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Reviewed, UniProtKB/Swiss-Prot Q15858 (SCN9A_HUMAN)

Last modified May 26, 2009. Version 82. Feed History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Sodium channel protein type 9 subunit alpha
Alternative name(s):
    Sodium channel protein type IX subunit alpha
    Voltage-gated sodium channel subunit alpha Nav1.7
    Neuroendocrine sodium channel
      Short name=hNE-Na
    Peripheral sodium channel 1
Gene names
Name: SCN9A
Synonyms: NENA, PN1
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1988 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Mediates the voltage-dependent sodium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium-selective channel through which Na+ ions may pass in accordance with their electrochemical gradient. It is a tetrodotoxin-sensitive Na+ channel isoform. Plays a role in pain mechanisms, especially in the development of inflammatory pain By similarity.

Subunit structure

The sodium channel consists of a large polypeptide and 2-3 smaller ones. This sequence represents a large polypeptide. Interacts with NEDD4 and NEDD4L By similarity.

Subcellular location

Membrane; Multi-pass membrane protein. Note: In neurite terminals By similarity.

Tissue specificity

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 while isoform 2 is expressed preferentially in the dorsal root ganglion. Ref.1 Ref.3 Ref.6 Ref.7

Domain

The sequence contains 4 internal repeats, each with 5 hydrophobic segments (S1,S2,S3,S5,S6) and one positively charged segment (S4). Segments S4 are probably the voltage-sensors and are characterized by a series of positively charged amino acids at every third position.

Post-translational modification

Ubiquitinated by NEDD4L; which may promote its endocytosis. Does not seem to be ubiquitinated by NEDD4 By similarity.

Involvement in disease

Defects in SCN9A are the cause of primary erythermalgia [MIM:133020]. It is an autosomal dominant disease characterized by recurrent episodes of severe pain associated with redness and warmth in the feet or hands. Ref.5 Ref.9 Ref.10 Ref.11 Ref.13

Defects in SCN9A are the cause of autosomal recessive congenital indifference to pain [MIM:243000]; also known as channelopathy-associated insensitivity to pain. Affected individuals have a 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.

Defects in SCN9A are a cause of paroxysmal extreme pain disorder (PEPD) [MIM:167400]; previously known as familial rectal pain (FRP). PEPD is an autosomal 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. Ref.12

Sequence similarities

Belongs to the sodium channel family.

Contains 1 IQ domain.

Ontologies

Keywords
   Biological processIon transport
Sodium transport
Transport
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   DomainRepeat
Transmembrane
   LigandSodium
   Molecular functionIonic channel
Sodium channel
Voltage-gated channel
   PTMGlycoprotein
Phosphoprotein
Ubl conjugation
Gene Ontology (GO)
   Biological processsodium ion transport Ref.1

Traceable author statement. Source: ProtInc

   Cellular componentvoltage-gated sodium channel complex

Inferred from electronic annotation. Source: InterPro

   Molecular functionsodium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

voltage-gated sodium channel activity Ref.1

Traceable author statement. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q15858-1)

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.
Isoform 2 (identifier: Q15858-2)

The sequence of this isoform differs from the canonical sequence as follows:
     200-229: YLTEFVNLGNVSALRTFRVLRALKTISVIP → YVTEFVDLGNVSALRTFRVLRALKTISVIP
Isoform 3 (identifier: Q15858-3)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 19881988Sodium channel protein type 9 subunit alpha
PRO_0000048502

Regions

Transmembrane122 – 14524S1 of repeat I By similarity
Transmembrane154 – 17320S2 of repeat I By similarity
Transmembrane187 – 20519S3 of repeat I By similarity
Transmembrane212 – 23120S4 of repeat I By similarity
Transmembrane248 – 27124S5 of repeat I By similarity
Transmembrane379 – 40426S6 of repeat I By similarity
Transmembrane739 – 76325S1 of repeat II By similarity
Transmembrane775 – 79824S2 of repeat II By similarity
Transmembrane807 – 82620S3 of repeat II By similarity
Transmembrane833 – 85220S4 of repeat II By similarity
Transmembrane869 – 88921S5 of repeat II By similarity
Transmembrane943 – 96826S6 of repeat II By similarity
Transmembrane1188 – 121124S1 of repeat III By similarity
Transmembrane1225 – 125026S2 of repeat III By similarity
Transmembrane1257 – 127822S3 of repeat III By similarity
Transmembrane1283 – 130422S4 of repeat III By similarity
Transmembrane1324 – 135128S5 of repeat III By similarity
Transmembrane1431 – 145727S6 of repeat III By similarity
Transmembrane1511 – 153424S1 of repeat IV By similarity
Transmembrane1546 – 156924S2 of repeat IV By similarity
Transmembrane1576 – 159924S3 of repeat IV By similarity
Transmembrane1610 – 163122S4 of repeat IV By similarity
Transmembrane1647 – 166923S5 of repeat IV By similarity
Transmembrane1736 – 176025S6 of repeat IV By similarity
Repeat121 – 405285I
Repeat738 – 969232II
Repeat1187 – 1458272III
Repeat1510 – 1761252IV
Domain1889 – 191830IQ

Amino acid modifications

Modified residue14131Phosphotyrosine Ref.8
Modified residue14181Phosphoserine Ref.8
Glycosylation2091N-linked (GlcNAc...) Potential
Glycosylation2831N-linked (GlcNAc...) Potential
Glycosylation13521N-linked (GlcNAc...) Potential
Glycosylation13661N-linked (GlcNAc...) Potential
Glycosylation13751N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence200 – 22930YLTEF…ISVIP → YVTEFVDLGNVSALRTFRVL RALKTISVIP in isoform 2.
VSP_012028
Alternative sequence648 – 65811Missing in isoform 3.
VSP_012029
Natural variant2411S → T in primary erythermalgia. Ref.10
VAR_032014
Natural variant8591I → T in primary erythermalgia; sporadic; activated at more negative potentials; slower inactivation kinetics than wild-type channels. Ref.5 Ref.9
VAR_019947
Natural variant8691L → H in primary erythermalgia; activated at more negative potentials; slower inactivation kinetics than wild-type channels. Ref.5 Ref.9 Ref.13
VAR_019948
Natural variant9321M → L: dbSNP rs12478318.
VAR_030444
Natural variant9431M → L: dbSNP rs12478318.
VAR_055646
Natural variant10071R → C in PEPD. Ref.12
VAR_032015
Natural variant11611R → W: dbSNP rs6746030.
VAR_019949
Natural variant13091V → D in PEPD. Ref.12
VAR_032016
Natural variant13091V → F in PEPD. Ref.12
VAR_032017
Natural variant13101V → F in PEPD. Ref.12
VAR_032018
Natural variant14601F → V in primary erythermalgia; produces a hyperpolarizing shift in channel activation and a depolarizing shift in steady-state activation. Ref.11
VAR_032019
Natural variant14721I → T in PEPD; reduction in fast inactivation leading to persistent sodium current. Ref.12
VAR_032020
Natural variant14731F → V in PEPD. Ref.12
VAR_032021
Natural variant14751T → I in PEPD; reduction in fast inactivation leading to persistent sodium current. Ref.12
VAR_032022
Natural variant16381M → K in PEPD; reduction in fast inactivation leading to persistent sodium current. Ref.12
VAR_032023
Natural variant19191D → G: dbSNP rs3750904.
VAR_019950

Experimental info

Sequence conflict2011L → V in AAT85835. Ref.3
Sequence conflict2011L → V in AAT85833. Ref.3
Sequence conflict2061N → D in AAT85835. Ref.3
Sequence conflict2061N → D in AAT85833. Ref.3
Sequence conflict2671F → S in AAT85834. Ref.3
Sequence conflict3011K → R in AAT85835. Ref.3
Sequence conflict3091S → P in AAT85834. Ref.3
Sequence conflict4201E → G in AAT85834. Ref.3
Sequence conflict4301L → P in AAT85834. Ref.3
Sequence conflict5011S → P in AAT85835. Ref.3
Sequence conflict6101P → T in AAT85835. Ref.3
Sequence conflict6421G → R in AAT85835. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 23, 2004. Version 2.
Checksum: 875311807A5C506B

