Kcnmb1

Potassium large conductance calcium-activated channel, subfamily M, beta member 1

Identifiers

KCNMB1; K(VCA)beta; SLO-BETA; hslo-beta

External IDs

OMIM: 603951 MGI: 1334203 HomoloGene: 3054 ChEMBL: 5078 GeneCards: KCNMB1 Gene

Gene Ontology
Molecular function	• ion channel activity • potassium channel activity • calcium-activated potassium channel activity • potassium channel regulator activity
Cellular component	• plasma membrane • voltage-gated potassium channel complex • integral to membrane
Biological process	• ion transport • potassium ion transport • synaptic transmission • blood coagulation • response to calcium ion • potassium ion transmembrane transport
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 5:
169.81 – 169.82 Mb

Chr 11:
33.86 – 33.87 Mb

PubMed search

[1]

[2]

Calcium-activated potassium channel subunit beta-1 is a protein that in humans is encoded by the KCNMB1 gene.^[1]^[2]^[3]

MaxiK channels are large conductance, voltage and calcium-sensitive potassium channels which are fundamental to the control of smooth muscle tone and neuronal excitability. MaxiK channels can be formed by 2 subunits: the pore-forming alpha subunit and the product of this gene, the modulatory beta subunit. Intracellular calcium regulates the physical association between the alpha and beta subunits.^[3]

References [link]

^ Tseng-Crank J, Godinot N, Johansen TE, Ahring PK, Strobaek D, Mertz R, Foster CD, Olesen SP, Reinhart PH (Oct 1996). "Cloning, expression, and distribution of a Ca(2+)-activated K+ channel beta-subunit from human brain". Proc Natl Acad Sci U S A 93 (17): 9200–5. DOI:10.1073/pnas.93.17.9200. PMC 38619. PMID 8799178. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=38619.
^ Jiang Z, Wallner M, Meera P, Toro L (Mar 1999). "Human and rodent MaxiK channel beta-subunit genes: cloning and characterization". Genomics 55 (1): 57–67. DOI:10.1006/geno.1998.5627. PMID 9888999.
^ ^a ^b "Entrez Gene: KCNMB1 potassium large conductance calcium-activated channel, subfamily M, beta member 1". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3779.

Further reading [link]

Orio P, Rojas P, Ferreira G, Latorre R (2002). "New disguises for an old channel: MaxiK channel beta-subunits". News Physiol. Sci. 17: 156–61. PMID 12136044.
Knaus HG, Folander K, Garcia-Calvo M et al. (1994). "Primary sequence and immunological characterization of beta-subunit of high conductance Ca(2+)-activated K+ channel from smooth muscle". J. Biol. Chem. 269 (25): 17274–8. PMID 8006036.
Meera P, Wallner M, Jiang Z, Toro L (1996). "A calcium switch for the functional coupling between alpha (hslo) and beta subunits (KV,Ca beta) of maxi K channels". FEBS Lett. 382 (1–2): 84–8. DOI:10.1016/0014-5793(96)00151-2. PMID 8612769.
Dworetzky SI, Boissard CG, Lum-Ragan JT et al. (1996). "Phenotypic alteration of a human BK (hSlo) channel by hSlobeta subunit coexpression: changes in blocker sensitivity, activation/relaxation and inactivation kinetics, and protein kinase A modulation". J. Neurosci. 16 (15): 4543–50. PMID 8764643.
Valverde MA, Rojas P, Amigo J et al. (1999). "Acute activation of Maxi-K channels (hSlo) by estradiol binding to the beta subunit". Science 285 (5435): 1929–31. DOI:10.1126/science.285.5435.1929. PMID 10489376.
Meera P, Wallner M, Toro L (2000). "A neuronal β subunit (KCNMB4) makes the large conductance, voltage- and Ca2+-activated K+ channel resistant to charybdotoxin and iberiotoxin". Proc. Natl. Acad. Sci. U.S.A. 97 (10): 5562–7. DOI:10.1073/pnas.100118597. PMC 25868. PMID 10792058. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=25868.
Jin P, Weiger TM, Wu Y, Levitan IB (2002). "Phosphorylation-dependent functional coupling of hSlo calcium-dependent potassium channel and its hbeta 4 subunit". J. Biol. Chem. 277 (12): 10014–20. DOI:10.1074/jbc.M107682200. PMID 11790768.
Greenwood IA, Miller LJ, Ohya S, Horowitz B (2002). "The large conductance potassium channel beta-subunit can interact with and modulate the functional properties of a calcium-activated chloride channel, CLCA1". J. Biol. Chem. 277 (25): 22119–22. DOI:10.1074/jbc.C200215200. PMID 11994272.
Gollasch M, Tank J, Luft FC et al. (2002). "The BK channel beta1 subunit gene is associated with human baroreflex and blood pressure regulation". J. Hypertens. 20 (5): 927–33. DOI:10.1097/00004872-200205000-00028. PMID 12011654.
Jin P, Weiger TM, Levitan IB (2003). "Reciprocal modulation between the alpha and beta 4 subunits of hSlo calcium-dependent potassium channels". J. Biol. Chem. 277 (46): 43724–9. DOI:10.1074/jbc.M205795200. PMID 12223479.
Mazzone JN, Kaiser RA, Buxton IL (2003). "Calcium-activated potassium channel expression in human myometrium: effect of pregnancy". Proc. West. Pharmacol. Soc. 45: 184–6. PMID 12434576.
Strausberg RL, Feingold EA, Grouse LH et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. DOI:10.1073/pnas.242603899. PMC 139241. PMID 12477932. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
Kudlacek PE, Pluznick JL, Ma R et al. (2003). "Role of hbeta1 in activation of human mesangial BK channels by cGMP kinase". Am. J. Physiol. Renal Physiol. 285 (2): F289–94. DOI:10.1152/ajprenal.00046.2003. PMID 12670831.
Qian X, Magleby KL (2003). "β1 subunits facilitate gating of BK channels by acting through the Ca2+, but not the Mg2+, activating mechanisms". Proc. Natl. Acad. Sci. U.S.A. 100 (17): 10061–6. DOI:10.1073/pnas.1731650100. PMC 187764. PMID 12893878. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=187764.
Ransom CB, Liu X, Sontheimer H (2004). "Current transients associated with BK channels in human glioma cells". J. Membr. Biol. 193 (3): 201–13. DOI:10.1007/s00232-003-2019-7. PMID 12962281.
Hartness ME, Brazier SP, Peers C et al. (2004). "Post-transcriptional control of human maxiK potassium channel activity and acute oxygen sensitivity by chronic hypoxia". J. Biol. Chem. 278 (51): 51422–32. DOI:10.1074/jbc.M309463200. PMID 14522958.
Fernández-Fernández JM, Tomás M, Vázquez E et al. (2004). "Gain-of-function mutation in the KCNMB1 potassium channel subunit is associated with low prevalence of diastolic hypertension". J. Clin. Invest. 113 (7): 1032–9. DOI:10.1172/JCI200420347. PMC 379324. PMID 15057310. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=379324.

