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Q9JJV9 (SCN5A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Sodium channel protein type 5 subunit alpha
Alternative name(s):
Sodium channel protein cardiac muscle subunit alpha
Sodium channel protein type V subunit alpha
Voltage-gated sodium channel subunit alpha Nav1.5
mH1
Gene names
Name:Scn5a
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length2019 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This protein 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-resistant Na+ channel isoform. Channel inactivation is regulated by intracellular calcium levels By similarity.

Subunit structure

Interacts with the PDZ domain of the syntrophin SNTA1, SNTB1 and SNTB2 By similarity. Interacts with NEDD4, NEDD4L, WWP2 and GPD1L. Interacts with CALM By similarity. Interacts with FGF13; the interaction is direct and may regulate SNC5A density at membranes and function. Ref.5

Subcellular location

Membrane; Multi-pass membrane protein.

Tissue specificity

Expressed in the myocardium. Ref.1

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.

The IQ domain mediates association with calmodulin By similarity.

Post-translational modification

Regulated through phosphorylation by CaMK2D.

Ubiquitinated by NEDD4L; which promotes its endocytosis By similarity.

Phosphorylation at Ser-1505 by PKC in a highly conserved cytoplasmic loop slows inactivation of the sodium channel and reduces peak sodium currents By similarity.

Sequence similarities

Belongs to the sodium channel (TC 1.A.1.10) family. Nav1.5/SCN5A subfamily. [View classification]

Contains 1 IQ domain.

Ontologies

Keywords
   Biological processIon transport
Sodium transport
Transport
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
   DomainRepeat
Transmembrane
Transmembrane helix
   LigandCalmodulin-binding
Sodium
   Molecular functionIon channel
Sodium channel
Voltage-gated channel
   PTMGlycoprotein
Methylation
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcardiac ventricle development

Inferred from mutant phenotype PubMed 11972032. Source: MGI

cellular response to calcium ion

Inferred from sequence or structural similarity. Source: UniProtKB

membrane depolarization during SA node cell action potential

Inferred from mutant phenotype PubMed 15932895. Source: GOC

membrane depolarization during cardiac muscle cell action potential

Inferred from mutant phenotype PubMed 11972032. Source: GOC

regulation of cardiac muscle cell contraction

Inferred from mutant phenotype PubMed 16172272. Source: MGI

regulation of heart rate by cardiac conduction

Inferred from mutant phenotype PubMed 11972032PubMed 15809371PubMed 15932895PubMed 16172272. Source: MGI

response to organic cyclic compound

Inferred from mutant phenotype PubMed 19745168. Source: MGI

sodium ion transmembrane transport

Inferred from direct assay Ref.1. Source: GOC

sodium ion transport

Inferred from direct assay Ref.1. Source: MGI

   Cellular_componentT-tubule

Inferred from direct assay PubMed 15746173PubMed 18178574. Source: MGI

cell surface

Inferred from direct assay PubMed 17884088. Source: BHF-UCL

integral component of membrane

Inferred from sequence or structural similarity. Source: UniProtKB

intercalated disc

Inferred from direct assay PubMed 17884088PubMed 18184654. Source: BHF-UCL

plasma membrane

Inferred from direct assay PubMed 15746173. Source: MGI

sodium channel complex

Inferred from physical interaction PubMed 15272007. Source: MGI

voltage-gated sodium channel complex

Inferred by curator Ref.1. Source: MGI

   Molecular_functionscaffold protein binding

Inferred from physical interaction PubMed 18591664. Source: BHF-UCL

voltage-gated sodium channel activity

Inferred from direct assay Ref.1. Source: MGI

voltage-gated sodium channel activity involved in SA node cell action potential

Inferred from mutant phenotype PubMed 15932895. Source: MGI

voltage-gated sodium channel activity involved in cardiac muscle cell action potential

Inferred from mutant phenotype PubMed 11972032. Source: MGI

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: Q9JJV9-1)

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: Q9JJV9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     206-211: TTEFVD → VSENIK

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 20192019Sodium channel protein type 5 subunit alpha
PRO_0000376895

