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Q9UQD0

- SCN8A_HUMAN

UniProt

Q9UQD0 - SCN8A_HUMAN

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Protein

Sodium channel protein type 8 subunit alpha

Gene

SCN8A

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

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. In macrophages and melanoma cells, isoform 5 may participate in the control of podosome and invadopodia formation.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi893 – 9008ATPSequence Analysis

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. voltage-gated sodium channel activity Source: UniProtKB

GO - Biological processi

  1. adult walking behavior Source: Ensembl
  2. axon guidance Source: Reactome
  3. membrane depolarization during action potential Source: RefGenome
  4. muscle organ development Source: Ensembl
  5. myelination Source: BHF-UCL
  6. nervous system development Source: ProtInc
  7. neuromuscular process Source: Ensembl
  8. neuronal action potential Source: RefGenome
  9. peripheral nervous system development Source: BHF-UCL
  10. response to toxic substance Source: Ensembl
  11. sensory perception of sound Source: Ensembl
  12. sodium ion transmembrane transport Source: GOC
  13. sodium ion transport Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Ion channel, Sodium channel, Voltage-gated channel

Keywords - Biological processi

Ion transport, Sodium transport, Transport

Keywords - Ligandi

ATP-binding, Nucleotide-binding, Sodium

Enzyme and pathway databases

ReactomeiREACT_22266. Interaction between L1 and Ankyrins.

Protein family/group databases

TCDBi1.A.1.10.8. the voltage-gated ion channel (vic) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
Sodium channel protein type 8 subunit alpha
Alternative name(s):
Sodium channel protein type VIII subunit alpha
Voltage-gated sodium channel subunit alpha Nav1.6
Gene namesi
Name:SCN8A
Synonyms:MED
OrganismiHomo sapiens (Human)Imported
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:10596. SCN8A.

Subcellular locationi

Membrane 1 Publication; Multi-pass membrane protein 1 Publication
Isoform 5 : Cytoplasmic vesicle
Note: Some vesicles are localized adjacent to melanoma invadopodia and macrophage podosomes. Does not localize to the plasma membrane.

GO - Cellular componenti

  1. axon initial segment Source: BHF-UCL
  2. cytoplasmic vesicle Source: UniProtKB-KW
  3. dendrite Source: Ensembl
  4. integral component of membrane Source: ProtInc
  5. neuronal cell body Source: Ensembl
  6. node of Ranvier Source: BHF-UCL
  7. plasma membrane Source: RefGenome
  8. voltage-gated sodium channel complex Source: UniProtKB
  9. Z disc Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle, Membrane

Pathology & Biotechi

Involvement in diseasei

Cognitive impairment with or without cerebellar ataxia (CIAT) [MIM:614306]: A disorder characterized by markedly delayed cognitive and motor development, attention deficit disorder, and cerebellar ataxia. Features include bilateral esophoria, strabismatic amblyopia, unsustained gaze evoked nystagmus on horizontal gaze, ataxic gait, dysmetria in the upper limbs and dysarthria, with normal strength, tone, and reflexes.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Epileptic encephalopathy, early infantile, 13 (EIEE13) [MIM:614558]: A form of epilepsy characterized by frequent tonic seizures or spasms beginning in infancy with a specific EEG finding of suppression-burst patterns, characterized by high-voltage bursts alternating with almost flat suppression phases. Patients may progress to West syndrome, which is characterized by tonic spasms with clustering, arrest of psychomotor development, and hypsarrhythmia on EEG. EIEE13 is a severe form consisting of early-onset seizures, features of autism, intellectual disability, ataxia, and sudden unexplained death in epilepsy.3 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti216 – 2161V → D in EIEE13. 1 Publication
VAR_071674
Natural varianti846 – 8461F → S in EIEE13. 1 Publication
VAR_071675
Natural varianti1327 – 13271I → V in EIEE13. 1 Publication
VAR_071676
Natural varianti1466 – 14661N → K in EIEE13. 1 Publication
VAR_071677
Natural varianti1466 – 14661N → T in EIEE13. 1 Publication
VAR_071678
Natural varianti1617 – 16171R → Q in EIEE13. 1 Publication
VAR_071679
Natural varianti1650 – 16501A → T in EIEE13. 1 Publication
VAR_071680
Natural varianti1768 – 17681N → D in EIEE13; gain-of-function mutation; results in increased persistent sodium currents and incomplete channel inactivation. 1 Publication
VAR_067539
Natural varianti1872 – 18721R → W in EIEE13. 1 Publication
VAR_071681

