| + |
WNK4 | up-regulates activity 
phosphorylation
|
SLC12A3 |
0.598 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264631 |
Thr50 |
SHLTHSStFCMRTFG |
in vitro |
|
| pmid |
sentence |
| 22342722 |
Threonine 48 was identified as the WNK4 phosphorylation site at mouse NCC|. Thus, WNK4 stimulates NCC in three ways: (1) direct phosphorylation and in turn increasing NCC protein abundance; (2) facilitating the phosphorylation of NCC by SPAK/OSR1 indirectly, and (3) phosphorylating and activating SPAK/OSR1.|Evidences from early studies using Xenopus oocytes and mammalian cells indicate that WNK4 inhibits NCC and PHAII-causing mutations relieve the inhibition |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
STK39 | down-regulates activity 
phosphorylation
|
SLC12A3 |
0.5 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264623 |
Thr55 |
SSTFCMRtFGYNTID |
Mus musculus |
|
| pmid |
sentence |
| 25651566 |
SPAK directly phosphorylates NCC and its effects on NCC are universally associated with phosphorylation|This adds to the evidence that SPAK-mediated phosphorylation acts primarily to increase activity of individual cotransporters without affecting the amount of NCC on the surface| the kinase (SPAK) that phosphorylates NCC at T53 |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
OXSR1 | up-regulates
phosphorylation
|
SLC12A3 |
0.398 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-160833 |
Thr60 |
MRTFGYNtIDVVPTY |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 18270262 |
We demonstrate that the spak and osr1 kinases that are activated by wnk1 phosphorylate human ncc at three conserved residues (thr46, thr55 and thr60) / our results also indicate that phosphorylation of thr60 plays the most crucial role in triggering the activation of ncc in hek293 cells and its mutation also inhibits phosphorylation of the adjacent thr46 and thr55 sites. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Kidney |
| + |
WNK3 | up-regulates activity
phosphorylation
|
SLC12A3 |
0.468 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264624 |
|
|
|
|
| pmid |
sentence |
| 21613606 |
We have shown that with-no-lysine kinase 3 (WNK3) possesses several properties that suggest it could be the Cl−/volume-sensitive regulatory kinase that, in association with protein phosphatases, reciprocally modifies the phosphorylation/dephosphorylation states of the SLC12 proteins and thus their activities|WNK3 activates NKCC1/2 and NCC and inhibits the KCCs |
|
| Publications: |
1 |
| + |
SLC12A3 | up-regulates quantity
phosphorylation
|
chloride |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264633 |
|
|
|
|
| pmid |
sentence |
| 21613606 |
Eukaryotic cells regulate their volume in the long term through the coordinated function of the Na+-coupled chloride (NKCC1/2 and NCC) and K+-coupled chloride (KCC1–4) cotransporters, which encompass two branches of the SLC12|The K+-Cl− cotransporters move chloride outside the cell, are inhibited by phosphorylation, and are activated by dephosphorylation. In contrast, the Na+-K+-2Cl− cotransporters introduce chloride into the cell, are inhibited by dephosphorylation, and are activated by phosphorylation gene family of solute transporters (12). |
|
| Publications: |
1 |
| + |
WNK4 | down-regulates activity 
|
SLC12A3 |
0.598 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264632 |
|
|
|
|
| pmid |
sentence |
| 22342722 |
Evidences from early studies using Xenopus oocytes and mammalian cells indicate that WNK4 inhibits NCC and PHAII-causing mutations relieve the inhibition |
|
| Publications: |
1 |
3.0
SLC12A3
- 
- 