KCNAB2

KCNAB2
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1ZSX
Identifiers
Aliases	KCNAB2, AKR6A5, HKvbeta2, HKvbeta2.1, HKvbeta2.2, KCNA2B, KV-BETA-2, potassium voltage-gated channel subfamily A regulatory beta subunit 2
External IDs	OMIM: 601142; MGI: 109239; HomoloGene: 56492; GeneCards: KCNAB2; OMA:KCNAB2 - orthologs
Gene location (Human) Chr. Chromosome 1 (human)[1] Band 1p36.31 Start 5,990,927 bp[1] End 6,101,193 bp[1]
Gene location (Mouse) Chr. Chromosome 4 (mouse)[2] Band 4 E2|4 83.08 cM Start 152,475,199 bp[2] End 152,562,367 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in Brodmann area 10 right frontal lobe pons cingulate gyrus anterior cingulate cortex granulocyte Brodmann area 9 nucleus accumbens amygdala spinal ganglia Top expressed in dentate gyrus of hippocampal formation granule cell neural layer of retina superior frontal gyrus hippocampus proper primary visual cortex primary motor cortex pontine nuclei lateral geniculate nucleus anterior horn of spinal cord medial geniculate nucleus More reference expression data BioGPS More reference expression data
Gene ontology Molecular function aldo-keto reductase (NADP) activity voltage-gated ion channel activity potassium channel regulator activity voltage-gated potassium channel activity oxidoreductase activity Cellular component axon terminus cytoplasm integral component of membrane cytosol cell projection membrane postsynaptic density extrinsic component of cytoplasmic side of plasma membrane voltage-gated potassium channel complex plasma membrane synapse axon cell junction pinceau fiber neuron projection microtubule cytoskeleton juxtaparanode region of axon specific granule membrane tertiary granule membrane Biological process NADPH oxidation regulation of protein localization to cell surface regulation of ion transmembrane transport ion transport potassium ion transport neuromuscular process hematopoietic progenitor cell differentiation potassium ion transmembrane transport regulation of potassium ion transmembrane transport neutrophil degranulation ion transmembrane transport Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 8514 16498 Ensembl ENSG00000069424 ENSMUSG00000028931 UniProt Q13303 P62482 RefSeq (mRNA) NM_001199860 NM_001199861 NM_001199862 NM_001199863 NM_003636 NM_172130 NM_001252654 NM_001252655 NM_001252656 NM_010598 NM_001355172 NM_001355173 RefSeq (protein) NP_001186789 NP_001186790 NP_001186791 NP_001186792 NP_003627 NP_742128 NP_001186789.1 NP_001186790.1 NP_003627.1 NP_001239583 NP_001239584 NP_001239585 NP_034728 NP_001342101 NP_001342102 Location (UCSC) Chr 1: 5.99 – 6.1 Mb Chr 4: 152.48 – 152.56 Mb PubMed search [3] [4]
Wikidata
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Voltage-gated potassium channel subunit beta-2 is a protein that in humans is encoded by the KCNAB2 gene.^[5][6]

Function

Voltage-gated potassium (Kv) channels represent the most complex class of voltage-gated ion channels from both functional and structural standpoints. Their diverse functions include regulating neurotransmitter release, heart rate, insulin secretion, neuronal excitability, epithelial electrolyte transport, smooth muscle contraction, and cell volume. Four sequence-related potassium channel genes - shaker, shaw, shab, and shal - have been identified in Drosophila, and each has been shown to have human homolog(s). This gene encodes a member of the potassium channel, voltage-gated, shaker-related subfamily. This member is one of the beta subunits, which are auxiliary proteins associating with functional Kv-alpha subunits. This member alters functional properties of the KCNA4 gene product. Alternative splicing of this gene results in two transcript variants encoding distinct isoforms.^[6]

In melanocytic cells KCNAB2 gene expression may be regulated by MITF.^[7]

Interactions

KCNAB2 has been shown to interact with KCNA2.^[8][9]

