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Entry version 178 (13 Feb 2019)
Sequence version 3 (05 Apr 2011)
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Protein

Sodium channel protein type 9 subunit alpha

Gene

SCN9A

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

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 (PubMed:7720699, PubMed:17167479, PubMed:25240195, PubMed:26680203, PubMed:15385606, PubMed:16988069, PubMed:17145499, PubMed:19369487, PubMed:24311784). It is a tetrodotoxin-sensitive Na+ channel isoform (PubMed:7720699). Plays a role in pain mechanisms, especially in the development of inflammatory pain (PubMed:17167479, PubMed:17145499, PubMed:19369487, PubMed:24311784).10 Publications

<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

  • behavioral response to pain Source: Ensembl
  • inflammatory response Source: Ensembl
  • membrane depolarization during action potential Source: GO_Central
  • neuronal action potential Source: GO_Central
  • post-embryonic development Source: Ensembl
  • regulation of ion transmembrane transport Source: UniProtKB-KW
  • response to toxic substance Source: Ensembl
  • sensory perception of pain 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
Q15858

Protein family/group databases

Transport Classification Database

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TCDBi
1.A.1.10.5 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 9 subunit alphaCurated
Alternative name(s):
Neuroendocrine sodium channel1 Publication
Short name:
hNE-Na1 Publication
Peripheral sodium channel 1
Short name:
PN1By similarity
Sodium channel protein type IX subunit alpha
Voltage-gated sodium channel subunit alpha Nav1.7
<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:SCN9AImported
Synonyms:NENA
<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 2

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000169432.14

Human Gene Nomenclature Database

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HGNCi
HGNC:10597 SCN9A

Online Mendelian Inheritance in Man (OMIM)

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MIMi
603415 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_Q15858

<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 – 126CytoplasmicCuratedAdd BLAST126
<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>Transmembranei127 – 145Helical; Name=S1 of repeat IBy similarityAdd BLAST19
Topological domaini146 – 152ExtracellularCurated7
Transmembranei153 – 173Helical; Name=S2 of repeat IBy similarityAdd BLAST21
Topological domaini174 – 187CytoplasmicCuratedAdd BLAST14
Transmembranei188 – 205Helical; Name=S3 of repeat IBy similarityAdd BLAST18
Topological domaini206 – 211ExtracellularCurated6
Transmembranei212 – 228Helical; Name=S4 of repeat IBy similarityAdd BLAST17
Topological domaini229 – 247CytoplasmicCuratedAdd BLAST19
Transmembranei248 – 267Helical; Name=S5 of repeat IBy similarityAdd BLAST20
Topological domaini268 – 346ExtracellularCuratedAdd BLAST79
<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>Intramembranei347 – 371Pore-formingBy similarityAdd BLAST25
Topological domaini372 – 378ExtracellularCurated7
Transmembranei379 – 399Helical; Name=S6 of repeat IBy similarityAdd BLAST21
Topological domaini400 – 744CytoplasmicCuratedAdd BLAST345
Transmembranei745 – 763Helical; Name=S1 of repeat IIBy similarityAdd BLAST19
Topological domaini764 – 774ExtracellularCuratedAdd BLAST11
Transmembranei775 – 794Helical; Name=S2 of repeat IIBy similarityAdd BLAST20
Topological domaini795 – 808CytoplasmicCuratedAdd BLAST14
Transmembranei809 – 828Helical; Name=S3 of repeat IIBy similarityAdd BLAST20
Topological domaini829 – 830ExtracellularCurated2
Transmembranei831 – 848Helical; Name=S4 of repeat IIBy similarityAdd BLAST18
Topological domaini849 – 864CytoplasmicCuratedAdd BLAST16
Transmembranei865 – 883Helical; Name=S5 of repeat IIBy similarityAdd BLAST19
Topological domaini884 – 912ExtracellularCuratedAdd BLAST29
Intramembranei913 – 933Pore-formingBy similarityAdd BLAST21
Topological domaini934 – 946ExtracellularCuratedAdd BLAST13
Transmembranei947 – 967Helical; Name=S6 of repeat IIBy similarityAdd BLAST21
Topological domaini968 – 1193CytoplasmicCuratedAdd BLAST226
Transmembranei1194 – 1211Helical; Name=S1 of repeat IIIBy similarityAdd BLAST18
Topological domaini1212 – 1224ExtracellularCuratedAdd BLAST13
Transmembranei1225 – 1243Helical; Name=S2 of repeat IIIBy similarityAdd BLAST19
Topological domaini1244 – 1257CytoplasmicCuratedAdd BLAST14
Transmembranei1258 – 1276Helical; Name=S3 of repeat IIIBy similarityAdd BLAST19
Topological domaini1277 – 1284ExtracellularCurated8
Transmembranei1285 – 1303Helical; Name=S4 of repeat IIIBy similarityAdd BLAST19
Topological domaini1304 – 1320CytoplasmicCuratedAdd BLAST17
Transmembranei1321 – 1340Helical; Name=S5 of repeat IIIBy similarityAdd BLAST20
Topological domaini1341 – 1392ExtracellularCuratedAdd BLAST52
Intramembranei1393 – 1414Pore-formingBy similarityAdd BLAST22
Topological domaini1415 – 1431ExtracellularCuratedAdd BLAST17
Transmembranei1432 – 1453Helical; Name=S6 of repeat IIIBy similarityAdd BLAST22
Topological domaini1454 – 1516CytoplasmicCuratedAdd BLAST63
Transmembranei1517 – 1534Helical; Name=S1 of repeat IVBy similarityAdd BLAST18
Topological domaini1535 – 1545ExtracellularCuratedAdd BLAST11
Transmembranei1546 – 1564Helical; Name=S2 of repeat IVBy similarityAdd BLAST19
Topological domaini1565 – 1576CytoplasmicCuratedAdd BLAST12
Transmembranei1577 – 1594Helical; Name=S3 of repeat IVBy similarityAdd BLAST18
Topological domaini1595 – 1607ExtracellularCuratedAdd BLAST13
Transmembranei1608 – 1624Helical; Name=S4 of repeat IVBy similarityAdd BLAST17
Topological domaini1625 – 1643CytoplasmicCuratedAdd BLAST19
Transmembranei1644 – 1661Helical; Name=S5 of repeat IVBy similarityAdd BLAST18
Topological domaini1662 – 1683ExtracellularCuratedAdd BLAST22
Intramembranei1684 – 1706Pore-formingBy similarityAdd BLAST23
Topological domaini1707 – 1736ExtracellularCuratedAdd BLAST30
Transmembranei1737 – 1759Helical; Name=S6 of repeat IVBy similarityAdd BLAST23
Topological domaini1760 – 1988CytoplasmicCuratedAdd BLAST229

Keywords - Cellular componenti

Cell membrane, Cell projection, 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

Primary erythermalgia (PERYTHM)11 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAutosomal dominant disease characterized by recurrent episodes of severe pain associated with redness and warmth in the feet or hands.
See also OMIM:133020
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_06459510Q → R in PERYTHM; causes a hyperpolarizing shift of -5.3 mV for the midpoint of activation which is smaller than that seen in other mutations causing early-onset erythromelalgia mutations; also causes a faster rate of activation and slower deactivation compared to wild-type; expression of the mutant protein induced hyperexcitability in dorsal root ganglion neurons but the increase is smaller than that produced by Thr-859. 1 PublicationCorresponds to variant dbSNP:rs267607030EnsemblClinVar.1
Natural variantiVAR_064598216F → S in PERYTHM; hyperpolarizes the voltage dependence of activation by 11 mV, accelerates activation, slows deactivation and enhances the response to slow, small depolarizations. 2 PublicationsCorresponds to variant dbSNP:rs80356469EnsemblClinVar.1
Natural variantiVAR_032014241S → T in PERYTHM. 1 PublicationCorresponds to variant dbSNP:rs80356470EnsemblClinVar.1
Natural variantiVAR_064600395N → K in PERYTHM. 1 PublicationCorresponds to variant dbSNP:rs80356471EnsemblClinVar.1
Natural variantiVAR_064601406E → K in PERYTHM. 1
Natural variantiVAR_019947859I → T in PERYTHM; sporadic; activated at more negative potentials; slower inactivation kinetics than wild-type channels. 4 PublicationsCorresponds to variant dbSNP:rs80356474Ensembl.1
Natural variantiVAR_064609869L → F in PERYTHM; causes a hyperpolarizing shift in channel activation, a depolarizing shift of inactivation and an 18-fold increase in deactivation time compared to wild-type; the mean ramp current amplitude in response to slow depolarization is higher in the mutant channels. 2 PublicationsCorresponds to variant dbSNP:rs80356476Ensembl.1
Natural variantiVAR_019948869L → H in PERYTHM; activated at more negative potentials; slower inactivation kinetics than wild-type channels. 3 PublicationsCorresponds to variant dbSNP:rs80356475Ensembl.1
Natural variantiVAR_0320191460F → V in PERYTHM; produces a hyperpolarizing shift in channel activation and a depolarizing shift in steady-state activation. 1 PublicationCorresponds to variant dbSNP:rs80356478Ensembl.1
Natural variantiVAR_0722801643A → E in PERYTHM and PEPD; hyperpolarizes voltage-dependence of channel activation; depolarizes the voltage-dependence of steady-state fast inactivation; slows channel deactivation; enhances persistent and resurgent current; enhances neuronal hyperexcitability in dorsal root ganglion neurons. 2 PublicationsCorresponds to variant dbSNP:rs879253994Ensembl.1
Natural variantiVAR_0722811643A → T in PERYTHM; no effect on voltage-dependence of channel activation; depolarizes the voltage dependence of steady-state fast inactivation; accelerates channel deactivation; no increase in persistent and resurgent currents; enhances neuronal hyperexcitability in dorsal root ganglion neurons. 1 Publication1
Indifference to pain, congenital, autosomal recessive (CIP)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder characterized by congenital inability to perceive any form of pain, in any part of the body. All other sensory modalities are preserved and the peripheral and central nervous systems are apparently intact. Patients perceive the sensations of touch, warm and cold temperature, proprioception, tickle and pressure, but not painful stimuli. There is no evidence of a motor or sensory neuropathy, either axonal or demyelinating.
See also OMIM:243000
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_064610907R → Q in CIP; significant reduction in membrane localization of the mutant protein compared to the wild-type; complete loss of function of the sodium channel. 1 PublicationCorresponds to variant dbSNP:rs1024152367Ensembl.1
Natural variantiVAR_0646141381 – 1385Missing in CIP; significant reduction in membrane localization of the mutant protein compared to the wild-type; complete loss of function of the sodium channel. 1 Publication5
Paroxysmal extreme pain disorder (PEPD)3 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAutosomal dominant paroxysmal disorder of pain and autonomic dysfunction. The distinctive features are paroxysmal episodes of burning pain in the rectal, ocular, and mandibular areas accompanied by autonomic manifestations such as skin flushing.
See also OMIM:167400
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0320151007R → C in PEPD. 1 PublicationCorresponds to variant dbSNP:rs121908910Ensembl.1
Natural variantiVAR_0320161309V → D in PEPD. 1 PublicationCorresponds to variant dbSNP:rs121908911Ensembl.1
Natural variantiVAR_0320171309V → F in PEPD. 1 PublicationCorresponds to variant dbSNP:rs121908912Ensembl.1
Natural variantiVAR_0320181310V → F in PEPD. 1 PublicationCorresponds to variant dbSNP:rs121908913Ensembl.1
Natural variantiVAR_0320201472I → T in PEPD; reduction in fast inactivation leading to persistent sodium current. 1 PublicationCorresponds to variant dbSNP:rs121908914Ensembl.1
Natural variantiVAR_0320211473F → V in PEPD. 1 Publication1
Natural variantiVAR_0320221475T → I in PEPD; reduction in fast inactivation leading to persistent sodium current. 1 PublicationCorresponds to variant dbSNP:rs121908915Ensembl.1
Natural variantiVAR_0722791623L → P in PEPD; depolarizes the voltage-dependence of channel activation and steady-state fast inactivation; increases ramp current. 1 PublicationCorresponds to variant dbSNP:rs1131691776Ensembl.1
Natural variantiVAR_0320231638M → K in PEPD; reduction in fast inactivation leading to persistent sodium current. 1 Publication1
Natural variantiVAR_0722801643A → E in PERYTHM and PEPD; hyperpolarizes voltage-dependence of channel activation; depolarizes the voltage-dependence of steady-state fast inactivation; slows channel deactivation; enhances persistent and resurgent current; enhances neuronal hyperexcitability in dorsal root ganglion neurons. 2 PublicationsCorresponds to variant dbSNP:rs879253994Ensembl.1
Generalized epilepsy with febrile seizures plus 7 (GEFS+7)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA rare autosomal dominant, familial condition with incomplete penetrance and large intrafamilial variability. Patients display febrile seizures persisting sometimes beyond the age of 6 years and/or a variety of afebrile seizure types. This disease combines febrile seizures, generalized seizures often precipitated by fever at age 6 years or more, and partial seizures, with a variable degree of severity.
See also OMIM:613863
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_064604641N → Y in GEFS+7. 1 PublicationCorresponds to variant dbSNP:rs121908918EnsemblClinVar.1
Natural variantiVAR_064605666K → R in GEFS+7; also found in a patient with severe myoclonic epilepsy in infancy. 1 PublicationCorresponds to variant dbSNP:rs121908919Ensembl.1
Febrile seizures, familial, 3B (FEB3B)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionSeizures associated with febrile episodes in childhood without any evidence of intracranial infection or defined pathologic or traumatic cause. It is a common condition, affecting 2-5% of children aged 3 months to 5 years. The majority are simple febrile seizures (generally defined as generalized onset, single seizures with a duration of less than 30 minutes). Complex febrile seizures are characterized by focal onset, duration greater than 30 minutes, and/or more than one seizure in a 24 hour period. The likelihood of developing epilepsy following simple febrile seizures is low. Complex febrile seizures are associated with a moderately increased incidence of epilepsy.
See also OMIM:613863
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_06459662I → V in FEB3B. 1 PublicationCorresponds to variant dbSNP:rs121908920EnsemblClinVar.1
Natural variantiVAR_064597149P → Q in FEB3B. 1 PublicationCorresponds to variant dbSNP:rs121908921EnsemblClinVar.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi764E → Q: 5-fold less blocked by the spider toxin huwentoxin-IV. 1 Publication1
Mutagenesisi822E → Q: 18-fold less blocked by the spider toxin huwentoxin-IV. 1 Publication1
Mutagenesisi825L → C: 19-fold less blocked by the spider toxin huwentoxin-IV. 1 Publication1
Mutagenesisi827D → A: 13-fold less blocked by the spider toxin huwentoxin-IV. 1 Publication1
Mutagenesisi829E → C: 400-fold less blocked by the spider toxin huwentoxin-IV. 1 Publication1
Mutagenesisi1490S → A: Abolishes stimulation by agents that stimulate PKC activity. 1 Publication1
Mutagenesisi1490S → D or E: Increases current amplitude. 1 Publication1
Mutagenesisi1597D → A: Decrease of the inhibition of fast inactivation produced by the scorpion alpha-toxin CvIV4 on this channel. 1 Publication1
Mutagenesisi1600E → Q: Decrease of the inhibition of fast inactivation produced by the scorpion alpha-toxin CvIV4 on this channel. 1 Publication1
Mutagenesisi1643A → D: Depolarizes the voltage-dependence of steady-state fast inactivation; enhances persistent current. 1 Publication1
Mutagenesisi1643A → K: No effect on voltage-dependence of steady-state fast inactivation. 1 Publication1
Mutagenesisi1643A → V: No effect on voltage-dependence of steady-state fast inactivation. 1 Publication1

Keywords - Diseasei

Disease mutation, Epilepsy

Organism-specific databases

DisGeNET

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DisGeNETi
6335

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

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GeneReviewsi
SCN9A

MalaCards human disease database

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MalaCardsi
SCN9A
MIMi133020 phenotype
167400 phenotype
243000 phenotype
613863 phenotype

Open Targets

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OpenTargetsi
ENSG00000169432

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

More...
Orphaneti
88642 Channelopathy-associated congenital insensitivity to pain
33069 Dravet syndrome
1956 Erythromelalgia
36387 Generalized epilepsy with febrile seizures-plus
970 Hereditary sensory and autonomic neuropathy type 2
46348 Paroxysmal extreme pain disorder
90026 Primary erythromelalgia
306577 Sodium channelopathy-related small fiber neuropathy