Keywords - Diseasei

Disease mutation, Epilepsy, Mental retardation

Organism-specific databases

MIMi614306. phenotype.
614558. phenotype.
Orphaneti157938. Joker disease.
PharmGKBiPA35009.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 19801980Sodium channel protein type 8 subunit alphaPRO_0000048500Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi215 – 2151N-linked (GlcNAc...)Sequence Analysis
Glycosylationi289 – 2891N-linked (GlcNAc...)Sequence Analysis
Glycosylationi295 – 2951N-linked (GlcNAc...)Sequence Analysis
Glycosylationi308 – 3081N-linked (GlcNAc...)Sequence Analysis
Glycosylationi326 – 3261N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1358 – 13581N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1372 – 13721N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1383 – 13831N-linked (GlcNAc...)Sequence Analysis
Modified residuei1497 – 14971Phosphoserine; by PKCBy similarity

Post-translational modificationi

May be ubiquitinated by NEDD4L; which would promote its endocytosis.By similarity
Phosphorylation at Ser-1497 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

PaxDbiQ9UQD0.
PRIDEiQ9UQD0.

PTM databases

PhosphoSiteiQ9UQD0.

Expressioni

Tissue specificityi

Isoform 5 is expressed in non-neuronal tissues, such as monocytes/macrophages.1 Publication

Gene expression databases

BgeeiQ9UQD0.
CleanExiHS_SCN8A.
ExpressionAtlasiQ9UQD0. baseline and differential.
GenevestigatoriQ9UQD0.

Organism-specific databases

HPAiCAB022169.

Interactioni

Subunit structurei

Interacts with NEDD4 and NEDD4L (By similarity). Interacts with FGF13; may regulate SCN8A activity.By similarity1 Publication

Protein-protein interaction databases

BioGridi112238. 1 interaction.
IntActiQ9UQD0. 1 interaction.
STRINGi9606.ENSP00000346534.

Structurei

3D structure databases

ProteinModelPortaliQ9UQD0.
SMRiQ9UQD0. Positions 128-273, 352-415, 749-968, 1194-1465, 1515-1872.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 127127CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini152 – 1598ExtracellularSequence Analysis
Topological domaini180 – 19213CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini212 – 2176ExtracellularSequence Analysis
Topological domaini238 – 25215CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini278 – 387110ExtracellularSequence AnalysisAdd
BLAST
Topological domaini414 – 747334CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini773 – 78311ExtracellularSequence AnalysisAdd
BLAST
Topological domaini808 – 8158CytoplasmicSequence Analysis
Topological domaini836 – 8416ExtracellularSequence Analysis
Topological domaini863 – 87715CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini899 – 95153ExtracellularSequence AnalysisAdd
BLAST
Topological domaini978 – 1193216CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini1218 – 123013ExtracellularSequence AnalysisAdd
BLAST
Topological domaini1257 – 12626CytoplasmicSequence Analysis
Topological domaini1285 – 12884ExtracellularSequence Analysis
Topological domaini1311 – 132919CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini1352 – 143786ExtracellularSequence AnalysisAdd
BLAST
Topological domaini1465 – 151753CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini1542 – 155211ExtracellularSequence AnalysisAdd
BLAST
Topological domaini1577 – 15826CytoplasmicSequence Analysis
Topological domaini1607 – 161610ExtracellularSequence Analysis
Topological domaini1639 – 165315CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini1677 – 174165ExtracellularSequence AnalysisAdd
BLAST
Topological domaini1767 – 1980214CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei128 – 15124Helical; Name=S1 of repeat ISequence AnalysisAdd
BLAST
Transmembranei160 – 17920Helical; Name=S2 of repeat ISequence AnalysisAdd
BLAST
Transmembranei193 – 21119Helical; Name=S3 of repeat ISequence AnalysisAdd
BLAST
Transmembranei218 – 23720Helical; Voltage-sensor; Name=S4 of repeat ISequence AnalysisAdd
BLAST
Transmembranei253 – 27725Helical; Name=S5 of repeat ISequence AnalysisAdd
BLAST
Transmembranei388 – 41326Helical; Name=S6 of repeat ISequence AnalysisAdd
BLAST
Transmembranei748 – 77225Helical; Name=S1 of repeat IISequence AnalysisAdd
BLAST
Transmembranei784 – 80724Helical; Name=S2 of repeat IISequence AnalysisAdd
BLAST
Transmembranei816 – 83520Helical; Name=S3 of repeat IISequence AnalysisAdd
BLAST
Transmembranei842 – 86221Helical; Voltage-sensor; Name=S4 of repeat IISequence AnalysisAdd
BLAST
Transmembranei878 – 89821Helical; Name=S5 of repeat IISequence AnalysisAdd
BLAST
Transmembranei952 – 97726Helical; Name=S6 of repeat IISequence AnalysisAdd
BLAST
Transmembranei1194 – 121724Helical; Name=S1 of repeat IIISequence AnalysisAdd
BLAST
Transmembranei1231 – 125626Helical; Name=S2 of repeat IIISequence AnalysisAdd
BLAST
Transmembranei1263 – 128422Helical; Name=S3 of repeat IIISequence AnalysisAdd
BLAST
Transmembranei1289 – 131022Helical; Voltage-sensor; Name=S4 of repeat IIISequence AnalysisAdd
BLAST
Transmembranei1330 – 135122Helical; Name=S5 of repeat IIISequence AnalysisAdd
BLAST
Transmembranei1438 – 146427Helical; Name=S6 of repeat IIISequence AnalysisAdd
BLAST
Transmembranei1518 – 154124Helical; Name=S1 of repeat IVSequence AnalysisAdd
BLAST
Transmembranei1553 – 157624Helical; Name=S2 of repeat IVSequence AnalysisAdd
BLAST
Transmembranei1583 – 160624Helical; Name=S3 of repeat IVSequence AnalysisAdd
BLAST
Transmembranei1617 – 163822Helical; Voltage-sensor; Name=S4 of repeat IVSequence AnalysisAdd
BLAST
Transmembranei1654 – 167623Helical; Name=S5 of repeat IVSequence AnalysisAdd
BLAST
Transmembranei1742 – 176625Helical; Name=S6 of repeat IVSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati114 – 442329ICuratedAdd
BLAST
Repeati735 – 1007273IICuratedAdd
BLAST
Repeati1180 – 1495316IIICuratedAdd
BLAST
Repeati1504 – 1801298IVCuratedAdd
BLAST
Domaini1895 – 192430IQCuratedPROSITE-ProRule annotationAdd
BLAST

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

Sequence similaritiesi

Contains 1 IQ domain.CuratedPROSITE-ProRule annotation

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1226.
GeneTreeiENSGT00760000118827.
HOGENOMiHOG000231755.
HOVERGENiHBG053100.
InParanoidiQ9UQD0.
KOiK04840.
OMAiGFICKKT.
PhylomeDBiQ9UQD0.
TreeFamiTF323985.