FASTA1,988226,342
        10         20         30         40         50         60 
MAMLPPPGPQ SFVHFTKQSL ALIEQRIAER KSKEPKEEKK DDDEEAPKPS SDLEAGKQLP 

        70         80         90        100        110        120 
FIYGDIPPGM VSEPLEDLDP YYADKKTFIV LNKGKTIFRF NATPALYMLS PFSPLRRISI 

       130        140        150        160        170        180 
KILVHSLFSM LIMCTILTNC IFMTMNNPPD WTKNVEYTFT GIYTFESLVK ILARGFCVGE 

       190        200        210        220        230        240 
FTFLRDPWNW LDFVVIVFAY LTEFVNLGNV SALRTFRVLR ALKTISVIPG LKTIVGALIQ 

       250        260        270        280        290        300 
SVKKLSDVMI LTVFCLSVFA LIGLQLFMGN LKHKCFRNSL ENNETLESIM NTLESEEDFR 

       310        320        330        340        350        360 
KYFYYLEGSK DALLCGFSTD SGQCPEGYTC VKIGRNPDYG YTSFDTFSWA FLALFRLMTQ 

       370        380        390        400        410        420 
DYWENLYQQT LRAAGKTYMI FFVVVIFLGS FYLINLILAV VAMAYEEQNQ ANIEEAKQKE 

       430        440        450        460        470        480 
LEFQQMLDRL KKEQEEAEAI AAAAAEYTSI RRSRIMGLSE SSSETSKLSS KSAKERRNRR 

       490        500        510        520        530        540 
KKKNQKKLSS GEEKGDAEKL SKSESEDSIR RKSFHLGVEG HRRAHEKRLS TPNQSPLSIR 

       550        560        570        580        590        600 
GSLFSARRSS RTSLFSFKGR GRDIGSETEF ADDEHSIFGD NESRRGSLFV PHRPQERRSS 

       610        620        630        640        650        660 
NISQASRSPP MLPVNGKMHS AVDCNGVVSL VDGRSALMLP NGQLLPEVII DKATSDDSGT 

       670        680        690        700        710        720 
TNQIHKKRRC SSYLLSEDML NDPNLRQRAM SRASILTNTV EELEESRQKC PPWWYRFAHK 

       730        740        750        760        770        780 
FLIWNCSPYW IKFKKCIYFI VMDPFVDLAI TICIVLNTLF MAMEHHPMTE EFKNVLAIGN 

       790        800        810        820        830        840 
LVFTGIFAAE MVLKLIAMDP YEYFQVGWNI FDSLIVTLSL VELFLADVEG LSVLRSFRLL 

       850        860        870        880        890        900 
RVFKLAKSWP TLNMLIKIIG NSVGALGNLT LVLAIIVFIF AVVGMQLFGK SYKECVCKIN 

       910        920        930        940        950        960 
DDCTLPRWHM NDFFHSFLIV FRVLCGEWIE TMWDCMEVAG QAMCLIVYMM VMVIGNLVVL 

       970        980        990       1000       1010       1020 
NLFLALLLSS FSSDNLTAIE EDPDANNLQI AVTRIKKGIN YVKQTLREFI LKAFSKKPKI 

      1030       1040       1050       1060       1070       1080 
SREIRQAEDL NTKKENYISN HTLAEMSKGH NFLKEKDKIS GFGSSVDKHL MEDSDGQSFI 

      1090       1100       1110       1120       1130       1140 
HNPSLTVTVP IAPGESDLEN MNAEELSSDS DSEYSKVRLN RSSSSECSTV DNPLPGEGEE 

