+ |
RAB12 | down-regulates quantity by destabilization
relocalization
|
SLC36A4 |
0.457 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-264763 |
|
|
Mus musculus |
MEF Cell |
pmid |
sentence |
23478338 |
We also found that Rab12 promotes constitutive degradation of PAT4 (proton‐coupled amino‐acid transporter 4|Rab12 regulates lysosomal localization or degradation of amino‐acid transporters. |
|
Publications: |
1 |
Organism: |
Mus Musculus |
+ |
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 |
+ |
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 |