| + |
AMPK | up-regulates activity 
phosphorylation
|
SLC12A1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263103 |
Ser122 |
YRNTGSIsGPKVNRP |
Mus musculus |
MMDD1 Cell |
| pmid |
sentence |
| 17341212 |
In the present study, we demonstrate that the metabolic sensing kinase AMPK (AMP-activated protein kinase) phosphorylates NKCC2 on Ser126 in vitro. Activation of AMPK in the MMDD1 (mouse macula densa-derived 1) cell line resulted in an increase in Ser126 phosphorylation in situ, suggesting that AMPK may phosphorylate NKCC2 in vivo. The functional significance of Ser126 phosphorylation was examined by mutating the serine residue to an alanine residue resulting in a marked reduction in co-transporter activity when exogenously expressed in Xenopus laevis oocytes under isotonic conditions. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
OXSR1 | up-regulates activity
phosphorylation
|
SLC12A1 |
0.522 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276309 |
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-276312 |
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-276311 |
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-276310 |
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). |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| + |
STK39 | up-regulates activity
phosphorylation
|
SLC12A1 |
0.604 |
| 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-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-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-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-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-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-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-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 |
| + |
SLC12A1 | up-regulates quantity
phosphorylation
|
chloride |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264635 |
|
|
|
|
| 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 |
| + |
WNK3 | up-regulates activity
phosphorylation
|
SLC12A1 |
0.521 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264626 |
|
|
|
|
| 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 |
3.0
SLC12A1
- 
- 