Voltage-gated potassium channel subunit beta-1

Details

Name
Voltage-gated potassium channel subunit beta-1
Synonyms
  • 1.1.1.-
  • K(+) channel subunit beta-1
  • KCNA1B
  • Kv-beta-1
Gene Name
KCNAB1
Organism
Humans
Amino acid sequence
>lcl|BSEQ0052265|Voltage-gated potassium channel subunit beta-1
MLAARTGAAGSQISEENTKLRRQSGFSVAGKDKSPKKASENAKDSSLSPSGESQLRARQL
ALLREVEMNWYLKLCDLSSEHTTVCTTGMPHRNLGKSGLRVSCLGLGTWVTFGGQISDEV
AERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVITTKLYWGGKAETE
RGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTS
RWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLAC
GIISGKYGNGVPESSRASLKCYQWLKERIVSEEGRKQQNKLKDLSPIAERLGCTLPQLAV
AWCLRNEGVSSVLLGSSTPEQLIENLGAIQVLPKMTSHVVNEIDNILRNKPYSKKDYRS
Number of residues
419
Molecular Weight
46563.13
Theoretical pI
Not Available
GO Classification
Functions
aldo-keto reductase (NADP) activity / ion channel binding / NADPH binding / potassium channel regulator activity / protein domain specific binding / voltage-gated potassium channel activity
Processes
brain development / diaphragm development / heart development / learning or memory / myoblast differentiation / negative regulation of delayed rectifier potassium channel activity / negative regulation of voltage-gated potassium channel activity / oxidation-reduction process / potassium ion transport / regulation of delayed rectifier potassium channel activity / regulation of potassium ion transmembrane transport / skeletal muscle tissue development
Components
cytosol / dendrite cytoplasm / extrinsic component of cytoplasmic side of plasma membrane / juxtaparanode region of axon / perikaryon / plasma membrane / potassium channel complex / proximal dendrite / voltage-gated potassium channel complex
General Function
Cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits (PubMed:7499366, PubMed:7603988, PubMed:17156368,PubMed:17540341, PubMed:19713757). Modulates action potentials via its effect on the pore-forming alpha subunits (By similarity). Promotes expression of the pore-forming alpha subunits at the cell membrane, and thereby increases channel activity (By similarity). Mediates closure of delayed rectifier potassium channels by physically obstructing the pore via its N-terminal domain and increases the speed of channel closure for other family members (PubMed:9763623). Promotes the closure of KCNA1, KCNA2 and KCNA5 channels (PubMed:7499366, PubMed:7890032, PubMed:7603988, PubMed:7649300, PubMed:8938711, PubMed:12077175, PubMed:12130714, PubMed:15361858, PubMed:17540341, PubMed:19713757). Accelerates KCNA4 channel closure (PubMed:7890032, PubMed:7649300, PubMed:7890764, PubMed:9763623). Accelerates the closure of heteromeric channels formed by KCNA1 and KCNA4 (PubMed:17156368). Accelerates the closure of heteromeric channels formed by KCNA2, KCNA5 and KCNA6 (By similarity). Isoform KvB1.2 has no effect on KCNA1, KCNA2 or KCNB1 (PubMed:7890032, PubMed:7890764). Enhances KCNB1 and KCNB2 channel activity (By similarity). Binds NADPH; this is required for efficient down-regulation of potassium channel activity (PubMed:17540341). Has NADPH-dependent aldoketoreductase activity (By similarity). Oxidation of the bound NADPH strongly decreases N-type inactivation of potassium channel activity (By similarity).
Specific Function
Aldo-keto reductase (nadp) activity
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0052266|Voltage-gated potassium channel subunit beta-1 (KCNAB1)
ATGCTGGCAGCCCGGACAGGGGCAGCGGGGAGTCAGATCTCAGAGGAGAACACCAAGTTA
AGGAGACAGTCTGGGTTTTCTGTAGCAGGGAAAGACAAATCTCCCAAGAAAGCCTCAGAA
AACGCTAAAGACAGCAGCCTTAGTCCCTCAGGGGAAAGCCAGCTCAGGGCGCGTCAACTG
GCTCTGCTGCGCGAAGTGGAGATGAACTGGTACCTAAAGCTCTGCGACCTGTCCAGCGAG
CACACCACCGTCTGCACCACAGGCATGCCGCACAGGAATCTTGGAAAATCAGGACTCAGA
GTTTCTTGCTTGGGTCTTGGAACATGGGTGACATTTGGAGGTCAAATTTCAGATGAGGTT
GCTGAACGGCTGATGACCATCGCCTATGAAAGTGGTGTTAACCTCTTTGATACTGCCGAA
GTCTATGCTGCTGGAAAGGCTGAAGTGATTCTGGGGAGCATCATCAAGAAGAAAGGCTGG
AGGAGGTCCAGTCTGGTCATAACAACCAAACTCTACTGGGGTGGAAAAGCTGAAACAGAA
AGAGGGCTGTCAAGAAAGCATATTATTGAAGGATTGAAGGGCTCCCTCCAGAGGCTGCAG
