The gene is located on the Watson (plus) strand of the short arm of chromosome 12 (12p13.32). The gene itself is 8,348 bases in length and encodes a protein of 495 amino acids (predicted molecular weight 56.466 kilodaltons).
Alternative namesedit
The recommended name for this protein is potassium voltage-gated channel subfamily A member 1 but a number of alternatives have been used in the literature including HuK1 (human K+ channel I), RBK1 (rubidium potassium channel 1), MBK (mouse brain K+ channel), voltage gated potassium channel HBK1, voltage gated potassium channel subunit Kv1.1, voltage-gated K+ channel HuKI and AEMK (associated with myokymia with periodic ataxia).
Structureedit
The protein is believed to have six domains (S1-S6) with the loop between S5 and S6 forming the channel pore. This region also has a conserved selectivity filter motif. The functional channel is a homotetramer. The N-terminus of the protein associates with β subunits. These subunits regulate channel inactivation as well as its expression. The C-terminus is associated with a PDZ domain protein involved in channel targeting.[9][10]
Functionedit
The protein functions as a potassium selective channel through which the potassium ion may pass in consensus with the electrochemical gradient. They play a role in repolarisation of membranes.[9]
A to I RNA editing is catalyzed by a family of adenosine deaminases acting on RNA (ADARs) that specifically recognize adenosines within double-stranded regions of pre-mRNAs (e.g. Potassium channel RNA editing signal) and deaminate them to inosine. Inosines are recognised as guanosine by the cells translational machinery. There are three members of the ADAR family ADARs 1-3 with ADAR1 and ADAR2 being the only enzymatically active members. ADAR3 is thought to have a regulatory role in the brain. ADAR1 and ADAR2 are widely expressed in tissues while ADAR3 is restricted to the brain. The double stranded regions of RNA are formed by base-pairing between residues in the region close to the editing site with residues usually in a neighboring intron but can sometimes be an exonic sequence too. The region that base pairs with the editing region is known as an Editing Complementary Sequence (ECS).
Locationedit
The modified residue is found at amino acid 400 of the final protein. This is located in the sixth transmembrane region found, which corresponds to the inner vestibule of the pore. A stem loop hairpin structure mediates the RNA editing. ADAR2 is likely to be the preferred editing enzyme at the I/V site. Editing results in a codon alteration from ATT to GTT, resulting in an amino acid change from isoleucine to valine. ADAR2 enzyme is the major editing enzyme. The MFOLD programme predicted that the minimum region required for editing would form an imperfect inverted repeat hairpin. This region is composed of a 114 base pairs. Similar regions have been identified in mouse and rat. The edited adenosine is found in a 6-base pair duplex region. Mutation experiment in the region near the 6-base pair duplex have shown that the specific bases in this region were also essential for editing to occur. The region required for editing is unusual in that the hairpin structure is formed by exonic sequences only. In the majority of A to I editing the ECS is found within an intronic sequence.[11]
Conservationedit
The editing is highly conserved having been observed in squid, fruit fly, mouse, and rat.[11]
Editing results in a codon (I/V) change from (ATT) to (GTT) resulting in translation of a valine instead of an isoleucine at the position of the editing site. Valine has a larger side-chain. RNA editing at this position occurs at a highly conserved ion conducting pore of the channel. This may affect the channels role in the process of fast inactivation.[13]
Functionedit
Voltage-dependent potassium channels modulate excitability by opening and closing a potassium selective pore in response to voltage. The flow of potassium ions is interrupted by interaction of an inactivating particle, an auxiliary protein in humans but an intrinsic part of the channel in other species. The I to V amino acid change is thought to disrupt the hydrophobic interaction between the inactivating particle and the pore lining. This interrupts the process of fast inactivation. Activation kinetics are unaffected by RNA editing.[11] Changes in inactivation kinetics affect the duration and frequency of the action potential. An edited channel passes more current and has a shorter action potential than the non-edited type due to the inability of the inactivating particle to interact with the residue in the ion-conducting pore of the channel. This was determined by electrophysiology analysis.[14] The length of time the membrane is depolarised is decreased, which also reduces the efficiency of transmitter release.[12] Since editing can cause amino acid changes in 1- 4 in potassium channel tetramers, it can have a wide variety of effects on channel inactivation.
