| + |
Multiaminoacyl-tRNA synthetase | down-regulates quantity 
chemical modification
|
lysine |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270405 |
|
|
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 |
| + |
Multiaminoacyl-tRNA synthetase | down-regulates quantity
chemical modification
|
tRNA(Pro) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270427 |
|
|
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 |
| + |
Multiaminoacyl-tRNA synthetase | up-regulates quantity 
chemical modification
|
diphosphate(3-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270423 |
|
|
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. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270375 |
|
|
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. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270415 |
|
|
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. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270383 |
|
|
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. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270367 |
|
|
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. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270431 |
|
|
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. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270399 |
|
|
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. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270391 |
|
|
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. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270407 |
|
|
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: |
9 |
Organism: |
Homo Sapiens |
| + |
Multiaminoacyl-tRNA synthetase | up-regulates quantity
chemical modification
|
AMP |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270416 |
|
|
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. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270400 |
|
|
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. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270408 |
|
|
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. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270368 |
|
|
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. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270384 |
|
|
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. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270392 |
|
|
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. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270376 |
|
|
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. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270424 |
|
|
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. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270432 |
|
|
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: |
9 |
Organism: |
Homo Sapiens |
| + |
Multiaminoacyl-tRNA synthetase | down-regulates quantity
chemical modification
|
tRNA(Lys) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270403 |
|
|
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 |
| + |
AIMP2 | form complex 
binding
|
Multiaminoacyl-tRNA synthetase |
0.919 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270361 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 32644155 |
In mammalian cells, eight cytoplasmic aminoacyl-tRNA synthetases (AARS), and three non-synthetase proteins, reside in a large multi-tRNA synthetase complex (MSC). the MSC is suggested to be a super-complex of two identical, symmetrically arranged sub-units, each containing a single copy of the constituents, with the exception of LysRS which is present as a dimer in each sub-unit (Figure (Figure1B,1B, adapted from (27,28)). The sub-units are proposed to be joined by dimers of AspRS and the ProRS domain of GluProRS, and possibly by LysRS tetramers (20). Four AARSs containing GST-like domains important in protein-protein interactions form a MetRS-AIMP3–GluProRS–AIMP2 core of the complex (27,29). These proteins, together with AspRS, and possibly LeuRS and IleRS (30), form a distinct sub-complex denoted as sub-complex I (27). Sub-complex II consists of AIMP1, GlnRS, ArgRS, a dimer of LysRS, and AIMP2 (which is shared by both sub-complexes). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Multiaminoacyl-tRNA synthetase | up-regulates quantity
chemical modification
|
Arg-tRNA(Arg) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270366 |
|
|
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 |
| Pathways: | Translation elongation and termination |
| + |
Multiaminoacyl-tRNA synthetase | down-regulates quantity
chemical modification
|
tRNA(Ile) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270419 |
|
|
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 |
| + |
Multiaminoacyl-tRNA synthetase | down-regulates quantity
chemical modification
|
ATP(4-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270380 |
|
|
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. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270396 |
|
|
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. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270428 |
|
|
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. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270404 |
|
|
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. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270412 |
|
|
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. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270364 |
|
|
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. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270372 |
|
|
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. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270420 |
|
|
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. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270388 |
|
|
