+ |
PKA | up-regulates activity
phosphorylation
|
KLHL3 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273824 |
Ser433 |
PMNTRRSsVGVGVVE |
in vitro |
|
pmid |
sentence |
26435498 |
Consistent with the fact that S433 is a component of Akt and PKA phosphorylation motifs, in vitro kinase assay demonstrated that Akt and PKA can phosphorylate KLHL3 at S433, that was previously reported to be phosphorylated by PKC. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
AKT | up-regulates activity
phosphorylation
|
KLHL3 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273825 |
Ser433 |
PMNTRRSsVGVGVVE |
in vitro |
|
pmid |
sentence |
26435498 |
Consistent with the fact that S433 is a component of Akt and PKA phosphorylation motifs, in vitro kinase assay demonstrated that Akt and PKA can phosphorylate KLHL3 at S433, that was previously reported to be phosphorylated by PKC. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
PKC | up-regulates quantity by stabilization
phosphorylation
|
KLHL3 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273780 |
Ser433 |
PMNTRRSsVGVGVVE |
Chlorocebus aethiops |
COS-7 Cell |
pmid |
sentence |
25313067 |
We show that KLHL3 is phosphorylated at serine 433 in the Kelch domain (a site frequently mutated in hypertension with hyperkalemia) by protein kinase C in cultured cells and that this phosphorylation prevents WNK4 binding and degradation. |
|
Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
+ |
KLHL3 | up-regulates activity
binding
|
Cullin 3-RBX1-Skp1 |
0.643 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272101 |
|
|
Homo sapiens |
HeLa Cell |
pmid |
sentence |
23387299 |
CUL3 assembles with BTB proteins to form Cullin-RING E3 ubiquitin ligase complexes. To explore how a CUL3-KLHL3 complex might operate, we immunoprecipitated KLHL3 and found that it associated strongly with WNK isoforms and CUL3. These results suggest that the CUL3-KLHL3 E3 ligase complex regulates blood pressure via its ability to interact with and ubiquitylate WNK isoforms. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272106 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
23453970 |
Here, we found that KLHL3 interacted with Cullin3 and WNK4, induced WNK4 ubiquitination, and reduced the WNK4 protein level. The reduced interaction of KLHL3 and WNK4 by PHAII-causing mutations in either protein reduced the ubiquitination of WNK4, resulting in an increased level of WNK4 protein. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
KLHL3 | down-regulates quantity by destabilization
binding
|
WNK4 |
0.604 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272105 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
23453970 |
Here, we found that KLHL3 interacted with Cullin3 and WNK4, induced WNK4 ubiquitination, and reduced the WNK4 protein level. The reduced interaction of KLHL3 and WNK4 by PHAII-causing mutations in either protein reduced the ubiquitination of WNK4, resulting in an increased level of WNK4 protein. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
KLHL3 | down-regulates quantity by destabilization
binding
|
WNK1 |
0.581 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272099 |
|
|
Homo sapiens |
HeLa Cell |
pmid |
sentence |
23387299 |
CUL3 assembles with BTB proteins to form Cullin-RING E3 ubiquitin ligase complexes. To explore how a CUL3-KLHL3 complex might operate, we immunoprecipitated KLHL3 and found that it associated strongly with WNK isoforms and CUL3. These results suggest that the CUL3-KLHL3 E3 ligase complex regulates blood pressure via its ability to interact with and ubiquitylate WNK isoforms. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |