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Potassium voltage-gated channel subfamily KQT member 1 (IKs producing slow voltage-gated potassium channel subunit alpha KvLQT1) (KQT-like 1) (Voltage-gated potassium channel subunit Kv7.1)

 KCNQ1_HUMAN             Reviewed;         676 AA.
P51787; O00347; O60607; O94787; Q14D14; Q7Z6G9; Q92960; Q9UMN8;
Q9UMN9;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
15-JUL-1999, sequence version 3.
30-AUG-2017, entry version 194.
RecName: Full=Potassium voltage-gated channel subfamily KQT member 1 {ECO:0000305};
AltName: Full=IKs producing slow voltage-gated potassium channel subunit alpha KvLQT1 {ECO:0000305|PubMed:9312006};
AltName: Full=KQT-like 1 {ECO:0000305};
AltName: Full=Voltage-gated potassium channel subunit Kv7.1 {ECO:0000305|PubMed:20533308};
Name=KCNQ1 {ECO:0000312|HGNC:HGNC:6294};
Synonyms=KCNA8 {ECO:0000312|HGNC:HGNC:6294},
KCNA9 {ECO:0000312|HGNC:HGNC:6294},
KVLQT1 {ECO:0000303|PubMed:9312006};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND CHARACTERIZATION
OF VARIANT LQT1 CYS-555.
TISSUE=Kidney;
PubMed=9312006; DOI=10.1093/emboj/16.17.5472;
Chouabe C., Neyroud N., Guicheney P., Lazdunski M., Romey G.,
Barhanin J.;
"Properties of KvLQT1 K+ channel mutations in Romano-Ward and Jervell
and Lange-Nielsen inherited cardiac arrhythmias.";
EMBO J. 16:5472-5479(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND FUNCTION (ISOFORM 2).
TISSUE=Heart;
PubMed=9305853; DOI=10.1074/jbc.272.39.24109;
Jiang M., Tseng-Crank J., Tseng G.-N.;
"Suppression of slow delayed rectifier current by a truncated isoform
of KvLQT1 cloned from normal human heart.";
J. Biol. Chem. 272:24109-24112(1997).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2), VARIANTS LQT1
ASN-242; HIS-250; SER-314 AND MET-587, AND VARIANT SER-643.
PubMed=9799083; DOI=10.1007/s004390050819;
Itoh T., Tanaka T., Nagai R., Kikuchi K., Ogawa S., Okada S.,
Yamagata S., Yano K., Yazaki Y., Nakamura Y.;
"Genomic organization and mutational analysis of KVLQT1, a gene
responsible for familial long QT syndrome.";
Hum. Genet. 103:290-294(1998).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2), AND VARIANTS
LQT1 MET-587 AND HIS-591.
PubMed=10024302; DOI=10.1161/01.RES.84.3.290;
Neyroud N., Richard P., Vignier N., Donger C., Denjoy I., Demay L.,
Shkolnikova M., Pesce R., Chevalier P., Hainque B., Coumel P.,
Schwartz K., Guicheney P.;
"Genomic organization of the KCNQ1 K+ channel gene and identification
of C-terminal mutations in the long-QT syndrome.";
Circ. Res. 84:290-297(1999).
[5]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Heart;
Seebohm G.;
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Heart;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-129, AND FUNCTION.
PubMed=9108097; DOI=10.1073/pnas.94.8.4017;
Yang W.-P., Levesque P.C., Little W.A., Conder M.L., Shalaby F.Y.,
Blanar M.A.;
"KvLQT1, a voltage-gated potassium channel responsible for human
cardiac arrhythmias.";
Proc. Natl. Acad. Sci. U.S.A. 94:4017-4021(1997).
[11]
NUCLEOTIDE SEQUENCE [MRNA] OF 107-676, AND FUNCTION.
TISSUE=Pancreas;
PubMed=8900283; DOI=10.1038/384080a0;
Sanguinetti M.C., Curran M.E., Zou A., Shen J., Spector P.S.,
Atkinson D.L., Keating M.T.;
"Coassembly of K(V)LQT1 and minK (IsK) proteins to form cardiac I(Ks)
potassium channel.";
Nature 384:80-83(1996).
[12]
NUCLEOTIDE SEQUENCE [MRNA] OF 130-676, AND VARIANTS LQT1.
PubMed=8528244; DOI=10.1038/ng0196-17;
Wang Q., Curran M.E., Splawski I., Burn T.C., Millholland J.M.,
Vanraay T.J., Shen J., Timothy K.W., Vincent G.M., de Jager T.,
Schwartz P.J., Towbin J.A., Moss A.J., Atkinson D.L., Landes G.M.,
Connors T.D., Keating M.T.;
"Positional cloning of a novel potassium channel gene: KVLQT1
mutations cause cardiac arrhythmias.";
Nat. Genet. 12:17-23(1996).
[13]
IDENTIFICATION OF C-TERMINAL ASSEMBLY DOMAIN.
PubMed=10654932; DOI=10.1093/emboj/19.3.332;
Schmitt N., Schwarz M., Peretz A., Abitbol I., Attali B., Pongs O.;
"A recessive C-terminal Jervell and Lange-Nielsen mutation of the
KCNQ1 channel impairs subunit assembly.";
EMBO J. 19:332-340(2000).
[14]
INTERACTION WITH KCNE2, AND FUNCTION.
PubMed=11101505; DOI=10.1093/emboj/19.23.6326;
Tinel N., Diochot S., Borsotto M., Lazdunski M., Barhanin J.;
"KCNE2 confers background current characteristics to the cardiac KCNQ1
potassium channel.";
EMBO J. 19:6326-6330(2000).
[15]
FUNCTION.
PubMed=10713961; DOI=10.1111/j.1469-7793.2000.t01-2-00349.x;
Selyanko A.A., Hadley J.K., Wood I.C., Abogadie F.C., Jentsch T.J.,
Brown D.A.;
"Inhibition of KCNQ1-4 potassium channels expressed in mammalian cells
via M1 muscarinic acetylcholine receptors.";
J. Physiol. (Lond.) 522:349-355(2000).
[16]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=10646604; DOI=10.1038/35003200;
Schroeder B.C., Waldegger S., Fehr S., Bleich M., Warth R., Greger R.,
Jentsch T.J.;
"A constitutively open potassium channel formed by KCNQ1 and KCNE3.";
Nature 403:196-199(2000).
[17]
FUNCTION.
PubMed=12324418; DOI=10.1016/S0006-3495(02)73961-1;
Angelo K., Jespersen T., Grunnet M., Nielsen M.S., Klaerke D.A.,
Olesen S.P.;
"KCNE5 induces time- and voltage-dependent modulation of the KCNQ1
current.";
Biophys. J. 83:1997-2006(2002).
[18]
INTERACTION WITH AKAP9, PHOSPHORYLATION AT SER-27, CHARACTERIZATION OF
VARIANT LQT1 ASP-589, AND MUTAGENESIS OF SER-27; LEU-602 AND ILE-609.
PubMed=11799244; DOI=10.1126/science.1066843;
Marx S.O., Kurokawa J., Reiken S., Motoike H., D'Armiento J.,
Marks A.R., Kass R.S.;
"Requirement of a macromolecular signaling complex for beta adrenergic
receptor modulation of the KCNQ1-KCNE1 potassium channel.";
Science 295:496-499(2002).
[19]
FUNCTION, DOMAIN, INTERACTION WITH KCNE4, AND MUTAGENESIS OF VAL-324;
LYS-326; THR-327; ILE-328; SER-338 AND PHE-340.
PubMed=19687231; DOI=10.1085/jgp.200910234;
Vanoye C.G., Welch R.C., Daniels M.A., Manderfield L.J., Tapper A.R.,
Sanders C.R., George A.L. Jr.;
"Distinct subdomains of the KCNQ1 S6 segment determine channel
modulation by different KCNE subunits.";
J. Gen. Physiol. 134:207-217(2009).
[20]
SUBCELLULAR LOCATION, AND INTERACTION WITH KCNE1; KCNE2; KCNE3; KCNE4
AND KCNE5.
PubMed=20533308; DOI=10.1002/jcp.22265;
Roura-Ferrer M., Sole L., Oliveras A., Dahan R., Bielanska J.,
Villarroel A., Comes N., Felipe A.;
"Impact of KCNE subunits on KCNQ1 (Kv7.1) channel membrane surface
targeting.";
J. Cell. Physiol. 225:692-700(2010).
[21]
SUBCELLULAR LOCATION.
PubMed=21228319; DOI=10.1152/ajpcell.00390.2010;
Andersen M.N., Olesen S.P., Rasmussen H.B.;
"Kv7.1 surface expression is regulated by epithelial cell
polarization.";
Am. J. Physiol. 300:C814-C824(2011).
[22]
INTERACTION WITH NEDD4L AND USP2, UBIQUITINATED, DEUBIQUITINATED, AND
SUBCELLULAR LOCATION.
PubMed=22024150; DOI=10.1016/j.hrthm.2011.10.026;
Krzystanek K., Rasmussen H.B., Grunnet M., Staub O., Olesen S.P.,
Abriel H., Jespersen T.;
"Deubiquitylating enzyme USP2 counteracts Nedd4-2-mediated
downregulation of KCNQ1 potassium channels.";
Heart Rhythm 9:440-448(2012).
[23]
INTERACTION WITH AP2M1 AND NEDD4L, AND SUBCELLULAR LOCATION.
PubMed=23529131; DOI=10.1113/jphysiol.2013.251678;
Rapetti-Mauss R., O'Mahony F., Sepulveda F.V., Urbach V., Harvey B.J.;
"Oestrogen promotes KCNQ1 potassium channel endocytosis and
postendocytic trafficking in colonic epithelium.";
J. Physiol. (Lond.) 591:2813-2831(2013).
[24]
INTERACTION WITH KCNQ5, SUBCELLULAR LOCATION, AND FUNCTION.
PubMed=24855057; DOI=10.1161/ATVBAHA.114.303801;
Oliveras A., Roura-Ferrer M., Sole L., de la Cruz A., Prieto A.,
Etxebarria A., Manils J., Morales-Cano D., Condom E., Soler C.,
Cogolludo A., Valenzuela C., Villarroel A., Comes N., Felipe A.;
"Functional assembly of Kv7.1/Kv7.5 channels with emerging properties
on vascular muscle physiology.";
Arterioscler. Thromb. Vasc. Biol. 34:1522-1530(2014).
[25]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 574-622, INTERACTION WITH
CALM, SUBCELLULAR LOCATION, MUTAGENESIS OF GLY-589; ALA-590 AND
ASN-593, CHARACTERIZATION OF VARIANT LQT1 ASP-589, AND
TETRAMERIZATION.
PubMed=18165683; DOI=10.1074/jbc.M707541200;
Wiener R., Haitin Y., Shamgar L., Fernandez-Alonso M.C., Martos A.,
Chomsky-Hecht O., Rivas G., Attali B., Hirsch J.A.;
"The KCNQ1 (Kv7.1) COOH terminus, a multitiered scaffold for subunit
assembly and protein interaction.";
J. Biol. Chem. 283:5815-5830(2008).
[26]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 583-611, SUBUNIT, AND
COILED-COIL.
PubMed=19693805; DOI=10.1002/pro.224;
Xu Q., Minor D.L. Jr.;
"Crystal structure of a trimeric form of the K(V)7.1 (KCNQ1) A-domain
tail coiled-coil reveals structural plasticity and context dependent
changes in a putative coiled-coil trimerization motif.";
Protein Sci. 18:2100-2114(2009).
[27]
CHARACTERIZATION OF VARIANTS LQT1 PRO-178; PHE-273 AND ILE-312.
PubMed=9323054; DOI=10.1161/01.CIR.96.6.1733;
Shalaby F.Y., Levesque P.C., Yang W.-P., Little W.A., Conder M.L.,
Jenkins-West T., Blanar M.A.;
"Dominant-negative KvLQT1 mutations underlie the LQT1 form of long QT
syndrome.";
Circulation 96:1733-1736(1997).
[28]
REVIEW ON VARIANTS.
PubMed=10704188;
DOI=10.1002/(SICI)1096-8628(19990924)89:3<137::AID-AJMG4>3.3.CO;2-3;
Tranebjaerg L., Bathen J., Tyson J., Bitner-Glindzicz M.;
"Jervell and Lange-Nielsen syndrome: a Norwegian perspective.";
Am. J. Med. Genet. 89:137-146(1999).
[29]
VARIANTS LQT1 SER-314 AND VAL-341.
PubMed=8872472; DOI=10.1093/hmg/5.9.1319;
Russell M.W., Dick M. II, Collins F.S., Brody L.C.;
"KVLQT1 mutations in three families with familial or sporadic long QT
syndrome.";
Hum. Mol. Genet. 5:1319-1324(1996).
[30]
VARIANT LQT1 VAL-341.
PubMed=8818942; DOI=10.1136/jmg.33.7.567;
de Jager T., Corbett C.H., Badenhorst J.C., Brink P.A., Corfield V.A.;
"Evidence of a long QT founder gene with varying phenotypic expression
in South African families.";
J. Med. Genet. 33:567-573(1996).
[31]
VARIANTS LQT1 MET-254 AND MET-417.
Wedekind H., Schulze-Bahr E., Lange S., Rubie C., Haverkamp W.,
Hoerdt M., Borggrefe M., Assmann G., Breithardt G., Funke H.;
"A severe form of long-QT syndrome caused by KVLQT1 mutations located
in cis (Abstract #2051).";
Am. J. Hum. Genet. Suppl. 61:A350-A350(1997).
[32]
VARIANTS LQT1 THR-178; MET-313; ARG-325 AND PRO-366.
PubMed=9024139; DOI=10.1161/01.CIR.95.3.565;
Tanaka T., Nagai R., Tomoike H., Takata S., Yano K., Yabuta K.,
Haneda N., Nakano O., Shibata A., Sawayama T., Kasai H., Yazaki Y.,
Nakamura Y.;
"Four novel KVLQT1 and four novel HERG mutations in familial long-QT
syndrome.";
Circulation 95:565-567(1997).
[33]
VARIANTS LQT1.
PubMed=9386136; DOI=10.1161/01.CIR.96.9.2778;
Donger C., Denjoy I., Berthet M., Neyroud N., Cruaud C., Bennaceur M.,
Chivoret G., Schwartz K., Coumel P., Guicheney P.;
"KVLQT1 C-terminal missense mutation causes a forme fruste long-QT
syndrome.";
Circulation 96:2778-2781(1997).
[34]
VARIANT LQT1 ARG-216.
PubMed=9272155; DOI=10.1007/s004390050516;
van den Berg M.H., Wilde A.A.M., Robles de Medina E.O., Meyer H.,
Geelen J.L.M.C., Jongbloed R.J.E., Wellens H.J., Geraedts J.P.M.;
"The long QT syndrome: a novel missense mutation in the S6 region of
the KVLQT1 gene.";
Hum. Genet. 100:356-361(1997).
[35]
VARIANT LQT1 ASN-317.
PubMed=9302275; DOI=10.1093/hmg/6.11.1943;
Wollnik B., Schroeder B.C., Kubisch C., Esperer H.D., Wieacker P.,
Jentsch T.J.;
"Pathophysiological mechanisms of dominant and recessive KVLQT1 K+
channel mutations found in inherited cardiac arrhythmias.";
Hum. Mol. Genet. 6:1943-1949(1997).
[36]
VARIANT LQT1 VAL-341.
PubMed=9570196; DOI=10.1161/01.CIR.97.13.1264;
Li H., Chen Q., Moss A.J., Robinson J.L., Goytia V., Perry J.C.,
Vincent G.M., Priori S.G., Lehmann M.H., Denfield S.W., Duff D.,
Kaine S., Shimizu W., Schwartz P.J., Wang Q., Towbin J.A.;
"New mutations in the KVLQT1 potassium channel that cause long-QT
syndrome.";
Circulation 97:1264-1269(1998).
[37]
VARIANT LQT1 THR-300.
PubMed=9641694; DOI=10.1161/01.CIR.97.24.2420;
Priori S.G., Schwartz P.J., Napolitano C., Bianchi L., Dennis A.T.,
de Fusco M., Brown A.M., Casari G.;
"A recessive variant of the Romano-Ward Long-QT syndrome?";
Circulation 97:2420-2425(1998).
[38]
VARIANT JLNS1 SER-305.
PubMed=9781056; DOI=10.1038/sj.ejhg.5200165;
Neyroud N., Denjoy I., Donger C., Gary F., Villain E., Leenhardt A.,
Benali K., Schwartz K., Coumel P., Guicheney P.;
"Heterozygous mutation in the pore of potassium channel gene KvLQT1
causes an apparently normal phenotype in long QT syndrome.";
Eur. J. Hum. Genet. 6:129-133(1998).
[39]
VARIANTS LQT1 ARG-168; SER-314; CYS-315; ASN-318; PRO-353 AND TRP-366.
PubMed=9693036; DOI=10.1006/geno.1998.5361;
Splawski I., Shen J., Timothy K.W., Vincent G.M., Lehmann M.H.,
Keating M.T.;
"Genomic structure of three long QT syndrome genes: KVLQT1, HERG, and
KCNE1.";
Genomics 51:86-97(1998).
[40]
VARIANTS LQT1 ILE-311 AND ASN-317.
PubMed=9482580;
DOI=10.1002/(SICI)1098-1004(1998)11:2<158::AID-HUMU9>3.0.CO;2-F;
Saarinen K., Swan H., Kainulainen K., Toivonen L., Viitasalo M.,
Kontula K.;
"Molecular genetics of the long QT syndrome: two novel mutations of
the KVLQT1 gene and phenotypic expression of the mutant gene in a
large kindred.";
Hum. Mutat. 11:158-165(1998).
[41]
VARIANT LQT1 PHE-339 DEL.
PubMed=9702906; DOI=10.1203/00006450-199808000-00002;
Ackerman M.J., Schroeder J.J., Berry R., Schaid D.J., Porter C.-B.J.,
Michels V.V., Thibodeau S.N.;
"A novel mutation in KVLQT1 is the molecular basis of inherited long
QT syndrome in a near-drowning patient's family.";
Pediatr. Res. 44:148-153(1998).
[42]
VARIANT JLNS1 HIS-243.
PubMed=10090886; DOI=10.1086/302346;
Mohammad-Panah R., Demolombe S., Neyroud N., Guicheney P., Kyndt F.,
van den Hoff M., Baro I., Escande D.;
"Mutations in a dominant-negative isoform correlate with phenotype in
inherited cardiac arrhythmias.";
Am. J. Hum. Genet. 64:1015-1023(1999).
[43]
VARIANT LQT1 HIS-174.
PubMed=10367071;
Denjoy I., Lupoglazoff J.M., Donger C., Berthet M., Richard P.,
Neyroud N., Villain E., Lucet V., Coumel P., Guicheney P.;
"Congenital long QT syndrome. The value of genetics in prognostic
evaluation.";
Arch. Mal. Coeur Vaiss. 92:557-563(1999).
[44]
VARIANTS LQT1 LEU-225; CYS-281 AND CYS-315.
PubMed=9927399; DOI=10.1161/01.CIR.99.4.529;
Priori S.G., Napolitano C., Schwartz P.J.;
"Low penetrance in the long-QT syndrome: clinical impact.";
Circulation 99:529-533(1999).
[45]
VARIANT LQT1 THR-525.
PubMed=10482963; DOI=10.1038/sj.ejhg.5200323;
Larsen L.A., Fosdal I., Andersen P.S., Kanters J.K., Vuust J.,
Wettrell G., Christiansen M.;
"Recessive Romano-Ward syndrome associated with compound
heterozygosity for two mutations in the KVLQT1 gene.";
Eur. J. Hum. Genet. 7:724-728(1999).
[46]
VARIANTS LQT1 SER-184; ARG-189; SER-314; SER-315; ARG-345; PRO-373 AND
ARG-392.
PubMed=10220144;
DOI=10.1002/(SICI)1098-1004(1999)13:4<301::AID-HUMU7>3.0.CO;2-V;
Jongbloed R.J.E., Wilde A.A.M., Geelen J.L.M.C., Doevendans P.,
Schaap C., van Langen I., van Tintelen J.P., Cobben J.M.,
Beaufort-Krol G.C.M., Geraedts J.P.M., Smeets H.J.M.;
"Novel KCNQ1 and HERG missense mutations in Dutch long-QT families.";
Hum. Mutat. 13:301-310(1999).
[47]
VARIANT LQT1 CYS-157.
PubMed=10220146;
DOI=10.1002/(SICI)1098-1004(1999)13:4<318::AID-HUMU9>3.0.CO;2-F;
Larsen L.A., Christiansen M., Vuust J., Andersen P.S.;
"High-throughput single-strand conformation polymorphism analysis by
automated capillary electrophoresis: robust multiplex analysis and
pattern-based identification of allelic variants.";
Hum. Mutat. 13:318-327(1999).
[48]
CHARACTERIZATION OF VARIANTS LQT1 CYS-243; ARG-248 AND LYS-261.
PubMed=10409658; DOI=10.1074/jbc.274.30.21063;
Franqueza L., Lin M., Shen J., Keating M.T., Sanguinetti M.C.;
"Long QT syndrome-associated mutations in the S4-S5 linker of KvLQT1
potassium channels modify gating and interaction with minK subunits.";
J. Biol. Chem. 274:21063-21070(1999).
[49]
ERRATUM.
Franqueza L., Lin M., Shen J., Keating M.T., Sanguinetti M.C.;
J. Biol. Chem. 274:25188-25188(1999).
[50]
VARIANTS LQT1 GLN-190; TRP-533 AND TRP-539, VARIANT JLNS1 HIS-243,
CHARACTERIZATION OF VARIANTS LQT1 GLN-190; TRP-533 AND TRP-539, AND
CHARACTERIZATION OF VARIANT JLNS1 HIS-243.
PubMed=10728423; DOI=10.1016/S0008-6363(99)00411-3;
Chouabe C., Neyroud N., Richard P., Denjoy I., Hainque B., Romey G.,
Drici M.-D., Guicheney P., Barhanin J.;
"Novel mutations in KvLQT1 that affect Iks activation through
interactions with Isk.";
Cardiovasc. Res. 45:971-980(2000).
[51]
VARIANTS LQT1.
PubMed=10973849; DOI=10.1161/01.CIR.102.10.1178;
Splawski I., Shen J., Timothy K.W., Lehmann M.H., Priori S.G.,
Robinson J.L., Moss A.J., Schwartz P.J., Towbin J.A., Vincent G.M.,
Keating M.T.;
"Spectrum of mutations in long-QT syndrome genes. KVLQT1, HERG, SCN5A,
KCNE1, and KCNE2.";
Circulation 102:1178-1185(2000).
[52]
VARIANTS LQT1 PRO-191; SER-275; LEU-277 AND VAL-306.
PubMed=12442276; DOI=10.1002/humu.9085;
Liu W., Yang J., Hu D., Kang C., Li C., Zhang S., Li P., Chen Z.,
Qin X., Ying K., Li Y., Li Y., Li Z., Cheng X., Li L., Qi Y., Chen S.,
Wang Q.;
"KCNQ1 and KCNH2 mutations associated with long QT syndrome in a
Chinese population.";
Hum. Mutat. 20:475-476(2002).
[53]
VARIANT ATFB3 GLY-140.
PubMed=12522251; DOI=10.1126/science.1077771;
Chen Y.-H., Xu S.-J., Bendahhou S., Wang X.-L., Wang Y., Xu W.-Y.,
Jin H.-W., Sun H., Su X.-Y., Zhuang Q.-N., Yang Y.-Q., Li Y.-B.,
Liu Y., Xu H.-J., Li X.-F., Ma N., Mou C.-P., Chen Z., Barhanin J.,
Huang W.;
"KCNQ1 gain-of-function mutation in familial atrial fibrillation.";
Science 299:251-254(2003).
[54]
VARIANT SQT2 LEU-307, AND CHARACTERIZATION OF VARIANT SQT2 LEU-307.
PubMed=15159330; DOI=10.1161/01.CIR.0000130409.72142.FE;
Bellocq C., van Ginneken A.C.G., Bezzina C.R., Alders M., Escande D.,
Mannens M.M.A.M., Baro I., Wilde A.A.M.;
"Mutation in the KCNQ1 gene leading to the short QT-interval
syndrome.";
Circulation 109:2394-2397(2004).
[55]
VARIANTS LQT1 71-ALA--PRO-73 DEL; THR-73; GLY-115; TYR-122; ILE-133;
PHE-136; LYS-160; ARG-168; CYS-174; GLN-190; PHE-204; LEU-225;
ASN-235; ASN-242; CYS-243; MET-254; 254-VAL--PHE-256 DEL; CYS-259;
LEU-259; ASP-261; PRO-266; SER-269; ASP-269; PHE-273; ARG-273; SER-276
DEL; LEU-277; HIS-278; LYS-290; ASP-292; CYS-293; VAL-302; ARG-304;
SER-305; ILE-312; SER-314; ARG-314; ASP-314; CYS-315; ARG-316;
ALA-322; PHE-339 DEL; VAL-341; SER-343; GLU-344; VAL-344; GLU-345;
TRP-349; PRO-353; ARG-362; TRP-366; HIS-374; SER-380; TYR-389;
TRP-452; GLY-524; GLU-526; TRP-539; LEU-546; CYS-555; HIS-555;
TYR-566; SER-567; ARG-568; MET-587; THR-590; HIS-591; GLN-594; MET-619
AND SER-626.
PubMed=15840476; DOI=10.1016/j.hrthm.2005.01.020;
Tester D.J., Will M.L., Haglund C.M., Ackerman M.J.;
"Compendium of cardiac channel mutations in 541 consecutive unrelated
patients referred for long QT syndrome genetic testing.";
Heart Rhythm 2:507-517(2005).
[56]
VARIANTS LQT1 THR-46; PHE-137; LYS-146; ASP-173; PRO-174; TRP-190;
PRO-192; HIS-202; MET-204; PHE-209; MET-215; HIS-231; PRO-239;
LEU-254; ARG-258; ASN-258; VAL-262; ASP-272; TRP-277; GLU-280;
GLU-287; THR-302; ASP-308; GLU-316; MET-322; ARG-343; LEU-343;
PRO-349; ARG-350; SER-351; THR-360; ASP-372; MET-393; GLY-518;
PRO-518; ASP-548; ALA-554; THR-567; LEU-573; HIS-583 AND ASP-586.
PubMed=16414944; DOI=10.1001/jama.294.23.2975;
Napolitano C., Priori S.G., Schwartz P.J., Bloise R., Ronchetti E.,
Nastoli J., Bottelli G., Cerrone M., Leonardi S.;
"Genetic testing in the long QT syndrome: development and validation
of an efficient approach to genotyping in clinical practice.";
JAMA 294:2975-2980(2005).
[57]
VARIANTS LQT1 CYS-231; PRO-243; CYS-259; HIS-259; PHE-273; SER-314;
GLU-316; VAL-341; VAL-344 AND SER-626.
PubMed=16922724; DOI=10.1111/j.1399-0004.2006.00671.x;
Millat G., Chevalier P., Restier-Miron L., Da Costa A., Bouvagnet P.,
Kugener B., Fayol L., Gonzalez Armengod C., Oddou B., Chanavat V.,
Froidefond E., Perraudin R., Rousson R., Rodriguez-Lafrasse C.;
"Spectrum of pathogenic mutations and associated polymorphisms in a
cohort of 44 unrelated patients with long QT syndrome.";
Clin. Genet. 70:214-227(2006).
[58]
VARIANT JLNS1 MET-322, AND VARIANT LQT1 MET-322.
PubMed=18400097; DOI=10.1186/1471-2350-9-24;
Zhang S., Yin K., Ren X., Wang P., Zhang S., Cheng L., Yang J.,
Liu J.Y., Liu M., Wang Q.K.;
"Identification of a novel KCNQ1 mutation associated with both Jervell
and Lange-Nielsen and Romano-Ward forms of long QT syndrome in a
Chinese family.";
BMC Med. Genet. 9:24-24(2008).
[59]
VARIANT JLNS1 PHE-248, AND CHARACTERIZATION OF VARIANT JLNS1 PHE-248.
PubMed=18441444; DOI=10.1253/circj.72.687;
Ohno S., Kubota T., Yoshida H., Tsuji K., Makiyama T., Yamada S.,
Kuga K., Yamaguchi I., Kita T., Horie M.;
"A novel mutation associated with Jervell and Lange-Nielsen syndrome
in a Japanese family.";
Circ. J. 72:687-693(2008).
[60]
INVOLVEMENT IN NIDDM.
PubMed=18711367; DOI=10.1038/ng.207;
Yasuda K., Miyake K., Horikawa Y., Hara K., Osawa H., Furuta H.,
Hirota Y., Mori H., Jonsson A., Sato Y., Yamagata K., Hinokio Y.,
Wang H.Y., Tanahashi T., Nakamura N., Oka Y., Iwasaki N., Iwamoto Y.,
Yamada Y., Seino Y., Maegawa H., Kashiwagi A., Takeda J., Maeda E.,
Shin H.D., Cho Y.M., Park K.S., Lee H.K., Ng M.C., Ma R.C., So W.Y.,
Chan J.C., Lyssenko V., Tuomi T., Nilsson P., Groop L., Kamatani N.,
Sekine A., Nakamura Y., Yamamoto K., Yoshida T., Tokunaga K.,
Itakura M., Makino H., Nanjo K., Kadowaki T., Kasuga M.;
"Variants in KCNQ1 are associated with susceptibility to type 2
diabetes mellitus.";
Nat. Genet. 40:1092-1097(2008).
[61]
INVOLVEMENT IN NIDDM.
PubMed=18711366; DOI=10.1038/ng.208;
Unoki H., Takahashi A., Kawaguchi T., Hara K., Horikoshi M.,
Andersen G., Ng D.P., Holmkvist J., Borch-Johnsen K., Jorgensen T.,
Sandbaek A., Lauritzen T., Hansen T., Nurbaya S., Tsunoda T., Kubo M.,
Babazono T., Hirose H., Hayashi M., Iwamoto Y., Kashiwagi A., Kaku K.,
Kawamori R., Tai E.S., Pedersen O., Kamatani N., Kadowaki T.,
Kikkawa R., Nakamura Y., Maeda S.;
"SNPs in KCNQ1 are associated with susceptibility to type 2 diabetes
in East Asian and European populations.";
Nat. Genet. 40:1098-1102(2008).
[62]
INVOLVEMENT IN NIDDM.
PubMed=24390345; DOI=10.1038/nature12828;
The SIGMA Type 2 Diabetes Consortium;
"Sequence variants in SLC16A11 are a common risk factor for type 2
diabetes in Mexico.";
Nature 506:97-101(2014).
[63]
VARIANTS LQT1 VAL-2; SER-7; THR-46; 64-PRO--PRO-70 DEL; PHE-66;
THR-73; CYS-111; LEU-117; LEU-127; ILE-133; PRO-134; ALA-144; MET-153;
MET-162; ARG-168; MET-172; CYS-174; HIS-174; THR-178; SER-179;
HIS-184; ARG-186; GLN-190; LEU-190; TRP-195; VAL-198; ALA-199;
MET-204; MET-215; MET-224; LEU-225; CYS-231; HIS-231; ASN-235;
GLY-241; ASN-242; CYS-243; PRO-250; MET-254; CYS-259; LEU-259;
VAL-262; PRO-266; SER-268; ASP-269; SER-269; ASP-272; PHE-273;
VAL-274; LEU-277; PRO-277; GLU-280; CYS-281; PRO-282; GLY-283;
ASP-292; CYS-293; GLU-302; VAL-302; PRO-303; ARG-305; SER-305;
ARG-306; ILE-312; CYS-314; SER-314; CYS-315; VAL-316; SER-320;
ALA-322; MET-322; ARG-325; TYR-339; GLU-341; GLY-341; VAL-341;
PHE-342; LEU-343; ARG-350; SER-351; ARG-354; MET-360; ARG-362;
HIS-365; GLN-366; TRP-366; HIS-374; GLY-379; LYS-385; PRO-389; THR-391
INS; TRP-397; ARG-398; GLU-446; LEU-448; TRP-451; SER-460; LEU-477;
TRP-511; GLN-518; ARG-520; SER-522; GLY-524; THR-525; VAL-525;
TRP-533; GLN-539; TRP-539; ILE-541; LYS-543; LEU-546; ARG-547;
CYS-555; HIS-555; SER-555; GLU-557; PHE-566; PRO-566; TYR-566;
THR-567; ARG-568; GLU-569; LEU-571; MET-587; ASP-589; CYS-591;
HIS-591; GLN-594; PRO-594; GLU-596 DEL; LYS-596; MET-600; ASN-611;
HIS-614 DEL; SER-626 AND ARG-635.
PubMed=19716085; DOI=10.1016/j.hrthm.2009.05.021;
Kapplinger J.D., Tester D.J., Salisbury B.A., Carr J.L.,
Harris-Kerr C., Pollevick G.D., Wilde A.A., Ackerman M.J.;
"Spectrum and prevalence of mutations from the first 2,500 consecutive
unrelated patients referred for the FAMILION long QT syndrome genetic
test.";
Heart Rhythm 6:1297-1303(2009).
[64]
VARIANT LQT1 HIS-320, AND CHARACTERIZATION OF VARIANTS LQT1 ALA-320
AND HIS-320.
PubMed=19540844; DOI=10.1016/j.yjmcc.2009.06.009;
Thomas D., Khalil M., Alter M., Schweizer P.A., Karle C.A.,
Wimmer A.B., Licka M., Katus H.A., Koenen M., Ulmer H.E., Zehelein J.;
"Biophysical characterization of KCNQ1 P320 mutations linked to long
QT syndrome 1.";
J. Mol. Cell. Cardiol. 48:230-237(2010).
[65]
VARIANT LQT1 LEU-277, AND CHARACTERIZATION OF VARIANT LQT1 LEU-277.
PubMed=21241800; DOI=10.1016/j.bbadis.2011.01.008;
Aidery P., Kisselbach J., Schweizer P.A., Becker R., Katus H.A.,
Thomas D.;
"Biophysical properties of mutant KCNQ1 S277L channels linked to
hereditary long QT syndrome with phenotypic variability.";
Biochim. Biophys. Acta 1812:488-494(2011).
[66]
VARIANT LQT1 GLU-557, AND CHARACTERIZATION OF VARIANT LQT1 GLU-557.
PubMed=25139741; DOI=10.1093/cvr/cvu191;
Spaetjens R.L., Bebarova M., Seyen S.R., Lentink V., Jongbloed R.J.,
Arens Y.H., Heijman J., Volders P.G.;
"Long-QT mutation p.K557E-Kv7.1: dominant-negative suppression of IKs,
but preserved cAMP-dependent up-regulation.";
Cardiovasc. Res. 104:216-225(2014).
[67]
VARIANTS LQT1 ASN-235; CYS-315 AND ALA-322, AND CHARACTERIZATION OF
VARIANT LQT1 ASN-235.
PubMed=24269949; DOI=10.1016/j.hrthm.2013.11.021;
Bartos D.C., Giudicessi J.R., Tester D.J., Ackerman M.J., Ohno S.,
Horie M., Gollob M.H., Burgess D.E., Delisle B.P.;
"A KCNQ1 mutation contributes to the concealed type 1 long QT
phenotype by limiting the Kv7.1 channel conformational changes
associated with protein kinase A phosphorylation.";
Heart Rhythm 11:459-468(2014).
[68]
VARIANT LQT1 SER-269, AND CHARACTERIZATION OF VARIANT LQT1 SER-269.
PubMed=24184248; DOI=10.1016/j.jacc.2013.08.1648;
Wu J., Naiki N., Ding W.G., Ohno S., Kato K., Zang W.J., Delisle B.P.,
Matsuura H., Horie M.;
"A molecular mechanism for adrenergic-induced long QT syndrome.";
J. Am. Coll. Cardiol. 63:819-827(2014).
[69]
CHARACTERIZATION OF VARIANTS LQT1 LEU-546; CYS-555; HIS-555; GLU-557
AND ASP-589, INTERACTION WITH KCNE1 AND AKAP9, SUBCELLULAR LOCATION,
AND FUNCTION.
PubMed=25037568; DOI=10.1242/jcs.147033;
Dvir M., Strulovich R., Sachyani D., Ben-Tal Cohen I., Haitin Y.,
Dessauer C., Pongs O., Kass R., Hirsch J.A., Attali B.;
"Long QT mutations at the interface between KCNQ1 helix C and KCNE1
disrupt I(KS) regulation by PKA and PIP(2).";
J. Cell Sci. 127:3943-3955(2014).
[70]
VARIANT LQT1 THR-590, AND CHARACTERIZATION OF VARIANT LQT1 THR-590.
PubMed=24713462; DOI=10.1016/j.yjmcc.2014.03.019;
Kinoshita K., Komatsu T., Nishide K., Hata Y., Hisajima N.,
Takahashi H., Kimoto K., Aonuma K., Tsushima E., Tabata T.,
Yoshida T., Mori H., Nishida K., Yamaguchi Y., Ichida F.,
Fukurotani K., Inoue H., Nishida N.;
"A590T mutation in KCNQ1 C-terminal helix D decreases IKs channel
trafficking and function but not Yotiao interaction.";
J. Mol. Cell. Cardiol. 72:273-280(2014).
[71]
CHARACTERIZATION OF VARIANTS LQT1 ASN-242; PRO-243; HIS-250; VAL-306;
ASN-317; ASP-586 AND MET-619, AND CHARACTERIZATION OF VARIANTS JLNS1
PHE-248; ILE-311; MET-322 AND ASP-589.
PubMed=25705178; DOI=10.3389/fncel.2015.00032;
Mousavi Nik A., Gharaie S., Jeong Kim H.;
"Cellular mechanisms of mutations in Kv7.1: auditory functions in
Jervell and Lange-Nielsen syndrome vs. Romano-Ward syndrome.";
Front. Cell. Neurosci. 9:32-32(2015).
-!- FUNCTION: Potassium channel that plays an important role in a
number of tissues, including heart, inner ear, stomach and colon
(By similarity) (PubMed:10646604). Associates with KCNE beta
subunits that modulates current kinetics (By similarity)
(PubMed:9312006, PubMed:9108097, PubMed:8900283, PubMed:10646604,
PubMed:11101505, PubMed:19687231). Induces a voltage-dependent by
rapidly activating and slowly deactivating potassium-selective
outward current (By similarity) (PubMed:9312006, PubMed:9108097,
PubMed:8900283, PubMed:10646604, PubMed:11101505). Promotes also a
delayed voltage activated potassium current showing outward
rectification characteristic (By similarity). During beta-
adrenergic receptor stimulation participates in cardiac
repolarization by associating with KCNE1 to form the I(Ks) cardiac
potassium current that increases the amplitude and slows down the
activation kinetics of outward potassium current I(Ks) (By
similarity) (PubMed:9312006, PubMed:9108097, PubMed:8900283,
PubMed:10646604, PubMed:11101505). Muscarinic agonist
oxotremorine-M strongly suppresses KCNQ1/KCNE1 current
(PubMed:10713961). When associated with KCNE3, forms the potassium
channel that is important for cyclic AMP-stimulated intestinal
secretion of chloride ions (PubMed:10646604). This interaction
with KCNE3 is reduced by 17beta-estradiol, resulting in the
reduction of currents (By similarity). During conditions of
increased substrate load, maintains the driving force for proximal
tubular and intestinal sodium ions absorption, gastric acid
secretion, and cAMP-induced jejunal chloride ions secretion (By
similarity). Allows the provision of potassium ions to the luminal
membrane of the secretory canaliculus in the resting state as well
as during stimulated acid secretion (By similarity). When
associated with KCNE2, forms a heterooligomer complex leading to
currents with an apparently instantaneous activation, a rapid
deactivation process and a linear current-voltage relationship and
decreases the amplitude of the outward current (PubMed:11101505).
When associated with KCNE4, inhibits voltage-gated potassium
channel activity (PubMed:19687231). When associated with KCNE5,
this complex only conducts current upon strong and continued
depolarization (PubMed:12324418). Also forms a heterotetramer with
KCNQ5; has a voltage-gated potassium channel activity
(PubMed:24855057). Binds with phosphatidylinositol 4,5-
bisphosphate (PubMed:25037568). {ECO:0000250|UniProtKB:P97414,
ECO:0000250|UniProtKB:Q9Z0N7, ECO:0000269|PubMed:10646604,
ECO:0000269|PubMed:10713961, ECO:0000269|PubMed:11101505,
ECO:0000269|PubMed:12324418, ECO:0000269|PubMed:19687231,
ECO:0000269|PubMed:24855057, ECO:0000269|PubMed:25037568,
ECO:0000269|PubMed:8900283, ECO:0000269|PubMed:9108097,
ECO:0000269|PubMed:9312006}.
-!- FUNCTION: Isoform 2: Non-functional alone but modulatory when
coexpressed with the full-length isoform 1.
{ECO:0000269|PubMed:9305853}.
-!- SUBUNIT: Tetramer (PubMed:18165683, PubMed:19693805).
Heterotetramer with KCNE1; targets to the membrane raft
(PubMed:25037568, PubMed:19693805, PubMed:20533308). Interacts
(via C-terminus) with CALM; forms a heterotetramer in a calcium-
independent manner (PubMed:18165683). Interacts with AKAP9;
targets protein kinase A (PKA) catalytic and regulatory subunits
and protein phosphatase 1 (PP1) to the KCNQ1-KCNE1 complex,
allowing PKA-mediated phosphorylation and increase of delayed
rectifier potassium channel activity (PubMed:11799244,
PubMed:25037568). Interacts with KCNE2; forms a heterooligomer
complex that targets to the membrane raft and leading to currents
with an apparently instantaneous activation, a rapid deactivation
process and a linear current-voltage relationship and decreases
the amplitude of the outward current (PubMed:11101505,
PubMed:20533308). Interacts with AP2M1; mediates estrogen-induced
internalization via clathrin-coated vesicles (PubMed:23529131).
Interacts with NEDD4L; promotes internalization and decreases
I(Ks) currents (PubMed:23529131, PubMed:22024150). Interacts with
USP2; counteracts the NEDD4L-specific down-regulation of I(Ks) and
restore plasma membrane localization (PubMed:22024150).
Heterotetramer with KCNQ5; has a voltage-gated potassium channel
activity (PubMed:24855057). Interacts with KCNE3; alters membrane
raft localization (PubMed:20533308). Interacts with KCNE4; impairs
KCNQ1 localization in lipid rafts and inhibits voltage-gated
potassium channel activity (PubMed:19687231, PubMed:20533308).
Interacts with KCNE5; impairs KCNQ1 localization in lipid rafts
and only conducts current upon strong and continued depolarization
(PubMed:20533308, PubMed:12324418). {ECO:0000269|PubMed:11101505,
ECO:0000269|PubMed:11799244, ECO:0000269|PubMed:12324418,
ECO:0000269|PubMed:18165683, ECO:0000269|PubMed:19687231,
ECO:0000269|PubMed:19693805, ECO:0000269|PubMed:20533308,
ECO:0000269|PubMed:22024150, ECO:0000269|PubMed:23529131,
ECO:0000269|PubMed:24855057, ECO:0000269|PubMed:25037568}.
-!- INTERACTION:
P15382:KCNE1; NbExp=4; IntAct=EBI-359667, EBI-7043557;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10646604,
ECO:0000269|PubMed:18165683, ECO:0000269|PubMed:21228319,
ECO:0000269|PubMed:22024150, ECO:0000269|PubMed:25037568}; Multi-
pass membrane protein {ECO:0000269|PubMed:18165683}. Cytoplasmic
vesicle membrane {ECO:0000269|PubMed:18165683,
ECO:0000269|PubMed:23529131}. Early endosome
{ECO:0000269|PubMed:23529131}. Membrane raft
{ECO:0000269|PubMed:20533308, ECO:0000269|PubMed:24855057}.
Endoplasmic reticulum {ECO:0000269|PubMed:21228319,
ECO:0000269|PubMed:24855057}. Basolateral cell membrane
{ECO:0000269|PubMed:21228319}. Note=Colocalized with KCNE3 at the
plasma membrane (PubMed:10646604). Upon 17beta-oestradiol
treatment, colocalizes with RAB5A at early endosome
(PubMed:23529131). Heterotetramer with KCNQ5 is highly retained at
the endoplasmic reticulum and is localized outside of lipid raft
microdomains (PubMed:24855057). During the early stages of
epithelial cell polarization induced by the calcium switch it
removed from plasma membrane to the endoplasmic reticulum where it
retained and it is redistributed to the basolateral cell surface
in a PI3K-dependent manner at a later stage (PubMed:21228319).
