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Entry version 196 (13 Feb 2019)
Sequence version 4 (23 Mar 2010)
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Protein

Sodium channel protein type 4 subunit alpha

Gene

SCN4A

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Pore-forming subunit of a voltage-gated sodium channel complex through which Na+ ions pass in accordance with their electrochemical gradient. Alternates between resting, activated and inactivated states (PubMed:12766226, PubMed:29992740, PubMed:30190309, PubMed:15318338, PubMed:16890191, PubMed:18690054, PubMed:17898326, PubMed:19347921, PubMed:25707578, PubMed:26700687). Required for normal muscle fiber excitability, normal muscle contraction and relaxation cycles, and constant muscle strength in the presence of fluctuating K+ levels (PubMed:12766226, PubMed:15318338, PubMed:16890191, PubMed:19347921, PubMed:25707578, PubMed:26700687, PubMed:26659129).11 Publications

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Channel activity is regulated by the ancillary beta subunit SCN1B (PubMed:29992740). SCN1B strongly enhances the presence of the pore-forming alpha subunit at the cell surface (PubMed:29992740, PubMed:30190309). Interaction with SCN1B is required for rapid channel inactivation and rapid recovery after inactivation, and prevents decrease of channel activity in response to repetitive, high-frequency depolarizations (By similarity). The channel is inhibited by tetrodotoxin and saxitoxin (PubMed:30190309).By similarity2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei407Important for inhibition by tetrodotoxinBy similarity1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

  • membrane depolarization during action potential Source: GO_Central
  • muscle contraction Source: ProtInc
  • neuronal action potential Source: GO_Central
  • regulation of ion transmembrane transport Source: UniProtKB-KW
  • regulation of skeletal muscle contraction by action potential Source: UniProtKB
  • sodium ion transmembrane transport Source: UniProtKB
  • sodium ion transport Source: ProtInc

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionIon channel, Sodium channel, Voltage-gated channel
Biological processIon transport, Sodium transport, Transport
LigandSodium

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-445095 Interaction between L1 and Ankyrins
R-HSA-5576892 Phase 0 - rapid depolarisation

SIGNOR Signaling Network Open Resource

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SIGNORi
P35499

Protein family/group databases

Transport Classification Database

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TCDBi
1.A.1.10.4 the voltage-gated ion channel (vic) superfamily

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Sodium channel protein type 4 subunit alpha
Alternative name(s):
SkM11 Publication
Sodium channel protein skeletal muscle subunit alpha
Sodium channel protein type IV subunit alpha
Voltage-gated sodium channel subunit alpha Nav1.4
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:SCN4A
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 17

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000007314.11

Human Gene Nomenclature Database

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HGNCi
HGNC:10591 SCN4A

Online Mendelian Inheritance in Man (OMIM)

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MIMi
603967 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_P35499

