+ |
PRKCD | up-regulates activity
phosphorylation
|
KCNE3 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-275964 |
Ser82 |
LILGYTRsRKVDKRS |
|
|
pmid |
sentence |
21911611 |
Currents mediated by the complex formed by KCNQ1 and the mutant KCNE3-S82A β-subunit (mutation of the site for PKCdelta-promoted phosphorylation and modulation of the activity of KCNE3) showed rapid run-down and insensitivity to E2. |
|
Publications: |
1 |
+ |
KCNE3 | down-regulates quantity
relocalization
|
potassium(1+) |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-265589 |
|
|
Homo sapiens |
|
pmid |
sentence |
11506885 |
Kv3 currents are activated specifically during action potential repolarization. Analysis of the Kv3 subfamily of K+ channel subunits has lead to the discovery of a new class of neuronal voltage-gated K+ channels characterized by positively shifted voltage dependencies and very fast deactivation rates. These properties are adaptations that allow these channels to produce currents that can specifically enable fast repolarization of action potentials without compromising spike initiation or height |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
KCNE3 | up-regulates activity
binding
|
KCNQ1 |
0.648 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-275923 |
|
|
|
|
pmid |
sentence |
21911611 |
Sexual dimorphism and oestrogen regulation of KCNE3 expression modulates the functional properties of KCNQ1 K⁺ channels|The KCNQ1 potassium channel associates with various KCNE ancillary subunits that drastically affect channel gating and pharmacology. Co-assembly with KCNE3 produces a current with nearly instantaneous activation |
|
Publications: |
1 |