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Sodium channel protein type 8 subunit alpha (Sodium channel protein type VIII subunit alpha) (Voltage-gated sodium channel subunit alpha Nav1.6)

 SCN8A_HUMAN             Reviewed;        1980 AA.
Q9UQD0; B9VWG8; O95788; Q9NYX2; Q9UPB2;
15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
27-SEP-2017, entry version 160.
RecName: Full=Sodium channel protein type 8 subunit alpha;
AltName: Full=Sodium channel protein type VIII subunit alpha;
AltName: Full=Voltage-gated sodium channel subunit alpha Nav1.6;
Name=SCN8A; Synonyms=MED;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606 {ECO:0000312|EMBL:BAA78033.1};
[1]
NUCLEOTIDE SEQUENCE (ISOFORM 4).
TISSUE=Brain, and Fetal brain;
PubMed=9295353; DOI=10.1074/jbc.272.38.24008;
Plummer N.W., McBurney M.W., Meisler M.H.;
"Alternative splicing of the sodium channel SCN8A predicts a truncated
two-domain protein in fetal brain and non-neuronal cells.";
J. Biol. Chem. 272:24008-24015(1997).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1; 2 AND 3).
PubMed=9828131; DOI=10.1006/geno.1998.5550;
Plummer N.W., Galt J., Jones J.M., Burgess D.L., Sprunger L.K.,
Kohrman D.C., Meisler M.H.;
"Exon organization, coding sequence, physical mapping, and polymorphic
intragenic markers for the human neuronal sodium channel gene SCN8A.";
Genomics 54:287-296(1998).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), FUNCTION, SUBCELLULAR
LOCATION, AND TISSUE SPECIFICITY.
TISSUE=Monocytic leukemia;
PubMed=19136557; DOI=10.1074/jbc.M801892200;
Carrithers M.D., Chatterjee G., Carrithers L.M., Offoha R.,
Iheagwara U., Rahner C., Graham M., Waxman S.G.;
"Regulation of podosome formation in macrophages by a splice variant
of the sodium channel SCN8A.";
J. Biol. Chem. 284:8114-8126(2009).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Lin C., Numakura C., Kiyoshi H.;
"cDNA sequence of human sodium channel, SCN8A.";
Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Jeong S.-Y., Goto J., Kanazawa I.;
"Cloning of cDNA for human voltage-gated sodium channel alpha subunit,
SCN8A.";
Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[7]
INTERACTION WITH FGF13.
PubMed=15282281; DOI=10.1523/JNEUROSCI.1628-04.2004;
Wittmack E.K., Rush A.M., Craner M.J., Goldfarb M., Waxman S.G.,
Dib-Hajj S.D.;
"Fibroblast growth factor homologous factor 2B: association with
Nav1.6 and selective colocalization at nodes of Ranvier of dorsal root
axons.";
J. Neurosci. 24:6765-6775(2004).
[8]
INVOLVEMENT IN CIAT.
PubMed=16236810; DOI=10.1136/jmg.2005.035667;
Trudeau M.M., Dalton J.C., Day J.W., Ranum L.P., Meisler M.H.;
"Heterozygosity for a protein truncation mutation of sodium channel
SCN8A in a patient with cerebellar atrophy, ataxia, and mental
retardation.";
J. Med. Genet. 43:527-530(2006).
[9]
INTERACTION WITH THE CONOTOXIN GVIIJ.
PubMed=24497506; DOI=10.1073/pnas.1324189111;
Gajewiak J., Azam L., Imperial J., Walewska A., Green B.R.,
Bandyopadhyay P.K., Raghuraman S., Ueberheide B., Bern M., Zhou H.M.,
Minassian N.A., Hagan R.H., Flinspach M., Liu Y., Bulaj G.,
Wickenden A.D., Olivera B.M., Yoshikami D., Zhang M.M.;
"A disulfide tether stabilizes the block of sodium channels by the
conotoxin muO[section sign]-GVIIJ.";
Proc. Natl. Acad. Sci. U.S.A. 111:2758-2763(2014).
[10]
SUBUNIT, INTERACTION WITH THE SPIDER BETA/DELTA-THERAPHOTOXIN-PRE1A,
AND SITE SER-1574.
PubMed=28428547; DOI=10.1038/s41598-017-01129-0;
Wingerd J.S., Mozar C.A., Ussing C.A., Murali S.S., Chin Y.K.,
Cristofori-Armstrong B., Durek T., Gilchrist J., Vaughan C.W.,
Bosmans F., Adams D.J., Lewis R.J., Alewood P.F., Mobli M.,
Christie M.J., Rash L.D.;
"The tarantula toxin beta/delta-TRTX-Pre1a highlights the importance
of the S1-S2 voltage-sensor region for sodium channel subtype
selectivity.";
Sci. Rep. 7:974-988(2017).
[11]
VARIANT EIEE13 ASP-1768, AND CHARACTERIZATION OF VARIANT EIEE13
ASP-1768.
PubMed=22365152; DOI=10.1016/j.ajhg.2012.01.006;
Veeramah K.R., O'Brien J.E., Meisler M.H., Cheng X., Dib-Hajj S.D.,
Waxman S.G., Talwar D., Girirajan S., Eichler E.E., Restifo L.L.,
Erickson R.P., Hammer M.F.;
"de novo pathogenic SCN8A mutation identified by whole-genome
sequencing of a family quartet affected by infantile epileptic
encephalopathy and SUDEP.";
Am. J. Hum. Genet. 90:502-510(2012).
[12]
VARIANT EIEE13 VAL-1327.
PubMed=24352161; DOI=10.1177/0883073813511300;
Vaher U., Noukas M., Nikopensius T., Kals M., Annilo T., Nelis M.,
Ounap K., Reimand T., Talvik I., Ilves P., Piirsoo A., Seppet E.,
Metspalu A., Talvik T.;
"De novo SCN8A mutation identified by whole-exome sequencing in a boy
with neonatal epileptic encephalopathy, multiple congenital anomalies,
and movement disorders.";
J. Child Neurol. 0:0-0(2013).
[13]
VARIANTS EIEE13 CYS-662 AND VAL-1279.
PubMed=23708187; DOI=10.1038/ng.2646;
Carvill G.L., Heavin S.B., Yendle S.C., McMahon J.M., O'Roak B.J.,
Cook J., Khan A., Dorschner M.O., Weaver M., Calvert S., Malone S.,
Wallace G., Stanley T., Bye A.M., Bleasel A., Howell K.B., Kivity S.,
Mackay M.T., Rodriguez-Casero V., Webster R., Korczyn A., Afawi Z.,
Zelnick N., Lerman-Sagie T., Lev D., Moeller R.S., Gill D.,
Andrade D.M., Freeman J.L., Sadleir L.G., Shendure J., Berkovic S.F.,
Scheffer I.E., Mefford H.C.;
"Targeted resequencing in epileptic encephalopathies identifies de
novo mutations in CHD2 and SYNGAP1.";
Nat. Genet. 45:825-830(2013).
[14]
VARIANTS EIEE13 ASP-216; SER-846; LYS-1466; THR-1466; GLN-1617;
THR-1650 AND TRP-1872.
PubMed=24888894; DOI=10.1111/epi.12668;
Ohba C., Kato M., Takahashi S., Lerman-Sagie T., Lev D., Terashima H.,
Kubota M., Kawawaki H., Matsufuji M., Kojima Y., Tateno A.,
Goldberg-Stern H., Straussberg R., Marom D., Leshinsky-Silver E.,
Nakashima M., Nishiyama K., Tsurusaki Y., Miyake N., Tanaka F.,
Matsumoto N., Saitsu H.;
"Early onset epileptic encephalopathy caused by de novo SCN8A
mutations.";
Epilepsia 55:994-1000(2014).
[15]
VARIANT EIEE13 GLY-223, AND CHARACTERIZATION OF VARIANT EIEE13
GLY-223.
PubMed=25239001; DOI=10.1016/j.eplepsyres.2014.08.020;
de Kovel C.G., Meisler M.H., Brilstra E.H., van Berkestijn F.M.,
Slot R.V., van Lieshout S., Nijman I.J., O'Brien J.E., Hammer M.F.,
Estacion M., Waxman S.G., Dib-Hajj S.D., Koeleman B.P.;
"Characterization of a de novo SCN8A mutation in a patient with
epileptic encephalopathy.";
Epilepsy Res. 108:1511-1518(2014).
[16]
VARIANT EIEE13 ILE-767, AND CHARACTERIZATION OF VARIANT EIEE13
ILE-767.
PubMed=24874546; DOI=10.1016/j.nbd.2014.05.017;
Estacion M., O'Brien J.E., Conravey A., Hammer M.F., Waxman S.G.,
Dib-Hajj S.D., Meisler M.H.;
"A novel de novo mutation of SCN8A (Nav1.6) with enhanced channel
activation in a child with epileptic encephalopathy.";
Neurobiol. Dis. 69:117-123(2014).
[17]
VARIANTS EIEE13 PHE-407; GLN-850; THR-890; CYS-1596 AND GLN-1617.
PubMed=25785782; DOI=10.1111/epi.12925;
Kong W., Zhang Y., Gao Y., Liu X., Gao K., Xie H., Wang J., Wu Y.,
Zhang Y., Wu X., Jiang Y.;
"SCN8A mutations in Chinese children with early onset epilepsy and
intellectual disability.";
Epilepsia 56:431-438(2015).
[18]
VARIANT EIEE13 LEU-210.
PubMed=25818041; DOI=10.1111/epi.12954;
Mercimek-Mahmutoglu S., Patel J., Cordeiro D., Hewson S., Callen D.,
Donner E.J., Hahn C.D., Kannu P., Kobayashi J., Minassian B.A.,
Moharir M., Siriwardena K., Weiss S.K., Weksberg R., Snead O.C. III;
"Diagnostic yield of genetic testing in epileptic encephalopathy in
childhood.";
Epilepsia 56:707-716(2015).
[19]
VARIANTS EIEE13 ASN-58; LYS-984 AND SER-1451, AND CHARACTERIZATION OF
VARIANTS EIEE13 ASN-58; LYS-984 AND SER-1451.
PubMed=25725044; DOI=10.1136/jmedgenet-2014-102813;
Blanchard M.G., Willemsen M.H., Walker J.B., Dib-Hajj S.D.,
Waxman S.G., Jongmans M.C., Kleefstra T., van de Warrenburg B.P.,
Praamstra P., Nicolai J., Yntema H.G., Bindels R.J., Meisler M.H.,
Kamsteeg E.J.;
"De novo gain-of-function and loss-of-function mutations of SCN8A in
patients with intellectual disabilities and epilepsy.";
J. Med. Genet. 52:330-337(2015).
[20]
VARIANTS EIEE13 ARG-215; SER-260; LEU-410; VAL-479; THR-890; ASP-960;
VAL-1331; VAL-1479; LEU-1592; ARG-1605; GLN-1617; THR-1650; GLU-1801;
GLN-1872 AND TRP-1872.
PubMed=25568300; DOI=10.1212/WNL.0000000000001211;
EuroEPINOMICS RES Consortium CRP;
Larsen J., Carvill G.L., Gardella E., Kluger G., Schmiedel G.,
Barisic N., Depienne C., Brilstra E., Mang Y., Nielsen J.E.,
Kirkpatrick M., Goudie D., Goldman R., Jaehn J.A., Jepsen B., Gill D.,
Doecker M., Biskup S., McMahon J.M., Koeleman B., Harris M., Braun K.,
de Kovel C.G., Marini C., Specchio N., Djemie T., Weckhuysen S.,
Tommerup N., Troncoso M., Troncoso L., Bevot A., Wolff M.,
Hjalgrim H., Guerrini R., Scheffer I.E., Mefford H.C., Moeller R.S.;
"The phenotypic spectrum of SCN8A encephalopathy.";
Neurology 84:480-489(2015).
[21]
VARIANT EIEE13 SER-1877, AND VARIANT BFIS5 SER-1877.
PubMed=27210545; DOI=10.1016/j.ejpn.2016.04.015;
Anand G., Collett-White F., Orsini A., Thomas S., Jayapal S.,
Trump N., Zaiwalla Z., Jayawant S.;
"Autosomal dominant SCN8A mutation with an unusually mild phenotype.";
Eur. J. Paediatr. Neurol. 20:761-765(2016).
[22]
VARIANTS EIEE13 GLN-1617; GLN-1872; LEU-1872 AND TRP-1872,
CHARACTERIZATION OF VARIANTS EIEE13 GLN-1617; GLN-1872; LEU-1872 AND
TRP-1872, AND INTERACTION WITH FGF14; GBG3; GBB2 AND SCN1B.
PubMed=26900580; DOI=10.1002/acn3.276;
Wagnon J.L., Barker B.S., Hounshell J.A., Haaxma C.A., Shealy A.,
Moss T., Parikh S., Messer R.D., Patel M.K., Meisler M.H.;
"Pathogenic mechanism of recurrent mutations of SCN8A in epileptic
encephalopathy.";
Ann. Clin. Transl. Neurol. 3:114-123(2016).
[23]
VARIANT BFIS5 LYS-1483, AND INVOLVEMENT IN BFIS5.
PubMed=26677014; DOI=10.1002/ana.24580;
Gardella E., Becker F., Moeller R.S., Schubert J., Lemke J.R.,
Larsen L.H., Eiberg H., Nothnagel M., Thiele H., Altmueller J.,
Syrbe S., Merkenschlager A., Bast T., Steinhoff B., Nuernberg P.,
Mang Y., Bakke Moeller L., Gellert P., Heron S.E., Dibbens L.M.,
Weckhuysen S., Dahl H.A., Biskup S., Tommerup N., Hjalgrim H.,
Lerche H., Beniczky S., Weber Y.G.;
"Benign infantile seizures and paroxysmal dyskinesia caused by an
SCN8A mutation.";
Ann. Neurol. 79:428-436(2016).
[24]
VARIANTS EIEE13 THR-408; SER-1323; VAL-1327; SER-1754 AND PRO-1865.
PubMed=26993267; DOI=10.1136/jmedgenet-2015-103263;
Trump N., McTague A., Brittain H., Papandreou A., Meyer E., Ngoh A.,
Palmer R., Morrogh D., Boustred C., Hurst J.A., Jenkins L.,
Kurian M.A., Scott R.H.;
"Improving diagnosis and broadening the phenotypes in early-onset
seizure and severe developmental delay disorders through gene panel
analysis.";
J. Med. Genet. 53:310-317(2016).
[25]
VARIANTS EIEE13 SER-307; GLY-978; ARG-1475; THR-1650 AND TRP-1872, AND
VARIANT SER-1877.
PubMed=27864847; DOI=10.1002/humu.23149;
Clinical Study Group;
Parrini E., Marini C., Mei D., Galuppi A., Cellini E., Pucatti D.,
Chiti L., Rutigliano D., Bianchini C., Virdo S., De Vita D.,
Bigoni S., Barba C., Mari F., Montomoli M., Pisano T., Rosati A.,
Guerrini R.;
"Diagnostic targeted resequencing in 349 patients with drug-resistant
pediatric epilepsies identifies causative mutations in 30 different
genes.";
Hum. Mutat. 38:216-225(2017).
-!- FUNCTION: Mediates the voltage-dependent sodium ion permeability
of excitable membranes. Assuming opened or closed conformations in
response to the voltage difference across the membrane, the
protein forms a sodium-selective channel through which Na(+) ions
may pass in accordance with their electrochemical gradient. In
macrophages and melanoma cells, isoform 5 may participate in the
control of podosome and invadopodia formation.
{ECO:0000269|PubMed:19136557}.
-!- SUBUNIT: The voltage-sensitive sodium channel consists of an ion
conducting pore forming alpha-subunit regulated by one or more
beta-1 (SCN1B), beta-2 (SCN2B), beta-3 (SCN3B) and/or beta-4
(SCN4B). Beta-1 (SCN1B) and beta-3 (SCN3B) are non-covalently
associated with alpha, while beta-2 (SCN2B) and beta-4 (SCN4B) are
covalently linked by disulfide bonds. Interacts with NEDD4 and
NEDD4L (By similarity). Interacts with FGF13. Interacts with
FGF14, GBG3, GBB2 and SCN1B (PubMed:26900580). Interacts with the
conotoxin GVIIJ (PubMed:24497506). Interacts with the conotoxin
GVIIJ (PubMed:24497506). Interacts with the spider beta/delta-
theraphotoxin-Pre1a (PubMed:28428547).
{ECO:0000250|UniProtKB:Q9WTU3, ECO:0000269|PubMed:15282281,
ECO:0000269|PubMed:24497506, ECO:0000269|PubMed:26900580,
ECO:0000269|PubMed:28428547}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19136557};
Multi-pass membrane protein {ECO:0000269|PubMed:19136557}.
-!- SUBCELLULAR LOCATION: Isoform 5: Cytoplasmic vesicle. Note=Some
vesicles are localized adjacent to melanoma invadopodia and
macrophage podosomes. Does not localize to the plasma membrane.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1 {ECO:0000269|PubMed:9828131};
IsoId=Q9UQD0-1; Sequence=Displayed;
Name=2 {ECO:0000269|PubMed:9828131}; Synonyms=5A
{ECO:0000269|PubMed:9828131};
IsoId=Q9UQD0-2; Sequence=VSP_050589, VSP_050590;
Name=3 {ECO:0000269|PubMed:9828131};
IsoId=Q9UQD0-3; Sequence=VSP_050591;
Name=4 {ECO:0000269|PubMed:9295353}; Synonyms=18N
{ECO:0000269|PubMed:9295353};
IsoId=Q9UQD0-4; Sequence=VSP_050592, VSP_050593;
Name=5;
IsoId=Q9UQD0-5; Sequence=VSP_038651;
-!- TISSUE SPECIFICITY: Isoform 5 is expressed in non-neuronal
tissues, such as monocytes/macrophages.
{ECO:0000269|PubMed:19136557}.
-!- DOMAIN: The sequence contains 4 internal repeats, each with 5
hydrophobic segments (S1, S2, S3, S5, S6) and one positively
charged segment (S4). Segments S4 are probably the voltage-sensors
and are characterized by a series of positively charged amino
acids at every third position. {ECO:0000305}.
-!- PTM: May be ubiquitinated by NEDD4L; which would promote its
endocytosis. {ECO:0000250}.
-!- PTM: Phosphorylation at Ser-1497 by PKC in a highly conserved
cytoplasmic loop slows inactivation of the sodium channel and
reduces peak sodium currents. {ECO:0000250}.
-!- DISEASE: Cognitive impairment with or without cerebellar ataxia
(CIAT) [MIM:614306]: A disorder characterized by markedly delayed
cognitive and motor development, attention deficit disorder, and
cerebellar ataxia. Features include bilateral esophoria,
strabismatic amblyopia, unsustained gaze evoked nystagmus on
horizontal gaze, ataxic gait, dysmetria in the upper limbs and
dysarthria, with normal strength, tone, and reflexes.
{ECO:0000269|PubMed:16236810}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Epileptic encephalopathy, early infantile, 13 (EIEE13)
[MIM:614558]: A form of epilepsy characterized by frequent tonic
seizures or spasms beginning in infancy with a specific EEG
finding of suppression-burst patterns, characterized by high-
voltage bursts alternating with almost flat suppression phases.
Patients may progress to West syndrome, which is characterized by
tonic spasms with clustering, arrest of psychomotor development,
and hypsarrhythmia on EEG. EIEE13 is a severe form consisting of
early-onset seizures, features of autism, intellectual disability,
ataxia, and sudden unexplained death in epilepsy.
{ECO:0000269|PubMed:22365152, ECO:0000269|PubMed:23708187,
ECO:0000269|PubMed:24352161, ECO:0000269|PubMed:24874546,
ECO:0000269|PubMed:24888894, ECO:0000269|PubMed:25239001,
ECO:0000269|PubMed:25568300, ECO:0000269|PubMed:25725044,
ECO:0000269|PubMed:25785782, ECO:0000269|PubMed:25818041,
ECO:0000269|PubMed:26900580, ECO:0000269|PubMed:26993267,
ECO:0000269|PubMed:27210545, ECO:0000269|PubMed:27864847}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Seizures, benign familial infantile, 5 (BFIS5)
[MIM:617080]: A form of benign familial infantile epilepsy, a
neurologic disorder characterized by afebrile seizures occurring
in clusters during the first year of life, without neurologic
sequelae. BFIS5 inheritance is autosomal dominant.
{ECO:0000269|PubMed:26677014, ECO:0000269|PubMed:27210545}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the sodium channel (TC 1.A.1.10) family.
Nav1.6/SCN8A subfamily. {ECO:0000305}.
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EMBL; AF050736; AAD15789.1; -; Genomic_DNA.
EMBL; AF050711; AAD15789.1; JOINED; Genomic_DNA.
EMBL; AF050712; AAD15789.1; JOINED; Genomic_DNA.
EMBL; AF050713; AAD15789.1; JOINED; Genomic_DNA.
EMBL; AF050714; AAD15789.1; JOINED; Genomic_DNA.
EMBL; AF050715; AAD15789.1; JOINED; Genomic_DNA.
EMBL; AF050716; AAD15789.1; JOINED; Genomic_DNA.
EMBL; AF050717; AAD15789.1; JOINED; Genomic_DNA.
EMBL; AF050718; AAD15789.1; JOINED; Genomic_DNA.
EMBL; AF050719; AAD15789.1; JOINED; Genomic_DNA.
EMBL; AF050720; AAD15789.1; JOINED; Genomic_DNA.
EMBL; AF050721; AAD15789.1; JOINED; Genomic_DNA.
EMBL; AF050722; AAD15789.1; JOINED; Genomic_DNA.
EMBL; AF050723; AAD15789.1; JOINED; Genomic_DNA.
EMBL; AF050724; AAD15789.1; JOINED; Genomic_DNA.
EMBL; AF050725; AAD15789.1; JOINED; Genomic_DNA.
EMBL; AF050726; AAD15789.1; JOINED; Genomic_DNA.
EMBL; AF050727; AAD15789.1; JOINED; Genomic_DNA.
EMBL; AF050728; AAD15789.1; JOINED; Genomic_DNA.
EMBL; AF050729; AAD15789.1; JOINED; Genomic_DNA.
EMBL; AF050730; AAD15789.1; JOINED; Genomic_DNA.
EMBL; AF050731; AAD15789.1; JOINED; Genomic_DNA.
EMBL; AF050732; AAD15789.1; JOINED; Genomic_DNA.
EMBL; AF050733; AAD15789.1; JOINED; Genomic_DNA.
EMBL; AF050734; AAD15789.1; JOINED; Genomic_DNA.
EMBL; AF050735; AAD15789.1; JOINED; Genomic_DNA.
EMBL; AF049618; AAD20439.1; -; Genomic_DNA.
EMBL; FJ611941; ACM63162.1; -; mRNA.
EMBL; AB027567; BAA78033.1; -; mRNA.
EMBL; AF225988; AAF35390.1; -; mRNA.
EMBL; AC013421; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC025097; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC068987; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC140060; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS44891.1; -. [Q9UQD0-1]
CCDS; CCDS53794.1; -. [Q9UQD0-5]
CCDS; CCDS81692.1; -. [Q9UQD0-2]
RefSeq; NP_001171455.1; NM_001177984.2. [Q9UQD0-5]
RefSeq; NP_001317189.1; NM_001330260.1. [Q9UQD0-2]
RefSeq; NP_055006.1; NM_014191.3. [Q9UQD0-1]
RefSeq; XP_006719619.1; XM_006719556.3. [Q9UQD0-2]
RefSeq; XP_011536953.1; XM_011538651.2. [Q9UQD0-2]
RefSeq; XP_016875283.1; XM_017019794.1. [Q9UQD0-1]
UniGene; Hs.436550; -.
UniGene; Hs.710638; -.
ProteinModelPortal; Q9UQD0; -.
SMR; Q9UQD0; -.
BioGrid; 112238; 2.
IntAct; Q9UQD0; 1.
STRING; 9606.ENSP00000346534; -.
BindingDB; Q9UQD0; -.
ChEMBL; CHEMBL5202; -.
DrugBank; DB05232; Tetrodotoxin.
DrugBank; DB00313; Valproic Acid.
GuidetoPHARMACOLOGY; 583; -.
TCDB; 1.A.1.10.8; the voltage-gated ion channel (vic) superfamily.
iPTMnet; Q9UQD0; -.
PhosphoSitePlus; Q9UQD0; -.
BioMuta; SCN8A; -.
DMDM; 34098756; -.
PaxDb; Q9UQD0; -.
PeptideAtlas; Q9UQD0; -.
PRIDE; Q9UQD0; -.
Ensembl; ENST00000354534; ENSP00000346534; ENSG00000196876. [Q9UQD0-1]
Ensembl; ENST00000355133; ENSP00000347255; ENSG00000196876. [Q9UQD0-5]
Ensembl; ENST00000545061; ENSP00000440360; ENSG00000196876. [Q9UQD0-5]
Ensembl; ENST00000599343; ENSP00000476447; ENSG00000196876. [Q9UQD0-3]
Ensembl; ENST00000627620; ENSP00000487583; ENSG00000196876. [Q9UQD0-2]
GeneID; 6334; -.
KEGG; hsa:6334; -.
UCSC; uc001ryw.4; human. [Q9UQD0-1]
CTD; 6334; -.
DisGeNET; 6334; -.
EuPathDB; HostDB:ENSG00000196876.13; -.
GeneCards; SCN8A; -.
HGNC; HGNC:10596; SCN8A.
HPA; CAB022169; -.
MalaCards; SCN8A; -.
MIM; 600702; gene.
MIM; 614306; phenotype.
MIM; 614558; phenotype.
MIM; 617080; phenotype.
neXtProt; NX_Q9UQD0; -.
OpenTargets; ENSG00000196876; -.
Orphanet; 1934; Early infantile epileptic encephalopathy.
PharmGKB; PA35009; -.
eggNOG; KOG2301; Eukaryota.
eggNOG; ENOG410XNP6; LUCA.
GeneTree; ENSGT00830000128242; -.
HOGENOM; HOG000231755; -.
HOVERGEN; HBG053100; -.
InParanoid; Q9UQD0; -.
KO; K04840; -.
OMA; YMIDEDH; -.
OrthoDB; EOG091G00FK; -.
PhylomeDB; Q9UQD0; -.
TreeFam; TF323985; -.
Reactome; R-HSA-445095; Interaction between L1 and Ankyrins.
Reactome; R-HSA-5576892; Phase 0 - rapid depolarisation.
SIGNOR; Q9UQD0; -.
ChiTaRS; SCN8A; human.
GeneWiki; SCN8A; -.
GenomeRNAi; 6334; -.
PRO; PR:Q9UQD0; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000196876; -.
CleanEx; HS_SCN8A; -.
ExpressionAtlas; Q9UQD0; baseline and differential.
Genevisible; Q9UQD0; HS.
GO; GO:0043194; C:axon initial segment; ISS:BHF-UCL.
GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
GO; GO:0033268; C:node of Ranvier; ISS:BHF-UCL.
GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
GO; GO:0001518; C:voltage-gated sodium channel complex; IC:UniProtKB.
GO; GO:0030018; C:Z disc; ISS:BHF-UCL.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005248; F:voltage-gated sodium channel activity; IDA:UniProtKB.
GO; GO:0086010; P:membrane depolarization during action potential; IBA:GO_Central.
GO; GO:0042552; P:myelination; ISS:BHF-UCL.
GO; GO:0007399; P:nervous system development; TAS:ProtInc.
GO; GO:0019228; P:neuronal action potential; IBA:GO_Central.
GO; GO:0007422; P:peripheral nervous system development; ISS:BHF-UCL.
GO; GO:0006814; P:sodium ion transport; NAS:UniProtKB.
InterPro; IPR005821; Ion_trans_dom.
InterPro; IPR000048; IQ_motif_EF-hand-BS.
InterPro; IPR008054; Na_channel_a8su.
InterPro; IPR001696; Na_channel_asu.
InterPro; IPR010526; Na_trans_assoc.
InterPro; IPR024583; Na_trans_cytopl.
Pfam; PF00520; Ion_trans; 4.
Pfam; PF00612; IQ; 1.
Pfam; PF06512; Na_trans_assoc; 1.
Pfam; PF11933; Na_trans_cytopl; 1.
PRINTS; PR00170; NACHANNEL.
PRINTS; PR01667; NACHANNEL8.
SMART; SM00015; IQ; 1.
PROSITE; PS50096; IQ; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Cell membrane; Complete proteome;
Cytoplasmic vesicle; Disease mutation; Disulfide bond; Epilepsy;
Glycoprotein; Ion channel; Ion transport; Membrane;
Mental retardation; Nucleotide-binding; Phosphoprotein;
Reference proteome; Repeat; Sodium; Sodium channel; Sodium transport;
Transmembrane; Transmembrane helix; Transport; Ubl conjugation;
Voltage-gated channel.
CHAIN 1 1980 Sodium channel protein type 8 subunit
alpha.
/FTId=PRO_0000048500.
TOPO_DOM 1 132 Cytoplasmic. {ECO:0000305}.
TRANSMEM 133 151 Helical; Name=S1 of repeat I.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 152 158 Extracellular. {ECO:0000305}.
TRANSMEM 159 179 Helical; Name=S2 of repeat I.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 180 193 Cytoplasmic. {ECO:0000305}.
TRANSMEM 194 211 Helical; Name=S3 of repeat I.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 212 217 Extracellular. {ECO:0000305}.
TRANSMEM 218 234 Helical; Name=S4 of repeat I.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 235 253 Cytoplasmic. {ECO:0000305}.
TRANSMEM 254 273 Helical; Name=S5 of repeat I.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 274 355 Extracellular. {ECO:0000305}.
INTRAMEM 356 380 Pore-forming.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 381 387 Extracellular. {ECO:0000305}.
TRANSMEM 388 408 Helical; Name=S6 of repeat I.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 409 753 Cytoplasmic. {ECO:0000305}.
TRANSMEM 754 772 Helical; Name=S1 of repeat II.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 773 783 Extracellular. {ECO:0000305}.
TRANSMEM 784 803 Helical; Name=S2 of repeat II.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 804 817 Cytoplasmic. {ECO:0000305}.
TRANSMEM 818 837 Helical; Name=S3 of repeat II.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 838 839 Extracellular. {ECO:0000305}.
TRANSMEM 840 857 Helical; Name=S4 of repeat II.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 858 873 Cytoplasmic. {ECO:0000305}.
TRANSMEM 874 892 Helical; Name=S5 of repeat II.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 893 921 Extracellular. {ECO:0000305}.
INTRAMEM 922 942 Pore-forming.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 943 955 Extracellular. {ECO:0000305}.
TRANSMEM 956 976 Helical; Name=S6 of repeat II.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 977 1199 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1200 1217 Helical; Name=S1 of repeat III.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1218 1230 Extracellular. {ECO:0000305}.
