| + |
WARS1 | down-regulates quantity 
chemical modification
|
tryptophan |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270510 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 14660560 |
Aminoacyl-tRNA synthetases (aaRSs)1 are a family of ancient enzymes that catalyze amino acid activation by ATP and the subsequent aminoacylation to its cognate tRNA. Alternative splicing produces two forms of hTrpRS in human cells: full-length hTrpRS (residues 1-471) and mini-hTrpRS (residues 48-471) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
tryptophan | up-regulates quantity 
|
AminoAcids |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264743 |
|
|
|
|
| pmid |
sentence |
| 29259120 |
All extant life employs the same 20 amino acids for protein biosynthesis |
|
| Publications: |
1 |
| + |
TPH2 | down-regulates quantity
chemical modification
|
tryptophan |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264011 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 31024440 |
In serotonergic neurons Trp serves as the precursor for 5-HT. The 5-HT metabolic pathway is initiated by Trp being hydroxylated to the intermediate 5-hydroxytryptophan (5-HTP), which is subsequently decarboxylated to become 5-HT|Thus, the rate limiting step in the biosynthesis of 5-HT is the hydroxylation of Trp which is catalyzed by the enzyme tryptophan hydroxylase (TPH) (Figure 1). This enzyme is specific for 5-HT producing cells, however, it is present in two different isoforms, TPH1 and TPH2 [reviewed in (22, 23)]. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
tryptophan | up-regulates quantity
precursor of
|
Trp-tRNA(Trp) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270516 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 14660560 |
Aminoacyl-tRNA synthetases (aaRSs)1 are a family of ancient enzymes that catalyze amino acid activation by ATP and the subsequent aminoacylation to its cognate tRNA. Alternative splicing produces two forms of hTrpRS in human cells: full-length hTrpRS (residues 1-471) and mini-hTrpRS (residues 48-471) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SLC36A4 | up-regulates quantity
relocalization
|
tryptophan |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264735 |
|
|
Xenopus laevis |
|
| pmid |
sentence |
| 21097500 |
HPAT4 in Xenopus oocytes mediated sodium-independent, electroneutral uptake of [(3)H]proline, with the highest rate of uptake when the uptake medium pH was 7.4 and an affinity of 3.13 μM. Tryptophan was also an excellently transported substrate with a similarly high affinity (1.72 μM). |
|
| Publications: |
1 |
Organism: |
Xenopus Laevis |
| + |
TPH1 | down-regulates quantity
chemical modification
|
tryptophan |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264009 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 31024440 |
In serotonergic neurons Trp serves as the precursor for 5-HT. The 5-HT metabolic pathway is initiated by Trp being hydroxylated to the intermediate 5-hydroxytryptophan (5-HTP), which is subsequently decarboxylated to become 5-HT|Thus, the rate limiting step in the biosynthesis of 5-HT is the hydroxylation of Trp which is catalyzed by the enzyme tryptophan hydroxylase (TPH) (Figure 1). This enzyme is specific for 5-HT producing cells, however, it is present in two different isoforms, TPH1 and TPH2 [reviewed in (22, 23)]. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
tryptophan