+ |
ROCK1 | down-regulates
phosphorylation
|
KCNK3 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-176025 |
Ser336 |
IPRDLSTsDTCVEQS |
Homo sapiens |
|
pmid |
sentence |
21838752 |
Task1 channels contain two putative rho kinase phosphorylation sites, ser(336) and ser(393) . Mutation of ser(393) rendered task1 channels insensitive to et(a) - or et(b)-mediated current inhibition. In contrast, removal of ser(336) selectively attenuated et(a) -dependent task1 regulation without affecting the et(b) pathway. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
ROCK1 | up-regulates activity
phosphorylation
|
KCNK3 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-176029 |
Ser393 |
GLMKRRSsV |
Homo sapiens |
|
pmid |
sentence |
21838752 |
Task1 channels contain two putative rho kinase phosphorylation sites, ser(336) and ser(393) . Mutation of ser(393) rendered task1 channels insensitive to et(a) - or et(b)-mediated current inhibition. In contrast, removal of ser(336) selectively attenuated et(a) -dependent task1 regulation without affecting the et(b) pathway. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
RPS6KA3 | up-regulates activity
phosphorylation
|
KCNK3 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-172470 |
Ser393 |
GLMKRRSsV |
Homo sapiens |
|
pmid |
sentence |
21357689 |
The chaperone protein, 14-3-3, binds to a critical phosphorylated serine in the channel c termini of k2p3.1 and k2p9.1 (ser(393) and ser(373), respectively) and overcomes retention in the endoplasmic reticulum by ?COP. We sought to identify the kinase responsible for phosphorylation of the terminal serine in human and rat variants of k2p3.1 and k2p9.1. Adopting a bioinformatic approach, three candidate protein kinases were identified: camp-dependent protein kinase, ribosomal s6 kinase, and protein kinase c. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PRKACA | up-regulates activity
phosphorylation
|
KCNK3 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-172430 |
Ser393 |
GLMKRRSsV |
Homo sapiens |
|
pmid |
sentence |
21357689 |
Mutation of the ser393 to alanine, which can neither be phosphorylated nor mimic a phosphorylated residue, resulted in the channel failing to pass current all of our findings support the conclusion that camp-dependent protein kinase is responsible for the phosphorylation of the terminal serine in both k2p3.1 and k2p9.1. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PRKCE | down-regulates activity
phosphorylation
|
KCNK3 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276431 |
Thr383 |
TGLHSLStFRGLMKR |
in vitro |
|
pmid |
sentence |
23229553 |
We have previously shown that carbamylated PAF-induced repolarization abnormalities result from the protein kinase C (PKC) ε-dependent phosphorylation of the two-pore domain potassium channel TASK-1. Further studies identified threonine 383 in the C terminus of human and canine TASK-1 as the phosphorylation site required for PAF-dependent inhibition of the channel. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
halothane | up-regulates activity
chemical activation
|
KCNK3 |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-257846 |
|
|
Mus musculus |
|
pmid |
sentence |
20519544 |
We further demonstrate that TASK channels are required for normal sensitivity to immobilizing effects of halothane and isoflurane and to sedative/hypnotic effects of halothane. |
|
Publications: |
1 |
Organism: |
Mus Musculus |