SCN8A_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SCN8A_RAT
• UniProt AC: O88420
• Protein Name: Sodium channel protein type 8 subunit alpha
• Gene Name: Scn8a
• Organism: Rattus norvegicus (Rat).
• 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..
• Protein Sequence: MAARLLAPPGPDSFKPFTPESLANIERRIAESKLKKPPKADGSHREDDEDSKPKPNSDLEAGKSLPFIYGDIPQGLVAVPLEDFDPYYLTQKTFVVLNRGKTLFRFSATPALYILSPFNLIRRIAIKILIHSVFSMIIMCTILTNCVFMTFSNPPEWSKNVEYTFTGIYTFESLVKIIARGFCIDGFTFLRDPWNWLDFSVIMMAYVTEFVDLGNVSALRTFRVLRALKTISVIPGLKTIVGALIQSVKKLSDVMILTVFCLSVFALIGLQLFMGNLRNKCVVWPINFNESYLENGTRGFDWEEYINNKTNFYMVPGMLEPLLCGNSSDAGQCPEGFQCMKAGRNPNYGYTSFDTFSWAFLALFRLMTQDYWENLYQLTLRAAGKTYMIFFVLVIFVGSFYLVNLILAVVAMAYEEQNQATLEEAEQKEAEFKAMLEQLKKQQEEAQAAAMATSAGTVSEDAIEEEGEDGVGSPRSSSELSKLSSKSAKERRNRRKKRKQKELSEGEEKGDPEKVFKSESEDGMRRKAFRLPDNRIGRKFSIMNQSLLSIPGSPFLSRHNSKSSIFSFRGPGRFRDPGSENEFADDEHSTVEESEGRRDSLFIPIRARERRSSYSGYSGYSQCSRSSRIFPSLRRSVKRNSTVDCNGVVSLIGPGSHIGRLLPEATTEVEIKKKGPGSLLVSMDQLASYGRKDRINSIMSVVTNTLVEELEESQRKCPPCWYKFANTFLIWECHPYWIKLKEIVNLIVMDPFVDLAITICIVLNTLFMAMEHHPMTPQFEHVLAVGNLVFTGIFTAEMFLKLIAMDPYYYFQEGWNIFDGFIVSLSLMELSLADVEGLSVLRSFRLLRVFKLAKSWPTLNMLIKIIGNSVGALGNLTLVLAIIVFIFAVVGMQLFGKSYKECVCKINQECKLPRWHMNDFFHSFLIVFRVLCGEWIETMWDCMEVAGQAMCLIVFMMVMVIGNLVVLNLFLALLLSSFSADNLAATDDDGEMNNLQISVIRIKKGVAWTKVKVHAFMQAHFKQREADEVKPLDELYEKKANCIANHTGVDIHRNGDFQKNGNGTTSGIGSSVEKYIIDEDHMSFINNPNLTVRVPIAVGESDFENLNTEDVSSESDPEGSKDKLDDTSSSEGSTIDIKPEVEEVPVEQPEEYLDPDACFTEGCVQRFKCCQVNIEEGLGKSWWILRKTCFLIVEHNWFETFIIFMILLSSGALAFEDIYIEQRKTIRTILEYADKVFTYIFILEMLLKWTAYGFVKFFTNAWCWLDFLIVAVSLVSLIANALGYSELGAIKSLRTLRALRPLRALSRFEGMRVVVNALVGAIPSIMNVLLVCLIFWLIFSIMGVNLFAGKYHYCFNETSEIRFEIDIVNNKTDCEKLMEGNSTEIRWKNVKINFDNVGAGYLALLQVATFKGWMDIMYAAVDSRKPDEQPDYEGNIYMYIYFVIFIIFGSFFTLNLFIGVIIDNFNQQKKKFGGQDIFMTEEQKKYYNAMKKLGSKKPQKPIPRPLNKIQGIVFDFVTQQAFDIVIMMLICLNMVTMMVETDTQSKQMENILYWINLVFVIFFTCECVLKMFALRHYYFTIGWNIFDFVVVILSIVGMFLADIIEKYFVSPTLFRVIRLARIGRILRLIKGAKGIRTLLFALMMSLPALFNIGLLLFLVMFIFSIFGMSNFAYVKHEAGIDDMFNFETFGNSMICLFQITTSAGWDGLLLPILNRPPDCSLDKEHPGSGFKGDCGNPSVGIFFFVSYIIISFLIVVNMYIAIILENFSVATEESADPLSEDDFETFYEIWEKFDPDATQFIEYCKLADFADALEHPLRVPKPNTIELIAMDLPMVSGDRIHCLDILFAFTKRVLGDSGELDILRQQMEERFVASNPSKVSYEPITTTLRRKQEEVSAVVLQRAYRGHLARRGFICRKMASNKLENGGTHRDKKESTPSTASLPSYDSVTKPDKEKQQRAEEGRRERAKRQKEVRESKC

