| + |
ERK1/2 | up-regulates activity 
phosphorylation
|
MARS1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276671 |
Ser209 |
LQKQPQPsPAEGRAV |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 25097229 |
Here, we report that methionyl-tRNA synthetase (MRS) is phosphorylated at Ser209 and Ser825 by extracellular signal-related kinase (ERK1/2) under conditions of stress caused by reactive oxygen species (ROS), and that this phosphorylated MRS shows increased affinity for non-cognate tRNAs with lower affinity for tRNA(Met), leading to an increase in Met residues in cellular proteins. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276670 |
Ser825 |
GGGQAKTsPKPAVVE |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 25097229 |
Here, we report that methionyl-tRNA synthetase (MRS) is phosphorylated at Ser209 and Ser825 by extracellular signal-related kinase (ERK1/2) under conditions of stress caused by reactive oxygen species (ROS), and that this phosphorylated MRS shows increased affinity for non-cognate tRNAs with lower affinity for tRNA(Met), leading to an increase in Met residues in cellular proteins. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
EIF2AK4 | down-regulates 
phosphorylation
|
MARS1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-177648 |
Ser662 |
NRAGMFVsKFFGGYV |
Homo sapiens |
|
| pmid |
sentence |
| 22106287 |
Here we demonstrate that aimp3 is released from mrs by uv irradiation-induced stress. Dissociation was induced by phosphorylation of mrs at ser662 by general control nonrepressed-2 (gcn2) following uv irradiation. Substitution of ser662 to asp (s662d) induced a conformational change in mrs and significantly reduced its interaction with aimp3. This mutant possessed significantly reduced mrs catalytic activity because of loss of trna(met) binding, resulting in down-regulation of global translation. |
|
| 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 |
3.0
MARS1
- 
- 