      1150       1160       1170       1180       1190       1200 
AEAEPMNSDE PEACFTDGCV RRFSCCQVNI ESGKGKIWWN IRKTCYKIVE HSWFESFIVL 

      1210       1220       1230       1240       1250       1260 
MILLSSGALA FEDIYIERKK TIKIILEYAD KIFTYIFILE MLLKWIAYGY KTYFTNAWCW 

      1270       1280       1290       1300       1310       1320 
LDFLIVDVSL VTLVANTLGY SDLGPIKSLR TLRALRPLRA LSRFEGMRVV VNALIGAIPS 

      1330       1340       1350       1360       1370       1380 
IMNVLLVCLI FWLIFSIMGV NLFAGKFYEC INTTDGSRFP ASQVPNRSEC FALMNVSQNV 

      1390       1400       1410       1420       1430       1440 
RWKNLKVNFD NVGLGYLSLL QVATFKGWTI IMYAAVDSVN VDKQPKYEYS LYMYIYFVVF 

      1450       1460       1470       1480       1490       1500 
IIFGSFFTLN LFIGVIIDNF NQQKKKLGGQ DIFMTEEQKK YYNAMKKLGS KKPQKPIPRP 

      1510       1520       1530       1540       1550       1560 
GNKIQGCIFD LVTNQAFDIS IMVLICLNMV TMMVEKEGQS QHMTEVLYWI NVVFIILFTG 

      1570       1580       1590       1600       1610       1620 
ECVLKLISLR HYYFTVGWNI FDFVVVIISI VGMFLADLIE TYFVSPTLFR VIRLARIGRI 

      1630       1640       1650       1660       1670       1680 
LRLVKGAKGI RTLLFALMMS LPALFNIGLL LFLVMFIYAI FGMSNFAYVK KEDGINDMFN 

      1690       1700       1710       1720       1730       1740 
FETFGNSMIC LFQITTSAGW DGLLAPILNS KPPDCDPKKV HPGSSVEGDC GNPSVGIFYF 

      1750       1760       1770       1780       1790       1800 
VSYIIISFLV VVNMYIAVIL ENFSVATEES TEPLSEDDFE MFYEVWEKFD PDATQFIEFS 

      1810       1820       1830       1840       1850       1860 
KLSDFAAALD PPLLIAKPNK VQLIAMDLPM VSGDRIHCLD ILFAFTKRVL GESGEMDSLR 

      1870       1880       1890       1900       1910       1920 
SQMEERFMSA NPSKVSYEPI TTTLKRKQED VSATVIQRAY RRYRLRQNVK NISSIYIKDG 

      1930       1940       1950       1960       1970       1980 
DRDDDLLNKK DMAFDNVNEN SSPEKTDATS STTSPPSYDS VTKPDKEKYE QDRTEKEDKG 


KDSKESKK 

« Hide

Isoform 2.

Checksum: 106DCFDE02F78851
Show »

FASTA1,988226,329
Isoform 3.

Checksum: 17D67CBC32BC15FB
Show »

FASTA1,977225,197

References

« Hide 'large scale' references
[1]"Structure and functional expression of a new member of the tetrodotoxin-sensitive voltage-activated sodium channel family from human neuroendocrine cells."
Klugbauer N., Lacinova L., Flockerzi V., Hofmann F.
EMBO J. 14:1084-1090(1995) [PubMed: 7720699] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION IN VOLTAGE-EVOKED DEPOLARIZATION, TISSUE SPECIFICITY.
Tissue: Thyroid.
[2]"An SCN9A channelopathy causes congenital inability to experience pain."
Cox J.J., Reimann F., Nicholas A.K., Thornton G., Roberts E., Springell K., Karbani G., Jafri H., Mannan J., Raashid Y., Al-Gazali L., Hamamy H., Valente E.M., Gorman S., Williams R., McHale D.P., Wood J.N., Gribble F.M., Woods C.G.
Nature 444:894-898(2006) [PubMed: 17167479] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), INVOLVEMENT IN CONGENITAL INSENSITIVITY TO PAIN, CHARACTERIZATION.
[3]"Expression of alternatively spliced sodium channel alpha-subunit genes: unique splicing patterns are observed in dorsal root ganglia."
Raymond C.K., Castle J.C., Garrett-Engele P.W., Armour C.D., Kan Z.G., Tsinoremas N.T., Johnson J.M.
J. Biol. Chem. 279:46234-46241(2004) [PubMed: 15302875] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 136-674 (ISOFORMS 1; 2 AND 3), TISSUE SPECIFICITY.
Tissue: Spinal ganglion.
[4]"Upregulation of voltage-gated Na+ channel expression and metastatic potential in human breast cancer: correlative studies on cell lines and biopsy tissues."
Diss J.K.J., Fraser S.P., Coombes R.C., Djamgoz M.B.A.
Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 150-264 AND 1340-1400.
[5]"Mutations in SCN9A, encoding a sodium channel alpha subunit, in patients with primary erythermalgia."
Yang Y., Wang Y., Li S., Xu Z., Li H., Ma L., Fan J., Bu D., Liu B., Fan Z., Wu G., Jin J., Ding B., Zhu X., Shen Y.
J. Med. Genet. 41:171-174(2004) [PubMed: 14985375] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 840-958, VARIANTS PRIMARY ERYTHERMALGIA THR-859 AND HIS-869.
[6]"A novel tetrodotoxin-sensitive, voltage-gated sodium channel expressed in rat and human dorsal root ganglia."
Sangameswaran L., Fish L.M., Koch B.D., Rabert D.K., Delgado S.G., Ilnicka M., Jakeman L.B., Novakovic S., Wong K., Sze P., Tzoumaka E., Stewart G.R., Herman R.C., Chan H., Eglen R.M., Hunter J.C.
J. Biol. Chem. 272:14805-14809(1997) [PubMed: 9169448] [Abstract]
Cited for: TISSUE SPECIFICITY.
[7]"Voltage-gated sodium channel expressed in cultured human smooth muscle cells: involvement of SCN9A."
Jo T., Nagata T., Iida H., Imuta H., Iwasawa K., Ma J., Hara K., Omata M., Nagai R., Takizawa H., Nagase T., Nakajima T.
FEBS Lett. 567:339-343(2004) [PubMed: 15178348] [Abstract]
Cited for: FUNCTION IN VOLTAGE-EVOKED DEPOLARIZATION, TISSUE SPECIFICITY.
[8]"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1413 AND SER-1418, MASS SPECTROMETRY.
Tissue: Epithelium.
[9]"Electrophysiological properties of mutant Nav1.7 sodium channels in a painful inherited neuropathy."
Cummins T.R., Dib-Hajj S.D., Waxman S.G.
J. Neurosci. 24:8232-8236(2004) [PubMed: 15385606] [Abstract]
Cited for: CHARACTERIZATION OF VARIANTS PRIMARY ERYTHERMALGIA THR-859 AND HIS-869.
[10]"Autosomal dominant erythermalgia associated with a novel mutation in the voltage-gated sodium channel alpha subunit Nav1.7."
Michiels J.J., te Morsche R.H.M., Jansen J.B.M.J., Drenth J.P.H.
Arch. Neurol. 62:1587-1590(2005) [PubMed: 16216943] [Abstract]
Cited for: VARIANT PRIMARY ERYTHERMALGIA THR-241.
[11]"Gain-of-function mutation in Nav1.7 in familial erythromelalgia induces bursting of sensory neurons."
Dib-Hajj S.D., Rush A.M., Cummins T.R., Hisama F.M., Novella S., Tyrrell L., Marshall L., Waxman S.G.
Brain 128:1847-1854(2005) [PubMed: 15958509] [Abstract]
Cited for: VARIANT PRIMARY ERYTHERMALGIA VAL-1460, CHARACTERIZATION OF VARIANT PRIMARY ERYTHERMALGIA VAL-1460.
[12]"SCN9A mutations in paroxysmal extreme pain disorder: allelic variants underlie distinct channel defects and phenotypes."
Fertleman C.R., Baker M.D., Parker K.A., Moffatt S., Elmslie F.V., Abrahamsen B., Ostman J., Klugbauer N., Wood J.N., Gardiner R.M., Rees M.
Neuron 52:767-774(2006) [PubMed: 17145499] [Abstract]
Cited for: VARIANTS PEPD CYS-1007; PHE-1309; ASP-1309; PHE-1310; THR-1472; VAL-1473; ILE-1475 AND LYS-1638, CHARACTERIZATION OF VARIANTS PEPD THR-1472; ILE-1475 AND LYS-1638.
[13]"A single sodium channel mutation produces hyper- or hypoexcitability in different types of neurons."
Rush A.M., Dib-Hajj S.D., Liu S., Cummins T.R., Black J.A., Waxman S.G.
Proc. Natl. Acad. Sci. U.S.A. 103:8245-8250(2006) [PubMed: 16702558] [Abstract]
Cited for: CHARACTERIZATION OF VARIANT PRIMARY ERYTHERMALGIA HIS-869.
+Additional computationally mapped references.

Web resources

GeneReviews
Wikipedia

SCN9A entry

Protein Spotlight

Silent pain - Issue 102 of February 2009

Cross-references

Sequence databases

X82835 mRNA. Translation: CAA58042.1.
DQ857292 mRNA. Translation: ABI51981.1.
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.
IPIIPI00154944.
IPI00479414.
IPI00745570.
PIRS54771.
RefSeqNP_002968.1.
UniGeneHs.439145

3D structure databases

HSSPHSSP built from PDB template 1BYY based on UniProtKB P04775.
ModBaseSearch...

Protein family/group databases

TCDB1.A.1.10.5. voltage-gated ion channel (VIC) superfamily.

Proteomic databases

PRIDEQ15858.

Genome annotation databases

EnsemblENSG00000169432. Homo sapiens. [Contig view]
GeneID6335.
KEGGhsa:6335.

Organism-specific databases

GeneCardsGC02M166763.
H-InvDBHIX0029861.
HGNCHGNC:10597. SCN9A.
HPACAB013679.
MIM133020. phenotype.
167400. phenotype.
243000. phenotype.
603415. gene.
Orphanet88642. Congenital indifference to pain.
1956. Erythromelalgia.
46348. Paroxysmal extreme pain disorder.
90026. Primary erythermalgia.
PharmGKBPA35010.
GenAtlasSearch...

Phylogenomic databases

HOVERGENQ15858.

Gene expression databases

ArrayExpressQ15858.
BgeeQ15858.
CleanExHS_SCN9A.
GermOnlineENSG00000169432. Homo sapiens.

Family and domain databases

InterProIPR005821. Ion_trans.
IPR000048. IQ_CaM_bd_region.
IPR001696. Na_channel.
IPR010526. Na_trans_assoc.
[Graphical view]
PfamPF00520. Ion_trans. 4 hits.
PF00612. IQ. 1 hit.
PF06512. Na_trans_assoc. 1 hit.
[Graphical view]
PRINTSPR00170. NACHANNEL.
SMARTSM00015. IQ. 1 hit.
[Graphical view]
PROSITEPS50096. IQ. False negative.
[Graphical view]
ProtoNetSearch...

Other Resources

DrugBankDB00555. Lamotrigine.
DB00281. Lidocaine.
NextBio24600.
SOURCESearch...

Entry information

Entry nameSCN9A_HUMAN
AccessionPrimary (citable) accession number: Q15858
Secondary accession number(s): A1BUH5 expand/collapse secondary AC list , Q6B4R9, Q6B4S0, Q6B4S1, Q70HX1, Q70HX2, Q8WTU1, Q8WWN4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 23, 2004
Last sequence update: November 23, 2004
Last modified: May 26, 2009
This is version 82 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents