SCNAA_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SCNAA_MOUSE
• UniProt AC: Q6QIY3
• Protein Name: Sodium channel protein type 10 subunit alpha
• Gene Name: Scn10a
• Organism: Mus musculus (Mouse).
• Sequence Length: 1958
• Subcellular Localization: Cell membrane ; Multi-pass membrane protein . It can be translocated to the cell membrane through association with S100A10..
• Protein Description: Tetrodotoxin-resistant channel that 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 sodium ions may pass in accordance with their electrochemical gradient. Plays a role in neuropathic pain mechanisms..
• Protein Sequence: MEFPFGSVGTTNFRRFTPESLAEIEKQIAAHRAAKKGRPKQRGQKDKSEKPRPQLDLKACNQLPRFYGELPAELVGEPLEDLDPFYSTHRTFIVLDKSRTISRFSATWALWLFSPFNLIRRTAIKVSVHSWFSIFITVTILVNCVCMTRTDLPEKLEYAFTVVYTFEALIKILARGFCLNEFTYLRDPWNWLDFSVITLAYVGAAIDLRGISGLRTFRVLRALKTVSVIPGLKVIVGALIHSVRKLADVTILTVFCLSVFALVGLQLFKGNLKNKCIKNGTDPHKADNLSSEMAGDIFIKPGTTDPLLCGNGSDAGHCPNDYVCRKTSDNPDFNYTSFDSFAWAFLSLFRLMTQDSWERLYQQTLRASGKMYMVFFVLVIFLGSFYLVNLILAVVTMAYEEQSQATIAEIEAKEKKFKEALEVLQKEQEVLAALGIDTTSLYSHNGSPLAPKNANERRPRVKSRMSEGSTDDNRSLQSDPYNQRRMSFLGLSSGRRRASHSSVFHFRAPSQDVSFPDGILDDGVFHGDQESRRSSILLGRGAGQAGPLPRSPLPQSPNPGPRRGEEGQRGVPTGELATGAPEGPALDAAGQKNFLSADYLNEPFRAQRAMSVVSIMTSVIEELEESKLKCPPCLISLAQKYLIWECCPKWKKFKMVLFELVTDPFAELTITLCIVVNTVFMAMEHYPMTDAFDAMLQAGNIVFTVFFTMEMAFKIIAFDPYYYFQKKWNIFDCVIVTVSLLELSTSKKGSLSVLRTFRLLRVFKLAKSWPTLNMLIKIIGNSVGALGNLTFILAIIVFIFALVGKQLLSENYGCRRDGISVWNGERLRWHMCDFFHSFLVVFRILCGEWIENMWVCMEVSQDYICLTLFLTVMVLGNLVVLNLFIALLLNSFSADNLTAPEDDGEVNNLQVALARIQVFGHRASRAITSYIRSHCRLRWPKVETQLGMKPPLTSCKAENHIATDAVNAAVGNLAKPALGGPKENHGDFITDPNVWVSVPIAEGESDLDELEEDVEHASQSSWQEESPKGQQELLQQVQKCEDHQAARSPPSGMSSEDLAPYLGERWQREESPRVPAEGVDDTSSSEGSTVDCPDPEEILRKIPELAEELDEPDDCFPEGCTRRCPCCKVNTSKFPWATGWQVRKTCYRIVEHSWFESFIIFMILLSSGALAFEDNYLEEKPRVKSVLEYTDRVFTFIFVFEMLLKWVAYGFKKYFTNAWCWLDFLIVNISLTSLIAKILEYSDVASIKALRTLRALRPLRALSRFEGMRVVVDALVGAIPSIMNVLLVCLIFWLIFSIMGVNLFAGKFSRCVDTRSNPFSVVNSTFVTNKSDCYNQNNTGHFFWVNVKVNFDNVAMGYLALLQVATFKGWMDIMYAAVDSRDINSQPNWEESLYMYLYFVVFIIFGGFFTLNLFVGVIIDNFNQQKKKLGGQDIFMTEEQKKYYNAMKKLGSKKPQKPIPRPLNKYQGFVFDIVTRQAFDIIIMALICLNMITMMVETDNQSEEKTKVLGRINQFFVAVFTGECVMKMFALRQYYFTNGWNVFDFIVVILSISSLLFSAILSSLESYFSPTLLRVIRLARIGRILRLIRAAKGIRTLLFALMMSLPALFNIGLLLFLVMFIYSIFGMASFANVIDEAGIDDMFNFKTFGNSMLCLFQITTSAGWDGLLSPILNTGPPYCDPNRPNSNGSKGNCGSPAVGILFFTTYIIISFLIVVNMYIAVILENFNVATEESTEPLSEDDFDMFYETWEKFDPEATQFIAFSALSDFADTLSGPLRIPKPNQNILIQMDLPLVPGDKIHCLDILFAFTKNVLGESGELDSLKTNMEEKFMATNLSKASYEPIATTLRCKQEDISATIIQKAYRNYMLQRSLMLSNPLHVPRAEEDGVSLPREGYVTFMANDNGGLPDKSETASATSFPPSYDSVTRGLSDRANISTSSSMQNEDEVTAKEGKSPGPQ

