dbPTM

SCN5A_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SCN5A_MOUSE
UniProt AC	Q9JJV9
Protein Name	Sodium channel protein type 5 subunit alpha
Gene Name	Scn5a
Organism	Mus musculus (Mouse).
Sequence Length	2019
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: 11834499]
Protein Sequence	MANFLLPRGTSSFRRFTRESLAAIEKRMAEKQARGSATSQESREGLPEEEAPRPQLDLQASKKLPDLYGNPPRELIGEPLEDLDPFYSTQKTFIVLNKGKTIFRFSATNALYVLSPFHPVRRAAVKILVHSLFSMLIMCTILTNCVFMAQHDPPPWTKYVEYTFTAIYTFESLVKILARGFCLHAFTFLRDPWNWLDFSVIVMAYTTEFVDLGNVSALRTFRVLRALKTISVISGLKTIVGALIQSVKKLADVMVLTVFCLSVFALIGLQLFMGNLRHKCVRNFTELNGTNGSVEADGIVWNSLDVYLNDPANYLLKNGTTDVLLCGNSSDAGTCPEGYRCLKAGENPDHGYTSFDSFAWAFLALFRLMTQDCWERLYQQTLRSAGKIYMIFFMLVIFLGSFYLVNLILAVVAMAYEEQNQATIAETEEKEKRFQEAMEMLKKEHEALTIRGVDTVSRSSLEMSPLAPVTNHERRSKRRKRLSSGTEDGGDDRLPKSDSEDGPRALNQLSLTHGLSRTSMRPRSSRGSIFTFRRRDQGSEADFADDENSTAGESESHRTSLLVPWPLRRPSTQGQPGFGTSAPGHVLNGKRNSTVDCNGVVSLLGAGDAEATSPGSHLLRPIVLDRPPDTTTPSEEPGGPQMLTPQAPCADGFEEPGARQRALSAVSVLTSALEELEESHRKCPPCWNRFAQHYLIWECCPLWMSIKQKVKFVVMDPFADLTITMCIVLNTLFMALEHYNMTAEFEEMLQVGNLVFTGIFTAEMTFKIIALDPYYYFQQGWNIFDSIIVILSLMELGLSRMGNLSVLRSFRLLRVFKLAKSWPTLNTLIKIIGNSVGALGNLTLVLAIIVFIFAVVGMQLFGKNYSELRHRISDSGLLPRWHMMDFFHAFLIIFRILCGEWIETMWDCMEVSGQSLCLLVFLLVMVIGNLVVLNLFLALLLSSFSADNLTAPDEDGEMNNLQLALARIQRGLRFVKRTTWDFCCGLLRRRPKKPAALATHSQLPSCIAAPRSPPPPEVEKAPPARKETRFEEDKRPGQGTPGDTEPVCVPIAVAESDTDDQEEDEENSLGTEEEESSKQESQVVSGGHEPPQEPRAWSQVSETTSSEAEASTSQADWQQEREAEPRAPGCGETPEDSYSEGSTADMTNTADLLEQIPDLGEDVKDPEDCFTEGCVRRCPCCMVDTTQAPGKVWWRLRKTCYRIVEHSWFETFIIFMILLSSGALAFEDIYLEERKTIKVLLEYADKMFTYVFVLEMLLKWVAYGFKKYFTNAWCWLDFLIVDVSLVSLVANTLGFAEMGPIKSLRTLRALRPLRALSRFEGMRVVVNALVGAIPSIMNVLLVCLIFWLIFSIMGVNLFAGKFGRCINQTEGDLPLNYTIVNNKSECESFNVTGELYWTKVKVNFDNVGAGYLALLQVATFKGWMDIMYAAVDSRGYEEQPQWEDNLYMYIYFVVFIIFGSFFTLNLFIGVIIDNFNQQKKKLGGQDIFMTEEQKKYYNAMKKLGSKKPQKPIPRPLNKYQGFIFDIVTKQAFDVTIMFLICLNMVTMMVETDDQSPEKVNILAKINLLFVAIFTGECIVKMAALRHYYFTNSWNIFDFVVVILSIVGTVLSDIIQKYFFSPTLFRVIRLARIGRILRLIRGAKGIRTLLFALMMSLPALFNIGLLLFLVMFIYSIFGMANFAYVKWEAGIDDMFNFQTFANSMLCLFQITTSAGWDGLLSPILNTGPPYCDPNLPNSNGSRGNCGSPAVGILFFTTYIIISFLIVVNMYIAIILENFSVATEESTEPLSEDDFDMFYEIWEKFDPEATQFIEYLALSDFADALSEPLRIAKPNQISLINMDLPMVSGDRIHCMDILFAFTKRVLGESGEMDALKIQMEEKFMAANPSKISYEPITTTLRRKHEEVSATVIQRAFRRHLLQRSVKHASFLFRQQAGSSGLSDEDAPEREGLIAYMMNENFSRRSGPLSSSSISSTSFPPSYDSVTRATSDNLPVRASDYSRSEDLADFPPSPDRDRESIV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
36	Phosphorylation	AEKQARGSATSQESR HHHHHHCCCCCHHHH	23.87	24759943
38	Phosphorylation	KQARGSATSQESREG HHHHCCCCCHHHHCC	32.42	24759943
39	Phosphorylation	QARGSATSQESREGL HHHCCCCCHHHHCCC	31.50	24759943
42	Phosphorylation	GSATSQESREGLPEE CCCCCHHHHCCCCCC	28.17	-
91	Ubiquitination	DPFYSTQKTFIVLNK CCCCCCCCEEEEECC	45.55	-
214	N-linked_Glycosylation	TEFVDLGNVSALRTF CCEECCCCHHHHHHH	31.69	-
283	N-linked_Glycosylation	LRHKCVRNFTELNGT CHHHHHHCCHHCCCC	28.00	-
288	N-linked_Glycosylation	VRNFTELNGTNGSVE HHCCHHCCCCCCCEE	49.35	-
291	N-linked_Glycosylation	FTELNGTNGSVEADG CHHCCCCCCCEEECC	41.98	-
318	N-linked_Glycosylation	PANYLLKNGTTDVLL HHHHHCCCCCCCEEE	53.68	-
328	N-linked_Glycosylation	TDVLLCGNSSDAGTC CCEEECCCCCCCCCC	37.03	-
455	Phosphorylation	LTIRGVDTVSRSSLE HHHCCCCCCCCCCCC	20.27	23737553
457	Phosphorylation	IRGVDTVSRSSLEMS HCCCCCCCCCCCCCC	28.65	24899341
459	Phosphorylation	GVDTVSRSSLEMSPL CCCCCCCCCCCCCCC	31.59	23737553
460	Phosphorylation	VDTVSRSSLEMSPLA CCCCCCCCCCCCCCC	27.52	24899341
464	Phosphorylation	SRSSLEMSPLAPVTN CCCCCCCCCCCCCCC	13.85	27742792
483	Phosphorylation	SKRRKRLSSGTEDGG HHHHHHCCCCCCCCC	30.65	27742792
484	Phosphorylation	KRRKRLSSGTEDGGD HHHHHCCCCCCCCCC	55.09	24899341
486	Phosphorylation	RKRLSSGTEDGGDDR HHHCCCCCCCCCCCC	32.62	27742792
497	Phosphorylation	GDDRLPKSDSEDGPR CCCCCCCCCCCCCHH	44.42	27742792
499	Phosphorylation	DRLPKSDSEDGPRAL CCCCCCCCCCCHHHH	44.68	27742792
510	Phosphorylation	PRALNQLSLTHGLSR HHHHHHHHHHCCCCC	22.81	-
516	Phosphorylation	LSLTHGLSRTSMRPR HHHHCCCCCCCCCCC	37.80	23737553
524	Phosphorylation	RTSMRPRSSRGSIFT CCCCCCCCCCCCEEE	27.37	-
525	Phosphorylation	TSMRPRSSRGSIFTF CCCCCCCCCCCEEEE	41.77	-
526	Dimethylation	SMRPRSSRGSIFTFR CCCCCCCCCCEEEEE	44.09	-
526	Methylation	SMRPRSSRGSIFTFR CCCCCCCCCCEEEEE	44.09	24129315
528	Phosphorylation	RPRSSRGSIFTFRRR CCCCCCCCEEEEEEC	17.26	23737553
539	Phosphorylation	FRRRDQGSEADFADD EEECCCCCCCCCCCC	24.79	19060867
549	Phosphorylation	DFADDENSTAGESES CCCCCCCCCCCCCCC	20.00	23737553
550	Phosphorylation	FADDENSTAGESESH CCCCCCCCCCCCCCC	50.71	23737553
571	Phosphorylation	PWPLRRPSTQGQPGF EECCCCCCCCCCCCC	31.39	-
664	Phosphorylation	GARQRALSAVSVLTS CHHHHHHHHHHHHHH	26.16	23737553
667	Phosphorylation	QRALSAVSVLTSALE HHHHHHHHHHHHHHH	15.89	23737553
670	Phosphorylation	LSAVSVLTSALEELE HHHHHHHHHHHHHHH	15.14	23737553
671	Phosphorylation	SAVSVLTSALEELEE HHHHHHHHHHHHHHH	27.05	23737553
740	N-linked_Glycosylation	FMALEHYNMTAEFEE HHHHHHCCCCHHHHH	24.20	-
775	Phosphorylation	IIALDPYYYFQQGWN EEEECCHHHHHCCCC	11.82	25521595
799	Phosphorylation	SLMELGLSRMGNLSV HHHHHCCCCCCCHHH	20.58	25521595
803	N-linked_Glycosylation	LGLSRMGNLSVLRSF HCCCCCCCHHHHHHH	21.57	-
864	N-linked_Glycosylation	GMQLFGKNYSELRHR HHHHHCCCHHHHHHH	46.04	-
1012	Phosphorylation	SCIAAPRSPPPPEVE CCCCCCCCCCCCCHH	40.47	-
1367	N-linked_Glycosylation	GKFGRCINQTEGDLP CCCCHHHCCCCCCCC	46.47	-
1376	N-linked_Glycosylation	TEGDLPLNYTIVNNK CCCCCCCEEEEECCC	29.93	-
1382	N-linked_Glycosylation	LNYTIVNNKSECESF CEEEEECCCCCCEEE	38.03	-
1390	N-linked_Glycosylation	KSECESFNVTGELYW CCCCEEEECCCEEEE	39.46	-
1481	Acetylation	NFNQQKKKLGGQDIF CCHHHHHHHCCCCCC	60.44	126089613
1501	Ubiquitination	KKYYNAMKKLGSKKP HHHHHHHHHHCCCCC	42.30	-
1505	Phosphorylation	NAMKKLGSKKPQKPI HHHHHHCCCCCCCCC	48.20	-
1887	Phosphorylation	KFMAANPSKISYEPI HHHHCCCCCCCCCCC	42.29	-
1927	Phosphorylation	QRSVKHASFLFRQQA HHHHHHHHHHHHHCC	23.38	21183079
1936	Phosphorylation	LFRQQAGSSGLSDED HHHHCCCCCCCCCCC	25.01	-
1937	Phosphorylation	FRQQAGSSGLSDEDA HHHCCCCCCCCCCCC	42.72	-
1960	Phosphorylation	YMMNENFSRRSGPLS HHHCCCCCCCCCCCC	38.06	28285833
1963	Phosphorylation	NENFSRRSGPLSSSS CCCCCCCCCCCCCCC	43.59	29119230
1967	Phosphorylation	SRRSGPLSSSSISST CCCCCCCCCCCCCCC	31.16	29119230
1968	Phosphorylation	RRSGPLSSSSISSTS CCCCCCCCCCCCCCC	35.47	29119230
1969	Phosphorylation	RSGPLSSSSISSTSF CCCCCCCCCCCCCCC	28.45	29119230
1970	Phosphorylation	SGPLSSSSISSTSFP CCCCCCCCCCCCCCC	28.56	29119230
1972	Phosphorylation	PLSSSSISSTSFPPS CCCCCCCCCCCCCCC	29.52	29119230
1973	Phosphorylation	LSSSSISSTSFPPSY CCCCCCCCCCCCCCC	26.80	29119230
1974	Phosphorylation	SSSSISSTSFPPSYD CCCCCCCCCCCCCCC	27.83	29119230
1975	Phosphorylation	SSSISSTSFPPSYDS CCCCCCCCCCCCCCC	37.39	29119230
1979	Phosphorylation	SSTSFPPSYDSVTRA CCCCCCCCCCCCCCC	41.64	29119230
1980	Phosphorylation	STSFPPSYDSVTRAT CCCCCCCCCCCCCCC	20.29	29119230
1982	Phosphorylation	SFPPSYDSVTRATSD CCCCCCCCCCCCCCC	19.70	29119230
1984	Phosphorylation	PPSYDSVTRATSDNL CCCCCCCCCCCCCCC	20.66	29119230
1987	Phosphorylation	YDSVTRATSDNLPVR CCCCCCCCCCCCCCC	33.07	29119230
1988	Phosphorylation	DSVTRATSDNLPVRA CCCCCCCCCCCCCCH	24.42	29119230

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
571	S	Phosphorylation	Kinase	CAMK2A	Q9UQM7	PSP
571	S	Phosphorylation	Kinase	CAMK2A	P11798	PSP
1505	S	Phosphorylation	Kinase	PKC	-	Uniprot
-	K	Ubiquitination	E3 ubiquitin ligase	Nedd4l	Q8CFI0	PMID:22199232

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
1505	S	Phosphorylation		17124532
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).

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_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
NEDD4_MOUSE	Nedd4	physical	15123669

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of SCN5A_MOUSE

Related Literatures of Post-Translational Modification

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