+ |
SGK1 | up-regulates activity
phosphorylation
|
WNK4 |
0.425 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276421 |
Ser1201 |
FPTSRRNsLQRSEPP |
in vitro |
|
pmid |
sentence |
23054253 |
In addition, we identified a novel SGK1 phosphorylation site (S1201) in WNK4, and phosphorylation at this site is reduced by Ca(2+)/CaM. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
WNK4 | down-regulates activity
phosphorylation
|
WNK4 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276871 |
Ser335 |
KRASFAKsVIGTPEF |
in vitro |
|
pmid |
sentence |
25542968 |
Elimination of the catalytic activity (D321A or D321K-K186D) or the autophosphorylation site (S335A) in mutant WNK4-L322F abrogated the positive effect on NCC. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
WNK4 | up-regulates activity
phosphorylation
|
STK39 |
0.521 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-264641 |
Ser371 |
VRRVPGSsGHLHKTE |
|
|
pmid |
sentence |
16990453 |
Vitari et al. (76) and Moriguchi et al. (52) demonstrated that WNK4 bound and phosphorylated PASK at Thr-233 and Ser-373 in mammalian cells.| this phosphorylation event activates PASK, which in turn phosphorylates and activates NKCC1 |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-264640 |
Thr231 |
TRNKVRKtFVGTPCW |
|
|
pmid |
sentence |
16990453 |
Vitari et al. (76) and Moriguchi et al. (52) demonstrated that WNK4 bound and phosphorylated PASK at Thr-233 and Ser-373 in mammalian cells.| this phosphorylation event activates PASK, which in turn phosphorylates and activates NKCC1 |
|
Publications: |
2 |
+ |
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 |
+ |
SRC | down-regulates activity
phosphorylation
|
WNK4 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276897 |
Tyr1113 |
PSPVWMNySYSSLCL |
Homo sapiens |
HEK-293T Cell |
pmid |
sentence |
25805816 |
Using Western blot and mass spectrometry, we now identify three sites in WNK4 that are phosphorylated by c-Src: Tyr(1092), Tyr(1094), and Tyr(1143), and show that both c-Src and protein tyrosine phosphatase type 1D (PTP-1D) coimmunoprecipitate with WNK4. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276895 |
Tyr1115 |
PVWMNYSySSLCLSS |
Homo sapiens |
HEK-293T Cell |
pmid |
sentence |
25805816 |
Using Western blot and mass spectrometry, we now identify three sites in WNK4 that are phosphorylated by c-Src: Tyr(1092), Tyr(1094), and Tyr(1143), and show that both c-Src and protein tyrosine phosphatase type 1D (PTP-1D) coimmunoprecipitate with WNK4. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276896 |
Tyr1164 |
KKEIEDLySRLGKQP |
Homo sapiens |
HEK-293T Cell |
pmid |
sentence |
25805816 |
Using Western blot and mass spectrometry, we now identify three sites in WNK4 that are phosphorylated by c-Src: Tyr(1092), Tyr(1094), and Tyr(1143), and show that both c-Src and protein tyrosine phosphatase type 1D (PTP-1D) coimmunoprecipitate with WNK4. |
|
Publications: |
3 |
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 |
+ |
Cullin 3-RBX1-Skp1 | down-regulates quantity by destabilization
polyubiquitination
|
WNK4 |
0.398 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272107 |
|
|
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. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272123 |
|
|
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 |
+ |
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 |
+ |
KLHL2 | down-regulates quantity by destabilization
binding
|
WNK4 |
0.536 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272118 |
|
|
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 |