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
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	-
440	Ubiquitination	KAMLEQLKKQQEEAQ HHHHHHHHHHHHHHH	48.51	-
477	Phosphorylation	GVGSPRSSSELSKLS CCCCCCCHHHHHHHC	29.16	-
504	Phosphorylation	KRKQKELSEGEEKGD HHHHHHHHHCCCCCC	44.65	22673903
518	Phosphorylation	DPEKVFKSESEDGMR CHHHHCCCCCCCCCC	34.58	22673903
520	Phosphorylation	EKVFKSESEDGMRRK HHHCCCCCCCCCCCH	48.34	22673903
546	Phosphorylation	KFSIMNQSLLSIPGS CEEECCHHHHCCCCC	26.69	-
553	Phosphorylation	SLLSIPGSPFLSRHN HHHCCCCCCCCCCCC	13.71	16014723
561	Phosphorylation	PFLSRHNSKSSIFSF CCCCCCCCCCCCEEE	27.99	28432305
563	Phosphorylation	LSRHNSKSSIFSFRG CCCCCCCCCCEEECC	28.61	28432305
564	Phosphorylation	SRHNSKSSIFSFRGP CCCCCCCCCEEECCC	31.24	28432305
567	Phosphorylation	NSKSSIFSFRGPGRF CCCCCCEEECCCCCC	16.62	28432305
579	Phosphorylation	GRFRDPGSENEFADD CCCCCCCCCCCCCCC	42.51	-
613	Phosphorylation	RARERRSSYSGYSGY EECCCCCCCCCCCCC	22.85	-
650	Phosphorylation	VDCNGVVSLIGPGSH CCCCCEEEEECCCCH	16.32	26022182
672	Ubiquitination	ATTEVEIKKKGPGSL CCCEEEEEHHCCCCE	34.62	-
688	Phosphorylation	VSMDQLASYGRKDRI EEHHHHHHCCCHHHH	36.39	22673903
689	Phosphorylation	SMDQLASYGRKDRIN EHHHHHHCCCHHHHH	18.49	22673903
697	Phosphorylation	GRKDRINSIMSVVTN CCHHHHHHHHHHHHH	19.80	-
700	Phosphorylation	DRINSIMSVVTNTLV HHHHHHHHHHHHHHH	16.27	-
1075	Phosphorylation	IGSSVEKYIIDEDHM CCCCEEEEEECCCCH	6.93	-
1356	N-linked_Glycosylation	GKYHYCFNETSEIRF CEEEECCCCCCEEEE	48.34	-
1370	N-linked_Glycosylation	FEIDIVNNKTDCEKL EEEEEECCCCCHHHH	37.40	-
1381	N-linked_Glycosylation	CEKLMEGNSTEIRWK HHHHHCCCCCEEEEE	32.24	-
1486	Phosphorylation	MTEEQKKYYNAMKKL CCHHHHHHHHHHHHH	14.69	17959797
1487	Phosphorylation	TEEQKKYYNAMKKLG CHHHHHHHHHHHHHC	12.81	17959797
1495	Phosphorylation	NAMKKLGSKKPQKPI HHHHHHCCCCCCCCC	48.20	22426212
1881	Phosphorylation	SNPSKVSYEPITTTL CCCCCCCCCCCCHHH	28.81	-
1936	Phosphorylation	HRDKKESTPSTASLP CCCCCCCCCCCCCCC	23.50	-

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	MAPK12	Q63538	GPS
553	S	Phosphorylation	Kinase	MAPK14	P47811	GPS
1495	S	Phosphorylation	Kinase	PKC	-	Uniprot
1936	T	Phosphorylation	Kinase	GSK3B	P49841	PSP

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_RAT !!

Protein-Protein Interaction

Oops, there are no PPI records of SCN8A_RAT !!

Drug and Disease Associations

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