Family and domain databases

Gene3Di1.20.120.350. 4 hits.
InterProiIPR027359. Channel_four-helix_dom.
IPR024583. DUF3451.
IPR005821. Ion_trans_dom.
IPR000048. IQ_motif_EF-hand-BS.
IPR008054. Na_channel_a8su.
IPR001696. Na_channel_asu.
IPR010526. Na_trans_assoc.
[Graphical view]
PfamiPF11933. DUF3451. 1 hit.
PF00520. Ion_trans. 4 hits.
PF00612. IQ. 1 hit.
PF06512. Na_trans_assoc. 1 hit.
[Graphical view]
PRINTSiPR00170. NACHANNEL.
PR01667. NACHANNEL8.
SMARTiSM00015. IQ. 1 hit.
[Graphical view]
PROSITEiPS50096. IQ. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. Align

Isoform 11 Publication (identifier: Q9UQD0-1) [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
MAARLLAPPG PDSFKPFTPE SLANIERRIA ESKLKKPPKA DGSHREDDED
60 70 80 90 100
SKPKPNSDLE AGKSLPFIYG DIPQGLVAVP LEDFDPYYLT QKTFVVLNRG
110 120 130 140 150
KTLFRFSATP ALYILSPFNL IRRIAIKILI HSVFSMIIMC TILTNCVFMT
160 170 180 190 200
FSNPPDWSKN VEYTFTGIYT FESLVKIIAR GFCIDGFTFL RDPWNWLDFS
210 220 230 240 250
VIMMAYITEF VNLGNVSALR TFRVLRALKT ISVIPGLKTI VGALIQSVKK
260 270 280 290 300
LSDVMILTVF CLSVFALIGL QLFMGNLRNK CVVWPINFNE SYLENGTKGF
310 320 330 340 350
DWEEYINNKT NFYTVPGMLE PLLCGNSSDA GQCPEGYQCM KAGRNPNYGY
360 370 380 390 400
TSFDTFSWAF LALFRLMTQD YWENLYQLTL RAAGKTYMIF FVLVIFVGSF
410 420 430 440 450
YLVNLILAVV AMAYEEQNQA TLEEAEQKEA EFKAMLEQLK KQQEEAQAAA
460 470 480 490 500
MATSAGTVSE DAIEEEGEEG GGSPRSSSEI SKLSSKSAKE RRNRRKKRKQ
510 520 530 540 550
KELSEGEEKG DPEKVFKSES EDGMRRKAFR LPDNRIGRKF SIMNQSLLSI
560 570 580 590 600
PGSPFLSRHN SKSSIFSFRG PGRFRDPGSE NEFADDEHST VEESEGRRDS
610 620 630 640 650
LFIPIRARER RSSYSGYSGY SQGSRSSRIF PSLRRSVKRN STVDCNGVVS
660 670 680 690 700
LIGGPGSHIG GRLLPEATTE VEIKKKGPGS LLVSMDQLAS YGRKDRINSI
710 720 730 740 750
MSVVTNTLVE ELEESQRKCP PCWYKFANTF LIWECHPYWI KLKEIVNLIV
760 770 780 790 800
MDPFVDLAIT ICIVLNTLFM AMEHHPMTPQ FEHVLAVGNL VFTGIFTAEM
810 820 830 840 850
FLKLIAMDPY YYFQEGWNIF DGFIVSLSLM ELSLADVEGL SVLRSFRLLR
860 870 880 890 900
