| UniProt ID | DSC1_HUMAN | |
|---|---|---|
| UniProt AC | Q08554 | |
| Protein Name | Desmocollin-1 | |
| Gene Name | DSC1 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 894 | |
| 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. Linked to the keratinization of epithelial tissues.. | |
| Protein Sequence | MALASAAPGSIFCKQLLFSLLVLTLLCDACQKVYLRVPSHLQAETLVGKVNLEECLKSASLIRSSDPAFRILEDGSIYTTHDLILSSERKSFSIFLSDGQRREQQEIKVVLSARENKSPKKRHTKDTALKRSKRRWAPIPASLMENSLGPFPQHVQQIQSDAAQNYTIFYSISGPGVDKEPFNLFYIEKDTGDIFCTRSIDREKYEQFALYGYATTADGYAPEYPLPLIIKIEDDNDNAPYFEHRVTIFTVPENCRSGTSVGKVTATDLDEPDTLHTRLKYKILQQIPDHPKHFSIHPDTGVITTTTPFLDREKCDTYQLIMEVRDMGGQPFGLFNTGTITISLEDENDNPPSFTETSYVTEVEENRIDVEILRMKVQDQDLPNTPHSKAVYKILQGNENGNFIISTDPNTNEGVLCVVKPLNYEVNRQVILQVGVINEAQFSKAASSQTPTMCTTTVTVKIIDSDEGPECHPPVKVIQSQDGFPAGQELLGYKALDPEISSGEGLRYQKLGDEDNWFEINQHTGDLRTLKVLDRESKFVKNNQYNISVVAVDAVGRSCTGTLVVHLDDYNDHAPQIDKEVTICQNNEDFAVLKPVDPDGPENGPPFQFFLDNSASKNWNIEEKDGKTAILRQRQNLDYNYYSVPIQIKDRHGLVATHMLTVRVCDCSTPSECRMKDKSTRDVRPNVILGRWAILAMVLGSVLLLCILFTCFCVTAKRTVKKCFPEDIAQQNLIVSNTEGPGEEVTEANIRLPMQTSNICDTSMSVGTVGGQGIKTQQSFEMVKGGYTLDSNKGGGHQTLESVKGVGQGDTGRYAYTDWQSFTQPRLGEKVYLCGQDEEHKHCEDYVCSYNYEGKGSLAGSVGCCSDRQEEEGLEFLDHLEPKFRTLAKTCIKK | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 60 | Phosphorylation | EECLKSASLIRSSDP HHHHHHHHHHCCCCC | 31.27 | 24719451 | |
| 60 (in isoform 2) | Phosphorylation | - | 31.27 | 24719451 | |
| 86 | Phosphorylation | TTHDLILSSERKSFS EECCEEECCCCCEEE | 24.14 | - | |
| 112 | Phosphorylation | QEIKVVLSARENKSP HEEEEHHHHCCCCCC | 17.42 | 20068231 | |
| 118 | Phosphorylation | LSARENKSPKKRHTK HHHCCCCCCCCCCCH | 54.24 | 20068231 | |
| 165 | N-linked_Glycosylation | IQSDAAQNYTIFYSI HHHHHHHCEEEEEEE | 31.05 | UniProtKB CARBOHYD | |
| 211 | Phosphorylation | KYEQFALYGYATTAD HHHHEEEEEEEECCC | 12.50 | - | |
| 385 | Phosphorylation | QDQDLPNTPHSKAVY CCCCCCCCCCCHHHH | 22.05 | 17924679 | |
| 385 (in isoform 2) | Phosphorylation | - | 22.05 | - | |
| 406 | Phosphorylation | ENGNFIISTDPNTNE CCCCEEEECCCCCCC | 23.18 | 24719451 | |
| 406 (in isoform 2) | Phosphorylation | - | 23.18 | 24719451 | |
| 443 | Phosphorylation | VINEAQFSKAASSQT CCCHHHHHHHHCCCC | 14.87 | 21406692 | |
| 480 | Phosphorylation | PPVKVIQSQDGFPAG CCEEEEECCCCCCCC | 21.08 | 22210691 | |
| 493 | Phosphorylation | AGQELLGYKALDPEI CCHHHCCCEECCCCC | 7.95 | 22210691 | |
| 546 | N-linked_Glycosylation | FVKNNQYNISVVAVD HCCCCCEEEEEEEEE | 15.42 | UniProtKB CARBOHYD | |
| 639 | Phosphorylation | RQRQNLDYNYYSVPI HCCCCCCCCEEEECE | 14.29 | - | |
| 642 | Phosphorylation | QNLDYNYYSVPIQIK CCCCCCEEEECEEEE | 10.27 | - | |
| 657 | Phosphorylation | DRHGLVATHMLTVRV CCCCEEEEEEEEEEE | 10.59 | - | |
| 676 | Acetylation | TPSECRMKDKSTRDV CCHHHCCCCCCCCCC | 42.53 | 20167786 | |
| 791 | Phosphorylation | KGGYTLDSNKGGGHQ ECCEECCCCCCCCCC | 43.48 | 24247654 | |
| 831 (in isoform 2) | Phosphorylation | - | 3.72 | 28348404 | |
| 836 (in isoform 2) | Phosphorylation | - | 54.68 | 24719451 | |
| 846 | Phosphorylation | EHKHCEDYVCSYNYE CCCCCCCCEEECCCC | 4.89 | - | |
| 857 | Phosphorylation | YNYEGKGSLAGSVGC CCCCCCCCCCCCEEE | 20.66 | - | |
| 861 | Phosphorylation | GKGSLAGSVGCCSDR CCCCCCCCEEECCCC | 15.10 | - | |
| 866 | Phosphorylation | AGSVGCCSDRQEEEG CCCEEECCCCCHHHH | 39.65 | - |
| 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 DSC1_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of DSC1_HUMAN !! | ||||||
* 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 DSC1_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| DSG2_HUMAN | DSG2 | physical | 9214392 | |
| DESP_HUMAN | DSP | physical | 9606214 |
| 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. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-385, AND MASSSPECTROMETRY. | |
| "Toward a global characterization of the phosphoproteome in prostatecancer cells: identification of phosphoproteins in the LNCaP cellline."; Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.; Electrophoresis 28:2027-2034(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-385, AND MASSSPECTROMETRY. | |