Dysregulationedit
Changes in the process of fast inactivation are known to have behavioral and neurological consequences in vivo.[11]
GABRA3 - a channel subunit which undergoes similar RNA editing
Referencesedit
^ abcGRCh38: Ensembl release 89: ENSG00000111262 - Ensembl, May 2017
^ abcGRCm38: Ensembl release 89: ENSMUSG00000047976 - 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.
^Curran ME, Landes GM, Keating MT (1992). "Molecular cloning, characterization, and genomic localization of a human potassium channel gene". Genomics. 12 (4): 729–37. doi:10.1016/0888-7543(92)90302-9. PMID 1349297.
^Albrecht B, Weber K, Pongs O (1995). "Characterization of a voltage-activated K-channel gene cluster on human chromosome 12p13". Recept. Channels. 3 (3): 213–20. PMID 8821794.
^Gutman GA, Chandy KG, Grissmer S, Lazdunski M, McKinnon D, Pardo LA, Robertson GA, Rudy B, Sanguinetti MC, Stühmer W, Wang X (2005). "International Union of Pharmacology. LIII. Nomenclature and molecular relationships of voltage-gated potassium channels". Pharmacol. Rev. 57 (4): 473–508. doi:10.1124/pr.57.4.10. PMID 16382104. S2CID 219195192.
^Newsom-Davis J (1997). "Autoimmune neuromyotonia (Isaacs' syndrome): an antibody-mediated potassium channelopathy". Ann. N. Y. Acad. Sci. 835 (1): 111–9. Bibcode:1997NYASA.835..111N. doi:10.1111/j.1749-6632.1997.tb48622.x. PMID 9616766. S2CID 13231594.[permanent dead link]
^"KCNA1 - Potassium voltage-gated channel subfamily A member 1 - Homo sapiens (Human) - KCNA1 gene & protein". www.uniprot.org.
^ abcdeBhalla T, Rosenthal JJ, Holmgren M, Reenan R (October 2004). "Control of human potassium channel inactivation by editing of a small mRNA hairpin". Nat. Struct. Mol. Biol. 11 (10): 950–6. doi:10.1038/nsmb825. PMID 15361858. S2CID 34081059.
^ abHoopengardner B, Bhalla T, Staber C, Reenan R (August 2003). "Nervous system targets of RNA editing identified by comparative genomics". Science. 301 (5634): 832–6. Bibcode:2003Sci...301..832H. doi:10.1126/science.1086763. PMID 12907802. S2CID 782642.
^Bhalla, Tarun; Rosenthal, Joshua J C; Holmgren, Miguel; Reenan, Robert (2004). "Control of human potassium channel inactivation by editing of a small mRNA hairpin". Nature Structural & Molecular Biology. 11 (10): 950–956. doi:10.1038/nsmb825. ISSN 1545-9993. PMID 15361858. S2CID 34081059.
^Bezanilla, Francisco (2004). "RNA editing of a human potassium channel modifies its inactivation". Nature Structural & Molecular Biology. 11 (10): 915–916. doi:10.1038/nsmb1004-915. ISSN 1545-9993. PMID 15452561. S2CID 40545616.
Further readingedit
Grunnet M, Rasmussen HB, Hay-Schmidt A, et al. (2003). "KCNE4 is an inhibitory subunit to Kv1.1 and Kv1.3 potassium channels". Biophys. J. 85 (3): 1525–37. Bibcode:2003BpJ....85.1525G. doi:10.1016/S0006-3495(03)74585-8. PMC1303329. PMID 12944270.
Nie DY, Zhou ZH, Ang BT, et al. (2003). "Nogo-A at CNS paranodes is a ligand of Caspr: possible regulation of K(+) channel localization". EMBO J. 22 (21): 5666–78. doi:10.1093/emboj/cdg570. PMC275427. PMID 14592966.
Imbrici P, Cusimano A, D'Adamo MC, et al. (2003). "Functional characterization of an episodic ataxia type-1 mutation occurring in the S1 segment of hKv1.1 channels". Pflügers Arch. 446 (3): 373–9. doi:10.1007/s00424-002-0962-2. PMID 12799903. S2CID 21478393.
