SCNND_HUMAN - dbPTM
SCNND_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SCNND_HUMAN
UniProt AC P51172
Protein Name Amiloride-sensitive sodium channel subunit delta
Gene Name SCNN1D
Organism Homo sapiens (Human).
Sequence Length 638
Subcellular Localization Cell membrane
Multi-pass membrane protein .
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. Controls the reabsorption of sodium in kidney, colon, lung and sweat glands. Also plays a role in taste perception..
Protein Sequence MAEHRSMDGRMEAATRGGSHLQAAAQTPPRPGPPSAPPPPPKEGHQEGLVELPASFRELLTFFCTNATIHGAIRLVCSRGNRLKTTSWGLLSLGALVALCWQLGLLFERHWHRPVLMAVSVHSERKLLPLVTLCDGNPRRPSPVLRHLELLDEFARENIDSLYNVNLSKGRAALSATVPRHEPPFHLDREIRLQRLSHSGSRVRVGFRLCNSTGGDCFYRGYTSGVAAVQDWYHFHYVDILALLPAAWEDSHGSQDGHFVLSCSYDGLDCQARQFRTFHHPTYGSCYTVDGVWTAQRPGITHGVGLVLRVEQQPHLPLLSTLAGIRVMVHGRNHTPFLGHHSFSVRPGTEATISIREDEVHRLGSPYGHCTAGGEGVEVELLHNTSYTRQACLVSCFQQLMVETCSCGYYLHPLPAGAEYCSSARHPAWGHCFYRLYQDLETHRLPCTSRCPRPCRESAFKLSTGTSRWPSAKSAGWTLATLGEQGLPHQSHRQRSSLAKINIVYQELNYRSVEEAPVYSVPQLLSAMGSLCSLWFGASVLSLLELLELLLDASALTLVLGGRRLRRAWFSWPRASPASGASSIKPEASQMPPPAGGTSDDPEPSGPHLPRVMLPGVLAGVSAEESWAGPQPLETLDT
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
24 (in isoform 2)Phosphorylation-6.2722210691
29 (in isoform 2)Phosphorylation-59.4922210691
43 (in isoform 2)Phosphorylation-68.6222210691
61PhosphorylationASFRELLTFFCTNAT
HHHHHHHHHHHCCCC
27.5625072903
65PhosphorylationELLTFFCTNATIHGA
HHHHHHHCCCCHHHH
23.8025072903
68PhosphorylationTFFCTNATIHGAIRL
HHHHCCCCHHHHHHH
18.6425072903
78PhosphorylationGAIRLVCSRGNRLKT
HHHHHHCCCCCCCCC
35.43-
122PhosphorylationVLMAVSVHSERKLLP
EEEEEEECCCCCCCC
19.2122210691
127PhosphorylationSVHSERKLLPLVTLC
EECCCCCCCCEEEEC
8.1422210691
132PhosphorylationRKLLPLVTLCDGNPR
CCCCCEEEECCCCCC
29.38-
141PhosphorylationCDGNPRRPSPVLRHL
CCCCCCCCCHHHHHH
44.2422210691
166N-linked_GlycosylationIDSLYNVNLSKGRAA
HHHHEECCCCCCCHH
34.65UniProtKB CARBOHYD
175PhosphorylationSKGRAALSATVPRHE
CCCCHHHCCCCCCCC
19.7123403867
177PhosphorylationGRAALSATVPRHEPP
CCHHHCCCCCCCCCC
27.8923403867
199PhosphorylationRLQRLSHSGSRVRVG
HHHHCCCCCCCEEEE
34.7824275569
330N-linked_GlycosylationAGIRVMVHGRNHTPF
HCCEEEEECCCCCCC
16.05-
342PhosphorylationTPFLGHHSFSVRPGT
CCCCCEEEEEECCCC
17.34-
344PhosphorylationFLGHHSFSVRPGTEA
CCCEEEEEECCCCEE
21.89-
349PhosphorylationSFSVRPGTEATISIR
EEEECCCCEEEEEEE
25.7320363803
352PhosphorylationVRPGTEATISIREDE
ECCCCEEEEEEEHHH
14.7120363803
354PhosphorylationPGTEATISIREDEVH
CCCEEEEEEEHHHHH
15.9624719451
384N-linked_GlycosylationVEVELLHNTSYTRQA
EEEEEEECCCCHHHH
30.59UniProtKB CARBOHYD
548N-linked_GlycosylationLSLLELLELLLDASA
HHHHHHHHHHHHHHH
50.42-
571PhosphorylationRLRRAWFSWPRASPA
HHHEEECCCCCCCCC
26.0124719451
626PhosphorylationAGVSAEESWAGPQPL
CCCCHHHCCCCCCCC
17.46-

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

Oops, there are no upstream regulatory protein records of SCNND_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SCNND_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 SCNND_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
COMD1_HUMANCOMMD1physical
21741370
COMD1_HUMANCOMMD1physical
14645214
ABHGA_HUMANABHD16Aphysical
28514442
MTFR2_HUMANMTFR2physical
28514442
TAP2_HUMANTAP2physical
28514442
D19L1_HUMANDPY19L1physical
28514442
CSTN3_HUMANCLSTN3physical
28514442
AMGO1_HUMANAMIGO1physical
28514442
CFA74_HUMANCFAP74physical
28514442
LRRC3_HUMANLRRC3physical
28514442
CLPT1_HUMANCLPTM1physical
28514442
ANGE1_HUMANANGEL1physical
28514442
ALG9_HUMANALG9physical
28514442
ERMP1_HUMANERMP1physical
28514442
LRP12_HUMANLRP12physical
28514442
POMT1_HUMANPOMT1physical
28514442
CALX_HUMANCANXphysical
28514442
DJC16_HUMANDNAJC16physical
28514442

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00594Amiloride
DB00384Triamterene
Regulatory Network of SCNND_HUMAN

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Related Literatures of Post-Translational Modification

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