{ECO:0000269|PubMed:10646604, ECO:0000269|PubMed:21228319,
ECO:0000269|PubMed:23529131, ECO:0000269|PubMed:24855057}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Comment=Additional isoforms seem to exist.;
Name=1;
IsoId=P51787-1; Sequence=Displayed;
Name=2; Synonyms=TKvLQT1;
IsoId=P51787-2; Sequence=VSP_000981, VSP_000982;
-!- TISSUE SPECIFICITY: Abundantly expressed in heart, pancreas,
prostate, kidney, small intestine and peripheral blood leukocytes.
Less abundant in placenta, lung, spleen, colon, thymus, testis and
ovaries.
-!- DOMAIN: The segment S4 is probably the voltage-sensor and is
characterized by a series of positively charged amino acids at
every third position.
-!- DOMAIN: The coiled-coil domain mediates tetramerization.
{ECO:0000269|PubMed:18165683, ECO:0000269|PubMed:19693805}.
-!- DOMAIN: The segment S6 is involved in the inhibition of voltage-
gated potassium channel activity by KCNE4.
{ECO:0000269|PubMed:19687231}.
-!- DOMAIN: The C-terminal assembly domain promotes self-interactiona;
allows functional channel. {ECO:0000269|PubMed:10654932}.
-!- PTM: Phosphorylation at Ser-27 by PKA; increases delayed rectifier
potassium channel activity of the KCNQ1-KCNE1 complex through a
macromolecular complex that includes PKA, PP1, and the targeting
protein AKAP9. {ECO:0000269|PubMed:11799244,
ECO:0000269|PubMed:25037568}.
-!- PTM: Ubiquitinated by NEDD4L; promotes internalization
(PubMed:22024150). The ubiquitinylated form is internalized
through a clathrin-mediated endocytosis by interacting with AP2M1
and is recycled back to the cell membrane via RAB4A and RAB11A
(PubMed:23529131). {ECO:0000269|PubMed:22024150,
ECO:0000269|PubMed:23529131}.
-!- PTM: Deubiquitinated by USP2; counteracts the NEDD4L-specific
down-regulation of I(Ks) and restores the membrane localization.
{ECO:0000269|PubMed:22024150}.
-!- DISEASE: Long QT syndrome 1 (LQT1) [MIM:192500]: A heart disorder
characterized by a prolonged QT interval on the ECG and
polymorphic ventricular arrhythmias. They cause syncope and sudden
death in response to exercise or emotional stress, and can present
with a sentinel event of sudden cardiac death in infancy.
{ECO:0000269|PubMed:10024302, ECO:0000269|PubMed:10220144,
ECO:0000269|PubMed:10220146, ECO:0000269|PubMed:10367071,
ECO:0000269|PubMed:10409658, ECO:0000269|PubMed:10482963,
ECO:0000269|PubMed:10728423, ECO:0000269|PubMed:10973849,
ECO:0000269|PubMed:11799244, ECO:0000269|PubMed:12442276,
ECO:0000269|PubMed:15840476, ECO:0000269|PubMed:16414944,
ECO:0000269|PubMed:16922724, ECO:0000269|PubMed:18165683,
ECO:0000269|PubMed:18400097, ECO:0000269|PubMed:19540844,
ECO:0000269|PubMed:19716085, ECO:0000269|PubMed:21241800,
ECO:0000269|PubMed:24184248, ECO:0000269|PubMed:24269949,
ECO:0000269|PubMed:24713462, ECO:0000269|PubMed:25037568,
ECO:0000269|PubMed:25139741, ECO:0000269|PubMed:25705178,
ECO:0000269|PubMed:8528244, ECO:0000269|PubMed:8818942,
ECO:0000269|PubMed:8872472, ECO:0000269|PubMed:9024139,
ECO:0000269|PubMed:9272155, ECO:0000269|PubMed:9302275,
ECO:0000269|PubMed:9312006, ECO:0000269|PubMed:9323054,
ECO:0000269|PubMed:9386136, ECO:0000269|PubMed:9482580,
ECO:0000269|PubMed:9570196, ECO:0000269|PubMed:9641694,
ECO:0000269|PubMed:9693036, ECO:0000269|PubMed:9702906,
ECO:0000269|PubMed:9799083, ECO:0000269|PubMed:9927399,
ECO:0000269|Ref.31}. Note=The disease is caused by mutations
affecting the gene represented in this entry.
-!- DISEASE: Jervell and Lange-Nielsen syndrome 1 (JLNS1)
[MIM:220400]: An autosomal recessive disorder characterized by
congenital deafness, prolongation of the QT interval, syncopal
attacks due to ventricular arrhythmias, and a high risk of sudden
death. {ECO:0000269|PubMed:10090886, ECO:0000269|PubMed:10728423,
ECO:0000269|PubMed:18400097, ECO:0000269|PubMed:18441444,
ECO:0000269|PubMed:25705178, ECO:0000269|PubMed:9781056}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Atrial fibrillation, familial, 3 (ATFB3) [MIM:607554]: An
autosomal dominant form of atrial fibrillation, a common sustained
cardiac rhythm disturbance. Atrial fibrillation is characterized
by disorganized atrial electrical activity and ineffective atrial
contraction promoting blood stasis in the atria and reduces
ventricular filling. It can result in palpitations, syncope,
thromboembolic stroke, and congestive heart failure.
{ECO:0000269|PubMed:12522251}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Short QT syndrome 2 (SQT2) [MIM:609621]: A heart disorder
characterized by idiopathic persistently and uniformly short QT
interval on ECG in the absence of structural heart disease in
affected individuals. It causes syncope and sudden death.
{ECO:0000269|PubMed:15159330}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Diabetes mellitus, non-insulin-dependent (NIDDM)
[MIM:125853]: A multifactorial disorder of glucose homeostasis
caused by a lack of sensitivity to the body's own insulin.
Affected individuals usually have an obese body habitus and
manifestations of a metabolic syndrome characterized by diabetes,
insulin resistance, hypertension and hypertriglyceridemia. The
disease results in long-term complications that affect the eyes,
kidneys, nerves, and blood vessels. {ECO:0000269|PubMed:18711366,
ECO:0000269|PubMed:18711367, ECO:0000269|PubMed:24390345}.
Note=Disease susceptibility is associated with variations
affecting the gene represented in this entry.
-!- MISCELLANEOUS: Mutagenesis experiments were carried out by
expressing in Xenopus oocytes or COS-7 cells KCNQ1 mutants either
individually (homomultimers) or in combination with both wild-type
KCNQ1 (mut/wt homomultimers) and minK (heteromultimers).
-!- SIMILARITY: Belongs to the potassium channel family. KQT (TC
1.A.1.15) subfamily. Kv7.1/KCNQ1 sub-subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAC51781.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part.; Evidence={ECO:0000305};
Sequence=BAA34739.1; Type=Frameshift; Positions=129, 159; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Wikipedia; Note=KvLQT1 entry;
URL="https://en.wikipedia.org/wiki/KvLQT1";
-----------------------------------------------------------------------
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EMBL; AF000571; AAC51776.1; -; mRNA.
EMBL; AF051426; AAC05705.1; -; mRNA.
EMBL; AB015163; BAA34738.1; -; Genomic_DNA.
EMBL; AB015163; BAA34739.1; ALT_FRAME; Genomic_DNA.
EMBL; AJ006345; CAB44649.1; -; Genomic_DNA.
EMBL; AJ006345; CAB44650.1; -; Genomic_DNA.
EMBL; AY114213; AAM94040.1; -; mRNA.
EMBL; AK290618; BAF83307.1; -; mRNA.
EMBL; AC013791; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC021424; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC124055; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC124057; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP006463; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; KF455303; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; KF455304; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; KF455305; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; KF455306; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; KF459741; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471158; EAX02517.1; -; Genomic_DNA.
EMBL; BC113545; AAI13546.1; -; mRNA.
EMBL; U86146; AAB53974.1; -; mRNA.
EMBL; U89364; AAC51781.1; ALT_SEQ; mRNA.
CCDS; CCDS7736.1; -. [P51787-1]
RefSeq; NP_000209.2; NM_000218.2. [P51787-1]
RefSeq; NP_861463.1; NM_181798.1. [P51787-2]
UniGene; Hs.95162; -.
PDB; 3BJ4; X-ray; 2.00 A; A/B=574-622.
PDB; 3HFC; X-ray; 2.45 A; A/B/C=583-611.
PDB; 3HFE; X-ray; 1.70 A; A/B/C=583-611.
PDB; 4UMO; X-ray; 3.00 A; A/B=352-539.
PDB; 4V0C; X-ray; 2.86 A; A/B=352-539.
PDBsum; 3BJ4; -.
PDBsum; 3HFC; -.
PDBsum; 3HFE; -.
PDBsum; 4UMO; -.
PDBsum; 4V0C; -.
ProteinModelPortal; P51787; -.
SMR; P51787; -.
BioGrid; 109985; 15.
DIP; DIP-27591N; -.
DIP; DIP-29941N; -.
IntAct; P51787; 4.
MINT; MINT-1145466; -.
STRING; 9606.ENSP00000155840; -.
BindingDB; P51787; -.
ChEMBL; CHEMBL1866; -.
DrugBank; DB04957; Azimilide.
DrugBank; DB01244; Bepridil.
DrugBank; DB06089; ICA-105665.
DrugBank; DB00808; Indapamide.
GuidetoPHARMACOLOGY; 560; -.
TCDB; 1.A.1.15.6; the voltage-gated ion channel (vic) superfamily.
iPTMnet; P51787; -.
PhosphoSitePlus; P51787; -.
BioMuta; KCNQ1; -.
DMDM; 6166005; -.
PaxDb; P51787; -.
PeptideAtlas; P51787; -.
PRIDE; P51787; -.
DNASU; 3784; -.
Ensembl; ENST00000155840; ENSP00000155840; ENSG00000053918. [P51787-1]
Ensembl; ENST00000335475; ENSP00000334497; ENSG00000053918. [P51787-2]
GeneID; 3784; -.
KEGG; hsa:3784; -.
UCSC; uc001lwn.4; human. [P51787-1]
CTD; 3784; -.
DisGeNET; 3784; -.
GeneCards; KCNQ1; -.
GeneReviews; KCNQ1; -.
HGNC; HGNC:6294; KCNQ1.
HPA; CAB018656; -.
HPA; HPA048553; -.
MalaCards; KCNQ1; -.
MIM; 125853; phenotype.
MIM; 192500; phenotype.
MIM; 220400; phenotype.
MIM; 607542; gene.
MIM; 607554; phenotype.
MIM; 609621; phenotype.
neXtProt; NX_P51787; -.
OpenTargets; ENSG00000053918; -.
Orphanet; 334; Familial atrial fibrillation.
Orphanet; 51083; Familial short QT syndrome.
Orphanet; 90647; Jervell and Lange-Nielsen syndrome.
Orphanet; 101016; Romano-Ward syndrome.
PharmGKB; PA223; -.
eggNOG; KOG1419; Eukaryota.
eggNOG; COG1226; LUCA.
GeneTree; ENSGT00550000074513; -.
HOGENOM; HOG000220839; -.
HOVERGEN; HBG059014; -.
InParanoid; P51787; -.
KO; K04926; -.
OMA; ERKRWGW; -.
OrthoDB; EOG091G02ZT; -.
PhylomeDB; P51787; -.
TreeFam; TF315186; -.
Reactome; R-HSA-1296072; Voltage gated Potassium channels.
Reactome; R-HSA-5576890; Phase 3 - rapid repolarisation.
Reactome; R-HSA-5576893; Phase 2 - plateau phase.
SignaLink; P51787; -.
ChiTaRS; KCNQ1; human.
EvolutionaryTrace; P51787; -.
GeneWiki; KvLQT1; -.
GenomeRNAi; 3784; -.
PRO; PR:P51787; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000053918; -.
CleanEx; HS_KCNQ1; -.
ExpressionAtlas; P51787; baseline and differential.
Genevisible; P51787; HS.
GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0005769; C:early endosome; IDA:BHF-UCL.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0034702; C:ion channel complex; IPI:UniProtKB.
GO; GO:0005770; C:late endosome; IDA:BHF-UCL.
GO; GO:0005764; C:lysosome; IDA:BHF-UCL.
GO; GO:0045121; C:membrane raft; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0008076; C:voltage-gated potassium channel complex; IDA:BHF-UCL.
GO; GO:0005516; F:calmodulin binding; IDA:BHF-UCL.
GO; GO:0005251; F:delayed rectifier potassium channel activity; IDA:UniProtKB.
GO; GO:0044325; F:ion channel binding; IPI:UniProtKB.
GO; GO:0015271; F:outward rectifier potassium channel activity; IDA:UniProtKB.
GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:UniProtKB.
GO; GO:0034236; F:protein kinase A catalytic subunit binding; IDA:BHF-UCL.
GO; GO:0034237; F:protein kinase A regulatory subunit binding; IDA:BHF-UCL.
GO; GO:0008157; F:protein phosphatase 1 binding; IDA:BHF-UCL.
GO; GO:0097110; F:scaffold protein binding; IPI:BHF-UCL.
GO; GO:0005249; F:voltage-gated potassium channel activity; IDA:UniProtKB.
GO; GO:0086089; F:voltage-gated potassium channel activity involved in atrial cardiac muscle cell action potential repolarization; IMP:BHF-UCL.
GO; GO:0086008; F:voltage-gated potassium channel activity involved in cardiac muscle cell action potential repolarization; IMP:BHF-UCL.
GO; GO:1902282; F:voltage-gated potassium channel activity involved in ventricular cardiac muscle cell action potential repolarization; IMP:BHF-UCL.
GO; GO:0086014; P:atrial cardiac muscle cell action potential; IMP:BHF-UCL.
GO; GO:0061337; P:cardiac conduction; TAS:Reactome.
GO; GO:0060048; P:cardiac muscle contraction; IMP:BHF-UCL.
GO; GO:0072358; P:cardiovascular system development; IEA:Ensembl.
GO; GO:0071320; P:cellular response to cAMP; IDA:BHF-UCL.
GO; GO:0035690; P:cellular response to drug; IDA:BHF-UCL.
GO; GO:0071872; P:cellular response to epinephrine stimulus; TAS:BHF-UCL.
GO; GO:0016458; P:gene silencing; IEA:Ensembl.
GO; GO:0048839; P:inner ear development; ISS:UniProtKB.
GO; GO:0050892; P:intestinal absorption; ISS:UniProtKB.
GO; GO:0086011; P:membrane repolarization during action potential; IDA:BHF-UCL.
GO; GO:0098914; P:membrane repolarization during atrial cardiac muscle cell action potential; IMP:BHF-UCL.
GO; GO:0086013; P:membrane repolarization during cardiac muscle cell action potential; IMP:BHF-UCL.
GO; GO:0098915; P:membrane repolarization during ventricular cardiac muscle cell action potential; IMP:BHF-UCL.