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 131Cytoplasmic1 PublicationAdd BLAST131
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei132 – 150Helical; Name=S1 of repeat I1 PublicationAdd BLAST19
Topological domaini151 – 157Extracellular1 Publication7
Transmembranei158 – 178Helical; Name=S2 of repeat I1 PublicationAdd BLAST21
Topological domaini179 – 192Cytoplasmic1 PublicationAdd BLAST14
Transmembranei193 – 210Helical; Name=S3 of repeat I1 PublicationAdd BLAST18
Topological domaini211 – 216Extracellular1 Publication6
Transmembranei217 – 233Helical; Name=S4 of repeat I1 PublicationAdd BLAST17
Topological domaini234 – 252Cytoplasmic1 PublicationAdd BLAST19
Transmembranei253 – 272Helical; Name=S5 of repeat I1 PublicationAdd BLAST20
Topological domaini273 – 391Extracellular1 PublicationAdd BLAST119
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a region that is buried within a membrane, but does not cross it.<p><a href='/help/intramem' target='_top'>More...</a></p>Intramembranei392 – 416Pore-forming1 PublicationAdd BLAST25
Topological domaini417 – 423Extracellular1 Publication7
Transmembranei424 – 444Helical; Name=S6 of repeat I1 PublicationAdd BLAST21
Topological domaini445 – 578Cytoplasmic1 PublicationAdd BLAST134
Transmembranei579 – 597Helical; Name=S1 of repeat II1 PublicationAdd BLAST19
Topological domaini598 – 608Extracellular1 PublicationAdd BLAST11
Transmembranei609 – 628Helical; Name=S2 of repeat II1 PublicationAdd BLAST20
Topological domaini629 – 642Cytoplasmic1 PublicationAdd BLAST14
Transmembranei643 – 662Helical; Name=S3 of repeat II1 PublicationAdd BLAST20
Topological domaini663 – 664Extracellular1 Publication2
Transmembranei665 – 682Helical; Name=S4 of repeat II1 PublicationAdd BLAST18
Topological domaini683 – 698Cytoplasmic1 PublicationAdd BLAST16
Transmembranei699 – 717Helical; Name=S5 of repeat II1 PublicationAdd BLAST19
Topological domaini718 – 746Extracellular1 PublicationAdd BLAST29
Intramembranei747 – 767Pore-forming1 PublicationAdd BLAST21
Topological domaini768 – 778Extracellular1 PublicationAdd BLAST11
Transmembranei779 – 797Helical; Name=S6 of repeat II1 PublicationAdd BLAST19
Topological domaini798 – 1032Cytoplasmic1 PublicationAdd BLAST235
Transmembranei1033 – 1050Helical; Name=S1 of repeat III1 PublicationAdd BLAST18
Topological domaini1051 – 1063Extracellular1 PublicationAdd BLAST13
Transmembranei1064 – 1082Helical; Name=S2 of repeat III1 PublicationAdd BLAST19
Topological domaini1083 – 1096Cytoplasmic1 PublicationAdd BLAST14
Transmembranei1097 – 1115Helical; Name=S3 of repeat III1 PublicationAdd BLAST19
Topological domaini1116 – 1123Extracellular1 Publication8
Transmembranei1124 – 1142Helical; Name=S4 of repeat III1 PublicationAdd BLAST19
Topological domaini1143 – 1159Cytoplasmic1 PublicationAdd BLAST17
Transmembranei1160 – 1179Helical; Name=S5 of repeat III1 PublicationAdd BLAST20
Topological domaini1180 – 1230Extracellular1 PublicationAdd BLAST51
Intramembranei1231 – 1252Pore-forming1 PublicationAdd BLAST22
Topological domaini1253 – 1269Extracellular1 PublicationAdd BLAST17
Transmembranei1270 – 1291Helical; Name=S6 of repeat III1 PublicationAdd BLAST22
Topological domaini1292 – 1354Cytoplasmic1 PublicationAdd BLAST63
Transmembranei1355 – 1372Helical; Name=S1 of repeat IV1 PublicationAdd BLAST18
Topological domaini1373 – 1383Extracellular1 PublicationAdd BLAST11
Transmembranei1384 – 1402Helical; Name=S2 of repeat IV1 PublicationAdd BLAST19
Topological domaini1403 – 1414Cytoplasmic1 PublicationAdd BLAST12
Transmembranei1415 – 1432Helical; Name=S3 of repeat IV1 PublicationAdd BLAST18
Topological domaini1433 – 1445Extracellular1 PublicationAdd BLAST13
Transmembranei1446 – 1462Helical; Name=S4 of repeat IV1 PublicationAdd BLAST17
Topological domaini1463 – 1481Cytoplasmic1 PublicationAdd BLAST19
Transmembranei1482 – 1499Helical; Name=S5 of repeat IV1 PublicationAdd BLAST18
Topological domaini1500 – 1521Extracellular1 PublicationAdd BLAST22
Intramembranei1522 – 1544Pore-forming1 PublicationAdd BLAST23
Topological domaini1545 – 1574Extracellular1 PublicationAdd BLAST30
Transmembranei1575 – 1597Helical; Name=S6 of repeat IV1 PublicationAdd BLAST23
Topological domaini1598 – 1836Cytoplasmic1 PublicationAdd BLAST239

Keywords - Cellular componenti

Cell membrane, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Paramyotonia congenita of von Eulenburg (PMC)16 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal dominant channelopathy characterized by myotonia, increased by exposure to cold, intermittent flaccid paresis, not necessarily dependent on cold or myotonia, lability of serum potassium, non-progressive nature and lack of atrophy or hypertrophy of muscles. In some patients, myotonia is not increased by cold exposure (paramyotonia without cold paralysis). Patients may have a combination phenotype of PMC and HYPP.
See also OMIM:168300
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_054936270Q → K in PMC. 2 Publications1
Natural variantiVAR_065231693I → T in PMC. 1 PublicationCorresponds to variant dbSNP:rs80338956EnsemblClinVar.1
Natural variantiVAR_001562704T → M in HYPP and PMC. 3 PublicationsCorresponds to variant dbSNP:rs80338957EnsemblClinVar.1
Natural variantiVAR_001563804S → F in PMC. 1 PublicationCorresponds to variant dbSNP:rs121908546EnsemblClinVar.1
Natural variantiVAR_0223411152A → D in PMC. 1 Publication1
Natural variantiVAR_0015651156A → T in PMC, MYOSCN4A and HYPP. 2 PublicationsCorresponds to variant dbSNP:rs80338958EnsemblClinVar.1
Natural variantiVAR_0015661293V → I in PMC; without cold paralysis. 1 PublicationCorresponds to variant dbSNP:rs121908551EnsemblClinVar.1
Natural variantiVAR_0015671306G → A in PMC. 2 PublicationsCorresponds to variant dbSNP:rs80338792EnsemblClinVar.1
Natural variantiVAR_0015681306G → E in MYOSCN4A and PMC; severe. 4 PublicationsCorresponds to variant dbSNP:rs80338792EnsemblClinVar.1
Natural variantiVAR_0015691306G → V in MYOSCN4A and PMC. 3 PublicationsCorresponds to variant dbSNP:rs80338792EnsemblClinVar.1
Natural variantiVAR_0015701313T → M in PMC; changes the voltage-gated sodium channel activity; increases membrane hyperexcitability at low temperature; decreases channel activation, deactivation, fast inactivation and recovery delay from fast inactivation. 3 PublicationsCorresponds to variant dbSNP:rs121908547EnsemblClinVar.1
Natural variantiVAR_0015711433L → R in PMC and HYPP. 1 PublicationCorresponds to variant dbSNP:rs121908550EnsemblClinVar.1
Natural variantiVAR_0549471436L → P in PMC. 1 Publication1
Natural variantiVAR_0015721448R → C in PMC; changes the voltage-gated sodium channel activity; increases membrane hyperexcitability at low temperature; decreases channel activation, deactivation, fast inactivation and recovery delay from fast inactivation. 3 PublicationsCorresponds to variant dbSNP:rs121908544EnsemblClinVar.1
Natural variantiVAR_0015731448R → H in PMC. 2 PublicationsCorresponds to variant dbSNP:rs121908545EnsemblClinVar.1
Natural variantiVAR_0549481448R → L in PMC. 1 Publication1
Natural variantiVAR_0371071456G → E in PMC. 3 PublicationsCorresponds to variant dbSNP:rs121908554EnsemblClinVar.1
Natural variantiVAR_0549491473F → S in PMC; accelerates deactivation from the inactivated state and enhances the remobilization of gating charge. 2 Publications1
Natural variantiVAR_0015741589V → M in PMC. 2 PublicationsCorresponds to variant dbSNP:rs121908548EnsemblClinVar.1
Natural variantiVAR_0549521705F → I in PMC; increases the extent of charge immobilization in response to strong depolarization. 1 PublicationCorresponds to variant dbSNP:rs1064794243Ensembl.1
Periodic paralysis hypokalemic 2 (HOKPP2)12 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal dominant disorder manifested by episodic flaccid generalized muscle weakness associated with falls of serum potassium levels.
See also OMIM:613345
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_054935222R → W in HOKPP2. 1 PublicationCorresponds to variant dbSNP:rs527236148EnsemblClinVar.1
Natural variantiVAR_017788669R → H in HOKPP2. 2 PublicationsCorresponds to variant dbSNP:rs80338784EnsemblClinVar.1
Natural variantiVAR_054939672R → C in HOKPP2. 2 PublicationsCorresponds to variant dbSNP:rs80338785EnsemblClinVar.1
Natural variantiVAR_017789672R → G in HOKPP2. 3 PublicationsCorresponds to variant dbSNP:rs80338785EnsemblClinVar.1
Natural variantiVAR_017790672R → H in HOKPP2. 3 PublicationsCorresponds to variant dbSNP:rs80338788EnsemblClinVar.1
Natural variantiVAR_017791672R → S in HOKPP2. 3 PublicationsCorresponds to variant dbSNP:rs80338785EnsemblClinVar.1
Natural variantiVAR_0649871129R → Q in NKPP and HOKPP2; detected in a family where three affected members manifested hypokalemic periodic paralysis whereas five other patients had normokalemic periodic paralysis. 1 PublicationCorresponds to variant dbSNP:rs527236149EnsemblClinVar.1
Natural variantiVAR_0549431132R → Q in HOKPP2; changes the voltage-gated sodium channel activity; increases membrane hypoexcitability; increases channel activation and both fast and slow channel inactivation. 2 PublicationsCorresponds to variant dbSNP:rs80338789EnsemblClinVar.1
Natural variantiVAR_0754341135R → C in HOKPP2; also found in patients with severe fetal hypokinesia or congenital myopathy; increased depolarization tendency at normal and reduced extracellular potassium and reduced amplitude and rise time of action potentials. 2 PublicationsCorresponds to variant dbSNP:rs1287863349Ensembl.1
Natural variantiVAR_0549441135R → H in HOKPP2; increased depolarization tendency at normal and reduced extracellular potassium and reduced amplitude and rise time of action potentials. 2 PublicationsCorresponds to variant dbSNP:rs527236150EnsemblClinVar.1
Natural variantiVAR_0177921158P → S in HOKPP2; atypical phenotype with heat-induced myotonia and cold-induced paralysis with hypokalemia; changes the voltage-gated sodium channel activity; increases channel activation and slow inactivation at low temperature. 2 PublicationsCorresponds to variant dbSNP:rs121908555EnsemblClinVar.1
Periodic paralysis hyperkalemic (HYPP)3 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal dominant channelopathy characterized by episodic flaccid generalized muscle weakness associated with high levels of serum potassium. Concurrence of myotonia is found in HYPP patients.
See also OMIM:170500
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_001562704T → M in HYPP and PMC. 3 PublicationsCorresponds to variant dbSNP:rs80338957EnsemblClinVar.1
Natural variantiVAR_0015651156A → T in PMC, MYOSCN4A and HYPP. 2 PublicationsCorresponds to variant dbSNP:rs80338958EnsemblClinVar.1
Natural variantiVAR_0015711433L → R in PMC and HYPP. 1 PublicationCorresponds to variant dbSNP:rs121908550EnsemblClinVar.1
Natural variantiVAR_0015751592M → V in HYPP and NKPP. 2 PublicationsCorresponds to variant dbSNP:rs80338962EnsemblClinVar.1
Periodic paralysis normokalemic (NKPP)3 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder closely related to hyperkalemic periodic paralysis, but marked by a lack of alterations in potassium levels during attacks of muscle weakness.
See also OMIM:170500
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_037104675R → G in NKPP. 1 PublicationCorresponds to variant dbSNP:rs121908556EnsemblClinVar.1
Natural variantiVAR_037105675R → Q in NKPP. 2 PublicationsCorresponds to variant dbSNP:rs121908557EnsemblClinVar.1
Natural variantiVAR_037106675R → W in NKPP. 1 PublicationCorresponds to variant dbSNP:rs121908556EnsemblClinVar.1
Natural variantiVAR_0649871129R → Q in NKPP and HOKPP2; detected in a family where three affected members manifested hypokalemic periodic paralysis whereas five other patients had normokalemic periodic paralysis. 1 PublicationCorresponds to variant dbSNP:rs527236149EnsemblClinVar.1
Natural variantiVAR_0015751592M → V in HYPP and NKPP. 2 PublicationsCorresponds to variant dbSNP:rs80338962EnsemblClinVar.1
Myotonia SCN4A-related (MYOSCN4A)13 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA phenotypically highly variable myotonia aggravated by potassium loading, and sometimes by cold. Myotonia is characterized by sustained muscle tensing that prevents muscles from relaxing normally. It causes muscle stiffness that can interfere with movement. In some people the stiffness is very mild, while in other cases it may be severe enough to interfere with walking, running, and other activities of daily life. Myotonia SCN4A-related includes myotonia permanens and myotonia fluctuans. In myotonia permanens, the myotonia is generalized and there is a hypertrophy of the muscle, particularly in the neck and the shoulder. Attacks of severe muscle stiffness of the thoracic muscles may be life threatening due to impaired ventilation. In myotonia fluctuans, the muscle stiffness may fluctuate from day to day, provoked by exercise.
See also OMIM:608390
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_054934141I → V in MYOSCN4A; causes a hyperpolarizing shift of the activation curve; enhances channel slow inactivation. 1 PublicationCorresponds to variant dbSNP:rs121908561EnsemblClinVar.1
