DSG3_HUMAN - dbPTM
DSG3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DSG3_HUMAN
UniProt AC P32926
Protein Name Desmoglein-3
Gene Name DSG3
Organism Homo sapiens (Human).
Sequence Length 999
Subcellular Localization Cell membrane
Single-pass type I membrane protein. Cell junction, desmosome.
Protein Description Component of intercellular desmosome junctions. Involved in the interaction of plaque proteins and intermediate filaments mediating cell-cell adhesion..
Protein Sequence MMGLFPRTTGALAIFVVVILVHGELRIETKGQYDEEEMTMQQAKRRQKREWVKFAKPCREGEDNSKRNPIAKITSDYQATQKITYRISGVGIDQPPFGIFVVDKNTGDINITAIVDREETPSFLITCRALNAQGLDVEKPLILTVKILDINDNPPVFSQQIFMGEIEENSASNSLVMILNATDADEPNHLNSKIAFKIVSQEPAGTPMFLLSRNTGEVRTLTNSLDREQASSYRLVVSGADKDGEGLSTQCECNIKVKDVNDNFPMFRDSQYSARIEENILSSELLRFQVTDLDEEYTDNWLAVYFFTSGNEGNWFEIQTDPRTNEGILKVVKALDYEQLQSVKLSIAVKNKAEFHQSVISRYRVQSTPVTIQVINVREGIAFRPASKTFTVQKGISSKKLVDYILGTYQAIDEDTNKAASNVKYVMGRNDGGYLMIDSKTAEIKFVKNMNRDSTFIVNKTITAEVLAIDEYTGKTSTGTVYVRVPDFNDNCPTAVLEKDAVCSSSPSVVVSARTLNNRYTGPYTFALEDQPVKLPAVWSITTLNATSALLRAQEQIPPGVYHISLVLTDSQNNRCEMPRSLTLEVCQCDNRGICGTSYPTTSPGTRYGRPHSGRLGPAAIGLLLLGLLLLLLAPLLLLTCDCGAGSTGGVTGGFIPVPDGSEGTIHQWGIEGAHPEDKEITNICVPPVTANGADFMESSEVCTNTYARGTAVEGTSGMEMTTKLGAATESGGAAGFATGTVSGAASGFGAATGVGICSSGQSGTMRTRHSTGGTNKDYADGAISMNFLDSYFSQKAFACAEEDDGQEANDCLLIYDNEGADATGSPVGSVGCCSFIADDLDDSFLDSLGPKFKKLAEISLGVDGEGKEVQPPSKDSGYGIESCGHPIEVQQTGFVKCQTLSGSQGASALSTSGSVQPAVSIPDPLQHGNYLVTETYSASGSLVQPSTAGFDPLLTQNVIVTERVICPISSVPGNLAGPTQLRGSHTMLCTEDPCSRLI
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
33PhosphorylationRIETKGQYDEEEMTM
EEEECCCCCHHHHHH
33.71-
65PhosphorylationCREGEDNSKRNPIAK
CCCCCCCCCCCCCHH
45.3630301811
110N-linked_GlycosylationDKNTGDINITAIVDR
ECCCCCEEEEEEECC
30.23UniProtKB CARBOHYD
180N-linked_GlycosylationNSLVMILNATDADEP
CEEEEEEECCCCCCC
29.84UniProtKB CARBOHYD
387PhosphorylationGIAFRPASKTFTVQK
CEEEEECCCEEEEEC
34.6120058876
389PhosphorylationAFRPASKTFTVQKGI
EEEECCCEEEEECCC
23.26-
391PhosphorylationRPASKTFTVQKGISS
EECCCEEEEECCCCH
27.53-
404PhosphorylationSSKKLVDYILGTYQA
CHHHHHHHHHHHHCC
7.2029759185
408PhosphorylationLVDYILGTYQAIDED
HHHHHHHHHCCCCCC
14.7129759185
416PhosphorylationYQAIDEDTNKAASNV
HCCCCCCCCCHHHCC
36.2529759185
459N-linked_GlycosylationRDSTFIVNKTITAEV
CCCEEEEECCEEEEE
30.8216740002
545N-linked_GlycosylationVWSITTLNATSALLR
EEEEEECCHHHHHHH
38.8016740002
545N-linked_GlycosylationVWSITTLNATSALLR
EEEEEECCHHHHHHH
38.8017623646
601O-linked_GlycosylationICGTSYPTTSPGTRY
CCCCCCCCCCCCCCC
31.5055828611
602O-linked_GlycosylationCGTSYPTTSPGTRYG
CCCCCCCCCCCCCCC
28.5555828615
603PhosphorylationGTSYPTTSPGTRYGR
CCCCCCCCCCCCCCC
24.6620068231
606PhosphorylationYPTTSPGTRYGRPHS
CCCCCCCCCCCCCCC
24.8920068231
608PhosphorylationTTSPGTRYGRPHSGR
CCCCCCCCCCCCCCC
19.8222964224
690PhosphorylationNICVPPVTANGADFM
CEECCCCCCCCCHHH
21.8528348404
699PhosphorylationNGADFMESSEVCTNT
CCCHHHCCCCCCCCC
21.7328348404
700PhosphorylationGADFMESSEVCTNTY
CCHHHCCCCCCCCCC
22.2728348404
716PhosphorylationRGTAVEGTSGMEMTT
CCCCEECCCCCCEEE
14.4928348404
717PhosphorylationGTAVEGTSGMEMTTK
CCCEECCCCCCEEEC
47.1824719451
723PhosphorylationTSGMEMTTKLGAATE
CCCCCEEECCCEEEC
23.98-
731PhosphorylationKLGAATESGGAAGFA
CCCEEECCCCCCCCC
37.8724275569
739PhosphorylationGGAAGFATGTVSGAA
CCCCCCCCCCCCCCC
30.9924275569
743PhosphorylationGFATGTVSGAASGFG
CCCCCCCCCCCCCCC
23.6625332170
747PhosphorylationGTVSGAASGFGAATG
CCCCCCCCCCCCCCC
33.8425332170
759PhosphorylationATGVGICSSGQSGTM
CCCEEECCCCCCCCC
35.2724275569
760PhosphorylationTGVGICSSGQSGTMR
CCEEECCCCCCCCCE
36.1225332170
765PhosphorylationCSSGQSGTMRTRHST
CCCCCCCCCEEECCC
14.5524275569
768PhosphorylationGQSGTMRTRHSTGGT
CCCCCCEEECCCCCC
23.1624719451
771PhosphorylationGTMRTRHSTGGTNKD
CCCEEECCCCCCCCC
26.0026356563
772PhosphorylationTMRTRHSTGGTNKDY
CCEEECCCCCCCCCC
33.2426356563
775PhosphorylationTRHSTGGTNKDYADG
EECCCCCCCCCCCCC
40.2026356563
779PhosphorylationTGGTNKDYADGAISM
CCCCCCCCCCCCCCH
14.2726356563
785PhosphorylationDYADGAISMNFLDSY
CCCCCCCCHHHHHHH
13.7227251275
860PhosphorylationFKKLAEISLGVDGEG
HHHHHEEECCCCCCC
15.5828348404
883PhosphorylationDSGYGIESCGHPIEV
CCCCCCCCCCCCEEE
24.3928348404
970PhosphorylationERVICPISSVPGNLA
EEEEEECCCCCCCCC
15.4920639409
971PhosphorylationRVICPISSVPGNLAG
EEEEECCCCCCCCCC
32.8126657352
980PhosphorylationPGNLAGPTQLRGSHT
CCCCCCCCCCCCCCE
39.0420639409
985PhosphorylationGPTQLRGSHTMLCTE
CCCCCCCCCEEEECC
14.8926657352
987PhosphorylationTQLRGSHTMLCTEDP
CCCCCCCEEEECCCC
17.3423927012
991PhosphorylationGSHTMLCTEDPCSRL
CCCEEEECCCCHHCC
39.1923927012
996PhosphorylationLCTEDPCSRLI----
EECCCCHHCCC----
35.1920639409

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 DSG3_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DSG3_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 DSG3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PLAK_HUMANJUPphysical
7738346

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
There are no disease associations of PTM sites.
Regulatory Network of DSG3_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Identification of N-linked glycoproteins in human saliva byglycoprotein capture and mass spectrometry.";
Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T.,Loo J.A.;
J. Proteome Res. 5:1493-1503(2006).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-459 AND ASN-545, AND MASSSPECTROMETRY.

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