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Q9JJV9

- SCN5A_MOUSE

UniProt

Q9JJV9 - SCN5A_MOUSE

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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

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. scaffold protein binding Source: BHF-UCL
  2. voltage-gated sodium channel activity Source: MGI
  3. voltage-gated sodium channel activity involved in cardiac muscle cell action potential Source: MGI
  4. 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
Complete GO annotation...

Keywords - Molecular functioni

Ion channel, Sodium channel, Voltage-gated channel

Keywords - Biological processi

Ion transport, Sodium transport, Transport

Keywords - Ligandi

Calmodulin-binding, Sodium

Enzyme and pathway databases

ReactomeiREACT_244931. Interaction between L1 and Ankyrins.

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 126126CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei127 – 15024Helical; Name=S1 of repeat ISequence AnalysisAdd
BLAST
Topological domaini151 – 1588ExtracellularSequence Analysis
Transmembranei159 – 17820Helical; Name=S2 of repeat ISequence AnalysisAdd
BLAST
Topological domaini179 – 19113CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei192 – 21019Helical; Name=S3 of repeat ISequence AnalysisAdd
BLAST
Topological domaini211 – 2166ExtracellularSequence Analysis
Transmembranei217 – 23620Helical; Voltage-sensor; Name=S4 of repeat ISequence AnalysisAdd
BLAST
Topological domaini237 – 25216CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei253 – 27624Helical; Name=S5 of repeat ISequence AnalysisAdd
BLAST
Topological domaini277 – 389113ExtracellularSequence AnalysisAdd
BLAST
Transmembranei390 – 41526Helical; Name=S6 of repeat ISequence AnalysisAdd
BLAST
Topological domaini416 – 711296CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei712 – 73625Helical; Name=S1 of repeat IISequence AnalysisAdd
BLAST
Topological domaini737 – 74711ExtracellularSequence AnalysisAdd
BLAST
Transmembranei748 – 77124Helical; Name=S2 of repeat IISequence AnalysisAdd
BLAST
Topological domaini772 – 7798CytoplasmicSequence Analysis
Transmembranei780 – 79920Helical; Name=S3 of repeat IISequence AnalysisAdd
BLAST
Topological domaini800 – 8056ExtracellularSequence Analysis
Transmembranei806 – 82520Helical; Voltage-sensor; Name=S4 of repeat IISequence AnalysisAdd
BLAST
Topological domaini826 – 84116CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei842 – 86221Helical; Name=S5 of repeat IISequence AnalysisAdd
BLAST
Topological domaini863 – 91553ExtracellularSequence AnalysisAdd
BLAST
Transmembranei916 – 94126Helical; Name=S6 of repeat IISequence AnalysisAdd
BLAST
Topological domaini942 – 1202261CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei1203 – 122624Helical; Name=S1 of repeat IIISequence AnalysisAdd
BLAST
Topological domaini1227 – 123913ExtracellularSequence AnalysisAdd
BLAST
Transmembranei1240 – 126526Helical; Name=S2 of repeat IIISequence AnalysisAdd
BLAST
Topological domaini1266 – 12716CytoplasmicSequence Analysis
Transmembranei1272 – 129322Helical; Name=S3 of repeat IIISequence AnalysisAdd
BLAST
Topological domaini1294 – 12974ExtracellularSequence Analysis
Transmembranei1298 – 131922Helical; Voltage-sensor; Name=S4 of repeat IIISequence AnalysisAdd
BLAST
Topological domaini1320 – 133819CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei1339 – 136123Helical; Name=S5 of repeat IIISequence AnalysisAdd
BLAST
Topological domaini1362 – 144584ExtracellularSequence AnalysisAdd
BLAST
Transmembranei1446 – 147227Helical; Name=S6 of repeat IIISequence AnalysisAdd
BLAST
Topological domaini1473 – 152553CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei1526 – 154924Helical; Name=S1 of repeat IVSequence AnalysisAdd
BLAST
Topological domaini1550 – 156011ExtracellularSequence AnalysisAdd
BLAST
Transmembranei1561 – 158424Helical; Name=S2 of repeat IVSequence AnalysisAdd
BLAST
Topological domaini1585 – 15906CytoplasmicSequence Analysis
Transmembranei1591 – 161424Helical; Name=S3 of repeat IVSequence AnalysisAdd
BLAST
Topological domaini1615 – 162410ExtracellularSequence Analysis
Transmembranei1625 – 164622Helical; Voltage-sensor; Name=S4 of repeat IVSequence AnalysisAdd
BLAST
Topological domaini1647 – 166115CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei1662 – 168423Helical; Name=S5 of repeat IVSequence AnalysisAdd
BLAST
Topological domaini1685 – 174965ExtracellularSequence AnalysisAdd
BLAST
Transmembranei1750 – 177425Helical; Name=S6 of repeat IVSequence AnalysisAdd
BLAST
Topological domaini1775 – 2019245CytoplasmicSequence AnalysisAdd
BLAST

