+ |
OXSR1 | up-regulates activity
phosphorylation
|
SLC12A1 |
0.517 |
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 |
+ |
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 |
+ |
OXSR1 | up-regulates
phosphorylation
|
SLC12A2 |
0.54 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-90927 |
Thr203 |
HQHYYYDtHTNTYYL |
Homo sapiens |
|
pmid |
sentence |
12145304 |
The secretory na-k-cl cotransporter nkcc1 is activated by secretagogues through a phosphorylation-dependent mechanism. three phosphoacceptor sites were identified in the n-terminal domain of the protein (at thr184, thr189, and thr202) none of these residues occurs in the context of strong consensus sites for known ser/thr kinases. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-146513 |
Thr203 |
HQHYYYDtHTNTYYL |
Homo sapiens |
|
pmid |
sentence |
16669787 |
We have identified three residues in nkcc1 (thr175/thr179/thr184 in shark or thr203/thr207/thr212 in human) that are phosphorylated by spak and osr1 / exposure of hek-293 (human embryonic kidney) cells to osmotic stress, which leads to phosphorylation and activation of nkcc1, increased phosphorylation of nkcc1 at the sites targeted by spak/osr1 |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-146517 |
Thr207 |
YYDTHTNtYYLRTFG |
Homo sapiens |
|
pmid |
sentence |
16669787 |
We have identified three residues in nkcc1 (thr175/thr179/thr184 in shark or thr203/thr207/thr212 in human) that are phosphorylated by spak and osr1 / exposure of hek-293 (human embryonic kidney) cells to osmotic stress, which leads to phosphorylation and activation of nkcc1, increased phosphorylation of nkcc1 at the sites targeted by spak/osr1 |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-90931 |
Thr212 |
TNTYYLRtFGHNTMD |
Homo sapiens |
|
pmid |
sentence |
12145304 |
Oxidative stress-responsive kinase-1 (osr1) is a known upstream regulator of n(k)ccs. these results suggest that, globally, osr1 is involved in the regulation of bp and renal tubular na(+) reabsorption mainly via the activation of nkcc1 and nkcc2. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-146521 |
Thr212 |
TNTYYLRtFGHNTMD |
Homo sapiens |
|
pmid |
sentence |
16669787 |
We have identified three residues in nkcc1 (thr175/thr179/thr184 in shark or thr203/thr207/thr212 in human) that are phosphorylated by spak and osr1 / exposure of hek-293 (human embryonic kidney) cells to osmotic stress, which leads to phosphorylation and activation of nkcc1, increased phosphorylation of nkcc1 at the sites targeted by spak/osr1 |
|
Publications: |
5 |
Organism: |
Homo Sapiens |
+ |
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 |
+ |
OXSR1 | down-regulates activity
phosphorylation
|
PAK1 |
0.39 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250210 |
Thr84 |
LPSDFEHtIHVGFDA |
Homo sapiens |
HeLa Cell |
pmid |
sentence |
14707132 |
OSR1 phosphorylated threonine 84 in the N-terminal regulatory domain of PAK1. phosphorylation of PAK1 by OSR1 desensitizes PAK1 to activation by small G proteins, providing a modulatory input to PAK1 activity. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |