dbPTM

SCNNA_RAT - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SCNNA_RAT
UniProt AC	P37089
Protein Name	Amiloride-sensitive sodium channel subunit alpha
Gene Name	Scnn1a
Organism	Rattus norvegicus (Rat).
Sequence Length	698
Subcellular Localization	Apical cell membrane Multi-pass membrane protein . Cell projection, cilium . Cytoplasmic granule . Cytoplasm . Cytoplasmic vesicle, secretory vesicle, acrosome . Cell projection, cilium, flagellum . In multi-ciliated cells, located on cilia. In non
Protein Description	Sodium permeable non-voltage-sensitive ion channel inhibited by the diuretic amiloride. Mediates the electrodiffusion of the luminal sodium (and water, which follows osmotically) through the apical membrane of epithelial cells. [PubMed: 8382172 Plays an essential role in electrolyte and blood pressure homeostasis, but also in airway surface liquid homeostasis, which is important for proper clearance of mucus. Controls the reabsorption of sodium in kidney, colon, lung and eccrine sweat glands. Also plays a role in taste perception (By similarity]
Protein Sequence	MLDHTRAPELNIDLDLHASNSPKGSMKGNQFKEQDPCPPQPMQGLGKGDKREEQGLGPEPSAPRQPTEEEEALIEFHRSYRELFQFFCNNTTIHGAIRLVCSKHNRMKTAFWAVLWLCTFGMMYWQFALLFEEYLSYPVSLNINLNSDKLVFPAVTVCTLNPYRYTEIKEELEELDRITEQTLFDLYKYNSSYTRQAGARRRSSRDLLGAFPHPLQRLRTPPPPYSGRTARSGSSSVRDNNPQVDRKDWKIGFQLCNQNKSDCFYQTYSSGVDAVREWYRFHYINILSRLSDTSPALEEEALGNFIFTCRFNQAPCNQANYSKFHHPMYGNCYTFNDKNNSNLWMSSMPGVNNGLSLTLRTEQNDFIPLLSTVTGARVMVHGQDEPAFMDDGGFNLRPGVETSISMRKEALDSLGGNYGDCTENGSDVPVKNLYPSKYTQQVCIHSCFQENMIKKCGCAYIFYPKPKGVEFCDYRKQSSWGYCYYKLQGAFSLDSLGCFSKCRKPCSVINYKLSAGYSRWPSVKSQDWIFEMLSLQNNYTINNKRNGVAKLNIFFKELNYKTNSESPSVTMVSLLSNLGSQWSLWFGSSVLSVVEMAELIFDLLVITLLMLLRRFRSRYWSPGRGARGAREVASTPASSFPSRFCPHPTSPPPSLPQQGMTPPLALTAPPPAYATLGPSAPPLDSAAPDCSACALAAL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
190	N-linked_Glycosylation	LFDLYKYNSSYTRQA HHHHHHCCCHHHHCC	21.96	7929098
259	N-linked_Glycosylation	GFQLCNQNKSDCFYQ EEECCCCCCCCCEEE	31.63	7929098
283	Phosphorylation	REWYRFHYINILSRL HHHHHHHHHHHHHHH	7.92	25575281
288	Phosphorylation	FHYINILSRLSDTSP HHHHHHHHHHCCCCH	27.64	25575281
291	Phosphorylation	INILSRLSDTSPALE HHHHHHHCCCCHHHH	37.42	25575281
293	Phosphorylation	ILSRLSDTSPALEEE HHHHHCCCCHHHHHH	32.98	25575281
294	Phosphorylation	LSRLSDTSPALEEEA HHHHCCCCHHHHHHH	17.11	25575281
320	N-linked_Glycosylation	QAPCNQANYSKFHHP CCCCCCCCHHCCCCC	31.67	7929098
339	N-linked_Glycosylation	CYTFNDKNNSNLWMS EEEEECCCCCCCEEC	61.09	7929098
424	N-linked_Glycosylation	NYGDCTENGSDVPVK CCCCCCCCCCCCCCC	36.80	7929098
538	N-linked_Glycosylation	EMLSLQNNYTINNKR HHHHHCCCCEECCCC	23.51	7929098
621	Phosphorylation	RFRSRYWSPGRGARG HHHHHHCCCCCCCCC	14.45	21220922

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
621	S	Phosphorylation	Kinase	AKT1	P31749	PSP
621	S	Phosphorylation	Kinase	SGK1	O00141	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of SCNNA_RAT !!

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 SCNNA_RAT !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
UBC_HUMAN	UBC	physical	16099816
NEDD4_RAT	Nedd4	physical	8665844

Drug and Disease Associations

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

Regulatory Network of SCNNA_RAT

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Membrane topology of the amiloride-sensitive epithelial sodiumchannel."; Snyder P.M., McDonald F.J., Stokes J.B., Welsh M.J.; J. Biol. Chem. 269:24379-24383(1994). Cited for: TOPOLOGY, AND GLYCOSYLATION AT ASN-190; ASN-259; ASN-320; ASN-339;ASN-424 AND ASN-538.	7929098 [Abstract]