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Protein

Sodium channel protein type 10 subunit alpha

Gene

SCN10A

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Tetrodotoxin-resistant channel that 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 sodium ions may pass in accordance with their electrochemical gradient. Plays a role in neuropathic pain mechanisms.1 Publication

GO - Molecular functioni

  • ion channel binding Source: BHF-UCL
  • voltage-gated sodium channel activity Source: BHF-UCL

GO - Biological processi

  • AV node cell action potential Source: BHF-UCL
  • bundle of His cell action potential Source: BHF-UCL
  • membrane depolarization during action potential Source: GO_Central
  • neuronal action potential Source: GO_Central
  • odontogenesis of dentin-containing tooth Source: Ensembl
  • regulation of atrial cardiac muscle cell membrane depolarization Source: BHF-UCL
  • regulation of cardiac muscle contraction Source: BHF-UCL
  • regulation of heart rate Source: BHF-UCL
  • regulation of ion transmembrane transport Source: BHF-UCL
  • sensory perception Source: ProtInc
  • sensory perception of pain Source: Ensembl
  • sodium ion transmembrane transport Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Ion channel, Sodium channel, Voltage-gated channel

Keywords - Biological processi

Ion transport, Sodium transport, Transport

Keywords - Ligandi

Sodium

Enzyme and pathway databases

BioCyciZFISH:G66-31820-MONOMER.
ReactomeiR-HSA-445095. Interaction between L1 and Ankyrins.
R-HSA-5576892. Phase 0 - rapid depolarisation.

Names & Taxonomyi

Protein namesi
Recommended name:
Sodium channel protein type 10 subunit alpha
Alternative name(s):
Peripheral nerve sodium channel 3
Short name:
PN3
Short name:
hPN3
Sodium channel protein type X subunit alpha
Voltage-gated sodium channel subunit alpha Nav1.8
Gene namesi
Name:SCN10A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:10582. SCN10A.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 125CytoplasmicSequence analysisAdd BLAST125
Transmembranei126 – 149Helical; Name=S1 of repeat ISequence analysisAdd BLAST24
Topological domaini150 – 154ExtracellularSequence analysis5
Transmembranei155 – 174Helical; Name=S2 of repeat ISequence analysisAdd BLAST20
Topological domaini175 – 187CytoplasmicSequence analysisAdd BLAST13
Transmembranei188 – 206Helical; Name=S3 of repeat ISequence analysisAdd BLAST19
Topological domaini207 – 212ExtracellularSequence analysis6
Transmembranei213 – 232Helical; Voltage-sensor; Name=S4 of repeat ISequence analysisAdd BLAST20
Topological domaini233 – 248CytoplasmicSequence analysisAdd BLAST16
Transmembranei249 – 272Helical; Name=S5 of repeat ISequence analysisAdd BLAST24
Topological domaini273 – 373ExtracellularSequence analysisAdd BLAST101
Transmembranei374 – 399Helical; Name=S6 of repeat ISequence analysisAdd BLAST26
Topological domaini400 – 659CytoplasmicSequence analysisAdd BLAST260
Transmembranei660 – 684Helical; Name=S1 of repeat IISequence analysisAdd BLAST25
Topological domaini685 – 695ExtracellularSequence analysisAdd BLAST11
Transmembranei696 – 719Helical; Name=S2 of repeat IISequence analysisAdd BLAST24
Topological domaini720 – 727CytoplasmicSequence analysis8
Transmembranei728 – 747Helical; Name=S3 of repeat IISequence analysisAdd BLAST20
Topological domaini748 – 753ExtracellularSequence analysis6
Transmembranei754 – 773Helical; Voltage-sensor; Name=S4 of repeat IISequence analysisAdd BLAST20
Topological domaini774 – 789CytoplasmicSequence analysisAdd BLAST16
Transmembranei790 – 810Helical; Name=S5 of repeat IISequence analysisAdd BLAST21
Topological domaini811 – 864ExtracellularSequence analysisAdd BLAST54
Transmembranei865 – 890Helical; Name=S6 of repeat IISequence analysisAdd BLAST26
Topological domaini891 – 1147CytoplasmicSequence analysisAdd BLAST257
Transmembranei1148 – 1171Helical; Name=S1 of repeat IIISequence analysisAdd BLAST24
Topological domaini1172 – 1184ExtracellularSequence analysisAdd BLAST13
Transmembranei1185 – 1210Helical; Name=S2 of repeat IIISequence analysisAdd BLAST26
Topological domaini1211 – 1216CytoplasmicSequence analysis6
Transmembranei1217 – 1238Helical; Name=S3 of repeat IIISequence analysisAdd BLAST22
Topological domaini1239 – 1242ExtracellularSequence analysis4
Transmembranei1243 – 1264Helical; Voltage-sensor; Name=S4 of repeat IIISequence analysisAdd BLAST22
Topological domaini1265 – 1283CytoplasmicSequence analysisAdd BLAST19
Transmembranei1284 – 1311Helical; Name=S5 of repeat IIISequence analysisAdd BLAST28
Topological domaini1312 – 1391ExtracellularSequence analysisAdd BLAST80
Transmembranei1392 – 1418Helical; Name=S6 of repeat IIISequence analysisAdd BLAST27
Topological domaini1419 – 1471CytoplasmicSequence analysisAdd BLAST53
Transmembranei1472 – 1495Helical; Name=S1 of repeat IVSequence analysisAdd BLAST24
Topological domaini1496 – 1506ExtracellularSequence analysisAdd BLAST11
Transmembranei1507 – 1530Helical; Name=S2 of repeat IVSequence analysisAdd BLAST24
Topological domaini1531 – 1536CytoplasmicSequence analysis6
Transmembranei1537 – 1560Helical; Name=S3 of repeat IVSequence analysisAdd BLAST24
Topological domaini1561 – 1572ExtracellularSequence analysisAdd BLAST12
Transmembranei1573 – 1594Helical; Voltage-sensor; Name=S4 of repeat IVSequence analysisAdd BLAST22
Topological domaini1595 – 1609CytoplasmicSequence analysisAdd BLAST15
Transmembranei1610 – 1632Helical; Name=S5 of repeat IVSequence analysisAdd BLAST23
Topological domaini1633 – 1697ExtracellularSequence analysisAdd BLAST65
Transmembranei1698 – 1722Helical; Name=S6 of repeat IVSequence analysisAdd BLAST25
Topological domaini1723 – 1956CytoplasmicSequence analysisAdd BLAST234