See also

• Voltage-gated potassium channel

References

1. GRCh38: Ensembl release 89: ENSG00000069424 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000028931 – Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Schultz D, Litt M, Smith L, Thayer M, McCormack K (Mar 1997). "Localization of two potassium channel beta subunit genes, KCNA1B and KCNA2B". Genomics. 31 (3): 389–91. doi:10.1006/geno.1996.0065. PMID 8838324.
6. "Entrez Gene: KCNAB2 potassium voltage-gated channel, shaker-related subfamily, beta member 2".
7. Hoek KS, Schlegel NC, Eichhoff OM, Widmer DS, Praetorius C, Einarsson SO, Valgeirsdottir S, Bergsteinsdottir K, Schepsky A, Dummer R, Steingrimsson E (2008). "Novel MITF targets identified using a two-step DNA microarray strategy". Pigment Cell Melanoma Res. 21 (6): 665–76. doi:10.1111/j.1755-148X.2008.00505.x. PMID 19067971.
8. Coleman SK, Newcombe J, Pryke J, Dolly JO (Aug 1999). "Subunit composition of Kv1 channels in human CNS". J. Neurochem. 73 (2): 849–58. doi:10.1046/j.1471-4159.1999.0730849.x. PMID 10428084.
9. Nakahira K, Shi G, Rhodes KJ, Trimmer JS (Mar 1996). "Selective interaction of voltage-gated K+ channel beta-subunits with alpha-subunits". J. Biol. Chem. 271 (12): 7084–9. doi:10.1074/jbc.271.12.7084. PMID 8636142.

Further reading

• McCormack K, McCormack T, Tanouye M, Rudy B, Stühmer W (1995). "Alternative splicing of the human Shaker K+ channel beta 1 gene and functional expression of the beta 2 gene product". FEBS Lett. 370 (1–2): 32–6. Bibcode:1995FEBSL.370...32M. doi:10.1016/0014-5793(95)00785-8. PMID 7649300.
• McCormack T, McCormack K (1995). "Shaker K+ channel beta subunits belong to an NAD(P)H-dependent oxidoreductase superfamily". Cell. 79 (7): 1133–5. doi:10.1016/0092-8674(94)90004-3. PMID 8001150. S2CID 10080280.
• Nakahira K, Shi G, Rhodes KJ, Trimmer JS (1996). "Selective interaction of voltage-gated K+ channel beta-subunits with alpha-subunits". J. Biol. Chem. 271 (12): 7084–9. doi:10.1074/jbc.271.12.7084. PMID 8636142.
• Kääb S, Dixon J, Duc J, Ashen D, Näbauer M, Beuckelmann DJ, Steinbeck G, McKinnon D, Tomaselli GF (1998). "Molecular basis of transient outward potassium current downregulation in human heart failure: a decrease in Kv4.3 mRNA correlates with a reduction in current density". Circulation. 98 (14): 1383–93. doi:10.1161/01.cir.98.14.1383. PMID 9760292.
• Coleman SK, Newcombe J, Pryke J, Dolly JO (1999). "Subunit composition of Kv1 channels in human CNS". J. Neurochem. 73 (2): 849–58. doi:10.1046/j.1471-4159.1999.0730849.x. PMID 10428084.
• Poliak S, Gollan L, Martinez R, Custer A, Einheber S, Salzer JL, Trimmer JS, Shrager P, Peles E (2000). "Caspr2, a new member of the neurexin superfamily, is localized at the juxtaparanodes of myelinated axons and associates with K+ channels". Neuron. 24 (4): 1037–47. doi:10.1016/S0896-6273(00)81049-1. PMID 10624965. S2CID 12444497.
• Croci C, Brändstatter JH, Enz R (2003). "ZIP3, a new splice variant of the PKC-zeta-interacting protein family, binds to GABAC receptors, PKC-zeta, and Kv beta 2". J. Biol. Chem. 278 (8): 6128–35. doi:10.1074/jbc.M205162200. PMID 12431995.
• Gu C, Jan YN, Jan LY (2003). "A conserved domain in axonal targeting of Kv1 (Shaker) voltage-gated potassium channels". Science. 301 (5633): 646–9. Bibcode:2003Sci...301..646G. doi:10.1126/science.1086998. PMID 12893943. S2CID 9924760.
• Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ (2005). "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells". Nat. Biotechnol. 23 (1): 94–101. doi:10.1038/nbt1046. PMID 15592455. S2CID 7200157.
• Lim J, Hao T, Shaw C, Patel AJ, Szabó G, Rual JF, Fisk CJ, Li N, Smolyar A, Hill DE, Barabási AL, Vidal M, Zoghbi HY (2006). "A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration". Cell. 125 (4): 801–14. doi:10.1016/j.cell.2006.03.032. PMID 16713569. S2CID 13709685.

External links

• KCNAB2+protein,+human at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

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