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Statements

databases
phosphosite cbn pc11 biopax bel_lc signor biogrid tas lincs_drug hprd trrust | geneways tees isi trips rlimsp medscan sparser reach
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AKT1 phosphorylates TSC2. 8 / 21
| 2 7 9
reach
"Phosphorylation of TSC2 by Akt1 inhibits its GTPase activity leading to increased GTP loading on Rheb and consequent increase in mTORC1 activity."
reach
"Activated AKT1 modulates MTORC1 signaling in different ways : On the one hand, several studies indicate that AKT1 is able to phosphorylate TSC2 and thereby activate the TSC1/2 complex [XREF_BIBR]."
rlimsp
"Moreover, Akt/PKB can phosphorylate tuberin in vitro and in vivo."
sparser
"TORC1 is activated by an Akt1-dependent derepression mechanism: Through phosphorylation of the (TORC1) negative regulator Tsc2 by Akt1, the GTPase Ras homolog enriched in brain (Rheb) and consequently TORC1 are activated. xref TORC1 activity is central to the control of growth and metabolism, acting as a nutrient sensor for growth regulation. xref Hence, Akt1 serves as a link between InR and TOR pathways."
sparser
"Phosphorylation of TSC2 by Akt1 inhibits its GTPase activity leading to increased GTP loading on Rheb and consequent increase in mTORC1 activity (see reviews xref – xref and references therein)."
reach
"Active AMPK positively regulates the activity of the TSC1 and TSC2 complex by phosphorylating the TSC2 protein (resulting in the opposite activity to the AKT-1 phosphorylation of TSC2), which then turns off the RHEB G protein and reduces TOR activity [XREF_BIBR]."
reach
"Upon insulin stimulation, PI3K activates protein kinase B (Akt and PKB), which then directly phosphorylates TSC2 resulting in the dissociation of the TSC1/2 complex from lysosomes where mTORC1 activation takes place 2."
sparser
"This is accomplished by AKT-1 phosphorylation and inactivation of TSC2 [ xref - xref ], which forms a TSC1–TSC2 protein complex that is a GAP for the RHEB G-protein."
AKT1 phosphorylates TSC2 on S939. 10 / 10
1 1 8 |
biopax:phosphositeplus
No evidence text available
signor
"We demonstrate that, upon activation of PI3K, tuberin is phosphorylated on consensus recognition sites for PI3K-dependent S/T kinases. Moreover, Akt/PKB can phosphorylate tuberin in vitro and in vivo. We also show that S939 and T1462 of tuberin are PI3K-regulated phosphorylation sites and that T1462 is constitutively phosphorylated in PTEN(-/-) tumor-derived cell lines."
hprd
No evidence text available
hprd
No evidence text available
hprd
No evidence text available
hprd
No evidence text available
hprd
No evidence text available
hprd
No evidence text available
hprd
No evidence text available
hprd
No evidence text available
AKT1 phosphorylates TSC2 on T1462. 5 / 5
1 1 3 |
biopax:phosphositeplus
No evidence text available
hprd
No evidence text available
signor
"We demonstrate that, upon activation of PI3K, tuberin is phosphorylated on consensus recognition sites for PI3K-dependent S/T kinases. Moreover, Akt/PKB can phosphorylate tuberin in vitro and in vivo. We also show that S939 and T1462 of tuberin are PI3K-regulated phosphorylation sites and that T1462 is constitutively phosphorylated in PTEN(-/-) tumor-derived cell lines."
hprd
No evidence text available
hprd
No evidence text available
Kinase-active AKT1 phosphorylates TSC2 on T1462. 4 / 4
2 2 |
bel
"Figure 4. S939 and T1462 Are the Major PI3K-Dependent Phosphorylation Sites on Tuberin"
bel
"Akt then phosphorylates tuberin on three residues (S939, S1130 and T1462 of full length human tuberin), and this inhibits the tuberin-hamartin complex through an as-yet-undefined mechanism (reviewed in [8])."
bel
"Figure 4. S939 and T1462 Are the Major PI3K-Dependent Phosphorylation Sites on Tuberin"
bel
"Akt then phosphorylates tuberin on three residues (S939, S1130 and T1462 of full length human tuberin), and this inhibits the tuberin-hamartin complex through an as-yet-undefined mechanism (reviewed in [8])."
AKT1 phosphorylated on T308 phosphorylates TSC2 on T1462. 3 / 3
3 |
biopax:pid
No evidence text available
biopax:pid
No evidence text available
biopax:pid
No evidence text available
Kinase-active AKT1 phosphorylates TSC2 on S939. 3 / 3
3 |
bel
"These data demonstrate that Ser 939, Ser 1086/Ser 1088 and Thr 1422 are required for proper in vivo phosphorylation of TSC2 and suggest that they are the Akt-dependent phosphorylation sites."
bel
"Akt then phosphorylates tuberin on three residues (S939, S1130 and T1462 of full length human tuberin), and this inhibits the tuberin-hamartin complex through an as-yet-undefined mechanism (reviewed in [8])."
bel
"Figure 4. S939 and T1462 Are the Major PI3K-Dependent Phosphorylation Sites on Tuberin"
AKT1 phosphorylated on T308 phosphorylates TSC2 on S939. 3 / 3
3 |
biopax:pid
No evidence text available
biopax:pid
No evidence text available
biopax:pid
No evidence text available
AKT1 phosphorylates TSC2 at position 1462. 2 / 2
2 |
biopax:inoh
No evidence text available
biopax:inoh
No evidence text available
AKT1 phosphorylates TSC2 at position 1132. 2 / 2
2 |
biopax:inoh
No evidence text available
biopax:inoh
No evidence text available
AKT1 phosphorylates TSC2 at position 939. 2 / 2
2 |
biopax:inoh
No evidence text available
biopax:inoh
No evidence text available
AKT1 phosphorylated on S473 and T308 phosphorylates TSC2 on S939. 2 / 2
2 |
biopax:reactome
No evidence text available
biopax:reactome
No evidence text available
AKT1 phosphorylates TSC2 at position 1130. 2 / 2
2 |
biopax:inoh
No evidence text available
biopax:inoh
No evidence text available
AKT1 phosphorylated on S473 and T308 phosphorylates TSC2 on T1462. 2 / 2
2 |
biopax:reactome
No evidence text available
biopax:reactome
No evidence text available
AKT1 phosphorylates TSC2 at position 981. 2 / 2
2 |
biopax:inoh
No evidence text available
biopax:inoh
No evidence text available
AKT1 phosphorylates TSC2 on S981. 1 / 1
1 |
biopax:phosphositeplus
No evidence text available
Kinase-active AKT1 phosphorylates TSC2 on S1130. 1 / 1
1 |
bel
"Akt then phosphorylates tuberin on three residues (S939, S1130 and T1462 of full length human tuberin), and this inhibits the tuberin-hamartin complex through an as-yet-undefined mechanism (reviewed in [8])."