Regions

Topological domain1 – 126126Cytoplasmic Potential
Transmembrane127 – 15024Helical; Name=S1 of repeat I; Potential
Topological domain151 – 1588Extracellular Potential
Transmembrane159 – 17820Helical; Name=S2 of repeat I; Potential
Topological domain179 – 19113Cytoplasmic Potential
Transmembrane192 – 21019Helical; Name=S3 of repeat I; Potential
Topological domain211 – 2166Extracellular Potential
Transmembrane217 – 23620Helical; Voltage-sensor; Name=S4 of repeat I; Potential
Topological domain237 – 25216Cytoplasmic Potential
Transmembrane253 – 27624Helical; Name=S5 of repeat I; Potential
Topological domain277 – 389113Extracellular Potential
Transmembrane390 – 41526Helical; Name=S6 of repeat I; Potential
Topological domain416 – 711296Cytoplasmic Potential
Transmembrane712 – 73625Helical; Name=S1 of repeat II; Potential
Topological domain737 – 74711Extracellular Potential
Transmembrane748 – 77124Helical; Name=S2 of repeat II; Potential
Topological domain772 – 7798Cytoplasmic Potential
Transmembrane780 – 79920Helical; Name=S3 of repeat II; Potential
Topological domain800 – 8056Extracellular Potential
Transmembrane806 – 82520Helical; Voltage-sensor; Name=S4 of repeat II; Potential
Topological domain826 – 84116Cytoplasmic Potential
Transmembrane842 – 86221Helical; Name=S5 of repeat II; Potential
Topological domain863 – 91553Extracellular Potential
Transmembrane916 – 94126Helical; Name=S6 of repeat II; Potential
Topological domain942 – 1202261Cytoplasmic Potential
Transmembrane1203 – 122624Helical; Name=S1 of repeat III; Potential
Topological domain1227 – 123913Extracellular Potential
Transmembrane1240 – 126526Helical; Name=S2 of repeat III; Potential
Topological domain1266 – 12716Cytoplasmic Potential
Transmembrane1272 – 129322Helical; Name=S3 of repeat III; Potential
Topological domain1294 – 12974Extracellular Potential
Transmembrane1298 – 131922Helical; Voltage-sensor; Name=S4 of repeat III; Potential
Topological domain1320 – 133819Cytoplasmic Potential
Transmembrane1339 – 136123Helical; Name=S5 of repeat III; Potential
Topological domain1362 – 144584Extracellular Potential
Transmembrane1446 – 147227Helical; Name=S6 of repeat III; Potential
Topological domain1473 – 152553Cytoplasmic Potential
Transmembrane1526 – 154924Helical; Name=S1 of repeat IV; Potential
Topological domain1550 – 156011Extracellular Potential
Transmembrane1561 – 158424Helical; Name=S2 of repeat IV; Potential
Topological domain1585 – 15906Cytoplasmic Potential
Transmembrane1591 – 161424Helical; Name=S3 of repeat IV; Potential
Topological domain1615 – 162410Extracellular Potential
Transmembrane1625 – 164622Helical; Voltage-sensor; Name=S4 of repeat IV; Potential
Topological domain1647 – 166115Cytoplasmic Potential
Transmembrane1662 – 168423Helical; Name=S5 of repeat IV; Potential
Topological domain1685 – 174965Extracellular Potential
Transmembrane1750 – 177425Helical; Name=S6 of repeat IV; Potential
Topological domain1775 – 2019245Cytoplasmic Potential
Domain1903 – 193230IQ
Region1841 – 190363Interaction with FGF13 By similarity
Region1977 – 19804Interaction with NEDD4, NEDD4L and WWP2 By similarity

