SCN9A_MOUSE - dbPTM
SCN9A_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SCN9A_MOUSE
UniProt AC Q62205
Protein Name Sodium channel protein type 9 subunit alpha {ECO:0000250|UniProtKB:Q15858}
Gene Name Scn9a {ECO:0000312|MGI:MGI:107636}
Organism Mus musculus (Mouse).
Sequence Length 1984
Subcellular Localization Cell membrane
Multi-pass membrane protein . Cell projection . In neurite terminals.
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. [PubMed: 15123669 It is a tetrodotoxin-sensitive Na(+) channel isoform. Plays a role in pain mechanisms, especially in the development of inflammatory pain]
Protein Sequence MAMLPPPGPQSFVHFTKQSLALIEQRISEEKAKGHKDEKKDDEEEGPKPSSDLEAGKQLPFIYGDIPPGMVSEPLEDLDPYYADKKTFIVLNKGKAIFRFNATPALYMLSPFSPLRRISIKILVHSLFSMLIMCTILTNCIFMTMSNPPDWTKNVEYTFTGIYTFESLIKILARGFCVGEFTFLRDPWNWLDFVVIVFAYLTEFVNLGNVSALRTFRVLRALKTISVIPGLKTIVGALIQSVKKLSDVMILTVFCLSVFALIGLQLFMGNLKHKCFRKDLEQNETLESIMSTAESEEELKRYFYYLEGSKDALLCGFSTDSGQCPEGYECVTAGRNPDYGYTSFDTFGWAFLALFRLMTQDYWENLYQQTLRAAGKTYMIFFVVVIFLGSFYLINLILAVVAMAYEEQNQANIEEAKQKELEFQQMLDRLKKEQEEAEAIAAAAAEYTSLGRSRIMGLSESSSETSRLSSKSAKERRNRRKKKKQKLSSGEEKGDDEKLSKSGSEESIRKKSFHLGVEGHHRAREKRLSTPNQSPLSIRGSLFSARRSSRTSLFSFKGRGRDLGSETEFADDEHSIFGDNESRRGSLFVPHRPRERRSSNISQASRSPPVLPVNGKMHSAVDCNGVVSLVDGPSALMLPNGQLLPEVIIDKATSDDSGTTNQMRKKRLSSSYFLSEDMLNDPHLRQRAMSRASILTNTVEELEESRQKCPPWWYRFAHTFLIWNCSPYWIKFKKFIYFIVMDPFVDLAITICIVLNTLFMAMEHHPMTDEFKNVLAVGNLVFTGIFAAEMVLKLIAMDPYEYFQVGWNIFDSLIVTLSLVELFLADVEGLSVLRSFRLLRVFKLAKSWPTLNMLIKIIGNSVGALGNLTLVLAIIVFIFAVVGMQLFGKSYKECVCKINENCKLPRWHMNDFFHSFLIVFRVLCGEWIETMWDCMEVAGQTMCLIVYMMVMVIGNLVVLNLFLALLLSSFSSDNLTAIEEDTDANNLQIAVARIKRGINYVKQTLREFILKSFSKKPKGSKDTKRTADPNNKRENYISNRTLAEISKDHNFLKEKDKISGFSSSLDKSFMDENDYQSFIHNPSLTVTVPIAPGESDLENMNTEELSSDSDSDYSKERRNRSSSSECSTVDNPLPGEEEAEAEPINADEPEACFTDGCVRRFPCCQVNIDSGKGKVWWTIRKTCYRIVEHSWFESFIVLMILLSSGALAFEDIYIEKKKTIKIILEYADKIFTYIFILEMLLKWVAYGYKTYFTNAWCWLDFLIVDVSLVTLVANTLGYSDLGPIKSLRTLRALRPLRALSRFEGMRVVVNALIGAIPSIMNVLLVCLIFWLIFSIMGVNLFAGKFYECVNTTDGSRFSVSQVANRSECFALMNVSGNVRWKNLKVNFDNVGLGYLSLLQVATFKGWMDIMYAAVDSVNVNAQPIYEYNLYMYIYFVIFIIFGSFFTLNLFIGVIIDNFNQQKKKLGGQDIFMTEEQKKYYNAMKKLGSKKPQKPIPRPGNKFQGCIFDLVTNQAFDITIMVLICLNMVTMMVEKEGQTDYMSFVLYWINVVFIILFTGECVLKLISLRHYYFTVGWNIFDFVVVILSIVGMFLAEMIEKYFVSPTLFRVIRLARIGRILRLIKGAKGIRTLLFALMMSLPALFNIGLLLFLVMFIYAIFGMSNFAYVKKEAGINDMFNFETFGNSMICLFQITTSAGWDGLLAPILNSAPPDCDPKKVHPGSSVEGDCGNPSVGIFYFVSYIIISFLVVVNMYIAVILENFSVATEESTEPLSEDDFEMFYEVWEKFDPDATQFIEFCKLSDFAAALDPPLLIAKPNKVQLIAMDLPMVSGDRIHCLDILFAFTKRVLGESGEMDSLRSQMEERFMSANPSKVSYEPITTTLKRKQEDVSATIIQRAYRRYRLRQNVKNISSIYIKDGDRDDDLPNKEDIVFDNVNENSSPEKTDATASTISPPSYDSVTKPDQEKYETDKTEKEDKEKDESRK
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 Orthologous
Protein Cluster
86UbiquitinationDPYYADKKTFIVLNK
CCCCCCCCEEEEEEC
49.57-
302PhosphorylationSEEELKRYFYYLEGS
CHHHHHHHHHHHHCC
8.37-
304PhosphorylationEELKRYFYYLEGSKD
HHHHHHHHHHHCCCC
9.75-
305PhosphorylationELKRYFYYLEGSKDA
HHHHHHHHHHCCCCE
6.59-
309PhosphorylationYFYYLEGSKDALLCG
HHHHHHCCCCEEEEC
20.28-
447PhosphorylationIAAAAAEYTSLGRSR
HHHHHHHHHHHCCHH
9.2629899451
448PhosphorylationAAAAAEYTSLGRSRI
HHHHHHHHHHCCHHH
14.6928066266
449PhosphorylationAAAAEYTSLGRSRIM
