UniProt ID | CADH1_MOUSE | |
---|---|---|
UniProt AC | P09803 | |
Protein Name | Cadherin-1 | |
Gene Name | Cdh1 | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 884 | |
Subcellular Localization |
Cell junction . Cell membrane Single-pass type I membrane protein. Endosome. Golgi apparatus, trans-Golgi network. Colocalizes with DLGAP5 at sites of cell-cell contact in intestinal epithelial cells. Anchored to actin microfilaments through associa |
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Protein Description | Cadherins are calcium-dependent cell adhesion proteins. [PubMed: 11976333 They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. CDH1 is involved in mechanisms regulating cell-cell adhesions, mobility and proliferation of epithelial cells] | |
Protein Sequence | MGARCRSFSALLLLLQVSSWLCQELEPESCSPGFSSEVYTFPVPERHLERGHVLGRVRFEGCTGRPRTAFFSEDSRFKVATDGTITVKRHLKLHKLETSFLVRARDSSHRELSTKVTLKSMGHHHHRHHHRDPASESNPELLMFPSVYPGLRRQKRDWVIPPISCPENEKGEFPKNLVQIKSNRDKETKVFYSITGQGADKPPVGVFIIERETGWLKVTQPLDREAIAKYILYSHAVSSNGEAVEDPMEIVITVTDQNDNRPEFTQEVFEGSVAEGAVPGTSVMKVSATDADDDVNTYNAAIAYTIVSQDPELPHKNMFTVNRDTGVISVLTSGLDRESYPTYTLVVQAADLQGEGLSTTAKAVITVKDINDNAPVFNPSTYQGQVPENEVNARIATLKVTDDDAPNTPAWKAVYTVVNDPDQQFVVVTDPTTNDGILKTAKGLDFEAKQQYILHVRVENEEPFEGSLVPSTATVTVDVVDVNEAPIFMPAERRVEVPEDFGVGQEITSYTAREPDTFMDQKITYRIWRDTANWLEINPETGAIFTRAEMDREDAEHVKNSTYVALIIATDDGSPIATGTGTLLLVLLDVNDNAPIPEPRNMQFCQRNPQPHIITILDPDLPPNTSPFTAELTHGASVNWTIEYNDAAQESLILQPRKDLEIGEYKIHLKLADNQNKDQVTTLDVHVCDCEGTVNNCMKAGIVAAGLQVPAILGILGGILALLILILLLLLFLRRRTVVKEPLLPPDDDTRDNVYYYDEEGGGEEDQDFDLSQLHRGLDARPEVTRNDVAPTLMSVPQYRPRPANPDEIGNFIDENLKAADSDPTAPPYDSLLVFDYEGSGSEAASLSSLNSSESDQDQDYDYLNEWGNRFKKLADMYGGGEDD | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
135 | Phosphorylation | HHHRDPASESNPELL CCCCCCCCCCCCHHH | 47.12 | 28973931 | |
282 | O-linked_Glycosylation | EGAVPGTSVMKVSAT CCCCCCCEEEEEEEC | 26.57 | 28973932 | |
287 | O-linked_Glycosylation | GTSVMKVSATDADDD CCEEEEEEECCCCCC | 21.67 | 28973932 | |
360 | O-linked_Glycosylation | QGEGLSTTAKAVITV CCCCCCCCEEEEEEE | 23.84 | 28973932 | |
415 | Phosphorylation | TPAWKAVYTVVNDPD CCCEEEEEEEECCCC | 9.93 | 25777480 | |
416 | Phosphorylation | PAWKAVYTVVNDPDQ CCEEEEEEEECCCCC | 16.04 | 25777480 | |
429 | Phosphorylation | DQQFVVVTDPTTNDG CCCEEEEECCCCCCC | 25.34 | 25777480 | |
432 | Phosphorylation | FVVVTDPTTNDGILK EEEEECCCCCCCHHH | 40.83 | 25777480 | |
433 | Phosphorylation | VVVTDPTTNDGILKT EEEECCCCCCCHHHC | 36.38 | 25777480 | |
472 | O-linked_Glycosylation | EGSLVPSTATVTVDV CCCCCCCCCEEEEEE | 21.93 | 28973932 | |
474 | O-linked_Glycosylation | SLVPSTATVTVDVVD CCCCCCCEEEEEEEE | 19.46 | 28973932 | |
511 | O-linked_Glycosylation | GQEITSYTAREPDTF CCEEEEEECCCCCCC | 21.00 | 28973932 | |
560 | N-linked_Glycosylation | EDAEHVKNSTYVALI HHHHHHCCCCEEEEE | 38.20 | - | |
578 | O-linked_Glycosylation | DDGSPIATGTGTLLL CCCCCCCCCCCEEEE | 35.68 | 28973932 | |
580 | O-linked_Glycosylation | GSPIATGTGTLLLVL CCCCCCCCCEEEEEE | 23.73 | 28973932 | |
582 | O-linked_Glycosylation | PIATGTGTLLLVLLD CCCCCCCEEEEEEEE | 17.67 | 28973932 | |
639 | N-linked_Glycosylation | LTHGASVNWTIEYND ECCCCCEEEEEEECC | 27.90 | - | |
740 | Ubiquitination | LRRRTVVKEPLLPPD HHHCCCCCCCCCCCC | 49.64 | - | |
750 | Phosphorylation | LLPPDDDTRDNVYYY CCCCCCCCCCCEEEE | 47.09 | 28507225 | |
755 | Phosphorylation | DDTRDNVYYYDEEGG CCCCCCEEEECCCCC | 11.54 | 22817900 | |
756 | Phosphorylation | DTRDNVYYYDEEGGG CCCCCEEEECCCCCC | 10.52 | 22817900 | |
757 | Phosphorylation | TRDNVYYYDEEGGGE CCCCEEEECCCCCCC | 10.13 | - | |
772 | Phosphorylation | EDQDFDLSQLHRGLD CCCCCCHHHHHCCCC | 32.32 | - | |
795 | Phosphorylation | DVAPTLMSVPQYRPR CCCCCCCCCCCCCCC | 33.48 | - | |
840 | Phosphorylation | LVFDYEGSGSEAASL EEEECCCCCCCCCCH | 27.49 | 11348595 | |
842 | Phosphorylation | FDYEGSGSEAASLSS EECCCCCCCCCCHHH | 26.26 | 11348595 | |
846 | Phosphorylation | GSGSEAASLSSLNSS CCCCCCCCHHHCCCC | 35.51 | - | |
848 | Phosphorylation | GSEAASLSSLNSSES CCCCCCHHHCCCCCC | 30.22 | 11348595 | |
849 | Phosphorylation | SEAASLSSLNSSESD CCCCCHHHCCCCCCC | 36.54 | 22817900 | |
853 | Phosphorylation | SLSSLNSSESDQDQD CHHHCCCCCCCCCCC | 39.79 | 22817900 | |
855 | Phosphorylation | SSLNSSESDQDQDYD HHCCCCCCCCCCCHH | 42.38 | 22817900 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
755 | Y | Phosphorylation | Kinase | SRC | P05480 | Uniprot |
756 | Y | Phosphorylation | Kinase | SRC | P05480 | Uniprot |
757 | Y | Phosphorylation | Kinase | SRC | P05480 | Uniprot |
840 | S | Phosphorylation | Kinase | CSNK2A1 | P68400 | GPS |
840 | S | Phosphorylation | Kinase | CSK21 | Q60737 | PhosphoELM |
842 | S | Phosphorylation | Kinase | CSNK2A1 | P68400 | GPS |
848 | S | Phosphorylation | Kinase | CSNK2A1 | P68400 | GPS |
849 | S | Phosphorylation | Kinase | GSK3B | P49841 | PSP |
849 | S | Phosphorylation | Kinase | GSK-FAMILY | - | GPS |
849 | S | Phosphorylation | Kinase | GSK-3_GROUP | - | PhosphoELM |
853 | S | Phosphorylation | Kinase | CSNK2A1 | P68400 | GPS |
853 | S | Phosphorylation | Kinase | CSK21 | Q60737 | PhosphoELM |
855 | S | Phosphorylation | Kinase | CSNK2A1 | P68400 | GPS |
855 | S | Phosphorylation | Kinase | CSK21 | Q60737 | PhosphoELM |
- | K | Ubiquitination | E3 ubiquitin ligase | Cbll1 | Q9JIY2 | PMID:22199232 |
Modified Location | Modified Residue | Modification | Function | Reference |
---|---|---|---|---|
639 | N | Glycosylation |
| - |
* 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 CADH1_MOUSE !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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