GO - Cellular componenti

  • clathrin complex Source: Ensembl
  • extracellular exosome Source: UniProtKB
  • voltage-gated sodium channel complex Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Involvement in diseasei

Episodic pain syndrome, familial, 2 (FEPS2)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal dominant neurologic disorder characterized by adult-onset of paroxysmal pain mainly affecting the distal lower extremities.
See also OMIM:615551
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_070878554L → P in FEPS2; increases the excitability of small DRG neurons. 1 PublicationCorresponds to variant rs138404783dbSNPEnsembl.1
Natural variantiVAR_0708821304A → T in FEPS2; increases the excitability of small DRG neurons. 1 PublicationCorresponds to variant rs142173735dbSNPEnsembl.1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi6336.
MalaCardsiSCN10A.
MIMi615551. phenotype.
OpenTargetsiENSG00000185313.
Orphaneti88642. Channelopathy-associated congenital insensitivity to pain.
46348. Paroxysmal extreme pain disorder.
90026. Primary erythermalgia.
306577. Sodium channelopathy-related small fiber neuropathy.
PharmGKBiPA35000.

Chemistry databases

ChEMBLiCHEMBL5451.
DrugBankiDB01086. Benzocaine.
DB00297. Bupivacaine.
DB01161. Chloroprocaine.
DB00527. Cinchocaine.
DB00907. Cocaine.
DB00645. Dyclonine.
DB00473. Hexylcaine.
DB06218. Lacosamide.
DB01002. Levobupivacaine.
DB00281. Lidocaine.
DB00961. Mepivacaine.
DB01173. Orphenadrine.
DB00892. Oxybuprocaine.
DB00721. Procaine.
DB00807. Proparacaine.
DB00296. Ropivacaine.
DB00313. Valproic Acid.
GuidetoPHARMACOLOGYi585.

