CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012324
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Sodium channel protein type 5 subunit alpha 
Protein Synonyms/Alias
 HH1; Sodium channel protein cardiac muscle subunit alpha; Sodium channel protein type V subunit alpha; Voltage-gated sodium channel subunit alpha Nav1.5 
Gene Name
 SCN5A 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
590PGHALHGKKNSTVDCubiquitination[1]
Reference
 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983] 
Functional Description
 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. This channel is responsible for the initial upstroke of the action potential. Channel inactivation is regulated by intracellular calcium levels. 
Sequence Annotation
 DOMAIN 1901 1930 IQ.
 REGION 1974 1977 Interaction with NEDD4, NEDD4L and WWP2.
 MOD_RES 513 513 Dimethylated arginine; alternate.
 MOD_RES 513 513 Omega-N-methylarginine; alternate.
 MOD_RES 526 526 Dimethylated arginine; alternate.
 MOD_RES 526 526 Omega-N-methylarginine; alternate.
 MOD_RES 680 680 Dimethylated arginine; alternate.
 MOD_RES 680 680 Omega-N-methylarginine; alternate.
 CARBOHYD 214 214 N-linked (GlcNAc...) (Potential).
 CARBOHYD 283 283 N-linked (GlcNAc...) (Potential).
 CARBOHYD 288 288 N-linked (GlcNAc...) (Potential).
 CARBOHYD 291 291 N-linked (GlcNAc...) (Potential).
 CARBOHYD 318 318 N-linked (GlcNAc...) (Potential).
 CARBOHYD 328 328 N-linked (GlcNAc...) (Potential).
 CARBOHYD 548 548 N-linked (GlcNAc...) (Potential).
 CARBOHYD 592 592 N-linked (GlcNAc...) (Potential).
 CARBOHYD 740 740 N-linked (GlcNAc...) (Potential).
 CARBOHYD 803 803 N-linked (GlcNAc...) (Potential).
 CARBOHYD 841 841 N-linked (GlcNAc...) (Potential).
 CARBOHYD 864 864 N-linked (GlcNAc...) (Potential).
 CARBOHYD 946 946 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1365 1365 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1374 1374 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1380 1380 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1388 1388 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1736 1736 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1774 1774 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1955 1955 N-linked (GlcNAc...) (Potential).  
Keyword
 3D-structure; Alternative splicing; Atrial fibrillation; Brugada syndrome; Calmodulin-binding; Cardiomyopathy; Complete proteome; Disease mutation; Glycoprotein; Ion channel; Ion transport; Long QT syndrome; Membrane; Methylation; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Sodium; Sodium channel; Sodium transport; Transmembrane; Transmembrane helix; Transport; Ubl conjugation; Voltage-gated channel. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2016 AA 
Protein Sequence
MANFLLPRGT SSFRRFTRES LAAIEKRMAE KQARGSTTLQ ESREGLPEEE APRPQLDLQA 60
SKKLPDLYGN PPQELIGEPL EDLDPFYSTQ KTFIVLNKGK TIFRFSATNA LYVLSPFHPI 120
RRAAVKILVH SLFNMLIMCT ILTNCVFMAQ HDPPPWTKYV EYTFTAIYTF ESLVKILARG 180
FCLHAFTFLR DPWNWLDFSV IIMAYTTEFV DLGNVSALRT FRVLRALKTI SVISGLKTIV 240
GALIQSVKKL ADVMVLTVFC LSVFALIGLQ LFMGNLRHKC VRNFTALNGT NGSVEADGLV 300
WESLDLYLSD PENYLLKNGT SDVLLCGNSS DAGTCPEGYR CLKAGENPDH GYTSFDSFAW 360
AFLALFRLMT QDCWERLYQQ TLRSAGKIYM IFFMLVIFLG SFYLVNLILA VVAMAYEEQN 420
QATIAETEEK EKRFQEAMEM LKKEHEALTI RGVDTVSRSS LEMSPLAPVN SHERRSKRRK 480
RMSSGTEECG EDRLPKSDSE DGPRAMNHLS LTRGLSRTSM KPRSSRGSIF TFRRRDLGSE 540
ADFADDENST AGESESHHTS LLVPWPLRRT SAQGQPSPGT SAPGHALHGK KNSTVDCNGV 600
VSLLGAGDPE ATSPGSHLLR PVMLEHPPDT TTPSEEPGGP QMLTSQAPCV DGFEEPGARQ 660
RALSAVSVLT SALEELEESR HKCPPCWNRL AQRYLIWECC PLWMSIKQGV KLVVMDPFTD 720
LTITMCIVLN TLFMALEHYN MTSEFEEMLQ VGNLVFTGIF TAEMTFKIIA LDPYYYFQQG 780
WNIFDSIIVI LSLMELGLSR MSNLSVLRSF RLLRVFKLAK SWPTLNTLIK IIGNSVGALG 840
NLTLVLAIIV FIFAVVGMQL FGKNYSELRD SDSGLLPRWH MMDFFHAFLI IFRILCGEWI 900
ETMWDCMEVS GQSLCLLVFL LVMVIGNLVV LNLFLALLLS SFSADNLTAP DEDREMNNLQ 960
LALARIQRGL RFVKRTTWDF CCGLLRQRPQ KPAALAAQGQ LPSCIATPYS PPPPETEKVP 1020
PTRKETRFEE GEQPGQGTPG DPEPVCVPIA VAESDTDDQE EDEENSLGTE EESSKQQESQ 1080
PVSGGPEAPP DSRTWSQVSA TASSEAEASA SQADWRQQWK AEPQAPGCGE TPEDSCSEGS 1140
TADMTNTAEL LEQIPDLGQD VKDPEDCFTE GCVRRCPCCA VDTTQAPGKV WWRLRKTCYH 1200
IVEHSWFETF IIFMILLSSG ALAFEDIYLE ERKTIKVLLE YADKMFTYVF VLEMLLKWVA 1260
YGFKKYFTNA WCWLDFLIVD VSLVSLVANT LGFAEMGPIK SLRTLRALRP LRALSRFEGM 1320
RVVVNALVGA IPSIMNVLLV CLIFWLIFSI MGVNLFAGKF GRCINQTEGD LPLNYTIVNN 1380
KSQCESLNLT GELYWTKVKV NFDNVGAGYL ALLQVATFKG WMDIMYAAVD SRGYEEQPQW 1440
EYNLYMYIYF VIFIIFGSFF TLNLFIGVII DNFNQQKKKL GGQDIFMTEE QKKYYNAMKK 1500
LGSKKPQKPI PRPLNKYQGF IFDIVTKQAF DVTIMFLICL NMVTMMVETD DQSPEKINIL 1560
AKINLLFVAI FTGECIVKLA ALRHYYFTNS WNIFDFVVVI LSIVGTVLSD IIQKYFFSPT 1620
LFRVIRLARI GRILRLIRGA KGIRTLLFAL MMSLPALFNI GLLLFLVMFI YSIFGMANFA 1680
YVKWEAGIDD MFNFQTFANS MLCLFQITTS AGWDGLLSPI LNTGPPYCDP TLPNSNGSRG 1740
DCGSPAVGIL FFTTYIIISF LIVVNMYIAI ILENFSVATE ESTEPLSEDD FDMFYEIWEK 1800
FDPEATQFIE YSVLSDFADA LSEPLRIAKP NQISLINMDL PMVSGDRIHC MDILFAFTKR 1860
VLGESGEMDA LKIQMEEKFM AANPSKISYE PITTTLRRKH EEVSAMVIQR AFRRHLLQRS 1920
LKHASFLFRQ QAGSGLSEED APEREGLIAY VMSENFSRPL GPPSSSSISS TSFPPSYDSV 1980
TRATSDNLQV RGSDYSHSED LADFPPSPDR DRESIV 2016 
Gene Ontology
 GO:0009986; C:cell surface; IDA:BHF-UCL.
 GO:0005783; C:endoplasmic reticulum; IDA:BHF-UCL.
 GO:0014704; C:intercalated disc; IDA:BHF-UCL.
 GO:0030315; C:T-tubule; IDA:BHF-UCL.
 GO:0001518; C:voltage-gated sodium channel complex; IDA:BHF-UCL.
 GO:0030506; F:ankyrin binding; IDA:BHF-UCL.
 GO:0086006; F:voltage-gated sodium channel activity involved in regulation of cardiac muscle cell action potential; IDA:BHF-UCL.
 GO:0086067; P:AV node cell to bundle of His cell communication; IMP:BHF-UCL.
 GO:0003360; P:brainstem development; ISS:BHF-UCL.
 GO:0086069; P:bundle of His cell to Purkinje myocyte communication; IMP:BHF-UCL.
 GO:0060048; P:cardiac muscle contraction; IMP:BHF-UCL.
 GO:0003231; P:cardiac ventricle development; ISS:BHF-UCL.
 GO:0071277; P:cellular response to calcium ion; IDA:UniProtKB.
 GO:0021549; P:cerebellum development; ISS:BHF-UCL.
 GO:0086046; P:membrane depolarization involved in regulation of SA node cell action potential; ISS:BHF-UCL.
 GO:0042475; P:odontogenesis of dentin-containing tooth; ISS:BHF-UCL.
 GO:0045760; P:positive regulation of action potential; ISS:BHF-UCL.
 GO:0050679; P:positive regulation of epithelial cell proliferation; ISS:BHF-UCL.
 GO:0010765; P:positive regulation of sodium ion transport; IDA:BHF-UCL.
 GO:0060371; P:regulation of atrial cardiac muscle cell membrane depolarization; IMP:BHF-UCL.
 GO:0060372; P:regulation of atrial cardiac muscle cell membrane repolarization; IMP:BHF-UCL.
 GO:0086091; P:regulation of heart rate by cardiac conduction; IMP:BHF-UCL.
 GO:0086005; P:regulation of ventricular cardiac muscle cell action potential; IMP:BHF-UCL.
 GO:0060373; P:regulation of ventricular cardiac muscle cell membrane depolarization; IMP:BHF-UCL.
 GO:0060307; P:regulation of ventricular cardiac muscle cell membrane repolarization; IMP:BHF-UCL.
 GO:0014894; P:response to denervation involved in regulation of muscle adaptation; ISS:BHF-UCL.
 GO:0021537; P:telencephalon development; ISS:BHF-UCL. 
Interpro
 IPR024583; DUF3451.
 IPR005821; Ion_trans_dom.
 IPR000048; IQ_motif_EF-hand-BS.
 IPR027359; K_channel_four-helix_dom.
 IPR008053; Na_channel_a5su.
 IPR001696; Na_channel_asu.
 IPR010526; Na_trans_assoc. 
Pfam
 PF11933; DUF3451
 PF00520; Ion_trans
 PF06512; Na_trans_assoc 
SMART
 SM00015; IQ 
PROSITE
 PS50096; IQ 
PRINTS
 PR00170; NACHANNEL.
 PR01666; NACHANNEL5.