| + |
SGK1 | down-regulates activity 
phosphorylation
|
TSC2 |
0.597 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277266 |
Ser1130 |
GARDRVRsMSGGHGL |
in vitro |
|
| pmid |
sentence |
| 27451907 |
SGK1, which is activated by PDK1, contributes to the maintenance of residual mTORC1 activity through direct phosphorylation and inhibition of TSC2. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277265 |
Ser1132 |
RDRVRSMsGGHGLRV |
in vitro |
|
| pmid |
sentence |
| 27451907 |
SGK1, which is activated by PDK1, contributes to the maintenance of residual mTORC1 activity through direct phosphorylation and inhibition of TSC2. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
CyclinD1/CDK6 | up-regulates activity 
phosphorylation
|
TSC2 |
0.415 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274101 |
Ser1217 |
MSLENPLsPFSSDIN |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 32294430 |
We show here that CyclinD-Cdk4/6 activates mTORC1 by binding and phosphorylating TSC2 on Ser1217 and Ser1452. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274102 |
Ser1452 |
LPSSSPRsPSGLRPR |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 32294430 |
We show here that CyclinD-Cdk4/6 activates mTORC1 by binding and phosphorylating TSC2 on Ser1217 and Ser1452. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
CyclinD/CDK4 | up-regulates activity
phosphorylation
|
TSC2 |
0.481 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274099 |
Ser1217 |
MSLENPLsPFSSDIN |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 32294430 |
We show here that CyclinD-Cdk4/6 activates mTORC1 by binding and phosphorylating TSC2 on Ser1217 and Ser1452. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274100 |
Ser1452 |
LPSSSPRsPSGLRPR |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 32294430 |
We show here that CyclinD-Cdk4/6 activates mTORC1 by binding and phosphorylating TSC2 on Ser1217 and Ser1452. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
MAPKAPK2 |
phosphorylation
|
TSC2 |
0.645 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-98201 |
Ser1254 |
TALYKSLsVPAASTA |
Homo sapiens |
|
| pmid |
sentence |
| 12582162 |
Both in vitro and in vivo experiments demonstrate that the p38-activated kinase mk2 (also known as mapkapk2) is directly responsible for the phosphorylation of ser(1210). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AMPK | up-regulates
phosphorylation
|
TSC2 |
0.516 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-216438 |
Ser1387 |
QPLSKSSsSPELQTL |
Homo sapiens |
|
| pmid |
sentence |
| 16959574 |
We have observed that ampk directly phosphorylates tsc2, and the ampk-dependent phosphorylation of tsc2 is critical for the coordination between cell growth and cellular energy levels. Phosphorylation of tsc2 by ampk is required for translation regulation and cell size control in response to energy deprivation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKAA2 | up-regulates
phosphorylation
|
TSC2 |
0.56 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-149388 |
Ser1387 |
QPLSKSSsSPELQTL |
Homo sapiens |
|
| pmid |
sentence |
| 16959574 |
We have observed that ampk directly phosphorylates tsc2, and the ampk-dependent phosphorylation of tsc2 is critical for the coordination between cell growth and cellular energy levels. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RPS6K | down-regulates
phosphorylation
|
TSC2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252801 |
Ser1798 |
GQRKRLIsSVEDFTE |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 15342917 |
The mitogen-activated protein kinase (mapk)-activated kinase, p90 ribosomal s6 kinase (rsk) 1, was found to interact with and phosphorylate tuberin at a regulatory site, ser-1798, located at the evolutionarily conserved c terminus of tuberin. Rsk1 phosphorylation of ser-1798 inhibits the tumor suppressor function of the tuberin/hamartin complex, resulting in increased mtor signaling to s6k1 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RPS6KA1 | down-regulates
phosphorylation
|
TSC2 |
0.76 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-128634 |
Ser1798 |
GQRKRLIsSVEDFTE |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 15342917 |
