SCNBA_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SCNBA_MOUSE
• UniProt AC: Q9R053
• Protein Name: Sodium channel protein type 11 subunit alpha
• Gene Name: Scn11a
• Organism: Mus musculus (Mouse).
• Sequence Length: 1765
• Subcellular Localization: Cell membrane ; Multi-pass membrane protein .
• 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 sodium ions may pass in accordance with their electrochemical gradient. It is a tetrodotoxin-resistant sodium channel isoform. Also involved, with the contribution of the receptor tyrosine kinase NTRK2, in rapid BDNF-evoked neuronal depolarization (By similarity)..
• Protein Sequence: MEERYYPVIFPDERNFRPFTFDSLAAIEKRITIQKEKKKSKDKAATEPQPRPQLDLKASRKLPKLYGDVPPDLIAKPLEDLDPFYKDHKTFMVLNKKRTIYRFSAKRALFILGPFNPIRSFMIRISVHSVFSMFIICTVIINCMFMANNSSVDSRPSSNIPEYVFIGIYVLEAVIKILARGFIVDEFSYLRDPWNWLDFIVIGTAIAPCFLGNKVNNLSTLRTFRVLRALKAISVISGLKVIVGALLRSVKKLVDVMVLTLFCLSIFALVGQQLFMGILSQKCIKDDCGPNAFSNKDCFVKENDSEDFIMCGNWLGRRSCPDGSTCNKTTFNPDYNYTNFDSFGWSFLAMFRVMTQDSWEKLYRQILRTSGIYFVFFFVVVIFLGSFYLLNLTLAVVTMAYEEQNRNVAAETEAKEKMFQEAQQLLREEKEALVAMGIDRTSLNSLQASSFSPKKRKFFGSKTRKSFFMRGSKTARASASDSEDDASKNPQLLEQTKRLSQNLPVELFDEHVDPLHRQRALSAVSILTITMQEQEKSQEPCFPCGKNLASKYLVWECSPPWLCIKKVLQTIMTDPFTELAITICIIVNTVFLAMEHHNMDNSLKDILKIGNWVFTGIFIAEMCLKIIALDPYHYFRHGWNIFDSIVALVSLADVLFHKLSKNLSFLASLRVLRVFKLAKSWPTLNTLIKIIGHSVGALGNLTVVLTIVVFIFSVVGMRLFGAKFNKTCSTSPESLRRWHMGDFYHSFLVVFRILCGEWIENMWECMQEMEGSPLCVIVFVLIMVVGKLVVLNLFIALLLNSFSNEEKDGNPEGETRKTKVQLALDRFSRAFYFMARALQNFCCKRCRRQNSPKPNEATESFAGESRDTATLDTRSWKEYDSEMTLYTGQAGAPLAPLAKEEDDMECCGECDASPTSQPSEEAQACDLPLKTKRLPSPDDHGVEMEVFSEEDPNLTIQSARKKSDAASMLSECSTIDLNDIFRNLQKTVSPQKQPDRCFPKGLSCIFLCCKTIKKKSPWVLWWNLRKTCYQIVKHSWFESFIIFVILLSSGALIFEDVNLPSRPQVEKLLKCTDNIFTFIFLLEMILKWVAFGFRKYFTSAWCWLDFLIVVVSGLSLTNLPNLKSFRNLRALRPLRALSQFEGMKVVVNALMSAIPAILNVLLVCLIFWLIFCILGVNFFSGKFGRCINGTDINKYFNASNVPNQSQCLVSNYTWKVPNVNFDNVGNAYLALLQVATYKGWLDIMNAAVDSRGKDEQPAFEANLYAYLYFVVFIIFGSFFTLNLFIGVIIDNFNQQQKKLGGQDIFMTEEQKKYYNAMKKLGTKKPQKPIPRPLNKCQAFVFDLVTSQVFDVIILGLIVTNMIIMMAESEGQPNEVKKIFDILNIVFVVIFTVECLIKVFALRQHYFTNGWNLFDCVVVVLSIISTLVSGLENSNVFPPTLFRIVRLARIGRILRLVRAARGIRTLLFALMMSLPSLFNIGLLLFLVMFIYAIFGMNWFSKVKRGSGIDDIFNFDTFSGSMLCLFQITTSAGWDALLNPMLESKASCNSSSQESCQQPQIAIVYFVSYIIISFLIVVNMYIAVILENFNTATEESEDPLGEDDFEIFYEIWEKFDPEATQFIQYSSLSDFADALPEPLRVAKPNRFQFLMMDLPMVMGDRLHCMDVLFAFTTRVLGNSSGLDTMKAMMEEKFMEANPFKKLYEPIVTTTKRKEEEECAAVIQRAYRRHMEKMIKLKLKGRSSSSLQVFCNGDLSSLDVPKIKVHCD