Natural variantiVAR_065230225R → W in MYOSCN4A; also found in patients with severe fetal hypokinesia or congenital myopathy; impaired sodium channel function. 2 PublicationsCorresponds to variant dbSNP:rs764718003Ensembl.1
Natural variantiVAR_017786445V → M in MYOSCN4A. 3 PublicationsCorresponds to variant dbSNP:rs121908552EnsemblClinVar.1
Natural variantiVAR_054937452E → K in MYOSCN4A; variable phenotype ranging from mild to severe myotonia. 1 PublicationCorresponds to variant dbSNP:rs372631097Ensembl.1
Natural variantiVAR_054938671F → S in MYOSCN4A. 1 Publication1
Natural variantiVAR_054940715A → T in MYOSCN4A. 1 PublicationCorresponds to variant dbSNP:rs749400108Ensembl.1
Natural variantiVAR_054942804S → N in MYOSCN4A. 1 Publication1
Natural variantiVAR_0177931160I → V in MYOSCN4A; acetazolamide-responsive myotonia. 1 PublicationCorresponds to variant dbSNP:rs121908549EnsemblClinVar.1
Natural variantiVAR_0795191290F → L in MYOSCN4A; enhances voltage-gated sodium channel activation inducing membrane hyperexcitability. 1 Publication1
Natural variantiVAR_0549451297N → K in MYOSCN4A; unusually severe and lethal phenotype with neonatal onset. 1 PublicationCorresponds to variant dbSNP:rs121908560EnsemblClinVar.1
Natural variantiVAR_0015681306G → E in MYOSCN4A and PMC; severe. 4 PublicationsCorresponds to variant dbSNP:rs80338792EnsemblClinVar.1
Natural variantiVAR_0015691306G → V in MYOSCN4A and PMC. 3 PublicationsCorresponds to variant dbSNP:rs80338792EnsemblClinVar.1
Natural variantiVAR_0549461310I → N in MYOSCN4A. 1 Publication1
Natural variantiVAR_0549501476M → I in MYOSCN4A; highly variable severity. 2 PublicationsCorresponds to variant dbSNP:rs121908559EnsemblClinVar.1
Natural variantiVAR_0549511481A → D in MYOSCN4A; fluctuating cold-induced and exercise-induced stiffness. 1 Publication1
Natural variantiVAR_0745811633Q → E in MYOSCN4A; changes the voltage-gated sodium channel activity; increases membrane hyperexcitability; decreases channel fast inactivation. 1 Publication1
Myasthenic syndrome, congenital, 16 (CMS16)3 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of congenital myasthenic syndrome, a group of disorders characterized by failure of neuromuscular transmission, including pre-synaptic, synaptic, and post-synaptic disorders that are not of autoimmune origin. Clinical features are easy fatigability and muscle weakness. CMS16 is characterized by fatigable generalized weakness and recurrent attacks of respiratory and bulbar paralysis since birth. The fatigable weakness involves lid-elevator, external ocular, facial, limb and truncal muscles and an decremental response of the compound muscle action potential on repetitive stimulation.
See also OMIM:614198
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0177951442V → E in CMS16; leads to fast inactivation. 1 PublicationCorresponds to variant dbSNP:rs121908553EnsemblClinVar.1
Natural variantiVAR_0754361454R → W in CMS16; leads to hyperpolarization of the steady-state fast inactivation, slow recovery from inactivation and reduces the channel ability to activate in response to repetitive stimulating pulses. 1 PublicationCorresponds to variant dbSNP:rs879253789EnsemblClinVar.1
Natural variantiVAR_0754371457R → H in CMS16; enhanced fast inactivation and slowed recovery from fast inactivation. 1 PublicationCorresponds to variant dbSNP:rs863225046EnsemblClinVar.1
SCN4A mutations are the cause of an autosomal recessive neuromuscular disorder characterized by severe fetal hypokinesia, neonatal hypotonia and congenital myopathy of variable severity. The most severe clinical features include reduced or absent fetal movements, in-utero upper and lower limb contractures, talipes and hydrops, and intrauterine or early postnatal death. Mildly affected patients present with generalized hypotonia and weakness at birth or within the first few days of life, mild-to-moderate facial muscle weakness without ptosis, significant early respiratory and feeding difficulties, and skeletal abnormalities of the spine and palate. Symptoms improve over time in patients who survive infancy, resulting in gain of muscle strength and motor skills and concomitant resolution of early respiratory and feeding difficulties. In contrast to other SCN4A-related channelopathies, affected individuals manifest in-utero or neonatal onset of permanent muscle weakness, rather than later-onset episodic muscle weakness.1 Publication