The mitogen-activated protein kinase (mapk)-activated kinase, p90 ribosomal s6 kinase (rsk) 1, was found to interact with and phosphorylate tuberin at a regulatory site, ser-1798, located at the evolutionarily conserved c terminus of tuberin. Rsk1 phosphorylation of ser-1798 inhibits the tumor suppressor function of the tuberin/hamartin complex, resulting in increased mtor signaling to s6k1 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MAPK3 | down-regulates activity
phosphorylation
|
TSC2 |
0.682 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249458 |
Ser540 |
KVMARSLsPPPELEE |
Mus musculus |
|
| pmid |
sentence |
| 15851026 |
Here, we show that Erk may play a critical role in TSC progression through posttranslational inactivation of TSC2. Erk-dependent phosphorylation leads to TSC1-TSC2 dissociation and markedly impairs TSC2 ability to inhibit mTOR signaling, cell proliferation, and oncogenic transformation. |Serine to alanine substitution at S664 or double S664A/S540A mutagenesis resulted in a marked reduction in TSC2 phosphorylation to a similar extent. In contrast, S540A substitution only moderately impaired TSC2 phosphorylation (Figure 3D), corroborating the notion that in vivo S664 is the most relevant residue for Erk-mediated phosphorylation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249457 |
Ser664 |
KKTSGPLsPPTGPPG |
Mus musculus |
NIH-3T3 Cell |
| pmid |
sentence |
| 15851026 |
Here, we show that Erk may play a critical role in TSC progression through posttranslational inactivation of TSC2. Erk-dependent phosphorylation leads to TSC1-TSC2 dissociation and markedly impairs TSC2 ability to inhibit mTOR signaling, cell proliferation, and oncogenic transformation. |Serine to alanine substitution at S664 or double S664A/S540A mutagenesis resulted in a marked reduction in TSC2 phosphorylation to a similar extent. In contrast, S540A substitution only moderately impaired TSC2 phosphorylation (Figure 3D), corroborating the notion that in vivo S664 is the most relevant residue for Erk-mediated phosphorylation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-183695 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19188143 |
Phosphorylation of tsc2 (by akt and erk;refs. 28, 29) and tsc1(by ikkbeta;ref. 30) results in the disruption of the tsc1/2 complex, and thereby activates the oncogenic mtor signaling contributing to tumor progression |
|
| Publications: |
3 |
Organism: |
Mus Musculus, Homo Sapiens |
| + |
ERK1/2 | down-regulates activity
phosphorylation
|
TSC2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249455 |
Ser540 |
KVMARSLsPPPELEE |
Mus musculus |
NIH-3T3 Cell |
| pmid |
sentence |
| 15851026 |
Here, we show that Erk may play a critical role in TSC progression through posttranslational inactivation of TSC2. Erk-dependent phosphorylation leads to TSC1-TSC2 dissociation and markedly impairs TSC2 ability to inhibit mTOR signaling, cell proliferation, and oncogenic transformation. |Serine to alanine substitution at S664 or double S664A/S540A mutagenesis resulted in a marked reduction in TSC2 phosphorylation to a similar extent. In contrast, S540A substitution only moderately impaired TSC2 phosphorylation (Figure 3D), corroborating the notion that in vivo S664 is the most relevant residue for Erk-mediated phosphorylation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-244602 |
|
|
Homo sapiens |
Breast Cancer Cell, Prostate Gland Cancer Cell, Leukemia Cell, Glioblastoma Cell |
| pmid |
sentence |
| 19188143 |
Phosphorylation of tsc2 (by akt and erk;refs. 28, 29) and tsc1(by ikkbeta;ref. 30) results in the disruption of the tsc1/2 complex, and thereby activates the oncogenic mtor signaling contributing to tumor progression |
|
| Publications: |
2 |
Organism: |
Mus Musculus, Homo Sapiens |
| + |
MAPK1 | down-regulates activity
phosphorylation
|
TSC2 |
0.668 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249454 |
Ser540 |
KVMARSLsPPPELEE |
Mus musculus |
NIH-3T3 Cell |
| pmid |
sentence |
| 15851026 |