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA35010

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL4296

Drug and drug target database

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DrugBanki
DB06218 Lacosamide
DB00281 Lidocaine
DB00243 Ranolazine
DB06201 Rufinamide
DB00313 Valproic Acid
DB00909 Zonisamide

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
584

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
SCN9A

Domain mapping of disease mutations (DMDM)

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DMDMi
327478559

<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_00000485021 – 1988Sodium channel protein type 9 subunit alphaAdd BLAST1988

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>Glycosylationi209N-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 bondi275 ↔ 324By similarity
Glycosylationi283N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi895Interchain; with SCN2B or SCN4BBy similarity
Disulfide bondi895Interchain; 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 bondi935 ↔ 944By similarity
Glycosylationi1352N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1366N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1375N-linked (GlcNAc...) asparagineSequence analysis1
<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 residuei1490Phosphoserine; by PKC1 Publication1

<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-1490 by PKC in a highly conserved cytoplasmic loop increases peak sodium currents.1 Publication
Ubiquitinated by NEDD4L; which may promote its endocytosis. Does not seem to be ubiquitinated by NEDD4.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q15858

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

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PaxDbi
Q15858

PeptideAtlas

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PeptideAtlasi
Q15858

PRoteomics IDEntifications database

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PRIDEi
Q15858

ProteomicsDB human proteome resource

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ProteomicsDBi
60797
60798 [Q15858-2]
60799 [Q15858-3]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q15858

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

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PhosphoSitePlusi
Q15858

<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

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed strongly in dorsal root ganglion, with only minor levels elsewhere in the body, smooth muscle cells, MTC cell line and C-cell carcinoma. Isoform 1 is expressed preferentially in the central and peripheral nervous system. Isoform 2 is expressed preferentially in the dorsal root ganglion.4 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000169432 Expressed in 141 organ(s), highest expression level in dorsal root ganglion

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q15858 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q15858 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB013679
HPA061843

<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

The sodium channel complex consists of a large, channel-forming alpha subunit and 2-3 smaller, ancillary beta subunits (PubMed:7720699, PubMed:17167479, PubMed:25240195). Interacts with NEDD4 and NEDD4L (By similarity). Interacts with the scorpion alpha-toxin CvIV4 (PubMed:21887265). Interacts with the conotoxin GVIIJ (PubMed:24497506). Interacts with the spider toxins huwentoxin-IV and ProTx-II (PubMed:20855463, PubMed:21659528). Interacts with the spider beta/delta-theraphotoxin-Pre1a (PubMed:28428547).By similarity7 Publications

Protein-protein interaction databases

Protein interaction database and analysis system

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IntActi
Q15858, 3 interactors

Molecular INTeraction database

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MINTi
Q15858

STRING: functional protein association networks

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STRINGi
9606.ENSP00000386306

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
Q15858

<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

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
5EK0X-ray3.53A/B/C/D1527-1559[»]
A/B/C/D1581-1622[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
Q15858

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

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SMRi
Q15858

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>Repeati112 – 410ICuratedAdd BLAST299
Repeati726 – 989IICuratedAdd BLAST264
Repeati1180 – 1488IIICuratedAdd BLAST309
Repeati1497 – 1795IVCuratedAdd 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>Domaini1889 – 1918IQAdd BLAST30

<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.Curated

<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

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eggNOGi
KOG2301 Eukaryota
ENOG410XNP6 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000161368

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG053100

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q15858

KEGG Orthology (KO)

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KOi
K04841

Identification of Orthologs from Complete Genome Data

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OMAi
QNVRWKN

Database of Orthologous Groups

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OrthoDBi
56920at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q15858

TreeFam database of animal gene trees

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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

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InterProi
View protein in InterPro
IPR005821 Ion_trans_dom
IPR000048 IQ_motif_EF-hand-BS
IPR001696 Na_channel_asu
IPR010526 Na_trans_assoc
IPR024583 Na_trans_cytopl
IPR028803 SCN9A
IPR027359 Volt_channel_dom_sf

The PANTHER Classification System

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PANTHERi
PTHR10037:SF221 PTHR10037:SF221, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF00520 Ion_trans, 4 hits
PF06512 Na_trans_assoc, 1 hit
PF11933 Na_trans_cytopl, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00170 NACHANNEL

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00015 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>Sequences (4+)i

<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.

This entry describes 4 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 4 described isoforms and 5 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: Q15858-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MAMLPPPGPQ SFVHFTKQSL ALIEQRIAER KSKEPKEEKK DDDEEAPKPS
60 70 80 90 100
SDLEAGKQLP FIYGDIPPGM VSEPLEDLDP YYADKKTFIV LNKGKTIFRF
110 120 130 140 150
NATPALYMLS PFSPLRRISI KILVHSLFSM LIMCTILTNC IFMTMNNPPD
160 170 180 190 200
WTKNVEYTFT GIYTFESLVK ILARGFCVGE FTFLRDPWNW LDFVVIVFAY
210 220 230 240 250
LTEFVNLGNV SALRTFRVLR ALKTISVIPG LKTIVGALIQ SVKKLSDVMI
260 270 280 290 300
LTVFCLSVFA LIGLQLFMGN LKHKCFRNSL ENNETLESIM NTLESEEDFR
310 320 330 340 350
KYFYYLEGSK DALLCGFSTD SGQCPEGYTC VKIGRNPDYG YTSFDTFSWA
360 370 380 390 400
FLALFRLMTQ DYWENLYQQT LRAAGKTYMI FFVVVIFLGS FYLINLILAV
410 420 430 440 450
VAMAYEEQNQ ANIEEAKQKE LEFQQMLDRL KKEQEEAEAI AAAAAEYTSI
460 470 480 490 500
RRSRIMGLSE SSSETSKLSS KSAKERRNRR KKKNQKKLSS GEEKGDAEKL
510 520 530 540 550
SKSESEDSIR RKSFHLGVEG HRRAHEKRLS TPNQSPLSIR GSLFSARRSS
560 570 580 590 600
RTSLFSFKGR GRDIGSETEF ADDEHSIFGD NESRRGSLFV PHRPQERRSS
610 620 630 640 650
NISQASRSPP MLPVNGKMHS AVDCNGVVSL VDGRSALMLP NGQLLPEVII
660 670 680 690 700
DKATSDDSGT TNQIHKKRRC SSYLLSEDML NDPNLRQRAM SRASILTNTV
710 720 730 740 750
EELEESRQKC PPWWYRFAHK FLIWNCSPYW IKFKKCIYFI VMDPFVDLAI
760 770 780 790 800
TICIVLNTLF MAMEHHPMTE EFKNVLAIGN LVFTGIFAAE MVLKLIAMDP
810 820 830 840 850
YEYFQVGWNI FDSLIVTLSL VELFLADVEG LSVLRSFRLL RVFKLAKSWP
860 870 880 890 900
TLNMLIKIIG NSVGALGNLT LVLAIIVFIF AVVGMQLFGK SYKECVCKIN
910 920 930 940 950
DDCTLPRWHM NDFFHSFLIV FRVLCGEWIE TMWDCMEVAG QAMCLIVYMM
960 970 980 990 1000
VMVIGNLVVL NLFLALLLSS FSSDNLTAIE EDPDANNLQI AVTRIKKGIN
1010 1020 1030 1040 1050
YVKQTLREFI LKAFSKKPKI SREIRQAEDL NTKKENYISN HTLAEMSKGH
1060 1070 1080 1090 1100
NFLKEKDKIS GFGSSVDKHL MEDSDGQSFI HNPSLTVTVP IAPGESDLEN
1110 1120 1130 1140 1150
MNAEELSSDS DSEYSKVRLN RSSSSECSTV DNPLPGEGEE AEAEPMNSDE
1160 1170 1180 1190 1200
PEACFTDGCV WRFSCCQVNI ESGKGKIWWN IRKTCYKIVE HSWFESFIVL
1210 1220 1230 1240 1250
MILLSSGALA FEDIYIERKK TIKIILEYAD KIFTYIFILE MLLKWIAYGY
1260 1270 1280 1290 1300
KTYFTNAWCW LDFLIVDVSL VTLVANTLGY SDLGPIKSLR TLRALRPLRA
1310 1320 1330 1340 1350
LSRFEGMRVV VNALIGAIPS IMNVLLVCLI FWLIFSIMGV NLFAGKFYEC
1360 1370 1380 1390 1400
INTTDGSRFP ASQVPNRSEC FALMNVSQNV RWKNLKVNFD NVGLGYLSLL
1410 1420 1430 1440 1450
QVATFKGWTI IMYAAVDSVN VDKQPKYEYS LYMYIYFVVF IIFGSFFTLN
1460 1470 1480 1490 1500
LFIGVIIDNF NQQKKKLGGQ DIFMTEEQKK YYNAMKKLGS KKPQKPIPRP
1510 1520 1530 1540 1550
GNKIQGCIFD LVTNQAFDIS IMVLICLNMV TMMVEKEGQS QHMTEVLYWI
1560 1570 1580 1590 1600
NVVFIILFTG ECVLKLISLR HYYFTVGWNI FDFVVVIISI VGMFLADLIE
1610 1620 1630 1640 1650
TYFVSPTLFR VIRLARIGRI LRLVKGAKGI RTLLFALMMS LPALFNIGLL
1660 1670 1680 1690 1700
LFLVMFIYAI FGMSNFAYVK KEDGINDMFN FETFGNSMIC LFQITTSAGW
1710 1720 1730 1740 1750
DGLLAPILNS KPPDCDPKKV HPGSSVEGDC GNPSVGIFYF VSYIIISFLV
1760 1770 1780 1790 1800
VVNMYIAVIL ENFSVATEES TEPLSEDDFE MFYEVWEKFD PDATQFIEFS
1810 1820 1830 1840 1850
KLSDFAAALD PPLLIAKPNK VQLIAMDLPM VSGDRIHCLD ILFAFTKRVL
1860 1870 1880 1890 1900
GESGEMDSLR SQMEERFMSA NPSKVSYEPI TTTLKRKQED VSATVIQRAY
1910 1920 1930 1940 1950
RRYRLRQNVK NISSIYIKDG DRDDDLLNKK DMAFDNVNEN SSPEKTDATS
1960 1970 1980
STTSPPSYDS VTKPDKEKYE QDRTEKEDKG KDSKESKK
Length:1,988
Mass (Da):226,372
Last modified:April 5, 2011 - v3
<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:i1BAEB8F32EBF5438
GO
Isoform 2 (identifier: Q15858-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     200-229: YLTEFVNLGNVSALRTFRVLRALKTISVIP → YVTEFVDLGNVSALRTFRVLRALKTISVIP

Show »
Length:1,988
Mass (Da):226,359
Checksum:i8C9066AD56148C02
GO
Isoform 3 (identifier: Q15858-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     648-658: Missing.