Keywords - Diseasei

Congenital myasthenic syndrome, Disease mutation

Organism-specific databases

DisGeNET

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DisGeNETi
6329

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

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GeneReviewsi
SCN4A

MalaCards human disease database

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MalaCardsi
SCN4A
MIMi168300 phenotype
170500 phenotype
608390 phenotype
613345 phenotype
614198 phenotype

Open Targets

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OpenTargetsi
ENSG00000007314

Orphanet; a database dedicated to information on rare diseases and orphan drugs

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Orphaneti
99736 Acetazolamide-responsive myotonia
682 Hyperkalemic periodic paralysis
681 Hypokalemic periodic paralysis
99734 Myotonia fluctuans
99735 Myotonia permanens
684 Paramyotonia congenita of Von Eulenburg
98913 Postsynaptic congenital myasthenic syndromes

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA35006

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL2072

Drug and drug target database

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DrugBanki
DB00586 Diclofenac
DB01195 Flecainide
DB00818 Propofol
DB00313 Valproic Acid
DB00909 Zonisamide

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
581

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
SCN4A

Domain mapping of disease mutations (DMDM)

More...
DMDMi
292495096

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000484951 – 1836Sodium channel protein type 4 subunit alphaAdd BLAST1836

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi214N-linked (GlcNAc...) asparagineSequence analysis1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi280 ↔ 360Combined sources1 Publication
Glycosylationi288N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi291N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi297N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi303N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi315N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi321N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi333N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi362N-linked (GlcNAc...) asparagineCombined sources1 Publication1
Disulfide bondi369 ↔ 375Combined sources1 Publication
Disulfide bondi729Interchain; with SCN2B or SCN4BBy similarity
Disulfide bondi729Interchain; 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)By similarity
Disulfide bondi731 ↔ 737Combined sources1 Publication
Disulfide bondi769 ↔ 778Combined sources1 Publication
Disulfide bondi1189 ↔ 1209Combined sources1 Publication
Glycosylationi1191N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1205N-linked (GlcNAc...) asparagineCombined sources1 Publication1
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei1328Phosphoserine; by PKCBy similarity1
Disulfide bondi1553 ↔ 1568Combined sources1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylation at Ser-1328 by PKC in a highly conserved cytoplasmic loop slows inactivation of the sodium channel and reduces peak sodium currents.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P35499

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
P35499

PeptideAtlas

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PeptideAtlasi
P35499

PRoteomics IDEntifications database

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PRIDEi
P35499

ProteomicsDB human proteome resource

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ProteomicsDBi
55071

PTM databases

GlyConnect protein glycosylation platform

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GlyConnecti
1752

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P35499

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
P35499

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000007314 Expressed in 99 organ(s), highest expression level in muscle of leg

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P35499 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
HPA053992

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Component of a voltage-sensitive sodium channel complex that consists of an ion-conducting pore-forming alpha subunit and one or more regulatory beta subunits (PubMed:29992740, PubMed:30190309). Interacts with SCN1B (PubMed:29992740, PubMed:30190309). Heterooligomer with SCN2B or SCN4B; disulfide-linked (By similarity). Interacts with the PDZ domain of the syntrophins SNTA1, SNTB1 and SNTB2 (By similarity). Interacts with the conotoxin GVIIJ (PubMed:24497506).By similarity3 Publications

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
112234, 4 interactors

Protein interaction database and analysis system

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IntActi
P35499, 6 interactors

STRING: functional protein association networks

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STRINGi
9606.ENSP00000396320

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P35499

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

11836
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
6AGFelectron microscopy3.20A1-1836[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P35499

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P35499

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati113 – 454ICuratedAdd BLAST342
Repeati560 – 832IICuratedAdd BLAST273
Repeati1013 – 1326IIICuratedAdd BLAST314
Repeati1335 – 1633IVCuratedAdd BLAST299
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini1727 – 1756IQPROSITE-ProRule annotationAdd BLAST30

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1310 – 1312Important for rapid channel inactivationBy similarity3

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

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.1 Publication

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG410INF8 Eukaryota
COG1226 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000159417

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000231755

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG053100

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P35499

KEGG Orthology (KO)

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KOi
K04837

Database of Orthologous Groups

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OrthoDBi
1579815at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P35499

TreeFam database of animal gene trees

More...
TreeFami
TF323985

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.20.120.350, 4 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR005821 Ion_trans_dom
IPR000048 IQ_motif_EF-hand-BS
IPR008052 Na_channel_a4su_mammal
IPR001696 Na_channel_asu
IPR010526 Na_trans_assoc
IPR027359 Volt_channel_dom_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00520 Ion_trans, 4 hits
PF06512 Na_trans_assoc, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00170 NACHANNEL
PR01665 NACHANNEL4

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50096 IQ, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

