UniProtKB - Q9JJV9 (SCN5A_MOUSE)
Sodium channel protein type 5 subunit alpha
Scn5a
Functioni
GO - Molecular functioni
- ankyrin binding Source: MGI
- calmodulin binding Source: MGI
- cation channel activity Source: GO_Central
- enzyme binding Source: MGI
- fibroblast growth factor binding Source: MGI
- ion channel binding Source: MGI
- nitric-oxide synthase binding Source: MGI
- protein domain specific binding Source: MGI
- protein kinase binding Source: MGI
- scaffold protein binding Source: BHF-UCL
- ubiquitin protein ligase binding Source: MGI
- voltage-gated ion channel activity Source: UniProtKB-KW
- voltage-gated sodium channel activity Source: MGI
- voltage-gated sodium channel activity involved in AV node cell action potential Source: MGI
- voltage-gated sodium channel activity involved in bundle of His cell action potential Source: MGI
- voltage-gated sodium channel activity involved in cardiac muscle cell action potential Source: MGI
- voltage-gated sodium channel activity involved in Purkinje myocyte action potential Source: MGI
- voltage-gated sodium channel activity involved in SA node cell action potential Source: MGI
GO - Biological processi
- atrial cardiac muscle cell action potential Source: MGI
- AV node cell action potential Source: MGI
- AV node cell to bundle of His cell communication Source: MGI
- bundle of His cell action potential Source: MGI
- cardiac muscle cell action potential involved in contraction Source: MGI
- cardiac muscle contraction Source: MGI
- cardiac ventricle development Source: MGI
- cell communication involved in cardiac conduction Source: MGI
- cellular response to calcium ion Source: UniProtKB
- membrane depolarization Source: MGI
- membrane depolarization during action potential Source: MGI
- membrane depolarization during atrial cardiac muscle cell action potential Source: MGI
- membrane depolarization during AV node cell action potential Source: MGI
- membrane depolarization during bundle of His cell action potential Source: MGI
- membrane depolarization during cardiac muscle cell action potential Source: MGI
- membrane depolarization during Purkinje myocyte cell action potential Source: MGI
- membrane depolarization during SA node cell action potential Source: MGI
- neuronal action potential Source: GO_Central
- positive regulation of action potential Source: MGI
- positive regulation of epithelial cell proliferation Source: MGI
- positive regulation of heart rate Source: MGI
- positive regulation of sodium ion transport Source: MGI
- regulation of atrial cardiac muscle cell membrane depolarization Source: MGI
- regulation of atrial cardiac muscle cell membrane repolarization Source: MGI
- regulation of cardiac muscle cell contraction Source: MGI
- regulation of heart rate Source: MGI
- regulation of heart rate by cardiac conduction Source: MGI
- regulation of sodium ion transmembrane transport Source: MGI
- regulation of ventricular cardiac muscle cell membrane depolarization Source: MGI
- regulation of ventricular cardiac muscle cell membrane repolarization Source: MGI
- response to denervation involved in regulation of muscle adaptation Source: MGI
- response to organic cyclic compound Source: MGI
- SA node cell action potential Source: MGI
- sodium ion import across plasma membrane Source: MGI
- sodium ion transmembrane transport Source: MGI
- sodium ion transport Source: MGI
- ventricular cardiac muscle cell action potential Source: MGI
Keywordsi
Molecular function | Calmodulin-binding, Ion channel, Sodium channel, Voltage-gated channel |
Biological process | Ion transport, Sodium transport, Transport |
Ligand | Sodium |
Enzyme and pathway databases
Reactomei | R-MMU-5576892, Phase 0 - rapid depolarisation |
Names & Taxonomyi
Protein namesi | Recommended name: Sodium channel protein type 5 subunit alphaAlternative 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 |
Organismi | Mus musculus (Mouse) |
Taxonomic identifieri | 10090 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus |
Proteomesi |
|
Organism-specific databases
MGIi | MGI:98251, Scn5a |
