| + |
CDK1 |
phosphorylation
|
RPTOR |
0.401 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-163849 |
Ser696 |
EKNYALPsPATTEGG |
Homo sapiens |
|
| pmid |
sentence |
| 20169205 |
Cdc2 is the raptor ser696, thr706 kinase |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-163853 |
Thr706 |
TTEGGSLtPVRDSPC |
Homo sapiens |
|
| pmid |
sentence |
| 20169205 |
Cdc2 is the raptor ser696, thr706 kinase |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
MAPK3 | up-regulates activity 
phosphorylation
|
RPTOR |
0.487 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-169526 |
Ser696 |
EKNYALPsPATTEGG |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 21071439 |
We found three proline-directed residues within raptor, ser(8), ser(696), and ser(863), which are directly phosphorylated by erk1/2. Expression of phosphorylation-deficient alleles of raptor revealed that phosphorylation of these sites by erk1/2 normally promotes mtorc1 activity and signaling to downstream substrates, such as 4e-bp1. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-169530 |
Ser8 |
MESEMLQsPLLGLGE |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 21071439 |
We found three proline-directed residues within raptor, ser(8), ser(696), and ser(863), which are directly phosphorylated by erk1/2. Expression of phosphorylation-deficient alleles of raptor revealed that phosphorylation of these sites by erk1/2 normally promotes mtorc1 activity and signaling to downstream substrates, such as 4e-bp1. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-169534 |
Ser863 |
LTQSAPAsPTNKGVH |
Homo sapiens |
|
| pmid |
sentence |
| 21071439 |
We found three proline-directed residues within raptor, ser(8), ser(696), and ser(863), which are directly phosphorylated by erk1/2. Expression of phosphorylation-deficient alleles of raptor revealed that phosphorylation of these sites by erk1/2 normally promotes mtorc1 activity and signaling to downstream substrates, such as 4e-bp1. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
MAPK1 |
phosphorylation
|
RPTOR |
0.539 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-169514 |
Ser696 |
EKNYALPsPATTEGG |
Homo sapiens |
|
| pmid |
sentence |
| 21071439 |
We found three proline-directed residues within raptor, ser(8), ser(696), and ser(863), which are directly phosphorylated by erk1/2. Expression of phosphorylation-deficient alleles of raptor revealed that phosphorylation of these sites by erk1/2 normally promotes mtorc1 activity and signaling to downstream substrates, such as 4e-bp1. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-169518 |
Ser8 |
MESEMLQsPLLGLGE |
Homo sapiens |
|
| pmid |
sentence |
| 21071439 |
We found three proline-directed residues within raptor, ser(8), ser(696), and ser(863), which are directly phosphorylated by erk1/2. Expression of phosphorylation-deficient alleles of raptor revealed that phosphorylation of these sites by erk1/2 normally promotes mtorc1 activity and signaling to downstream substrates, such as 4e-bp1. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-169522 |
Ser863 |
LTQSAPAsPTNKGVH |
Homo sapiens |
|
| pmid |
sentence |
| 21071439 |
We found three proline-directed residues within raptor, ser(8), ser(696), and ser(863), which are directly phosphorylated by erk1/2. Expression of phosphorylation-deficient alleles of raptor revealed that phosphorylation of these sites by erk1/2 normally promotes mtorc1 activity and signaling to downstream substrates, such as 4e-bp1. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
RPS6KA1 | up-regulates
phosphorylation
|
RPTOR |
0.571 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-180458 |
Ser719 |
PCTPRLRsVSSYGNI |
Homo sapiens |
|
| pmid |
sentence |
| 18722121 |
Ser719, ser721, and ser722 are the predominant rsk-dependent phosphorylation sites in raptor raptor phosphorylation regulates mtorc1 activity |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-180462 |
Ser721 |
TPRLRSVsSYGNIRA |
Homo sapiens |
|
| pmid |
sentence |
| 18722121 |
Ser719, ser721, and ser722 are the predominant rsk-dependent phosphorylation sites in raptor raptor phosphorylation regulates mtorc1 activity |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-180466 |
Ser722 |
PRLRSVSsYGNIRAV |
Homo sapiens |
|
| pmid |
sentence |
| 18722121 |
Ser719, ser721, and ser722 are the predominant rsk-dependent phosphorylation sites in raptor raptor phosphorylation regulates mtorc1 activity |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| Pathways: | MTOR Signaling |
| + |
RPS6K | up-regulates
phosphorylation
|
RPTOR |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252772 |
Ser719 |
PCTPRLRsVSSYGNI |
Homo sapiens |
|
| pmid |
sentence |
| 18722121 |
Ser719, ser721, and ser722 are the predominant rsk-dependent phosphorylation sites in raptor raptor phosphorylation regulates mtorc1 activity |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252774 |
Ser721 |
TPRLRSVsSYGNIRA |
Homo sapiens |
|
| pmid |
sentence |
| 18722121 |
