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Q9JJV9

- SCN5A_MOUSE

UniProt

Q9JJV9 - SCN5A_MOUSE

Protein

Sodium channel protein type 5 subunit alpha

Gene

Scn5a

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 94 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    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.By similarity

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. scaffold protein binding Source: BHF-UCL
    3. voltage-gated sodium channel activity Source: MGI
    4. voltage-gated sodium channel activity involved in cardiac muscle cell action potential Source: MGI
    5. voltage-gated sodium channel activity involved in SA node cell action potential Source: MGI

    GO - Biological processi

    1. cardiac ventricle development Source: MGI
    2. cellular response to calcium ion Source: UniProtKB
    3. membrane depolarization during cardiac muscle cell action potential Source: GOC
    4. membrane depolarization during SA node cell action potential Source: GOC
    5. neuronal action potential Source: RefGenome
    6. regulation of cardiac muscle cell contraction Source: MGI
    7. regulation of heart rate by cardiac conduction Source: MGI
    8. response to organic cyclic compound Source: MGI
    9. sodium ion transmembrane transport Source: GOC
    10. sodium ion transport Source: MGI

    Keywords - Molecular functioni

    Ion channel, Sodium channel, Voltage-gated channel

    Keywords - Biological processi

    Ion transport, Sodium transport, Transport

    Keywords - Ligandi

    Calmodulin-binding, Sodium

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:Scn5a
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 9

    Organism-specific databases

    MGIiMGI:98251. Scn5a.

    Subcellular locationi

    GO - Cellular componenti

    1. cell surface Source: BHF-UCL
    2. integral component of membrane Source: UniProtKB
    3. intercalated disc Source: BHF-UCL
    4. plasma membrane Source: MGI
    5. sodium channel complex Source: MGI
    6. T-tubule Source: MGI
    7. voltage-gated sodium channel complex Source: MGI

    Keywords - Cellular componenti

    Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 20192019Sodium channel protein type 5 subunit alphaPRO_0000376895Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei36 – 361PhosphoserineBy similarity
    Modified residuei38 – 381PhosphothreonineBy similarity
    Glycosylationi214 – 2141N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi283 – 2831N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi288 – 2881N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi291 – 2911N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi318 – 3181N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi328 – 3281N-linked (GlcNAc...)Sequence Analysis
    Modified residuei457 – 4571PhosphoserineBy similarity
    Modified residuei460 – 4601PhosphoserineBy similarity
    Modified residuei483 – 4831PhosphoserineBy similarity
    Modified residuei484 – 4841PhosphoserineBy similarity
    Modified residuei497 – 4971PhosphoserineBy similarity
    Modified residuei510 – 5101PhosphoserineBy similarity
    Modified residuei526 – 5261Dimethylated arginine; alternateBy similarity
    Modified residuei526 – 5261Omega-N-methylarginine; alternateBy similarity
    Modified residuei571 – 5711PhosphoserineBy similarity
    Modified residuei664 – 6641PhosphoserineBy similarity
    Modified residuei667 – 6671PhosphoserineBy similarity
    Glycosylationi740 – 7401N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi803 – 8031N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi864 – 8641N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1367 – 13671N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1376 – 13761N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1382 – 13821N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1390 – 13901N-linked (GlcNAc...)Sequence Analysis
    Modified residuei1505 – 15051Phosphoserine; by PKCBy similarity

    Post-translational modificationi

    Regulated through phosphorylation by CaMK2D.1 Publication
    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

    Keywords - PTMi

    Glycoprotein, Methylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiQ9JJV9.
    PRIDEiQ9JJV9.

    PTM databases

    PhosphoSiteiQ9JJV9.

    Expressioni

    Tissue specificityi

    Expressed in the myocardium.1 Publication

    Gene expression databases

    BgeeiQ9JJV9.
    GenevestigatoriQ9JJV9.

