UniProt ID | CADH1_HUMAN | |
---|---|---|
UniProt AC | P12830 | |
Protein Name | Cadherin-1 | |
Gene Name | CDH1 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 882 | |
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 associ |
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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 | MGPWSRSLSALLLLLQVSSWLCQEPEPCHPGFDAESYTFTVPRRHLERGRVLGRVNFEDCTGRQRTAYFSLDTRFKVGTDGVITVKRPLRFHNPQIHFLVYAWDSTYRKFSTKVTLNTVGHHHRPPPHQASVSGIQAELLTFPNSSPGLRRQKRDWVIPPISCPENEKGPFPKNLVQIKSNKDKEGKVFYSITGQGADTPPVGVFIIERETGWLKVTEPLDRERIATYTLFSHAVSSNGNAVEDPMEILITVTDQNDNKPEFTQEVFKGSVMEGALPGTSVMEVTATDADDDVNTYNAAIAYTILSQDPELPDKNMFTINRNTGVISVVTTGLDRESFPTYTLVVQAADLQGEGLSTTATAVITVTDTNDNPPIFNPTTYKGQVPENEANVVITTLKVTDADAPNTPAWEAVYTILNDDGGQFVVTTNPVNNDGILKTAKGLDFEAKQQYILHVAVTNVVPFEVSLTTSTATVTVDVLDVNEAPIFVPPEKRVEVSEDFGVGQEITSYTAQEPDTFMEQKITYRIWRDTANWLEINPDTGAISTRAELDREDFEHVKNSTYTALIIATDNGSPVATGTGTLLLILSDVNDNAPIPEPRTIFFCERNPKPQVINIIDADLPPNTSPFTAELTHGASANWTIQYNDPTQESIILKPKMALEVGDYKINLKLMDNQNKDQVTTLEVSVCDCEGAAGVCRKAQPVEAGLQIPAILGILGGILALLILILLLLLFLRRRAVVKEPLLPPEDDTRDNVYYYDEEGGGEEDQDFDLSQLHRGLDARPEVTRNDVAPTLMSVPRYLPRPANPDEIGNFIDENLKAADTDPTAPPYDSLLVFDYEGSGSEAASLSSLNSSESDKDQDYDYLNEWGNRFKKLADMYGGGEDD | |
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 |
---|---|---|---|---|---|
66 | Phosphorylation | DCTGRQRTAYFSLDT HCCCCCEEEEEEEEC | 19.85 | 26074081 | |
68 | Phosphorylation | TGRQRTAYFSLDTRF CCCCEEEEEEEECCE | 7.96 | 26074081 | |
70 | Phosphorylation | RQRTAYFSLDTRFKV CCEEEEEEEECCEEE | 16.80 | 26074081 | |
73 | Phosphorylation | TAYFSLDTRFKVGTD EEEEEEECCEEECCC | 43.21 | 26074081 | |
211 | Phosphorylation | VFIIERETGWLKVTE EEEEEECCCEEEECC | 39.62 | 17855441 | |
217 | Phosphorylation | ETGWLKVTEPLDRER CCCEEEECCCCCHHH | 30.23 | - | |
217 | O-linked_Glycosylation | ETGWLKVTEPLDRER CCCEEEECCCCCHHH | 30.23 | 55829909 | |
232 | Phosphorylation | IATYTLFSHAVSSNG HHHHHHHHHHHCCCC | 17.41 | 22468782 | |
237 | Phosphorylation | LFSHAVSSNGNAVED HHHHHHCCCCCCCCC | 42.00 | 22468782 | |
280 | O-linked_Glycosylation | EGALPGTSVMEVTAT CCCCCCCEEEEEEEC | 25.94 | - | |
285 | O-linked_Glycosylation | GTSVMEVTATDADDD CCEEEEEEECCCCCC | 15.55 | - | |
330 | Phosphorylation | TGVISVVTTGLDRES CCEEEEEECCCCCCC | 17.00 | 17855441 | |
358 | O-linked_Glycosylation | QGEGLSTTATAVITV CCCCCCCCEEEEEEE | 20.73 | - | |
394 | Phosphorylation | NEANVVITTLKVTDA CCCCEEEEEEEECCC | 17.92 | 26270265 | |
395 | Phosphorylation | EANVVITTLKVTDAD CCCEEEEEEEECCCC | 17.29 | 26270265 | |
470 | O-linked_Glycosylation | EVSLTTSTATVTVDV EEEEECCCEEEEEEE | 25.02 | - | |
472 | O-linked_Glycosylation | SLTTSTATVTVDVLD EEECCCEEEEEEEEE | 19.46 | - | |
