiated non-Rac pathway as a second input.	pip(3)	22-28	AKT serine/threonine kinase 1	Homo sapiens	132-135
18728784-8	2008	Thus, the increase in PIP(3) concentration at the leading edge is generated by positive feedback with an AND gate logic with a PI3K-Rac-actin polymerization pathway as a first input and a PI3K initiated non-Rac pathway as a second input.	pip(3)	22-28	AKT serine/threonine kinase 1	Homo sapiens	207-210
17623817-3	2007	RESEARCH DESIGN AND METHODS: We evaluated the expression and activity of PTEN, the phosphatase converting PIP(3) to inactive phosphatidylinositol 4,5-bisphosphate, and studied how PTEN influences muscle protein in diabetic wild-type mice and in mice with partial deficiency of PTEN(+/-).	pip(3)	106-112	phosphatase and tensin homolog	Mus musculus	73-77
18579679-10	2008	Based on our results, we propose that sdf1-expressing mesodermal cells, which overlie the endodermal layer, guide the cxcr4a-expressing endodermal cells to the dorsal side of the embryo during gastrulation, possibly through a PIP(3)-independent pathway.	pip(3)	226-232	chemokine (C-X-C motif) ligand 12a (stromal cell-derived factor 1)	Danio rerio	38-42
18579679-10	2008	Based on our results, we propose that sdf1-expressing mesodermal cells, which overlie the endodermal layer, guide the cxcr4a-expressing endodermal cells to the dorsal side of the embryo during gastrulation, possibly through a PIP(3)-independent pathway.	pip(3)	226-232	chemokine (C-X-C motif) receptor 4a	Danio rerio	118-124
18025104-6	2008	Therefore, Ras/ERK1-2 depends on PI3K only when PIP(3) is required to recruit Gab1/Shp2, which occurs only under weak EGFR mobilization.	pip(3)	48-54	mitogen-activated protein kinase 3	Homo sapiens	15-21
18025104-6	2008	Therefore, Ras/ERK1-2 depends on PI3K only when PIP(3) is required to recruit Gab1/Shp2, which occurs only under weak EGFR mobilization.	pip(3)	48-54	GRB2 associated binding protein 1	Homo sapiens	78-82
18025104-6	2008	Therefore, Ras/ERK1-2 depends on PI3K only when PIP(3) is required to recruit Gab1/Shp2, which occurs only under weak EGFR mobilization.	pip(3)	48-54	protein tyrosine phosphatase non-receptor type 11	Homo sapiens	83-87
18236401-3	2008	Cultured SWAP-70(-/-) immature bone marrow mast cells (BMMC) are also impaired in FcepsilonRI-mediated degranulation, which can be restored by expression of exogenous wild-type SWAP-70, but less so if a phosphatidylinositol trisphosphate (PIP(3)) binding mutant is expressed.	pip(3)	239-245	SWA-70 protein	Mus musculus	9-16
18236401-4	2008	SWAP-70 itself supports inositol-3-phosphate and PIP(3) production, the latter indicating a potential feedback from SWAP-70 towards PI3K.	pip(3)	49-55	SWA-70 protein	Mus musculus	0-7
17880912-4	2007	It is known that p-FAK is a substrate of PTEN and p-Akt can be regulated by PTEN via PIP(3).	pip(3)	85-91	protein tyrosine kinase 2	Homo sapiens	19-22
17880912-4	2007	It is known that p-FAK is a substrate of PTEN and p-Akt can be regulated by PTEN via PIP(3).	pip(3)	85-91	phosphatase and tensin homolog	Homo sapiens	41-45
17880912-4	2007	It is known that p-FAK is a substrate of PTEN and p-Akt can be regulated by PTEN via PIP(3).	pip(3)	85-91	phosphatase and tensin homolog	Homo sapiens	76-80
17761400-3	2007	Over-expression of PTEN inhibited EGF-induced chemotaxis, probably due to an overall reduction of PIP(3) levels.	pip(3)	98-104	phosphatase and tensin homolog	Homo sapiens	19-23
17761400-3	2007	Over-expression of PTEN inhibited EGF-induced chemotaxis, probably due to an overall reduction of PIP(3) levels.	pip(3)	98-104	epidermal growth factor	Homo sapiens	34-37