Subcellular locationi
Plasma membrane
- Cell membrane 2 Publications; Multi-pass membrane protein By similarity
- T-tubule By similarity
Other locations
- perinuclear region By similarity
Note: RANGRF promotes trafficking to the cell membrane.1 Publication
Endoplasmic reticulum
- endoplasmic reticulum Source: MGI
Nucleus
- nucleolus Source: MGI
- nucleoplasm Source: MGI
Plasma Membrane
- caveola Source: MGI
- lateral plasma membrane Source: BHF-UCL
- plasma membrane Source: MGI
- sarcolemma Source: MGI
- T-tubule Source: MGI
- voltage-gated sodium channel complex Source: MGI
Other locations
- cell surface Source: BHF-UCL
- integral component of membrane Source: UniProtKB
- intercalated disc Source: BHF-UCL
- perinuclear region of cytoplasm Source: UniProtKB-SubCell
- sodium channel complex Source: MGI
- Z disc Source: MGI
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 1 – 131 | CytoplasmicCuratedAdd BLAST | 131 | |
Transmembranei | 132 – 150 | Helical; Name=S1 of repeat IBy similarityAdd BLAST | 19 | |
Topological domaini | 151 – 157 | ExtracellularCurated | 7 | |
Transmembranei | 158 – 178 | Helical; Name=S2 of repeat IBy similarityAdd BLAST | 21 | |
Topological domaini | 179 – 192 | CytoplasmicCuratedAdd BLAST | 14 | |
Transmembranei | 193 – 210 | Helical; Name=S3 of repeat IBy similarityAdd BLAST | 18 | |
Topological domaini | 211 – 216 | ExtracellularCurated | 6 | |
Transmembranei | 217 – 233 | Helical; Name=S4 of repeat IBy similarityAdd BLAST | 17 | |
Topological domaini | 234 – 252 | CytoplasmicCuratedAdd BLAST | 19 | |
Transmembranei | 253 – 272 | Helical; Name=S5 of repeat IBy similarityAdd BLAST | 20 | |
Topological domaini | 273 – 357 | ExtracellularCuratedAdd BLAST | 85 | |
Intramembranei | 358 – 382 | Pore-formingBy similarityAdd BLAST | 25 | |
Topological domaini | 383 – 389 | ExtracellularCurated | 7 | |
Transmembranei | 390 – 410 | Helical; Name=S6 of repeat IBy similarityAdd BLAST | 21 | |
Topological domaini | 411 – 717 | CytoplasmicCuratedAdd BLAST | 307 | |
Transmembranei | 718 – 736 | Helical; Name=S1 of repeat IIBy similarityAdd BLAST | 19 | |
Topological domaini | 737 – 747 | ExtracellularCuratedAdd BLAST | 11 | |
Transmembranei | 748 – 767 | Helical; Name=S2 of repeat IIBy similarityAdd BLAST | 20 | |
Topological domaini | 768 – 781 | CytoplasmicCuratedAdd BLAST | 14 | |
Transmembranei | 782 – 801 | Helical; Name=S3 of repeat IIBy similarityAdd BLAST | 20 | |
Topological domaini | 802 – 803 | ExtracellularCurated | 2 | |
Transmembranei | 804 – 821 | Helical; Name=S4 of repeat IIBy similarityAdd BLAST | 18 | |
Topological domaini | 822 – 837 | CytoplasmicCuratedAdd BLAST | 16 | |
Transmembranei | 838 – 856 | Helical; Name=S5 of repeat IIBy similarityAdd BLAST | 19 | |
Topological domaini | 857 – 885 | ExtracellularCuratedAdd BLAST | 29 | |
Intramembranei | 886 – 906 | Pore-formingBy similarityAdd BLAST | 21 | |
Topological domaini | 907 – 919 | ExtracellularCuratedAdd BLAST | 13 | |
Transmembranei | 920 – 940 | Helical; Name=S6 of repeat IIBy similarityAdd BLAST | 21 | |
Topological domaini | 941 – 1208 | CytoplasmicCuratedAdd BLAST | 268 | |
Transmembranei | 1209 – 1226 | Helical; Name=S1 of repeat IIIBy similarityAdd BLAST | 18 | |
Topological domaini | 1227 – 1239 | ExtracellularCuratedAdd BLAST | 13 | |
Transmembranei | 1240 – 1258 | Helical; Name=S2 of repeat IIIBy similarityAdd BLAST | 19 | |
Topological domaini | 1259 – 1272 | CytoplasmicCuratedAdd BLAST | 14 | |
Transmembranei | 1273 – 1291 | Helical; Name=S3 of repeat IIIBy similarityAdd BLAST | 19 | |
Topological domaini | 1292 – 1299 | ExtracellularCurated | 8 | |
Transmembranei | 1300 – 1318 | Helical; Name=S4 of repeat IIIBy similarityAdd BLAST | 19 | |
Topological domaini | 1319 – 1335 | CytoplasmicCuratedAdd BLAST | 17 | |
Transmembranei | 1336 – 1355 | Helical; Name=S5 of repeat IIIBy similarityAdd BLAST | 20 | |
Topological domaini | 1356 – 1407 | ExtracellularCuratedAdd BLAST | 52 | |
Intramembranei | 1408 – 1429 | Pore-formingBy similarityAdd BLAST | 22 | |
Topological domaini | 1430 – 1446 | ExtracellularCuratedAdd BLAST | 17 | |