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
17	Phosphorylation	TTNFRRFTPESLAEI CCCHHCCCHHHHHHH	25.08	27180971
20	Phosphorylation	FRRFTPESLAEIEKQ HHCCCHHHHHHHHHH	33.80	29899451
279	N-linked_Glycosylation	LKNKCIKNGTDPHKA CCCCHHHCCCCHHHC	38.39	-
288	N-linked_Glycosylation	TDPHKADNLSSEMAG CCHHHCCCCCHHHCC	46.83	-
311	N-linked_Glycosylation	TDPLLCGNGSDAGHC CCCEECCCCCCCCCC	45.88	-
334	N-linked_Glycosylation	TSDNPDFNYTSFDSF CCCCCCCCCCCHHHH	46.70	-
440	Phosphorylation	ALGIDTTSLYSHNGS HCCCCCHHCCCCCCC	27.66	-
443	Phosphorylation	IDTTSLYSHNGSPLA CCCHHCCCCCCCCCC	18.77	-
466	Phosphorylation	PRVKSRMSEGSTDDN CCHHHHCCCCCCCCC	37.38	-
478	Phosphorylation	DDNRSLQSDPYNQRR CCCCCCCCCCCCHHH	45.93	-
611	Phosphorylation	FRAQRAMSVVSIMTS HHHHHHHHHHHHHHH	20.55	-
614	Phosphorylation	QRAMSVVSIMTSVIE HHHHHHHHHHHHHHH	12.41	-
617	Phosphorylation	MSVVSIMTSVIEELE HHHHHHHHHHHHHHH	20.40	-
618	Phosphorylation	SVVSIMTSVIEELEE HHHHHHHHHHHHHHH	12.06	-
626	Phosphorylation	VIEELEESKLKCPPC HHHHHHHHCCCCCHH	33.63	-
1071	Phosphorylation	ERWQREESPRVPAEG HHHCCCCCCCCCCCC	17.16	23832136
1323	N-linked_Glycosylation	SNPFSVVNSTFVTNK CCCCCEEECEEECCH	32.93	-
1329	N-linked_Glycosylation	VNSTFVTNKSDCYNQ EECEEECCHHHHCCC	36.21	-
1337	N-linked_Glycosylation	KSDCYNQNNTGHFFW HHHHCCCCCCCCEEE	44.38	-
1448	Ubiquitination	KKYYNAMKKLGSKKP HHHHHHHHHHCCCCC	42.30	-
1452	Phosphorylation	NAMKKLGSKKPQKPI HHHHHHCCCCCCCCC	48.20	-
1498	Phosphorylation	MITMMVETDNQSEEK HHHHHHHCCCCCHHH	28.92	28576409
1500	N-linked_Glycosylation	TMMVETDNQSEEKTK HHHHHCCCCCHHHHH	55.48	-
1569	Phosphorylation	SSLESYFSPTLLRVI HHHHHHCCHHHHHHH	14.56	30387612
1571	Phosphorylation	LESYFSPTLLRVIRL HHHHCCHHHHHHHHH	36.91	28973931
1687	N-linked_Glycosylation	DPNRPNSNGSKGNCG CCCCCCCCCCCCCCC	66.45	-

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
-	K	Ubiquitination	E3 ubiquitin ligase	Nedd4l	Q8CFI0	PMID:22199232

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 SCNAA_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.