Amino acid modifications

Modified residue361Phosphoserine By similarity
Modified residue381Phosphothreonine By similarity
Modified residue4571Phosphoserine By similarity
Modified residue4601Phosphoserine By similarity
Modified residue4831Phosphoserine By similarity
Modified residue4841Phosphoserine By similarity
Modified residue4971Phosphoserine By similarity
Modified residue5101Phosphoserine By similarity
Modified residue5261Dimethylated arginine; alternate By similarity
Modified residue5261Omega-N-methylarginine; alternate By similarity
Modified residue5711Phosphoserine By similarity
Modified residue6641Phosphoserine By similarity
Modified residue6671Phosphoserine By similarity
Modified residue15051Phosphoserine; by PKC By similarity
Glycosylation2141N-linked (GlcNAc...) Potential
Glycosylation2831N-linked (GlcNAc...) Potential
Glycosylation2881N-linked (GlcNAc...) Potential
Glycosylation2911N-linked (GlcNAc...) Potential
Glycosylation3181N-linked (GlcNAc...) Potential
Glycosylation3281N-linked (GlcNAc...) Potential
Glycosylation7401N-linked (GlcNAc...) Potential
Glycosylation8031N-linked (GlcNAc...) Potential
Glycosylation8641N-linked (GlcNAc...) Potential
Glycosylation13671N-linked (GlcNAc...) Potential
Glycosylation13761N-linked (GlcNAc...) Potential
Glycosylation13821N-linked (GlcNAc...) Potential
Glycosylation13901N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence206 – 2116TTEFVD → VSENIK in isoform 2.
VSP_037444

Experimental info

Sequence conflict2151V → L in BAE27966. Ref.2
Sequence conflict2151V → L in BAE27800. Ref.2
Sequence conflict2341S → P in BAE27966. Ref.2
Sequence conflict2341S → P in BAE27800. Ref.2
Sequence conflict1008 – 10092AA → TT in CAB70096. Ref.1
Sequence conflict10781K → KQ in BAE27966. Ref.2
Sequence conflict10781K → KQ in BAE27800. Ref.2
Sequence conflict11331T → S in CAB70096. Ref.1

Sequences

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

Last modified July 27, 2011. Version 2.
Checksum: 5A3BC3C191859E79

FASTA2,019227,576
        10         20         30         40         50         60 
MANFLLPRGT SSFRRFTRES LAAIEKRMAE KQARGSATSQ ESREGLPEEE APRPQLDLQA 

        70         80         90        100        110        120 
SKKLPDLYGN PPRELIGEPL EDLDPFYSTQ KTFIVLNKGK TIFRFSATNA LYVLSPFHPV 

       130        140        150        160        170        180 
RRAAVKILVH SLFSMLIMCT ILTNCVFMAQ HDPPPWTKYV EYTFTAIYTF ESLVKILARG 

       190        200        210        220        230        240 
FCLHAFTFLR DPWNWLDFSV IVMAYTTEFV DLGNVSALRT FRVLRALKTI SVISGLKTIV 

       250        260        270        280        290        300 
GALIQSVKKL ADVMVLTVFC LSVFALIGLQ LFMGNLRHKC VRNFTELNGT NGSVEADGIV 

       310        320        330        340        350        360 
WNSLDVYLND PANYLLKNGT TDVLLCGNSS DAGTCPEGYR CLKAGENPDH GYTSFDSFAW 

       370        380        390        400        410        420 
AFLALFRLMT QDCWERLYQQ TLRSAGKIYM IFFMLVIFLG SFYLVNLILA VVAMAYEEQN 

       430        440        450        460        470        480 
QATIAETEEK EKRFQEAMEM LKKEHEALTI RGVDTVSRSS LEMSPLAPVT NHERRSKRRK 

       490        500        510        520        530        540 
RLSSGTEDGG DDRLPKSDSE DGPRALNQLS LTHGLSRTSM RPRSSRGSIF TFRRRDQGSE 

       550        560        570        580        590        600 
ADFADDENST AGESESHRTS LLVPWPLRRP STQGQPGFGT SAPGHVLNGK RNSTVDCNGV 

       610        620        630        640        650        660 
VSLLGAGDAE ATSPGSHLLR PIVLDRPPDT TTPSEEPGGP QMLTPQAPCA DGFEEPGARQ 

       670        680        690        700        710        720 
RALSAVSVLT SALEELEESH RKCPPCWNRF AQHYLIWECC PLWMSIKQKV KFVVMDPFAD 