Transmembranei | 1447 – 1468 | Helical; Name=S6 of repeat IIIBy similarityAdd BLAST | 22 | |
Topological domaini | 1469 – 1531 | CytoplasmicCuratedAdd BLAST | 63 | |
Transmembranei | 1532 – 1549 | Helical; Name=S1 of repeat IVBy similarityAdd BLAST | 18 | |
Topological domaini | 1550 – 1560 | ExtracellularCuratedAdd BLAST | 11 | |
Transmembranei | 1561 – 1579 | Helical; Name=S2 of repeat IVBy similarityAdd BLAST | 19 | |
Topological domaini | 1580 – 1591 | CytoplasmicCuratedAdd BLAST | 12 | |
Transmembranei | 1592 – 1609 | Helical; Name=S3 of repeat IVBy similarityAdd BLAST | 18 | |
Topological domaini | 1610 – 1622 | ExtracellularCuratedAdd BLAST | 13 | |
Transmembranei | 1623 – 1639 | Helical; Name=S4 of repeat IVBy similarityAdd BLAST | 17 | |
Topological domaini | 1640 – 1658 | CytoplasmicCuratedAdd BLAST | 19 | |
Transmembranei | 1659 – 1676 | Helical; Name=S5 of repeat IVBy similarityAdd BLAST | 18 | |
Topological domaini | 1677 – 1698 | ExtracellularCuratedAdd BLAST | 22 | |
Intramembranei | 1699 – 1721 | Pore-formingBy similarityAdd BLAST | 23 | |
Topological domaini | 1722 – 1750 | ExtracellularCuratedAdd BLAST | 29 | |
Transmembranei | 1751 – 1773 | Helical; Name=S6 of repeat IVBy similarityAdd BLAST | 23 | |
Topological domaini | 1774 – 2019 | CytoplasmicCuratedAdd BLAST | 246 |
Keywords - Cellular componenti
Cell membrane, Cytoplasm, MembranePTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000376895 | 1 – 2019 | Sodium channel protein type 5 subunit alphaAdd BLAST | 2019 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 36 | PhosphoserineBy similarity | 1 | |
Modified residuei | 38 | PhosphothreonineBy similarity | 1 | |
Glycosylationi | 214 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 280 ↔ 335 | By similarity | ||
Glycosylationi | 283 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 288 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 291 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 318 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 328 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Modified residuei | 457 | PhosphoserineCombined sources | 1 | |
Modified residuei | 460 | PhosphoserineBy similarity | 1 | |
Modified residuei | 483 | PhosphoserineBy similarity | 1 | |
Modified residuei | 484 | PhosphoserineCombined sources | 1 | |
Modified residuei | 486 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 497 | PhosphoserineBy similarity | 1 | |
Modified residuei | 510 | PhosphoserineBy similarity | 1 | |
Modified residuei | 526 | Dimethylated arginine; alternateBy similarity | 1 | |
Modified residuei | 526 | Omega-N-methylarginine; alternateCombined sources | 1 | |
Modified residuei | 539 | PhosphoserineCombined sources | 1 | |
Modified residuei | 571 | PhosphoserineBy similarity | 1 | |
Modified residuei | 664 | PhosphoserineBy similarity | 1 | |
Modified residuei | 667 | PhosphoserineBy similarity | 1 | |
Glycosylationi | 740 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 803 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 864 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 908 ↔ 917 | By similarity | ||
Glycosylationi | 1367 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 1376 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 1382 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 1390 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Modified residuei | 1505 | Phosphoserine; by PKCBy similarity | 1 |
Post-translational modificationi
Keywords - PTMi
Disulfide bond, Glycoprotein, Methylation, Phosphoprotein, Ubl conjugationProteomic databases
CPTACi | non-CPTAC-4004 |
PaxDbi | Q9JJV9 |
PRIDEi | Q9JJV9 |
PTM databases
GlyGeni | Q9JJV9, 13 sites |
iPTMneti | Q9JJV9 |
PhosphoSitePlusi | Q9JJV9 |
Expressioni
Tissue specificityi
Gene expression databases
Bgeei | ENSMUSG00000032511, Expressed in heart and 162 other tissues |
ExpressionAtlasi | Q9JJV9, baseline and differential |
Genevisiblei | Q9JJV9, MM |
Interactioni
Subunit structurei
Interacts with the PDZ domain of the syntrophin SNTA1, SNTB1 and SNTB2 (PubMed:9412493).