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
Complete GO annotation...

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.
ExpressionAtlasiQ9JJV9. baseline and differential.
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...

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.
GeneTreeiENSGT00760000118827.
HOGENOMiHOG000231755.
InParanoidiQ9JJV9.
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

        10         20         30         40         50
MANFLLPRGT SSFRRFTRES LAAIEKRMAE KQARGSATSQ ESREGLPEEE
60 70 80 90 100
APRPQLDLQA SKKLPDLYGN PPRELIGEPL EDLDPFYSTQ KTFIVLNKGK
110 120 130 140 150
TIFRFSATNA LYVLSPFHPV RRAAVKILVH SLFSMLIMCT ILTNCVFMAQ
160 170 180 190 200
HDPPPWTKYV EYTFTAIYTF ESLVKILARG FCLHAFTFLR DPWNWLDFSV
210 220 230 240 250
IVMAYTTEFV DLGNVSALRT FRVLRALKTI SVISGLKTIV GALIQSVKKL
260 270 280 290 300
ADVMVLTVFC LSVFALIGLQ LFMGNLRHKC VRNFTELNGT NGSVEADGIV
310 320 330 340 350
WNSLDVYLND PANYLLKNGT TDVLLCGNSS DAGTCPEGYR CLKAGENPDH
360 370 380 390 400
GYTSFDSFAW AFLALFRLMT QDCWERLYQQ TLRSAGKIYM IFFMLVIFLG
410 420 430 440 450
SFYLVNLILA VVAMAYEEQN QATIAETEEK EKRFQEAMEM LKKEHEALTI
460 470 480 490 500
RGVDTVSRSS LEMSPLAPVT NHERRSKRRK RLSSGTEDGG DDRLPKSDSE
510 520 530 540 550
DGPRALNQLS LTHGLSRTSM RPRSSRGSIF TFRRRDQGSE ADFADDENST
560 570 580 590 600
AGESESHRTS LLVPWPLRRP STQGQPGFGT SAPGHVLNGK RNSTVDCNGV
610 620 630 640 650
VSLLGAGDAE ATSPGSHLLR PIVLDRPPDT TTPSEEPGGP QMLTPQAPCA
660 670 680 690 700
DGFEEPGARQ RALSAVSVLT SALEELEESH RKCPPCWNRF AQHYLIWECC
710 720 730 740 750
PLWMSIKQKV KFVVMDPFAD LTITMCIVLN TLFMALEHYN MTAEFEEMLQ
760 770 780 790 800
VGNLVFTGIF TAEMTFKIIA LDPYYYFQQG WNIFDSIIVI LSLMELGLSR
810 820 830 840 850
MGNLSVLRSF RLLRVFKLAK SWPTLNTLIK IIGNSVGALG NLTLVLAIIV
860 870 880 890 900
FIFAVVGMQL FGKNYSELRH RISDSGLLPR WHMMDFFHAF LIIFRILCGE
910 920 930 940 950
WIETMWDCME VSGQSLCLLV FLLVMVIGNL VVLNLFLALL LSSFSADNLT
960 970 980 990 1000
APDEDGEMNN LQLALARIQR GLRFVKRTTW DFCCGLLRRR PKKPAALATH
1010 1020 1030 1040 1050
SQLPSCIAAP RSPPPPEVEK APPARKETRF EEDKRPGQGT PGDTEPVCVP
1060 1070 1080 1090 1100
