| + |
mTORC2 | up-regulates activity 
phosphorylation
|
ELP1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275542 |
Ser1174 |
SETSSVVsGSEMSGK |
|
|
| pmid |
sentence |
| 29925953 |
Human ELP1 S1174 phosphorylation was triggered by insulin treatment, as shown by the specific phosphorylated (p)ELP1 (S1174) antibody, and addition of a phosphorylation-mutant variant of the ELP1 protein (ELP1(S1174A)) to ELP1-depleted BRAFV600E melanoma cells failed to rescue cell survival |In line with these findings, mTORC2 activity, but not mTORC1, was required for the insulin-induced phosphorylation of Elp1 S1174 |
|
| Publications: |
1 |
| + |
mTORC2 | down-regulates activity 
phosphorylation
|
SLC7A11 |
0.279 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273682 |
Ser26 |
NVNGRLPsLGNKEPP |
Homo sapiens |
U-87MG Cell |
| pmid |
sentence |
| 28648777 |
MTORC2 phosphorylates serine 26 at the cytosolic N terminus of xCT, inhibiting its activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
mTORC2 | up-regulates
phosphorylation
|
SGK1 |
0.654 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-217016 |
Ser422 |
AEAFLGFsYAPPTDS |
Homo sapiens |
|
| pmid |
sentence |
| 18925875 |
Mtorc2 immunoprecipitated from wild-type, but not from mlst8- or rictor-knockout cells, phosphorylated sgk1 at ser(422) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
mTORC2 | up-regulates activity
phosphorylation
|
YAP1 |
0.285 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277569 |
Ser436 |
INQSTLPsQQNRFPD |
Homo sapiens |
U-87MG Cell |
| pmid |
sentence |
| 34343821 |
Here we report the ability of mTORC2 to directly phosphorylate YAP at serine 436 (Ser436) positively regulating YAP activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
mTORC2 | up-regulates activity
phosphorylation
|
AKT1 |
0.634 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-217012 |
Ser473 |
RPHFPQFsYSASGTA |
Homo sapiens |
Blood Platelet |
| pmid |
sentence |
| 21592956 |
Protein kinase B (PKB, Akt) is a Ser/Thr kinase involved in the regulation of cell survival, proliferation, and metabolism and is activated by dual phosphorylation on Thr(308) in the activation loop and Ser(473) in the hydrophobic motif. It plays a contributory role to platelet function, although little is known about its regulation. In this study, we investigated the role of the mammalian target of rapamycin complex (mTORC)-2 in Akt regulation using the recently identified small molecule ATP competitive mTOR inhibitors PP242 and Torin1. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-217004 |
Ser473 |
RPHFPQFsYSASGTA |
Homo sapiens |
|
| pmid |
sentence |
| 21157483 |
Mammalian TOR complex 1 (mTORC1) and mTORC2 exert their actions by regulating other important kinases, such as S6 kinase (S6K) and Akt.Recent findings have revealed novel important roles for mTORC2 in the phosphorylation of AGC kinase family members. mTORC2 phosphorylates and activates Akt, SGK, and PKC, which regulate cell survival, cell cycle progression and anabolism |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252600 |
Ser473 |
RPHFPQFsYSASGTA |
Homo sapiens |
HT-29 Cell, A-549 Cell |
| pmid |
sentence |
| 15718470 |
The rictor-mtor complex directly phosphorylated akt/pkb on ser473 in vitro and facilitated thr308 phosphorylation by pdk1 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252441 |
Ser477 |
PQFSYSAsGTA |
Homo sapiens |
MCF-7 Cell |
| pmid |
sentence |
| 24670654 |
Phosphorylation of S477 and T479 at the Akt extreme carboxy terminus by cyclin-dependent kinase 2 (Cdk2)/cyclin A or mTORC2, under distinct physiological conditions, promotes Akt activation through facilitating, or functionally compensating for, S473 phosphorylation |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252438 |
Thr450 |
TAQMITItPPDQDDS |
Mus musculus |
MEF Cell |
| pmid |
sentence |
| 18566586 |
MTORC2 phosphorylates newly synthesized Akt at the TM (Thr450) site to facilitate carboxyl-terminal folding and to stabilize Akt |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252444 |
Thr479 |
FSYSASGtA |
Homo sapiens |
MCF-7 Cell |
| pmid |
sentence |
| 24670654 |
Phosphorylation of S477 and T479 at the Akt extreme carboxy terminus by cyclin-dependent kinase 2 (Cdk2)/cyclin A or mTORC2, under distinct physiological conditions, promotes Akt activation through facilitating, or functionally compensating for, S473 phosphorylation |
|
| Publications: |
6 |
Organism: |
Homo Sapiens, Mus Musculus |
| Pathways: | FLT3-ITD signaling |
| + |
mTORC2 | up-regulates activity
phosphorylation
|
AKT |
0.634 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-217008 |
Ser473 |
RPHFPQFsYSASGTA |
Homo sapiens |
HT-29 Cell, A-549 Cell |
| pmid |
sentence |
| 15718470 |
The rictor-mtor complex directly phosphorylated akt/pkb on ser473 in vitro and facilitated thr308 phosphorylation by pdk1 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252451 |
Ser477 |
PQFSYSAsGTA |
Homo sapiens |
MCF-7 Cell |
| pmid |
sentence |
| 24670654 |
Phosphorylation of S477 and T479 at the Akt extreme carboxy terminus by cyclin-dependent kinase 2 (Cdk2)/cyclin A or mTORC2, under distinct physiological conditions, promotes Akt activation through facilitating, or functionally compensating for, S473 phosphorylation |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252448 |