Glaudemans B, van der Wijst J, Scola RH, et al. (2009). "A missense mutation in the Kv1.1 voltage-gated potassium channel-encoding gene KCNA1 is linked to human autosomal dominant hypomagnesemia". J. Clin. Invest. 119 (4): 936–42. doi:10.1172/JCI36948. PMC2662556. PMID 19307729.
Shook SJ, Mamsa H, Jen JC, et al. (2008). "Novel mutation in KCNA1 causes episodic ataxia with paroxysmal dyspnea". Muscle Nerve. 37 (3): 399–402. doi:10.1002/mus.20904. PMID 17912752. S2CID 26175513.
Gubitosi-Klug RA, Mancuso DJ, Gross RW (2005). "The human Kv1.1 channel is palmitoylated, modulating voltage sensing: Identification of a palmitoylation consensus sequence". Proc. Natl. Acad. Sci. U.S.A. 102 (17): 5964–8. Bibcode:2005PNAS..102.5964G. doi:10.1073/pnas.0501999102. PMC1087951. PMID 15837928.
Zhang ZH, Rhodes KJ, Childers WE, et al. (2004). "Disinactivation of N-type inactivation of voltage-gated K channels by an erbstatin analogue". J. Biol. Chem. 279 (28): 29226–30. doi:10.1074/jbc.M403290200. PMID 15136567.
Kimura K, Wakamatsu A, Suzuki Y, et al. (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC1356129. PMID 16344560.
Jow F, Zhang ZH, Kopsco DC, et al. (2004). "Functional coupling of intracellular calcium and inactivation of voltage-gated Kv1.1/Kvbeta1.1 A-type K+ channels". Proc. Natl. Acad. Sci. U.S.A. 101 (43): 15535–40. Bibcode:2004PNAS..10115535J. doi:10.1073/pnas.0402081101. PMC524431. PMID 15486093.
Imbrici P, Grottesi A, D'Adamo MC, et al. (2009). "Contribution of the central hydrophobic residue in the PXP motif of voltage-dependent K+ channels to S6 flexibility and gating properties". Channels (Austin). 3 (1): 39–45. doi:10.4161/chan.3.1.7548. PMID 19202350.
Kinali M, Jungbluth H, Eunson LH, et al. (2004). "Expanding the phenotype of potassium channelopathy: severe neuromyotonia and skeletal deformities without prominent Episodic Ataxia". Neuromuscul. Disord. 14 (10): 689–93. doi:10.1016/j.nmd.2004.06.007. PMID 15351427. S2CID 44972020.
Demos MK, Macri V, Farrell K, et al. (2009). "A novel KCNA1 mutation associated with global delay and persistent cerebellar dysfunction". Mov. Disord. 24 (5): 778–82. doi:10.1002/mds.22467. PMID 19205071. S2CID 25655998.
Imbrici P, Gualandi F, D'Adamo MC, et al. (2008). "A novel KCNA1 mutation identified in an Italian family affected by episodic ataxia type 1". Neuroscience. 157 (3): 577–87. doi:10.1016/j.neuroscience.2008.09.022. PMID 18926884. S2CID 15772885.
Tan KM, Lennon VA, Klein CJ, et al. (2008). "Clinical spectrum of voltage-gated potassium channel autoimmunity". Neurology. 70 (20): 1883–90. doi:10.1212/01.wnl.0000312275.04260.a0. PMID 18474843. S2CID 34815377.
Chen H, von Hehn C, Kaczmarek LK, et al. (2007). "Functional analysis of a novel potassium channel (KCNA1) mutation in hereditary myokymia". Neurogenetics. 8 (2): 131–5. doi:10.1007/s10048-006-0071-z. PMC1820748. PMID 17136396.
Strausberg RL, Feingold EA, Grouse LH, et al. (2002). "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. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC139241. PMID 12477932.
Gutman GA, Chandy KG, Grissmer S, et al. (2005). "International Union of Pharmacology. LIII. Nomenclature and molecular relationships of voltage-gated potassium channels". Pharmacol. Rev. 57 (4): 473–508. doi:10.1124/pr.57.4.10. PMID 16382104. S2CID 219195192.
Lee H, Wang H, Jen JC, et al. (2004). "A novel mutation in KCNA1 causes episodic ataxia without myokymia". Hum. Mutat. 24 (6): 536. doi:10.1002/humu.9295. PMID 15532032. S2CID 2542180.
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.
External linksedit
GeneReviews/NCBI/NIH/UW entry on Episodic Ataxia Type 1, Episodic Ataxia with Myokymia, Hereditary Cerebellar Ataxia with Neuromyotonia
Kv1.1+Potassium+Channel at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
confused, with, potassium, voltage, gated, channel, subfamily, member, also, known, shaker, related, voltage, gated, potassium, channel, that, humans, encoded, kcna1, gene, isaacs, syndrome, result, autoimmune, reaction, against, channel, kcna1available, struc. Not to be confused with KV 1 Potassium voltage gated channel subfamily A member 1 also known as Kv1 1 is a shaker related voltage gated potassium channel that in humans is encoded by the KCNA1 gene 5 6 7 Isaacs syndrome is a result of an autoimmune reaction against the Kv1 1 ion channel 8 KCNA1Available structuresPDBOrtholog search PDBe RCSBList of PDB id codes2AFLIdentifiersAliasesKCNA1 AEMK EA1 HBK1 HUK1 KV1 1 MBK1 MK1 RBK1 potassium voltage gated channel subfamily A member 1External IDsOMIM 176260 MGI 96654 HomoloGene 183 GeneCards KCNA1Gene location Human Chr Chromosome 12 human 1 Band12p13 32Start4 909 905 bp 1 End4 918 256 bp 1 Gene location Mouse Chr Chromosome 6 mouse 2 Band6 F3 6 61 57 cMStart126 617 360 bp 2 End126 623 347 bp 2 RNA expression patternBgeeHumanMouse ortholog Top expressed inendothelial cellBrodmann area 23middle temporal gyruscerebellar hemispherepostcentral gyrusputamencaudate nucleusponsspinal gangliaexternal globus pallidusTop expressed insciatic nervepontine nucleilateral geniculate nucleusmedulla oblongatamedial vestibular nucleuscerebellar vermisolfactory tubercleinferior colliculusanterior horn of spinal cordglobus pallidusMore reference expression dataBioGPSn aGene ontologyMolecular functionpotassium channel activity delayed rectifier potassium channel activity voltage gated ion channel activity potassium ion transmembrane transporter activity ion channel activity protein binding voltage gated potassium channel activity disordered domain specific binding voltage gated ion channel activity involved in regulation of presynaptic membrane potential voltage gated ion channel activity involved in regulation of postsynaptic membrane potentialCellular componentaxon terminus juxtaparanode region of axon integral component of membrane cytosol perikaryon cell projection membrane plasma membrane synapse integral component of plasma membrane cell surface cell junction neuronal cell body dendrite axon potassium channel complex apical plasma membrane endoplasmic reticulum paranode region of axon presynaptic membrane cytoplasmic vesicle voltage gated potassium channel complex calyx of Held glutamatergic synapse integral component of postsynaptic membrane integral component of presynaptic membraneBiological processregulation of muscle contraction detection of mechanical stimulus involved in sensory perception of pain cellular response to magnesium ion startle response regulation of membrane potential cell communication by electrical coupling neuronal signal transduction regulation of ion transmembrane transport ion transport magnesium ion homeostasis potassium ion transport brain development neuromuscular process transmembrane transport potassium ion transmembrane transport neuroblast proliferation detection of mechanical stimulus involved in sensory perception of touch protein homooligomerization hippocampus development neuronal action potential chemical synaptic transmission positive regulation of voltage gated potassium channel activity regulation of postsynaptic membrane potential regulation of presynaptic membrane potentialSources Amigo QuickGOOrthologsSpeciesHumanMouseEntrez373616485EnsemblENSG00000111262ENSMUSG00000047976UniProtQ09470P16388RefSeq mRNA NM 000217NM 010595RefSeq protein NP 000208NP 034725Location UCSC Chr 12 4 91 4 92 MbChr 6 126 62 126 62 MbPubMed search 3 4 WikidataView Edit HumanView Edit Mouse Contents 1 Genomics 2 Alternative names 3 Structure 4 Function 5 RNA editing 5 1 Type 5 2 Location 5 3 Conservation 5 4 Regulation 5 5 Consequences 5 5 1 Structure 5 5 2 Function 5 6 Dysregulation 6 Clinical 7 See also 8 References 9 Further reading 10 External linksGenomics editThe gene is located on the Watson plus strand of the short arm of chromosome 12 12p13 32 The gene itself is 8 348 bases in length and encodes a protein of 495 amino acids predicted molecular weight 56 466 kilodaltons Alternative names editThe recommended name for this protein is potassium voltage gated channel subfamily A member 1 but a number of alternatives have been used in the literature including HuK1 human K channel I RBK1 rubidium potassium channel 1 MBK mouse brain K channel voltage gated potassium channel HBK1 voltage gated potassium channel subunit Kv1 1 voltage gated K channel HuKI and AEMK associated with myokymia with periodic ataxia Structure editThe protein is believed to have six domains S1 S6 with the loop between S5 and S6 forming the channel pore This region also has a conserved selectivity filter motif The functional channel is a homotetramer The N terminus of the protein associates with b subunits These subunits regulate channel inactivation as well as its expression The C terminus is associated with a PDZ domain protein involved in channel targeting 9 10 Function editThe protein functions as a potassium selective channel through which the potassium ion may pass in consensus with the electrochemical gradient They play a role in repolarisation of membranes 9 RNA editing editThe pre mRNA of this protein is subject to RNA editing 11 Type edit A to I RNA editing is catalyzed by a family of adenosine deaminases acting on RNA ADARs that specifically recognize adenosines within double stranded regions of pre mRNAs e g Potassium channel RNA editing signal and deaminate them to inosine Inosines are recognised as guanosine by the cells translational machinery There are three members of the ADAR family ADARs 1 3 with ADAR1 and ADAR2 being the only enzymatically active members ADAR3 is thought to have a regulatory role in the brain ADAR1 and ADAR2 are widely expressed in tissues while ADAR3 is restricted to the brain The double stranded regions of RNA are formed by base pairing between residues in the region close to the editing site with residues usually in a neighboring intron but can sometimes be an exonic sequence too The region that base pairs with the editing region is known as an Editing Complementary Sequence ECS Location edit The modified residue is found at amino acid 400 of the final protein This is located in the sixth transmembrane region found which corresponds to the inner vestibule of the pore A stem loop hairpin structure mediates the RNA editing ADAR2 is likely to be the preferred editing enzyme at the I V site Editing results in a codon alteration from ATT to GTT resulting in an amino acid change from isoleucine to valine ADAR2 enzyme is the major editing enzyme The MFOLD programme predicted that the minimum region required for editing would form an imperfect inverted repeat hairpin This region is composed of a 114 base pairs Similar regions have been identified in mouse and rat The edited adenosine is found in a 6 base pair duplex region Mutation experiment in the region near the 6 base pair duplex have shown that the specific bases in this region were also essential for editing to occur The region required for editing is unusual in that the hairpin structure is formed by exonic sequences only In the majority of A to I editing the ECS is found within an intronic sequence 11 Conservation edit The editing is highly conserved having been observed in squid fruit fly mouse and rat 11 Regulation edit Editing levels vary in different tissues 17 in the caudate nucleus 68 in the spinal cord and 77 in the medulla 12 Consequences edit Structure edit Editing results in a codon I V change from ATT to GTT resulting in translation of a valine instead of an isoleucine at the position of the editing site Valine has a larger side chain RNA editing at this position occurs at a highly conserved ion conducting pore of the channel This may affect the channels role in the process of fast inactivation 13 Function edit Voltage