IAVAESDTDD QEEDEENSLG TEEEESSKQE SQVVSGGHEP PQEPRAWSQV
1110 1120 1130 1140 1150
SETTSSEAEA STSQADWQQE REAEPRAPGC GETPEDSYSE GSTADMTNTA
1160 1170 1180 1190 1200
DLLEQIPDLG EDVKDPEDCF TEGCVRRCPC CMVDTTQAPG KVWWRLRKTC
1210 1220 1230 1240 1250
YRIVEHSWFE TFIIFMILLS SGALAFEDIY LEERKTIKVL LEYADKMFTY
1260 1270 1280 1290 1300
VFVLEMLLKW VAYGFKKYFT NAWCWLDFLI VDVSLVSLVA NTLGFAEMGP
1310 1320 1330 1340 1350
IKSLRTLRAL RPLRALSRFE GMRVVVNALV GAIPSIMNVL LVCLIFWLIF
1360 1370 1380 1390 1400
SIMGVNLFAG KFGRCINQTE GDLPLNYTIV NNKSECESFN VTGELYWTKV
1410 1420 1430 1440 1450
KVNFDNVGAG YLALLQVATF KGWMDIMYAA VDSRGYEEQP QWEDNLYMYI
1460 1470 1480 1490 1500
YFVVFIIFGS FFTLNLFIGV IIDNFNQQKK KLGGQDIFMT EEQKKYYNAM
1510 1520 1530 1540 1550
KKLGSKKPQK PIPRPLNKYQ GFIFDIVTKQ AFDVTIMFLI CLNMVTMMVE
1560 1570 1580 1590 1600
TDDQSPEKVN ILAKINLLFV AIFTGECIVK MAALRHYYFT NSWNIFDFVV
1610 1620 1630 1640 1650
VILSIVGTVL SDIIQKYFFS PTLFRVIRLA RIGRILRLIR GAKGIRTLLF
1660 1670 1680 1690 1700
ALMMSLPALF NIGLLLFLVM FIYSIFGMAN FAYVKWEAGI DDMFNFQTFA
1710 1720 1730 1740 1750
NSMLCLFQIT TSAGWDGLLS PILNTGPPYC DPNLPNSNGS RGNCGSPAVG
1760 1770 1780 1790 1800
ILFFTTYIII SFLIVVNMYI AIILENFSVA TEESTEPLSE DDFDMFYEIW
1810 1820 1830 1840 1850
EKFDPEATQF IEYLALSDFA DALSEPLRIA KPNQISLINM DLPMVSGDRI
1860 1870 1880 1890 1900
HCMDILFAFT KRVLGESGEM DALKIQMEEK FMAANPSKIS YEPITTTLRR
1910 1920 1930 1940 1950
KHEEVSATVI QRAFRRHLLQ RSVKHASFLF RQQAGSSGLS DEDAPEREGL
1960 1970 1980 1990 2000
IAYMMNENFS RRSGPLSSSS ISSTSFPPSY DSVTRATSDN LPVRASDYSR
2010
SEDLADFPPS PDRDRESIV
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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 ENSGT00760000118827.
HOGENOMi HOG000231755.
InParanoidi Q9JJV9.
KOi K04838.
OrthoDBi EOG7DJSK9.
TreeFami TF323985.

Enzyme and pathway databases

Reactomei REACT_244931. Interaction between L1 and Ankyrins.

Miscellaneous databases

NextBioi 297947.
PROi Q9JJV9.
SOURCEi Search...

Gene expression databases

Bgeei Q9JJV9.
ExpressionAtlasi Q9JJV9. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 96 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