SCN3A_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SCN3A_RAT
• UniProt AC: P08104
• Protein Name: Sodium channel protein type 3 subunit alpha
• Gene Name: Scn3a
• Organism: Rattus norvegicus (Rat).
• Sequence Length: 1951
• 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: MAQALLVPPGPESFRLFTRESLAAIEKRAAEEKAKKPKKEQDIDDENKPKPNSDLEAGKNLPFIYGDIPPEMVSEPLEDLDPYYVSKKTFVVLNKGKAIFRFSATSALYILTPLNPVRKIAIKILVHSLFSMLIMCTILTNCVFMTLSNPPDWTKNVEYTFTGIYTFESLIKILARGFCLEDFTFLRDPWNWLDFSVIVMAYVTEFVDLGNVSALRTFRVLRALKTISVIPGLKTIVGALIQSVKKLSDVMILTVFCLSVFALIGLQLFMGNLRNKCSQWPPSDSAFETNTTSYFNGTMDSNGTFVNVTMSTFNWKDYIADDSHFYVLDGQKDPLLCGNGSDAGQCPEGYICVKAGRNPNYGYTSFDTFSWAFLSLFRLMTQDYWENLYQLTLRAAGKTYMIFFVLVIFLGSFYLVNLILAVVAMAYEEQNQATLEEAEQKEAEFQQMLEQLKKQQEEAQAVAAASAASRDFSGIGGLGELLESSSEASKLSSKSAKEWRNRRKKRRQREHLEGNHRADGDRFPKSESEDSVKRRSFLLSLDGNPLTGDKKLCSPHQSLLSIRGSLFSPRRNSKTSIFSFRGRAKDVGSENDFADDEHSTFEDSESRRDSLFVPHRPGERRNSNGTTTETEVRKRRLSSYQISMEMLEDSSGRQRSMSIASILTNTMEELEESRQKCPPCWYRFANVFLIWDCCDAWLKVKHLVNLIVMDPFVDLAITICIVLNTLFMAMEHYPMTQQFSSVLTVGNLVFTGIFTAEMVLKIIAMDPYYYFQEGWNIFDGIIVSLSLMELGLANVEGLSVLRSFRLLRVFKLAKSWPTLNMLIKIIGNSVGALGNLTLVLAIIVFIFAVVGMQLFGKSYKECVCKINVDCKLPRWHMNDFFHSFLIVFRVLCGEWIETMWDCMEVAGQTMCLIVFMLVMVIGNLVVLNLFLALLLSSFSSDNLAATDDDNEMNNLQIAVGRMQKGIDFVKNKIRECFRKAFFRKPKVIEIQEGNKIDSCMSNNTGIEISKELNYLKDGNGTTSGVGTGSSVEKYVIDENDYMSFINNPSLTVTVPIAVGESDFENLNTEEFSSESELEESKEKLNATSSSEGSTVDVAPPREGEQAEIEPEEDLKPEACFTEGCIKKFPFCQVSTEEGKGKIWWNLRKTCYSIVEHNWFETFIVFMILLSSGALAFEDIYIEQRKTIKTMLEYADKVFTYIFILEMLLKWVAYGFQTYFTNAWCWLDFLIVDVSLVSLVANALGYSELGAIKSLRTLRALRPLRALSRFEGMRVVVNALVGAIPSIMNVLLVCLIFWLIFSIMGVNLFAGKFYHCVNTTTGNMFEIKEVNNFSDCQALGKQARWKNVKVNFDNVGAGYLALLQVATFKGWMDIMYAAVDSRDVKLQPIYEENLYMYLYFVIFIIFGSFFTLNLFIGVIIDNFNQQKKKFGGQDIFMTEEQKKYYNAMKKLGSKKPQKPIPRPANKFQGMVFDFVTRQVFDISIMILICLNMVTMMVETDDQSKYMTLVLSRINLVFIVLFTGEFLLKLISLRYYYFTIGWNIFDFVVVILSIVGMFLAELIEKYFVSPTLFRVIRLARIGRILRLIKGAKGIRTLLFALMMSLPALFNIGLLLFLVMFIYAIFGMSNFAYVKKEAGIDDMFNFETFGNSMICLFQITTSAGWDGLLAPILNSAPPDCDPDAIHPGSSVKGDCGNPSVGIFFFVSYIIISFLVVVNMYIAVILENFSVATEESAEPLSEDDFEMFYEVWEKFDPDATQFIEFCKLSDFAAALDPPLLIAKPNKVQLIAMDLPMVSGDRIHCLDILFAFTKRVLGESGEMDALRIQMEDRFMASNPSKVSYEPITTTLKRKQEEVSAAIIQRNYRCYLLKQRLKNISSKYDKETIKGRIDLPIKGDMVIDKLNGNSTPEKTDGSSSTTSPPSYDSVTKPDKEKFEKDKPEKEIKGKEVRENQK