dependent potassium channels modulate excitability by opening and closing a potassium selective pore in response to voltage The flow of potassium ions is interrupted by interaction of an inactivating particle an auxiliary protein in humans but an intrinsic part of the channel in other species The I to V amino acid change is thought to disrupt the hydrophobic interaction between the inactivating particle and the pore lining This interrupts the process of fast inactivation Activation kinetics are unaffected by RNA editing 11 Changes in inactivation kinetics affect the duration and frequency of the action potential An edited channel passes more current and has a shorter action potential than the non edited type due to the inability of the inactivating particle to interact with the residue in the ion conducting pore of the channel This was determined by electrophysiology analysis 14 The length of time the membrane is depolarised is decreased which also reduces the efficiency of transmitter release 12 Since editing can cause amino acid changes in 1 4 in potassium channel tetramers it can have a wide variety of effects on channel inactivation Dysregulation edit Changes in the process of fast inactivation are known to have behavioral and neurological consequences in vivo 11 Clinical editMutations in this gene cause episodic ataxia type 1 See also editGABRA3 a channel subunit which undergoes similar RNA editingReferences edit a b c GRCh38 Ensembl release 89 ENSG00000111262 Ensembl May 2017 a b c GRCm38 Ensembl release 89 ENSMUSG00000047976 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 Curran ME Landes GM Keating MT 1992 Molecular cloning characterization and genomic localization of a human potassium channel gene Genomics 12 4 729 37 doi 10 1016 0888 7543 92 90302 9 PMID 1349297 Albrecht B Weber K Pongs O 1995 Characterization of a voltage activated K channel gene cluster on human chromosome 12p13 Recept Channels 3 3 213 20 PMID 8821794 Gutman GA Chandy KG Grissmer S Lazdunski M McKinnon D Pardo LA Robertson GA Rudy B Sanguinetti MC Stuhmer W Wang X 2005 International Union of Pharmacology LIII Nomenclature and molecular relationships of voltage gated potassium channels Pharmacol Rev 57 4 473 508 doi 10 1124 pr 57 4 10 PMID 16382104 S2CID 219195192 Newsom Davis J 1997 Autoimmune neuromyotonia Isaacs syndrome an antibody mediated potassium channelopathy Ann N Y Acad Sci 835 1 111 9 Bibcode 1997NYASA 835 111N doi 10 1111 j 1749 6632 1997 tb48622 x PMID 9616766 S2CID 13231594 permanent dead link a b Entrez Gene KCNA1 potassium voltage gated channel KCNA1 Potassium voltage gated channel subfamily A member 1 Homo sapiens Human KCNA1 gene amp protein www uniprot org a b c d e Bhalla T Rosenthal JJ Holmgren M Reenan R October 2004 Control of human potassium channel inactivation by editing of a small mRNA hairpin Nat Struct Mol Biol 11 10 950 6 doi 10 1038 nsmb825 PMID 15361858 S2CID 34081059 a b Hoopengardner B Bhalla T Staber C Reenan R August 2003 Nervous system targets of RNA editing identified by comparative genomics Science 301 5634 832 6 Bibcode 2003Sci 301 832H doi 10 1126 science 1086763 PMID 12907802 S2CID 782642 Bhalla Tarun Rosenthal Joshua J C Holmgren Miguel Reenan Robert 2004 Control of human potassium channel inactivation by editing of a small mRNA hairpin Nature Structural amp Molecular Biology 11 10 950 956 doi 10 1038 nsmb825 ISSN 1545 9993 PMID 15361858 S2CID 34081059 Bezanilla Francisco 2004 RNA editing of a human potassium channel modifies its inactivation Nature Structural amp Molecular Biology 11 10 915 916 doi 10 1038 nsmb1004 915 ISSN 1545 9993 PMID 15452561 S2CID 40545616 Further reading editGrunnet M Rasmussen HB Hay Schmidt A et al 2003 KCNE4 is an inhibitory subunit to Kv1 1 and Kv1 3 potassium channels Biophys J 85 3 1525 37 Bibcode 2003BpJ 85 1525G doi 10 1016 S0006 3495 03 74585 8 PMC 1303329 PMID 12944270 Nie DY Zhou ZH Ang BT et al 2003 Nogo A at CNS paranodes is a ligand of Caspr possible regulation of K channel localization EMBO J 22 21 5666 78 doi 10 1093 emboj cdg570 PMC 275427 PMID 14592966 Imbrici P Cusimano A