SCNNB_HUMAN - dbPTM
SCNNB_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SCNNB_HUMAN
UniProt AC P51168
Protein Name Amiloride-sensitive sodium channel subunit beta
Gene Name SCNN1B
Organism Homo sapiens (Human).
Sequence Length 640
Subcellular Localization Apical cell membrane
Multi-pass membrane protein . Cytoplasmic vesicle membrane . Apical membrane of epithelial cells.
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. 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 sweat glands. Also plays a role in taste perception..
Protein Sequence MHVKKYLLKGLHRLQKGPGYTYKELLVWYCDNTNTHGPKRIICEGPKKKAMWFLLTLLFAALVCWQWGIFIRTYLSWEVSVSLSVGFKTMDFPAVTICNASPFKYSKIKHLLKDLDELMEAVLERILAPELSHANATRNLNFSIWNHTPLVLIDERNPHHPMVLDLFGDNHNGLTSSSASEKICNAHGCKMAMRLCSLNRTQCTFRNFTSATQALTEWYILQATNIFAQVPQQELVEMSYPGEQMILACLFGAEPCNYRNFTSIFYPHYGNCYIFNWGMTEKALPSANPGTEFGLKLILDIGQEDYVPFLASTAGVRLMLHEQRSYPFIRDEGIYAMSGTETSIGVLVDKLQRMGEPYSPCTVNGSEVPVQNFYSDYNTTYSIQACLRSCFQDHMIRNCNCGHYLYPLPRGEKYCNNRDFPDWAHCYSDLQMSVAQRETCIGMCKESCNDTQYKMTISMADWPSEASEDWIFHVLSQERDQSTNITLSRKGIVKLNIYFQEFNYRTIEESAANNIVWLLSNLGGQFGFWMGGSVLCLIEFGEIIIDFVWITIIKLVALAKSLRQRRAQASYAGPPPTVAELVEAHTNFGFQPDTAPRSPNTGPYPSEQALPIPGTPPPNYDSLRLQPLDVIESDSEGDAI
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
16UbiquitinationKGLHRLQKGPGYTYK
HHHHHHHCCCCCCCH
72.21-
20PhosphorylationRLQKGPGYTYKELLV
HHHCCCCCCCHHEEE
15.2722210691
21PhosphorylationLQKGPGYTYKELLVW
HHCCCCCCCHHEEEE
33.7522210691
182UbiquitinationTSSSASEKICNAHGC
CCCCHHHHHHHHHHC
50.49-
260N-linked_GlycosylationAEPCNYRNFTSIFYP
CCCCCCCCCCEEEEC
33.90UniProtKB CARBOHYD
296UbiquitinationPGTEFGLKLILDIGQ
CCCHHHCEEEEEECC
33.58-
350UbiquitinationSIGVLVDKLQRMGEP
CHHHHHHHHHHCCCC
38.75-
413UbiquitinationYPLPRGEKYCNNRDF
EECCCCCCCCCCCCC
58.91-
488PhosphorylationQSTNITLSRKGIVKL
CCCCEEEECCCEEEE
24.24-
498PhosphorylationGIVKLNIYFQEFNYR
CEEEEEEEEEECCCH
9.72-
504PhosphorylationIYFQEFNYRTIEESA
EEEEECCCHHHHHHH
17.91-
561PhosphorylationKLVALAKSLRQRRAQ
HHHHHHHHHHHHHHH
24.1522496350
570PhosphorylationRQRRAQASYAGPPPT
HHHHHHHHHCCCCCC
11.93-
594PhosphorylationNFGFQPDTAPRSPNT
HCCCCCCCCCCCCCC
45.29-
615PhosphorylationQALPIPGTPPPNYDS
HCCCCCCCCCCCCCC
27.5424719451
633PhosphorylationQPLDVIESDSEGDAI
CCCCEEECCCCCCCC
35.0024719451
635PhosphorylationLDVIESDSEGDAI--
CCEEECCCCCCCC--
53.4028857561

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
-KUbiquitinationE3 ubiquitin ligaseNEDD4P46934
PMID:19953087
-KUbiquitinationE3 ubiquitin ligaseNEDD4LQ96PU5
PMID:17502380

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

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

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 SCNNB_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NEDD4_HUMANNEDD4physical
10642508
NEDD4_HUMANNEDD4physical
11244092
NED4L_HUMANNEDD4Lphysical
11244092
HECW1_HUMANHECW1physical
11244092
ITCH_HUMANITCHphysical
11244092
WWP2_HUMANWWP2physical
11244092
EPN1_HUMANEPN1physical
16574660
SGK1_HUMANSGK1physical
20237237
NEDD4_HUMANNEDD4physical
20237237
NED4L_HUMANNEDD4Lphysical
16416336
UBP2_HUMANUSP2physical
18701608
SCNNG_HUMANSCNN1Gphysical
22526458
SCNNA_HUMANSCNN1Aphysical
22526458
SERP1_HUMANSERP1physical
22526458
NED4L_HUMANNEDD4Lphysical
15814530
UBP8_HUMANUSP8physical
23297398
HGS_HUMANHGSphysical
20675381

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

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Related Literatures of Post-Translational Modification

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