Polymorphism and mutation databases

BioMutaiSCN10A.
DMDMi205371821.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000485071 – 1956Sodium channel protein type 10 subunit alphaAdd BLAST1956

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi284N-linked (GlcNAc...)Sequence analysis1
Glycosylationi288N-linked (GlcNAc...)Sequence analysis1
Glycosylationi312N-linked (GlcNAc...)Sequence analysis1
Glycosylationi335N-linked (GlcNAc...)Sequence analysis1
Modified residuei441PhosphoserineBy similarity1
Modified residuei444PhosphoserineBy similarity1
Modified residuei467PhosphoserineBy similarity1
Modified residuei479PhosphoserineBy similarity1
Modified residuei612PhosphoserineBy similarity1
Modified residuei615PhosphoserineBy similarity1
Glycosylationi819N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1312N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1328N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1336N-linked (GlcNAc...)Sequence analysis1
Modified residuei1451Phosphoserine; by PKCBy similarity1
Glycosylationi1686N-linked (GlcNAc...)Sequence analysis1

Post-translational modificationi

Ubiquitinated by NEDD4L; which promotes its endocytosis.By similarity
Phosphorylation at Ser-1451 by PKC in a highly conserved cytoplasmic loop slows inactivation of the sodium channel and reduces peak sodium currents.By similarity

Keywords - PTMi

Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ9Y5Y9.
PeptideAtlasiQ9Y5Y9.
PRIDEiQ9Y5Y9.

PTM databases

iPTMnetiQ9Y5Y9.
PhosphoSitePlusiQ9Y5Y9.

Expressioni

Tissue specificityi

Expressed in the dorsal root ganglia and sciatic nerve.1 Publication

Gene expression databases

BgeeiENSG00000185313.
CleanExiHS_SCN10A.
GenevisibleiQ9Y5Y9. HS.

Interactioni

Subunit structurei

The channel consists of an ion conducting pore forming alpha-subunit regulated by one or more associated auxiliary subunits SCN1B, SCN2B and SCN3B; electrophysiological properties may vary depending on the type of the associated beta subunits. Found in a number of complexes with PRX, DYNLT1 and PDZD2. Interacts with proteins such as FSTL1, PRX, DYNLT1, PDZD2, S100A10 and many others (By similarity). Interacts with NEDD4 and NEDD4L.By similarity

GO - Molecular functioni

  • ion channel binding Source: BHF-UCL

Protein-protein interaction databases

STRINGi9606.ENSP00000390600.

Chemistry databases

BindingDBiQ9Y5Y9.

Structurei

3D structure databases

ProteinModelPortaliQ9Y5Y9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati116 – 405ICuratedAdd BLAST290
Repeati647 – 911IICuratedAdd BLAST265
Repeati1140 – 1449IIICuratedAdd BLAST310
Repeati1458 – 1757IVCuratedAdd BLAST300
Domaini1851 – 1880IQAdd BLAST30

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.

Sequence similaritiesi

Contains 1 IQ domain.Curated

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2301. Eukaryota.
ENOG410XNP6. LUCA.
GeneTreeiENSGT00830000128242.
HOGENOMiHOG000231755.
HOVERGENiHBG053100.
InParanoidiQ9Y5Y9.
KOiK04842.
OMAiMAMEHHG.
OrthoDBiEOG091G00FK.
PhylomeDBiQ9Y5Y9.
TreeFamiTF323985.

Family and domain databases

Gene3Di1.20.120.350. 4 hits.
InterProiIPR027359. Channel_four-helix_dom.
IPR005821. Ion_trans_dom.
IPR028809. Na_channel_a10su.
IPR001696. Na_channel_asu.
IPR010526. Na_trans_assoc.
[Graphical view]
PANTHERiPTHR10037:SF208. PTHR10037:SF208. 3 hits.
PfamiPF00520. Ion_trans. 4 hits.
PF06512. Na_trans_assoc. 1 hit.
[Graphical view]
PRINTSiPR00170. NACHANNEL.

Sequencei

Sequence statusi: Complete.