       730        740        750        760        770        780 
LTITMCIVLN TLFMALEHYN MTAEFEEMLQ VGNLVFTGIF TAEMTFKIIA LDPYYYFQQG 

       790        800        810        820        830        840 
WNIFDSIIVI LSLMELGLSR MGNLSVLRSF RLLRVFKLAK SWPTLNTLIK IIGNSVGALG 

       850        860        870        880        890        900 
NLTLVLAIIV FIFAVVGMQL FGKNYSELRH RISDSGLLPR WHMMDFFHAF LIIFRILCGE 

       910        920        930        940        950        960 
WIETMWDCME VSGQSLCLLV FLLVMVIGNL VVLNLFLALL LSSFSADNLT APDEDGEMNN 

       970        980        990       1000       1010       1020 
LQLALARIQR GLRFVKRTTW DFCCGLLRRR PKKPAALATH SQLPSCIAAP RSPPPPEVEK 

      1030       1040       1050       1060       1070       1080 
APPARKETRF EEDKRPGQGT PGDTEPVCVP IAVAESDTDD QEEDEENSLG TEEEESSKQE 

      1090       1100       1110       1120       1130       1140 
SQVVSGGHEP PQEPRAWSQV SETTSSEAEA STSQADWQQE REAEPRAPGC GETPEDSYSE 

      1150       1160       1170       1180       1190       1200 
GSTADMTNTA DLLEQIPDLG EDVKDPEDCF TEGCVRRCPC CMVDTTQAPG KVWWRLRKTC 

      1210       1220       1230       1240       1250       1260 
YRIVEHSWFE TFIIFMILLS SGALAFEDIY LEERKTIKVL LEYADKMFTY VFVLEMLLKW 

      1270       1280       1290       1300       1310       1320 
VAYGFKKYFT NAWCWLDFLI VDVSLVSLVA NTLGFAEMGP IKSLRTLRAL RPLRALSRFE 

      1330       1340       1350       1360       1370       1380 
GMRVVVNALV GAIPSIMNVL LVCLIFWLIF SIMGVNLFAG KFGRCINQTE GDLPLNYTIV 

      1390       1400       1410       1420       1430       1440 
NNKSECESFN VTGELYWTKV KVNFDNVGAG YLALLQVATF KGWMDIMYAA VDSRGYEEQP 

      1450       1460       1470       1480       1490       1500 
QWEDNLYMYI YFVVFIIFGS FFTLNLFIGV IIDNFNQQKK KLGGQDIFMT EEQKKYYNAM 

      1510       1520       1530       1540       1550       1560 
KKLGSKKPQK PIPRPLNKYQ GFIFDIVTKQ AFDVTIMFLI CLNMVTMMVE TDDQSPEKVN 

      1570       1580       1590       1600       1610       1620 
ILAKINLLFV AIFTGECIVK MAALRHYYFT NSWNIFDFVV VILSIVGTVL SDIIQKYFFS 

      1630       1640       1650       1660       1670       1680 
PTLFRVIRLA RIGRILRLIR GAKGIRTLLF ALMMSLPALF NIGLLLFLVM FIYSIFGMAN 

      1690       1700       1710       1720       1730       1740 
FAYVKWEAGI DDMFNFQTFA NSMLCLFQIT TSAGWDGLLS PILNTGPPYC DPNLPNSNGS 

      1750       1760       1770       1780       1790       1800 
RGNCGSPAVG ILFFTTYIII SFLIVVNMYI AIILENFSVA TEESTEPLSE DDFDMFYEIW 

      1810       1820       1830       1840       1850       1860 
EKFDPEATQF IEYLALSDFA DALSEPLRIA KPNQISLINM DLPMVSGDRI HCMDILFAFT 

      1870       1880       1890       1900       1910       1920 
KRVLGESGEM DALKIQMEEK FMAANPSKIS YEPITTTLRR KHEEVSATVI QRAFRRHLLQ 

      1930       1940       1950       1960       1970       1980 
RSVKHASFLF RQQAGSSGLS DEDAPEREGL IAYMMNENFS RRSGPLSSSS ISSTSFPPSY 

      1990       2000       2010 
DSVTRATSDN LPVRASDYSR SEDLADFPPS PDRDRESIV 

« Hide

Isoform 2 [UniParc].