VFKLAKSWPT LNMLIKIIGN SVGALGNLTL VLAIIVFIFA VVGMQLFGKS
910 920 930 940 950
YKECVCKINQ DCELPRWHMH DFFHSFLIVF RVLCGEWIET MWDCMEVAGQ
960 970 980 990 1000
AMCLIVFMMV MVIGNLVVLN LFLALLLSSF SADNLAATDD DGEMNNLQIS
1010 1020 1030 1040 1050
VIRIKKGVAW TKLKVHAFMQ AHFKQREADE VKPLDELYEK KANCIANHTG
1060 1070 1080 1090 1100
ADIHRNGDFQ KNGNGTTSGI GSSVEKYIID EDHMSFINNP NLTVRVPIAV
1110 1120 1130 1140 1150
GESDFENLNT EDVSSESDPE GSKDKLDDTS SSEGSTIDIK PEVEEVPVEQ
1160 1170 1180 1190 1200
PEEYLDPDAC FTEGCVQRFK CCQVNIEEGL GKSWWILRKT CFLIVEHNWF
1210 1220 1230 1240 1250
ETFIIFMILL SSGALAFEDI YIEQRKTIRT ILEYADKVFT YIFILEMLLK
1260 1270 1280 1290 1300
WTAYGFVKFF TNAWCWLDFL IVAVSLVSLI ANALGYSELG AIKSLRTLRA
1310 1320 1330 1340 1350
LRPLRALSRF EGMRVVVNAL VGAIPSIMNV LLVCLIFWLI FSIMGVNLFA
1360 1370 1380 1390 1400
GKYHYCFNET SEIRFEIEDV NNKTECEKLM EGNNTEIRWK NVKINFDNVG
1410 1420 1430 1440 1450
AGYLALLQVA TFKGWMDIMY AAVDSRKPDE QPKYEDNIYM YIYFVIFIIF
1460 1470 1480 1490 1500
GSFFTLNLFI GVIIDNFNQQ KKKFGGQDIF MTEEQKKYYN AMKKLGSKKP
1510 1520 1530 1540 1550
QKPIPRPLNK IQGIVFDFVT QQAFDIVIMM LICLNMVTMM VETDTQSKQM
1560 1570 1580 1590 1600
ENILYWINLV FVIFFTCECV LKMFALRHYY FTIGWNIFDF VVVILSIVGM
1610 1620 1630 1640 1650
FLADIIEKYF VSPTLFRVIR LARIGRILRL IKGAKGIRTL LFALMMSLPA
1660 1670 1680 1690 1700
LFNIGLLLFL VMFIFSIFGM SNFAYVKHEA GIDDMFNFET FGNSMICLFQ
1710 1720 1730 1740 1750
ITTSAGWDGL LLPILNRPPD CSLDKEHPGS GFKGDCGNPS VGIFFFVSYI
1760 1770 1780 1790 1800
IISFLIVVNM YIAIILENFS VATEESADPL SEDDFETFYE IWEKFDPDAT
1810 1820 1830 1840 1850
QFIEYCKLAD FADALEHPLR VPKPNTIELI AMDLPMVSGD RIHCLDILFA
1860 1870 1880 1890 1900
FTKRVLGDSG ELDILRQQME ERFVASNPSK VSYEPITTTL RRKQEEVSAV
1910 1920 1930 1940 1950
VLQRAYRGHL ARRGFICKKT TSNKLENGGT HREKKESTPS TASLPSYDSV
1960 1970 1980
TKPEKEKQQR AEEGRRERAK RQKEVRESKC
Length:1,980
Mass (Da):225,280
Last modified:May 1, 2000 - v1
Checksum:i0EFC7BFB137FD4F0
GO
Isoform 21 Publication (identifier: Q9UQD0-2) [UniParc]FASTAAdd to Basket

