| + |
OAT | up-regulates quantity 
chemical modification
|
proline |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256033 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 14617280 |
Arginase generates ornithine, an aminoacid that can be further metabolized to proline via ornithine aminotransferase and to polyamines via ornithine decarboxylase (ODC) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
proline | up-regulates quantity
precursor of
|
Pro-tRNA(Pro) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270434 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 28271488 |
Aminoacyl-tRNA synthetases (AARSs) are essential enzymes that specifically aminoacylate one tRNA molecule by the cognate amino acid. In mammals, nine synthetases, those specific for amino acids Arg, Asp, Gln, Glu, Ile, Leu, Lys, Met and Pro, associate into a multi-aminoacyl-tRNA synthetase complex, an association which is believed to play a key role in the cellular organization of translation, but also in the regulation of the translational and nontranslational functions of these enzymes. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
proline | up-regulates quantity
|
AminoAcids |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264744 |
|
|
|
|
| pmid |
sentence |
| 29259120 |
All extant life employs the same 20 amino acids for protein biosynthesis |
|
| Publications: |
1 |
| + |
SLC36A2 | up-regulates quantity
relocalization
|
proline |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264742 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12748860 |
Both PAT1 and PAT2 mediate 1:1 symport of protons and small neutral amino acids such as glycine, alanine, and proline.|The first member of the SLC36 family, present in both intracellular and plasma membranes, was identified independently as a lysosomal amino acid transporter (LYAAT1) responsible for the export of lysosomal proteolysis products into the cytosol and as a proton/amino acid transporter (PAT1) responsible for the absorption of amino acids in the gut. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SLC36A1 | up-regulates quantity
relocalization
|
proline |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264741 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12748860 |
Both PAT1 and PAT2 mediate 1:1 symport of protons and small neutral amino acids such as glycine, alanine, and proline.|The first member of the SLC36 family, present in both intracellular and plasma membranes, was identified independently as a lysosomal amino acid transporter (LYAAT1) responsible for the export of lysosomal proteolysis products into the cytosol and as a proton/amino acid transporter (PAT1) responsible for the absorption of amino acids in the gut. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SLC36A4 | up-regulates quantity
relocalization
|
proline |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264736 |
|
|
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 |
| + |
proline | up-regulates 
|
ECM_synthesis |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255550 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 25386178 |
Ornithine, via the enzyme OAT, is also a precursor amino acid for the synthesis of proline, which itself is essential for the synthesis of collagen. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Multiaminoacyl-tRNA synthetase | down-regulates quantity 
chemical modification
|
proline |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270429 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 28271488 |
Aminoacyl-tRNA synthetases (AARSs) are essential enzymes that specifically aminoacylate one tRNA molecule by the cognate amino acid. In mammals, nine synthetases, those specific for amino acids Arg, Asp, Gln, Glu, Ile, Leu, Lys, Met and Pro, associate into a multi-aminoacyl-tRNA synthetase complex, an association which is believed to play a key role in the cellular organization of translation, but also in the regulation of the translational and nontranslational functions of these enzymes. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
proline