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
211	N-linked_Glycosylation	TEFVDLGNVSALRTF HCCCCCCCHHHHHHH	31.69	-
290	N-linked_Glycosylation	SDSAFETNTTSYFNG CCCCCCCCCCCCCCC	33.87	-
296	N-linked_Glycosylation	TNTTSYFNGTMDSNG CCCCCCCCCEECCCC	36.47	-
302	N-linked_Glycosylation	FNGTMDSNGTFVNVT CCCEECCCCCEEEEE	49.62	-
307	N-linked_Glycosylation	DSNGTFVNVTMSTFN CCCCCEEEEEEEECC	21.25	-
339	N-linked_Glycosylation	KDPLLCGNGSDAGQC CCCEECCCCCCCCCC	45.88	-
454	Ubiquitination	QMLEQLKKQQEEAQA HHHHHHHHHHHHHHH	66.85	-
484	Phosphorylation	GLGELLESSSEASKL HHHHHHHCCHHHHHH	38.85	28551015
485	Phosphorylation	LGELLESSSEASKLS HHHHHHCCHHHHHHC	23.87	28551015
486	Phosphorylation	GELLESSSEASKLSS HHHHHCCHHHHHHCH	46.60	28551015
489	Phosphorylation	LESSSEASKLSSKSA HHCCHHHHHHCHHHH	30.03	28551015
528	Phosphorylation	DRFPKSESEDSVKRR CCCCCCCCCCCHHHH	54.52	28432305
531	Phosphorylation	PKSESEDSVKRRSFL CCCCCCCCHHHHHEE	26.03	28432305
536	Phosphorylation	EDSVKRRSFLLSLDG CCCHHHHHEEEEECC	25.03	28432305
540	Phosphorylation	KRRSFLLSLDGNPLT HHHHEEEEECCCCCC	26.93	28432305
554	Phosphorylation	TGDKKLCSPHQSLLS CCCCCCCCHHHHHHH	35.53	28432305
568	Phosphorylation	SIRGSLFSPRRNSKT HHCCCCCCCCCCCCC	23.84	30411139
610	Phosphorylation	DSESRRDSLFVPHRP CCCHHCCCCCCCCCC	23.15	28432305
643	Phosphorylation	RLSSYQISMEMLEDS HHHHCCCCHHHHHCC	7.99	28551015
650	Phosphorylation	SMEMLEDSSGRQRSM CHHHHHCCCCCCHHH	25.89	28551015
651	Phosphorylation	MEMLEDSSGRQRSMS HHHHHCCCCCCHHHH	50.76	28551015
673	Phosphorylation	TMEELEESRQKCPPC HHHHHHHHHHHCCCH	30.54	22673903
1317	N-linked_Glycosylation	GKFYHCVNTTTGNMF CCCHHEEECCCCCEE	36.78	-
1331	N-linked_Glycosylation	FEIKEVNNFSDCQAL EEEEEECCHHHHHHH	42.87	-
1443	Phosphorylation	MTEEQKKYYNAMKKL CCHHHHHHHHHHHHH	14.69	17959797
1444	Phosphorylation	TEEQKKYYNAMKKLG CHHHHHHHHHHHHHC	12.81	17959797
1452	Phosphorylation	NAMKKLGSKKPQKPI HHHHHHCCCCCCCCC	48.20	22426212
1839	Phosphorylation	SNPSKVSYEPITTTL CCCCCCCCCCCCHHH	28.81	17959797
1876	Phosphorylation	QRLKNISSKYDKETI HHHHHCCCCCCHHHH	31.29	27097102
1917	Phosphorylation	DGSSSTTSPPSYDSV CCCCCCCCCCCCCCC	34.60	30240740

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
1452	S	Phosphorylation	Kinase	PKC	-	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
1452	S	Phosphorylation	Phosphorylation at Ser-1452 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 SCN3A_RAT !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference

Drug and Disease Associations

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