Q9Y5Y9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEFPIGSLET NNFRRFTPES LVEIEKQIAA KQGTKKAREK HREQKDQEEK
60 70 80 90 100
PRPQLDLKAC NQLPKFYGEL PAELIGEPLE DLDPFYSTHR TFMVLNKGRT
110 120 130 140 150
ISRFSATRAL WLFSPFNLIR RTAIKVSVHS WFSLFITVTI LVNCVCMTRT
160 170 180 190 200
DLPEKIEYVF TVIYTFEALI KILARGFCLN EFTYLRDPWN WLDFSVITLA
210 220 230 240 250
YVGTAIDLRG ISGLRTFRVL RALKTVSVIP GLKVIVGALI HSVKKLADVT
260 270 280 290 300
ILTIFCLSVF ALVGLQLFKG NLKNKCVKND MAVNETTNYS SHRKPDIYIN
310 320 330 340 350
KRGTSDPLLC GNGSDSGHCP DGYICLKTSD NPDFNYTSFD SFAWAFLSLF
360 370 380 390 400
RLMTQDSWER LYQQTLRTSG KIYMIFFVLV IFLGSFYLVN LILAVVTMAY
410 420 430 440 450
EEQNQATTDE IEAKEKKFQE ALEMLRKEQE VLAALGIDTT SLHSHNGSPL
460 470 480 490 500
TSKNASERRH RIKPRVSEGS TEDNKSPRSD PYNQRRMSFL GLASGKRRAS
510 520 530 540 550
HGSVFHFRSP GRDISLPEGV TDDGVFPGDH ESHRGSLLLG GGAGQQGPLP
560 570 580 590 600
RSPLPQPSNP DSRHGEDEHQ PPPTSELAPG AVDVSAFDAG QKKTFLSAEY
610 620 630 640 650
LDEPFRAQRA MSVVSIITSV LEELEESEQK CPPCLTSLSQ KYLIWDCCPM
660 670 680 690 700
WVKLKTILFG LVTDPFAELT ITLCIVVNTI FMAMEHHGMS PTFEAMLQIG
710 720 730 740 750
NIVFTIFFTA EMVFKIIAFD PYYYFQKKWN IFDCIIVTVS LLELGVAKKG
760 770 780 790 800
SLSVLRSFRL LRVFKLAKSW PTLNTLIKII GNSVGALGNL TIILAIIVFV
810 820 830 840 850
FALVGKQLLG ENYRNNRKNI SAPHEDWPRW HMHDFFHSFL IVFRILCGEW
860 870 880 890 900
IENMWACMEV GQKSICLILF LTVMVLGNLV VLNLFIALLL NSFSADNLTA
910 920 930 940 950
PEDDGEVNNL QVALARIQVF GHRTKQALCS FFSRSCPFPQ PKAEPELVVK
960 970 980 990 1000
LPLSSSKAEN HIAANTARGS SGGLQAPRGP RDEHSDFIAN PTVWVSVPIA
1010 1020 1030 1040 1050
EGESDLDDLE DDGGEDAQSF QQEVIPKGQQ EQLQQVERCG DHLTPRSPGT
1060 1070 1080 1090 1100
GTSSEDLAPS LGETWKDESV PQVPAEGVDD TSSSEGSTVD CLDPEEILRK
1110 1120 1130 1140 1150
IPELADDLEE PDDCFTEGCI RHCPCCKLDT TKSPWDVGWQ VRKTCYRIVE
1160 1170 1180 1190 1200
HSWFESFIIF MILLSSGSLA FEDYYLDQKP TVKALLEYTD RVFTFIFVFE
1210 1220 1230 1240 1250
MLLKWVAYGF KKYFTNAWCW LDFLIVNISL ISLTAKILEY SEVAPIKALR
1260 1270 1280 1290 1300
TLRALRPLRA LSRFEGMRVV VDALVGAIPS IMNVLLVCLI FWLIFSIMGV
1310 1320 1330 1340 1350
NLFAGKFWRC INYTDGEFSL VPLSIVNNKS DCKIQNSTGS FFWVNVKVNF
1360 1370 1380 1390 1400
DNVAMGYLAL LQVATFKGWM DIMYAAVDSR EVNMQPKWED NVYMYLYFVI
1410 1420 1430 1440 1450
FIIFGGFFTL NLFVGVIIDN FNQQKKKLGG QDIFMTEEQK KYYNAMKKLG
1460 1470 1480 1490 1500
SKKPQKPIPR PLNKFQGFVF DIVTRQAFDI TIMVLICLNM ITMMVETDDQ
1510 1520 1530 1540 1550
SEEKTKILGK INQFFVAVFT GECVMKMFAL RQYYFTNGWN VFDFIVVVLS
1560 1570 1580 1590 1600
IASLIFSAIL KSLQSYFSPT LFRVIRLARI GRILRLIRAA KGIRTLLFAL
1610 1620 1630 1640 1650
MMSLPALFNI GLLLFLVMFI YSIFGMSSFP HVRWEAGIDD MFNFQTFANS
1660 1670 1680 1690 1700
MLCLFQITTS AGWDGLLSPI LNTGPPYCDP NLPNSNGTRG DCGSPAVGII
1710 1720 1730 1740 1750
FFTTYIIISF LIMVNMYIAV ILENFNVATE ESTEPLSEDD FDMFYETWEK
1760 1770 1780 1790 1800
FDPEATQFIT FSALSDFADT LSGPLRIPKP NRNILIQMDL PLVPGDKIHC
1810 1820 1830 1840 1850
LDILFAFTKN VLGESGELDS LKANMEEKFM ATNLSKSSYE PIATTLRWKQ
1860 1870 1880 1890 1900
EDISATVIQK AYRSYVLHRS MALSNTPCVP RAEEEAASLP DEGFVAFTAN
1910 1920 1930 1940 1950
ENCVLPDKSE TASATSFPPS YESVTRGLSD RVNMRTSSSI QNEDEATSME