GO; GO:1902260; P:negative regulation of delayed rectifier potassium channel activity; IDA:UniProtKB.
GO; GO:1903817; P:negative regulation of voltage-gated potassium channel activity; IDA:UniProtKB.
GO; GO:0060452; P:positive regulation of cardiac muscle contraction; IMP:BHF-UCL.
GO; GO:0010460; P:positive regulation of heart rate; IMP:BHF-UCL.
GO; GO:1901381; P:positive regulation of potassium ion transmembrane transport; IDA:BHF-UCL.
GO; GO:0071435; P:potassium ion export; IDA:BHF-UCL.
GO; GO:0097623; P:potassium ion export across plasma membrane; IDA:BHF-UCL.
GO; GO:0071805; P:potassium ion transmembrane transport; IDA:BHF-UCL.
GO; GO:0060372; P:regulation of atrial cardiac muscle cell membrane repolarization; IMP:BHF-UCL.
GO; GO:0060453; P:regulation of gastric acid secretion; ISS:UniProtKB.
GO; GO:0006349; P:regulation of gene expression by genetic imprinting; IEA:Ensembl.
GO; GO:0008016; P:regulation of heart contraction; IC:BHF-UCL.
GO; GO:0086091; P:regulation of heart rate by cardiac conduction; IMP:BHF-UCL.
GO; GO:0060306; P:regulation of membrane repolarization; IDA:BHF-UCL.
GO; GO:0060307; P:regulation of ventricular cardiac muscle cell membrane repolarization; IMP:BHF-UCL.
GO; GO:0070293; P:renal absorption; ISS:UniProtKB.
GO; GO:0007605; P:sensory perception of sound; TAS:ProtInc.
GO; GO:0086005; P:ventricular cardiac muscle cell action potential; IMP:BHF-UCL.
InterPro; IPR005821; Ion_trans_dom.
InterPro; IPR003937; K_chnl_volt-dep_KCNQ.
InterPro; IPR013821; K_chnl_volt-dep_KCNQ_C.
InterPro; IPR005827; K_chnl_volt-dep_KCQN1.
InterPro; IPR028325; VG_K_chnl.
PANTHER; PTHR11537; PTHR11537; 1.
PANTHER; PTHR11537:SF189; PTHR11537:SF189; 1.
Pfam; PF00520; Ion_trans; 1.
Pfam; PF03520; KCNQ_channel; 1.
PRINTS; PR00169; KCHANNEL.
PRINTS; PR01460; KCNQ1CHANNEL.
PRINTS; PR01459; KCNQCHANNEL.
1: Evidence at protein level;
3D-structure; Alternative splicing; Atrial fibrillation;
Calmodulin-binding; Cell membrane; Coiled coil; Complete proteome;
Cytoplasmic vesicle; Deafness; Diabetes mellitus; Disease mutation;
Endoplasmic reticulum; Endosome; Glycoprotein; Ion channel;
Ion transport; Long QT syndrome; Membrane; Phosphoprotein;
Polymorphism; Potassium; Potassium channel; Potassium transport;
Reference proteome; Short QT syndrome; Transmembrane;
Transmembrane helix; Transport; Ubl conjugation;
Voltage-gated channel.
CHAIN 1 676 Potassium voltage-gated channel subfamily
KQT member 1.
/FTId=PRO_0000054022.
TOPO_DOM 1 121 Cytoplasmic. {ECO:0000255}.
TRANSMEM 122 142 Helical; Name=Segment S1. {ECO:0000255}.
TOPO_DOM 143 147 Extracellular. {ECO:0000255}.
TRANSMEM 148 168 Helical; Name=Segment S2. {ECO:0000255}.
TOPO_DOM 169 196 Cytoplasmic. {ECO:0000255}.
TRANSMEM 197 217 Helical; Name=Segment S3. {ECO:0000255}.
TOPO_DOM 218 225 Extracellular. {ECO:0000255}.
TRANSMEM 226 248 Helical; Voltage-sensor; Name=Segment S4.
{ECO:0000255}.
TOPO_DOM 249 261 Cytoplasmic. {ECO:0000255}.
TRANSMEM 262 282 Helical; Name=Segment S5. {ECO:0000255}.
TOPO_DOM 283 299 Extracellular. {ECO:0000255}.
INTRAMEM 300 320 Pore-forming; Name=Segment H5.
{ECO:0000255}.
TOPO_DOM 321 327 Extracellular. {ECO:0000255}.
TRANSMEM 328 348 Helical; Name=Segment S6. {ECO:0000255}.
TOPO_DOM 349 676 Cytoplasmic. {ECO:0000255}.
REGION 535 572 Interaction with KCNE1 C-terminus.
{ECO:0000269|PubMed:25037568}.
REGION 588 616 Interaction with AKAP9.
{ECO:0000269|PubMed:11799244}.
REGION 589 620 C-terminal assembly domain.
{ECO:0000269|PubMed:10654932}.
COILED 585 621 {ECO:0000269|PubMed:19693805}.
MOTIF 312 317 Selectivity filter. {ECO:0000250}.
MOD_RES 27 27 Phosphoserine; by PKA.
{ECO:0000269|PubMed:11799244}.
MOD_RES 407 407 Phosphoserine.
{ECO:0000250|UniProtKB:P97414}.
MOD_RES 409 409 Phosphoserine.
{ECO:0000250|UniProtKB:P97414}.
CARBOHYD 289 289 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 1 127 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:9305853}.
/FTId=VSP_000981.
VAR_SEQ 128 129 AV -> MD (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:9305853}.
/FTId=VSP_000982.
VARIANT 2 2 A -> V (in LQT1; unknown pathological
significance; dbSNP:rs199473442).
{ECO:0000269|PubMed:19716085}.
/FTId=VAR_074927.
VARIANT 7 7 P -> S (in LQT1; unknown pathological
significance; dbSNP:rs199473443).
{ECO:0000269|PubMed:19716085}.
/FTId=VAR_074928.
VARIANT 46 46 A -> T (in LQT1; dbSNP:rs199473671).
{ECO:0000269|PubMed:16414944,
ECO:0000269|PubMed:19716085}.
/FTId=VAR_074929.
VARIANT 64 70 Missing (in LQT1; unknown pathological
significance).
{ECO:0000269|PubMed:19716085}.
/FTId=VAR_074930.
VARIANT 66 66 S -> F (in LQT1; unknown pathological
significance; dbSNP:rs199473446).
{ECO:0000269|PubMed:19716085}.
/FTId=VAR_074931.
VARIANT 71 73 Missing (in LQT1).
{ECO:0000269|PubMed:15840476}.
/FTId=VAR_009917.
VARIANT 73 73 P -> T (in LQT1; dbSNP:rs199472676).
{ECO:0000269|PubMed:15840476,
ECO:0000269|PubMed:19716085}.
/FTId=VAR_068287.
VARIANT 111 111 Y -> C (in LQT1; unknown pathological
significance; dbSNP:rs199472678).
{ECO:0000269|PubMed:19716085}.
/FTId=VAR_009918.
VARIANT 115 115 E -> G (in LQT1; dbSNP:rs199472679).
{ECO:0000269|PubMed:15840476}.
/FTId=VAR_068288.
VARIANT 117 117 P -> L (in LQT1; unknown pathological
significance; dbSNP:rs120074191).
{ECO:0000269|PubMed:19716085}.
/FTId=VAR_074932.
VARIANT 122 122 C -> Y (in LQT1; dbSNP:rs199472681).
{ECO:0000269|PubMed:15840476}.
/FTId=VAR_068289.
VARIANT 127 127 F -> L (in LQT1; unknown pathological
significance; dbSNP:rs199472682).
{ECO:0000269|PubMed:19716085}.
/FTId=VAR_074933.
VARIANT 133 133 V -> I (in LQT1; dbSNP:rs199473449).
{ECO:0000269|PubMed:15840476,
ECO:0000269|PubMed:19716085}.
/FTId=VAR_068290.
VARIANT 134 134 L -> P (in LQT1; unknown pathological
significance; dbSNP:rs199472685).
{ECO:0000269|PubMed:19716085}.
/FTId=VAR_074934.
VARIANT 136 136 C -> F (in LQT1; dbSNP:rs199472686).
{ECO:0000269|PubMed:15840476}.
/FTId=VAR_068291.
VARIANT 137 137 L -> F (in LQT1; unknown pathological
significance; dbSNP:rs199473450).
{ECO:0000269|PubMed:16414944}.
/FTId=VAR_074935.
VARIANT 140 140 S -> G (in ATFB3; gain of function;
dbSNP:rs120074192).
{ECO:0000269|PubMed:12522251}.
/FTId=VAR_015742.
VARIANT 144 144 T -> A (in LQT1; unknown pathological
significance; dbSNP:rs199473451).
{ECO:0000269|PubMed:19716085}.
/FTId=VAR_074936.
VARIANT 146 146 E -> K (in LQT1; unknown pathological
significance; dbSNP:rs199472688).
{ECO:0000269|PubMed:16414944}.
/FTId=VAR_074937.
VARIANT 153 153 T -> M (in LQT1; unknown pathological
significance; dbSNP:rs143709408).
{ECO:0000269|PubMed:19716085}.
/FTId=VAR_074938.
VARIANT 157 157 F -> C (in LQT1; dbSNP:rs199472690).
{ECO:0000269|PubMed:10220146}.
/FTId=VAR_008124.
VARIANT 160 160 E -> K (in LQT1; dbSNP:rs199473453).
{ECO:0000269|PubMed:15840476}.
/FTId=VAR_009919.
VARIANT 162 162 V -> M (in LQT1; unknown pathological
significance; dbSNP:rs199472692).
{ECO:0000269|PubMed:19716085}.
/FTId=VAR_074939.
VARIANT 167 168 FG -> W (in LQT1).
/FTId=VAR_001515.
VARIANT 168 168 G -> R (in LQT1; dbSNP:rs179489).
{ECO:0000269|PubMed:15840476,
ECO:0000269|PubMed:19716085,
ECO:0000269|PubMed:9693036}.
/FTId=VAR_001516.
VARIANT 172 172 V -> M (in LQT1; unknown pathological
significance; dbSNP:rs199472694).
{ECO:0000269|PubMed:19716085}.
/FTId=VAR_074940.
VARIANT 173 173 V -> D (in LQT1; unknown pathological
significance; dbSNP:rs199472695).
{ECO:0000269|PubMed:16414944}.
/FTId=VAR_074941.
VARIANT 174 174 R -> C (in LQT1; dbSNP:rs199472696).
{ECO:0000269|PubMed:15840476,
ECO:0000269|PubMed:19716085}.
/FTId=VAR_001517.
VARIANT 174 174 R -> H (in LQT1; dbSNP:rs199472697).
{ECO:0000269|PubMed:10367071,
ECO:0000269|PubMed:19716085}.
/FTId=VAR_008939.
VARIANT 174 174 R -> P (in LQT1; unknown pathological
significance; dbSNP:rs199472697).
{ECO:0000269|PubMed:16414944}.
/FTId=VAR_074942.
VARIANT 178 178 A -> P (in LQT1; loss of channel
activity; dbSNP:rs120074177).
{ECO:0000269|PubMed:9323054}.
/FTId=VAR_001518.
VARIANT 178 178 A -> T (in LQT1; dbSNP:rs120074177).
{ECO:0000269|PubMed:19716085,
ECO:0000269|PubMed:9024139}.
/FTId=VAR_009920.
VARIANT 179 179 G -> S (in LQT1; unknown pathological
significance; dbSNP:rs199473394).
{ECO:0000269|PubMed:19716085}.
/FTId=VAR_009921.
VARIANT 184 184 Y -> H (in LQT1; unknown pathological
significance; dbSNP:rs199473661).
{ECO:0000269|PubMed:19716085}.
/FTId=VAR_074943.
VARIANT 184 184 Y -> S (in LQT1; dbSNP:rs199473397).
{ECO:0000269|PubMed:10220144}.
/FTId=VAR_008125.
VARIANT 186 186 G -> R (in LQT1; unknown pathological
significance; dbSNP:rs199473398).
{ECO:0000269|PubMed:19716085}.
/FTId=VAR_074944.
VARIANT 189 189 G -> R (in LQT1; familial sudden death;
dbSNP:rs104894252).
{ECO:0000269|PubMed:10220144}.
/FTId=VAR_001519.
VARIANT 190 190 R -> L (in LQT1; unknown pathological
significance; dbSNP:rs120074178).
{ECO:0000269|PubMed:19716085}.
/FTId=VAR_074945.
VARIANT 190 190 R -> Q (in LQT1; loss of channel
activity; dbSNP:rs120074178).
{ECO:0000269|PubMed:10728423,
ECO:0000269|PubMed:15840476,
ECO:0000269|PubMed:19716085}.
/FTId=VAR_001520.
VARIANT 190 190 R -> W (in LQT1; unknown pathological
significance; dbSNP:rs199473662).
{ECO:0000269|PubMed:16414944}.
/FTId=VAR_074946.
VARIANT 191 191 L -> P (in LQT1; dbSNP:rs199473401).
{ECO:0000269|PubMed:12442276}.
/FTId=VAR_074687.
VARIANT 192 192 R -> P (in LQT1; unknown pathological
significance; dbSNP:rs199472698).
{ECO:0000269|PubMed:16414944}.
/FTId=VAR_074947.
VARIANT 194 194 A -> P (in LQT1; dbSNP:rs199472699).
/FTId=VAR_009922.
VARIANT 195 195 R -> W (in LQT1; unknown pathological
significance; dbSNP:rs150172393).
{ECO:0000269|PubMed:19716085}.
/FTId=VAR_074948.
VARIANT 198 198 I -> V (in LQT1; unknown pathological
significance; dbSNP:rs199472700).
{ECO:0000269|PubMed:19716085}.
/FTId=VAR_074949.
VARIANT 199 199 S -> A (in LQT1; unknown pathological
significance; dbSNP:rs199472701).
{ECO:0000269|PubMed:19716085}.
/FTId=VAR_074950.
VARIANT 202 202 D -> H (in LQT1; unknown pathological
significance; dbSNP:rs199472702).
{ECO:0000269|PubMed:16414944}.
/FTId=VAR_074951.
VARIANT 204 204 I -> F (in LQT1; dbSNP:rs199472703).
{ECO:0000269|PubMed:15840476}.
/FTId=VAR_068292.
VARIANT 204 204 I -> M (in LQT1; dbSNP:rs199473455).
{ECO:0000269|PubMed:16414944,
ECO:0000269|PubMed:19716085}.
/FTId=VAR_074952.
VARIANT 209 209 S -> F (in LQT1; unknown pathological
significance; dbSNP:rs199472704).
{ECO:0000269|PubMed:16414944}.
/FTId=VAR_074953.
VARIANT 215 215 V -> M (in LQT1; dbSNP:rs17215479).
{ECO:0000269|PubMed:16414944,
ECO:0000269|PubMed:19716085}.
/FTId=VAR_074954.
VARIANT 216 216 G -> R (in LQT1).
