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Protein Page:
ENaC-beta (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
ENaC-beta 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. Controls the reabsorption of sodium in kidney, colon, lung and sweat glands. Also plays a role in taste perception. Defects in SCNN1B are a cause of autosomal recessive pseudohypoaldosteronism type 1 (AR-PHA1). PHA1 is a rare salt wasting disease resulting from target organ unresponsiveness to mineralocorticoids. There are 2 forms of PHA1: the autosomal recessive form that is severe, and the dominant form which is milder and due to defects in mineralocorticoid receptor. AR-PHA1 is characterized by an often fulminant presentation in the neonatal period with dehydration, hyponatraemia, hyperkalaemia, metabolic acidosis, failure to thrive and weight loss. The degree of channel function impairment differentially affects the renin-aldosterone system and urinary Na/K ratios, resulting in distinct genotype-phenotype relationships in PHA1 patients. Loss- of-function mutations are associated with a severe clinical course and age-dependent hyperactivation of the renin-aldosterone system. This feature is not observed in patients with missense mutations that reduce but do not eliminate channel function. Markedly reduced channel activity results in impaired linear growth and delayed puberty. Defects in SCNN1B are a cause of Liddle syndrome (LIDDS). It is an autosomal dominant disorder characterized by pseudoaldosteronism and hypertension associated with hypokalemic alkalosis. The disease is caused by constitutive activation of the renal epithelial sodium channel. Defects in SCNN1B are the cause of bronchiectasis with or without elevated sweat chloride type 1 (BESC1). A debilitating respiratory disease characterized by chronic, abnormal dilatation of the bronchi and other cystic fibrosis-like symptoms in the absence of known causes of bronchiectasis (cystic fibrosis, autoimmune diseases, ciliary dyskinesia, common variable immunodeficiency, foreign body obstruction). Clinical features include sub-normal lung function, sinopulmonary infections, chronic productive cough, excessive sputum production, and elevated sweat chloride in some cases. Belongs to the amiloride-sensitive sodium channel (TC 1.A.6) family. SCNN1B subfamily. 2 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Channel, sodium; Membrane protein, multi-pass; Membrane protein, integral; Transporter, ion channel
Cellular Component: integral to plasma membrane; apical plasma membrane; plasma membrane; external side of plasma membrane
Molecular Function: amiloride-sensitive sodium channel activity; protein binding; WW domain binding
Biological Process: sensory perception of taste; sodium ion transport; response to stimulus; sodium ion homeostasis; multicellular organismal water homeostasis; excretion; transmembrane transport
Reference #:  P51168 (UniProtKB)
Alt. Names/Synonyms: Amiloride-sensitive sodium channel subunit beta; BESC1; Beta-ENaC; Beta-NaCH; ENaC beta; ENaC-beta; ENaCB; ENaCbeta; Epithelial Na(+) channel subunit beta; epithelial sodium channel beta-2 subunit; epithelial sodium channel beta-3 subunit; nasal epithelial sodium channel beta subunit; Nonvoltage-gated sodium channel 1 subunit beta; SCNEB; SCNN1B; SCNNB; sodium channel, nonvoltage-gated 1, beta
Gene Symbols: SCNN1B
Molecular weight: 72,659 Da
Basal Isoelectric point: 5.89  Predict pI for various phosphorylation states
CST Pathways:  Insulin Receptor Signaling
Select Structure to View Below

ENaC-beta

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 4 K16-ub KGLHRLQkGPGYTYK
0 1 K182-ub TSSSASEkICNAHGC
0 2 K296-ub PGTEFGLkLILDIGQ
0 2 K350-ub SIGVLVDkLQRMGEP
0 2 K413-ub YPLPRGEkYCNNRDF
0 1 S488-p QSTNITLsRKGIVKL
0 1 Y498-p GIVKLNIyFQEFNyR
0 1 Y504-p IyFQEFNyRTIEESA
0 1 S561-p KLVALAKsLRQRRAQ
0 1 S570-p RQRRAQAsYAGPPPT
0 1 T594-p NFGFQPDtAPRSPNT
4 0 T615 QALPIPGTPPPNYDS
1 1 S633 QPLDVIESDSEGDAI
0 1 S635 LDVIESDSEGDAI__
  mouse

 
K16 KCLHRLQKGPGYTYK
S180 SSNPAPGSTCNAQGC
K294 PGTEFGLKLILDIGQ
K348 SIGVLVDKLQRKGEP
K411 YPLPEGEKYCNNRDF
S486 QSSNITLSRKGIVKL
Y496 GIVKLNIYFQEFNYR
Y502 IYFQEFNYRTIEESP
G559 KLVASCKGLRRRRPQ
P568 RRRRPQAPYTGPPPT
T592 NFGFQPDTTSCRPHG
T613-p QTLPIPGtPPPNYDS
S631-p QPLDTMEsDsEVEAI
S633-p LDTMEsDsEVEAI__
  rat

 
K16 KCLHRLQKGPGYTYK
S180 SSNPAPGSTCNAQGC
K294 PGTEFGLKLILDIGQ
K348 SIGVLLDKLQGKGEP
K411 YPLPAGEKYCNNRDF
S486 QSSNITLSRKGIVKL
Y496 GIVKLNIYFQEFNYR
Y502 IYFQEFNYRTIEESP
G559 KLVASCKGLRRRRPQ
P568 RRRRPQAPYTGPPPT
T592 NFGFQPDTTSCRPNA
T613-p QTLPIPGtPPPNYDS
S631-p QPLDTMEsDSEVEAI
S633 LDTMEsDSEVEAI__
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