| + |
EEF1A1 | up-regulates 
relocalization
|
Phe-tRNA(Phe) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269520 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23699257 |
During protein synthesis, eEF1A binds to and delivers aminoacylated tRNAs (aa-tRNAs) to the elongating ribosome (Fig. 1). GTP bound to eEF1A is hydrolyzed upon codon-anticodon match between an aa-tRNA in the A site of the ribosome and mRNA bound to the ribosome. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Translation elongation and termination |
| + |
EEF1A2 | up-regulates
relocalization
|
Phe-tRNA(Phe) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269540 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23699257 |
During protein synthesis, eEF1A binds to and delivers aminoacylated tRNAs (aa-tRNAs) to the elongating ribosome (Fig. 1). GTP bound to eEF1A is hydrolyzed upon codon-anticodon match between an aa-tRNA in the A site of the ribosome and mRNA bound to the ribosome. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Phenylalanyl-tRNA synthetase | up-regulates quantity
chemical modification
|
Phe-tRNA(Phe) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270442 |
|
|
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 |
| Pathways: | Translation elongation and termination |
| + |
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 |
| + |
EEF1A1P5 | up-regulates
relocalization
|
Phe-tRNA(Phe) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269560 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23699257 |
During protein synthesis, eEF1A binds to and delivers aminoacylated tRNAs (aa-tRNAs) to the elongating ribosome (Fig. 1). GTP bound to eEF1A is hydrolyzed upon codon-anticodon match between an aa-tRNA in the A site of the ribosome and mRNA bound to the ribosome. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
phenylalanine | up-regulates quantity
precursor of
|
Phe-tRNA(Phe) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270444 |
|
|
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 |
3.0
Phe-tRNA(Phe)