LIAPGP
Length:1,956
Mass (Da):220,626
Last modified:September 2, 2008 - v2
Checksum:i4A4A2C5E135B6685
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_020605509S → P.Corresponds to variant rs7630989dbSNPEnsembl.1
Natural variantiVAR_070878554L → P in FEPS2; increases the excitability of small DRG neurons. 1 PublicationCorresponds to variant rs138404783dbSNPEnsembl.1
Natural variantiVAR_048696590G → R.Corresponds to variant rs35332705dbSNPEnsembl.1
Natural variantiVAR_064748916R → W Found in a renal cell carcinoma sample; somatic mutation. 1 PublicationCorresponds to variant rs370208223dbSNPEnsembl.1
Natural variantiVAR_070879939P → L.1 PublicationCorresponds to variant rs202174472dbSNPEnsembl.1
Natural variantiVAR_070880940Q → L.1 Publication1
Natural variantiVAR_0708811056D → N.1 PublicationCorresponds to variant rs751574392dbSNPEnsembl.1
Natural variantiVAR_0206061073V → A.1 PublicationCorresponds to variant rs6795970dbSNPEnsembl.1
Natural variantiVAR_0206071092L → P.Corresponds to variant rs12632942dbSNPEnsembl.1
Natural variantiVAR_0708821304A → T in FEPS2; increases the excitability of small DRG neurons. 1 PublicationCorresponds to variant rs142173735dbSNPEnsembl.1
Natural variantiVAR_0708831523C → Y No gain in function in response to depolarization. 1 PublicationCorresponds to variant rs142217269dbSNPEnsembl.1
Natural variantiVAR_0708841662G → S.1 PublicationCorresponds to variant rs151090729dbSNPEnsembl.1
Natural variantiVAR_0206081713M → V.1 PublicationCorresponds to variant rs6599241dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF117907 mRNA. Translation: AAD30863.1.
AC116038 Genomic DNA. No translation available.
AC137625 Genomic DNA. No translation available.
CCDSiCCDS33736.1.
RefSeqiNP_001280235.2. NM_001293306.2.
NP_001280236.2. NM_001293307.2.
NP_006505.3. NM_006514.3.
UniGeneiHs.250443.