Interacts with NEDD4, NEDD4L, WWP2 and GPD1L (By similarity).
Interacts with CALM (By similarity).
Interacts with FGF13; the interaction is direct and may regulate SNC5A density at membranes and function (PubMed:21817159).
Interacts with FGF12 and FGF14 (By similarity).
Interacts with ANK3 (By similarity).
By similarity2 PublicationsGO - Molecular functioni
- ankyrin binding Source: MGI
- calmodulin binding Source: MGI
- enzyme binding Source: MGI
- fibroblast growth factor binding Source: MGI
- ion channel binding Source: MGI
- nitric-oxide synthase binding Source: MGI
- protein domain specific binding Source: MGI
- protein kinase binding Source: MGI
- scaffold protein binding Source: BHF-UCL
- ubiquitin protein ligase binding Source: MGI
Protein-protein interaction databases
BioGRIDi | 203101, 14 interactors |
DIPi | DIP-46142N |
IntActi | Q9JJV9, 4 interactors |
MINTi | Q9JJV9 |
STRINGi | 10090.ENSMUSP00000112838 |
Miscellaneous databases
RNActi | Q9JJV9, protein |
Structurei
3D structure databases
BMRBi | Q9JJV9 |
ModBasei | Search... |
SWISS-MODEL-Workspacei | Submit a new modelling project... |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Repeati | 113 – 420 | ICuratedAdd BLAST | 308 | |
Repeati | 699 – 971 | IICuratedAdd BLAST | 273 | |
Repeati | 1189 – 1503 | IIICuratedAdd BLAST | 315 | |
Repeati | 1512 – 1809 | IVCuratedAdd BLAST | 298 | |
Domaini | 1903 – 1932 | IQAdd BLAST | 30 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 1841 – 1903 | Interaction with FGF13By similarityAdd BLAST | 63 | |
Regioni | 1977 – 1980 | Interaction with NEDD4, NEDD4L and WWP2By similarity | 4 |
Domaini
Sequence similaritiesi
Keywords - Domaini
Repeat, Transmembrane, Transmembrane helixPhylogenomic databases
eggNOGi | KOG2301, Eukaryota |
GeneTreei | ENSGT00940000161691 |
InParanoidi | Q9JJV9 |
OrthoDBi | 172471at2759 |
TreeFami | TF323985 |
Family and domain databases
Gene3Di | 1.20.120.350, 4 hits |
InterProi | View protein in InterPro IPR005821, Ion_trans_dom IPR008053, Na_channel_a5su IPR001696, Na_channel_asu IPR010526, Na_trans_assoc IPR024583, Na_trans_cytopl IPR043203, VGCC_Ca_Na IPR027359, Volt_channel_dom_sf |
PANTHERi | PTHR10037, PTHR10037, 1 hit |
Pfami | View protein in Pfam PF00520, Ion_trans, 4 hits PF06512, Na_trans_assoc, 1 hit PF11933, Na_trans_cytopl, 1 hit |
PRINTSi | PR00170, NACHANNEL PR01666, NACHANNEL5 |
s (2+)i Sequence
Sequence statusi: Complete.