Checksum: E382EEFD025079F9
Show »

FASTA2,019227,554

References

« Hide 'large scale' references
[1]"Mouse heart Na+ channels: primary structure and function of two isoforms and alternatively spliced variants."
Zimmer T., Bollensdorff C., Haufe V., Birch-Hirschfeld E., Benndorf K.
Am. J. Physiol. 282:H1007-H1017(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
Strain: BALB/c.
Tissue: Heart.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Strain: C57BL/6J.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[4]"Ca2+/calmodulin-dependent protein kinase II regulates cardiac Na+ channels."
Wagner S., Dybkova N., Rasenack E.C., Jacobshagen C., Fabritz L., Kirchhof P., Maier S.K., Zhang T., Hasenfuss G., Brown J.H., Bers D.M., Maier L.S.
J. Clin. Invest. 116:3127-3138(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION BY CAMK2D.
[5]"Fibroblast growth factor homologous factor 13 regulates Na+ channels and conduction velocity in murine hearts."
Wang C., Hennessey J.A., Kirkton R.D., Wang C., Graham V., Puranam R.S., Rosenberg P.B., Bursac N., Pitt G.S.
Circ. Res. 109:775-782(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FGF13.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ271477 mRNA. Translation: CAB70096.1.
AK147254 mRNA. Translation: BAE27800.1.
AK147517 mRNA. Translation: BAE27966.1.
AC121922 Genomic DNA. No translation available.
AC171201 Genomic DNA. No translation available.
RefSeqNP_001240789.1. NM_001253860.1.
NP_067519.2. NM_021544.4.
UniGeneMm.103584.

3D structure databases

ProteinModelPortalQ9JJV9.
SMRQ9JJV9. Positions 1775-1930.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid203101. 2 interactions.
DIPDIP-46142N.
IntActQ9JJV9. 1 interaction.
MINTMINT-4130032.
STRING10090.ENSMUSP00000112838.

PTM databases

PhosphoSiteQ9JJV9.

Proteomic databases

PaxDbQ9JJV9.
PRIDEQ9JJV9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000117911; ENSMUSP00000112838; ENSMUSG00000032511.
ENSMUST00000120420; ENSMUSP00000113272; ENSMUSG00000032511. [Q9JJV9-1]
GeneID20271.
KEGGmmu:20271.
UCSCuc009sbc.2. mouse. [Q9JJV9-2]
uc009sbe.2. mouse. [Q9JJV9-1]

Organism-specific databases

CTD6331.
MGIMGI:98251. Scn5a.

Phylogenomic databases

eggNOGCOG1226.
GeneTreeENSGT00750000117555.
HOGENOMHOG000231755.
InParanoidQ3UH91.
KOK04838.
OrthoDBEOG7DJSK9.
TreeFamTF323985.

Gene expression databases

BgeeQ9JJV9.
GenevestigatorQ9JJV9.

Family and domain databases

Gene3D1.20.120.350. 4 hits.
InterProIPR027359. Channel_four-helix_dom.
IPR024583. DUF3451.
IPR005821. Ion_trans_dom.
IPR000048. IQ_motif_EF-hand-BS.
IPR008053. Na_channel_a5su.
IPR001696. Na_channel_asu.
IPR010526. Na_trans_assoc.
[Graphical view]
PfamPF11933. DUF3451. 1 hit.
PF00520. Ion_trans. 4 hits.
PF06512. Na_trans_assoc. 1 hit.
[Graphical view]
PRINTSPR00170. NACHANNEL.
PR01666. NACHANNEL5.
SMARTSM00015. IQ. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio297947.
PROQ9JJV9.
SOURCESearch...

Entry information

Entry nameSCN5A_MOUSE
AccessionPrimary (citable) accession number: Q9JJV9
Secondary accession number(s): E9Q1D2, Q3UH91
Entry history
Integrated into UniProtKB/Swiss-Prot: June 16, 2009
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 92 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot