SCN4A_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SCN4A_HUMAN
• UniProt AC: P35499
• Protein Name: Sodium channel protein type 4 subunit alpha
• Gene Name: SCN4A
• Organism: Homo sapiens (Human).
• Sequence Length: 1836
• 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 Na(+) ions may pass in accordance with their electrochemical gradient. This sodium channel may be present in both denervated and innervated skeletal muscle..
• Protein Sequence: MARPSLCTLVPLGPECLRPFTRESLAAIEQRAVEEEARLQRNKQMEIEEPERKPRSDLEAGKNLPMIYGDPPPEVIGIPLEDLDPYYSNKKTFIVLNKGKAIFRFSATPALYLLSPFSVVRRGAIKVLIHALFSMFIMITILTNCVFMTMSDPPPWSKNVEYTFTGIYTFESLIKILARGFCVDDFTFLRDPWNWLDFSVIMMAYLTEFVDLGNISALRTFRVLRALKTITVIPGLKTIVGALIQSVKKLSDVMILTVFCLSVFALVGLQLFMGNLRQKCVRWPPPFNDTNTTWYSNDTWYGNDTWYGNEMWYGNDSWYANDTWNSHASWATNDTFDWDAYISDEGNFYFLEGSNDALLCGNSSDAGHCPEGYECIKTGRNPNYGYTSYDTFSWAFLALFRLMTQDYWENLFQLTLRAAGKTYMIFFVVIIFLGSFYLINLILAVVAMAYAEQNEATLAEDKEKEEEFQQMLEKFKKHQEELEKAKAAQALEGGEADGDPAHGKDCNGSLDTSQGEKGAPRQSSSGDSGISDAMEELEEAHQKCPPWWYKCAHKVLIWNCCAPWLKFKNIIHLIVMDPFVDLGITICIVLNTLFMAMEHYPMTEHFDNVLTVGNLVFTGIFTAEMVLKLIAMDPYEYFQQGWNIFDSIIVTLSLVELGLANVQGLSVLRSFRLLRVFKLAKSWPTLNMLIKIIGNSVGALGNLTLVLAIIVFIFAVVGMQLFGKSYKECVCKIALDCNLPRWHMHDFFHSFLIVFRILCGEWIETMWDCMEVAGQAMCLTVFLMVMVIGNLVVLNLFLALLLSSFSADSLAASDEDGEMNNLQIAIGRIKLGIGFAKAFLLGLLHGKILSPKDIMLSLGEADGAGEAGEAGETAPEDEKKEPPEEDLKKDNHILNHMGLADGPPSSLELDHLNFINNPYLTIQVPIASEESDLEMPTEEETDTFSEPEDSKKPPQPLYDGNSSVCSTADYKPPEEDPEEQAEENPEGEQPEECFTEACVQRWPCLYVDISQGRGKKWWTLRRACFKIVEHNWFETFIVFMILLSSGALAFEDIYIEQRRVIRTILEYADKVFTYIFIMEMLLKWVAYGFKVYFTNAWCWLDFLIVDVSIISLVANWLGYSELGPIKSLRTLRALRPLRALSRFEGMRVVVNALLGAIPSIMNVLLVCLIFWLIFSIMGVNLFAGKFYYCINTTTSERFDISEVNNKSECESLMHTGQVRWLNVKVNYDNVGLGYLSLLQVATFKGWMDIMYAAVDSREKEEQPQYEVNLYMYLYFVIFIIFGSFFTLNLFIGVIIDNFNQQKKKLGGKDIFMTEEQKKYYNAMKKLGSKKPQKPIPRPQNKIQGMVYDLVTKQAFDITIMILICLNMVTMMVETDNQSQLKVDILYNINMIFIIIFTGECVLKMLALRQYYFTVGWNIFDFVVVILSIVGLALSDLIQKYFVSPTLFRVIRLARIGRVLRLIRGAKGIRTLLFALMMSLPALFNIGLLLFLVMFIYSIFGMSNFAYVKKESGIDDMFNFETFGNSIICLFEITTSAGWDGLLNPILNSGPPDCDPNLENPGTSVKGDCGNPSIGICFFCSYIIISFLIVVNMYIAIILENFNVATEESSEPLGEDDFEMFYETWEKFDPDATQFIAYSRLSDFVDTLQEPLRIAKPNKIKLITLDLPMVPGDKIHCLDILFALTKEVLGDSGEMDALKQTMEEKFMAANPSKVSYEPITTTLKRKHEEVCAIKIQRAYRRHLLQRSMKQASYMYRHSHDGSGDDAPEKEGLLANTMSKMYGHENGNSSSPSPEEKGEAGDAGPTMGLMPISPSDTAWPPAPPPGQTVRPGVKESLV

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
172	Phosphorylation	TGIYTFESLIKILAR EEEEEHHHHHHHHHC	31.07	24719451
187	Phosphorylation	GFCVDDFTFLRDPWN CCCCCCCCCCCCCCC	28.84	-
214	N-linked_Glycosylation	TEFVDLGNISALRTF HHHCCCCCHHHHHHH	32.13	UniProtKB CARBOHYD
231	Phosphorylation	LRALKTITVIPGLKT HHHHCCCCCCCCHHH	20.02	-
288	N-linked_Glycosylation	VRWPPPFNDTNTTWY CCCCCCCCCCCCCCC	62.05	UniProtKB CARBOHYD
291	N-linked_Glycosylation	PPPFNDTNTTWYSND CCCCCCCCCCCCCCC	38.07	UniProtKB CARBOHYD
297	N-linked_Glycosylation	TNTTWYSNDTWYGND CCCCCCCCCCCCCCC	34.73	UniProtKB CARBOHYD
303	N-linked_Glycosylation	SNDTWYGNDTWYGNE CCCCCCCCCCEECCC	28.04	UniProtKB CARBOHYD
315	N-linked_Glycosylation	GNEMWYGNDSWYAND CCCEEECCCCCCCCC	25.17	UniProtKB CARBOHYD
321	N-linked_Glycosylation	GNDSWYANDTWNSHA CCCCCCCCCCCCCCC	31.39	UniProtKB CARBOHYD
333	N-linked_Glycosylation	SHASWATNDTFDWDA CCCHHCCCCCCCCEE	38.28	UniProtKB CARBOHYD
362	N-linked_Glycosylation	NDALLCGNSSDAGHC CCEEEECCCCCCCCC	37.03	30190309
457	Phosphorylation	YAEQNEATLAEDKEK HHHHCCCCCCCHHHH	21.96	-
666	Phosphorylation	LANVQGLSVLRSFRL CCCCCCHHHHHHHHH	26.40	24719451
850	Phosphorylation	LLHGKILSPKDIMLS HHHCCCCCHHHHHHH	33.12	24719451
1006	Phosphorylation	VQRWPCLYVDISQGR HHHCCEEEEECCCCC	11.64	25332170
1010	Phosphorylation	PCLYVDISQGRGKKW CEEEEECCCCCCCCH	23.32	25332170
1063	Phosphorylation	EQRRVIRTILEYADK HHHHHHHHHHHHHHH	20.84	29116813
1067	Phosphorylation	VIRTILEYADKVFTY HHHHHHHHHHHHHHH	19.36	29116813
1073	Phosphorylation	EYADKVFTYIFIMEM HHHHHHHHHHHHHHH	20.78	28348404
1074	Phosphorylation	YADKVFTYIFIMEML HHHHHHHHHHHHHHH	5.16	28348404
1191	N-linked_Glycosylation	GKFYYCINTTTSERF CEEEEEEECCCCCCC	28.01	UniProtKB CARBOHYD
1205	N-linked_Glycosylation	FDISEVNNKSECESL CCHHHCCCHHHHCHH	55.17	30190309
1318	Acetylation	FMTEEQKKYYNAMKK CCCHHHHHHHHHHHH	53.30	30592219
1319	Phosphorylation	MTEEQKKYYNAMKKL CCHHHHHHHHHHHHH	14.69	22817900
1320	Phosphorylation	TEEQKKYYNAMKKLG CHHHHHHHHHHHHHC	12.81	22817900
1328	Phosphorylation	NAMKKLGSKKPQKPI HHHHHHCCCCCCCCC	48.20	10532948
1443	Phosphorylation	LIQKYFVSPTLFRVI HHHHHCCCHHHHHHH	11.41	28348404
1445	Phosphorylation	QKYFVSPTLFRVIRL HHHCCCHHHHHHHHH	30.90	28348404
1711	Phosphorylation	KFMAANPSKVSYEPI HHHCCCCCCCCCCCC	45.56	-
1715	Phosphorylation	ANPSKVSYEPITTTL CCCCCCCCCCCCHHC	28.81	25884760
1719	Phosphorylation	KVSYEPITTTLKRKH CCCCCCCCHHCHHCH	25.17	-
1720	Phosphorylation	VSYEPITTTLKRKHE CCCCCCCHHCHHCHH	30.74	-
1721	Phosphorylation	SYEPITTTLKRKHEE CCCCCCHHCHHCHHH	22.95	-
1746	Phosphorylation	RRHLLQRSMKQASYM HHHHHHHHHHHHHHH	19.85	-
1751	Phosphorylation	QRSMKQASYMYRHSH HHHHHHHHHHHHCCC	14.13	23532336
1754	Phosphorylation	MKQASYMYRHSHDGS HHHHHHHHHCCCCCC	9.28	23532336
1761	Phosphorylation	YRHSHDGSGDDAPEK HHCCCCCCCCCCCHH	45.14	23532336
1780	Phosphorylation	ANTMSKMYGHENGNS HHHHHHHHCCCCCCC	21.04	24114839
1789	Phosphorylation	HENGNSSSPSPEEKG CCCCCCCCCCHHHCC	29.26	26437602
1791	Phosphorylation	NGNSSSPSPEEKGEA CCCCCCCCHHHCCCC	47.06	26437602

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
1328	S	Phosphorylation	Kinase	PKC	-	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
1328	S	Phosphorylation	Phosphorylation at Ser-1328 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 SCN4A_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NHRF1_HUMAN	SLC9A3R1	physical	9677412

Drug and Disease Associations

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