Here, we show that Erk may play a critical role in TSC progression through posttranslational inactivation of TSC2. Erk-dependent phosphorylation leads to TSC1-TSC2 dissociation and markedly impairs TSC2 ability to inhibit mTOR signaling, cell proliferation, and oncogenic transformation. |Serine to alanine substitution at S664 or double S664A/S540A mutagenesis resulted in a marked reduction in TSC2 phosphorylation to a similar extent. In contrast, S540A substitution only moderately impaired TSC2 phosphorylation (Figure 3D), corroborating the notion that in vivo S664 is the most relevant residue for Erk-mediated phosphorylation. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
MAPK1 | down-regulates
phosphorylation
|
TSC2 |
0.668 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-135696 |
Ser664 |
KKTSGPLsPPTGPPG |
Homo sapiens |
|
| pmid |
sentence |
| 15851026 |
Here, we show that erk may play a critical role in tsc progression through posttranslational inactivation of tsc2. s664 is the primary erk phosphorylation site on tsc2 in vitro and in vivo |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ERK1/2 | down-regulates
phosphorylation
|
TSC2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-244765 |
Ser664 |
KKTSGPLsPPTGPPG |
Homo sapiens |
|
| pmid |
sentence |
| 15851026 |
Here, we show that erk may play a critical role in tsc progression through posttranslational inactivation of tsc2. s664 is the primary erk phosphorylation site on tsc2 in vitro and in vivo |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCD | down-regulates activity
phosphorylation
|
TSC2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277426 |
Ser932 |
DDTPEKDsFRARSTS |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 30684133 |
In vivo kinase analysis further indicated that both S932 and S939 are phosphorylated in response to translation inhibitors. Finally, phosphorylation defective TSC2 mutants (S932A and S939A single mutants and a S932A/S939A double mutant) failed to upregulate mTORC1 activity in the presence of translation inhibitors, suggesting that activation of mTORC1 by translation inhibitors is mediated by PKC-δ phosphorylation of TSC2 at S932/S939, which inactivates TSC. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277427 |
Ser939 |
SFRARSTsLNERPKS |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 30684133 |
In vivo kinase analysis further indicated that both S932 and S939 are phosphorylated in response to translation inhibitors. Finally, phosphorylation defective TSC2 mutants (S932A and S939A single mutants and a S932A/S939A double mutant) failed to upregulate mTORC1 activity in the presence of translation inhibitors, suggesting that activation of mTORC1 by translation inhibitors is mediated by PKC-δ phosphorylation of TSC2 at S932/S939, which inactivates TSC. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
AKT2 | down-regulates
phosphorylation
|
TSC2 |
0.719 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-91041 |
Ser939 |
SFRARSTsLNERPKS |
Homo sapiens |
|
| pmid |
sentence |
| 12150915 |
We demonstrate here that tuberin is phosphorylated on s939 and t1462 in response to pi3k activation. Our results are consistent with akt being the pi3k-depen-dent tuberin kinase. The pi3k-akt-mediated phosphorylation of tuberin would inhibit the function of the tuberin-hamartin complex. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-91388 |
Ser939 |
SFRARSTsLNERPKS |
Homo sapiens |
|
| pmid |
sentence |
| 12172553 |
We demonstrate here that tuberin is phosphorylated on s939 and t1462 in response to pi3k activation. Our results are consistent with akt being the pi3k-depen-dent tuberin kinase. The pi3k-akt-mediated phosphorylation of tuberin would inhibit the function of the tuberin-hamartin complex. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-183636 |
Ser939 |
SFRARSTsLNERPKS |
Homo sapiens |
Breast Cancer Cell, Prostate Gland Cancer Cell, Leukemia Cell, Glioblastoma Cell |
| pmid |
sentence |
| 19188143 |
We demonstrate here that tuberin is phosphorylated on s939 and t1462 in response to pi3k activation. Our results are consistent with akt being the pi3k-depen-dent tuberin kinase. The pi3k-akt-mediated phosphorylation of tuberin would inhibit the function of the tuberin-hamartin complex. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-183640 |