D Adamo MC et al 2003 Functional characterization of an episodic ataxia type 1 mutation occurring in the S1 segment of hKv1 1 channels Pflugers Arch 446 3 373 9 doi 10 1007 s00424 002 0962 2 PMID 12799903 S2CID 21478393 Glaudemans B van der Wijst J Scola RH et al 2009 A missense mutation in the Kv1 1 voltage gated potassium channel encoding gene KCNA1 is linked to human autosomal dominant hypomagnesemia J Clin Invest 119 4 936 42 doi 10 1172 JCI36948 PMC 2662556 PMID 19307729 Shook SJ Mamsa H Jen JC et al 2008 Novel mutation in KCNA1 causes episodic ataxia with paroxysmal dyspnea Muscle Nerve 37 3 399 402 doi 10 1002 mus 20904 PMID 17912752 S2CID 26175513 Gubitosi Klug RA Mancuso DJ Gross RW 2005 The human Kv1 1 channel is palmitoylated modulating voltage sensing Identification of a palmitoylation consensus sequence Proc Natl Acad Sci U S A 102 17 5964 8 Bibcode 2005PNAS 102 5964G doi 10 1073 pnas 0501999102 PMC 1087951 PMID 15837928 Zhang ZH Rhodes KJ Childers WE et al 2004 Disinactivation of N type inactivation of voltage gated K channels by an erbstatin analogue J Biol Chem 279 28 29226 30 doi 10 1074 jbc M403290200 PMID 15136567 Kimura K Wakamatsu A Suzuki Y et al 2006 Diversification of transcriptional modulation large scale identification and characterization of putative alternative promoters of human genes Genome Res 16 1 55 65 doi 10 1101 gr 4039406 PMC 1356129 PMID 16344560 Jow F Zhang ZH Kopsco DC et al 2004 Functional coupling of intracellular calcium and inactivation of voltage gated Kv1 1 Kvbeta1 1 A type K channels Proc Natl Acad Sci U S A 101 43 15535 40 Bibcode 2004PNAS 10115535J doi 10 1073 pnas 0402081101 PMC 524431 PMID 15486093 Imbrici P Grottesi A D Adamo MC et al 2009 Contribution of the central hydrophobic residue in the PXP motif of voltage dependent K channels to S6 flexibility and gating properties Channels Austin 3 1 39 45 doi 10 4161 chan 3 1 7548 PMID 19202350 Kinali M Jungbluth H Eunson LH et al 2004 Expanding the phenotype of potassium channelopathy severe neuromyotonia and skeletal deformities without prominent Episodic Ataxia Neuromuscul Disord 14 10 689 93 doi 10 1016 j nmd 2004 06 007 PMID 15351427 S2CID 44972020 Demos MK Macri V Farrell K et al 2009 A novel KCNA1 mutation associated with global delay and persistent cerebellar dysfunction Mov Disord 24 5 778 82 doi 10 1002 mds 22467 PMID 19205071 S2CID 25655998 Imbrici P Gualandi F D Adamo MC et al 2008 A novel KCNA1 mutation identified in an Italian family affected by episodic ataxia type 1 Neuroscience 157 3 577 87 doi 10 1016 j neuroscience 2008 09 022 PMID 18926884 S2CID 15772885 Tan KM Lennon VA Klein CJ et al 2008 Clinical spectrum of voltage gated potassium channel autoimmunity Neurology 70 20 1883 90 doi 10 1212 01 wnl 0000312275 04260 a0 PMID 18474843 S2CID 34815377 Chen H von Hehn C Kaczmarek LK et al 2007 Functional analysis of a novel potassium channel KCNA1 mutation in hereditary myokymia Neurogenetics 8 2 131 5 doi 10 1007 s10048 006 0071 z PMC 1820748 PMID 17136396 Strausberg RL Feingold EA Grouse LH et al 2002 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 Bibcode 2002PNAS 9916899M doi 10 1073 pnas 242603899 PMC 139241 PMID 12477932 Gutman GA Chandy KG Grissmer S et al 2005 International Union of Pharmacology LIII Nomenclature and molecular relationships of voltage gated potassium channels Pharmacol Rev 57 4 473 508 doi 10 1124 pr 57 4 10 PMID 16382104 S2CID 219195192 Lee H Wang H Jen JC et al 2004 A novel mutation in KCNA1 causes episodic ataxia without myokymia Hum Mutat 24 6 536 doi 10 1002 humu 9295 PMID 15532032 S2CID 2542180 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 External links editGeneReviews NCBI NIH UW entry on Episodic Ataxia Type 1 Episodic Ataxia with Myokymia Hereditary Cerebellar Ataxia with Neuromyotonia Kv1 1 Potassium Channel at the U S National Library of Medicine Medical Subject Headings MeSH KCNA1 protein human at the U S National Library of Medicine Medical Subject Headings MeSH Retrieved from https en wikipedia org w index php title Kv1 1 amp oldid 1184672904, wikipedia, wiki, book, books, library,