17098372-6	2007	By increasing PIP(3) availability the adipokine amplifies the magnitude as well as duration of factors acting via the IRS-2-PI(3)K-Akt pathway.	pip(3)	14-20	insulin receptor substrate 2	Cricetulus griseus	118-123
17317623-6	2007	We found that PIP(3) binding disrupted the association of calmodulin (CaM) with TRPC6.	pip(3)	14-20	transient receptor potential cation channel subfamily C member 6	Homo sapiens	80-85
17317623-7	2007	We identified the PIP(3)-binding site and found that mutations that increased or decreased the affinity of the PIP(3)/TRPC6 interaction enhanced or reduced the TRPC6-dependent current, respectively.	pip(3)	18-24	transient receptor potential cation channel subfamily C member 6	Homo sapiens	118-123
17317623-7	2007	We identified the PIP(3)-binding site and found that mutations that increased or decreased the affinity of the PIP(3)/TRPC6 interaction enhanced or reduced the TRPC6-dependent current, respectively.	pip(3)	18-24	transient receptor potential cation channel subfamily C member 6	Homo sapiens	160-165
17317623-7	2007	We identified the PIP(3)-binding site and found that mutations that increased or decreased the affinity of the PIP(3)/TRPC6 interaction enhanced or reduced the TRPC6-dependent current, respectively.	pip(3)	111-117	transient receptor potential cation channel subfamily C member 6	Homo sapiens	118-123
17317623-7	2007	We identified the PIP(3)-binding site and found that mutations that increased or decreased the affinity of the PIP(3)/TRPC6 interaction enhanced or reduced the TRPC6-dependent current, respectively.	pip(3)	111-117	transient receptor potential cation channel subfamily C member 6	Homo sapiens	160-165
17535963-2	2007	To further explore the mechanism, we visualized PIP(3), phosphatidylinositol (3,4) bisphosphate, and Rac1/Cdc42 activities by fluorescence resonance energy transfer (FRET) imaging in NGF-stimulated PC12 cells.	pip(3)	48-54	nerve growth factor	Rattus norvegicus	183-186
17535963-3	2007	Based on the obtained FRET images, and with the help of in silico kinetic reaction model, we predicted that PI-5-phosphatase negatively regulates PIP(3) upon NGF stimulation.	pip(3)	146-152	nerve growth factor	Rattus norvegicus	158-161
17535963-4	2007	In agreement with this model, depletion of Src homology 2 domain-containing inositol polyphosphate 5-phosphatase 2 (SHIP2) markedly potentiated NGF-induced Rac1/Cdc42 activation and PIP(3) accumulation and considerably increased the number and the length of neurites in phosphate and tensin homologue-depleted PC12 cells.	pip(3)	182-188	inositol polyphosphate phosphatase-like 1	Rattus norvegicus	116-121
17535963-4	2007	In agreement with this model, depletion of Src homology 2 domain-containing inositol polyphosphate 5-phosphatase 2 (SHIP2) markedly potentiated NGF-induced Rac1/Cdc42 activation and PIP(3) accumulation and considerably increased the number and the length of neurites in phosphate and tensin homologue-depleted PC12 cells.	pip(3)	182-188	nerve growth factor	Rattus norvegicus	144-147
17535963-6	2007	We propose that the SHIP2-mediated negative feedback on PIP(3) coordinately works with the PI3-kinase-mediated positive feedback to form an initial protrusive pattern and, later, to punctuate the PIP(3) accumulation to maintain proper neurite outgrowth.	pip(3)	56-62	inositol polyphosphate phosphatase-like 1	Rattus norvegicus	20-25