    Interactioni

    Subunit structurei

    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.By similarity1 Publication

    Protein-protein interaction databases

    BioGridi203101. 2 interactions.
    DIPiDIP-46142N.
    IntActiQ9JJV9. 1 interaction.
    MINTiMINT-4130032.
    STRINGi10090.ENSMUSP00000112838.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9JJV9.
    SMRiQ9JJV9. Positions 1775-1930.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 126126CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini151 – 1588ExtracellularSequence Analysis
    Topological domaini179 – 19113CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini211 – 2166ExtracellularSequence Analysis
    Topological domaini237 – 25216CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini277 – 389113ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini416 – 711296CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini737 – 74711ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini772 – 7798CytoplasmicSequence Analysis
    Topological domaini800 – 8056ExtracellularSequence Analysis
    Topological domaini826 – 84116CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini863 – 91553ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini942 – 1202261CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1227 – 123913ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1266 – 12716CytoplasmicSequence Analysis
    Topological domaini1294 – 12974ExtracellularSequence Analysis
    Topological domaini1320 – 133819CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1362 – 144584ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1473 – 152553CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1550 – 156011ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1585 – 15906CytoplasmicSequence Analysis
    Topological domaini1615 – 162410ExtracellularSequence Analysis
    Topological domaini1647 – 166115CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1685 – 174965ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1775 – 2019245CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei127 – 15024Helical; Name=S1 of repeat ISequence AnalysisAdd
    BLAST
    Transmembranei159 – 17820Helical; Name=S2 of repeat ISequence AnalysisAdd
    BLAST
    Transmembranei192 – 21019Helical; Name=S3 of repeat ISequence AnalysisAdd
    BLAST
    Transmembranei217 – 23620Helical; Voltage-sensor; Name=S4 of repeat ISequence AnalysisAdd
    BLAST
    Transmembranei253 – 27624Helical; Name=S5 of repeat ISequence AnalysisAdd
    BLAST
    Transmembranei390 – 41526Helical; Name=S6 of repeat ISequence AnalysisAdd
    BLAST
    Transmembranei712 – 73625Helical; Name=S1 of repeat IISequence AnalysisAdd
    BLAST
    Transmembranei748 – 77124Helical; Name=S2 of repeat IISequence AnalysisAdd
    BLAST
    Transmembranei780 – 79920Helical; Name=S3 of repeat IISequence AnalysisAdd
    BLAST
    Transmembranei806 – 82520Helical; Voltage-sensor; Name=S4 of repeat IISequence AnalysisAdd
    BLAST
    Transmembranei842 – 86221Helical; Name=S5 of repeat IISequence AnalysisAdd
    BLAST
    Transmembranei916 – 94126Helical; Name=S6 of repeat IISequence AnalysisAdd
    BLAST
    Transmembranei1203 – 122624Helical; Name=S1 of repeat IIISequence AnalysisAdd
    BLAST
    Transmembranei1240 – 126526Helical; Name=S2 of repeat IIISequence AnalysisAdd
    BLAST
    Transmembranei1272 – 129322Helical; Name=S3 of repeat IIISequence AnalysisAdd
    BLAST
    Transmembranei1298 – 131922Helical; Voltage-sensor; Name=S4 of repeat IIISequence AnalysisAdd
    BLAST
    Transmembranei1339 – 136123Helical; Name=S5 of repeat IIISequence AnalysisAdd
    BLAST
    Transmembranei1446 – 147227Helical; Name=S6 of repeat IIISequence AnalysisAdd
    BLAST
    Transmembranei1526 – 154924Helical; Name=S1 of repeat IVSequence AnalysisAdd
    BLAST
    Transmembranei1561 – 158424Helical; Name=S2 of repeat IVSequence AnalysisAdd
    BLAST
    Transmembranei1591 – 161424Helical; Name=S3 of repeat IVSequence AnalysisAdd
    BLAST
    Transmembranei1625 – 164622Helical; Voltage-sensor; Name=S4 of repeat IVSequence AnalysisAdd
    BLAST
    Transmembranei1662 – 168423Helical; Name=S5 of repeat IVSequence AnalysisAdd
    BLAST
    Transmembranei1750 – 177425Helical; Name=S6 of repeat IVSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1903 – 193230IQAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1841 – 190363Interaction with FGF13By similarityAdd
    BLAST
    Regioni1977 – 19804Interaction with NEDD4, NEDD4L and WWP2By similarity

    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.
    The IQ domain mediates association with calmodulin.By similarity

    Sequence similaritiesi

    Contains 1 IQ domain.Curated

    Keywords - Domaini

    Repeat, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG1226.
    GeneTreeiENSGT00750000117555.
    HOGENOMiHOG000231755.
    InParanoidiQ3UH91.
    KOiK04838.
    OrthoDBiEOG7DJSK9.
    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.
    IPR008053. Na_channel_a5su.
    IPR001696. Na_channel_asu.
    IPR010526. Na_trans_assoc.
    [Graphical view]
    PfamiPF11933. DUF3451. 1 hit.
    PF00520. Ion_trans. 4 hits.
    PF06512. Na_trans_assoc. 1 hit.
    [Graphical view]
    PRINTSiPR00170. NACHANNEL.
    PR01666. NACHANNEL5.
    SMARTiSM00015. IQ. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Note: Additional isoforms seem to exist.

    Isoform 1 (identifier: Q9JJV9-1) [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

    MANFLLPRGT SSFRRFTRES LAAIEKRMAE KQARGSATSQ ESREGLPEEE     50
    APRPQLDLQA SKKLPDLYGN PPRELIGEPL EDLDPFYSTQ KTFIVLNKGK 100
    TIFRFSATNA LYVLSPFHPV RRAAVKILVH SLFSMLIMCT ILTNCVFMAQ 150
    HDPPPWTKYV EYTFTAIYTF ESLVKILARG FCLHAFTFLR DPWNWLDFSV 200
    IVMAYTTEFV DLGNVSALRT FRVLRALKTI SVISGLKTIV GALIQSVKKL 250
    ADVMVLTVFC LSVFALIGLQ LFMGNLRHKC VRNFTELNGT NGSVEADGIV 300
    WNSLDVYLND PANYLLKNGT TDVLLCGNSS DAGTCPEGYR CLKAGENPDH 350
    GYTSFDSFAW AFLALFRLMT QDCWERLYQQ TLRSAGKIYM IFFMLVIFLG 400
    SFYLVNLILA VVAMAYEEQN QATIAETEEK EKRFQEAMEM LKKEHEALTI 450
    RGVDTVSRSS LEMSPLAPVT NHERRSKRRK RLSSGTEDGG DDRLPKSDSE 500
    DGPRALNQLS LTHGLSRTSM RPRSSRGSIF TFRRRDQGSE ADFADDENST 550
    AGESESHRTS LLVPWPLRRP STQGQPGFGT SAPGHVLNGK RNSTVDCNGV 600
    VSLLGAGDAE ATSPGSHLLR PIVLDRPPDT TTPSEEPGGP QMLTPQAPCA 650
    DGFEEPGARQ RALSAVSVLT SALEELEESH RKCPPCWNRF AQHYLIWECC 700
    PLWMSIKQKV KFVVMDPFAD LTITMCIVLN TLFMALEHYN MTAEFEEMLQ 750
    VGNLVFTGIF TAEMTFKIIA LDPYYYFQQG WNIFDSIIVI LSLMELGLSR 800
    MGNLSVLRSF RLLRVFKLAK SWPTLNTLIK IIGNSVGALG NLTLVLAIIV 850
    FIFAVVGMQL FGKNYSELRH RISDSGLLPR WHMMDFFHAF LIIFRILCGE 900
    WIETMWDCME VSGQSLCLLV FLLVMVIGNL VVLNLFLALL LSSFSADNLT 950
    APDEDGEMNN LQLALARIQR GLRFVKRTTW DFCCGLLRRR PKKPAALATH 1000
    SQLPSCIAAP RSPPPPEVEK APPARKETRF EEDKRPGQGT PGDTEPVCVP 1050
    IAVAESDTDD QEEDEENSLG TEEEESSKQE SQVVSGGHEP PQEPRAWSQV 1100
    SETTSSEAEA STSQADWQQE REAEPRAPGC GETPEDSYSE GSTADMTNTA 1150
    DLLEQIPDLG EDVKDPEDCF TEGCVRRCPC CMVDTTQAPG KVWWRLRKTC 1200
    YRIVEHSWFE TFIIFMILLS SGALAFEDIY LEERKTIKVL LEYADKMFTY 1250
    VFVLEMLLKW VAYGFKKYFT NAWCWLDFLI VDVSLVSLVA NTLGFAEMGP 1300
    IKSLRTLRAL RPLRALSRFE GMRVVVNALV GAIPSIMNVL LVCLIFWLIF 1350
    SIMGVNLFAG KFGRCINQTE GDLPLNYTIV NNKSECESFN VTGELYWTKV 1400
    KVNFDNVGAG YLALLQVATF KGWMDIMYAA VDSRGYEEQP QWEDNLYMYI 1450
    YFVVFIIFGS FFTLNLFIGV IIDNFNQQKK KLGGQDIFMT EEQKKYYNAM 1500
    KKLGSKKPQK PIPRPLNKYQ GFIFDIVTKQ AFDVTIMFLI CLNMVTMMVE 1550
    TDDQSPEKVN ILAKINLLFV AIFTGECIVK MAALRHYYFT NSWNIFDFVV 1600
    VILSIVGTVL SDIIQKYFFS PTLFRVIRLA RIGRILRLIR GAKGIRTLLF 1650
    ALMMSLPALF NIGLLLFLVM FIYSIFGMAN FAYVKWEAGI DDMFNFQTFA 1700
    NSMLCLFQIT TSAGWDGLLS PILNTGPPYC DPNLPNSNGS RGNCGSPAVG 1750
    ILFFTTYIII SFLIVVNMYI AIILENFSVA TEESTEPLSE DDFDMFYEIW 1800
    EKFDPEATQF IEYLALSDFA DALSEPLRIA KPNQISLINM DLPMVSGDRI 1850
    HCMDILFAFT KRVLGESGEM DALKIQMEEK FMAANPSKIS YEPITTTLRR 1900
    KHEEVSATVI QRAFRRHLLQ RSVKHASFLF RQQAGSSGLS DEDAPEREGL 1950
    IAYMMNENFS RRSGPLSSSS ISSTSFPPSY DSVTRATSDN LPVRASDYSR 2000
    SEDLADFPPS PDRDRESIV 2019
    Length:2,019
    Mass (Da):227,576
    Last modified:July 27, 2011 - v2
    Checksum:i5A3BC3C191859E79
    GO
    Isoform 2 (identifier: Q9JJV9-2) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:2,019
    Mass (Da):227,554
    Checksum:iE382EEFD025079F9
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti215 – 2151V → L in BAE27966. (PubMed:16141072)Curated
    Sequence conflicti215 – 2151V → L in BAE27800. (PubMed:16141072)Curated
    Sequence conflicti234 – 2341S → P in BAE27966. (PubMed:16141072)Curated
    Sequence conflicti234 – 2341S → P in BAE27800. (PubMed:16141072)Curated
    Sequence conflicti1008 – 10092AA → TT in CAB70096. (PubMed:11834499)Curated
    Sequence conflicti1078 – 10781K → KQ in BAE27966. (PubMed:16141072)Curated
    Sequence conflicti1078 – 10781K → KQ in BAE27800. (PubMed:16141072)Curated
    Sequence conflicti1133 – 11331T → S in CAB70096. (PubMed:11834499)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei206 – 2116TTEFVD → VSENIK in isoform 2. 1 PublicationVSP_037444

