SCN8A_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SCN8A_MOUSE
• UniProt AC: Q9WTU3
• Protein Name: Sodium channel protein type 8 subunit alpha
• Gene Name: Scn8a
• Organism: Mus musculus (Mouse).
• Sequence Length: 1978
• Subcellular Localization: Cell membrane ; Multi-pass membrane protein .
• Protein Description: 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. In macrophages, isoform 5 may participate in the control of podosome and invadopodia formation..
• Protein Sequence: MAARVLAPPGPDSFKPFTPESLANIERRIAESKLKKPPKADGSHREDDEDSKPKPNSDLEAGKSLPFIYGDIPQGLVAVPLEDFDPYYLTQKTFVVLNRGKTLFRFSATPALYILSPFNLIRRIAIKILIHSVFSMIIMCTILTNCVFMTFSNPPEWSKNVEYTFTGIYTFESLVKIIARGFCIDGFTFLRDPWNWLDFSVIMMAYVTEFVDLGNVSALRTFRVLRALKTISVIPGLKTIVGALIQSVKKLSDVMILTVFCLSVFALIGLQLFMGNLRNKCVVWPINFNESYLENGTRGFDWEEYINNKTNFYMVPGMLEPLLCGNSSDAGQCPEGFQCMKAGRNPNYGYTSFDTFSWAFLALFRLMTQDYWENLYQLTLRAAGKTYMIFFVLVIFVGSFYLVNLILAVVAMAYEEQNQATLEEAEQKEAEFKAMLEQLKKQQEEAQAAAMATSAGTVSEDAIEEEGEDGVGSPRSSSELSKLSSKSAKERRNRRKKRKQKELSEGEEKGDPEKVFKSESEDGMRRKAFRLPDNRIGRKFSIMNQSLLSIPGSPFLSRHNSKSSIFSFRGPGRFRDPGSENEFADDEHSTVEESEGRRDSLFIPIRARERRSSYSGYSGYSQCSRSSRIFPSLRRSVKRNSTVDCNGVVSLIGPGSHIGRLLPEATTEVEIKKKGPGSLLVSMEQLASYGRKDRINSIMSVVTNTLVEELEESQRKCPPCWYKFANTFLIWECHPYWIKLKEIVNLIVMDPFVDLAITICIVLNTLFMAMEHHPMTPQFEHVLAVGNLVFTGIFTAEMFLKLIAMDPYYYFQEGWNIFDGFIVSLSLMELGLADVEGLSVLRSFRLLRVFKLAKSWPTLNMLIKIIGNSVGALGNLTLVLAIIVFIFAVVGMQLFGKSYKECVCKISQECKLPRWHMNDFFHSFLIVFRVLCGEWIETMWDCMEVAGQAMCLIVFMMVMVIGNLVVLNLFLALLLSSFSADNLAATDDDGEMNNLQISVIRIKKGVAWAKVKVHAFMQAHFKQREADEVKPLDELYEKKANCIANHTGVDIHRNGDFQKNGNGTTSGIGSSVEKYIIDEDHMSFINNPNLTVRVPIAVGESDFENLNTEDVSSESDPEGSKDKLDDTSSSEGSTIDIKPEVEEVPVEQPEEYLDPDACFTEGCVQRFKCCQVNIEEGLGKSWWILRKTCFLIVEHNWFETFIIFMILLSSGALAFEDIYIEQRKTIRTILEYADKVFTYIFILEMLLKWTAYGFVKFFTNAWCWLDFLIVAVSLVSLIANALGYSELGAIKSLRTLRALRPLRALSRFEGMRVVVNALVGAIPSIMNVLLVCLIFWLIFSIMGVNLFAGKYHYCFNETSEIRFEIDEVNNKTDCEKLMEGNNTEIRWKNVKINFDNVGAGYLALLQVATFKGWMDIMYAAVDSRKPDEQPDYEGNIYMYIYFVIFIIFGSFFTLNLFIGVIIDNFNQQKKKFGGQDIFMTEEQKKYYNAMKKLGSKKPQKPIPRPLNKIQGIVFDFVTQQAFDIVIMMLICLNMVTMMVETDTQSKQMENILYWINLVFVIFFTCECVLKMFALRHYYFTIGWNIFDFVVVILSIVGMFLADIIEKYFVSPTLFRVIRLARIGRILRLIKGAKGIRTLLFALMMSLPALFNIGLLLFLVMFIFSIFGMSNFAYVKHEAGIDDMFNFETFGNSMICLFQITTSAGWDGLLLPILNRPPDCSLDKEHPGSGFKGDCGNPSVGIFFFVSYIIISFLIVVNMYIAIILENFSVATEESADPLSEDDFETFYEIWEKFDPDATQFIEYCKLADFADALEHPLRVPKPNTIELIAMDLPMVSGDRIHCLDILFAFTKRVLGDSGELDILRQQMEERFVASNPSKVSYEPITTTLRRKQEEVSAVVLQRAYRGHLARRGFICRKITSNKLENGGTHREKKESTPSTASLPSYDSVTKPDKEKQQRAEEGRRERAKRQKEVRESKC

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
43	Phosphorylation	KPPKADGSHREDDED CCCCCCCCCCCCCCC	21.66	29899451
51	Phosphorylation	HREDDEDSKPKPNSD CCCCCCCCCCCCCCC	49.13	29899451
57	Phosphorylation	DSKPKPNSDLEAGKS CCCCCCCCCCCCCCC	52.69	29899451
215	N-linked_Glycosylation	TEFVDLGNVSALRTF HHHCCCCCHHHHHHH	31.69	-
289	N-linked_Glycosylation	VVWPINFNESYLENG EEEECCCCHHHHHCC	32.58	-
295	N-linked_Glycosylation	FNESYLENGTRGFDW CCHHHHHCCCCCCCH	55.32	-
308	N-linked_Glycosylation	DWEEYINNKTNFYMV CHHHHHCCCCCEEEC	42.86	-
326	N-linked_Glycosylation	LEPLLCGNSSDAGQC CCCCCCCCCCCCCCC	37.03	-
453	Phosphorylation	AQAAAMATSAGTVSE HHHHHHHHHHCCCCH	13.16	26239621
454	Phosphorylation	QAAAMATSAGTVSED HHHHHHHHHCCCCHH	18.37	26239621
457	Phosphorylation	AMATSAGTVSEDAIE HHHHHHCCCCHHHHH	22.15	26239621
459	Phosphorylation	ATSAGTVSEDAIEEE HHHHCCCCHHHHHHC	29.60	26239621
473	Phosphorylation	EGEDGVGSPRSSSEL CCCCCCCCCCCHHHH	18.09	26239621
477	Phosphorylation	GVGSPRSSSELSKLS CCCCCCCHHHHHHHC	29.16	-
504	Phosphorylation	KRKQKELSEGEEKGD HHHHHHHHHCCCCCC	44.65	25521595
518	Phosphorylation	DPEKVFKSESEDGMR CHHHHCCCCCCCCCC	34.58	29899451
520	Phosphorylation	EKVFKSESEDGMRRK HHHCCCCCCCCCCCH	48.34	29899451
541	Phosphorylation	NRIGRKFSIMNQSLL CCHHHCEEECCHHHH	24.78	29899451
546	Phosphorylation	KFSIMNQSLLSIPGS CEEECCHHHHCCCCC	26.69	-
553	Phosphorylation	SLLSIPGSPFLSRHN HHHCCCCCCCCCCCC	13.71	16014723
579	Phosphorylation	GRFRDPGSENEFADD CCCCCCCCCCCCCCC	42.51	29899451
589	Phosphorylation	EFADDEHSTVEESEG CCCCCCCCCCCCCCC	31.91	29899451
590	Phosphorylation	FADDEHSTVEESEGR CCCCCCCCCCCCCCC	33.57	29899451
594	Phosphorylation	EHSTVEESEGRRDSL CCCCCCCCCCCCCCC	31.67	29899451
600	Phosphorylation	ESEGRRDSLFIPIRA CCCCCCCCCEEEEEE	24.30	19060867
612	Phosphorylation	IRARERRSSYSGYSG EEECCCCCCCCCCCC	39.59	29899451
613	Phosphorylation	RARERRSSYSGYSGY EECCCCCCCCCCCCC	22.85	29899451
614	Phosphorylation	ARERRSSYSGYSGYS ECCCCCCCCCCCCCC	13.83	29899451
632	Phosphorylation	RSSRIFPSLRRSVKR HHCCCCHHHHHHHHC	24.61	24759943
641	Phosphorylation	RRSVKRNSTVDCNGV HHHHHCCCCCCCCCE	33.56	29899451
667	Phosphorylation	RLLPEATTEVEIKKK HHCCCCCCEEEEEHH	45.11	29899451
672	Ubiquitination	ATTEVEIKKKGPGSL CCCEEEEEHHCCCCE	34.62	22790023
678	Phosphorylation	IKKKGPGSLLVSMEQ EEHHCCCCEEEEHHH	22.97	22324799
682	Phosphorylation	GPGSLLVSMEQLASY CCCCEEEEHHHHHHC	19.30	22324799
688	Phosphorylation	VSMEQLASYGRKDRI EEHHHHHHCCCHHHH	36.39	22324799
689	Phosphorylation	SMEQLASYGRKDRIN EHHHHHHCCCHHHHH	18.49	22324799
697	Phosphorylation	GRKDRINSIMSVVTN CCHHHHHHHHHHHHH	19.80	-
700	Phosphorylation	DRINSIMSVVTNTLV HHHHHHHHHHHHHHH	16.27	-
1039	Ubiquitination	LDELYEKKANCIANH HHHHHHHHCCHHHCC	32.65	22790023
1083	Phosphorylation	IIDEDHMSFINNPNL EECCCCHHCCCCCCE	21.39	-
1112	Phosphorylation	NLNTEDVSSESDPEG CCCCCCCCCCCCCCC	40.48	29899451
1113	Phosphorylation	LNTEDVSSESDPEGS CCCCCCCCCCCCCCC	40.75	29899451
1115	Phosphorylation	TEDVSSESDPEGSKD CCCCCCCCCCCCCCC	61.48	29899451
1170	S-palmitoylation	CVQRFKCCQVNIEEG HHHHHEEEEEECCCC	5.36	28680068
1239	Phosphorylation	YADKVFTYIFILEML HHHHHHHHHHHHHHH	5.16	-
1356	N-linked_Glycosylation	GKYHYCFNETSEIRF CEEEECCCCCCEEEE	48.34	-
1370	N-linked_Glycosylation	FEIDEVNNKTDCEKL EEEECCCCCCCHHHH	54.50	-
1381	N-linked_Glycosylation	CEKLMEGNNTEIRWK HHHHHCCCCCEEEEE	38.66	-
1491	Ubiquitination	KKYYNAMKKLGSKKP HHHHHHHHHHCCCCC	42.30	-
1495	Phosphorylation	NAMKKLGSKKPQKPI HHHHHHCCCCCCCCC	48.20	-
1878	Ubiquitination	FVASNPSKVSYEPIT HCCCCCCCCCCCCCC	36.14	22790023
1881	Phosphorylation	SNPSKVSYEPITTTL CCCCCCCCCCCCHHH	28.81	21183079
1939	Phosphorylation	KKESTPSTASLPSYD CCCCCCCCCCCCCCC	22.82	-
1945	Phosphorylation	STASLPSYDSVTKPD CCCCCCCCCCCCCCC	15.42	20530479
1947	Phosphorylation	ASLPSYDSVTKPDKE CCCCCCCCCCCCCHH	24.37	-
1949	Phosphorylation	LPSYDSVTKPDKEKQ CCCCCCCCCCCHHHH	40.59	-

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
553	S	Phosphorylation	Kinase	MAPK14	Q16539	GPS
1495	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
1495	S	Phosphorylation	Phosphorylation at Ser-1495 by PKC in a highly conserved cytoplasmic loop slows inactivation of the sodium channel and reduces peak sodium currents.	-

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of SCN8A_MOUSE !!

Protein-Protein Interaction

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

Drug and Disease Associations

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