Also known as: 5A1 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     207-207: I → V
     212-212: N → D

Show »
Length:1,980
Mass (Da):225,267
Checksum:i0510CF3CC31892F0
GO
Isoform 31 Publication (identifier: Q9UQD0-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     666-666: E → EVKIDKAATDDS

Show »
Length:1,991
Mass (Da):226,424
Checksum:i8C830A4CA55C69DE
GO
Isoform 41 Publication (identifier: Q9UQD0-4) [UniParc]FASTAAdd to Basket

Also known as: 18N1 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     1275-1283: SLVSLIANA → PLNLSGLI
     1284-1980: Missing.

Show »
Length:1,282
Mass (Da):145,118
Checksum:i43D3C2BD00DD44E5
GO
Isoform 5 (identifier: Q9UQD0-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1275-1315: Missing.

Show »
Length:1,939
Mass (Da):220,798
Checksum:i3E44D910D3897BC4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti5 – 51L → V in AAF35390. 1 PublicationCurated
Sequence conflicti133 – 1331V → L in AAD15789. (PubMed:9295353)Curated
Sequence conflicti257 – 2571L → M in AAF35390. 1 PublicationCurated
Sequence conflicti273 – 2731F → I in ACM63162. (PubMed:19136557)Curated
Sequence conflicti274 – 2785MGNLR → HGEPS in AAF35390. 1 PublicationCurated
Sequence conflicti453 – 4531T → N in AAF35390. 1 PublicationCurated
Sequence conflicti477 – 4771S → F in AAF35390. 1 PublicationCurated
Sequence conflicti483 – 4831L → I in AAF35390. 1 PublicationCurated
Sequence conflicti492 – 4921R → S in AAF35390. 1 PublicationCurated
Sequence conflicti504 – 5041S → F in AAF35390. 1 PublicationCurated
Sequence conflicti547 – 5482LL → MF in AAF35390. 1 PublicationCurated
Sequence conflicti1416 – 14161M → V in ACM63162. (PubMed:19136557)Curated
Sequence conflicti1445 – 14451V → I in AAD15789. (PubMed:9295353)Curated
Sequence conflicti1519 – 15191V → I in AAD15789. (PubMed:9295353)Curated
Sequence conflicti1702 – 17021T → A in AAF35390. 1 PublicationCurated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti216 – 2161V → D in EIEE13. 1 Publication
VAR_071674
Natural varianti846 – 8461F → S in EIEE13. 1 Publication
VAR_071675
Natural varianti1327 – 13271I → V in EIEE13. 1 Publication
VAR_071676
Natural varianti1466 – 14661N → K in EIEE13. 1 Publication
VAR_071677
Natural varianti1466 – 14661N → T in EIEE13. 1 Publication
VAR_071678
Natural varianti1617 – 16171R → Q in EIEE13. 1 Publication
VAR_071679
Natural varianti1650 – 16501A → T in EIEE13. 1 Publication
VAR_071680
Natural varianti1768 – 17681N → D in EIEE13; gain-of-function mutation; results in increased persistent sodium currents and incomplete channel inactivation. 1 Publication
VAR_067539
Natural varianti1872 – 18721R → W in EIEE13. 1 Publication
VAR_071681

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei207 – 2071I → V in isoform 2. 1 PublicationVSP_050589
Alternative sequencei212 – 2121N → D in isoform 2. 1 PublicationVSP_050590
Alternative sequencei666 – 6661E → EVKIDKAATDDS in isoform 3. 1 PublicationVSP_050591
Alternative sequencei1275 – 131541Missing in isoform 5. 1 PublicationVSP_038651Add
BLAST
Alternative sequencei1275 – 12839SLVSLIANA → PLNLSGLI in isoform 4. 1 PublicationVSP_050592
Alternative sequencei1284 – 1980697Missing in isoform 4. 1 PublicationVSP_050593Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF050736
, AF050711, AF050712, AF050713, AF050714, AF050715, AF050716, AF050717, AF050718, AF050719, AF050720, AF050721, AF050722, AF050723, AF050724, AF050725, AF050726, AF050727, AF050728, AF050729, AF050730, AF050731, AF050732, AF050733, AF050734, AF050735 Genomic DNA. Translation: AAD15789.1.
AF049618 Genomic DNA. Translation: AAD20439.1.
FJ611941 mRNA. Translation: ACM63162.1.
AB027567 mRNA. Translation: BAA78033.1.
AF225988 mRNA. Translation: AAF35390.1.
AC013421 Genomic DNA. No translation available.
AC025097 Genomic DNA. No translation available.
AC068987 Genomic DNA. No translation available.
AC140060 Genomic DNA. No translation available.
CCDSiCCDS44891.1. [Q9UQD0-1]
CCDS53794.1. [Q9UQD0-5]
RefSeqiNP_001171455.1. NM_001177984.2. [Q9UQD0-5]
NP_055006.1. NM_014191.3. [Q9UQD0-1]
XP_006719619.1. XM_006719556.1. [Q9UQD0-2]
UniGeneiHs.436550.
Hs.710638.

