| + |
tRNA(Phe) | up-regulates quantity 
precursor of
|
Phe-tRNA(Phe) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270443 |
|
|
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 |
| + |
Phenylalanyl-tRNA synthetase | down-regulates quantity 
chemical modification
|
tRNA(Phe) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270438 |
|
|
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 |
| + |
RNA Polymerase III | up-regulates quantity
chemical modification
|
tRNA(Phe) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269492 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 27911719 |
RNAPIII is specialized for transcription of short, abundant nonprotein-coding RNA transcripts. In addition to all tRNAs, RNAPIII transcribes the 5S rRNA and other essential RNAs, including the U6 small nuclear RNA (snRNA), the snR52 small nucleolar RNA and the RNA components of the signal recognition particle (SRP1) and RNase P (RPR1) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
tRNA(Phe)