Show »
Length:1,977
Mass (Da):225,227
Checksum:i8B2BD5CF665F11A8
GO
Isoform 4 (identifier: Q15858-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     200-229: YLTEFVNLGNVSALRTFRVLRALKTISVIP → YVTEFVDLGNVSALRTFRVLRALKTISVIP
     648-658: Missing.

Show »
Length:1,977
Mass (Da):225,214
Checksum:i1701A8F994ADBC06
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 5 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A2R8YDP4A0A2R8YDP4_HUMAN
Sodium channel protein
SCN9A
1,936Annotation score:

Annotation score:2 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>
H7C064H7C064_HUMAN
Sodium channel protein type 9 subun...
SCN9A
378Annotation score:

Annotation score:1 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>
A0A0C4DG82A0A0C4DG82_HUMAN
Sodium channel protein type 9 subun...
SCN9A
832Annotation score:

Annotation score:1 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>
A0A2R8YCX9A0A2R8YCX9_HUMAN
Sodium channel protein type 9 subun...
SCN9A
118Annotation score:

Annotation score:1 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>
A0A2R8Y7G0A0A2R8Y7G0_HUMAN
Sodium channel protein type 9 subun...
SCN9A
194Annotation score:

Annotation score:1 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 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 conflicti267F → S in AAT85834 (PubMed:15302875).Curated1
Sequence conflicti301K → R in AAT85835 (PubMed:15302875).Curated1
Sequence conflicti309S → P in AAT85834 (PubMed:15302875).Curated1
Sequence conflicti420E → G in AAT85834 (PubMed:15302875).Curated1
Sequence conflicti430L → P in AAT85834 (PubMed:15302875).Curated1
Sequence conflicti501S → P in AAT85835 (PubMed:15302875).Curated1
Sequence conflicti610P → T in AAT85835 (PubMed:15302875).Curated1
Sequence conflicti642G → R in AAT85835 (PubMed:15302875).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_06459510Q → R in PERYTHM; causes a hyperpolarizing shift of -5.3 mV for the midpoint of activation which is smaller than that seen in other mutations causing early-onset erythromelalgia mutations; also causes a faster rate of activation and slower deactivation compared to wild-type; expression of the mutant protein induced hyperexcitability in dorsal root ganglion neurons but the increase is smaller than that produced by Thr-859. 1 PublicationCorresponds to variant dbSNP:rs267607030EnsemblClinVar.1
Natural variantiVAR_06459662I → V in FEB3B. 1 PublicationCorresponds to variant dbSNP:rs121908920EnsemblClinVar.1
Natural variantiVAR_064597149P → Q in FEB3B. 1 PublicationCorresponds to variant dbSNP:rs121908921EnsemblClinVar.1
Natural variantiVAR_064598216F → S in PERYTHM; hyperpolarizes the voltage dependence of activation by 11 mV, accelerates activation, slows deactivation and enhances the response to slow, small depolarizations. 2 PublicationsCorresponds to variant dbSNP:rs80356469EnsemblClinVar.1
Natural variantiVAR_064599228I → M1 PublicationCorresponds to variant dbSNP:rs71428908EnsemblClinVar.1
Natural variantiVAR_032014241S → T in PERYTHM. 1 PublicationCorresponds to variant dbSNP:rs80356470EnsemblClinVar.1
Natural variantiVAR_064600395N → K in PERYTHM. 1 PublicationCorresponds to variant dbSNP:rs80356471EnsemblClinVar.1
Natural variantiVAR_064601406E → K in PERYTHM. 1
Natural variantiVAR_064602490S → N1 PublicationCorresponds to variant dbSNP:rs58022607EnsemblClinVar.1
Natural variantiVAR_064603519E → K1 PublicationCorresponds to variant dbSNP:rs187453572EnsemblClinVar.1
Natural variantiVAR_064604641N → Y in GEFS+7. 1 PublicationCorresponds to variant dbSNP:rs121908918EnsemblClinVar.1
Natural variantiVAR_064605666K → R in GEFS+7; also found in a patient with severe myoclonic epilepsy in infancy. 1 PublicationCorresponds to variant dbSNP:rs121908919Ensembl.1
Natural variantiVAR_064606695I → M1 PublicationCorresponds to variant dbSNP:rs199588089Ensembl.1
Natural variantiVAR_064607710C → Y Found in a patient with severe myoclonic epilepsy in infancy. 1 PublicationCorresponds to variant dbSNP:rs201709980Ensembl.1
Natural variantiVAR_064608750I → V1 PublicationCorresponds to variant dbSNP:rs182650126Ensembl.1
Natural variantiVAR_019947859I → T in PERYTHM; sporadic; activated at more negative potentials; slower inactivation kinetics than wild-type channels. 4 PublicationsCorresponds to variant dbSNP:rs80356474Ensembl.1
Natural variantiVAR_064609869L → F in PERYTHM; causes a hyperpolarizing shift in channel activation, a depolarizing shift of inactivation and an 18-fold increase in deactivation time compared to wild-type; the mean ramp current amplitude in response to slow depolarization is higher in the mutant channels. 2 PublicationsCorresponds to variant dbSNP:rs80356476Ensembl.1
Natural variantiVAR_019948869L → H in PERYTHM; activated at more negative potentials; slower inactivation kinetics than wild-type channels. 3 PublicationsCorresponds to variant dbSNP:rs80356475Ensembl.1
Natural variantiVAR_064610907R → Q in CIP; significant reduction in membrane localization of the mutant protein compared to the wild-type; complete loss of function of the sodium channel. 1 PublicationCorresponds to variant dbSNP:rs1024152367Ensembl.1
Natural variantiVAR_030444932M → L. Corresponds to variant dbSNP:rs12478318EnsemblClinVar.1
Natural variantiVAR_055646943M → L. Corresponds to variant dbSNP:rs12478318EnsemblClinVar.1
Natural variantiVAR_0320151007R → C in PEPD. 1 PublicationCorresponds to variant dbSNP:rs121908910Ensembl.1
Natural variantiVAR_0646111134L → F1 PublicationCorresponds to variant dbSNP:rs200160858Ensembl.1
Natural variantiVAR_0199491161W → R3 PublicationsCorresponds to variant dbSNP:rs6746030Ensembl.1
Natural variantiVAR_0646121171E → Q Found in a patient with severe myoclonic epilepsy in infancy. 1 Publication1
Natural variantiVAR_0646131278L → V1 PublicationCorresponds to variant dbSNP:rs180922748Ensembl.1
Natural variantiVAR_0320161309V → D in PEPD. 1 PublicationCorresponds to variant dbSNP:rs121908911Ensembl.1
Natural variantiVAR_0320171309V → F in PEPD. 1 PublicationCorresponds to variant dbSNP:rs121908912Ensembl.1
Natural variantiVAR_0320181310V → F in PEPD. 1 PublicationCorresponds to variant dbSNP:rs121908913Ensembl.1
Natural variantiVAR_0646141381 – 1385Missing in CIP; significant reduction in membrane localization of the mutant protein compared to the wild-type; complete loss of function of the sodium channel. 1 Publication5
Natural variantiVAR_0320191460F → V in PERYTHM; produces a hyperpolarizing shift in channel activation and a depolarizing shift in steady-state activation. 1 PublicationCorresponds to variant dbSNP:rs80356478Ensembl.1
Natural variantiVAR_0320201472I → T in PEPD; reduction in fast inactivation leading to persistent sodium current. 1 PublicationCorresponds to variant dbSNP:rs121908914Ensembl.1
Natural variantiVAR_0320211473F → V in PEPD. 1 Publication1
Natural variantiVAR_0320221475T → I in PEPD; reduction in fast inactivation leading to persistent sodium current. 1 PublicationCorresponds to variant dbSNP:rs121908915Ensembl.1
Natural variantiVAR_0722791623L → P in PEPD; depolarizes the voltage-dependence of channel activation and steady-state fast inactivation; increases ramp current. 1 PublicationCorresponds to variant dbSNP:rs1131691776Ensembl.1
Natural variantiVAR_0320231638M → K in PEPD; reduction in fast inactivation leading to persistent sodium current. 1 Publication1
Natural variantiVAR_0722801643A → E in PERYTHM and PEPD; hyperpolarizes voltage-dependence of channel activation; depolarizes the voltage-dependence of steady-state fast inactivation; slows channel deactivation; enhances persistent and resurgent current; enhances neuronal hyperexcitability in dorsal root ganglion neurons. 2 PublicationsCorresponds to variant dbSNP:rs879253994Ensembl.1
Natural variantiVAR_0722811643A → T in PERYTHM; no effect on voltage-dependence of channel activation; depolarizes the voltage dependence of steady-state fast inactivation; accelerates channel deactivation; no increase in persistent and resurgent currents; enhances neuronal hyperexcitability in dorsal root ganglion neurons. 1 Publication1
Natural variantiVAR_0199501919D → G. Corresponds to variant dbSNP:rs3750904Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_012028200 – 229YLTEF…ISVIP → YVTEFVDLGNVSALRTFRVL RALKTISVIP in isoform 2 and isoform 4. 1 PublicationAdd BLAST30
Alternative sequenceiVSP_012029648 – 658Missing in isoform 3 and isoform 4. 3 PublicationsAdd BLAST11

