| + |
STK39 | up-regulates activity 
phosphorylation
|
SLC12A1 |
0.596 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276305 |
Ser130 |
GPKVNRPsLLEIHEQ |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 21321328 |
We establish that the SPAK and OSR1 kinases activated by WNK interact with an RFQV motif on NKCC2 and directly phosphorylate Thr95, Thr100, Thr105 and, possibly, Ser91.Using these phosphorylation-specific antibodies we establish that hypotonic low-chloride stimulation induces marked phosphorylation of overexpressed NKCC2 in HEK-293 cells at Ser91, Thr100, Thr105 and Ser130 (Fig. 3A). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263130 |
Ser91 |
ASFHAYDsHTNTYYL |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 21321328 |
We establish that the SPAK and OSR1 kinases activated by WNK interact with an RFQV motif on NKCC2 and directly phosphorylate Thr95, Thr100, Thr105 and, possibly, Ser91. Our data indicate that a SPAK-OSR1-independent kinase, perhaps AMP-activated protein kinase (AMPK), phosphorylates Ser130 and that phosphorylation of Thr105 and Ser130 plays the most important roles in stimulating NKCC2 activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276308 |
Ser91 |
ASFHAYDsHTNTYYL |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 21321328 |
We establish that the SPAK and OSR1 kinases activated by WNK interact with an RFQV motif on NKCC2 and directly phosphorylate Thr95, Thr100, Thr105 and, possibly, Ser91.Using these phosphorylation-specific antibodies we establish that hypotonic low-chloride stimulation induces marked phosphorylation of overexpressed NKCC2 in HEK-293 cells at Ser91, Thr100, Thr105 and Ser130 (Fig. 3A). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263129 |
Thr100 |
TNTYYLQtFGHNTMD |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 21321328 |
We establish that the SPAK and OSR1 kinases activated by WNK interact with an RFQV motif on NKCC2 and directly phosphorylate Thr95, Thr100, Thr105 and, possibly, Ser91. Our data indicate that a SPAK-OSR1-independent kinase, perhaps AMP-activated protein kinase (AMPK), phosphorylates Ser130 and that phosphorylation of Thr105 and Ser130 plays the most important roles in stimulating NKCC2 activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276307 |
Thr100 |
TNTYYLQtFGHNTMD |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 21321328 |
We establish that the SPAK and OSR1 kinases activated by WNK interact with an RFQV motif on NKCC2 and directly phosphorylate Thr95, Thr100, Thr105 and, possibly, Ser91.Using these phosphorylation-specific antibodies we establish that hypotonic low-chloride stimulation induces marked phosphorylation of overexpressed NKCC2 in HEK-293 cells at Ser91, Thr100, Thr105 and Ser130 (Fig. 3A). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263131 |
Thr105 |
LQTFGHNtMDAVPKI |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 21321328 |
We establish that the SPAK and OSR1 kinases activated by WNK interact with an RFQV motif on NKCC2 and directly phosphorylate Thr95, Thr100, Thr105 and, possibly, Ser91. Our data indicate that a SPAK-OSR1-independent kinase, perhaps AMP-activated protein kinase (AMPK), phosphorylates Ser130 and that phosphorylation of Thr105 and Ser130 plays the most important roles in stimulating NKCC2 activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276306 |
Thr105 |
LQTFGHNtMDAVPKI |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 21321328 |
We establish that the SPAK and OSR1 kinases activated by WNK interact with an RFQV motif on NKCC2 and directly phosphorylate Thr95, Thr100, Thr105 and, possibly, Ser91.Using these phosphorylation-specific antibodies we establish that hypotonic low-chloride stimulation induces marked phosphorylation of overexpressed NKCC2 in HEK-293 cells at Ser91, Thr100, Thr105 and Ser130 (Fig. 3A). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263132 |
Thr95 |
AYDSHTNtYYLQTFG |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 21321328 |
We establish that the SPAK and OSR1 kinases activated by WNK interact with an RFQV motif on NKCC2 and directly phosphorylate Thr95, Thr100, Thr105 and, possibly, Ser91. Our data indicate that a SPAK-OSR1-independent kinase, perhaps AMP-activated protein kinase (AMPK), phosphorylates Ser130 and that phosphorylation of Thr105 and Ser130 plays the most important roles in stimulating NKCC2 activity. |
|
| Publications: |
8 |
Organism: |
Homo Sapiens |
| + |
PRKCQ | up-regulates activity
phosphorylation
|
STK39 |
0.464 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276006 |
Ser309 |
MMKKYGKsFRKLLSL |
in vitro |
|
| pmid |
sentence |
| 14988727 |
Recombinant SPAK was phosphorylated on Ser-311 in its kinase domain by PKCtheta, but not by PKCalpha. This synergistic activity, as well as the receptor-induced SPAK activation, required the PKCtheta-interacting region of SPAK, and Ser-311 mutation greatly reduced these activities of SPAK. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276007 |
Ser323 |
LCLQKDPsKRPTAAE |
in vitro |
|
| pmid |
sentence |
| 14988727 |
