| + |
WNK1 | up-regulates 
phosphorylation
|
OXSR1 |
0.496 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-151659 |
Ser325 |
VRRVPGSsGRLHKTE |
Homo sapiens |
|
| pmid |
sentence |
| 17190791 |
Activation of wnk1 coincides with the phosphorylation and activation of two wnk1 substrates, namely, the protein kinases ste20/sps1-related proline alanine-rich kinase (spak) and oxidative stress response kinase-1 (osr1) |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-151663 |
Thr185 |
TRNKVRKtFVGTPCW |
Homo sapiens |
|
| pmid |
sentence |
| 17190791 |
Activation of wnk1 coincides with the phosphorylation and activation of two wnk1 substrates, namely, the protein kinases ste20/sps1-related proline alanine-rich kinase (spak) and oxidative stress response kinase-1 (osr1) |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
WNK1 | up-regulates
phosphorylation
|
STK39 |
0.457 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253553 |
Ser371 |
VRRVPGSsGHLHKTE |
Homo sapiens |
|
| pmid |
sentence |
| 16083423 |
Phosphorylation by WNK1 or WNK4 markedly increased SPAK and OSR1 activity. Phosphopeptide mapping studies demonstrated that WNK1 phosphorylated kinase-inactive SPAK and OSR1 at an equivalent residue located within the T-loop of the catalytic domain (Thr233 in SPAK, Thr185 in OSR1) and a serine residue located within a C-terminal non-catalytic region (Ser373 in SPAK, Ser325 in OSR1) |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-151667 |
Ser371 |
VRRVPGSsGHLHKTE |
Homo sapiens |
|
| pmid |
sentence |
| 17190791 |
Activation of wnk1 coincides with the phosphorylation and activation of two wnk1 substrates, namely, the protein kinases ste20/sps1-related proline alanine-rich kinase (spak) and oxidative stress response kinase-1 (osr1). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-160842 |
Ser371 |
VRRVPGSsGHLHKTE |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 18270262 |
Activation of wnk1 coincides with the phosphorylation and activation of two wnk1 substrates, namely, the protein kinases ste20/sps1-related proline alanine-rich kinase (spak) and oxidative stress response kinase-1 (osr1). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-151671 |
Thr231 |
TRNKVRKtFVGTPCW |
Homo sapiens |
|
| pmid |
sentence |
| 17190791 |
Activation of wnk1 coincides with the phosphorylation and activation of two wnk1 substrates, namely, the protein kinases ste20/sps1-related proline alanine-rich kinase (spak) and oxidative stress response kinase-1 (osr1). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-160846 |
Thr231 |
TRNKVRKtFVGTPCW |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 16083423 |
Phosphorylation by WNK1 or WNK4 markedly increased SPAK and OSR1 activity. Phosphopeptide mapping studies demonstrated that WNK1 phosphorylated kinase-inactive SPAK and OSR1 at an equivalent residue located within the T-loop of the catalytic domain (Thr233 in SPAK, Thr185 in OSR1) and a serine residue located within a C-terminal non-catalytic region (Ser373 in SPAK, Ser325 in OSR1) |
|
| Publications: |
5 |
Organism: |
Homo Sapiens |
| Tissue: |
Kidney |
| + |
WNK2 | up-regulates activity
phosphorylation
|
WNK1 |
0.56 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260790 |
Ser382 |
KRASFAKsVIGTPEF |
Homo sapiens |
|
| pmid |
sentence |
| 22032326 |
WNK1, which is activated in response to osmotic stress by phosphorylation of its T-loop residue (Ser382). | We found that wild-type WNK2 (Figure 8A) or WNK3 (Figure 8B) phosphorylated kinase-inactive WNK1 (1–667, D368A) at Ser382 in vitro. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
WNK1 | up-regulates
phosphorylation
|
WNK1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-160850 |
Ser382 |
KRASFAKsVIGTPEF |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 18270262 |
We demonstrate that wnk1 is rapidly activated and phosphorylated at multiple residues after exposure of cells to hyperosmotic conditions and that activation is mediated by the phosphorylation of its t-loop ser382 residue, possibly triggered by a transautophosphorylation reaction. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-151675 |
Ser382 |
KRASFAKsVIGTPEF |
Homo sapiens |
|
| pmid |
sentence |
| 17190791 |
We finally establish that full-length wnk1, wnk2 and wnk3, but not wnk4, are capable of directly phosphorylating ser382 of wnk1 in vitro. This supports the notion that t-loop phosphorylation of wnk isoforms is controlled by trans-autophosphorylation. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Tissue: |
Kidney |
| + |
WNK1 | up-regulates activity
phosphorylation
|
WNK1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260826 |
Ser382 |
LKRASFAkSVIGTPE |
Homo sapiens |
|
| pmid |
sentence |
| 12374799 |