P35499-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MARPSLCTLV PLGPECLRPF TRESLAAIEQ RAVEEEARLQ RNKQMEIEEP
60 70 80 90 100
ERKPRSDLEA GKNLPMIYGD PPPEVIGIPL EDLDPYYSNK KTFIVLNKGK
110 120 130 140 150
AIFRFSATPA LYLLSPFSVV RRGAIKVLIH ALFSMFIMIT ILTNCVFMTM
160 170 180 190 200
SDPPPWSKNV EYTFTGIYTF ESLIKILARG FCVDDFTFLR DPWNWLDFSV
210 220 230 240 250
IMMAYLTEFV DLGNISALRT FRVLRALKTI TVIPGLKTIV GALIQSVKKL
260 270 280 290 300
SDVMILTVFC LSVFALVGLQ LFMGNLRQKC VRWPPPFNDT NTTWYSNDTW
310 320 330 340 350
YGNDTWYGNE MWYGNDSWYA NDTWNSHASW ATNDTFDWDA YISDEGNFYF
360 370 380 390 400
LEGSNDALLC GNSSDAGHCP EGYECIKTGR NPNYGYTSYD TFSWAFLALF
410 420 430 440 450
RLMTQDYWEN LFQLTLRAAG KTYMIFFVVI IFLGSFYLIN LILAVVAMAY
460 470 480 490 500
AEQNEATLAE DKEKEEEFQQ MLEKFKKHQE ELEKAKAAQA LEGGEADGDP
510 520 530 540 550
AHGKDCNGSL DTSQGEKGAP RQSSSGDSGI SDAMEELEEA HQKCPPWWYK
560 570 580 590 600
CAHKVLIWNC CAPWLKFKNI IHLIVMDPFV DLGITICIVL NTLFMAMEHY
610 620 630 640 650
PMTEHFDNVL TVGNLVFTGI FTAEMVLKLI AMDPYEYFQQ GWNIFDSIIV
660 670 680 690 700
TLSLVELGLA NVQGLSVLRS FRLLRVFKLA KSWPTLNMLI KIIGNSVGAL
710 720 730 740 750
GNLTLVLAII VFIFAVVGMQ LFGKSYKECV CKIALDCNLP RWHMHDFFHS
760 770 780 790 800
FLIVFRILCG EWIETMWDCM EVAGQAMCLT VFLMVMVIGN LVVLNLFLAL
810 820 830 840 850
LLSSFSADSL AASDEDGEMN NLQIAIGRIK LGIGFAKAFL LGLLHGKILS
860 870 880 890 900
PKDIMLSLGE ADGAGEAGEA GETAPEDEKK EPPEEDLKKD NHILNHMGLA
910 920 930 940 950
DGPPSSLELD HLNFINNPYL TIQVPIASEE SDLEMPTEEE TDTFSEPEDS
960 970 980 990 1000
KKPPQPLYDG NSSVCSTADY KPPEEDPEEQ AEENPEGEQP EECFTEACVQ
1010 1020 1030 1040 1050
RWPCLYVDIS QGRGKKWWTL RRACFKIVEH NWFETFIVFM ILLSSGALAF
1060 1070 1080 1090 1100
EDIYIEQRRV IRTILEYADK VFTYIFIMEM LLKWVAYGFK VYFTNAWCWL
1110 1120 1130 1140 1150
DFLIVDVSII SLVANWLGYS ELGPIKSLRT LRALRPLRAL SRFEGMRVVV
1160 1170 1180 1190 1200
NALLGAIPSI MNVLLVCLIF WLIFSIMGVN LFAGKFYYCI NTTTSERFDI
1210 1220 1230 1240 1250
SEVNNKSECE SLMHTGQVRW LNVKVNYDNV GLGYLSLLQV ATFKGWMDIM
1260 1270 1280 1290 1300
YAAVDSREKE EQPQYEVNLY MYLYFVIFII FGSFFTLNLF IGVIIDNFNQ
1310 1320 1330 1340 1350
QKKKLGGKDI FMTEEQKKYY NAMKKLGSKK PQKPIPRPQN KIQGMVYDLV
1360 1370 1380 1390 1400
TKQAFDITIM ILICLNMVTM MVETDNQSQL KVDILYNINM IFIIIFTGEC
1410 1420 1430 1440 1450
VLKMLALRQY YFTVGWNIFD FVVVILSIVG LALSDLIQKY FVSPTLFRVI
1460 1470 1480 1490 1500
RLARIGRVLR LIRGAKGIRT LLFALMMSLP ALFNIGLLLF LVMFIYSIFG
1510 1520 1530 1540 1550
MSNFAYVKKE SGIDDMFNFE TFGNSIICLF EITTSAGWDG LLNPILNSGP
1560 1570 1580 1590 1600
PDCDPNLENP GTSVKGDCGN PSIGICFFCS YIIISFLIVV NMYIAIILEN
1610 1620 1630 1640 1650
FNVATEESSE PLGEDDFEMF YETWEKFDPD ATQFIAYSRL SDFVDTLQEP
1660 1670 1680 1690 1700
LRIAKPNKIK LITLDLPMVP GDKIHCLDIL FALTKEVLGD SGEMDALKQT
1710 1720 1730 1740 1750
MEEKFMAANP SKVSYEPITT TLKRKHEEVC AIKIQRAYRR HLLQRSMKQA
1760 1770 1780 1790 1800
SYMYRHSHDG SGDDAPEKEG LLANTMSKMY GHENGNSSSP SPEEKGEAGD
1810 1820 1830
AGPTMGLMPI SPSDTAWPPA PPPGQTVRPG VKESLV
Length:1,836
Mass (Da):208,061
Last modified:March 23, 2010 - v4
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iFA9A6B81B7C2D50F
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti10 – 11VP → AR in AAA60554 (PubMed:1315496).Curated2
Sequence conflicti371E → K in AAA60554 (PubMed:1315496).Curated1
Sequence conflicti371E → Q in AAB59624 (PubMed:1315496).Curated1
Sequence conflicti870A → G in AAB59624 (PubMed:1315496).Curated1
Sequence conflicti1151 – 1152NA → KP in AAB59624 (PubMed:1315496).Curated2

