| + |
IKBKB | down-regulates 
phosphorylation
|
TSC1 |
0.627 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-157296 |
Ser487 |
AAISRELsEITTAEA |
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 17693255 |
Here we show that ikkbeta, a major downstream kinase in the tnfalpha signaling pathway, physically interacts with and phosphorylates tsc1 at ser487 and ser511, resulting in suppression of tsc1phosphorylation 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. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-183688 |
Ser487 |
AAISRELsEITTAEA |
Homo sapiens |
Breast Cancer Cell, Prostate Gland Cancer Cell, Leukemia Cell, Glioblastoma Cell |
| pmid |
sentence |
| 19188143 |
Here we show that ikkbeta, a major downstream kinase in the tnfalpha signaling pathway, physically interacts with and phosphorylates tsc1 at ser487 and ser511, resulting in suppression of tsc1phosphorylation 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. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-183692 |
Ser511 |
DSPFYRDsLPGSQRK |
Homo sapiens |
Breast Cancer Cell, Prostate Gland Cancer Cell, Leukemia Cell, Glioblastoma Cell |
| pmid |
sentence |
| 19188143 |
Here we show that ikkbeta, a major downstream kinase in the tnfalpha signaling pathway, physically interacts with and phosphorylates tsc1 at ser487 and ser511, resulting in suppression of tsc1phosphorylation 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. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-157300 |
Ser511 |
DSPFYRDsLPGSQRK |
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 17693255 |
Here we show that ikkbeta, a major downstream kinase in the tnfalpha signaling pathway, physically interacts with and phosphorylates tsc1 at ser487 and ser511, resulting in suppression of tsc1phosphorylation 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: |
4 |
Organism: |
Homo Sapiens |
| + |
CyclinB/CDK1 | down-regulates
phosphorylation
|
TSC1 |
0.426 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-216944 |
Ser584 |
ETSIFTPsPCKIPPP |
Homo sapiens |
Kidney Cancer Cell, Brain Cancer Cell, Skin Cancer Cell |
| pmid |
sentence |
| 14551205 |
Cell cycle-regulated phosphorylation of hamartin, the product of the tuberous sclerosis complex 1 gene, by cyclin-dependent kinase 1/cyclin b.Cyclin-dependent kinase 1 phosphorylates hamartin at three sites, one of which (thr417) is in the hamartin-tuberin interaction domain. Tuberin interacts with phosphohamartin, and tuberin expression attenuates the phosphorylation of exogenous hamartin. Hamartin with alanine mutations in the three cyclin-dependent kinase 1 phosphorylation sites increased the inhibition of p70s6 kinase by the hamartin-tuberin complex |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-216949 |
Thr1047 |
SSSSELStPEKPPHQ |
Homo sapiens |
Kidney Cancer Cell, Brain Cancer Cell, Skin Cancer Cell |
| pmid |
sentence |
| 14551205 |
Cell cycle-regulated phosphorylation of hamartin, the product of the tuberous sclerosis complex 1 gene, by cyclin-dependent kinase 1/cyclin b.Cyclin-dependent kinase 1 phosphorylates hamartin at three sites, one of which (thr417) is in the hamartin-tuberin interaction domain. Tuberin interacts with phosphohamartin, and tuberin expression attenuates the phosphorylation of exogenous hamartin. Hamartin with alanine mutations in the three cyclin-dependent kinase 1 phosphorylation sites increased the inhibition of p70s6 kinase by the hamartin-tuberin complex |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-216953 |
Thr417 |
SLPQATVtPPRKEER |
Homo sapiens |
Kidney Cancer Cell, Brain Cancer Cell, Skin Cancer Cell |
| pmid |
sentence |
| 14551205 |
Cell cycle-regulated phosphorylation of hamartin, the product of the tuberous sclerosis complex 1 gene, by cyclin-dependent kinase 1/cyclin b.Cyclin-dependent kinase 1 phosphorylates hamartin at three sites, one of which (thr417) is in the hamartin-tuberin interaction domain. Tuberin interacts with phosphohamartin, and tuberin expression attenuates the phosphorylation of exogenous hamartin. Hamartin with alanine mutations in the three cyclin-dependent kinase 1 phosphorylation sites increased the inhibition of p70s6 kinase by the hamartin-tuberin complex |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
CDK1 |
phosphorylation
|
TSC1 |
0.503 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-118588 |
Ser584 |
ETSIFTPsPCKIPPP |
Homo sapiens |
|
| pmid |
sentence |
| 14551205 |
In vitro assays showed that cyclin-dependent kinase 1 phosphorylates hamartin at three sites, one of which (thr417) is in the hamartin-tuberin interaction domain. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-117339 |
Thr1047 |
SSSSELStPEKPPHQ |
Homo sapiens |
Kidney Cancer Cell, Brain Cancer Cell, Skin Cancer Cell |
| pmid |
sentence |
| 14551205 |
In vitro assays showed that cyclin-dependent kinase 1 phosphorylates hamartin at three sites, one of which (thr417) is in the hamartin-tuberin interaction domain. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-86696 |
Thr417 |
SLPQATVtPPRKEER |
Homo sapiens |
|
| pmid |
sentence |
| 14551205 |
In vitro assays showed that cyclin-dependent kinase 1 phosphorylates hamartin at three sites, one of which (thr417) is in the hamartin-tuberin interaction domain. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
CDK1 | down-regulates
phosphorylation
|
TSC1 |
0.503 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-118576 |
Ser584 |
ETSIFTPsPCKIPPP |
Homo sapiens |