{ECO:0000269|PubMed:9272155}.
/FTId=VAR_001521.
VARIANT 224 224 T -> M (in LQT1; unknown pathological
significance; dbSNP:rs199472706).
{ECO:0000269|PubMed:19716085}.
/FTId=VAR_074955.
VARIANT 225 225 S -> L (in LQT1; dbSNP:rs199473456).
{ECO:0000269|PubMed:15840476,
ECO:0000269|PubMed:19716085,
ECO:0000269|PubMed:9927399}.
/FTId=VAR_009923.
VARIANT 231 231 R -> C (in LQT1; dbSNP:rs199473457).
{ECO:0000269|PubMed:16922724,
ECO:0000269|PubMed:19716085}.
/FTId=VAR_074956.
VARIANT 231 231 R -> H (in LQT1; dbSNP:rs199472709).
{ECO:0000269|PubMed:16414944,
ECO:0000269|PubMed:19716085}.
/FTId=VAR_074957.
VARIANT 235 235 I -> N (in LQT1; decreases delayed
rectifier potassium current Iks; prevents
the up-regulation of Iks through PKA
activation; dbSNP:rs199472710).
{ECO:0000269|PubMed:15840476,
ECO:0000269|PubMed:19716085,
ECO:0000269|PubMed:24269949}.
/FTId=VAR_068293.
VARIANT 239 239 L -> P (in LQT1; unknown pathological
significance; dbSNP:rs199473458).
{ECO:0000269|PubMed:16414944}.
/FTId=VAR_074958.
VARIANT 241 241 V -> G (in LQT1; unknown pathological
significance; dbSNP:rs199472711).
{ECO:0000269|PubMed:19716085}.
/FTId=VAR_074959.
VARIANT 242 242 D -> N (in LQT1; decreases outward
potassium current; decreases plasma
membrane localization;
dbSNP:rs199472712).
{ECO:0000269|PubMed:15840476,
ECO:0000269|PubMed:19716085,
ECO:0000269|PubMed:25705178,
ECO:0000269|PubMed:9799083}.
/FTId=VAR_008940.
VARIANT 243 243 R -> C (in LQT1; slower rate of
activation and voltage dependence of
activation-inactivation shifted to more
positive potentials (homomultimers);
channels non-functional
(heteromultimers); dbSNP:rs199472713).
{ECO:0000269|PubMed:10409658,
ECO:0000269|PubMed:15840476,
ECO:0000269|PubMed:19716085}.
/FTId=VAR_010933.
VARIANT 243 243 R -> H (in JLNS1; minor changes of wt
current (homomultimers); positive voltage
shift of the channel activation
(heteromultimers); dbSNP:rs120074196).
{ECO:0000269|PubMed:10090886,
ECO:0000269|PubMed:10728423}.
/FTId=VAR_008941.
VARIANT 243 243 R -> P (in LQT1; complete loss of outward
potassium current; enhances outward
potassium current when co-transfected
with wild type; decreases plasma membrane
localization; dbSNP:rs120074196).
{ECO:0000269|PubMed:16922724,
ECO:0000269|PubMed:25705178}.
/FTId=VAR_074688.
VARIANT 248 248 W -> F (in JLNS1; requires 2 nucleotide
substitutions; does not affect plasma
membrane localization; complete loss of
outward currents; enhances outward
currents when coexpressed with wild type
at equimolar ratio; dbSNP:rs397508123).
{ECO:0000269|PubMed:18441444,
ECO:0000269|PubMed:25705178}.
/FTId=VAR_074689.
VARIANT 248 248 W -> R (in LQT1; slower rate of
activation and voltage dependence of
activation-inactivation shifted to more
positive potentials (homomultimers);
channels non-functional
(heteromultimers); dbSNP:rs199473459).
{ECO:0000269|PubMed:10409658}.
/FTId=VAR_008942.
VARIANT 250 250 L -> H (in LQT1; complete loss of outward
potassium current; enhances outward
potassium current when co-transfected
with wild type; decreases plasma membrane
localization; dbSNP:rs199472715).
{ECO:0000269|PubMed:25705178,
ECO:0000269|PubMed:9799083}.
/FTId=VAR_008943.
VARIANT 250 250 L -> P (in LQT1; unknown pathological
significance; dbSNP:rs199472715).
{ECO:0000269|PubMed:19716085}.
/FTId=VAR_074960.
VARIANT 254 256 Missing (in LQT1).
{ECO:0000269|PubMed:15840476}.
/FTId=VAR_068294.
VARIANT 254 254 V -> L (in LQT1; unknown pathological
significance; dbSNP:rs120074179).
{ECO:0000269|PubMed:16414944}.
/FTId=VAR_074961.
VARIANT 254 254 V -> M (in LQT1; associated with M-417 in
a patient; dbSNP:rs120074179).
{ECO:0000269|PubMed:15840476,
ECO:0000269|PubMed:19716085,
ECO:0000269|Ref.31}.
/FTId=VAR_001522.
VARIANT 258 258 H -> N (in LQT1; unknown pathological
significance; dbSNP:rs199472717).
{ECO:0000269|PubMed:16414944}.
/FTId=VAR_074962.
VARIANT 258 258 H -> R (in LQT1; unknown pathological
significance; dbSNP:rs199472718).
{ECO:0000269|PubMed:16414944}.
/FTId=VAR_074963.
VARIANT 259 259 R -> C (in LQT1; dbSNP:rs199472719).
{ECO:0000269|PubMed:15840476,
ECO:0000269|PubMed:16922724,
ECO:0000269|PubMed:19716085}.
/FTId=VAR_068295.
VARIANT 259 259 R -> H (in LQT1; unknown pathological
significance; dbSNP:rs199472720).
{ECO:0000269|PubMed:16922724}.
/FTId=VAR_074964.
VARIANT 259 259 R -> L (in LQT1; dbSNP:rs199472720).
{ECO:0000269|PubMed:15840476,
ECO:0000269|PubMed:19716085}.
/FTId=VAR_068296.
VARIANT 261 261 E -> D (in JLNS1; dbSNP:rs199472721).
{ECO:0000269|PubMed:15840476}.
/FTId=VAR_008944.
VARIANT 261 261 E -> K (in LQT1; loss of channel activity
and no interaction with wt KVLQT1 or MINK
subunits; dbSNP:rs199472722).
{ECO:0000269|PubMed:10409658}.
/FTId=VAR_001523.
VARIANT 262 262 L -> V (in LQT1; dbSNP:rs199472723).
{ECO:0000269|PubMed:16414944,
ECO:0000269|PubMed:19716085}.
/FTId=VAR_074965.
VARIANT 266 266 L -> P (in LQT1; dbSNP:rs199473460).
{ECO:0000269|PubMed:15840476,
ECO:0000269|PubMed:19716085}.
/FTId=VAR_009924.
VARIANT 268 268 I -> S (in LQT1; unknown pathological
significance; dbSNP:rs199472725).
{ECO:0000269|PubMed:19716085}.
/FTId=VAR_074966.
VARIANT 269 269 G -> D (in LQT1; dbSNP:rs120074194).
{ECO:0000269|PubMed:15840476,
ECO:0000269|PubMed:19716085}.
/FTId=VAR_001524.
VARIANT 269 269 G -> S (in LQT1; decreases IKs amplitude;
accelerates the IKs deactivation; effect
on plasma membrane localization; reduces
up-regulation of Iks through PKA
activation; dbSNP:rs120074193).
{ECO:0000269|PubMed:15840476,
ECO:0000269|PubMed:19716085,
ECO:0000269|PubMed:24184248}.
/FTId=VAR_009925.
VARIANT 272 272 G -> D (in LQT1; dbSNP:rs199472726).
{ECO:0000269|PubMed:16414944,
ECO:0000269|PubMed:19716085}.
/FTId=VAR_074967.
VARIANT 273 273 L -> F (in LQT1; functional channel with
reduced macroscopic conductance
(homomultimers); alteration of normal
KVLQT1 function (mut/wt homomultimers);
dbSNP:rs120074180).
{ECO:0000269|PubMed:15840476,
ECO:0000269|PubMed:16922724,
ECO:0000269|PubMed:19716085,
ECO:0000269|PubMed:9323054}.
/FTId=VAR_001525.
VARIANT 273 273 L -> R (in LQT1; dbSNP:rs199472727).
{ECO:0000269|PubMed:15840476}.
/FTId=VAR_068297.
VARIANT 274 274 I -> V (in LQT1; unknown pathological
significance; dbSNP:rs199472728).
{ECO:0000269|PubMed:19716085}.
/FTId=VAR_074968.
VARIANT 275 275 F -> S (in LQT1; dbSNP:rs199472729).
{ECO:0000269|PubMed:12442276}.
/FTId=VAR_074690.
VARIANT 276 276 Missing (in LQT1).
{ECO:0000269|PubMed:15840476}.
/FTId=VAR_068298.
VARIANT 277 277 S -> L (in LQT1; loss of function
mutation acting in a dominant-negative
manner; dbSNP:rs199472730).
{ECO:0000269|PubMed:12442276,
ECO:0000269|PubMed:15840476,
ECO:0000269|PubMed:19716085,
ECO:0000269|PubMed:21241800}.
/FTId=VAR_065777.
VARIANT 277 277 S -> P (in LQT1; unknown pathological
significance; dbSNP:rs199473461).
{ECO:0000269|PubMed:19716085}.
/FTId=VAR_074969.
VARIANT 277 277 S -> W (in LQT1; unknown pathological
significance; dbSNP:rs199472730).
{ECO:0000269|PubMed:16414944}.
/FTId=VAR_074970.
VARIANT 278 278 Y -> H (in LQT1; dbSNP:rs199472731).
{ECO:0000269|PubMed:15840476}.
/FTId=VAR_068299.
VARIANT 280 280 V -> E (in LQT1; dbSNP:rs199473462).
{ECO:0000269|PubMed:16414944,
ECO:0000269|PubMed:19716085}.
/FTId=VAR_074971.
VARIANT 281 281 Y -> C (in LQT1; dbSNP:rs199472732).
{ECO:0000269|PubMed:19716085,
ECO:0000269|PubMed:9927399}.
/FTId=VAR_008945.
VARIANT 282 282 L -> P (in LQT1; unknown pathological
significance; dbSNP:rs199472733).
{ECO:0000269|PubMed:19716085}.
/FTId=VAR_074972.
VARIANT 283 283 A -> G (in LQT1; unknown pathological
significance; dbSNP:rs199473463).
{ECO:0000269|PubMed:19716085}.
/FTId=VAR_074973.
VARIANT 287 287 A -> E (in LQT1; unknown pathological
significance; dbSNP:rs199472735).
{ECO:0000269|PubMed:16414944}.
/FTId=VAR_074974.
VARIANT 290 290 E -> K (in LQT1; dbSNP:rs199473464).
{ECO:0000269|PubMed:15840476}.
/FTId=VAR_068300.
VARIANT 292 292 G -> D (in LQT1; dbSNP:rs199472736).
{ECO:0000269|PubMed:15840476,
ECO:0000269|PubMed:19716085}.
/FTId=VAR_068301.
VARIANT 293 293 R -> C (in LQT1; dbSNP:rs199472737).
{ECO:0000269|PubMed:15840476,
ECO:0000269|PubMed:19716085}.
/FTId=VAR_068302.
VARIANT 300 300 A -> T (in LQT1; dbSNP:rs120074187).
{ECO:0000269|PubMed:9641694}.
/FTId=VAR_001526.
VARIANT 302 302 A -> E (in LQT1; unknown pathological
significance; dbSNP:rs193922365).
{ECO:0000269|PubMed:19716085}.
/FTId=VAR_074975.
VARIANT 302 302 A -> T (in LQT1; unknown pathological
significance; dbSNP:rs199472739).
{ECO:0000269|PubMed:16414944}.
/FTId=VAR_074976.
VARIANT 302 302 A -> V (in LQT1; dbSNP:rs193922365).
{ECO:0000269|PubMed:15840476,
ECO:0000269|PubMed:19716085}.
/FTId=VAR_068303.
VARIANT 303 303 L -> P (in LQT1; unknown pathological
significance; dbSNP:rs199472740).
{ECO:0000269|PubMed:19716085}.
/FTId=VAR_074977.
VARIANT 304 304 W -> R (in LQT1; dbSNP:rs199473466).
{ECO:0000269|PubMed:15840476}.
/FTId=VAR_068304.
VARIANT 305 305 W -> R (in LQT1; unknown pathological
significance; dbSNP:rs199472741).
{ECO:0000269|PubMed:19716085}.
/FTId=VAR_074978.
VARIANT 305 305 W -> S (in JLNS1; dbSNP:rs120074186).
{ECO:0000269|PubMed:15840476,
ECO:0000269|PubMed:19716085,
ECO:0000269|PubMed:9781056}.
/FTId=VAR_001527.
VARIANT 306 306 G -> R (in LQT1; unknown pathological
significance; dbSNP:rs120074181).
{ECO:0000269|PubMed:19716085}.
/FTId=VAR_001528.
VARIANT 306 306 G -> V (in LQT1; complete loss of outward
potassium current; enhances outward
potassium current when co-transfected
with wild type; decreases plasma membrane
localization; dbSNP:rs199472742).
{ECO:0000269|PubMed:12442276,
ECO:0000269|PubMed:25705178}.
/FTId=VAR_074691.
VARIANT 307 307 V -> L (in SQT2; gain of function;
dbSNP:rs120074195).
{ECO:0000269|PubMed:15159330}.
/FTId=VAR_023841.
VARIANT 308 308 V -> D (in LQT1; unknown pathological
significance; dbSNP:rs199473467).
{ECO:0000269|PubMed:16414944}.
/FTId=VAR_074979.
VARIANT 309 309 T -> R (in LQT1; dbSNP:rs199472743).
/FTId=VAR_001529.
VARIANT 310 310 V -> I (in LQT1; dbSNP:rs199472745).
/FTId=VAR_009926.
VARIANT 311 311 T -> I (in LQT1 and JLNS1; impairs
outward potassium current; affects plasma
membrane localization;
dbSNP:rs199472746).
{ECO:0000269|PubMed:25705178,
ECO:0000269|PubMed:9482580}.
/FTId=VAR_009927.
VARIANT 312 312 T -> I (in LQT1; loss of channel
activity; dbSNP:rs120074182).
{ECO:0000269|PubMed:15840476,
ECO:0000269|PubMed:19716085,
ECO:0000269|PubMed:9323054}.
/FTId=VAR_001530.
VARIANT 313 313 I -> M (in LQT1; dbSNP:rs199472747).
{ECO:0000269|PubMed:9024139}.
/FTId=VAR_001531.
VARIANT 314 314 G -> C (in LQT1; unknown pathological
significance; dbSNP:rs120074184).
{ECO:0000269|PubMed:19716085}.
/FTId=VAR_074980.
VARIANT 314 314 G -> D (in LQT1; dbSNP:rs199472748).
{ECO:0000269|PubMed:15840476}.
/FTId=VAR_068305.
