SCUBA

KCNE3 — Potassium voltage-gated channel subfamily E regulatory subunit 3

KCNE3 belongs to a gene co-expression module in 3 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.

KCNE3's module in each cell type

Cell typeModuleShares the module with
EndothelialInflammatory Stress Response
Inflammation
ADI1, APLN, ARL6IP1, ARL6IP4, CCDC88A, DAP, GPR68, HEBP2 +11 moreView in SCUBA
Goblet cellsInflammatory Goblet Remodeling
Stress
C2CD4A, CLCA1, COL16A1, FMOD, GALNT8, GPX2, IFITM2, LYZ +3 moreView in SCUBA
MacrophagesRetromer Endosomal Sorting
Vesicular traficking
ABHD15, ARHGAP45, ARHGAP9, CNPY3, CRBN, CTSO, DAB2, DRAM2 +20 moreView in SCUBA

About the gene

SynonymsHOKPP, MiRP2
Chromosome11: 74454841-74467729
Predicted locationIntracellular, Membrane
Essential geneNo
Protein classDisease related genes, Human disease related genes, Potential drug targets, Predicted intracellular proteins, Predicted membrane proteins, Transporters
Biological processIon transport, Potassium transport, Transport

Function

Ancillary protein that functions as a regulatory subunit of the voltage-gated potassium (Kv) channel complex composed of pore- forming and potassium-conducting alpha subunits and of regulatory beta subunits. KCNE3 beta subunit modulates the gating kinetics and enhances stability of the channel complex. Alters the gating of the delayed rectifier Kv channel containing KCNB1 alpha subunit. Associates with KCNC4/Kv3.4 alpha subunit to form the subthreshold Kv channel in skeletal muscle and to establish the resting membrane potential (RMP) in muscle cells. Association with KCNQ1/KCLQT1 alpha subunit may form the intestinal cAMP-stimulated potassium channel involved in chloride secretion that produces a current with nearly instantaneous activation with a linear current-voltage relationship (By similarity).

Human Protein Atlas · Open Targets · UniProt

Gene annotation from the Human Protein Atlas and UniProt; see sources & licences.