| + |
EEF1A1 | up-regulates 
relocalization
|
Gly-tRNA(Gly) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269521 |
|
|
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 |
| + |
GARS1 | up-regulates quantity
chemical modification
|
Gly-tRNA(Gly) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270482 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 24898252 |
Aminoacyl-tRNA synthetases are an ancient enzyme family that specifically charges tRNA molecules with cognate amino acids for protein synthesis. Glycyl- tRNA synthetase (GlyRS) is one of the most intriguing aminoacyl-tRNA synthetases due to its divergent quaternary structure and abnormal charging properties. . In this study we report crystal structures of wild type and mutant hGlyRS in complex with tRNA and with small substrates and describe the molecular details of enzymatic recognition of the key tRNA identity elements in the acceptor stem and the anticodon loop. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Translation elongation and termination |
| + |
tRNA(Gly) | up-regulates quantity
precursor of
|
Gly-tRNA(Gly) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270483 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 24898252 |
Aminoacyl-tRNA synthetases are an ancient enzyme family that specifically charges tRNA molecules with cognate amino acids for protein synthesis. Glycyl- tRNA synthetase (GlyRS) is one of the most intriguing aminoacyl-tRNA synthetases due to its divergent quaternary structure and abnormal charging properties. . In this study we report crystal structures of wild type and mutant hGlyRS in complex with tRNA and with small substrates and describe the molecular details of enzymatic recognition of the key tRNA identity elements in the acceptor stem and the anticodon loop. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
EEF1A2 | up-regulates
relocalization
|
Gly-tRNA(Gly) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269541 |
|
|
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 |
| + |
EEF1A1P5 | up-regulates
relocalization
|
Gly-tRNA(Gly) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269561 |
|
|
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 |
| + |
glycine | up-regulates quantity
precursor of
|
Gly-tRNA(Gly) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270484 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 24898252 |
Aminoacyl-tRNA synthetases are an ancient enzyme family that specifically charges tRNA molecules with cognate amino acids for protein synthesis. Glycyl- tRNA synthetase (GlyRS) is one of the most intriguing aminoacyl-tRNA synthetases due to its divergent quaternary structure and abnormal charging properties. . In this study we report crystal structures of wild type and mutant hGlyRS in complex with tRNA and with small substrates and describe the molecular details of enzymatic recognition of the key tRNA identity elements in the acceptor stem and the anticodon loop. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
Gly-tRNA(Gly)