VARIANT 314 314 G -> R (in LQT1; dbSNP:rs120074184).
{ECO:0000269|PubMed:15840476}.
/FTId=VAR_068306.
VARIANT 314 314 G -> S (in LQT1; dbSNP:rs120074184).
{ECO:0000269|PubMed:10220144,
ECO:0000269|PubMed:15840476,
ECO:0000269|PubMed:16922724,
ECO:0000269|PubMed:19716085,
ECO:0000269|PubMed:8872472,
ECO:0000269|PubMed:9693036,
ECO:0000269|PubMed:9799083}.
/FTId=VAR_001532.
VARIANT 315 315 Y -> C (in LQT1; dbSNP:rs74462309).
{ECO:0000269|PubMed:15840476,
ECO:0000269|PubMed:19716085,
ECO:0000269|PubMed:24269949,
ECO:0000269|PubMed:9693036,
ECO:0000269|PubMed:9927399}.
/FTId=VAR_008946.
VARIANT 315 315 Y -> S (in LQT1; dbSNP:rs74462309).
{ECO:0000269|PubMed:10220144}.
/FTId=VAR_001533.
VARIANT 316 316 G -> E (in LQT1; dbSNP:rs199472749).
{ECO:0000269|PubMed:16414944,
ECO:0000269|PubMed:16922724}.
/FTId=VAR_074981.
VARIANT 316 316 G -> R (in LQT1; dbSNP:rs104894255).
{ECO:0000269|PubMed:15840476}.
/FTId=VAR_068307.
VARIANT 316 316 G -> V (in LQT1; unknown pathological
significance; dbSNP:rs199472749).
{ECO:0000269|PubMed:19716085}.
/FTId=VAR_074982.
VARIANT 317 317 D -> N (in LQT1; complete loss of outward
potassium current when expressed alone
and even in the presence of the wild type
at variable ratios; decreases plasma
membrane localization;
dbSNP:rs199472751).
{ECO:0000269|PubMed:25705178,
ECO:0000269|PubMed:9302275,
ECO:0000269|PubMed:9482580}.
/FTId=VAR_001534.
VARIANT 318 318 K -> N (in LQT1; dbSNP:rs199472752).
{ECO:0000269|PubMed:9693036}.
/FTId=VAR_008947.
VARIANT 320 320 P -> A (in LQT1; loss of function
mutation acting in a dominant-negative
manner; dbSNP:rs199472753).
{ECO:0000269|PubMed:19540844}.
/FTId=VAR_001535.
VARIANT 320 320 P -> H (in LQT1; loss of function
mutation acting in a dominant-negative
manner; dbSNP:rs199473470).
{ECO:0000269|PubMed:19540844}.
/FTId=VAR_065778.
VARIANT 320 320 P -> S (in LQT1; unknown pathological
significance; dbSNP:rs199472753).
{ECO:0000269|PubMed:19716085}.
/FTId=VAR_074983.
VARIANT 322 322 T -> A (in LQT1; dbSNP:rs199472754).
{ECO:0000269|PubMed:15840476,
ECO:0000269|PubMed:19716085,
ECO:0000269|PubMed:24269949}.
/FTId=VAR_068308.
VARIANT 322 322 T -> M (in JLNS1 and LQT1; impairs
outward potassium current; affects plasma
membrane localization;
dbSNP:rs199472755).
{ECO:0000269|PubMed:16414944,
ECO:0000269|PubMed:18400097,
ECO:0000269|PubMed:19716085,
ECO:0000269|PubMed:25705178}.
/FTId=VAR_074692.
VARIANT 325 325 G -> R (in LQT1; dbSNP:rs199472756).
{ECO:0000269|PubMed:19716085,
ECO:0000269|PubMed:9024139}.
/FTId=VAR_001536.
VARIANT 339 339 F -> Y (in LQT1; unknown pathological
significance; dbSNP:rs199472759).
{ECO:0000269|PubMed:19716085}.
/FTId=VAR_074984.
VARIANT 339 339 Missing (in LQT1).
{ECO:0000269|PubMed:15840476,
ECO:0000269|PubMed:9702906}.
/FTId=VAR_001537.
VARIANT 341 341 A -> E (in LQT1; dbSNP:rs12720459).
{ECO:0000269|PubMed:19716085}.
/FTId=VAR_001538.
VARIANT 341 341 A -> G (in LQT1; unknown pathological
significance; dbSNP:rs12720459).
{ECO:0000269|PubMed:19716085}.
/FTId=VAR_074985.
VARIANT 341 341 A -> V (in LQT1; dbSNP:rs12720459).
{ECO:0000269|PubMed:15840476,
ECO:0000269|PubMed:16922724,
ECO:0000269|PubMed:19716085,
ECO:0000269|PubMed:8818942,
ECO:0000269|PubMed:8872472,
ECO:0000269|PubMed:9570196}.
/FTId=VAR_001539.
VARIANT 342 342 L -> F (in LQT1; dbSNP:rs199472760).
{ECO:0000269|PubMed:19716085}.
/FTId=VAR_001540.
VARIANT 343 343 P -> L (in LQT1; dbSNP:rs199472761).
{ECO:0000269|PubMed:16414944,
ECO:0000269|PubMed:19716085}.
/FTId=VAR_074986.
VARIANT 343 343 P -> R (in LQT1; unknown pathological
significance; dbSNP:rs199472761).
{ECO:0000269|PubMed:16414944}.
/FTId=VAR_074987.
VARIANT 343 343 P -> S (in LQT1; dbSNP:rs199472762).
{ECO:0000269|PubMed:15840476}.
/FTId=VAR_068309.
VARIANT 344 344 A -> E (in LQT1; dbSNP:rs199472763).
{ECO:0000269|PubMed:15840476}.
/FTId=VAR_068310.
VARIANT 344 344 A -> V (in LQT1; dbSNP:rs199472763).
{ECO:0000269|PubMed:15840476,
ECO:0000269|PubMed:16922724}.
/FTId=VAR_001541.
VARIANT 345 345 G -> E (in LQT1; dbSNP:rs120074183).
{ECO:0000269|PubMed:15840476}.
/FTId=VAR_001542.
VARIANT 345 345 G -> R (in LQT1; familial sudden death;
dbSNP:rs199473471).
{ECO:0000269|PubMed:10220144}.
/FTId=VAR_008126.
VARIANT 349 349 S -> P (in LQT1; unknown pathological
significance; dbSNP:rs199472764).
{ECO:0000269|PubMed:16414944}.
/FTId=VAR_074988.
VARIANT 349 349 S -> W (in LQT1; dbSNP:rs199472765).
{ECO:0000269|PubMed:15840476}.
/FTId=VAR_009928.
VARIANT 350 350 G -> R (in LQT1; dbSNP:rs199472824).
{ECO:0000269|PubMed:16414944,
ECO:0000269|PubMed:19716085}.
/FTId=VAR_074989.
VARIANT 351 351 F -> S (in LQT1; dbSNP:rs199473402).
{ECO:0000269|PubMed:16414944,
ECO:0000269|PubMed:19716085}.
/FTId=VAR_074990.
VARIANT 353 353 L -> P (in LQT1; dbSNP:rs199473403).
{ECO:0000269|PubMed:15840476,
ECO:0000269|PubMed:9693036}.
/FTId=VAR_009180.
VARIANT 354 354 K -> R (in LQT1; unknown pathological
significance; dbSNP:rs199473404).
{ECO:0000269|PubMed:19716085}.
/FTId=VAR_074991.
VARIANT 360 360 R -> M (in LQT1; unknown pathological
significance; dbSNP:rs199473407).
{ECO:0000269|PubMed:19716085}.
/FTId=VAR_074992.
VARIANT 360 360 R -> T (in LQT1; unknown pathological
significance; dbSNP:rs199473407).
{ECO:0000269|PubMed:16414944}.
/FTId=VAR_074993.
VARIANT 362 362 K -> R (in LQT1; dbSNP:rs12720458).
{ECO:0000269|PubMed:15840476,
ECO:0000269|PubMed:19716085}.
/FTId=VAR_048025.
VARIANT 365 365 N -> H (in LQT1; unknown pathological
significance; dbSNP:rs199473409).
{ECO:0000269|PubMed:19716085}.
/FTId=VAR_074994.
VARIANT 366 366 R -> P (in LQT1; dbSNP:rs199473410).
{ECO:0000269|PubMed:9024139}.
/FTId=VAR_001543.
VARIANT 366 366 R -> Q (in LQT1; dbSNP:rs199473410).
{ECO:0000269|PubMed:19716085}.
/FTId=VAR_009929.
VARIANT 366 366 R -> W (in LQT1; dbSNP:rs199473411).
{ECO:0000269|PubMed:15840476,
ECO:0000269|PubMed:19716085,
ECO:0000269|PubMed:9693036}.
/FTId=VAR_008948.
VARIANT 371 371 A -> T (in LQT1; dbSNP:rs199473412).
/FTId=VAR_001544.
VARIANT 372 372 A -> D (in LQT1; unknown pathological
significance; dbSNP:rs199473472).
{ECO:0000269|PubMed:16414944}.
/FTId=VAR_074995.
VARIANT 373 373 S -> P (in LQT1; dbSNP:rs199472766).
{ECO:0000269|PubMed:10220144}.
/FTId=VAR_008127.
VARIANT 374 374 L -> H (in LQT1; dbSNP:rs199472767).
{ECO:0000269|PubMed:15840476,
ECO:0000269|PubMed:19716085}.
/FTId=VAR_068311.
VARIANT 379 379 W -> G (in LQT1; unknown pathological
significance; dbSNP:rs199472768).
{ECO:0000269|PubMed:19716085}.
/FTId=VAR_074996.
VARIANT 380 380 R -> S (in LQT1; dbSNP:rs199472771).
{ECO:0000269|PubMed:15840476}.
/FTId=VAR_068312.
VARIANT 385 385 E -> K (in LQT1; unknown pathological
significance; dbSNP:rs199473473).
{ECO:0000269|PubMed:19716085}.
/FTId=VAR_074997.
VARIANT 389 389 S -> P (in LQT1; unknown pathological
significance; dbSNP:rs199472772).
{ECO:0000269|PubMed:19716085}.
/FTId=VAR_074998.
VARIANT 389 389 S -> Y (in LQT1; dbSNP:rs199472773).
{ECO:0000269|PubMed:15840476}.
/FTId=VAR_068313.
VARIANT 391 391 T -> I (in LQT1; dbSNP:rs199473474).
/FTId=VAR_009930.
VARIANT 391 391 T -> TT (in LQT1; unknown pathological
significance).
{ECO:0000269|PubMed:19716085}.
/FTId=VAR_074999.
VARIANT 392 392 W -> R (in LQT1; dbSNP:rs199472774).
{ECO:0000269|PubMed:10220144}.
/FTId=VAR_008128.
VARIANT 393 393 K -> M (in LQT1; unknown pathological
significance; dbSNP:rs199472775).
{ECO:0000269|PubMed:16414944}.
/FTId=VAR_075000.
VARIANT 393 393 K -> N (in dbSNP:rs12720457).
/FTId=VAR_048026.
VARIANT 397 397 R -> W (in LQT1; unknown pathological
significance; dbSNP:rs199472776).
{ECO:0000269|PubMed:19716085}.
/FTId=VAR_075001.
VARIANT 398 398 K -> R (in LQT1; unknown pathological
significance; dbSNP:rs199472777).
{ECO:0000269|PubMed:19716085}.
/FTId=VAR_075002.
VARIANT 417 417 V -> M (in LQT1; associated with M-254 in
a patient; dbSNP:rs267607197).
{ECO:0000269|Ref.31}.
/FTId=VAR_010934.
VARIANT 446 446 D -> E (in LQT1; unknown pathological
significance; dbSNP:rs199472780).
{ECO:0000269|PubMed:19716085}.
/FTId=VAR_075003.
VARIANT 448 448 P -> L (in LQT1; unknown pathological
significance; dbSNP:rs12720449).
{ECO:0000269|PubMed:19716085}.
/FTId=VAR_075004.
VARIANT 448 448 P -> R (in LQT1; dbSNP:rs12720449).
/FTId=VAR_009931.
VARIANT 451 451 R -> W (in LQT1; unknown pathological
significance; dbSNP:rs199472782).
{ECO:0000269|PubMed:19716085}.
/FTId=VAR_075005.
VARIANT 452 452 R -> W (in LQT1; dbSNP:rs140452381).
{ECO:0000269|PubMed:15840476}.
/FTId=VAR_068314.
VARIANT 460 460 G -> S (in LQT1; unknown pathological
significance; dbSNP:rs199472783).
{ECO:0000269|PubMed:19716085}.
/FTId=VAR_075006.
VARIANT 477 477 P -> L (in LQT1; unknown pathological
significance; dbSNP:rs199472784).
{ECO:0000269|PubMed:19716085}.
/FTId=VAR_075007.
VARIANT 511 511 R -> W (in LQT1; unknown pathological
significance; dbSNP:rs199472785).
{ECO:0000269|PubMed:19716085}.
/FTId=VAR_075008.
VARIANT 518 518 R -> G (in LQT1; unknown pathological
significance; dbSNP:rs17215500).
{ECO:0000269|PubMed:16414944}.
/FTId=VAR_075009.
VARIANT 518 518 R -> P (in LQT1; unknown pathological
significance; dbSNP:rs145974930).
{ECO:0000269|PubMed:16414944}.
/FTId=VAR_075010.
VARIANT 518 518 R -> Q (in LQT1; unknown pathological
significance; dbSNP:rs145974930).
{ECO:0000269|PubMed:19716085}.
/FTId=VAR_075011.
VARIANT 520 520 M -> R (in LQT1; unknown pathological
significance; dbSNP:rs199473479).
{ECO:0000269|PubMed:19716085}.
/FTId=VAR_075012.
VARIANT 522 522 Y -> S (in LQT1; unknown pathological
significance; dbSNP:rs199472789).
{ECO:0000269|PubMed:19716085}.
/FTId=VAR_075013.
VARIANT 524 524 V -> G (in LQT1; dbSNP:rs199472790).
{ECO:0000269|PubMed:15840476,
ECO:0000269|PubMed:19716085}.
/FTId=VAR_068315.
VARIANT 525 525 A -> T (in LQT1; dbSNP:rs120074188).
{ECO:0000269|PubMed:10482963,
ECO:0000269|PubMed:19716085}.
/FTId=VAR_009181.
VARIANT 525 525 A -> V (in LQT1; unknown pathological
significance; dbSNP:rs199472791).
{ECO:0000269|PubMed:19716085}.
/FTId=VAR_075014.
VARIANT 526 526 K -> E (in LQT1; dbSNP:rs199472792).
{ECO:0000269|PubMed:15840476}.
/FTId=VAR_068316.
VARIANT 533 533 R -> W (in LQT1; minor changes of wt
current (homomultimers); positive voltage
shift of the channel activation
(heteromultimers); dbSNP:rs199472793).
{ECO:0000269|PubMed:10728423,
ECO:0000269|PubMed:19716085}.