Thr450 |
TAQMITItPPDQDDS |
Mus musculus |
MEF Cell |
| pmid |
sentence |
| 18566586 |
MTORC2 phosphorylates newly synthesized Akt at the TM (Thr450) site to facilitate carboxyl-terminal folding and to stabilize Akt |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252454 |
Thr479 |
FSYSASGtA |
Homo sapiens |
MCF-7 Cell |
| pmid |
sentence |
| 24670654 |
Phosphorylation of S477 and T479 at the Akt extreme carboxy terminus by cyclin-dependent kinase 2 (Cdk2)/cyclin A or mTORC2, under distinct physiological conditions, promotes Akt activation through facilitating, or functionally compensating for, S473 phosphorylation |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251982 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21157483 |
Mammalian TOR complex 1 (mTORC1) and mTORC2 exert their actions by regulating other important kinases, such as S6 kinase (S6K) and Akt.Recent findings have revealed novel important roles for mTORC2 in the phosphorylation of AGC kinase family members. mTORC2 phosphorylates and activates Akt, SGK, and PKC, which regulate cell survival, cell cycle progression and anabolism |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251983 |
|
|
Homo sapiens |
Blood Platelet |
| pmid |
sentence |
| 21592956 |
Protein kinase B (PKB, Akt) is a Ser/Thr kinase involved in the regulation of cell survival, proliferation, and metabolism and is activated by dual phosphorylation on Thr(308) in the activation loop and Ser(473) in the hydrophobic motif. It plays a contributory role to platelet function, although little is known about its regulation. In this study, we investigated the role of the mammalian target of rapamycin complex (mTORC)-2 in Akt regulation using the recently identified small molecule ATP competitive mTOR inhibitors PP242 and Torin1. |
|
| Publications: |
6 |
Organism: |
Homo Sapiens, Mus Musculus |
| Pathways: | FLT3-ITD signaling, mTOR in cancer, MTOR Signaling, PI3K/AKT Signaling |
| + |
mTORC2 | up-regulates activity
phosphorylation
|
RRM1 |
0.308 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277566 |
Ser631 |
IYTRRVLsGEFQIVN |
Homo sapiens |
NCI-H1299 Cell |
| pmid |
sentence |
| 34126361 |
Mechanistically, mTORC2 directly interacted and phosphorylated RNR large subunit RRM1 at Ser 631. Ser631 phosphorylation of RRM1 enhanced its interaction with small subunit RRM2 to maintain sufficient RNR enzymatic activity for efficient DNA replication. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
mTORC2 | down-regulates activity
phosphorylation
|
AMOTL2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272085 |
Ser759 |
SSSQRAAsLDSVATS |
|
|
| pmid |
sentence |
| 25998128 |
AMOTL2 is phosphorylated at serine 760 by mTORC2. Mutation of AMOTL2 mimicking constitutive Ser(760) phosphorylation blocks its ability to bind and repress YAP leading to increased relative expression of known YAP gene targets. |
|
| Publications: |
1 |
| + |
mTORC2 | up-regulates quantity by stabilization
phosphorylation
|
FBXW8 |
0.268 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271940 |
Ser85 |
DVASRSRsPLAREGA |
Mus musculus |
MEF Cell |
| pmid |
sentence |
| 23142081 |
MTORC2 stabilizes Fbw8 by phosphorylation at Ser86 |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
mTORC2 | up-regulates activity
phosphorylation
|
PRKCE |
0.324 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276347 |
Thr710 |
TREEPVLtLVDEAIV |
Homo sapiens |
|
| pmid |
sentence |
| 21806543 |
In the present study, we have identified the mTORC2 subunit Sin1 as a direct binding partner of the PKC (protein kinase C) ε kinase domain and map the interaction to the central highly conserved region of Sin1. Exploiting the conformational dependence for PKC phosphorylation, we demonstrate that mTORC2 is essential for acute priming of PKC. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
DEPTOR | form complex 
binding
|
mTORC2 |
0.715 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-205603 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 25628925 |
Depending on their binding partners and sensitivities to rapamycin, mtor resides in at least two distinct complexes, termed mtor complex 1 (mtorc1, containing raptor, fkbp12, pras40 and mlst8) and mtor complex 2 (mtorc2, containing rictor, sin1, protor and mlst8) |
|
| 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 |
| + |
mTORC2 | up-regulates activity
phosphorylation
|
mTORC2 |
0.678 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-217000 |
|
|
Homo sapiens |
T-lymphocyte |
| pmid |
sentence |
| 10702316 |
We report here the identification of a FRAP autophosphorylation site. This site, Ser-2481, is located in a hydrophobic region near the conserved carboxyl-terminal FRAP tail. We demonstrate that the COOH-terminal tail is required for FRAP kinase activity and for signaling to the translational regulator p70(s6k) (ribosomal subunit S6 kinase). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-235484 |
|
|
Mus musculus |
NIH-3T3 Cell |
| pmid |
sentence |
| 20022946 |
These data suggest that mTORC1- and likely mTORC2-associated mTOR Ser-2481 autophosphorylation directly monitors intrinsic mTORC-specific catalytic activity |
|
| Publications: |
2 |
Organism: |
Homo Sapiens, Mus Musculus |
| Pathways: | FLT3-ITD signaling, mTOR in cancer, MTOR Signaling, PI3K/AKT Signaling |
| + |
GOLPH3 | up-regulates activity 
|
mTORC2 |
0.297 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253556 |
|
|
Homo sapiens |
A-549 Cell, 1205-Lu Cell |
| pmid |
sentence |
| 19553991 |
Mechanistically, GOLPH3 regulates cell size, enhances growth factor-induced mTOR signaling in human cancer cells and alters response to mTOR inhibitor in vivo. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PIP3 | up-regulates activity
chemical activation
|
mTORC2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252430 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 26293922 |
PtdIns(3,4,5)P3, but not other PtdInsPn species, interacts with SIN1-PH to release its inhibition on the mTOR kinase domain, thereby triggering mTORC2 activation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | FLT3-ITD signaling, mTOR in cancer, MTOR Signaling, PI3K/AKT Signaling |
| + |
mTORC2 | down-regulates activity 
|
FUS |
0.298 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262819 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 33082139 |
When mTORC2 is inhibited, FUS is recruited to polyribosomes to promote translation inhibition and polyribosome stalling. Panel iv, ALS-FUS R521G and P525L mutants that localize more prominently to the cytoplasm also associate more abundantly with polyribosomes to inhibit translation and protein synthesis. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
EEF1A1 | form complex
binding
|
mTORC2 |
0.303 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-205606 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 25628925 |
Depending on their binding partners and sensitivities to rapamycin, mtor resides in at least two distinct complexes, termed mtor complex 1 (mtorc1, containing raptor, fkbp12, pras40 and mlst8) and mtor complex 2 (mtorc2, containing rictor, sin1, protor and mlst8) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
mTORC2 | up-regulates
|
MYC |
0.361 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256171 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 24856037 |
MTORC1 and mTORC2 converge on c-Myc to control metabolic reprogramming in cancer. mTORC1 and mTORC2 conspire to link growth factor receptor–PI3K signaling with c-Myc-dependent metabolic reprogramming by controlling both c-Myc levels and activity |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | FLT3-ITD signaling, mTOR in cancer |
| + |
DEPTOR | down-regulates activity
binding
|
mTORC2 |
0.715 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251659 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 19446321 |
DEPTOR is an mTOR inhibitor frequently overexpressed in multiple myeloma cells and required for their survival |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RICTOR | form complex
binding
|
mTORC2 |
0.828 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-205624 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 25628925 |
Depending on their binding partners and sensitivities to rapamycin, mtor resides in at least two distinct complexes, termed mtor complex 1 (mtorc1, containing raptor, fkbp12, pras40 and mlst8) and mtor complex 2 (mtorc2, containing rictor, sin1, protor and mlst8) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRR5 | form complex
binding
|
mTORC2 |
0.666 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-205621 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 25628925 |
Depending on their binding partners and sensitivities to rapamycin, mtor resides in at least two distinct complexes, termed mtor complex 1 (mtorc1, containing raptor, fkbp12, pras40 and mlst8) and mtor complex 2 (mtorc2, containing rictor, sin1, protor and mlst8) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MTOR | form complex
binding
|
mTORC2 |
0.727 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262534 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 25628925 |
Depending on their binding partners and sensitivities to rapamycin, mtor resides in at least two distinct complexes, termed mtor complex 1 (mtorc1, containing raptor, fkbp12, pras40 and mlst8) and mtor complex 2 (mtorc2, containing rictor, sin1, protor and mlst8) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | FLT3-ITD signaling, MTOR Signaling |
| + |
MLST8 | form complex
binding
|
mTORC2 |
0.828 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-205612 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 25628925 |
Depending on their binding partners and sensitivities to rapamycin, mtor resides in at least two distinct complexes, termed mtor complex 1 (mtorc1, containing raptor, fkbp12, pras40 and mlst8) and mtor complex 2 (mtorc2, containing rictor, sin1, protor and mlst8) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TTI1 | up-regulates quantity by stabilization
binding
|
mTORC2 |
0.643 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272004 |
|
|
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 |
3.0
mTORC2