| + |
CSNK2A1 | down-regulates 
phosphorylation
|
TELO2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-200202 |
Ser487 |
AQLAGSDsDLDSDDE |
Homo sapiens |
|
| pmid |
sentence |
| 23263282 |
Here we report that tel2 and tti1 are targeted for degradation within mtorc1 by the scffbxo9 ubiquitin ligase to adjust mtor signalling to growth factor availability. This process is primed by ck2, which translocates to the cytoplasm to mediate mtorc1-specific phosphorylation of tel2/tti1. ere, we show that tel2 is constitutively phosphorylated on conserved serines 487 and 491 by casein kinase 2 (ck2) |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-168036 |
Ser487 |
AQLAGSDsDLDSDDE |
Homo sapiens |
|
| pmid |
sentence |
| 20864032 |
Here we report that tel2 and tti1 are targeted for degradation within mtorc1 by the scffbxo9 ubiquitin ligase to adjust mtor signalling to growth factor availability. This process is primed by ck2, which translocates to the cytoplasm to mediate mtorc1-specific phosphorylation of tel2/tti1. ere, we show that tel2 is constitutively phosphorylated on conserved serines 487 and 491 by casein kinase 2 (ck2) |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-168040 |
Ser491 |
GSDSDLDsDDEFVPY |
Homo sapiens |
|
| pmid |
sentence |
| 20864032 |
Here we report that tel2 and tti1 are targeted for degradation within mtorc1 by the scffbxo9 ubiquitin ligase to adjust mtor signalling to growth factor availability. This process is primed by ck2, which translocates to the cytoplasm to mediate mtorc1-specific phosphorylation of tel2/tti1. Here, we show that tel2 is constitutively phosphorylated on conserved serines 487 and 491 by casein kinase 2 (ck2) |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-200206 |
Ser491 |
GSDSDLDsDDEFVPY |
Homo sapiens |
|
| pmid |
sentence |
| 23263282 |
Here we report that tel2 and tti1 are targeted for degradation within mtorc1 by the scffbxo9 ubiquitin ligase to adjust mtor signalling to growth factor availability. This process is primed by ck2, which translocates to the cytoplasm to mediate mtorc1-specific phosphorylation of tel2/tti1. Here, we show that tel2 is constitutively phosphorylated on conserved serines 487 and 491 by casein kinase 2 (ck2) |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| + |
Cullin 1-RBX1-Skp1 | down-regulates quantity by destabilization
polyubiquitination
|
TELO2 |
0.259 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272000 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 23263282 |
Here we report that Tel2 and Tti1 are targeted for degradation within mTORC1 by the SCFFbxo9 ubiquitin ligase to adjust mTOR signalling to growth factor availability. The interaction between Tel2/Tti1 and Fbxo9 identified by mass spectrometry suggests that SCFFbxo9 is probably the ubiquitin ligase that mediates degradation of both proteins. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TELO2 | up-regulates quantity by stabilization 
binding
|
mTORC1 |
0.532 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272001 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 20427287 |
MTOR exists in two distinct complexes, mTORC1 and mTORC2, that differ in their subunit composition. In this study, we identified KIAA0406 as a novel mTOR-interacting protein. Because it has sequence homology with Schizosaccharomyces pombe Tti1, we named it mammalian Tti1. Tti1 constitutively interacts with mTOR in both mTORC1 and mTORC2. Knockdown of Tti1 suppresses phosphorylation of both mTORC1 substrates (S6K1 and 4E-BP1) and an mTORC2 substrate (Akt) and also induces autophagy. Furthermore, using immunoprecipitation and size-exclusion chromatography analyses, we found that knockdown of either Tti1 or Tel2 causes disassembly of mTORC1 and mTORC2. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TELO2 | up-regulates quantity by stabilization
binding
|
mTORC2 |
0.569 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272003 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 20427287 |
MTOR exists in two distinct complexes, mTORC1 and mTORC2, that differ in their subunit composition. In this study, we identified KIAA0406 as a novel mTOR-interacting protein. Because it has sequence homology with Schizosaccharomyces pombe Tti1, we named it mammalian Tti1. Tti1 constitutively interacts with mTOR in both mTORC1 and mTORC2. Knockdown of Tti1 suppresses phosphorylation of both mTORC1 substrates (S6K1 and 4E-BP1) and an mTORC2 substrate (Akt) and also induces autophagy. Furthermore, using immunoprecipitation and size-exclusion chromatography analyses, we found that knockdown of either Tti1 or Tel2 causes disassembly of mTORC1 and mTORC2. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FBXO9 | down-regulates quantity by destabilization
binding
|
TELO2 |
0.453 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271996 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 23263282 |
Here we report that Tel2 and Tti1 are targeted for degradation within mTORC1 by the SCFFbxo9 ubiquitin ligase to adjust mTOR signalling to growth factor availability. The interaction between Tel2/Tti1 and Fbxo9 identified by mass spectrometry suggests that SCFFbxo9 is probably the ubiquitin ligase that mediates degradation of both proteins. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
TELO2
- 
- 