KCNMB1

KCNMB1

Identifiers

KCNMB1, BKbeta1, K(VCA)beta, SLO-BETA, hbeta1, hslo-beta, k(VCA)beta-1, slo-beta-1, potassium calcium-activated channel subfamily M regulatory beta subunit 1

External IDs

OMIM: 603951 MGI: 1334203 HomoloGene: 3054 GeneCards: KCNMB1

Gene location (Human)

Chr.	Chromosome 5 (human)^[1]

Band	5q35.1	Start	170,374,671 bp^[1]
Band	5q35.1	End	170,389,634 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 11 (mouse)^[2]

Band	11\|11 A4	Start	33,913,013 bp^[2]
Band	11\|11 A4	End	33,923,641 bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

popliteal artery

right coronary artery

seminal vesicula

saphenous vein

thoracic aorta

ascending aorta

myometrium

left coronary artery

gastric mucosa

urethra

Top expressed in

ascending aorta

aortic valve

sphenoid bone

Meckel's cartilage

humerus

fibula

scapula

lesser wing of sphenoid bone

basisphenoid

More reference expression data

BioGPS


More reference expression data

Gene ontology
Molecular function	calcium-activated potassium channel activity potassium channel regulator activity
Cellular component	integral component of membrane voltage-gated potassium channel complex plasma membrane membrane
Biological process	detection of calcium ion response to calcium ion potassium ion transport ion transport chemical synaptic transmission human ageing cellular response to hypoxia cellular response to bile acid positive regulation of potassium ion transmembrane transport cellular response to ethanol potassium ion transmembrane transport
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


3779


16533

Ensembl


ENSG00000145936


ENSMUSG00000020155

UniProt


Q16558


Q8CAE3

RefSeq (mRNA)


NM_004137


NM_031169

RefSeq (protein)


NP_004128


NP_112446

Location (UCSC)

Chr 5: 170.37 – 170.39 Mb

Chr 11: 33.91 – 33.92 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

Calcium-activated potassium channel subunit beta-1 is a protein that in humans is encoded by the KCNMB1 gene.^[5]^[6]^[7]

Function

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.^[7] Beta subunits (beta 1-4) are highly tissue specific in their expression, with beta-1 being present predominantly on vascular smooth muscle. Endothelial cells are not known to express beta-1 subunits. Beta-1 is also known to be expressed in urinary bladder and in some regions of the brain. Association of the beta-1 subunit with the BK channel increases the apparent Ca²⁺ sensitivity of the channel and decreases voltage dependence.^[8]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000145936 - Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000020155 - Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Tseng-Crank J, Godinot N, Johansen TE, Ahring PK, Strøbaek D, Mertz R, Foster CD, Olesen SP, Reinhart PH (Aug 1996). "Cloning, expression, and distribution of a Ca(2+)-activated K+ channel beta-subunit from human brain". Proceedings of the National Academy of Sciences of the United States of America. 93 (17): 9200–5. Bibcode:1996PNAS...93.9200T. doi:10.1073/pnas.93.17.9200. PMC 38619. PMID 8799178.
^ Jiang Z, Wallner M, Meera P, Toro L (Jan 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".
^ Tano, J.-Y.; Gollasch, M. (2014). "Hypoxia and ischemia-reperfusion: a BiK contribution?". AJP: Heart and Circulatory Physiology. 307 (6): H811–H817. doi:10.1152/ajpheart.00319.2014. ISSN 0363-6135. PMID 25015960.