Genome annotation databases

GeneIDi6334.
KEGGihsa:6334.
UCSCiuc001ryw.4. human. [Q9UQD0-1]
uc010snl.3. human. [Q9UQD0-5]

Polymorphism databases

DMDMi34098756.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF050736
, AF050711 , AF050712 , AF050713 , AF050714 , AF050715 , AF050716 , AF050717 , AF050718 , AF050719 , AF050720 , AF050721 , AF050722 , AF050723 , AF050724 , AF050725 , AF050726 , AF050727 , AF050728 , AF050729 , AF050730 , AF050731 , AF050732 , AF050733 , AF050734 , AF050735 Genomic DNA. Translation: AAD15789.1 .
AF049618 Genomic DNA. Translation: AAD20439.1 .
FJ611941 mRNA. Translation: ACM63162.1 .
AB027567 mRNA. Translation: BAA78033.1 .
AF225988 mRNA. Translation: AAF35390.1 .
AC013421 Genomic DNA. No translation available.
AC025097 Genomic DNA. No translation available.
AC068987 Genomic DNA. No translation available.
AC140060 Genomic DNA. No translation available.
CCDSi CCDS44891.1. [Q9UQD0-1 ]
CCDS53794.1. [Q9UQD0-5 ]
RefSeqi NP_001171455.1. NM_001177984.2. [Q9UQD0-5 ]
NP_055006.1. NM_014191.3. [Q9UQD0-1 ]
XP_006719619.1. XM_006719556.1. [Q9UQD0-2 ]
UniGenei Hs.436550.
Hs.710638.

3D structure databases

ProteinModelPortali Q9UQD0.
SMRi Q9UQD0. Positions 128-273, 352-415, 749-968, 1194-1465, 1515-1872.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112238. 1 interaction.
IntActi Q9UQD0. 1 interaction.
STRINGi 9606.ENSP00000346534.

Chemistry

BindingDBi Q9UQD0.
ChEMBLi CHEMBL5202.
DrugBanki DB00313. Valproic Acid.
GuidetoPHARMACOLOGYi 583.

Protein family/group databases

TCDBi 1.A.1.10.8. the voltage-gated ion channel (vic) superfamily.

PTM databases

PhosphoSitei Q9UQD0.

Polymorphism databases

DMDMi 34098756.

Proteomic databases

PaxDbi Q9UQD0.
PRIDEi Q9UQD0.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 6334.
KEGGi hsa:6334.
UCSCi uc001ryw.4. human. [Q9UQD0-1 ]
uc010snl.3. human. [Q9UQD0-5 ]

Organism-specific databases

CTDi 6334.
GeneCardsi GC12P051987.
HGNCi HGNC:10596. SCN8A.
HPAi CAB022169.
MIMi 600702. gene.
614306. phenotype.
614558. phenotype.
neXtProti NX_Q9UQD0.
Orphaneti 157938. Joker disease.
PharmGKBi PA35009.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1226.
GeneTreei ENSGT00760000118827.
HOGENOMi HOG000231755.
HOVERGENi HBG053100.
InParanoidi Q9UQD0.
KOi K04840.
OMAi GFICKKT.
PhylomeDBi Q9UQD0.
TreeFami TF323985.

Enzyme and pathway databases

Reactomei REACT_22266. Interaction between L1 and Ankyrins.

Miscellaneous databases

ChiTaRSi SCN8A. human.
GeneWikii SCN8A.
GenomeRNAii 6334.
NextBioi 24596.
PROi Q9UQD0.
SOURCEi Search...

Gene expression databases

Bgeei Q9UQD0.
CleanExi HS_SCN8A.
ExpressionAtlasi Q9UQD0. baseline and differential.
Genevestigatori Q9UQD0.