17535963-6	2007	We propose that the SHIP2-mediated negative feedback on PIP(3) coordinately works with the PI3-kinase-mediated positive feedback to form an initial protrusive pattern and, later, to punctuate the PIP(3) accumulation to maintain proper neurite outgrowth.	pip(3)	196-202	inositol polyphosphate phosphatase-like 1	Rattus norvegicus	20-25
17371230-2	2007	The major substrate of PTEN is PIP(3) (phosphatidylinositol 3,4,5-trisphosphate) generated by the action of PI3Ks (phosphoinositide 3-kinases).	pip(3)	31-37	phosphatase and tensin homolog	Mus musculus	23-27
17371237-3	2007	Recruitment of the p85-p110 complex to receptors and adaptor proteins via the p85 SH2 (Src homology 2) domains alleviates this inhibition, leading to PI3K activation and production of PIP(3) (phosphatidylinositol 3,4,5-trisphosphate).	pip(3)	184-190	extracellular matrix protein 1	Mus musculus	19-22
17371237-3	2007	Recruitment of the p85-p110 complex to receptors and adaptor proteins via the p85 SH2 (Src homology 2) domains alleviates this inhibition, leading to PI3K activation and production of PIP(3) (phosphatidylinositol 3,4,5-trisphosphate).	pip(3)	184-190	phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit alpha	Mus musculus	23-27
17371237-3	2007	Recruitment of the p85-p110 complex to receptors and adaptor proteins via the p85 SH2 (Src homology 2) domains alleviates this inhibition, leading to PI3K activation and production of PIP(3) (phosphatidylinositol 3,4,5-trisphosphate).	pip(3)	184-190	extracellular matrix protein 1	Mus musculus	78-81
16179727-2	2005	Insulin regulates glucose transport by activating insulin receptor substrate-1 (IRS-1)-dependent phosphatidylinositol 3-kinase (PI3K) which, via increases in PI-3,4,5-triphosphate (PIP(3)), activates atypical protein kinase C (aPKC) and protein kinase B (PKB/Akt).	pip(3)	181-187	insulin	Homo sapiens	0-7
16971513-8	2006	Collectively, these results suggest that PICT-1 plays a role in PIP(3) signals through controlling PTEN protein stability and the impairment in the PICT-1-PTEN regulatory unit may become a causative factor in human tumor(s).	pip(3)	64-70	NOP53 ribosome biogenesis factor	Homo sapiens	41-47
16971513-8	2006	Collectively, these results suggest that PICT-1 plays a role in PIP(3) signals through controlling PTEN protein stability and the impairment in the PICT-1-PTEN regulatory unit may become a causative factor in human tumor(s).	pip(3)	64-70	phosphatase and tensin homolog	Homo sapiens	99-103
16971513-8	2006	Collectively, these results suggest that PICT-1 plays a role in PIP(3) signals through controlling PTEN protein stability and the impairment in the PICT-1-PTEN regulatory unit may become a causative factor in human tumor(s).	pip(3)	64-70	phosphatase and tensin homolog	Homo sapiens	155-159
16849598-9	2006	This implies that the signaling pathway from DAF-2 affecting this learning paradigm branches between PIP(3) production and DAF-16.	pip(3)	101-107	Insulin-like receptor subunit beta;Protein kinase domain-containing protein;Receptor protein-tyrosine kinase	Caenorhabditis elegans	45-50
16193492-3	2005	By dephosphorylating PIP(3), PTEN normally acts to inhibit the PI3-Kinase/AKT pathway.	pip(3)	21-27	phosphatase and tensin homolog B	Danio rerio	29-33
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	phosphatidylinositol-3,4,5-trisphosphate-dependent Rac exchange factor 1	Mus musculus	23-29
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
16601296-7	2006	The PIP(3) binding site in ENaC involved in this regulation is localized to the proximal region of the COOH terminus of gamma-ENaC just following the second transmembrane domain.	pip(3)	4-10	sodium channel epithelial 1 subunit gamma	Homo sapiens	120-130