HHHHHHHHHCCHHHC
28.1128066266
453PhosphorylationEYTSLGRSRIMGLSE
HHHHHCCHHHCCCCC
25.1029899451
502PhosphorylationDDEKLSKSGSEESIR
CHHHHHCCCCHHHHH
44.1420415495
504PhosphorylationEKLSKSGSEESIRKK
HHHHCCCCHHHHHHH
45.3320415495
507PhosphorylationSKSGSEESIRKKSFH
HCCCCHHHHHHHHHC
24.5220415495
512PhosphorylationEESIRKKSFHLGVEG
HHHHHHHHHCCCCCC
22.4229899451
529PhosphorylationRAREKRLSTPNQSPL
HHHHHCCCCCCCCCC
45.9428066266
530PhosphorylationAREKRLSTPNQSPLS
HHHHCCCCCCCCCCH
30.7428066266
534PhosphorylationRLSTPNQSPLSIRGS
CCCCCCCCCCHHCCC
34.1528066266
537PhosphorylationTPNQSPLSIRGSLFS
CCCCCCCHHCCCHHH
17.3928066266
551PhosphorylationSARRSSRTSLFSFKG
HCCCCCCCCCEEECC
31.5620139300
565PhosphorylationGRGRDLGSETEFADD
CCCCCCCCCCCCCCC
48.9528066266
567PhosphorylationGRDLGSETEFADDEH
CCCCCCCCCCCCCCC
37.7928066266
598PhosphorylationHRPRERRSSNISQAS
CCCCCCCCCCCCHHC
33.6829899451
599PhosphorylationRPRERRSSNISQASR
CCCCCCCCCCCHHCC
36.0529899451
605PhosphorylationSSNISQASRSPPVLP
CCCCCHHCCCCCEEC
26.1729899451
669PhosphorylationQMRKKRLSSSYFLSE
HHHHHHHCCHHCCCH
22.6729899451
670PhosphorylationMRKKRLSSSYFLSED
HHHHHHCCHHCCCHH
33.3829899451
671PhosphorylationRKKRLSSSYFLSEDM
HHHHHCCHHCCCHHH
19.2729899451
672PhosphorylationKKRLSSSYFLSEDML
HHHHCCHHCCCHHHH
15.5329899451
675PhosphorylationLSSSYFLSEDMLNDP
HCCHHCCCHHHHCCH
22.96-
690PhosphorylationHLRQRAMSRASILTN
HHHHHHHHHHHHHHH
24.58-
693PhosphorylationQRAMSRASILTNTVE
HHHHHHHHHHHHHHH
19.6128066266
696PhosphorylationMSRASILTNTVEELE
HHHHHHHHHHHHHHH
27.4628066266
698PhosphorylationRASILTNTVEELEES
HHHHHHHHHHHHHHH
24.8628066266
705PhosphorylationTVEELEESRQKCPPW
HHHHHHHHHHHCCCH
30.5428066266
968PhosphorylationLFLALLLSSFSSDNL
HHHHHHHHHCCCCCC
29.34-
1062PhosphorylationKDKISGFSSSLDKSF
HHCCCCCCCCCCHHH
23.6528066266
1063PhosphorylationDKISGFSSSLDKSFM
HCCCCCCCCCCHHHC
32.4328066266
1064PhosphorylationKISGFSSSLDKSFMD
CCCCCCCCCCHHHCC
39.1120415495
1075PhosphorylationSFMDENDYQSFIHNP
HHCCCCCHHHHCCCC
20.0325521595
1095PhosphorylationVPIAPGESDLENMNT
EEECCCCHHHHCCCH
54.1025521595
1484UbiquitinationKKYYNAMKKLGSKKP
HHHHHHHHHHCCCCC
42.30-
1488PhosphorylationNAMKKLGSKKPQKPI
HHHHHHCCCCCCCCC
48.20-
1867PhosphorylationQMEERFMSANPSKVS
HHHHHHHCCCCCCCC
23.3728059163
1874PhosphorylationSANPSKVSYEPITTT
CCCCCCCCCCCCCHH
27.7528059163
1883UbiquitinationEPITTTLKRKQEDVS
CCCCHHHHHCHHCHH
56.30-
1939PhosphorylationFDNVNENSSPEKTDA
EECCCCCCCCCCCCC
40.8823375375
1940PhosphorylationDNVNENSSPEKTDAT
ECCCCCCCCCCCCCC
48.9723375375

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
1488SPhosphorylationKinasePKC-Uniprot
-KUbiquitinationE3 ubiquitin ligaseNedd4lQ8CFI0
PMID:22199232

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
1488SPhosphorylation

-

Disease-associated PTM Sites based on SAP

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

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of SCN9A_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NEDD4_MOUSENedd4physical
15123669

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SCN9A_MOUSE

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Related Literatures of Post-Translational Modification

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