Activation of WNKs requires autophosphorylation of at least one serine residue, serine 382 in WNK1, within the WNK activation loop. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
WNK3 | up-regulates activity
phosphorylation
|
WNK1 |
0.287 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260789 |
Ser382 |
KRASFAKsVIGTPEF |
Homo sapiens |
|
| pmid |
sentence |
| 22032326 |
We found that wild-type WNK2 (Figure 8A) or WNK3 (Figure 8B) phosphorylated kinase-inactive WNK1 (1–667, D368A) at Ser382 in vitro. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
WNK1 | down-regulates 
phosphorylation
|
SLC12A6 |
0.467 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-187560 |
Thr1048 |
YQEKVHMtWTKDKYM |
Homo sapiens |
Neuron |
| pmid |
sentence |
| 19665974 |
We have attempted to identify kinases and phosphatases involved in the modulation of phosphorylation at kcc3 t991 and t1048. the wnk kinases and spak/osr1 are strong candidates for kcc3 regulatory kinases. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-187564 |
Thr991 |
SAYTYERtLMMEQRS |
Homo sapiens |
Neuron |
| pmid |
sentence |
| 19665974 |
We have attempted to identify kinases and phosphatases involved in the modulation of phosphorylation at kcc3 t991 and t1048. the wnk kinases and spak/osr1 are strong candidates for kcc3 regulatory kinases. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Tissue: |
Brain |
| + |
WNK1 | up-regulates activity
phosphorylation
|
SYT2 |
0.623 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263049 |
Thr199 |
ETKVHRKtLNPAFNE |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 15350218 |
Endogenous WNK1 and Syt2 coimmunoprecipitate and colocalize on a subset of secretory granules in INS-1 cells. Phosphorylation by WNK1 increases the amount of Ca2+ required for Syt2 binding to phospholipid vesicles; mutation of threonine 202, a WNK1 phosphorylation site, partially prevents this change. These findings suggest that phosphorylation of Syts by WNK1 can regulate Ca2+ sensing and the subsequent Ca2+-dependent interactions mediated by Syt C2 domains. . In contrast, WNK1 phosphorylated Syt2 on T202 and T386 within the C2 domains (Figure 6B). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AKT1 | up-regulates
phosphorylation
|
WNK1 |
0.402 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252481 |
Thr60 |
EYRRRRHtMDKDSRG |
Homo sapiens |
|
| pmid |
sentence |
| 16081417 |
Phosphorylation of wnk1 on thr-58 contributes to sgk1 activation. these data suggest that activation of sgk1 by wnk1 requires the catalytic activity of akt. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AKT | up-regulates
phosphorylation
|
WNK1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-139391 |
Thr60 |
EYRRRRHtMDKDSRG |
Homo sapiens |
|
| pmid |
sentence |
| 16081417 |
Phosphorylation of wnk1 on thr-58 contributes to sgk1 activation. these data suggest that activation of sgk1 by wnk1 requires the catalytic activity of akt. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
KLHL2 | down-regulates quantity by destabilization
binding
|
WNK1 |
0.482 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272119 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 23838290 |
We found that KLHL2, as well as KLHL3, was co-immunoprecipitated with all four WNK isoforms. The direct interaction of KLHL2 with WNKs was confirmed on fluorescence correlation spectroscopy. Co-expression of KLHL2 and Cullin3 decreased the abundance of WNK1, WNK3 and WNK4 within HEK293T cells, and a significant increase of WNK4 ubiquitination by KLHL2 and Cullin3 was observed both in HEK293T cells and in an in vitro ubiquitination assay. These results suggest that KLHL2-Cullin3 also functions as an E3-ligase for WNK isoforms within the body. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Cullin 3-RBX1-Skp1 | down-regulates quantity by destabilization
ubiquitination, polyubiquitination
|
WNK1 |
0.328 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272100 |
|
|
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-272124 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 23838290 |
We found that KLHL2, as well as KLHL3, was co-immunoprecipitated with all four WNK isoforms. The direct interaction of KLHL2 with WNKs was confirmed on fluorescence correlation spectroscopy. Co-expression of KLHL2 and Cullin3 decreased the abundance of WNK1, WNK3 and WNK4 within HEK293T cells, and a significant increase of WNK4 ubiquitination by KLHL2 and Cullin3 was observed both in HEK293T cells and in an in vitro ubiquitination assay. These results suggest that KLHL2-Cullin3 also functions as an E3-ligase for WNK isoforms within the body. |
|
| Publications: |
2 |
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 |
3.0
WNK1
- 
- 