This entry describes 2 produced by isoformsialternative splicing. AlignAdd to basketThis entry has 2 described isoforms and 3 potential isoforms that are computationally mapped.Show allAlign All
This isoform has been chosen as the sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. canonicali
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
Computationally mapped potential isoform sequencesi
There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketA0A0R4J1M7 | A0A0R4J1M7_MOUSE | Sodium channel protein | Scn5a | 2,020 | Annotation score: | ||
K3W4N7 | K3W4N7_MOUSE | Sodium channel protein | Scn5a | 2,020 | Annotation score: | ||
D3YXW2 | D3YXW2_MOUSE | Sodium channel protein type 5 subun... | Scn5a | 29 | Annotation score: |
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 215 | V → L in BAE27966 (PubMed:16141072).Curated | 1 | |
Sequence conflicti | 215 | V → L in BAE27800 (PubMed:16141072).Curated | 1 | |
Sequence conflicti | 234 | S → P in BAE27966 (PubMed:16141072).Curated | 1 | |
Sequence conflicti | 234 | S → P in BAE27800 (PubMed:16141072).Curated | 1 | |
Sequence conflicti | 1008 – 1009 | AA → TT in CAB70096 (PubMed:11834499).Curated | 2 | |
Sequence conflicti | 1078 | K → KQ in BAE27966 (PubMed:16141072).Curated | 1 | |
Sequence conflicti | 1078 | K → KQ in BAE27800 (PubMed:16141072).Curated | 1 | |
Sequence conflicti | 1133 | T → S in CAB70096 (PubMed:11834499).Curated | 1 |
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_037444 | 206 – 211 | TTEFVD → VSENIK in isoform 2. 1 Publication | 6 |
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 |
Genome annotation databases
Ensembli | ENSMUST00000120420; ENSMUSP00000113272; ENSMUSG00000032511 [Q9JJV9-1] |
GeneIDi | 20271 |
KEGGi | mmu:20271 |
UCSCi | uc009sbc.2, mouse [Q9JJV9-2] |
Keywords - Coding sequence diversityi
Alternative splicingSimilar proteinsi
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 |
3D structure databases
BMRBi | Q9JJV9 |
ModBasei | Search... |
SWISS-MODEL-Workspacei | Submit a new modelling project... |
Protein-protein interaction databases
BioGRIDi | 203101, 14 interactors |
DIPi | DIP-46142N |
IntActi | Q9JJV9, 4 interactors |
MINTi | Q9JJV9 |
STRINGi | 10090.ENSMUSP00000112838 |
PTM databases
GlyGeni | Q9JJV9, 13 sites |
iPTMneti | Q9JJV9 |
PhosphoSitePlusi | Q9JJV9 |
Proteomic databases
CPTACi | non-CPTAC-4004 |
PaxDbi | Q9JJV9 |
PRIDEi | Q9JJV9 |
Protocols and materials databases
ABCDi | Q9JJV9, 2 sequenced antibodies |
Antibodypediai | 6411, 307 antibodies |
Genome annotation databases
Ensembli | ENSMUST00000120420; ENSMUSP00000113272; ENSMUSG00000032511 [Q9JJV9-1] |
GeneIDi | 20271 |
KEGGi | mmu:20271 |
UCSCi | uc009sbc.2, mouse [Q9JJV9-2] |
Organism-specific databases
CTDi | 6331 |
MGIi | MGI:98251, Scn5a |
Phylogenomic databases
eggNOGi | KOG2301, Eukaryota |
GeneTreei | ENSGT00940000161691 |
InParanoidi | Q9JJV9 |
OrthoDBi | 172471at2759 |
TreeFami | TF323985 |
Enzyme and pathway databases
Reactomei | R-MMU-5576892, Phase 0 - rapid depolarisation |
Miscellaneous databases
BioGRID-ORCSi | 20271, 2 hits in 17 CRISPR screens |
PROi | PR:Q9JJV9 |
RNActi | Q9JJV9, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSMUSG00000032511, Expressed in heart and 162 other tissues |
ExpressionAtlasi | Q9JJV9, baseline and differential |
Genevisiblei | Q9JJV9, MM |
Family and domain databases
Gene3Di | 1.20.120.350, 4 hits |
InterProi | View protein in InterPro IPR005821, Ion_trans_dom IPR008053, Na_channel_a5su IPR001696, Na_channel_asu IPR010526, Na_trans_assoc IPR024583, Na_trans_cytopl IPR043203, VGCC_Ca_Na IPR027359, Volt_channel_dom_sf |
PANTHERi | PTHR10037, PTHR10037, 1 hit |
Pfami | View protein in Pfam PF00520, Ion_trans, 4 hits PF06512, Na_trans_assoc, 1 hit PF11933, Na_trans_cytopl, 1 hit |
PRINTSi | PR00170, NACHANNEL PR01666, NACHANNEL5 |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | SCN5A_MOUSE | |
Accessioni | Q9JJV9Primary (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: | December 2, 2020 | |
This is version 145 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- MGD cross-references
Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot - SIMILARITY comments
Index of protein domains and families