Orio P, Rojas P, Ferreira G, Latorre R (Aug 2002). "New disguises for an old channel: MaxiK channel beta-subunits". News in Physiological Sciences. 17 (4): 156–61. doi:10.1152/nips.01387.2002. hdl:10533/173696. PMID 12136044.
Knaus HG, Folander K, Garcia-Calvo M, Garcia ML, Kaczorowski GJ, Smith M, Swanson R (Jun 1994). "Primary sequence and immunological characterization of beta-subunit of high conductance Ca(2+)-activated K+ channel from smooth muscle". The Journal of Biological Chemistry. 269 (25): 17274–8. doi:10.1016/S0021-9258(17)32551-6. PMID 8006036.
Meera P, Wallner M, Jiang Z, Toro L (Mar 1996). "A calcium switch for the functional coupling between alpha (hslo) and beta subunits (KV,Ca beta) of maxi K channels". FEBS Letters. 382 (1–2): 84–8. doi:10.1016/0014-5793(96)00151-2. PMID 8612769. S2CID 81684849.
Dworetzky SI, Boissard CG, Lum-Ragan JT, McKay MC, Post-Munson DJ, Trojnacki JT, Chang CP, Gribkoff VK (Aug 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". The Journal of Neuroscience. 16 (15): 4543–50. doi:10.1523/JNEUROSCI.16-15-04543.1996. PMC 6579031. PMID 8764643.
Valverde MA, Rojas P, Amigo J, Cosmelli D, Orio P, Bahamonde MI, Mann GE, Vergara C, Latorre R (Sep 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 (May 2000). "A neuronal beta subunit (KCNMB4) makes the large conductance, voltage- and Ca2+-activated K+ channel resistant to charybdotoxin and iberiotoxin". Proceedings of the National Academy of Sciences of the United States of America. 97 (10): 5562–7. Bibcode:2000PNAS...97.5562M. doi:10.1073/pnas.100118597. PMC 25868. PMID 10792058.
Jin P, Weiger TM, Wu Y, Levitan IB (Mar 2002). "Phosphorylation-dependent functional coupling of hSlo calcium-dependent potassium channel and its hbeta 4 subunit". The Journal of Biological Chemistry. 277 (12): 10014–20. doi:10.1074/jbc.M107682200. PMID 11790768.
Greenwood IA, Miller LJ, Ohya S, Horowitz B (Jun 2002). "The large conductance potassium channel beta-subunit can interact with and modulate the functional properties of a calcium-activated chloride channel, CLCA1". The Journal of Biological Chemistry. 277 (25): 22119–22. doi:10.1074/jbc.C200215200. PMID 11994272.
Gollasch M, Tank J, Luft FC, Jordan J, Maass P, Krasko C, Sharma AM, Busjahn A, Bähring S (May 2002). "The BK channel beta1 subunit gene is associated with human baroreflex and blood pressure regulation". Journal of Hypertension. 20 (5): 927–33. doi:10.1097/00004872-200205000-00028. PMID 12011654. S2CID 88440283.
Jin P, Weiger TM, Levitan IB (Nov 2002). "Reciprocal modulation between the alpha and beta 4 subunits of hSlo calcium-dependent potassium channels". The Journal of Biological Chemistry. 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". Proceedings of the Western Pharmacology Society. 45: 184–6. PMID 12434576.
Kudlacek PE, Pluznick JL, Ma R, Padanilam B, Sansom SC (Aug 2003). "Role of hbeta1 in activation of human mesangial BK channels by cGMP kinase". American Journal of Physiology. Renal Physiology. 285 (2): F289-94. doi:10.1152/ajprenal.00046.2003. PMID 12670831. S2CID 3238002.
Qian X, Magleby KL (Aug 2003). "Beta1 subunits facilitate gating of BK channels by acting through the Ca2+, but not the Mg2+, activating mechanisms". Proceedings of the National Academy of Sciences of the United States of America. 100 (17): 10061–6. Bibcode:2003PNAS..10010061Q. doi:10.1073/pnas.1731650100. PMC 187764. PMID 12893878.
Ransom CB, Liu X, Sontheimer H (Jun 2003). "Current transients associated with BK channels in human glioma cells". The Journal of Membrane Biology. 193 (3): 201–13. doi:10.1007/s00232-003-2019-7. PMID 12962281. S2CID 20169684.
Hartness ME, Brazier SP, Peers C, Bateson AN, Ashford ML, Kemp PJ (Dec 2003). "Post-transcriptional control of human maxiK potassium channel activity and acute oxygen sensitivity by chronic hypoxia". The Journal of Biological Chemistry. 278 (51): 51422–32. doi:10.1074/jbc.M309463200. PMID 14522958.
Fernández-Fernández JM, Tomás M, Vázquez E, Orio P, Latorre R, Sentí M, Marrugat J, Valverde MA (Apr 2004). "Gain-of-function mutation in the KCNMB1 potassium channel subunit is associated with low prevalence of diastolic hypertension" (PDF). The Journal of Clinical Investigation. 113 (7): 1032–9. doi:10.1172/JCI20347. PMC 379324. PMID 15057310.
Leo MD, Bannister JP, Narayanan D, Nair A, Grubbs JE, Gabrick KS, Boop FA, Jaggar JH (Feb 2014). "Dynamic regulation of β1 subunit trafficking controls vascular contractility". Proceedings of the National Academy of Sciences of the United States of America. 111 (6): 2361–6. Bibcode:2014PNAS..111.2361L. doi:10.1073/pnas.1317527111. PMC 3926029. PMID 24464482.
Kuntamallappanavar G, Toro L, Dopico AM (2014). "Both transmembrane domains of BK β1 subunits are essential to confer the normal phenotype of β1-containing BK channels". PLOS ONE. 9 (10): e109306. Bibcode:2014PLoSO...9j9306K. doi:10.1371/journal.pone.0109306. PMC 4183656. PMID 25275635.

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

Ligand-gated	Inositol trisphosphate receptor 1 2 3 Ryanodine receptor 1 2 3
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

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

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
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)

Miscellaneous

Cl⁻: Chloride channel	Calcium-activated chloride channels Anoctamin ANO1 Bestrophin 1 2 Chloride Channel Accessory 1 2 3 4 CFTR CLCN 1 2 3 4 5 6 7 KA KB CLIC 1 2 3 4 5 6 L1 CLNS 1A 1B
H⁺: Proton channel	HVCN1
M⁺: CNG cation channel	α 1 2 3 4 β 1 2 3 HCN FC 1 2 3 4
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
H₂O (+ solutes): Porin	Aquaporin 0 1 2 3 4 5 6 7 8 9 Voltage-dependent anion channel 1 2 3 General bacterial porin family
Cytoplasm: 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

By gating mechanism

Ion channel class	Ligand-gated Light-gated Voltage-gated Stretch-activated

see also disorders

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This page was last edited on 3 December 2023, at 15:57

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Function

See also

References

Further reading