KCNAB1 — Potassium voltage-gated channel subfamily A regulatory beta subunit 1
KCNAB1 belongs to a gene co-expression module in 1 of 28 SCUBA cell types. Each module groups genes that rise and fall together in that cell type; the genes it shares a module with are its closest co-expression partners there.
KCNAB1's module in each cell type
| Cell type | Module | Shares the module with | |
|---|---|---|---|
| Smooth muscle cells | Vascular SMC Identity Contractility | ADIRF, ARPC1A, BCAM, CCDC3, CRIP1, EFHD1, GPRC5C, GPX3 +10 more | View in SCUBA |
About the gene
| Synonyms | AKR6A3, hKvb3, hKvBeta3, KCNA1B, Kvb1.3 |
|---|---|
| Chromosome | 3: 156037701-156539138 |
| Predicted location | Intracellular |
| Essential gene | No |
| Protein class | Predicted intracellular proteins, Transporters |
| Molecular function | Oxidoreductase |
| Biological process | Ion transport, Potassium transport, Transport |
Function
Regulatory subunit of the voltage-gated potassium (Kv) Shaker channels composed of pore-forming and potassium-conducting alpha subunits and of regulatory beta subunits. The beta-1/KCNAB1 cytoplasmic subunit mediates closure of delayed rectifier potassium channels by physically obstructing the pore via its N- terminal domain and increases the speed of channel closure for other family members. Promotes the inactivation of Kv1.1/KCNA1, Kv1.2/KCNA2, Kv1.4/KCNA4, Kv1.5/KCNA5 and Kv1.6/KCNA6 alpha subunit-containing channels. Displays nicotinamide adenine dinucleotide phosphate (NADPH)-dependent aldoketoreductase activity by catalyzing the NADPH- dependent reduction of a variety of endogenous aldehydes and ketones (By similarity). The binding of NADPH is required for efficient down- regulation of potassium channel activity. Oxidation of the bound NADPH restrains N-terminal domain from blocking the channel, thereby decreasing N-type inactivation of potassium channel activity (By similarity). Isoform KvB1.2 shows no effect on KCNA1, KCNA2 or KCNB1.
Human Protein Atlas · Open Targets · UniProt
Gene annotation from the Human Protein Atlas and UniProt; see sources & licences.