Kidney Cancer Cell, Brain Cancer Cell, Skin Cancer Cell |
| pmid |
sentence |
| 14551205 |
Cell cycle-regulated phosphorylation of hamartin, the product of the tuberous sclerosis complex 1 gene, by cyclin-dependent kinase 1/cyclin b.Cyclin-dependent kinase 1 phosphorylates hamartin at three sites, one of which (thr417) is in the hamartin-tuberin interaction domain. Tuberin interacts with phosphohamartin, and tuberin expression attenuates the phosphorylation of exogenous hamartin. Hamartin with alanine mutations in the three cyclin-dependent kinase 1 phosphorylation sites increased the inhibition of p70s6 kinase by the hamartin-tuberin complex |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-118580 |
Thr1047 |
SSSSELStPEKPPHQ |
Homo sapiens |
Kidney Cancer Cell, Brain Cancer Cell, Skin Cancer Cell |
| pmid |
sentence |
| 14551205 |
Cell cycle-regulated phosphorylation of hamartin, the product of the tuberous sclerosis complex 1 gene, by cyclin-dependent kinase 1/cyclin b.Cyclin-dependent kinase 1 phosphorylates hamartin at three sites, one of which (thr417) is in the hamartin-tuberin interaction domain. Tuberin interacts with phosphohamartin, and tuberin expression attenuates the phosphorylation of exogenous hamartin. Hamartin with alanine mutations in the three cyclin-dependent kinase 1 phosphorylation sites increased the inhibition of p70s6 kinase by the hamartin-tuberin complex |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-118584 |
Thr417 |
SLPQATVtPPRKEER |
Homo sapiens |
Kidney Cancer Cell, Brain Cancer Cell, Skin Cancer Cell |
| pmid |
sentence |
| 14551205 |
Cell cycle-regulated phosphorylation of hamartin, the product of the tuberous sclerosis complex 1 gene, by cyclin-dependent kinase 1/cyclin b.Cyclin-dependent kinase 1 phosphorylates hamartin at three sites, one of which (thr417) is in the hamartin-tuberin interaction domain. Tuberin interacts with phosphohamartin, and tuberin expression attenuates the phosphorylation of exogenous hamartin. Hamartin with alanine mutations in the three cyclin-dependent kinase 1 phosphorylation sites increased the inhibition of p70s6 kinase by the hamartin-tuberin complex |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
ERK1/2 | down-regulates
phosphorylation
|
TSC1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-244761 |
|
|
Homo sapiens |
|
| 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 signalin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Insulin Signaling |
| + |
PRKAA2 | up-regulates 
phosphorylation
|
TSC1 |
0.532 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-119541 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 14651849 |
Under energy starvation conditions, the amp-activated protein kinase (ampk) phosphorylates tsc2 and enhances its activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TSC1 | form complex 
binding
|
TSC |
0.933 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-217910 |
|
|
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 |
| Pathways: | Insulin Signaling |
| + |
TSC1 | down-regulates activity
binding
|
RHEB |
0.909 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-162096 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20006481 |
Tsc1 and tsc2 proteins, which together inhibit rheb through the gap activity of tsc2. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Insulin Signaling |
| + |
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 |
| + |
MAPK1 | down-regulates
phosphorylation
|
TSC1 |
0.469 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-157162 |
|
|
Homo sapiens |
Breast Cancer Cell, Brain Cancer Cell |
| pmid |
sentence |
| 17671177 |
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 signalin. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-135692 |
|
|
Homo sapiens |
|
| 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 signalin. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
AMPK | up-regulates
phosphorylation
|
TSC1 |
0.41 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-216441 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 14651849 |
Under energy starvation conditions, the amp-activated protein kinase (ampk) phosphorylates tsc2 and enhances its activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-216487 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19584320 |
Under energy starvation conditions, the amp-activated protein kinase (ampk) phosphorylates tsc2 and enhances its activity. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
TSC1 | down-regulates activity 
|
MTOR |
0.695 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-93130 |
|
|
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. Here, we show that hamartin and tuberin function together to inhibit mammalian target of rapamycin (mtor)-mediated signaling to eukaryotic initiation factor 4e-binding protein 1 (4e-bp1) and ribosomal protein s6 kinase 1 (s6k1). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FOXO3 | up-regulates quantity
transcriptional regulation
|
TSC1 |
0.461 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259382 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 20371605 |
FoxO3a binds to and transactivates the TSC1 promoter, indicating a key role for FoxO3a in regulating TSC1 expression. Together, these data demonstrate that FoxO3a regulates glycolysis downstream of Akt through transcriptional control of Tsc1 |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Pathways: | Insulin Signaling |
3.0
TSC1
- 
- 