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    RefSeqiNP_001240789.1. NM_001253860.1.
    NP_067519.2. NM_021544.4.
    UniGeneiMm.103584.

    Genome annotation databases

    EnsembliENSMUST00000117911; ENSMUSP00000112838; ENSMUSG00000032511.
    ENSMUST00000120420; ENSMUSP00000113272; ENSMUSG00000032511. [Q9JJV9-1]
    GeneIDi20271.
    KEGGimmu:20271.
    UCSCiuc009sbc.2. mouse. [Q9JJV9-2]
    uc009sbe.2. mouse. [Q9JJV9-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    RefSeqi NP_001240789.1. NM_001253860.1.
    NP_067519.2. NM_021544.4.
    UniGenei Mm.103584.

    3D structure databases

    ProteinModelPortali Q9JJV9.
    SMRi Q9JJV9. Positions 1775-1930.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 203101. 2 interactions.
    DIPi DIP-46142N.
    IntActi Q9JJV9. 1 interaction.
    MINTi MINT-4130032.
    STRINGi 10090.ENSMUSP00000112838.

    PTM databases

    PhosphoSitei Q9JJV9.

    Proteomic databases

    PaxDbi Q9JJV9.
    PRIDEi Q9JJV9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000117911 ; ENSMUSP00000112838 ; ENSMUSG00000032511 .
    ENSMUST00000120420 ; ENSMUSP00000113272 ; ENSMUSG00000032511 . [Q9JJV9-1 ]
    GeneIDi 20271.
    KEGGi mmu:20271.
    UCSCi uc009sbc.2. mouse. [Q9JJV9-2 ]
    uc009sbe.2. mouse. [Q9JJV9-1 ]

    Organism-specific databases

    CTDi 6331.
    MGIi MGI:98251. Scn5a.

    Phylogenomic databases

    eggNOGi COG1226.
    GeneTreei ENSGT00750000117555.
    HOGENOMi HOG000231755.
    InParanoidi Q3UH91.
    KOi K04838.
    OrthoDBi EOG7DJSK9.
    TreeFami TF323985.

    Miscellaneous databases

    NextBioi 297947.
    PROi Q9JJV9.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9JJV9.
    Genevestigatori Q9JJV9.

    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.
    IPR008053. Na_channel_a5su.
    IPR001696. Na_channel_asu.
    IPR010526. Na_trans_assoc.
    [Graphical view ]
    Pfami PF11933. DUF3451. 1 hit.
    PF00520. Ion_trans. 4 hits.
    PF06512. Na_trans_assoc. 1 hit.
    [Graphical view ]
    PRINTSi PR00170. NACHANNEL.
    PR01666. NACHANNEL5.
    SMARTi SM00015. IQ. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    4. 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.

    Entry informationi

    Entry nameiSCN5A_MOUSE
    AccessioniPrimary (citable) accession number: Q9JJV9
    Secondary accession number(s): E9Q1D2, Q3UH91
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 16, 2009
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 94 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3