Genome annotation databases

EnsembliENST00000449082; ENSP00000390600; ENSG00000185313.
GeneIDi6336.
KEGGihsa:6336.
UCSCiuc003ciq.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF117907 mRNA. Translation: AAD30863.1.
AC116038 Genomic DNA. No translation available.
AC137625 Genomic DNA. No translation available.
CCDSiCCDS33736.1.
RefSeqiNP_001280235.2. NM_001293306.2.
NP_001280236.2. NM_001293307.2.
NP_006505.3. NM_006514.3.
UniGeneiHs.250443.

3D structure databases

ProteinModelPortaliQ9Y5Y9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000390600.

Chemistry databases

BindingDBiQ9Y5Y9.
ChEMBLiCHEMBL5451.
DrugBankiDB01086. Benzocaine.
DB00297. Bupivacaine.
DB01161. Chloroprocaine.
DB00527. Cinchocaine.
DB00907. Cocaine.
DB00645. Dyclonine.
DB00473. Hexylcaine.
DB06218. Lacosamide.
DB01002. Levobupivacaine.
DB00281. Lidocaine.
DB00961. Mepivacaine.
DB01173. Orphenadrine.
DB00892. Oxybuprocaine.
DB00721. Procaine.
DB00807. Proparacaine.
DB00296. Ropivacaine.
DB00313. Valproic Acid.
GuidetoPHARMACOLOGYi585.

PTM databases

iPTMnetiQ9Y5Y9.
PhosphoSitePlusiQ9Y5Y9.

Polymorphism and mutation databases

BioMutaiSCN10A.
DMDMi205371821.

Proteomic databases

PaxDbiQ9Y5Y9.
PeptideAtlasiQ9Y5Y9.
PRIDEiQ9Y5Y9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000449082; ENSP00000390600; ENSG00000185313.
GeneIDi6336.
KEGGihsa:6336.
UCSCiuc003ciq.4. human.

Organism-specific databases

CTDi6336.
DisGeNETi6336.
GeneCardsiSCN10A.
H-InvDBHIX0030722.
HGNCiHGNC:10582. SCN10A.
MalaCardsiSCN10A.
MIMi604427. gene.
615551. phenotype.
neXtProtiNX_Q9Y5Y9.
OpenTargetsiENSG00000185313.
Orphaneti88642. Channelopathy-associated congenital insensitivity to pain.
46348. Paroxysmal extreme pain disorder.
90026. Primary erythermalgia.
306577. Sodium channelopathy-related small fiber neuropathy.
PharmGKBiPA35000.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2301. Eukaryota.
ENOG410XNP6. LUCA.
GeneTreeiENSGT00830000128242.
HOGENOMiHOG000231755.
HOVERGENiHBG053100.
InParanoidiQ9Y5Y9.
KOiK04842.
OMAiMAMEHHG.
OrthoDBiEOG091G00FK.
PhylomeDBiQ9Y5Y9.
TreeFamiTF323985.

Enzyme and pathway databases

BioCyciZFISH:G66-31820-MONOMER.
ReactomeiR-HSA-445095. Interaction between L1 and Ankyrins.
R-HSA-5576892. Phase 0 - rapid depolarisation.

Miscellaneous databases

GeneWikiiSCN10A.
GenomeRNAii6336.
PROiQ9Y5Y9.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000185313.
CleanExiHS_SCN10A.
GenevisibleiQ9Y5Y9. HS.

Family and domain databases

Gene3Di1.20.120.350. 4 hits.
InterProiIPR027359. Channel_four-helix_dom.
IPR005821. Ion_trans_dom.
IPR028809. Na_channel_a10su.
IPR001696. Na_channel_asu.
IPR010526. Na_trans_assoc.
[Graphical view]
PANTHERiPTHR10037:SF208. PTHR10037:SF208. 3 hits.
PfamiPF00520. Ion_trans. 4 hits.
PF06512. Na_trans_assoc. 1 hit.
[Graphical view]
PRINTSiPR00170. NACHANNEL.
ProtoNetiSearch...

Entry informationi

Entry nameiSCNAA_HUMAN
AccessioniPrimary (citable) accession number: Q9Y5Y9
Secondary accession number(s): A6NDQ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 21, 2004
Last sequence update: September 2, 2008
Last modified: November 2, 2016
This is version 136 of the entry and version 2 of the sequence. [Complete history]
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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.