TRANSMEM 1231 1249 Helical; Name=S2 of repeat III.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1250 1263 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1264 1282 Helical; Name=S3 of repeat III.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1283 1290 Extracellular. {ECO:0000305}.
TRANSMEM 1291 1309 Helical; Name=S4 of repeat III.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1310 1326 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1327 1346 Helical; Name=S5 of repeat III.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1347 1399 Extracellular. {ECO:0000305}.
INTRAMEM 1400 1421 Pore-forming.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1422 1438 Extracellular. {ECO:0000305}.
TRANSMEM 1439 1460 Helical; Name=S6 of repeat III.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1461 1523 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1524 1541 Helical; Name=S1 of repeat IV.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1542 1552 Extracellular. {ECO:0000305}.
TRANSMEM 1553 1571 Helical; Name=S2 of repeat IV.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1572 1583 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1584 1601 Helical; Name=S3 of repeat IV.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1602 1614 Extracellular. {ECO:0000305}.
TRANSMEM 1615 1631 Helical; Name=S4 of repeat IV.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1632 1650 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1651 1668 Helical; Name=S5 of repeat IV.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1669 1690 Extracellular. {ECO:0000305}.
INTRAMEM 1691 1713 Pore-forming.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1714 1742 Extracellular. {ECO:0000305}.
TRANSMEM 1743 1765 Helical; Name=S6 of repeat IV.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1766 1980 Cytoplasmic. {ECO:0000305}.
REPEAT 114 442 I. {ECO:0000305}.
REPEAT 735 1007 II. {ECO:0000305}.
REPEAT 1180 1495 III. {ECO:0000305}.
REPEAT 1504 1801 IV. {ECO:0000305}.
DOMAIN 1895 1924 IQ. {ECO:0000255|PROSITE-
ProRule:PRU00116, ECO:0000305}.
NP_BIND 893 900 ATP. {ECO:0000255}.
MOD_RES 518 518 Phosphoserine.
{ECO:0000250|UniProtKB:O88420}.
MOD_RES 520 520 Phosphoserine.
{ECO:0000250|UniProtKB:O88420}.
MOD_RES 1497 1497 Phosphoserine; by PKC.
{ECO:0000250|UniProtKB:Q15858}.
CARBOHYD 215 215 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 289 289 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 295 295 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 308 308 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 326 326 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1358 1358 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1372 1372 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1383 1383 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 281 333 {ECO:0000250|UniProtKB:D0E0C2}.
DISULFID 904 904 Interchain; with SCN2B or SCN4B.
{ECO:0000250|UniProtKB:P04775}.
DISULFID 904 904 Interchain; with the conotoxin GVIIJ
(when the channel is not linked to SCN2B
or SCN4B; the bond to SCN2B or SCN4B
protects the channel from the inhibition
by toxin).
{ECO:0000250|UniProtKB:P04775}.
DISULFID 944 953 {ECO:0000250|UniProtKB:D0E0C2}.
VAR_SEQ 207 207 I -> V (in isoform 2).
{ECO:0000303|PubMed:9828131}.
/FTId=VSP_050589.
VAR_SEQ 212 212 N -> D (in isoform 2).
{ECO:0000303|PubMed:9828131}.
/FTId=VSP_050590.
VAR_SEQ 666 666 E -> EVKIDKAATDDS (in isoform 3).
{ECO:0000303|PubMed:9828131}.
/FTId=VSP_050591.
VAR_SEQ 1275 1315 Missing (in isoform 5).
{ECO:0000303|PubMed:19136557}.
/FTId=VSP_038651.
VAR_SEQ 1275 1283 SLVSLIANA -> PLNLSGLI (in isoform 4).
{ECO:0000303|PubMed:9295353}.
/FTId=VSP_050592.
VAR_SEQ 1284 1980 Missing (in isoform 4).
{ECO:0000303|PubMed:9295353}.
/FTId=VSP_050593.
VARIANT 58 58 D -> N (in EIEE13; unknown pathological
significance; no effect on channel
activity). {ECO:0000269|PubMed:25725044}.
/FTId=VAR_076598.
VARIANT 210 210 F -> L (in EIEE13).
{ECO:0000269|PubMed:25818041}.
/FTId=VAR_078752.
VARIANT 215 215 N -> R (in EIEE13; unknown pathological
significance; requires 2 nucleotide
substitutions).
{ECO:0000269|PubMed:25568300}.
/FTId=VAR_076599.
VARIANT 216 216 V -> D (in EIEE13; dbSNP:rs879255696).
{ECO:0000269|PubMed:24888894}.
/FTId=VAR_071674.
VARIANT 223 223 R -> G (in EIEE13; loss of function
mutation; reduces channel activity;
dbSNP:rs672601319).
{ECO:0000269|PubMed:25239001}.
/FTId=VAR_072182.
VARIANT 260 260 F -> S (in EIEE13; unknown pathological
significance; dbSNP:rs879255697).
{ECO:0000269|PubMed:25568300}.
/FTId=VAR_076600.
VARIANT 307 307 N -> S (in EIEE13; unknown pathological
significance).
{ECO:0000269|PubMed:27864847}.
/FTId=VAR_078202.
VARIANT 407 407 L -> F (in EIEE13; unknown pathological
significance; dbSNP:rs879255698).
{ECO:0000269|PubMed:25785782}.
/FTId=VAR_076601.
VARIANT 408 408 A -> T (in EIEE13; unknown pathological
significance).
{ECO:0000269|PubMed:26993267}.
/FTId=VAR_078753.
VARIANT 410 410 V -> L (in EIEE13; unknown pathological
significance; dbSNP:rs879255699).
{ECO:0000269|PubMed:25568300}.
/FTId=VAR_076602.
VARIANT 479 479 E -> V (in EIEE13; unknown pathological
significance).
{ECO:0000269|PubMed:25568300}.
/FTId=VAR_076603.
VARIANT 662 662 R -> C (in EIEE13; unknown pathological
significance).
{ECO:0000269|PubMed:23708187}.
/FTId=VAR_078612.
VARIANT 767 767 T -> I (in EIEE13; gain-of-function
mutation; increases channel activity;
dbSNP:rs797045013).
{ECO:0000269|PubMed:24874546}.
/FTId=VAR_072183.
VARIANT 846 846 F -> S (in EIEE13; dbSNP:rs879255700).
{ECO:0000269|PubMed:24888894}.
/FTId=VAR_071675.
VARIANT 850 850 R -> Q (in EIEE13; unknown pathological
significance; dbSNP:rs587780586).
{ECO:0000269|PubMed:25785782}.
/FTId=VAR_076604.
VARIANT 890 890 A -> T (in EIEE13; dbSNP:rs879255702).
{ECO:0000269|PubMed:25568300,
ECO:0000269|PubMed:25785782}.
/FTId=VAR_076605.
VARIANT 960 960 V -> D (in EIEE13; unknown pathological
significance; dbSNP:rs879255703).
{ECO:0000269|PubMed:25568300}.
/FTId=VAR_076606.
VARIANT 978 978 S -> G (in EIEE13).
{ECO:0000269|PubMed:27864847}.
/FTId=VAR_078203.
VARIANT 984 984 N -> K (in EIEE13; gain-of-function
mutation; increased channel activity;
dbSNP:rs876657399).
{ECO:0000269|PubMed:25725044}.
/FTId=VAR_076607.
VARIANT 1279 1279 L -> V (in EIEE13).
{ECO:0000269|PubMed:23708187}.
/FTId=VAR_078613.
VARIANT 1323 1323 A -> S (in EIEE13; unknown pathological
significance).
{ECO:0000269|PubMed:26993267}.
/FTId=VAR_078754.
VARIANT 1327 1327 I -> V (in EIEE13; dbSNP:rs879255704).
{ECO:0000269|PubMed:24352161,
ECO:0000269|PubMed:26993267}.
/FTId=VAR_071676.
VARIANT 1331 1331 L -> V (in EIEE13; unknown pathological
significance; dbSNP:rs397514738).
{ECO:0000269|PubMed:25568300}.
/FTId=VAR_076608.
VARIANT 1451 1451 G -> S (in EIEE13; loss of channel
activity; dbSNP:rs863223345).
{ECO:0000269|PubMed:25725044}.
/FTId=VAR_076609.
VARIANT 1466 1466 N -> K (in EIEE13; dbSNP:rs587777722).
{ECO:0000269|PubMed:24888894}.
/FTId=VAR_071677.
VARIANT 1466 1466 N -> T (in EIEE13; dbSNP:rs587777723).
{ECO:0000269|PubMed:24888894}.
/FTId=VAR_071678.
VARIANT 1475 1475 G -> R (in EIEE13; dbSNP:rs796053216).
{ECO:0000269|PubMed:27864847}.
/FTId=VAR_078204.
VARIANT 1479 1479 I -> V (in EIEE13; unknown pathological
significance; dbSNP:rs796053217).
{ECO:0000269|PubMed:25568300}.
/FTId=VAR_076610.
VARIANT 1483 1483 E -> K (in BFIS5; dbSNP:rs879255652).
{ECO:0000269|PubMed:26677014}.
/FTId=VAR_076927.
VARIANT 1592 1592 V -> L (in EIEE13; unknown pathological
significance; dbSNP:rs587780454).
{ECO:0000269|PubMed:25568300}.
/FTId=VAR_076611.
VARIANT 1596 1596 S -> C (in EIEE13; unknown pathological
significance; dbSNP:rs879255705).
{ECO:0000269|PubMed:25785782}.
/FTId=VAR_076612.
VARIANT 1605 1605 I -> R (in EIEE13; unknown pathological
significance).
{ECO:0000269|PubMed:25568300}.
/FTId=VAR_076613.
VARIANT 1617 1617 R -> Q (in EIEE13; gain-of-function
mutation; increased channel activity;
impaired channel inactivation;
dbSNP:rs587777721).
{ECO:0000269|PubMed:24888894,
ECO:0000269|PubMed:25568300,
ECO:0000269|PubMed:25785782,
ECO:0000269|PubMed:26900580}.
/FTId=VAR_071679.
VARIANT 1650 1650 A -> T (in EIEE13; dbSNP:rs879255709).
{ECO:0000269|PubMed:24888894,
ECO:0000269|PubMed:25568300,
ECO:0000269|PubMed:27864847}.
/FTId=VAR_071680.
VARIANT 1754 1754 F -> S (in EIEE13; unknown pathological
significance).
{ECO:0000269|PubMed:26993267}.
/FTId=VAR_078755.
VARIANT 1768 1768 N -> D (in EIEE13; gain-of-function
mutation; results in increased persistent
sodium currents and incomplete channel
inactivation; dbSNP:rs202151337).
{ECO:0000269|PubMed:22365152}.
/FTId=VAR_067539.
VARIANT 1801 1801 Q -> E (in EIEE13; unknown pathological
significance; dbSNP:rs879255710).
{ECO:0000269|PubMed:25568300}.
/FTId=VAR_076614.
VARIANT 1865 1865 L -> P (in EIEE13; unknown pathological
significance).
{ECO:0000269|PubMed:26993267}.
/FTId=VAR_078756.
VARIANT 1872 1872 R -> L (in EIEE13; gain-of-function
mutation; increased channel activity;
impaired channel inactivation;
dbSNP:rs796053229).
{ECO:0000269|PubMed:26900580}.
/FTId=VAR_076615.
VARIANT 1872 1872 R -> Q (in EIEE13; gain-of-function
mutation; increased channel activity;
impaired channel inactivation).
{ECO:0000269|PubMed:25568300,
ECO:0000269|PubMed:26900580}.
/FTId=VAR_076616.
VARIANT 1872 1872 R -> W (in EIEE13; gain-of-function
mutation; increased channel activity;
impaired channel inactivation; no effect
on interactions with FGF14, SCN1B, GNB2
and GNG3; dbSNP:rs796053228).
{ECO:0000269|PubMed:24888894,
ECO:0000269|PubMed:25568300,
ECO:0000269|PubMed:26900580,
ECO:0000269|PubMed:27864847}.
/FTId=VAR_071681.
VARIANT 1877 1877 N -> S (in EIEE13 and BFIS5; also found
in a patient with drug-resistant focal
epilepsy and mild intellectual
disability; dbSNP:rs587780455).
{ECO:0000269|PubMed:27210545,
ECO:0000269|PubMed:27864847}.
/FTId=VAR_076617.
CONFLICT 5 5 L -> V (in Ref. 5; AAF35390).
{ECO:0000305}.
CONFLICT 133 133 V -> L (in Ref. 1; AAD15789).
{ECO:0000305}.
CONFLICT 257 257 L -> M (in Ref. 5; AAF35390).
{ECO:0000305}.
CONFLICT 273 273 F -> I (in Ref. 3; ACM63162).
{ECO:0000305}.
CONFLICT 274 278 MGNLR -> HGEPS (in Ref. 5; AAF35390).
{ECO:0000305}.
CONFLICT 453 453 T -> N (in Ref. 5; AAF35390).
{ECO:0000305}.
CONFLICT 477 477 S -> F (in Ref. 5; AAF35390).
{ECO:0000305}.
CONFLICT 483 483 L -> I (in Ref. 5; AAF35390).
{ECO:0000305}.
CONFLICT 492 492 R -> S (in Ref. 5; AAF35390).
{ECO:0000305}.
CONFLICT 504 504 S -> F (in Ref. 5; AAF35390).
{ECO:0000305}.
CONFLICT 547 548 LL -> MF (in Ref. 5; AAF35390).
{ECO:0000305}.
CONFLICT 1416 1416 M -> V (in Ref. 3; ACM63162).
{ECO:0000305}.
CONFLICT 1445 1445 V -> I (in Ref. 1; AAD15789).
{ECO:0000305}.
CONFLICT 1519 1519 V -> I (in Ref. 1; AAD15789).
{ECO:0000305}.
CONFLICT 1702 1702 T -> A (in Ref. 5; AAF35390).
{ECO:0000305}.
SEQUENCE 1980 AA; 225280 MW; 0EFC7BFB137FD4F0 CRC64;
MAARLLAPPG PDSFKPFTPE SLANIERRIA ESKLKKPPKA DGSHREDDED SKPKPNSDLE
AGKSLPFIYG DIPQGLVAVP LEDFDPYYLT QKTFVVLNRG KTLFRFSATP ALYILSPFNL
IRRIAIKILI HSVFSMIIMC TILTNCVFMT FSNPPDWSKN VEYTFTGIYT FESLVKIIAR
GFCIDGFTFL RDPWNWLDFS VIMMAYITEF VNLGNVSALR TFRVLRALKT ISVIPGLKTI
VGALIQSVKK LSDVMILTVF CLSVFALIGL QLFMGNLRNK CVVWPINFNE SYLENGTKGF
DWEEYINNKT NFYTVPGMLE PLLCGNSSDA GQCPEGYQCM KAGRNPNYGY TSFDTFSWAF
LALFRLMTQD YWENLYQLTL RAAGKTYMIF FVLVIFVGSF YLVNLILAVV AMAYEEQNQA
TLEEAEQKEA EFKAMLEQLK KQQEEAQAAA MATSAGTVSE DAIEEEGEEG GGSPRSSSEI
SKLSSKSAKE RRNRRKKRKQ KELSEGEEKG DPEKVFKSES EDGMRRKAFR LPDNRIGRKF
SIMNQSLLSI PGSPFLSRHN SKSSIFSFRG PGRFRDPGSE NEFADDEHST VEESEGRRDS
LFIPIRARER RSSYSGYSGY SQGSRSSRIF PSLRRSVKRN STVDCNGVVS LIGGPGSHIG
GRLLPEATTE VEIKKKGPGS LLVSMDQLAS YGRKDRINSI MSVVTNTLVE ELEESQRKCP
PCWYKFANTF LIWECHPYWI KLKEIVNLIV MDPFVDLAIT ICIVLNTLFM AMEHHPMTPQ
FEHVLAVGNL VFTGIFTAEM FLKLIAMDPY YYFQEGWNIF DGFIVSLSLM ELSLADVEGL
SVLRSFRLLR VFKLAKSWPT LNMLIKIIGN SVGALGNLTL VLAIIVFIFA VVGMQLFGKS
YKECVCKINQ DCELPRWHMH DFFHSFLIVF RVLCGEWIET MWDCMEVAGQ AMCLIVFMMV
MVIGNLVVLN LFLALLLSSF SADNLAATDD DGEMNNLQIS VIRIKKGVAW TKLKVHAFMQ
AHFKQREADE VKPLDELYEK KANCIANHTG ADIHRNGDFQ KNGNGTTSGI GSSVEKYIID
EDHMSFINNP NLTVRVPIAV GESDFENLNT EDVSSESDPE GSKDKLDDTS SSEGSTIDIK
PEVEEVPVEQ PEEYLDPDAC FTEGCVQRFK CCQVNIEEGL GKSWWILRKT CFLIVEHNWF
ETFIIFMILL SSGALAFEDI YIEQRKTIRT ILEYADKVFT YIFILEMLLK WTAYGFVKFF
TNAWCWLDFL IVAVSLVSLI ANALGYSELG AIKSLRTLRA LRPLRALSRF EGMRVVVNAL
VGAIPSIMNV LLVCLIFWLI FSIMGVNLFA GKYHYCFNET SEIRFEIEDV NNKTECEKLM
EGNNTEIRWK NVKINFDNVG AGYLALLQVA TFKGWMDIMY AAVDSRKPDE QPKYEDNIYM
YIYFVIFIIF GSFFTLNLFI GVIIDNFNQQ KKKFGGQDIF MTEEQKKYYN AMKKLGSKKP
QKPIPRPLNK IQGIVFDFVT QQAFDIVIMM LICLNMVTMM VETDTQSKQM ENILYWINLV
FVIFFTCECV LKMFALRHYY FTIGWNIFDF VVVILSIVGM FLADIIEKYF VSPTLFRVIR
LARIGRILRL IKGAKGIRTL LFALMMSLPA LFNIGLLLFL VMFIFSIFGM SNFAYVKHEA
GIDDMFNFET FGNSMICLFQ ITTSAGWDGL LLPILNRPPD CSLDKEHPGS GFKGDCGNPS
VGIFFFVSYI IISFLIVVNM YIAIILENFS VATEESADPL SEDDFETFYE IWEKFDPDAT
QFIEYCKLAD FADALEHPLR VPKPNTIELI AMDLPMVSGD RIHCLDILFA FTKRVLGDSG
ELDILRQQME ERFVASNPSK VSYEPITTTL RRKQEEVSAV VLQRAYRGHL ARRGFICKKT
TSNKLENGGT HREKKESTPS TASLPSYDSV TKPEKEKQQR AEEGRRERAK RQKEVRESKC


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