Ser719, ser721, and ser722 are the predominant rsk-dependent phosphorylation sites in raptor raptor phosphorylation regulates mtorc1 activity |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252773 |
Ser722 |
PRLRSVSsYGNIRAV |
Homo sapiens |
|
| pmid |
sentence |
| 18722121 |
Ser719, ser721, and ser722 are the predominant rsk-dependent phosphorylation sites in raptor raptor phosphorylation regulates mtorc1 activity |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
AMPK | down-regulates 
phosphorylation
|
RPTOR |
0.497 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263046 |
Ser722 |
PRLRSVSsYGNIRAV |
Mus musculus |
|
| pmid |
sentence |
| 18439900 |
These results suggest that AMPK activation can induce phosphorylation of both serine 722 and serine 792.|Raptor phosphorylation is required for inhibition of mTORC1 by AMPK |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263044 |
Ser792 |
LTQSAPAsPTNKGVH |
Mus musculus |
|
| pmid |
sentence |
| 18439900 |
These results suggest that AMPK activation can induce phosphorylation of both serine 722 and serine 792.|Raptor phosphorylation is required for inhibition of mTORC1 by AMPK |
|
| Publications: |
2 |
Organism: |
Mus Musculus |
| Pathways: | MTOR Signaling |
| + |
PRKAA2 | down-regulates
phosphorylation
|
RPTOR |
0.679 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263045 |
Ser722 |
PRLRSVSsYGNIRAV |
Mus musculus |
|
| pmid |
sentence |
| 18439900 |
These results suggest that AMPK activation can induce phosphorylation of both serine 722 and serine 792.|Raptor phosphorylation is required for inhibition of mTORC1 by AMPK |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
MAPK11 |
phosphorylation
|
RPTOR |
0.365 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-174870 |
Ser771 |
SASSTLGsPENEEHI |
Homo sapiens |
|
| pmid |
sentence |
| 21757713 |
Arsenite treatment of cells activates p38_ and induces interaction between p38_ and raptor, a regulatory component of mtorc1, resulting in phosphorylation of raptor on ser(863) and ser(771). The phosphorylation of raptor on these sites enhances mtorc1 activity, and contributes largely to arsenite-induced mtorc1 activation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-174874 |
Ser863 |
LTQSAPAsPTNKGVH |
Homo sapiens |
|
| pmid |
sentence |
| 21757713 |
Arsenite treatment of cells activates p38_ and induces interaction between p38_ and raptor, a regulatory component of mtorc1, resulting in phosphorylation of raptor on ser(863) and ser(771). The phosphorylation of raptor on these sites enhances mtorc1 activity, and contributes largely to arsenite-induced mtorc1 activation. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PRKAA2 | down-regulates activity
phosphorylation
|
RPTOR |
0.679 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-163463 |
Ser792 |
LTQSAPAsPTNKGVH |
Mus musculus |
|
| pmid |
sentence |
| 18439900 |
These results suggest that AMPK activation can induce phosphorylation of both serine 722 and serine 792.|Raptor phosphorylation is required for inhibition of mTORC1 by AMPK |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
PRKAA1 | down-regulates activity
phosphorylation
|
RPTOR |
0.671 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-161375 |
Ser792 |
DKMRRASsYSSLNSL |
Mus musculus |
MEF Cell |
| pmid |
sentence |
| 18439900 |
The phosphorylation of raptor by ampk is required for the inhibition of mtorc1 and cell-cycle arrest induced by energy stress. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-173035 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21460634 |
Ampk in turn inactivates mtorc1 directly by phosphorylating raptor and indirectly by phosphorylating tsc2. |
|
| Publications: |
2 |
Organism: |
Mus Musculus, Homo Sapiens |
| + |
MTOR | up-regulates activity
phosphorylation
|
RPTOR |
0.989 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-174882 |
Ser855 |
QRVLDTSsLTQSAPA |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 19864431 |
Strikingly, raptor Ser(863) phosphorylation is absolutely required for raptor Ser(859) and Ser(855) phosphorylation. These data suggest that mTORC1 activation leads to raptor multisite phosphorylation and that raptor Ser(863) phosphorylation functions as a master biochemical switch that modulates hierarchical raptor phosphorylation (e.g. on Ser(859) and Ser(855)) |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-184959 |
Ser859 |
DTSSLTQsAPASPTN |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 19346248 |
The phosphorylation of raptor is stimulated by insulin and inhibited by rapamycin. Importantly, the site-directed mutation of raptor at one phosphorylation site, Ser(863), reduced mTORC1 activity both in vitro and in vivo. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-188920 |
Ser859 |
DTSSLTQsAPASPTN |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 19864431 |
