DSC3_MOUSE - dbPTM
DSC3_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DSC3_MOUSE
UniProt AC P55850
Protein Name Desmocollin-3
Gene Name Dsc3
Organism Mus musculus (Mouse).
Sequence Length 896
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. May contribute to epidermal cell positioning (stratification) by mediating differential adhesiveness between cells that express different isoforms..
Protein Sequence MVVPEFRSPQCRALCTKLLLTLWVFSFVGEACKKVTFHVPSTLEADKIIGRVSLKECLSSADGIMPSDPDFRVLDDGSVYPTRAVVLSDEKRSFTIQLSDSKMQTQKEIPVILEHKKKVLKKRHTKETVLRRSKRRWAPIPCSMQENSLGPFPLFLQQVQSDAAQNYTVFYSISGRGADQEPLNWFFIERDTGNLYCTRPVDREEYDVFDLIAYASTADGYSADLPLPLPIKIEDENDNYPLFTEAIYAFEVPEGSRLGTVVGTVCATDKDEPDTMHTRLKYSILEQTPPSPGLFSVHPDTGVITTVSHYMDREVVDKYKLIMKVQDMNGQFFGLISTSTCIITVQDSNDNAPTFRQNTYETAVEENTYNVEILRIPVDDKDMINTANWKANFTILKGNENGWFKITTDPVTNEGVLCVVKPLDYEENRQVTLEIGVNNEAPFIKDVANRIPTMNRAMVTVHVKDQNEGPECKPPEQYVRIKENSAVGSKINGYKAYDPETKNSNGLRYKKLQDPKDWVSIEEVSGLLTISKTLDREIMAPRNDMYNITVMAIDQEGKSCTGTLAVNIEDVNDNAPEIIQDYIVICKPKMGYTDISAVDPDEPIHGPPFQFNLANTSPEVNRIWTLNQVNDTAARLSYQKTADVQIYNVPVTVKDRAGQSATKILRVNLCDCTHPSQCPLRSRSAGITLGKWAILAILLGIALLFSVLLTLVCGVVTARKGKHFPEDLAQQNLIISNTEAPGDDRVCSANGFTTHTANNSSQGFCGTMGSGMRNGGQETIEMMKGHQTLDSCRVAGHHHTLDSGRGGHMDTDNCRYTYSEWHSFTQPRLGEKLHVCNQNEDHIPSQDYVLTYNYEGRGSPAGSVGCCSEKQEEEGLDFLNNLEPKFLTLAETCTKR
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
166N-linked_GlycosylationVQSDAAQNYTVFYSI
HHHCHHCCEEEEEEE
29.71-
386PhosphorylationDDKDMINTANWKANF
CCHHHCCCCCEEEEE
15.50-
392N-linked_GlycosylationNTANWKANFTILKGN
CCCCEEEEEEEEECC
30.76-
547N-linked_GlycosylationAPRNDMYNITVMAID
CCCCCCEEEEEEEEC
19.47-
630N-linked_GlycosylationIWTLNQVNDTAARLS
EEEEHHCCCHHHHHH
31.0216170054
787PhosphorylationIEMMKGHQTLDSCRV
HHHHHCCCCHHHCEE
27.1919367708
788PhosphorylationEMMKGHQTLDSCRVA
HHHHCCCCHHHCEEC
3.5219367708
790PhosphorylationMKGHQTLDSCRVAGH
HHCCCCHHHCEECCC
13.6119367708
791PhosphorylationKGHQTLDSCRVAGHH
HCCCCHHHCEECCCC
3.9619367708
800PhosphorylationRVAGHHHTLDSGRGG
EECCCCCCCCCCCCC
4.2428507225
803PhosphorylationGHHHTLDSGRGGHMD
CCCCCCCCCCCCCCC
31.7328507225
823PhosphorylationYTYSEWHSFTQPRLG
EEHHHHHCCCCCCCC
4.8128507225
833 (in isoform 2)Phosphorylation-32.9019367708
858PhosphorylationTYNYEGRGSPAGSVG
EEEECCCCCCCCCCC
15.3719367708
859PhosphorylationYNYEGRGSPAGSVGC
EEECCCCCCCCCCCC
43.3919367708
862PhosphorylationEGRGSPAGSVGCCSE
CCCCCCCCCCCCCCC
19.9019367708
863PhosphorylationGRGSPAGSVGCCSEK
CCCCCCCCCCCCCCC
7.1419367708
867PhosphorylationPAGSVGCCSEKQEEE
CCCCCCCCCCCCHHH
52.4819367708
868PhosphorylationAGSVGCCSEKQEEEG
CCCCCCCCCCCHHHC
44.8619367708

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 DSC3_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DSC3_MOUSE !!

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 DSC3_MOUSE !!

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

Oops, there are no PPI records of DSC3_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DSC3_MOUSE

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"High throughput quantitative glycomics and glycoform-focusedproteomics of murine dermis and epidermis.";
Uematsu R., Furukawa J., Nakagawa H., Shinohara Y., Deguchi K.,Monde K., Nishimura S.;
Mol. Cell. Proteomics 4:1977-1989(2005).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-630, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-858; SER-862 ANDSER-867, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-832 (ISOFORM2), AND MASS SPECTROMETRY.

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