+ |
PRKD1 | up-regulates activity
phosphorylation
|
ATP7B |
0.301 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272295 |
Ser1121 |
AHSERPLsAPASHLN |
Homo sapiens |
Hep-G2 Cell |
pmid |
sentence |
21189263 |
ATP7B trafficking was markedly reduced by the Ser-478/481/1121/1453 to Ala mutation. We conclude that PKD plays a key role in copper-dependent serine phosphorylation, permitting high levels of ATP7B protein expression and trafficking. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272294 |
Ser1453 |
DDDGDKWsLLLNGRD |
Homo sapiens |
Hep-G2 Cell |
pmid |
sentence |
21189263 |
ATP7B trafficking was markedly reduced by the Ser-478/481/1121/1453 to Ala mutation. We conclude that PKD plays a key role in copper-dependent serine phosphorylation, permitting high levels of ATP7B protein expression and trafficking. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272296 |
Ser478 |
APDILAKsPQSTRAV |
Homo sapiens |
Hep-G2 Cell |
pmid |
sentence |
21189263 |
ATP7B trafficking was markedly reduced by the Ser-478/481/1121/1453 to Ala mutation. We conclude that PKD plays a key role in copper-dependent serine phosphorylation, permitting high levels of ATP7B protein expression and trafficking. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272293 |
Ser481 |
ILAKSPQsTRAVAPQ |
Homo sapiens |
Hep-G2 Cell |
pmid |
sentence |
21189263 |
ATP7B trafficking was markedly reduced by the Ser-478/481/1121/1453 to Ala mutation. We conclude that PKD plays a key role in copper-dependent serine phosphorylation, permitting high levels of ATP7B protein expression and trafficking. |
|
Publications: |
4 |
Organism: |
Homo Sapiens |
+ |
ATP7B | up-regulates quantity
relocalization
|
copper(1+) |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272297 |
|
|
|
|
pmid |
sentence |
24706876 |
WD is caused by mutations in ATP7B, a transporter that loads Cu(I) onto newly synthesized cupro-enzymes in the trans-Golgi network (TGN) and exports excess copper out of cells by trafficking from the TGN to the plasma membrane. |
|
Publications: |
1 |