Strikingly, raptor Ser(863) phosphorylation is absolutely required for raptor Ser(859) and Ser(855) phosphorylation. These data suggest that mTORC1 activation leads to raptor multisite phosphorylation and that raptor Ser(863) phosphorylation functions as a master biochemical switch that modulates hierarchical raptor phosphorylation (e.g. on Ser(859) and Ser(855)) |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-188924 |
Ser863 |
LTQSAPAsPTNKGVH |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 19864431 |
Our data that insulin-stimulated raptor ser863 phosphorylation requires kinase-active mtorc1 and displays rapamycin sensitivity in intact cells, together with the data of wang et al. (67) that mtor phosphorylates raptor ser863 in vitro, strongly suggest that mtor itself mediates raptor ser863 phosphorylation. / strikingly, raptor ser863 phosphorylation is absolutely required for raptor ser859 and ser855 phosphorylation. These data suggest that mtorc1 activation leads to raptor multisite phosphorylation and that raptor ser863 phosphorylation functions as a master biochemical switch that modulates hierarchical raptor phosphorylation |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| Pathways: | MTOR Signaling |
| + |
ERK1/2 | up-regulates activity
phosphorylation
|
RPTOR |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-174878 |
Ser863 |
LTQSAPAsPTNKGVH |
Homo sapiens |
|
| pmid |
sentence |
| 21071439 |
We found three proline-directed residues within raptor, ser(8), ser(696), and ser(863), which are directly phosphorylated by erk1/2. Expression of phosphorylation-deficient alleles of raptor revealed that phosphorylation of these sites by erk1/2 normally promotes mtorc1 activity and signaling to downstream substrates, such as 4e-bp1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | MTOR Signaling |
| + |
MAPK1 | up-regulates activity
phosphorylation
|
RPTOR |
0.539 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-188916 |
Ser863 |
LTQSAPAsPTNKGVH |
Homo sapiens |
|
| pmid |
sentence |
| 21071439 |
We found three proline-directed residues within raptor, ser(8), ser(696), and ser(863), which are directly phosphorylated by erk1/2. Expression of phosphorylation-deficient alleles of raptor revealed that phosphorylation of these sites by erk1/2 normally promotes mtorc1 activity and signaling to downstream substrates, such as 4e-bp1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NLK | down-regulates activity
phosphorylation
|
RPTOR |
0.338 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273908 |
Ser863 |
LTQSAPAsPTNKGVH |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 26588989 |
NLK inhibits mTORC1 lysosomal localization and thereby suppresses mTORC1 activation. Mechanistically, NLK phosphorylates Raptor on S863 to disrupt its interaction with the Rag GTPase, which is important for mTORC1 lysosomal recruitment. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CILK1 | up-regulates
phosphorylation
|
RPTOR |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-196198 |
Thr908 |
LPSGRPGtTGPAGAQ |
Homo sapiens |
|
| pmid |
sentence |
| 22356909 |
Our findings demonstrate an important role for ick in modulating the activity of mtorc1 through phosphorylation of raptor thr-908 and thus implicate a potential signaling mechanism by which ick regulates cell proliferation and division. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKAB1 | down-regulates
phosphorylation
|
RPTOR |
0.439 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-173041 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21460634 |
Ampk in turn inactivates mtorc1 directly by phosphorylating raptor and indirectly by phosphorylating tsc2. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RRAGC | up-regulates
binding
|
RPTOR |
0.939 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-162054 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20006481 |
Active rag and gtr heterodimers are able to bind and activate torc1, through direct interactions with raptor. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RPTOR | form complex 
binding
|
mTORC1 |
0.858 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-205627 |
|
|
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 |
| + |
RRAGD | up-regulates
binding
|
RPTOR |
0.902 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-162093 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20006481 |
Active rag and gtr heterodimers are able to bind and activate torc1, through direct interactions with raptor |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Gbeta | up-regulates activity
phosphorylation
|
RPTOR |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270032 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 21071439 |
We found three proline-directed residues within raptor, ser(8), ser(696), and ser(863), which are directly phosphorylated by erk1/2. Expression of phosphorylation-deficient alleles of raptor revealed that phosphorylation of these sites by erk1/2 normally promotes mtorc1 activity and signaling to downstream substrates, such as 4e-bp1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
RPTOR
- 
- 