Thr1462 |
GLRPRGYtISDSAPS |
Homo sapiens |
Breast Cancer Cell, Prostate Gland Cancer Cell, Leukemia Cell, Glioblastoma Cell |
| pmid |
sentence |
| 19188143 |
We demonstrate here that tuberin is phosphorylated on s939 and t1462 in response to pi3k activation. Our results are consistent with akt being the pi3k-depen-dent tuberin kinase. The pi3k-akt-mediated phosphorylation of tuberin would inhibit the function of the tuberin-hamartin complex. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-91392 |
Thr1462 |
GLRPRGYtISDSAPS |
Homo sapiens |
|
| pmid |
sentence |
| 12172553 |
We demonstrate here that tuberin is phosphorylated on s939 and t1462 in response to pi3k activation. Our results are consistent with akt being the pi3k-depen-dent tuberin kinase. The pi3k-akt-mediated phosphorylation of tuberin would inhibit the function of the tuberin-hamartin complex. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-91045 |
Thr1462 |
GLRPRGYtISDSAPS |
Homo sapiens |
|
| pmid |
sentence |
| 12150915 |
We demonstrate here that tuberin is phosphorylated on s939 and t1462 in response to pi3k activation. Our results are consistent with akt being the pi3k-depen-dent tuberin kinase. The pi3k-akt-mediated phosphorylation of tuberin would inhibit the function of the tuberin-hamartin complex. |
|
| Publications: |
6 |
Organism: |
Homo Sapiens |
| + |
AKT | down-regulates activity
phosphorylation
|
TSC2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-244369 |
Ser939 |
SFRARSTsLNERPKS |
Mus musculus |
NIH-3T3 Cell |
| pmid |
sentence |
| 12150915 |
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. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-244365 |
Thr1462 |
GLRPRGYtISDSAPS |
Mus musculus |
NIH-3T3 Cell |
| pmid |
sentence |
| 12150915 |
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. |
|
| Publications: |
2 |
Organism: |
Mus Musculus |
| + |
AKT1 | down-regulates activity
phosphorylation
|
TSC2 |
0.811 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-235511 |
Ser939 |
SFRARSTsLNERPKS |
Mus musculus |
NIH-3T3 Cell |
| pmid |
sentence |
| 12150915 |
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. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-235515 |
Thr1462 |
GLRPRGYtISDSAPS |
Mus musculus |
NIH-3T3 Cell |
| pmid |
sentence |
| 12150915 |
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. |
|
| Publications: |
2 |
Organism: |
Mus Musculus |
| + |
DDIT4 | up-regulates activity
binding
|
TSC2 |
0.626 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277469 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21460850 |
Redd1 is a negative regulator of mTOR, mediating dissociation of 14-3-3 from tuberous sclerosis complex (TSC)2, which allows formation of a TSC-TSC2 complex. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
GSK3A | up-regulates
phosphorylation
|
TSC2 |
0.37 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-164098 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20226003 |
Gsk3 inhibits the mtor pathway by phosphorylating tsc2 in a manner dependent on ampk-priming phosphorylation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-149377 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16959574 |
Gsk3 inhibits the mtor pathway by phosphorylating tsc2 in a manner dependent on ampk-priming phosphorylation. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
TSC2 | down-regulates activity 
|
MTOR |
0.844 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-93133 |
|
|
Homo sapiens |
HEK-293 Cell, U2-OS Cell |
| pmid |
sentence |
| 12271141 |
These findings strongly implicate the tuberin-hamartin tumor suppressor complex as an inhibitor of mtor |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Gbeta | down-regulates activity
phosphorylation
|
TSC2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270108 |
|
|
Mus musculus |
NIH-3T3 Cell |
| pmid |
sentence |
| 15851026 |