CTCGAGTATGTGGATGTGGTCTTTGCAAATCGACCGGACAGTAACACTCCCATGGAAGAA
ATTGTCCGAGCCATGACACATGTGATAAACCAAGGCATGGCGATGTACTGGGGCACCTCG
AGATGGAGTGCTATGGAGATCATGGAAGCCTATTCTGTAGCAAGACAGTTCAATATGATC
CCACCGGTCTGTGAACAAGCTGAGTACCATCTTTTCCAGAGAGAGAAAGTGGAGGTCCAG
CTGCCAGAGCTCTACCACAAAATAGGTGTTGGCGCAATGACATGGTCTCCACTTGCCTGT
GGAATCATCTCAGGAAAATACGGAAACGGGGTGCCTGAAAGTTCCAGGGCTTCACTGAAG
TGCTACCAGTGGTTGAAAGAAAGAATTGTAAGTGAAGAAGGGAGAAAACAGCAAAACAAG
CTAAAAGACCTTTCCCCAATTGCGGAGCGTCTGGGATGCACACTACCTCAGCTAGCTGTT
GCGTGGTGCCTGAGAAATGAAGGTGTGAGTTCTGTGCTCCTGGGATCATCCACTCCTGAA
CAACTCATTGAAAACCTTGGTGCCATTCAGGTTCTCCCAAAGATGACATCACATGTGGTA
AATGAGATTGATAACATACTGCGCAACAAGCCCTACAGCAAGAAGGACTATAGATCATAA
Chromosome Location
3
Locus
3q25.31
External Identifiers
ResourceLink
UniProtKB IDQ14722
UniProtKB Entry NameKCAB1_HUMAN
HGNC IDHGNC:6228
General References
  1. England SK, Uebele VN, Kodali J, Bennett PB, Tamkun MM: A novel K+ channel beta-subunit (hKv beta 1.3) is produced via alternative mRNA splicing. J Biol Chem. 1995 Dec 1;270(48):28531-4. doi: 10.1074/jbc.270.48.28531. [Article]
  2. Majumder K, De Biasi M, Wang Z, Wible BA: Molecular cloning and functional expression of a novel potassium channel beta-subunit from human atrium. FEBS Lett. 1995 Mar 13;361(1):13-6. doi: 10.1016/0014-5793(95)00120-x. [Article]
  3. England SK, Uebele VN, Shear H, Kodali J, Bennett PB, Tamkun MM: Characterization of a voltage-gated K+ channel beta subunit expressed in human heart. Proc Natl Acad Sci U S A. 1995 Jul 3;92(14):6309-13. doi: 10.1073/pnas.92.14.6309. [Article]
  4. McCormack K, McCormack T, Tanouye M, Rudy B, Stuhmer W: Alternative splicing of the human Shaker K+ channel beta 1 gene and functional expression of the beta 2 gene product. FEBS Lett. 1995 Aug 14;370(1-2):32-6. doi: 10.1016/0014-5793(95)00785-8. [Article]
  5. Leicher T, Roeper J, Weber K, Wang X, Pongs O: Structural and functional characterization of human potassium channel subunit beta 1 (KCNA1B). Neuropharmacology. 1996;35(7):787-95. doi: 10.1016/0028-3908(96)00133-5. [Article]
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  8. Morales MJ, Castellino RC, Crews AL, Rasmusson RL, Strauss HC: A novel beta subunit increases rate of inactivation of specific voltage-gated potassium channel alpha subunits. J Biol Chem. 1995 Mar 17;270(11):6272-7. doi: 10.1074/jbc.270.11.6272. [Article]
  9. Accili EA, Kuryshev YA, Wible BA, Brown AM: Separable effects of human Kvbeta1.2 N- and C-termini on inactivation and expression of human Kv1.4. J Physiol. 1998 Oct 15;512 ( Pt 2):325-36. doi: 10.1111/j.1469-7793.1998.325be.x. [Article]
  10. Maylie B, Bissonnette E, Virk M, Adelman JP, Maylie JG: Episodic ataxia type 1 mutations in the human Kv1.1 potassium channel alter hKvbeta 1-induced N-type inactivation. J Neurosci. 2002 Jun 15;22(12):4786-93. [Article]
  11. Williams CP, Hu N, Shen W, Mashburn AB, Murray KT: Modulation of the human Kv1.5 channel by protein kinase C activation: role of the Kvbeta1.2 subunit. J Pharmacol Exp Ther. 2002 Aug;302(2):545-50. [Article]
  12. Bhalla T, Rosenthal JJ, Holmgren M, Reenan R: Control of human potassium channel inactivation by editing of a small mRNA hairpin. Nat Struct Mol Biol. 2004 Oct;11(10):950-6. doi: 10.1038/nsmb825. Epub 2004 Sep 7. [Article]
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  14. Tipparaju SM, Liu SQ, Barski OA, Bhatnagar A: NADPH binding to beta-subunit regulates inactivation of voltage-gated K(+) channels. Biochem Biophys Res Commun. 2007 Jul 27;359(2):269-76. doi: 10.1016/j.bbrc.2007.05.102. Epub 2007 May 24. [Article]
  15. Peters CJ, Vaid M, Horne AJ, Fedida D, Accili EA: The molecular basis for the actions of KVbeta1.2 on the opening and closing of the KV1.2 delayed rectifier channel. Channels (Austin). 2009 Sep-Oct;3(5):314-22. Epub 2009 Sep 16. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB00228Enfluraneapproved, investigational, vet_approvedunknowninhibitoractivatorDetails
DB01069Promethazineapproved, investigationalunknowninducerDetails
DB01110Miconazoleapproved, investigational, vet_approvedunknowninhibitorDetails