| + |
Multiaminoacyl-tRNA synthetase | down-regulates quantity 
chemical modification
|
arginine |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270365 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 28271488 |
Aminoacyl-tRNA synthetases (AARSs) are essential enzymes that specifically aminoacylate one tRNA molecule by the cognate amino acid. In mammals, nine synthetases, those specific for amino acids Arg, Asp, Gln, Glu, Ile, Leu, Lys, Met and Pro, associate into a multi-aminoacyl-tRNA synthetase complex, an association which is believed to play a key role in the cellular organization of translation, but also in the regulation of the translational and nontranslational functions of these enzymes. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
arginine | up-regulates quantity 
precursor of
|
Arg-tRNA(Arg) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270370 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 28271488 |
Aminoacyl-tRNA synthetases (AARSs) are essential enzymes that specifically aminoacylate one tRNA molecule by the cognate amino acid. In mammals, nine synthetases, those specific for amino acids Arg, Asp, Gln, Glu, Ile, Leu, Lys, Met and Pro, associate into a multi-aminoacyl-tRNA synthetase complex, an association which is believed to play a key role in the cellular organization of translation, but also in the regulation of the translational and nontranslational functions of these enzymes. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
arginine | up-regulates quantity
|
AminoAcids |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264756 |
|
|
|
|
| pmid |
sentence |
| 29259120 |
All extant life employs the same 20 amino acids for protein biosynthesis |
|
| Publications: |
1 |
| + |
arginine | up-regulates activity 
|
mTORC1 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268013 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 27126896 |
Importantly, asparagine/glutamine pre-load only results in mTOR activation following amino acid stimulation (Fig. 5a), indicating that it is their exchange factor roles that elicit mTORC1 activation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
arginine | down-regulates activity
binding
|
CASTOR1-CASTOR2 arginine binding complex |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-281112 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 26972053 |
Here, we show that CASTOR1, a previously uncharacterized protein, interacts with GATOR2 and is required for arginine deprivation to inhibit mTORC1. CASTOR1 homodimerizes and can also heterodimerize with the related protein, CASTOR2. Arginine disrupts the CASTOR1-GATOR2 complex by binding to CASTOR1 with a dissociation constant of ~30 μM, and its arginine-binding capacity is required for arginine to activate mTORC1 in cells. Collectively, these results establish CASTOR1 as an arginine sensor for the mTORC1 pathway. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
arginine | down-regulates activity
binding
|
CASTOR1-GATOR2 arginine binding complex |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-281115 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 26972053 |
Here, we show that CASTOR1, a previously uncharacterized protein, interacts with GATOR2 and is required for arginine deprivation to inhibit mTORC1. CASTOR1 homodimerizes and can also heterodimerize with the related protein, CASTOR2. Arginine disrupts the CASTOR1-GATOR2 complex by binding to CASTOR1 with a dissociation constant of ~30 μM, and its arginine-binding capacity is required for arginine to activate mTORC1 in cells. Collectively, these results establish CASTOR1 as an arginine sensor for the mTORC1 pathway. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
4.0
arginine