16601296-8	2006	In complementary pathways, PIP(3) also impacts ENaC membrane levels through both direct actions on the channel and via a signaling cascade involving phosphoinositide 3-OH kinase (PI3-K) and the aldosterone-induced gene product serum and glucocorticoid-inducible kinase.	pip(3)	27-33	phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit gamma	Homo sapiens	149-177
16301320-5	2006	Phosphorylation of P-Rex1 with protein kinase A (PKA) inhibits the PIP(3)- and Gbetagamma-stimulated P-Rex1 guanine nucleotide exchange activity on Rac.	pip(3)	67-73	phosphatidylinositol-3,4,5-trisphosphate dependent Rac exchange factor 1	Homo sapiens	19-25
16301320-5	2006	Phosphorylation of P-Rex1 with protein kinase A (PKA) inhibits the PIP(3)- and Gbetagamma-stimulated P-Rex1 guanine nucleotide exchange activity on Rac.	pip(3)	67-73	phosphatidylinositol-3,4,5-trisphosphate dependent Rac exchange factor 1	Homo sapiens	101-107
16301320-5	2006	Phosphorylation of P-Rex1 with protein kinase A (PKA) inhibits the PIP(3)- and Gbetagamma-stimulated P-Rex1 guanine nucleotide exchange activity on Rac.	pip(3)	67-73	AKT serine/threonine kinase 1	Homo sapiens	148-151
16179727-2	2005	Insulin regulates glucose transport by activating insulin receptor substrate-1 (IRS-1)-dependent phosphatidylinositol 3-kinase (PI3K) which, via increases in PI-3,4,5-triphosphate (PIP(3)), activates atypical protein kinase C (aPKC) and protein kinase B (PKB/Akt).	pip(3)	181-187	insulin receptor substrate 1	Homo sapiens	50-78
16179727-2	2005	Insulin regulates glucose transport by activating insulin receptor substrate-1 (IRS-1)-dependent phosphatidylinositol 3-kinase (PI3K) which, via increases in PI-3,4,5-triphosphate (PIP(3)), activates atypical protein kinase C (aPKC) and protein kinase B (PKB/Akt).	pip(3)	181-187	insulin receptor substrate 1	Homo sapiens	80-85
16179727-2	2005	Insulin regulates glucose transport by activating insulin receptor substrate-1 (IRS-1)-dependent phosphatidylinositol 3-kinase (PI3K) which, via increases in PI-3,4,5-triphosphate (PIP(3)), activates atypical protein kinase C (aPKC) and protein kinase B (PKB/Akt).	pip(3)	181-187	phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit delta	Homo sapiens	97-126
16179727-2	2005	Insulin regulates glucose transport by activating insulin receptor substrate-1 (IRS-1)-dependent phosphatidylinositol 3-kinase (PI3K) which, via increases in PI-3,4,5-triphosphate (PIP(3)), activates atypical protein kinase C (aPKC) and protein kinase B (PKB/Akt).	pip(3)	181-187	AKT serine/threonine kinase 1	Homo sapiens	255-258
16179727-2	2005	Insulin regulates glucose transport by activating insulin receptor substrate-1 (IRS-1)-dependent phosphatidylinositol 3-kinase (PI3K) which, via increases in PI-3,4,5-triphosphate (PIP(3)), activates atypical protein kinase C (aPKC) and protein kinase B (PKB/Akt).	pip(3)	181-187	AKT serine/threonine kinase 1	Homo sapiens	259-262
16179727-4	2005	In most cases, defective muscle aPKC/PKB activation reflects both impaired activation of IRS-1/PI3K, the upstream activator of aPKC and PKB in muscle and, in the case of aPKC, poor responsiveness to PIP(3), the lipid product of PI3K.	pip(3)	199-205	AKT serine/threonine kinase 1	Homo sapiens	37-40
16179727-4	2005	In most cases, defective muscle aPKC/PKB activation reflects both impaired activation of IRS-1/PI3K, the upstream activator of aPKC and PKB in muscle and, in the case of aPKC, poor responsiveness to PIP(3), the lipid product of PI3K.	pip(3)	199-205	insulin receptor substrate 1	Homo sapiens	89-94