Here, we show that Erk may play a critical role in TSC progression through posttranslational inactivation of TSC2. Erk-dependent phosphorylation leads to TSC1-TSC2 dissociation and markedly impairs TSC2 ability to inhibit mTOR signaling, cell proliferation, and oncogenic transformation. |Serine to alanine substitution at S664 or double S664A/S540A mutagenesis resulted in a marked reduction in TSC2 phosphorylation to a similar extent. In contrast, S540A substitution only moderately impaired TSC2 phosphorylation (Figure 3D), corroborating the notion that in vivo S664 is the most relevant residue for Erk-mediated phosphorylation. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
TSC2 | down-regulates activity
gtpase-activating protein
|
RHEB |
0.92 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-128432 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15340059 |
Tsc2 functions as a gap to inhibit rheb activity. Tsc2 displays gap (gtpase-activating protein) activity specifically towards the small g protein rheb and inhibits its ability to stimulate the mtor signaling pathway. It has recently been shown that tsc2 has gtpase-activating protein (gap) activity towards the ras family small gtpase rheb (ras homolog enriched in brain), and tsc1/2 antagonizes the mtor signaling pathway via stimulation of gtp hydrolysis of rheb. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Brain |
| + |
GSK3B | up-regulates activity
phosphorylation
|
TSC2 |
0.721 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-149380 |
|
|
Rattus norvegicus |
Rat-1 Cell |
| pmid |
sentence |
| 16959574 |
Gsk3 inhibits the mtor pathway by phosphorylating tsc2 in a manner dependent on ampk-priming phosphorylation. |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
TSC2 | down-regulates
|
RPS6KB2 |
0.542 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-91395 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12172553 |
Here, we show that tsc1-tsc2 inhibits the p70 ribosomal protein s6 kinase 1 (an activator of translation) and activates the eukaryotic initiation factor 4e binding protein 1 (4e-bp1, an inhibitor of translational initiation). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TSC2 | up-regulates activity
binding
|
TSC1 |
0.933 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-77400 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10807585 |
Furthermore, tsc2 is directly phosphorylated by akt, which is involved in stimulating cell growth and is activated by growth stimulating signals, such as insulin. Tsc2 is inactivated by akt-dependent phosphorylation, which destabilizes tsc2 and disrupts its interaction with tsc1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Brain, Kidney |
| + |
UBE3A | down-regulates quantity by destabilization
ubiquitination
|
TSC2 |
0.617 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271396 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 18298802 |
An in vivo ubiquitination assay was done to reveal that E6AP promoted the ubiquitination of TSC2 independent of HPV16 E6. We further found that TSC2 bound E6AP in the presence as well as in the absence of HPV16 E6. The binding regions on E6AP and TSC2 have been identified as amino acid (aa) 260-316, aa 428-500 and aa 1-175, aa 1251-1807, respectively. Taken together, degradation of TSC2 is mediated by E6AP ubiquitin ligase. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TSC2 | form complex 
binding
|
TSC |
0.933 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-217913 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12172553 |
TSC1 and TSC2 proteins form a physical and functional complex in vivo. Here, we show that TSC1-TSC2 inhibits the p70 ribosomal protein S6 kinase 1 (an activator of translation) and activates the eukaryotic initiation factor 4E binding protein 1 (4E-BP1, an inhibitor of translational initiation). These functions of TSC1-TSC2 are mediated by inhibition of the mammalian target of rapamycin (mTOR). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CHUK | down-regulates
phosphorylation
|
TSC2 |
0.301 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-178664 |
|
|
Homo sapiens |
MCF-7 Cell |
| pmid |
sentence |
| 18490760 |
Insulin activation of mtor requires akt in a manner that involves ikkalpha, preferentially to ikkbeta, and tsc2 phosphorylation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
TSC2
- 
- 