| + |
FARSB | form complex 
binding
|
Phenylalanyl-tRNA synthetase |
0.994 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270435 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20223217 |
Here we report crystal structure of hcPheRS complexed with phenylalanine at 3.3 Å resolution. An essential feature of hcPheRS is a novel fold formed by the N-terminal part of the α subunit, whose functional role in tRNAPhe binding and complex formation was studied by truncation mutagenesis. Phenylalanine activation and formation of Phe-tRNAPhe catalyzed by modified hcPheRS have been compared with those of the wild-type enzyme. HcPheRS is a heterotetramer built of two αβ heterodimers. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
QRICH1 | up-regulates quantity by expression 
transcriptional regulation
|
FARSB |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269404 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 33384352 |
QRICH1 promotes the expression of translation-related genes. our combined ChIP-seq and RNA-seq analyses identified that QRICH1 and ATF4 were enriched at the promoters of these specific tRNA synthetases, and that ER stress positively regulated their transcription (Fig. 4I). Together, these findings suggest that QRICH1 and ATF4 modulate tRNA metabolic processes to promote secreted protein synthesis during ER stress. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
FARSB
- 
- 