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This article incorporates text from the United States National Library of Medicine, which is in the public domain.

Membrane transport protein: ion channels (TC 1A)

Ca²⁺: Calcium channel

Voltage-gated	L-type/Ca_vα (1.1, 1.2, 1.3, 1.4) · N-type/Ca_vα2.2 · P-type/Ca_vα(2.1) · Q-type/Ca_vα2.1 · R-type/Ca_vα2.3 · T-type/Ca_vα(3.1, 3.2, 3.3) α₂δ-subunits (1, 2) · β-subunits (β1, β2, β3, β4) · γ-subunits (γ1, γ2, γ3, γ4) Cation channels of sperm (1, 2, 3, 4) · Two-pore channel (1, 2)

Ligand-gated	Inositol trisphosphate receptor (1, 2, 3) · Ryanodine receptor (1, 2, 3)

Na⁺: Sodium channel

Constitutively active	Epithelial sodium channel (α, β, γ, δ)

Proton gated	Amiloride-sensitive cation channel (1, 2, 3, 4)

Voltage-gated	Na_vα (1.1, 1.2, 1.3, 1.4, 1.5, 1.6, 1.7, 1.8, 1.9, 7A) · Na_vβ (1, 2, 3, 4)

K⁺: Potassium channel

Voltage-gated	K_vα1-6 (1.1, 1.2, 1.3, 1.4, 1.5, 1.6, 1.7, 1.8) · (2.1, 2.2) · (3.1, 3.2, 3.3, 3.4) · (4.1, 4.2, 4.3) · (5.1) · (6.1, 6.2, 6.3, 6.4) K_vα7-12 (7.1, 7.2, 7.3, 7.4, 7.5) · (8.1, 8.2) · (9.1, 9.2, 9.3) · (10.1, 10.2) · (11.1/hERG, 11.2, 11.3) · (12.1, 12.2, 12.3) K_vβ (1, 2, 3) · KCNIP (1, 2, 3, 4) · minK/ISK · minK/ISK-like · MiRP (1, 2, 3) · Shaker gene

Calcium-activated	BK channel (α1, β1, β2, β3, β4) · SK channel (SK1, SK2, SK3) · IK channel (IK1) · K_Ca (1.1, 2.1, 2.2, 2.3, 3.1, 4.1, 4.2, 5.1)

Inward-rectifier	K_ATP · K_ir (1.1, 2.1, 2.2, 2.3, 2.4, 2.6) · GIRK/K_ir (3.1, 3.2, 3.3, 3.4) · K_ir (4.1, 4.2, 5.1, 6.1, 6.2, 7.1)

Tandem pore domain	K2P (1, 2, 3, 4, 5, 6, 7, 9, 10, 12, 13, 15, 16, 17, 18)

Other

Cl^-: Chloride channel	ANO1 · Bestrophin (1, 2) · CFTR · CLCA (1, 2, 3, 4) · CLCN (1, 2, 3, 4, 5, 6, 7, KA, KB) · CLIC (1, 2, 3, 4, 5, 6, L1) · CLNS (1A, 1B)

H⁺: Voltage-gated	HVCN1

M⁺: TRP cation channel	TRPA (1) · TRPC (1, 2, 3, 4, 4AP, 5, 6, 7) · TRPM (1, 2, 3, 4, 5, 6, 7, 8) · TRPML (1, 2, 3) · TRPN · TRPP (1, 2) · TRPV (1, 2, 3, 4, 5, 6)

Cyclic nucleotide-gated (FC)	α (1, 2, 3, 4) · β (1, 2, 3) · HCN (1, 2, 3, 4)

Porin	Aquaporin (0, 1, 2, 3, 4, 5, 6, 7, 8, 9) · Voltage-dependent anion channel (1, 2, 3) · General bacterial porin family

Gap junction	Connexin: A (GJA1, GJA3, GJA4, GJA5, GJA8, GJA9, GJA10) · B (GJB1, GJB2, GJB3, GJB4, GJB5, GJB6, GJB7) · C (GJC1, GJC2, GJC3) · D (GJD2, GJD3, GJD4)) Innexin

General	Ligand-gated ion channel · Voltage-gated ion channel · Stretch-activated ion channel

see also disorders
B memb: cead, trns (1A, 1C, 1F, 2A, 3A1, 3A2-3, 3D), othr

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References [link]

Further reading [link]

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