/FTId=VAR_008949.
VARIANT 539 539 R -> Q (in LQT1; unknown pathological
significance; dbSNP:rs199472794).
{ECO:0000269|PubMed:19716085}.
/FTId=VAR_075015.
VARIANT 539 539 R -> W (in LQT1; minor changes of wt
current (homomultimers); positive voltage
shift of the channel activation
(heteromultimers); dbSNP:rs199472795).
{ECO:0000269|PubMed:10728423,
ECO:0000269|PubMed:15840476,
ECO:0000269|PubMed:19716085}.
/FTId=VAR_008950.
VARIANT 541 541 V -> I (in LQT1; unknown pathological
significance; dbSNP:rs199472796).
{ECO:0000269|PubMed:19716085}.
/FTId=VAR_075016.
VARIANT 543 543 E -> K (in LQT1; unknown pathological
significance; dbSNP:rs199472797).
{ECO:0000269|PubMed:19716085}.
/FTId=VAR_075017.
VARIANT 546 546 S -> L (in LQT1; decreases interaction
with KCNE1 C-terminus; does not affect
plasma membrane localization; reduces IKS
current density; impairs binding with
Phosphatidylinositol 4,5-bisphosphate;
dbSNP:rs199473480).
{ECO:0000269|PubMed:15840476,
ECO:0000269|PubMed:19716085,
ECO:0000269|PubMed:25037568}.
/FTId=VAR_068317.
VARIANT 547 547 Q -> R (in LQT1; unknown pathological
significance; dbSNP:rs199472798).
{ECO:0000269|PubMed:19716085}.
/FTId=VAR_075018.
VARIANT 548 548 G -> D (in LQT1; unknown pathological
significance; dbSNP:rs199472799).
{ECO:0000269|PubMed:16414944}.
/FTId=VAR_075019.
VARIANT 554 554 V -> A (in LQT1; unknown pathological
significance; dbSNP:rs199473481).
{ECO:0000269|PubMed:16414944}.
/FTId=VAR_075020.
VARIANT 555 555 R -> C (in LQT1; associated with a fruste
phenotype; decreases interaction with
KCNE1 C-terminus; does not affect plasma
membrane localization; reduces IKS
current density; shifts activation of the
voltage dependence; deactivates more
rapidly; impairs binding with
phosphatidylinositol 4,5-bisphosphate;
dbSNP:rs120074185).
{ECO:0000269|PubMed:15840476,
ECO:0000269|PubMed:19716085,
ECO:0000269|PubMed:25037568,
ECO:0000269|PubMed:9312006}.
/FTId=VAR_001545.
VARIANT 555 555 R -> H (in LQT1; decreases interaction
with KCNE1 C-terminus; does not affect
plasma membrane localization; reduces IKS
current density; impairs binding with
Phosphatidylinositol 4,5-bisphosphate;
dbSNP:rs199472800).
{ECO:0000269|PubMed:15840476,
ECO:0000269|PubMed:19716085,
ECO:0000269|PubMed:25037568}.
/FTId=VAR_068318.
VARIANT 555 555 R -> S (in LQT1; unknown pathological
significance; dbSNP:rs120074185).
{ECO:0000269|PubMed:19716085}.
/FTId=VAR_075021.
VARIANT 557 557 K -> E (in LQT1; no effect on cell
membrane localization; slows activation
kinetics; accelerates deactivation
kinetics; rightshifts the voltage-
dependent activation; does not affect
cAMP-dependent up-regulation; decreases
interaction with KCNE1 C-terminus; does
not affect plasma membrane localization;
does not affect phosphorylation at S-27
during cAMP-dependent stimulation;
reduces IKS current density; impairs
binding with Phosphatidylinositol 4,5-
bisphosphate; dbSNP:rs199472801).
{ECO:0000269|PubMed:19716085,
ECO:0000269|PubMed:25037568,
ECO:0000269|PubMed:25139741}.
/FTId=VAR_074693.
VARIANT 566 566 S -> F (in LQT1; dbSNP:rs199472804).
{ECO:0000269|PubMed:19716085}.
/FTId=VAR_009932.
VARIANT 566 566 S -> P (in LQT1; unknown pathological
significance; dbSNP:rs199472803).
{ECO:0000269|PubMed:19716085}.
/FTId=VAR_075022.
VARIANT 566 566 S -> Y (in LQT1; dbSNP:rs199472804).
{ECO:0000269|PubMed:15840476,
ECO:0000269|PubMed:19716085}.
/FTId=VAR_068319.
VARIANT 567 567 I -> S (in LQT1; dbSNP:rs199472805).
{ECO:0000269|PubMed:15840476}.
/FTId=VAR_068320.
VARIANT 567 567 I -> T (in LQT1; dbSNP:rs199472805).
{ECO:0000269|PubMed:16414944,
ECO:0000269|PubMed:19716085}.
/FTId=VAR_075023.
VARIANT 568 568 G -> R (in LQT1; dbSNP:rs199472807).
{ECO:0000269|PubMed:15840476,
ECO:0000269|PubMed:19716085}.
/FTId=VAR_068321.
VARIANT 569 569 K -> E (in LQT1; unknown pathological
significance; dbSNP:rs199472808).
{ECO:0000269|PubMed:19716085}.
/FTId=VAR_075024.
VARIANT 571 571 S -> L (in LQT1; unknown pathological
significance; dbSNP:rs199472809).
{ECO:0000269|PubMed:19716085}.
/FTId=VAR_075025.
VARIANT 573 573 F -> L (in LQT1; unknown pathological
significance; dbSNP:rs199472810).
{ECO:0000269|PubMed:16414944}.
/FTId=VAR_075026.
VARIANT 583 583 R -> C (in LQT1; dbSNP:rs17221854).
/FTId=VAR_009933.
VARIANT 583 583 R -> H (in LQT1; unknown pathological
significance; dbSNP:rs199473482).
{ECO:0000269|PubMed:16414944}.
/FTId=VAR_075027.
VARIANT 586 586 N -> D (in LQT1; decreases outward
potassium current; decreases plasma
membrane localization;
dbSNP:rs199472812).
{ECO:0000269|PubMed:16414944,
ECO:0000269|PubMed:25705178}.
/FTId=VAR_074694.
VARIANT 587 587 T -> M (in LQT1; dbSNP:rs120074189).
{ECO:0000269|PubMed:10024302,
ECO:0000269|PubMed:15840476,
ECO:0000269|PubMed:19716085,
ECO:0000269|PubMed:9799083}.
/FTId=VAR_008951.
VARIANT 589 589 G -> D (in LQT1 and JLNS1; affects plasma
membrane localization; strongly reduces
potassium current; impairs binding to
AKAP9 and the targeting protein kinase A
(PKA) catalytic subunit and protein
phosphatase 1 (PP1); dbSNP:rs120074190).
{ECO:0000269|PubMed:11799244,
ECO:0000269|PubMed:18165683,
ECO:0000269|PubMed:25037568,
ECO:0000269|PubMed:25705178}.
/FTId=VAR_008952.
VARIANT 590 590 A -> T (in LQT1; reduces IKs density and
causes a right-shift of the
current?voltage relation of channel
activation; reduces cell surface
expression; no effect on interaction with
AKAP9; does not affect the cAMP-dependent
IKs up-regulation; dbSNP:rs199472813).
{ECO:0000269|PubMed:15840476,
ECO:0000269|PubMed:24713462}.
/FTId=VAR_068322.
VARIANT 591 591 R -> C (in LQT1; unknown pathological
significance; dbSNP:rs199473483).
{ECO:0000269|PubMed:19716085}.
/FTId=VAR_075028.
VARIANT 591 591 R -> H (in LQT1; dbSNP:rs199472814).
{ECO:0000269|PubMed:10024302,
ECO:0000269|PubMed:15840476,
ECO:0000269|PubMed:19716085}.
/FTId=VAR_008953.
VARIANT 594 594 R -> P (in LQT1; unknown pathological
significance; dbSNP:rs199472815).
{ECO:0000269|PubMed:19716085}.
/FTId=VAR_075029.
VARIANT 594 594 R -> Q (in LQT1; dbSNP:rs199472815).
{ECO:0000269|PubMed:15840476,
ECO:0000269|PubMed:19716085}.
/FTId=VAR_009934.
VARIANT 596 596 E -> K (in LQT1; unknown pathological
significance; dbSNP:rs199472816).
{ECO:0000269|PubMed:19716085}.
/FTId=VAR_075030.
VARIANT 596 596 Missing (in LQT1; unknown pathological
significance).
{ECO:0000269|PubMed:19716085}.
/FTId=VAR_075031.
VARIANT 600 600 T -> M (in LQT1; unknown pathological
significance; dbSNP:rs34516117).
{ECO:0000269|PubMed:19716085}.
/FTId=VAR_075032.
VARIANT 611 611 D -> N (in LQT1; unknown pathological
significance; dbSNP:rs147445322).
{ECO:0000269|PubMed:19716085}.
/FTId=VAR_075033.
VARIANT 614 614 Missing (in LQT1; unknown pathological
significance).
{ECO:0000269|PubMed:19716085}.
/FTId=VAR_075034.
VARIANT 619 619 L -> M (in LQT1; decreases outward
potassium current; decreases plasma
membrane localization;
dbSNP:rs199472819).
{ECO:0000269|PubMed:15840476,
ECO:0000269|PubMed:25705178}.
/FTId=VAR_068323.
VARIANT 626 626 G -> S (in LQT1; dbSNP:rs199472821).
{ECO:0000269|PubMed:15840476,
ECO:0000269|PubMed:16922724,
ECO:0000269|PubMed:19716085}.
/FTId=VAR_068324.
VARIANT 635 635 G -> R (in LQT1; unknown pathological
significance; dbSNP:rs199473484).
{ECO:0000269|PubMed:19716085}.
/FTId=VAR_075035.
VARIANT 643 643 G -> S (in dbSNP:rs1800172).
{ECO:0000269|PubMed:9799083}.
/FTId=VAR_008954.
MUTAGEN 27 27 S->A: No phosphorylation by PKA.
Decreases delayed rectifier potassium
channel activity.
{ECO:0000269|PubMed:11799244}.
MUTAGEN 324 324 V->L: Has a voltage-gated potassium
channel activity. Inhibition of voltage-
gated potassium channel activity by
KCNE4. {ECO:0000269|PubMed:19687231}.
MUTAGEN 326 326 K->R: Has a voltage-gated potassium
channel activity. Disrupts KCNE4-mediated
voltage-gated potassium channel activity
inhibition.
{ECO:0000269|PubMed:19687231}.
MUTAGEN 327 327 T->V: Has a voltage-gated potassium
channel activity. Disrupts KCNE4-mediated
voltage-gated potassium channel activity
inhibition.
{ECO:0000269|PubMed:19687231}.
MUTAGEN 328 328 I->L: Has a voltage-gated potassium
channel activity. Inhibition of voltage-
gated potassium channel activity by
KCNE4. {ECO:0000269|PubMed:19687231}.
MUTAGEN 338 338 S->C: Inhibits voltage-gated potassium
channel activity.
{ECO:0000269|PubMed:19687231}.
MUTAGEN 340 340 F->C: Inhibits voltage-gated potassium
channel activity.
{ECO:0000269|PubMed:19687231}.
MUTAGEN 589 589 G->M: No effect.
{ECO:0000269|PubMed:18165683}.
MUTAGEN 590 590 A->W: Reduced cell surface expression and
strongly reduced potassium current.
{ECO:0000269|PubMed:18165683}.
MUTAGEN 593 593 N->G: Reduced cell surface expression and
moderately reduced potassium current.
{ECO:0000269|PubMed:18165683}.
MUTAGEN 602 602 L->A: Does not interact with AKAP9 and
the targeting protein kinase A (PKA)
catalytic subunit and protein phosphatase
1 (PP1); when associated with I-609.
{ECO:0000269|PubMed:11799244}.
MUTAGEN 609 609 I->A: Does not interact with AKAP9 and
the kinase A (PKA) catalytic subunit and
protein phosphatase 1 (PP1); when
associated with L-602.
{ECO:0000269|PubMed:11799244}.
CONFLICT 64 65 PA -> HV (in Ref. 4; CAB44649).
{ECO:0000305}.
CONFLICT 370 370 Missing (in Ref. 2; AAC05705).
{ECO:0000305}.
CONFLICT 607 608 AL -> VI (in Ref. 5; AAM94040).
{ECO:0000305}.
CONFLICT 619 644 LHGGSTPGSGGPPREGGAHITQPCGS -> MQQGGPTCNSR
SQVVASNE (in Ref. 5; AAM94040).
{ECO:0000305}.
CONFLICT 648 649 VD -> IN (in Ref. 5; AAM94040).
{ECO:0000305}.
CONFLICT 658 658 T -> S (in Ref. 5; AAM94040).
{ECO:0000305}.
CONFLICT 669 670 RR -> QT (in Ref. 5; AAM94040).
{ECO:0000305}.
HELIX 359 384 {ECO:0000244|PDB:4V0C}.
STRAND 386 391 {ECO:0000244|PDB:4V0C}.
HELIX 392 394 {ECO:0000244|PDB:4V0C}.
HELIX 502 533 {ECO:0000244|PDB:4V0C}.
HELIX 588 609 {ECO:0000244|PDB:3HFE}.
SEQUENCE 676 AA; 74699 MW; ADFCA9E2B9763B21 CRC64;
MAAASSPPRA ERKRWGWGRL PGARRGSAGL AKKCPFSLEL AEGGPAGGAL YAPIAPGAPG
PAPPASPAAP AAPPVASDLG PRPPVSLDPR VSIYSTRRPV LARTHVQGRV YNFLERPTGW
KCFVYHFAVF LIVLVCLIFS VLSTIEQYAA LATGTLFWME IVLVVFFGTE YVVRLWSAGC
RSKYVGLWGR LRFARKPISI IDLIVVVASM VVLCVGSKGQ VFATSAIRGI RFLQILRMLH
VDRQGGTWRL LGSVVFIHRQ ELITTLYIGF LGLIFSSYFV YLAEKDAVNE SGRVEFGSYA
DALWWGVVTV TTIGYGDKVP QTWVGKTIAS CFSVFAISFF ALPAGILGSG FALKVQQKQR
QKHFNRQIPA AASLIQTAWR CYAAENPDSS TWKIYIRKAP RSHTLLSPSP KPKKSVVVKK
KKFKLDKDNG VTPGEKMLTV PHITCDPPEE RRLDHFSVDG YDSSVRKSPT LLEVSMPHFM
RTNSFAEDLD LEGETLLTPI THISQLREHH RATIKVIRRM QYFVAKKKFQ QARKPYDVRD
VIEQYSQGHL NLMVRIKELQ RRLDQSIGKP SLFISVSEKS KDRGSNTIGA RLNRVEDKVT
QLDQRLALIT DMLHQLLSLH GGSTPGSGGP PREGGAHITQ PCGSGGSVDP ELFLPSNTLP
TYEQLTVPRR GPDEGS


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