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: |
9 |
Organism: |
Homo Sapiens |
| + |
IARS1 | form complex
binding
|
Multiaminoacyl-tRNA synthetase |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270354 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 32644155 |
In mammalian cells, eight cytoplasmic aminoacyl-tRNA synthetases (AARS), and three non-synthetase proteins, reside in a large multi-tRNA synthetase complex (MSC). the MSC is suggested to be a super-complex of two identical, symmetrically arranged sub-units, each containing a single copy of the constituents, with the exception of LysRS which is present as a dimer in each sub-unit (Figure (Figure1B,1B, adapted from (27,28)). The sub-units are proposed to be joined by dimers of AspRS and the ProRS domain of GluProRS, and possibly by LysRS tetramers (20). Four AARSs containing GST-like domains important in protein-protein interactions form a MetRS-AIMP3–GluProRS–AIMP2 core of the complex (27,29). These proteins, together with AspRS, and possibly LeuRS and IleRS (30), form a distinct sub-complex denoted as sub-complex I (27). Sub-complex II consists of AIMP1, GlnRS, ArgRS, a dimer of LysRS, and AIMP2 (which is shared by both sub-complexes). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Multiaminoacyl-tRNA synthetase | up-regulates quantity
chemical modification
|
Asp-tRNA(Asp) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270374 |
|
|
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 |
| Pathways: | Translation elongation and termination |
| + |
Multiaminoacyl-tRNA synthetase | up-regulates quantity
chemical modification
|
Lys-tRNA(Lys) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270406 |
|
|
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 |
| Pathways: | Translation elongation and termination |
| + |
Multiaminoacyl-tRNA synthetase | down-regulates quantity
chemical modification
|
tRNA(Met) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270395 |
|
|
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 |
| + |
RARS1 | form complex
binding
|
Multiaminoacyl-tRNA synthetase |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270357 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 32644155 |
In mammalian cells, eight cytoplasmic aminoacyl-tRNA synthetases (AARS), and three non-synthetase proteins, reside in a large multi-tRNA synthetase complex (MSC). the MSC is suggested to be a super-complex of two identical, symmetrically arranged sub-units, each containing a single copy of the constituents, with the exception of LysRS which is present as a dimer in each sub-unit (Figure (Figure1B,1B, adapted from (27,28)). The sub-units are proposed to be joined by dimers of AspRS and the ProRS domain of GluProRS, and possibly by LysRS tetramers (20). Four AARSs containing GST-like domains important in protein-protein interactions form a MetRS-AIMP3–GluProRS–AIMP2 core of the complex (27,29). These proteins, together with AspRS, and possibly LeuRS and IleRS (30), form a distinct sub-complex denoted as sub-complex I (27). Sub-complex II consists of AIMP1, GlnRS, ArgRS, a dimer of LysRS, and AIMP2 (which is shared by both sub-complexes). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Multiaminoacyl-tRNA synthetase | up-regulates quantity
chemical modification
|
alpha-aminoacyl-tRNA |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270796 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 14660560 |
Aminoacyl-tRNA synthetases (aaRSs)1 are a family of ancient enzymes that catalyze amino acid activation by ATP and the subsequent aminoacylation to its cognate tRNA. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Translation elongation and termination |
| + |
KARS1 | form complex
binding
|
Multiaminoacyl-tRNA synthetase |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270353 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 32644155 |
In mammalian cells, eight cytoplasmic aminoacyl-tRNA synthetases (AARS), and three non-synthetase proteins, reside in a large multi-tRNA synthetase complex (MSC). the MSC is suggested to be a super-complex of two identical, symmetrically arranged sub-units, each containing a single copy of the constituents, with the exception of LysRS which is present as a dimer in each sub-unit (Figure (Figure1B,1B, adapted from (27,28)). The sub-units are proposed to be joined by dimers of AspRS and the ProRS domain of GluProRS, and possibly by LysRS tetramers (20). Four AARSs containing GST-like domains important in protein-protein interactions form a MetRS-AIMP3–GluProRS–AIMP2 core of the complex (27,29). These proteins, together with AspRS, and possibly LeuRS and IleRS (30), form a distinct sub-complex denoted as sub-complex I (27). Sub-complex II consists of AIMP1, GlnRS, ArgRS, a dimer of LysRS, and AIMP2 (which is shared by both sub-complexes). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Multiaminoacyl-tRNA synthetase | up-regulates quantity
chemical modification
|
Leu-tRNA(Leu) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270414 |
|
|
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 |
| Pathways: | Translation elongation and termination |
| + |
EEF1E1 | form complex
binding
|
Multiaminoacyl-tRNA synthetase |
0.907 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270360 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 32644155 |
In mammalian cells, eight cytoplasmic aminoacyl-tRNA synthetases (AARS), and three non-synthetase proteins, reside in a large multi-tRNA synthetase complex (MSC). the MSC is suggested to be a super-complex of two identical, symmetrically arranged sub-units, each containing a single copy of the constituents, with the exception of LysRS which is present as a dimer in each sub-unit (Figure (Figure1B,1B, adapted from (27,28)). The sub-units are proposed to be joined by dimers of AspRS and the ProRS domain of GluProRS, and possibly by LysRS tetramers (20). Four AARSs containing GST-like domains important in protein-protein interactions form a MetRS-AIMP3–GluProRS–AIMP2 core of the complex (27,29). These proteins, together with AspRS, and possibly LeuRS and IleRS (30), form a distinct sub-complex denoted as sub-complex I (27). Sub-complex II consists of AIMP1, GlnRS, ArgRS, a dimer of LysRS, and AIMP2 (which is shared by both sub-complexes). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
LARS1 | form complex
binding
|
Multiaminoacyl-tRNA synthetase |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270355 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 32644155 |
In mammalian cells, eight cytoplasmic aminoacyl-tRNA synthetases (AARS), and three non-synthetase proteins, reside in a large multi-tRNA synthetase complex (MSC). the MSC is suggested to be a super-complex of two identical, symmetrically arranged sub-units, each containing a single copy of the constituents, with the exception of LysRS which is present as a dimer in each sub-unit (Figure (Figure1B,1B, adapted from (27,28)). The sub-units are proposed to be joined by dimers of AspRS and the ProRS domain of GluProRS, and possibly by LysRS tetramers (20). Four AARSs containing GST-like domains important in protein-protein interactions form a MetRS-AIMP3–GluProRS–AIMP2 core of the complex (27,29). These proteins, together with AspRS, and possibly LeuRS and IleRS (30), form a distinct sub-complex denoted as sub-complex I (27). Sub-complex II consists of AIMP1, GlnRS, ArgRS, a dimer of LysRS, and AIMP2 (which is shared by both sub-complexes). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Multiaminoacyl-tRNA synthetase | down-regulates quantity
chemical modification
|
isoleucine |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270421 |
|
|
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 |
| + |
Multiaminoacyl-tRNA synthetase | down-regulates quantity
chemical modification
|
tRNA(Gln) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270387 |
|
|
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 |
| + |
Multiaminoacyl-tRNA synthetase | down-regulates quantity
chemical modification
|
tRNA(Asp) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270371 |
|
|
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 |
| + |
Multiaminoacyl-tRNA synthetase | down-regulates quantity
chemical modification
|
glutamic acid |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270381 |
|
|
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 |
| + |
Multiaminoacyl-tRNA synthetase | down-regulates quantity
chemical modification
|
methionine |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270397 |
|
|
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 |
| + |
Multiaminoacyl-tRNA synthetase | down-regulates quantity
chemical modification
|
leucine |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270413 |
|
|
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 |
| + |
AIMP1 | form complex
binding
|
Multiaminoacyl-tRNA synthetase |
0.915 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270359 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 32644155 |
In mammalian cells, eight cytoplasmic aminoacyl-tRNA synthetases (AARS), and three non-synthetase proteins, reside in a large multi-tRNA synthetase complex (MSC). the MSC is suggested to be a super-complex of two identical, symmetrically arranged sub-units, each containing a single copy of the constituents, with the exception of LysRS which is present as a dimer in each sub-unit (Figure 1B, adapted from (27,28)). The sub-units are proposed to be joined by dimers of AspRS and the ProRS domain of GluProRS, and possibly by LysRS tetramers (20). Four AARSs containing GST-like domains important in protein-protein interactions form a MetRS-AIMP3–GluProRS–AIMP2 core of the complex (27,29). These proteins, together with AspRS, and possibly LeuRS and IleRS (30), form a distinct sub-complex denoted as sub-complex I (27). Sub-complex II consists of AIMP1, GlnRS, ArgRS, a dimer of LysRS, and AIMP2 (which is shared by both sub-complexes). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
QARS1 | form complex
binding
|
Multiaminoacyl-tRNA synthetase |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270358 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 32644155 |
In mammalian cells, eight cytoplasmic aminoacyl-tRNA synthetases (AARS), and three non-synthetase proteins, reside in a large multi-tRNA synthetase complex (MSC). the MSC is suggested to be a super-complex of two identical, symmetrically arranged sub-units, each containing a single copy of the constituents, with the exception of LysRS which is present as a dimer in each sub-unit (Figure (Figure1B,1B, adapted from (27,28)). The sub-units are proposed to be joined by dimers of AspRS and the ProRS domain of GluProRS, and possibly by LysRS tetramers (20). Four AARSs containing GST-like domains important in protein-protein interactions form a MetRS-AIMP3–GluProRS–AIMP2 core of the complex (27,29). These proteins, together with AspRS, and possibly LeuRS and IleRS (30), form a distinct sub-complex denoted as sub-complex I (27). Sub-complex II consists of AIMP1, GlnRS, ArgRS, a dimer of LysRS, and AIMP2 (which is shared by both sub-complexes). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Multiaminoacyl-tRNA synthetase | up-regulates quantity
chemical modification
|
Ile-tRNA(Ile) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270422 |
|
|
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 |
| Pathways: | Translation elongation and termination |
| + |
EPRS1 | form complex
binding
|
Multiaminoacyl-tRNA synthetase |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270356 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 32644155 |
In mammalian cells, eight cytoplasmic aminoacyl-tRNA synthetases (AARS), and three non-synthetase proteins, reside in a large multi-tRNA synthetase complex (MSC). the MSC is suggested to be a super-complex of two identical, symmetrically arranged sub-units, each containing a single copy of the constituents, with the exception of LysRS which is present as a dimer in each sub-unit (Figure (Figure1B,1B, adapted from (27,28)). The sub-units are proposed to be joined by dimers of AspRS and the ProRS domain of GluProRS, and possibly by LysRS tetramers (20). Four AARSs containing GST-like domains important in protein-protein interactions form a MetRS-AIMP3–GluProRS–AIMP2 core of the complex (27,29). These proteins, together with AspRS, and possibly LeuRS and IleRS (30), form a distinct sub-complex denoted as sub-complex I (27). Sub-complex II consists of AIMP1, GlnRS, ArgRS, a dimer of LysRS, and AIMP2 (which is shared by both sub-complexes). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
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 |
| + |
DARS1 | form complex
binding
|
Multiaminoacyl-tRNA synthetase |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270362 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 32644155 |
In mammalian cells, eight cytoplasmic aminoacyl-tRNA synthetases (AARS), and three non-synthetase proteins, reside in a large multi-tRNA synthetase complex (MSC). the MSC is suggested to be a super-complex of two identical, symmetrically arranged sub-units, each containing a single copy of the constituents, with the exception of LysRS which is present as a dimer in each sub-unit (Figure (Figure1B,1B, adapted from (27,28)). The sub-units are proposed to be joined by dimers of AspRS and the ProRS domain of GluProRS, and possibly by LysRS tetramers (20). Four AARSs containing GST-like domains important in protein-protein interactions form a MetRS-AIMP3–GluProRS–AIMP2 core of the complex (27,29). These proteins, together with AspRS, and possibly LeuRS and IleRS (30), form a distinct sub-complex denoted as sub-complex I (27). Sub-complex II consists of AIMP1, GlnRS, ArgRS, a dimer of LysRS, and AIMP2 (which is shared by both sub-complexes). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Multiaminoacyl-tRNA synthetase | down-regulates quantity
chemical modification
|
tRNA(Arg) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270363 |
|
|
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 |
| + |
Multiaminoacyl-tRNA synthetase | down-regulates quantity
chemical modification
|
glutamine |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270389 |
|
|
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 |
| + |
Multiaminoacyl-tRNA synthetase | down-regulates quantity
chemical modification
|
proline |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270429 |
|
|
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 |
| + |
MARS1 | form complex
binding
|
Multiaminoacyl-tRNA synthetase |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270352 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 32644155 |
In mammalian cells, eight cytoplasmic aminoacyl-tRNA synthetases (AARS), and three non-synthetase proteins, reside in a large multi-tRNA synthetase complex (MSC). the MSC is suggested to be a super-complex of two identical, symmetrically arranged sub-units, each containing a single copy of the constituents, with the exception of LysRS which is present as a dimer in each sub-unit (Figure (Figure1B,1B, adapted from (27,28)). The sub-units are proposed to be joined by dimers of AspRS and the ProRS domain of GluProRS, and possibly by LysRS tetramers (20). Four AARSs containing GST-like domains important in protein-protein interactions form a MetRS-AIMP3–GluProRS–AIMP2 core of the complex (27,29). These proteins, together with AspRS, and possibly LeuRS and IleRS (30), form a distinct sub-complex denoted as sub-complex I (27). Sub-complex II consists of AIMP1, GlnRS, ArgRS, a dimer of LysRS, and AIMP2 (which is shared by both sub-complexes). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Multiaminoacyl-tRNA synthetase | down-regulates quantity
chemical modification
|
aspartic acid |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270373 |
|
|
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 |
| + |
Multiaminoacyl-tRNA synthetase | down-regulates quantity
chemical modification
|
tRNA(Glu) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270379 |
|
|
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 |
| + |
Multiaminoacyl-tRNA synthetase | up-regulates quantity
chemical modification
|
Gln-tRNA(Gln) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270390 |
|
|
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 |
| Pathways: | Translation elongation and termination |
| + |
Multiaminoacyl-tRNA synthetase | up-regulates quantity
chemical modification
|
Pro-tRNA(Pro) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270430 |
|
|
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 |
| Pathways: | Translation elongation and termination |
| + |
Multiaminoacyl-tRNA synthetase | up-regulates quantity
chemical modification
|
Met-tRNA(Met) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270398 |
|
|
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 |
| Pathways: | Translation elongation and termination |
| + |
Multiaminoacyl-tRNA synthetase | down-regulates quantity
chemical modification
|
tRNA(Leu) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270411 |
|
|
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 |
| + |
Multiaminoacyl-tRNA synthetase | up-regulates quantity
chemical modification
|
Glu-tRNA(Glu) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270382 |
|
|
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 |
| Pathways: | Translation elongation and termination |
3.0
Multiaminoacyl-tRNA synthetase
CPX-2469