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
X82835 mRNA Translation: CAA58042.1
DQ857292 mRNA Translation: ABI51981.1
AC074101 Genomic DNA No translation available.
AC107082 Genomic DNA No translation available.
AC108146 Genomic DNA No translation available.
AY682084 mRNA Translation: AAT85833.1
AY682085 mRNA Translation: AAT85834.1
AY682086 mRNA Translation: AAT85835.1
AJ310882 mRNA Translation: CAC84550.1
AJ310883 mRNA Translation: CAC84551.1
AJ310897 mRNA Translation: CAC84537.1
AJ580918 Genomic DNA Translation: CAE45644.1
AJ580919 Genomic DNA Translation: CAE45645.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS46441.1 [Q15858-3]

Protein sequence database of the Protein Information Resource

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PIRi
S54771

NCBI Reference Sequences

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RefSeqi
NP_002968.1, NM_002977.3
XP_005246814.1, XM_005246757.2
XP_011509918.1, XM_011511616.2 [Q15858-1]
XP_011509919.1, XM_011511617.2 [Q15858-2]
XP_011509920.1, XM_011511618.2 [Q15858-4]

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.439145

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000303354; ENSP00000304748; ENSG00000169432 [Q15858-1]
ENST00000409435; ENSP00000386330; ENSG00000169432 [Q15858-2]
ENST00000409672; ENSP00000386306; ENSG00000169432 [Q15858-3]
ENST00000642356; ENSP00000495601; ENSG00000169432 [Q15858-1]
ENST00000645907; ENSP00000495983; ENSG00000169432 [Q15858-4]

Database of genes from NCBI RefSeq genomes

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GeneIDi
6335

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:6335

UCSC genome browser

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UCSCi
uc002udr.2 human [Q15858-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Wikipedia

SCN9A entry

Protein Spotlight

Silent pain - Issue 102 of February 2009

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X82835 mRNA Translation: CAA58042.1
DQ857292 mRNA Translation: ABI51981.1
AC074101 Genomic DNA No translation available.
AC107082 Genomic DNA No translation available.
AC108146 Genomic DNA No translation available.
AY682084 mRNA Translation: AAT85833.1
AY682085 mRNA Translation: AAT85834.1
AY682086 mRNA Translation: AAT85835.1
AJ310882 mRNA Translation: CAC84550.1
AJ310883 mRNA Translation: CAC84551.1
AJ310897 mRNA Translation: CAC84537.1
AJ580918 Genomic DNA Translation: CAE45644.1
AJ580919 Genomic DNA Translation: CAE45645.1
CCDSiCCDS46441.1 [Q15858-3]
PIRiS54771
RefSeqiNP_002968.1, NM_002977.3
XP_005246814.1, XM_005246757.2
XP_011509918.1, XM_011511616.2 [Q15858-1]
XP_011509919.1, XM_011511617.2 [Q15858-2]
XP_011509920.1, XM_011511618.2 [Q15858-4]
UniGeneiHs.439145

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5EK0X-ray3.53A/B/C/D1527-1559[»]
A/B/C/D1581-1622[»]
ProteinModelPortaliQ15858
SMRiQ15858
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ15858, 3 interactors
MINTiQ15858
STRINGi9606.ENSP00000386306

Chemistry databases

BindingDBiQ15858
ChEMBLiCHEMBL4296
DrugBankiDB06218 Lacosamide
DB00281 Lidocaine
DB00243 Ranolazine
DB06201 Rufinamide
DB00313 Valproic Acid
DB00909 Zonisamide
GuidetoPHARMACOLOGYi584

Protein family/group databases

TCDBi1.A.1.10.5 the voltage-gated ion channel (vic) superfamily

PTM databases

iPTMnetiQ15858
PhosphoSitePlusiQ15858

Polymorphism and mutation databases

BioMutaiSCN9A
DMDMi327478559

Proteomic databases

jPOSTiQ15858
PaxDbiQ15858
PeptideAtlasiQ15858
PRIDEiQ15858
ProteomicsDBi60797
60798 [Q15858-2]
60799 [Q15858-3]

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000303354; ENSP00000304748; ENSG00000169432 [Q15858-1]
ENST00000409435; ENSP00000386330; ENSG00000169432 [Q15858-2]
ENST00000409672; ENSP00000386306; ENSG00000169432 [Q15858-3]
ENST00000642356; ENSP00000495601; ENSG00000169432 [Q15858-1]
ENST00000645907; ENSP00000495983; ENSG00000169432 [Q15858-4]
GeneIDi6335
KEGGihsa:6335
UCSCiuc002udr.2 human [Q15858-1]

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
6335
DisGeNETi6335
EuPathDBiHostDB:ENSG00000169432.14

GeneCards: human genes, protein and diseases

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GeneCardsi
SCN9A
GeneReviewsiSCN9A
HGNCiHGNC:10597 SCN9A
HPAiCAB013679
HPA061843
MalaCardsiSCN9A
MIMi133020 phenotype
167400 phenotype
243000 phenotype
603415 gene
613863 phenotype
neXtProtiNX_Q15858
OpenTargetsiENSG00000169432
Orphaneti88642 Channelopathy-associated congenital insensitivity to pain
33069 Dravet syndrome
1956 Erythromelalgia
36387 Generalized epilepsy with febrile seizures-plus
970 Hereditary sensory and autonomic neuropathy type 2
46348 Paroxysmal extreme pain disorder
90026 Primary erythromelalgia
306577 Sodium channelopathy-related small fiber neuropathy
PharmGKBiPA35010

GenAtlas: human gene database

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GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG2301 Eukaryota
ENOG410XNP6 LUCA
GeneTreeiENSGT00940000161368
HOVERGENiHBG053100
InParanoidiQ15858
KOiK04841
OMAiQNVRWKN
OrthoDBi56920at2759
PhylomeDBiQ15858
TreeFamiTF323985

Enzyme and pathway databases

ReactomeiR-HSA-445095 Interaction between L1 and Ankyrins
R-HSA-5576892 Phase 0 - rapid depolarisation
SIGNORiQ15858

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

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ChiTaRSi
SCN9A human

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
Nav1.7

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

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GenomeRNAii
6335

Protein Ontology

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PROi
PR:Q15858

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000169432 Expressed in 141 organ(s), highest expression level in dorsal root ganglion
ExpressionAtlasiQ15858 baseline and differential
GenevisibleiQ15858 HS

Family and domain databases

Gene3Di1.20.120.350, 4 hits
InterProiView protein in InterPro
IPR005821 Ion_trans_dom
IPR000048 IQ_motif_EF-hand-BS
IPR001696 Na_channel_asu
IPR010526 Na_trans_assoc
IPR024583 Na_trans_cytopl
IPR028803 SCN9A
IPR027359 Volt_channel_dom_sf
PANTHERiPTHR10037:SF221 PTHR10037:SF221, 1 hit
PfamiView protein in Pfam
PF00520 Ion_trans, 4 hits
PF06512 Na_trans_assoc, 1 hit
PF11933 Na_trans_cytopl, 1 hit
PRINTSiPR00170 NACHANNEL
SMARTiView protein in SMART
SM00015 IQ, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiSCN9A_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q15858
Secondary accession number(s): A1BUH5
, Q6B4R9, Q6B4S0, Q6B4S1, Q70HX1, Q70HX2, Q8WTU1, Q8WWN4
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 23, 2004
Last sequence update: April 5, 2011
Last modified: February 13, 2019
This is version 178 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  6. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  7. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
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