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07459872P → L Found in a patient with severe dystrophia myotonica 2 (DM2) carrying a pathogenic CCTG repeat expansion in CNBP; unknown pathological significance; may act as a disease modifier; changes the voltage-gated sodium channel activity; increases membrane hyperexcitability; decreases channel fast inactivation. 1 PublicationCorresponds to variant dbSNP:rs1303471186Ensembl.1
Natural variantiVAR_075430104R → H Probable disease-associated mutation found in patients with severe fetal hypokinesia or congenital myopathy; complete loss of sodium channel function. 1 PublicationCorresponds to variant dbSNP:rs1248025530Ensembl.1
Natural variantiVAR_001560135M → V. 1
Natural variantiVAR_054934141I → V in MYOSCN4A; causes a hyperpolarizing shift of the activation curve; enhances channel slow inactivation. 1 PublicationCorresponds to variant dbSNP:rs121908561EnsemblClinVar.1
Natural variantiVAR_075431203M → K Probable disease-associated mutation found in patients with severe fetal hypokinesia or congenital myopathy; impaired sodium channel function. 1 PublicationCorresponds to variant dbSNP:rs933258893Ensembl.1
Natural variantiVAR_054935222R → W in HOKPP2. 1 PublicationCorresponds to variant dbSNP:rs527236148EnsemblClinVar.1
Natural variantiVAR_065230225R → W in MYOSCN4A; also found in patients with severe fetal hypokinesia or congenital myopathy; impaired sodium channel function. 2 PublicationsCorresponds to variant dbSNP:rs764718003Ensembl.1
Natural variantiVAR_017785246S → L No significant effect on channel activity. 1 PublicationCorresponds to variant dbSNP:rs80338951EnsemblClinVar.1
Natural variantiVAR_054936270Q → K in PMC. 2 Publications1
Natural variantiVAR_075432382P → T Probable disease-associated mutation found in patients with severe fetal hypokinesia or congenital myopathy; complete loss of sodium channel function. 1 Publication1
Natural variantiVAR_017786445V → M in MYOSCN4A. 3 PublicationsCorresponds to variant dbSNP:rs121908552EnsemblClinVar.1
Natural variantiVAR_054937452E → K in MYOSCN4A; variable phenotype ranging from mild to severe myotonia. 1 PublicationCorresponds to variant dbSNP:rs372631097Ensembl.1
Natural variantiVAR_001561524S → G3 PublicationsCorresponds to variant dbSNP:rs6504191EnsemblClinVar.1
Natural variantiVAR_017787559N → D2 PublicationsCorresponds to variant dbSNP:rs1047705Ensembl.1
Natural variantiVAR_017788669R → H in HOKPP2. 2 PublicationsCorresponds to variant dbSNP:rs80338784EnsemblClinVar.1
Natural variantiVAR_054938671F → S in MYOSCN4A. 1 Publication1
Natural variantiVAR_054939672R → C in HOKPP2. 2 PublicationsCorresponds to variant dbSNP:rs80338785EnsemblClinVar.1
Natural variantiVAR_017789672R → G in HOKPP2. 3 PublicationsCorresponds to variant dbSNP:rs80338785EnsemblClinVar.1
Natural variantiVAR_017790672R → H in HOKPP2. 3 PublicationsCorresponds to variant dbSNP:rs80338788EnsemblClinVar.1
Natural variantiVAR_017791672R → S in HOKPP2. 3 PublicationsCorresponds to variant dbSNP:rs80338785EnsemblClinVar.1
Natural variantiVAR_037104675R → G in NKPP. 1 PublicationCorresponds to variant dbSNP:rs121908556EnsemblClinVar.1
Natural variantiVAR_037105675R → Q in NKPP. 2 PublicationsCorresponds to variant dbSNP:rs121908557EnsemblClinVar.1
Natural variantiVAR_037106675R → W in NKPP. 1 PublicationCorresponds to variant dbSNP:rs121908556EnsemblClinVar.1
Natural variantiVAR_065231693I → T in PMC. 1 PublicationCorresponds to variant dbSNP:rs80338956EnsemblClinVar.1
Natural variantiVAR_001562704T → M in HYPP and PMC. 3 Publications