509 | O-linked_Glycosylation | GQEITSYTAQEPDTF CCEEEEEECCCCCCC | 22.95 | - | |
558 | N-linked_Glycosylation | EDFEHVKNSTYTALI HHHHHHCCCCEEEEE | 38.20 | 18491227 | |
570 | N-linked_Glycosylation | ALIIATDNGSPVATG EEEEEECCCCCCCCC | 48.78 | 18491227 | |
576 | O-linked_Glycosylation | DNGSPVATGTGTLLL CCCCCCCCCCCEEEE | 35.19 | - | |
576 | Phosphorylation | DNGSPVATGTGTLLL CCCCCCCCCCCEEEE | 35.19 | 17855441 | |
578 | O-linked_Glycosylation | GSPVATGTGTLLLIL CCCCCCCCCEEEEEE | 23.73 | - | |
580 | O-linked_Glycosylation | PVATGTGTLLLILSD CCCCCCCEEEEEEEC | 17.67 | - | |
599 | Phosphorylation | APIPEPRTIFFCERN CCCCCCCEEEEECCC | 32.62 | 27251275 | |
622 | N-linked_Glycosylation | IDADLPPNTSPFTAE EECCCCCCCCCCEEE | 51.77 | 18491227 | |
637 | N-linked_Glycosylation | LTHGASANWTIQYND ECCCCCCEEEEEECC | 33.65 | 18491227 | |
663 | Phosphorylation | MALEVGDYKINLKLM EEEEECCEEEEEEEC | 14.08 | - | |
677 | Ubiquitination | MDNQNKDQVTTLEVS CCCCCCCCEEEEEEE | 35.75 | 21906983 | |
738 | Ubiquitination | LRRRAVVKEPLLPPE HHHCHHHCCCCCCCC | 47.19 | 21906983 | |
748 | Phosphorylation | LLPPEDDTRDNVYYY CCCCCCCCCCCEEEE | 52.85 | 25849741 | |
753 | Phosphorylation | DDTRDNVYYYDEEGG CCCCCCEEEECCCCC | 11.54 | 22252131 | |
754 | Phosphorylation | DTRDNVYYYDEEGGG CCCCCEEEECCCCCC | 10.52 | 22252131 | |
755 | Phosphorylation | TRDNVYYYDEEGGGE CCCCEEEECCCCCCC | 10.13 | 22252131 | |
770 | Phosphorylation | EDQDFDLSQLHRGLD CCCCCCHHHHHCCCC | 32.32 | 25849741 | |
790 | Phosphorylation | TRNDVAPTLMSVPRY CCCCCCCCHHCCCCC | 25.92 | 26657352 | |
793 | Phosphorylation | DVAPTLMSVPRYLPR CCCCCHHCCCCCCCC | 31.89 | 28355574 | |
797 | Phosphorylation | TLMSVPRYLPRPANP CHHCCCCCCCCCCCH | 18.26 | 26657352 | |
810 | Ubiquitination | NPDEIGNFIDENLKA CHHHHHHHHCCCHHC | 6.67 | 21906983 | |
827 | Phosphorylation | TDPTAPPYDSLLVFD CCCCCCCCCEEEEEE | 19.66 | 22817900 | |
835 | Phosphorylation | DSLLVFDYEGSGSEA CEEEEEECCCCCCCC | 15.66 | 22817900 | |
838 | Phosphorylation | LVFDYEGSGSEAASL EEEECCCCCCCCCCH | 27.49 | 10671552 | |
840 | Phosphorylation | FDYEGSGSEAASLSS EECCCCCCCCCCHHH | 26.26 | - | |
844 | Phosphorylation | GSGSEAASLSSLNSS CCCCCCCCHHHCCCC | 35.51 | 17353278 | |
846 | Phosphorylation | GSEAASLSSLNSSES CCCCCCHHHCCCCCC | 30.22 | - | |
847 | Phosphorylation | SEAASLSSLNSSESD CCCCCHHHCCCCCCC | 36.54 | 17353278 | |
850 | Phosphorylation | ASLSSLNSSESDKDQ CCHHHCCCCCCCCCC | 40.55 | 17353278 | |
851 | Phosphorylation | SLSSLNSSESDKDQD CHHHCCCCCCCCCCC | 39.79 | 10671552 | |
853 | Phosphorylation | SSLNSSESDKDQDYD HHCCCCCCCCCCCHH | 52.49 | 17353278 | |
859 | Phosphorylation | ESDKDQDYDYLNEWG CCCCCCCHHHHHHHH | 10.80 | 30576142 | |
871 | Ubiquitination | EWGNRFKKLADMYGG HHHHHHHHHHHHHCC | 46.31 | 21906983 | |
876 | Phosphorylation | FKKLADMYGGGEDD- HHHHHHHHCCCCCC- | 17.11 | 30576142 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
753 | Y | Phosphorylation | Kinase | SRC | P12931 | Uniprot |
754 | Y | Phosphorylation | Kinase | SRC | P12931 | Uniprot |
755 | Y | Phosphorylation | Kinase | SRC | P12931 | Uniprot |
790 | T | Phosphorylation | Kinase | PRKCD | Q05655 | GPS |
844 | S | Phosphorylation | Kinase | CSNK1A1 | P48729 | GPS |
844 | S | Phosphorylation | Kinase | CSNK1D | P48730 | GPS |
844 | S | Phosphorylation | Kinase | CSNK1E | P49674 | GPS |
846 | S | Phosphorylation | Kinase | CSNK1D | P48730 | GPS |
847 | S | Phosphorylation | Kinase | CSNK2A1 | P68400 | GPS |
850 | S | Phosphorylation | Kinase | CSNK2A1 | P68400 | GPS |
851 | S | Phosphorylation | Kinase | CK2-FAMILY | - | GPS |
851 | S | Phosphorylation | Kinase | CK2_GROUP | - | PhosphoELM |
853 | S | Phosphorylation | Kinase | CSNK2A1 | P68400 | GPS |
- | K | Ubiquitination | E3 ubiquitin ligase | SKP2 | Q13309 | PMID:26474281 |
- | K | Ubiquitination | E3 ubiquitin ligase | BTRC | Q9Y297 | PMID:24658274 |
- | K | Ubiquitination | E3 ubiquitin ligase | MDM2 | Q00987 | PMID:16980628 |
- | K | Ubiquitination | E3 ubiquitin ligase | CBLL1 | Q75N03 | PMID:11836526 |
Modified Location | Modified Residue | Modification | Function | Reference |
---|---|---|---|---|
637 | N | Glycosylation |
| 18491227 |
* 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_HUMAN !! |
Kegg Disease | ||||||
---|---|---|---|---|---|---|
H00018 | Gastric cancer | |||||
H00025 | Penile cancer | |||||
H00031 | Breast cancer | |||||
H00032 | Thyroid cancer | |||||
H00048 | Hepatocellular carcinoma | |||||
H00054 | Nasopharyngeal cancer | |||||
OMIM Disease | ||||||
137215 | Hereditary diffuse gastric cancer (HDGC) | |||||
608089 | Endometrial cancer (ENDMC) | |||||
167000 | Ovarian cancer (OC) | |||||
137215 | Breast cancer, lobular (LBC) | |||||
Kegg Drug | ||||||
There are no disease associations of PTM sites. | ||||||
DrugBank | ||||||
There are no disease associations of PTM sites. |
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N-linked Glycosylation | |
Reference | PubMed |
"Unglycosylation at Asn-633 made extracellular domain of E-cadherinfolded incorrectly and arrested in endoplasmic reticulum, thensequentially degraded by ERAD."; Zhou F., Su J., Fu L., Yang Y., Zhang L., Wang L., Zhao H., Zhang D.,Li Z., Zha X.; Glycoconj. J. 25:727-740(2008). Cited for: GLYCOSYLATION AT ASN-558; ASN-570; ASN-622 AND ASN-637, ANDMUTAGENESIS OF ASN-637. |