Recombinant SPAK was phosphorylated on Ser-311 in its kinase domain by PKCtheta, but not by PKCalpha. This synergistic activity, as well as the receptor-induced SPAK activation, required the PKCtheta-interacting region of SPAK, and Ser-311 mutation greatly reduced these activities of SPAK. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
WNK1 | up-regulates
phosphorylation
|
STK39 |
0.457 |
| 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-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-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 |
| + |
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 |
| + |
STK39 | down-regulates activity 
phosphorylation
|
SLC12A6 |
0.587 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276597 |
Ser96 |
IEDLSQNsITGEHSQ |
in vitro |
|
| pmid |
sentence |
| 24043619 |
We observed that in vitro activated STE20/SPS1-related proline/alanine-rich kinase (SPAK) complexed to its regulatory MO25 subunit phosphorylated KCC3 at Ser-96 and that in Xenopus laevis oocytes Ser-96 of human KCC3 is phosphorylated in isotonic conditions and becomes dephosphorylated during incubation in hypotonicity, leading to a dramatic increase in KCC3 function. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
STK39 | down-regulates activity
phosphorylation
|
SLC12A3 |
0.499 |
| 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 |
| + |
STK39 | up-regulates activity
phosphorylation
|
SLC12A2 |
0.62 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264642 |
|
|
|
|
| pmid |
sentence |
| 16990453 |
This phosphorylation event activates PASK, which in turn phosphorylates and activates NKCC1 |
|
| Publications: |
1 |
| + |
STK39 | down-regulates activity
phosphorylation
|
CFTR |
0.352 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263134 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 21317537 |
SPAK phosphorylates the transporters to reduce their surface expression and thus their activity and consequently inhibits ductal secretion to stabilize the resting state. PP1 reverses the effect of SPAK. Molecular analysis revealed that the WNK kinases acted as scaffolds to recruit SPAK, which phosphorylated CFTR and NBCe1-B, reducing their cell surface expression. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264643 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 21317537 |
WNK kinases acted as scaffolds to recruit SPAK, which phosphorylated CFTR and NBCe1-B, reducing their cell surface expression. IRBIT opposed the effects of WNKs and SPAK by recruiting PP1 to the complex to dephosphorylate CFTR and NBCe1-B, restoring their cell surface expression, |
|
| Publications: |
2 |
Organism: |
Homo Sapiens, Mus Musculus |
| Tissue: |
Pancreas |
| + |
STK39 | down-regulates activity
phosphorylation
|
SLC4A4 |
0.355 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264644 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 21317537 |
WNK kinases acted as scaffolds to recruit SPAK, which phosphorylated CFTR and NBCe1-B, reducing their cell surface expression. IRBIT opposed the effects of WNKs and SPAK by recruiting PP1 to the complex to dephosphorylate CFTR and NBCe1-B, restoring their cell surface expression, |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263133 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 21317537 |
SPAK phosphorylates the transporters to reduce their surface expression and thus their activity and consequently inhibits ductal secretion to stabilize the resting state. PP1 reverses the effect of SPAK. Molecular analysis revealed that the WNK kinases acted as scaffolds to recruit SPAK, which phosphorylated CFTR and NBCe1-B, reducing their cell surface expression. |
|
| Publications: |
2 |
Organism: |
Mus Musculus, Homo Sapiens |
| Tissue: |
Pancreas |
| + |
AATK | down-regulates 
|
STK39 |
0.349 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-152921 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17267545 |
Taken together, our data are consistent with aatyk1 indirectly inhibiting the spak/wnk4 activation of the cotransporter by scaffolding an inhibitory phosphatase in proximity to a stimulatory kinase. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
STK39 | up-regulates
binding
|
MAPK14 |
0.369 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-118848 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 14563843 |
Spak, a ste20/sps1-related kinase that activates the p38 pathway. p38, one of the three major mapks, can be coimmunoprecipitated with spak and with nkcc1 in an activity-dependent manner. The amount of p38 coimmunoprecipitated with the kinase and the cotransporter significantly decreases upon cellular stress, |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-81541 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10980603 |
Spak, a ste20/sps1-related kinase that activates the p38 pathway. p38, one of the three major mapks, can be coimmunoprecipitated with spak and with nkcc1 in an activity-dependent manner. The amount of p38 coimmunoprecipitated with the kinase and the cotransporter significantly decreases upon cellular stress, |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Tissue: |
Brain |
3.0
STK39
- 
- 