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
149	N-linked_Glycosylation	NCMFMANNSSVDSRP HHHHHCCCCCCCCCC	26.56	-
217	N-linked_Glycosylation	FLGNKVNNLSTLRTF HCCCCCCCHHHHHHH	38.05	-
303	N-linked_Glycosylation	KDCFVKENDSEDFIM CCCEECCCCCCCCEE	53.01	-
327	N-linked_Glycosylation	CPDGSTCNKTTFNPD CCCCCCCCCCCCCCC	44.81	-
336	N-linked_Glycosylation	TTFNPDYNYTNFDSF CCCCCCCCCCCCCHH	44.53	-
466	Phosphorylation	FGSKTRKSFFMRGSK CCCCCCCCHHCCCCC	22.04	24719451
472	Phosphorylation	KSFFMRGSKTARASA CCHHCCCCCCCCCCC	19.23	24719451
662	N-linked_Glycosylation	LFHKLSKNLSFLASL HHHHHCCCHHHHHHH	37.23	-
725	N-linked_Glycosylation	RLFGAKFNKTCSTSP HHHCCCCCCCCCCCH	37.71	-
734	Phosphorylation	TCSTSPESLRRWHMG CCCCCHHHHHHHHCC	30.47	17203969
879	Phosphorylation	DTRSWKEYDSEMTLY CCCCHHHCCCCCEEE	22.50	23140645
881	Phosphorylation	RSWKEYDSEMTLYTG CCHHHCCCCCEEEEC	28.50	23140645
884	Phosphorylation	KEYDSEMTLYTGQAG HHCCCCCEEEECCCC	16.74	23140645
886	Phosphorylation	YDSEMTLYTGQAGAP CCCCCEEEECCCCCC	10.31	23140645
887	Phosphorylation	DSEMTLYTGQAGAPL CCCCEEEECCCCCCC	26.40	23140645
932	Acetylation	CDLPLKTKRLPSPDD CCCCCCCCCCCCCCC	50.80	7721537
961	Acetylation	LTIQSARKKSDAASM CCHHHHHCHHHHHHH	57.24	7721545
962	Acetylation	TIQSARKKSDAASML CHHHHHCHHHHHHHH	48.27	7721557
963	Phosphorylation	IQSARKKSDAASMLS HHHHHCHHHHHHHHH	35.20	20139300
1072	Phosphorylation	VEKLLKCTDNIFTFI HHHHHHCCCHHHHHH	30.41	26643407
1188	N-linked_Glycosylation	GKFGRCINGTDINKY CCCCCCCCCCCHHHH	51.44	-
1197	N-linked_Glycosylation	TDINKYFNASNVPNQ CCHHHHCCCCCCCCH	39.09	-
1203	N-linked_Glycosylation	FNASNVPNQSQCLVS CCCCCCCCHHHCEEC	50.26	-
1211	N-linked_Glycosylation	QSQCLVSNYTWKVPN HHHCEECCCEEECCC	30.67	-
1250	Phosphorylation	IMNAAVDSRGKDEQP HHHHHHHCCCCCCCC	36.01	17203969
1318	Ubiquitination	KKYYNAMKKLGTKKP HHHHHHHHHHCCCCC	42.30	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of SCNBA_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of SCNBA_MOUSE !!

Disease-associated PTM Sites based on SAP

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

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

Protein-Protein Interaction

Oops, there are no PPI records of SCNBA_MOUSE !!

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry.";
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
J. Proteome Res. 6:250-262(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-734 AND SER-1250, ANDMASS SPECTROMETRY.
PubMed: 17203969