Family and domain databases

Gene3Di 1.20.120.350. 4 hits.
InterProi IPR027359. Channel_four-helix_dom.
IPR024583. DUF3451.
IPR005821. Ion_trans_dom.
IPR000048. IQ_motif_EF-hand-BS.
IPR008054. Na_channel_a8su.
IPR001696. Na_channel_asu.
IPR010526. Na_trans_assoc.
[Graphical view ]
Pfami PF11933. DUF3451. 1 hit.
PF00520. Ion_trans. 4 hits.
PF00612. IQ. 1 hit.
PF06512. Na_trans_assoc. 1 hit.
[Graphical view ]
PRINTSi PR00170. NACHANNEL.
PR01667. NACHANNEL8.
SMARTi SM00015. IQ. 1 hit.
[Graphical view ]
PROSITEi PS50096. IQ. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Alternative splicing of the sodium channel SCN8A predicts a truncated two-domain protein in fetal brain and non-neuronal cells."
    Plummer N.W., McBurney M.W., Meisler M.H.
    J. Biol. Chem. 272:24008-24015(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 4).
    Tissue: Brain1 Publication and Fetal brain1 Publication.
  2. "Exon organization, coding sequence, physical mapping, and polymorphic intragenic markers for the human neuronal sodium channel gene SCN8A."
    Plummer N.W., Galt J., Jones J.M., Burgess D.L., Sprunger L.K., Kohrman D.C., Meisler M.H.
    Genomics 54:287-296(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1; 2 AND 3).
  3. "Regulation of podosome formation in macrophages by a splice variant of the sodium channel SCN8A."
    Carrithers M.D., Chatterjee G., Carrithers L.M., Offoha R., Iheagwara U., Rahner C., Graham M., Waxman S.G.
    J. Biol. Chem. 284:8114-8126(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Monocytic leukemia.
  4. "cDNA sequence of human sodium channel, SCN8A."
    Lin C., Numakura C., Kiyoshi H.
    Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  5. "Cloning of cDNA for human voltage-gated sodium channel alpha subunit, SCN8A."
    Jeong S.-Y., Goto J., Kanazawa I.
    Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  6. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "Fibroblast growth factor homologous factor 2B: association with Nav1.6 and selective colocalization at nodes of Ranvier of dorsal root axons."
    Wittmack E.K., Rush A.M., Craner M.J., Goldfarb M., Waxman S.G., Dib-Hajj S.D.
    J. Neurosci. 24:6765-6775(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FGF13.
  8. "Heterozygosity for a protein truncation mutation of sodium channel SCN8A in a patient with cerebellar atrophy, ataxia, and mental retardation."
    Trudeau M.M., Dalton J.C., Day J.W., Ranum L.P., Meisler M.H.
    J. Med. Genet. 43:527-530(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN CIAT.
  9. "de novo pathogenic SCN8A mutation identified by whole-genome sequencing of a family quartet affected by infantile epileptic encephalopathy and SUDEP."
    Veeramah K.R., O'Brien J.E., Meisler M.H., Cheng X., Dib-Hajj S.D., Waxman S.G., Talwar D., Girirajan S., Eichler E.E., Restifo L.L., Erickson R.P., Hammer M.F.
    Am. J. Hum. Genet. 90:502-510(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT EIEE13 ASP-1768, CHARACTERIZATION OF VARIANT EIEE13 ASP-1768.
  10. "De novo SCN8A mutation identified by whole-exome sequencing in a boy with neonatal epileptic encephalopathy, multiple congenital anomalies, and movement disorders."
    Vaher U., Noukas M., Nikopensius T., Kals M., Annilo T., Nelis M., Ounap K., Reimand T., Talvik I., Ilves P., Piirsoo A., Seppet E., Metspalu A., Talvik T.
    J. Child Neurol. 0:0-0(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT EIEE13 VAL-1327.
  11. Cited for: VARIANTS EIEE13 ASP-216; SER-846; LYS-1466; THR-1466; GLN-1617; THR-1650 AND TRP-1872.

Entry informationi

Entry nameiSCN8A_HUMAN
AccessioniPrimary (citable) accession number: Q9UQD0
Secondary accession number(s): B9VWG8
, O95788, Q9NYX2, Q9UPB2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 15, 2003
Last sequence update: May 1, 2000
Last modified: October 29, 2014
This is version 129 of the entry and version 1 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 12
    Human chromosome 12: 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

External Data

Dasty 3