+ |
PRKCB | down-regulates
phosphorylation
|
KCNC4 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-58498 |
Ser15 |
SSYRGRKsGNKPPSK |
Homo sapiens |
|
pmid |
sentence |
9649584 |
This study investigated the molecular physiology of the nh2-terminal phosphorylation sites that regulate inactivation gating of an a-type k+ channel. The main results show that: (a) pkc acts on four phosphate acceptors (s8, s9, s15, and s21) within the inactivation domain because mutation of these residues to alanine is necessary and sufficient to remove the action of pkc on channel inactivation. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-35622 |
Ser15 |
SSYRGRKsGNKPPSK |
Homo sapiens |
|
pmid |
sentence |
7993631 |
We found that pkc specifically eliminates rapid inactivation of a cloned human a-type k+ channel (hkv3.4), converting this channel from a rapidly inactivating a type to a noninactivating delayed rectifier type. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-58502 |
Ser21 |
KSGNKPPsKTCLKEE |
Homo sapiens |
|
pmid |
sentence |
9649584 |
This study investigated the molecular physiology of the nh2-terminal phosphorylation sites that regulate inactivation gating of an a-type k+ channel. The main results show that: (a) pkc acts on four phosphate acceptors (s8, s9, s15, and s21) within the inactivation domain because mutation of these residues to alanine is necessary and sufficient to remove the action of pkc on channel inactivation. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-35626 |
Ser21 |
KSGNKPPsKTCLKEE |
Homo sapiens |
|
pmid |
sentence |
7993631 |
We found that pkc specifically eliminates rapid inactivation of a cloned human a-type k+ channel (hkv3.4), converting this channel from a rapidly inactivating a type to a noninactivating delayed rectifier type. |
|
Publications: |
4 |
Organism: |
Homo Sapiens |
+ |
KCNC4 | down-regulates quantity
relocalization
|
potassium(1+) |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-265588 |
|
|
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 |