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Open Access Articles- Top Results for KCNAB2

KCNAB2

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Identifiers
SymbolsKCNAB2 ; AKR6A5; HKvbeta2; HKvbeta2.1; HKvbeta2.2; KCNA2B; KV-BETA-2
External IDsOMIM601142 MGI109239 HomoloGene56492 GeneCards: KCNAB2 Gene
RNA expression pattern
File:PBB GE KCNAB2 211791 s at tn.png
File:PBB GE KCNAB2 203402 at tn.png
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez851416498
EnsemblENSG00000069424ENSMUSG00000028931
UniProtQ13303P62482
RefSeq (mRNA)NM_001199860NM_001252654
RefSeq (protein)NP_001186789NP_001239583
Location (UCSC)Chr 1:
6.05 – 6.16 Mb
Chr 4:
152.39 – 152.48 Mb
PubMed search[1][2]

Voltage-gated potassium channel subunit beta-2 is a protein that in humans is encoded by the KCNAB2 gene.[1][2]

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.[2]

In melanocytic cells KCNAB2 gene expression may be regulated by MITF.[3]

Interactions

KCNAB2 has been shown to interact with KCNA2.[4][5]

See also

References

  1. ^ 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. PMID 8838324. doi:10.1006/geno.1996.0065. 
  2. ^ a b "Entrez Gene: KCNAB2 potassium voltage-gated channel, shaker-related subfamily, beta member 2". 
  3. ^ Hoek KS, Schlegel NC, Eichhoff OM, Widmer DS, Praetorius C, Einarsson SO et al. (2008). "Novel MITF targets identified using a two-step DNA microarray strategy". Pigment Cell Melanoma Res. 21 (6): 665–76. PMID 19067971. doi:10.1111/j.1755-148X.2008.00505.x. 
  4. ^ Coleman SK, Newcombe J, Pryke J, Dolly JO (Aug 1999). "Subunit composition of Kv1 channels in human CNS". J. Neurochem. 73 (2): 849–58. PMID 10428084. doi:10.1046/j.1471-4159.1999.0730849.x. 
  5. ^ 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. PMID 8636142. doi:10.1074/jbc.271.12.7084. 

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. PMID 7649300. doi:10.1016/0014-5793(95)00785-8. 
  • McCormack T, McCormack K (1995). "Shaker K+ channel beta subunits belong to an NAD(P)H-dependent oxidoreductase superfamily.". Cell 79 (7): 1133–5. PMID 8001150. doi:10.1016/0092-8674(94)90004-3. 
  • 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. PMID 8636142. doi:10.1074/jbc.271.12.7084. 
  • Kääb S, Dixon J, Duc J, Ashen D, Näbauer M, Beuckelmann DJ et al. (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. PMID 9760292. doi:10.1161/01.cir.98.14.1383. 
  • Coleman SK, Newcombe J, Pryke J, Dolly JO (1999). "Subunit composition of Kv1 channels in human CNS.". J. Neurochem. 73 (2): 849–58. PMID 10428084. doi:10.1046/j.1471-4159.1999.0730849.x. 
  • Poliak S, Gollan L, Martinez R, Custer A, Einheber S, Salzer JL et al. (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. PMID 10624965. doi:10.1016/S0896-6273(00)81049-1. 
  • 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. PMID 12431995. doi:10.1074/jbc.M205162200. 
  • 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. PMID 12893943. doi:10.1126/science.1086998. 
  • Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ et al. (2005). "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.". Nat. Biotechnol. 23 (1): 94–101. PMID 15592455. doi:10.1038/nbt1046. 
  • Lim J, Hao T, Shaw C, Patel AJ, Szabó G, Rual JF et al. (2006). "A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration.". Cell 125 (4): 801–14. PMID 16713569. doi:10.1016/j.cell.2006.03.032. 
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External links

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

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