SCN5A_HUMAN - dbPTM
SCN5A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SCN5A_HUMAN
UniProt AC Q14524
Protein Name Sodium channel protein type 5 subunit alpha
Gene Name SCN5A
Organism Homo sapiens (Human).
Sequence Length 2016
Subcellular Localization Cell membrane
Multi-pass membrane protein . Cytoplasm, perinuclear region . RANGRF promotes trafficking to the cell membrane.
Protein 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. [PubMed: 1309946]
Protein Sequence MANFLLPRGTSSFRRFTRESLAAIEKRMAEKQARGSTTLQESREGLPEEEAPRPQLDLQASKKLPDLYGNPPQELIGEPLEDLDPFYSTQKTFIVLNKGKTIFRFSATNALYVLSPFHPIRRAAVKILVHSLFNMLIMCTILTNCVFMAQHDPPPWTKYVEYTFTAIYTFESLVKILARGFCLHAFTFLRDPWNWLDFSVIIMAYTTEFVDLGNVSALRTFRVLRALKTISVISGLKTIVGALIQSVKKLADVMVLTVFCLSVFALIGLQLFMGNLRHKCVRNFTALNGTNGSVEADGLVWESLDLYLSDPENYLLKNGTSDVLLCGNSSDAGTCPEGYRCLKAGENPDHGYTSFDSFAWAFLALFRLMTQDCWERLYQQTLRSAGKIYMIFFMLVIFLGSFYLVNLILAVVAMAYEEQNQATIAETEEKEKRFQEAMEMLKKEHEALTIRGVDTVSRSSLEMSPLAPVNSHERRSKRRKRMSSGTEECGEDRLPKSDSEDGPRAMNHLSLTRGLSRTSMKPRSSRGSIFTFRRRDLGSEADFADDENSTAGESESHHTSLLVPWPLRRTSAQGQPSPGTSAPGHALHGKKNSTVDCNGVVSLLGAGDPEATSPGSHLLRPVMLEHPPDTTTPSEEPGGPQMLTSQAPCVDGFEEPGARQRALSAVSVLTSALEELEESRHKCPPCWNRLAQRYLIWECCPLWMSIKQGVKLVVMDPFTDLTITMCIVLNTLFMALEHYNMTSEFEEMLQVGNLVFTGIFTAEMTFKIIALDPYYYFQQGWNIFDSIIVILSLMELGLSRMSNLSVLRSFRLLRVFKLAKSWPTLNTLIKIIGNSVGALGNLTLVLAIIVFIFAVVGMQLFGKNYSELRDSDSGLLPRWHMMDFFHAFLIIFRILCGEWIETMWDCMEVSGQSLCLLVFLLVMVIGNLVVLNLFLALLLSSFSADNLTAPDEDREMNNLQLALARIQRGLRFVKRTTWDFCCGLLRQRPQKPAALAAQGQLPSCIATPYSPPPPETEKVPPTRKETRFEEGEQPGQGTPGDPEPVCVPIAVAESDTDDQEEDEENSLGTEEESSKQQESQPVSGGPEAPPDSRTWSQVSATASSEAEASASQADWRQQWKAEPQAPGCGETPEDSCSEGSTADMTNTAELLEQIPDLGQDVKDPEDCFTEGCVRRCPCCAVDTTQAPGKVWWRLRKTCYHIVEHSWFETFIIFMILLSSGALAFEDIYLEERKTIKVLLEYADKMFTYVFVLEMLLKWVAYGFKKYFTNAWCWLDFLIVDVSLVSLVANTLGFAEMGPIKSLRTLRALRPLRALSRFEGMRVVVNALVGAIPSIMNVLLVCLIFWLIFSIMGVNLFAGKFGRCINQTEGDLPLNYTIVNNKSQCESLNLTGELYWTKVKVNFDNVGAGYLALLQVATFKGWMDIMYAAVDSRGYEEQPQWEYNLYMYIYFVIFIIFGSFFTLNLFIGVIIDNFNQQKKKLGGQDIFMTEEQKKYYNAMKKLGSKKPQKPIPRPLNKYQGFIFDIVTKQAFDVTIMFLICLNMVTMMVETDDQSPEKINILAKINLLFVAIFTGECIVKLAALRHYYFTNSWNIFDFVVVILSIVGTVLSDIIQKYFFSPTLFRVIRLARIGRILRLIRGAKGIRTLLFALMMSLPALFNIGLLLFLVMFIYSIFGMANFAYVKWEAGIDDMFNFQTFANSMLCLFQITTSAGWDGLLSPILNTGPPYCDPTLPNSNGSRGDCGSPAVGILFFTTYIIISFLIVVNMYIAIILENFSVATEESTEPLSEDDFDMFYEIWEKFDPEATQFIEYSVLSDFADALSEPLRIAKPNQISLINMDLPMVSGDRIHCMDILFAFTKRVLGESGEMDALKIQMEEKFMAANPSKISYEPITTTLRRKHEEVSAMVIQRAFRRHLLQRSLKHASFLFRQQAGSGLSEEDAPEREGLIAYVMSENFSRPLGPPSSSSISSTSFPPSYDSVTRATSDNLQVRGSDYSHSEDLADFPPSPDRDRESIV
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
11PhosphorylationFLLPRGTSSFRRFTR
CCCCCCCHHHHHHHH		30.24-
12PhosphorylationLLPRGTSSFRRFTRE
CCCCCCHHHHHHHHH		23.70-
17PhosphorylationTSSFRRFTRESLAAI
CHHHHHHHHHHHHHH		31.54-
20PhosphorylationFRRFTRESLAAIEKR
HHHHHHHHHHHHHHH		21.73-
36PhosphorylationAEKQARGSTTLQESR
HHHHHCCCCCHHHHH		16.8022210691
37PhosphorylationEKQARGSTTLQESRE
HHHHCCCCCHHHHHC		34.0622210691
38PhosphorylationKQARGSTTLQESREG
HHHCCCCCHHHHHCC		28.3023092124
42PhosphorylationGSTTLQESREGLPEE
CCCCHHHHHCCCCCC		23.7522210691
61PhosphorylationPQLDLQASKKLPDLY
CCCCHHHHHCCHHHH		19.8422210691
101PhosphorylationIVLNKGKTIFRFSAT
EEECCCCEEEEEECC		33.73-
214N-linked_GlycosylationTEFVDLGNVSALRTF
CCCCCCCCHHHHHHH		31.69UniProtKB CARBOHYD
231PhosphorylationLRALKTISVISGLKT
HHHHHHHHHHHCHHH		20.73-
283N-linked_GlycosylationLRHKCVRNFTALNGT
CHHHHHHCCCCCCCC		20.44UniProtKB CARBOHYD
288N-linked_GlycosylationVRNFTALNGTNGSVE
HHCCCCCCCCCCCEE		53.42UniProtKB CARBOHYD
291N-linked_GlycosylationFTALNGTNGSVEADG
CCCCCCCCCCEEECC		41.98UniProtKB CARBOHYD
318N-linked_GlycosylationPENYLLKNGTSDVLL
HHHHCCCCCCCCEEE		59.97UniProtKB CARBOHYD
328N-linked_GlycosylationSDVLLCGNSSDAGTC
CCEEECCCCCCCCCC		37.03UniProtKB CARBOHYD
329PhosphorylationDVLLCGNSSDAGTCP
CEEECCCCCCCCCCC		18.1922210691
330PhosphorylationVLLCGNSSDAGTCPE
EEECCCCCCCCCCCC		35.1622210691
334PhosphorylationGNSSDAGTCPEGYRC
CCCCCCCCCCCCCCE		26.9722210691
343AcetylationPEGYRCLKAGENPDH
CCCCCEECCCCCCCC		58.9518530527
455PhosphorylationLTIRGVDTVSRSSLE
HHHCCCCCCCCCCCC		20.2727732954
457PhosphorylationIRGVDTVSRSSLEMS
HCCCCCCCCCCCCCC		28.6527732954
459PhosphorylationGVDTVSRSSLEMSPL
CCCCCCCCCCCCCCC		31.5927732954
460PhosphorylationVDTVSRSSLEMSPLA
CCCCCCCCCCCCCCC		27.5227732954
464PhosphorylationSRSSLEMSPLAPVNS
CCCCCCCCCCCCCCH		13.8523312004
471PhosphorylationSPLAPVNSHERRSKR
CCCCCCCHHHHHHHH		27.2723312004
476PhosphorylationVNSHERRSKRRKRMS
CCHHHHHHHHHHHCC		36.41-
483PhosphorylationSKRRKRMSSGTEECG
HHHHHHCCCCCCCCC		29.6426657352
484PhosphorylationKRRKRMSSGTEECGE
HHHHHCCCCCCCCCC		40.1526657352
486PhosphorylationRKRMSSGTEECGEDR
HHHCCCCCCCCCCCC		30.4725690035
497PhosphorylationGEDRLPKSDSEDGPR
CCCCCCCCCCCCCHH		44.4226074081
499PhosphorylationDRLPKSDSEDGPRAM
CCCCCCCCCCCHHHH		44.6826074081
510PhosphorylationPRAMNHLSLTRGLSR
HHHHHHHHCCCCCCC		21.8326074081
512PhosphorylationAMNHLSLTRGLSRTS
HHHHHHCCCCCCCCC		21.2226074081
513DimethylationMNHLSLTRGLSRTSM
HHHHHCCCCCCCCCC		49.72-
513MethylationMNHLSLTRGLSRTSM
HHHHHCCCCCCCCCC		49.7221726068
516PhosphorylationLSLTRGLSRTSMKPR
HHCCCCCCCCCCCCC		36.0126074081
519PhosphorylationTRGLSRTSMKPRSSR
CCCCCCCCCCCCCCC		24.5721712546
524PhosphorylationRTSMKPRSSRGSIFT
CCCCCCCCCCCCEEE		32.68-
525PhosphorylationTSMKPRSSRGSIFTF
CCCCCCCCCCCEEEE		41.7712242273
526MethylationSMKPRSSRGSIFTFR
CCCCCCCCCCEEEEE		44.0921726068
528PhosphorylationKPRSSRGSIFTFRRR
CCCCCCCCEEEEEEC		17.2612242273
531PhosphorylationSSRGSIFTFRRRDLG
CCCCCEEEEEECCCC		17.98-
539PhosphorylationFRRRDLGSEADFADD
EEECCCCCCCCCCCC		36.59-
570PhosphorylationVPWPLRRTSAQGQPS
EECCCCCCCCCCCCC		23.2123312004
571PhosphorylationPWPLRRTSAQGQPSP
ECCCCCCCCCCCCCC		19.4523312004
577PhosphorylationTSAQGQPSPGTSAPG
CCCCCCCCCCCCCCC		28.2427732954
580PhosphorylationQGQPSPGTSAPGHAL
CCCCCCCCCCCCCCC		25.7127732954
581PhosphorylationGQPSPGTSAPGHALH
CCCCCCCCCCCCCCC		38.0823312004
590UbiquitinationPGHALHGKKNSTVDC
CCCCCCCCCCCCCCC		37.7321906983
590UbiquitinationPGHALHGKKNSTVDC
CCCCCCCCCCCCCCC		37.732190698
590 (in isoform 1)Ubiquitination-37.7321906983
590 (in isoform 2)Ubiquitination-37.7321906983
590 (in isoform 3)Ubiquitination-37.7321906983
590 (in isoform 4)Ubiquitination-37.7321906983
590 (in isoform 5)Ubiquitination-37.7321906983
590 (in isoform 6)Ubiquitination-37.7321906983
594PhosphorylationLHGKKNSTVDCNGVV
CCCCCCCCCCCCCHH		29.7422514276
664PhosphorylationGARQRALSAVSVLTS
CHHHHHHHHHHHHHH		26.1627732954
667PhosphorylationQRALSAVSVLTSALE
HHHHHHHHHHHHHHH		15.8927732954
670PhosphorylationLSAVSVLTSALEELE
HHHHHHHHHHHHHHH		15.1427732954
671PhosphorylationSAVSVLTSALEELEE
HHHHHHHHHHHHHHH		27.0527732954
680MethylationLEELEESRHKCPPCW
HHHHHHHHHCCCHHH		36.2421726068
694PhosphorylationWNRLAQRYLIWECCP
HHHHHHHHHHHHHCH		7.1722461510
740N-linked_GlycosylationFMALEHYNMTSEFEE
HHHHHHCCCCHHHHH		29.21UniProtKB CARBOHYD
803N-linked_GlycosylationLGLSRMSNLSVLRSF
HCCCCCCCHHHHHHH		27.30UniProtKB CARBOHYD
805PhosphorylationLSRMSNLSVLRSFRL
CCCCCCHHHHHHHHH		24.2924719451
864N-linked_GlycosylationGMQLFGKNYSELRDS
HHHHHCCCHHHHHCC		46.04UniProtKB CARBOHYD
981S-palmitoylationKRTTWDFCCGLLRQR
HHCHHHHHHHHHHHC		1.3427337590
1003PhosphorylationAAQGQLPSCIATPYS
HHCCCCCCCEECCCC		27.09-
1079PhosphorylationESSKQQESQPVSGGP
HHHHHCCCCCCCCCC		35.1323663014
1083PhosphorylationQQESQPVSGGPEAPP
HCCCCCCCCCCCCCC		44.7223663014
1094PhosphorylationEAPPDSRTWSQVSAT
CCCCCCCCHHCEECC		33.16-
1103PhosphorylationSQVSATASSEAEASA
HCEECCCCCHHHHHH		25.1022817900
1104PhosphorylationQVSATASSEAEASAS
CEECCCCCHHHHHHH		38.0622817900
1176S-palmitoylationTEGCVRRCPCCAVDT
CCCCHHHCCEEEEEC		1.8027337590
1178S-palmitoylationGCVRRCPCCAVDTTQ
CCHHHCCEEEEECCC		2.3927337590
1179S-palmitoylationCVRRCPCCAVDTTQA
CHHHCCEEEEECCCC		2.2027337590
1261PhosphorylationMLLKWVAYGFKKYFT
HHHHHHHHHHHHHHC		17.30-
1266PhosphorylationVAYGFKKYFTNAWCW
HHHHHHHHHCCHHHH		19.0722210691
1268PhosphorylationYGFKKYFTNAWCWLD
HHHHHHHCCHHHHHH		22.4222210691
1365N-linked_GlycosylationGKFGRCINQTEGDLP
CCCCHHHCCCCCCCC		46.47UniProtKB CARBOHYD
1374N-linked_GlycosylationTEGDLPLNYTIVNNK
CCCCCCCEEEEECCH		29.93UniProtKB CARBOHYD
1380N-linked_GlycosylationLNYTIVNNKSQCESL
CEEEEECCHHHCEEC		34.17UniProtKB CARBOHYD
1388N-linked_GlycosylationKSQCESLNLTGELYW
HHHCEECCCCCEEEE		44.85UniProtKB CARBOHYD
1479AcetylationNFNQQKKKLGGQDIF
CCHHHHHHHCCCCCC		60.44126089611
1493AcetylationFMTEEQKKYYNAMKK
CCCHHHHHHHHHHHH		53.3030592225
1494PhosphorylationMTEEQKKYYNAMKKL
CCHHHHHHHHHHHHH		14.6922817900
1495PhosphorylationTEEQKKYYNAMKKLG
CHHHHHHHHHHHHHC		12.8122817900
1503PhosphorylationNAMKKLGSKKPQKPI
HHHHHHCCCCCCCCC		48.2010532948
1736N-linked_GlycosylationDPTLPNSNGSRGDCG
CCCCCCCCCCCCCCC		60.13UniProtKB CARBOHYD
1832UbiquitinationLRIAKPNQISLINMD
HHCCCCCCEEEEECC		34.86-
1865PhosphorylationTKRVLGESGEMDALK
HHHHHCCCCCCCHHH		37.95-
1885PhosphorylationKFMAANPSKISYEPI
HHHHCCCCCCCCCCC		42.29-
1885 (in isoform 2)Ubiquitination-42.29-
1895PhosphorylationSYEPITTTLRRKHEE
CCCCCCHHHHHHHHH		15.04-
1920PhosphorylationRRHLLQRSLKHASFL
HHHHHHHHHHHHHHH		28.89-
1925PhosphorylationQRSLKHASFLFRQQA
HHHHHHHHHHHHHCC		23.3823312004
1934PhosphorylationLFRQQAGSGLSEEDA
HHHHCCCCCCCCCCC		39.31-
1937PhosphorylationQQAGSGLSEEDAPER
HCCCCCCCCCCCCCC		42.33-
1985PhosphorylationDSVTRATSDNLQVRG
CCCCEECCCCEEECC		24.42-
1998PhosphorylationRGSDYSHSEDLADFP
CCCCCCCCCCCCCCC		27.19-
2007PhosphorylationDLADFPPSPDRDRES
CCCCCCCCCCCCHHH		39.4024300666
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
11SPhosphorylationKinaseCAMK2AQ9UQM7
PSP
12SPhosphorylationKinaseCAMK2AQ9UQM7
PSP
17TPhosphorylationKinaseCAMK2AQ9UQM7
PSP
20SPhosphorylationKinaseCAMK2AQ9UQM7
PSP
42SPhosphorylationKinaseCAMK2AQ9UQM7
PSP
61SPhosphorylationKinaseCAMK2AQ9UQM7
PSP
101TPhosphorylationKinaseAMPKA1Q13131
PSP
455TPhosphorylationKinaseCAMK2AQ9UQM7
PSP
457SPhosphorylationKinaseCAMK2AQ9UQM7
PSP
460SPhosphorylationKinaseCAMK2AQ9UQM7
PSP
464SPhosphorylationKinaseCAMK2AQ9UQM7
PSP
471SPhosphorylationKinaseCAMK2AQ9UQM7
PSP
483SPhosphorylationKinaseCAMK2AQ9UQM7
PSP
484SPhosphorylationKinaseCAMK2AQ9UQM7
PSP
497SPhosphorylationKinaseCAMK2AQ9UQM7
PSP
499SPhosphorylationKinaseCAMK2AQ9UQM7
PSP
510SPhosphorylationKinaseCAMK2AQ9UQM7
PSP
516SPhosphorylationKinaseCAMK2DQ13557
PSP
516SPhosphorylationKinaseCAMK2AQ9UQM7
PSP
516SPhosphorylationKinaseCAMK2DP15791
PSP
528SPhosphorylationKinaseCAMK2AQ9UQM7
PSP
528SPhosphorylationKinasePKACAP17612
PSP
539SPhosphorylationKinaseCAMK2AQ9UQM7
PSP
570TPhosphorylationKinaseCAMK2AQ9UQM7
PSP
571SPhosphorylationKinaseCAMK2AQ9UQM7
PSP
577SPhosphorylationKinaseCAMK2AQ9UQM7
PSP
594TPhosphorylationKinaseCAMK2DP15791
PSP
594TPhosphorylationKinaseCAMK2DQ13557
PSP
664SPhosphorylationKinaseCAMK2AQ9UQM7
PSP
667SPhosphorylationKinaseCAMK2AQ9UQM7
PSP
1003SPhosphorylationKinaseCAMK2AQ9UQM7
PSP
1494YPhosphorylationKinaseFYNP06241
PSP
1495YPhosphorylationKinaseFYNP06241
PSP
1503SPhosphorylationKinaseCAMK2AQ9UQM7
PSP
1503SPhosphorylationKinasePKCAP17252
PSP
1503SPhosphorylationKinasePKC-Uniprot
1865SPhosphorylationKinaseCAMK2AQ9UQM7
PSP
1885SPhosphorylationKinaseCAMK2AQ9UQM7
PSP
1920SPhosphorylationKinaseCAMK2AQ9UQM7
PSP
1925SPhosphorylationKinaseCAMK2AQ9UQM7
PSP
1934SPhosphorylationKinaseCAMK2AQ9UQM7
PSP
1937SPhosphorylationKinaseCAMK2AQ9UQM7
PSP
1998SPhosphorylationKinaseCAMK2AQ9UQM7
PSP
2007SPhosphorylationKinaseCAMK2AQ9UQM7
PSP
-KUbiquitinationE3 ubiquitin ligaseNEDD4P46934
PMID:15217910
-KUbiquitinationE3 ubiquitin ligaseNEDD4LQ96PU5
PMID:15548568
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
1503SPhosphorylation

19666841
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of SCN5A_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SNTB2_HUMANSNTB2physical
9412493
SNTA1_HUMANSNTA1physical
9412493
SNTB1_HUMANSNTB1physical
9412493
NEDD4_HUMANNEDD4physical
15217910
NEDD4_MOUSENedd4physical
15548568
WWP2_HUMANWWP2physical
15548568
CRYAB_HUMANCRYABphysical
26961874
NED4L_HUMANNEDD4Lphysical
28296171
Drug and Disease Associations
Kegg Disease
H00294 Dilated cardiomyopathy (DCM)
H00720 Long QT syndrome, including: Romano-Ward syndrome; Jervell and Lange-Nielsen syndrome (JLNS)
H00728 Brugada syndrome (BRS)
H00729 Sick sinus syndrome (SSS); Sinus node dysfunction
H00730 Familial idiopathic ventricular fibrillation
H00731 Atrial fibrillation
H01263 Progressive cardiac conduction defect (PCCD); Progressive familial heart block (PFHB); Lenegre-Lev d
OMIM Disease
113900Progressive familial heart block 1A (PFHB1A)
603830Long QT syndrome 3 (LQT3)
601144Brugada syndrome 1 (BRGDA1)
608567Sick sinus syndrome 1 (SSS1)
603829Familial paroxysmal ventricular fibrillation 1 (VF1)
272120Sudden infant death syndrome (SIDS)
108770Atrial standstill 1 (ATRST1)
601154Cardiomyopathy, dilated 1E (CMD1E)
614022Atrial fibrillation, familial, 10 (ATFB10)
Kegg Drug
D00110 Cocaine (USP); Cocaine (TN)
D00199 Ajmaline (JP16); Ajimalin (TN)
D00252 Carbamazepine (JP16/USP/INN); Equetro (TN); Tegretol (TN)
D00303 Disopyramide (JP16/USAN/INN); Rythmodan P (TN)
D00354 Lamotrigine (JAN/USAN/INN); Lamictal (TN)
D00358 Lidocaine (JP16/USP/INN); Dentipatch (TN); Xylocaine (TN)
D00375 Mephenytoin (USP/INN); Mesantoin (TN)
D00477 Procainamide hydrochloride (JP16/USP); Procan SR (TN); Procanbid (TN); Pronestyl (TN)
D00512 Phenytoin (JP16/USP/INN); Dilantin (TN)
D00533 Oxcarbazepine (USAN/INN); Oxtellar (TN); Trileptal (TN)
D00537 Topiramate (JAN/USAN/INN); Topamax (TN); Trokendi xr (TN)
D00538 Zonisamide (JAN/USAN/INN); Excegran (TN)
D00551 Tetracaine (USP/INN); Amethocaine; Amethocaine (TN)
D00552 Ethyl aminobenzoate (JP16); Benzocaine (USP/INN); Parathesin (TN)
D00553 Propitocaine (JAN); Prilocaine (USP/INN)
D00637 Disopyramide phosphate (JAN/USP); Norpace (TN)
D00638 Flecainide acetate (JP16/USP); Tambocor (TN)
D00639 Mexiletine hydrochloride (JP16/USP); Mexitil (TN)
D00640 Propafenone hydrochloride (JP16/USP); Rythmol (TN)
D00642 Quinidine gluconate (USP); Quinaglute (TN)
D00643 Quinidine polygalacturonate; Cardioquin (TN)
D00732 Chloroprocaine hydrochloride (USP); Nesacaine (TN)
D00733 Dibucaine (USP); Cinchocaine (INN); Nupercaine (TN)
D00735 Dyclonine hydrochloride (USP); Dyclone (TN)
D00738 Mepivacaine hydrochloride (JP16/USP); Carbocaine (TN); Polocaine (TN); Scandonest plain (TN)
D00740 Procaine hydrochloride (JP16/USP); Novocain (TN)
D00741 Tetracaine hydrochloride (JP16/USP); Protocaine hydrochloride (TN)
D01287 Levobupivacaine hydrochloride (JAN/USAN); Chirocaine (TN)
D01326 Aprindine hydrochloride (JP16/USAN); Aspenon (TN)
D01450 Bupivacaine hydrochloride hydrate (JP16); Bupivacaine hydrochloride (USP); Marcaine (TN)
D01455 Cibenzoline succinate (JP16); Cifenline succinate (USAN); Cibenol (TN); Cipralan (TN)
D01479 Ambroxol hydrochloride (JAN); Hustless (TN)
D01554 Pilsicainide hydrochloride hydrate (JAN); Pilsicainide hydrochloride; SUN 1165 (TN); Sunrythm (TN)
D01785 Pirmenol hydrochloride hydrate (JAN); Pimenol (TN)
D02086 Lidocaine injection (JP16); Lidocaine hydrochloride (JAN/USP); Dalcaine (TN); Xylocaine (TN)
D02087 Moricizine hydrochloride (USP); Ethmozine (TN)
D02088 Tocainide hydrochloride (USP); Tonocard (TN)
D02096 Fosphenytoin sodium (USP); Cerebyx (TN)
D02098 Proparacaine hydrochloride (USP); Alcaine (TN); Ophthetic (TN)
D02103 Phenytoin sodium for injection (JP16); Phenytoin sodium (USP); Aleviatin (TN); Dilantin (TN)
D02182 Cocaine hydrochloride (JP16/USP); Cocaine hydrochloride (TN)
D02272 Quinidine sulfate hydrate (JP16); Quinidine sulfate (USP); Quinidex (TN)
D02969 Aprindine (USAN/INN)
D03492 Cifenline (USAN); Cibenzoline (INN)
D03991 Encainide hydrochloride (USAN)
D04048 Ropivacaine hydrochloride hydrate (JAN); Ropivacaine hydrochloride (USP); Anapeine (TN)
D05077 Moricizine (USAN); Moracizine (INN)
D06172 Tocainide (USAN/INN)
D06517 Pirmenol hydrochloride (USAN); Pirmavar (TN)
D07428 Bunaftine (INN)
D07442 Ambroxol (INN); Tabcin (TN)
D07595 Fosphenytoin sodium hydrate (JAN); Fostoin (TN)
D07894 Encainide (INN)
D07962 Flecainide (INN)
D07993 Fosphenytoin (INN)
D08048 Hydroquinidine (DCF); Dihydroquinidine
D08127 Lidocaine hydrochloride monohydrate; Lidocaine (TN)
D08215 Mexiletine (INN)
D08377 Pilsicainide (INN)
D08394 Pirmenol (INN)
D08421 Procainamide (INN)
D08422 Procaine (INN); Solution of novocain (TN)
D08435 Propafenone (INN); Propafenon hexal (TN)
D08458 Quinidine (BAN); Kinidin (TN)
D08459 Quinidine phenylethylbarbiturate; Quinidine 5-ethyl 5-phenyl barbiturate; Natisedine (TN)
D08490 Ropivacaine (INN); Naropin (TN)
D09215 Eslicarbazepine (USAN/INN)
D09612 Eslicarbazepine acetate (USAN)
DrugBank
DB01426Ajmaline
DB01429Aprindine
DB00868Benzonatate
DB00564Carbamazepine
DB00527Cinchocaine
DB00907Cocaine
DB00280Disopyramide
DB01228Encainide
DB00754Ethotoin
DB01195Flecainide
DB01320Fosphenytoin
DB00473Hexylcaine
DB00192Indecainide
DB00281Lidocaine
DB00379Mexiletine
DB00680Moricizine
DB00776Oxcarbazepine
DB00252Phenytoin
DB00750Prilocaine
DB01035Procainamide
DB01182Propafenone
DB00908Quinidine
DB01346Quinidine barbiturate
DB00243Ranolazine
DB00740Riluzole
DB01056Tocainide
DB00313Valproic Acid
DB00661Verapamil
DB00909Zonisamide
Regulatory Network of SCN5A_HUMAN

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Related Literatures of Post-Translational Modification
Methylation
ReferencePubMed
"The cardiac sodium channel is post-translationally modified byarginine methylation.";
Beltran-Alvarez P., Pagans S., Brugada R.;
J. Proteome Res. 10:3712-3719(2011).
Cited for: METHYLATION AT ARG-513; ARG-526 AND ARG-680.

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