CDH1
entrez
999
canonical
uniprot
P12830
canonical
ensembl
ENSG00000039068
resolver
ensp
ENSP00000261769
resolver
ensp
ENSP00000414946
resolver
genesymbol
CDH1
resolver
genesymbol_syn
CDHE
resolver
genesymbol_syn
UVO
resolver
hgnc
HGNC:1748
resolver
uniprot
A0A0U2ZQU7
resolver
uniprot
A8K1U7
resolver
uniprot
B3GN61
resolver
uniprot
Q13799
resolver
uniprot
Q14216
resolver
uniprot
Q15855
resolver
uniprot
Q16194
resolver
uniprot
Q4PJ14
resolver
uniprot
Q9UII7
resolver
uniprot
Q9UII8
resolver
uniprot_entry
A0A0U2ZQU7_HUMAN
resolver
uniprot_entry
B3GN61_HUMAN
resolver
uniprot_entry
CADH1_HUMAN
resolver
uniprot_entry
Q9UII7_HUMAN
resolver
uniprot_sec
A8K1U7
resolver
uniprot_sec
Q13799
resolver
uniprot_sec
Q14216
resolver
uniprot_sec
Q15855
resolver
uniprot_sec
Q16194
resolver
uniprot_sec
Q4PJ14
resolver
uniprot_sec
Q9UII8
resolver
amino_acid_sequence
MGPWSRSLSALLLLLQVSSWLCQEPEPCHPGFDAESYTFTVPRRHLERGRVLGRVNFEDCTGRQRTAYFSLDTRFKVGTDGVITVKRPLRFHNPQIHFLVYAWDSTYRKFSTKVTLNTVGHHHRPPPHQASVSGIQAELLTFPNSSPGLRRQKRDWVIPPISCPENEKGPFPKNLVQIKSNKDKEGKVFYSITGQGADTPPVGVFIIERETGWLKVTEPLDRERIATYTLFSHAVSSNGNAVEDPMEILITVTDQNDNKPEFTQEVFKGSVMEGALPGTSVMEVTATDADDDVNTYNAAIAYTILSQDPELPDKNMFTINRNTGVISVVTTGLDRESFPTYTLVVQAADLQGEGLSTTATAVITVTDTNDNPPIFNPTTYKGQVPENEANVVITTLKVTDADAPNTPAWEAVYTILNDDGGQFVVTTNPVNNDGILKTAKGLDFEAKQQYILHVAVTNVVPFEVSLTTSTATVTVDVLDVNEAPIFVPPEKRVEVSEDFGVGQEITSYTAQEPDTFMEQKITYRIWRDTANWLEINPDTGAISTRAELDREDFEHVKNSTYTALIIATDNGSPVATGTGTLLLILSDVNDNAPIPEPRTIFFCERNPKPQVINIIDADLPPNTSPFTAELTHGASANWTIQYNDPTQESIILKPKMALEVGDYKINLKLMDNQNKDQVTTLEVSVCDCEGAAGVCRKAQPVEAGLQIPAILGILGGILALLILILLLLLFLRRRAVVKEPLLPPEDDTRDNVYYYDEEGGGEEDQDFDLSQLHRGLDARPEVTRNDVAPTLMSVPRYLPRPANPDEIGNFIDENLKAADTDPTAPPYDSLLVFDYEGSGSEAASLSSLNSSESDKDQDYDYLNEWGNRFKKLADMYGGGEDD
uniprot
proteins
disease_involvement
DISEASE: Diffuse gastric and lobular breast cancer syndrome (DGLBC) [MIM:137215]: A cancer predisposition syndrome with increased susceptibility to diffuse gastric cancer. Diffuse gastric cancer is a malignant disease characterized by poorly differentiated infiltrating lesions resulting in thickening of the stomach. Malignant tumors start in the stomach, can spread to the esophagus or the small intestine, and can extend through the stomach wall to nearby lymph nodes and organs. It also can metastasize to other parts of the body. In addition to gastric cancer, most female mutation carriers develop lobular carcinoma of the breast. {ECO:0000269|PubMed:10319582, ECO:0000269|PubMed:12216071, ECO:0000269|PubMed:9537325}. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry. Heterozygous CDH1 germline mutations are responsible for familial cases of diffuse gastric cancer. Somatic mutations has also been found in patients with sporadic diffuse gastric cancer and lobular breast cancer.; DISEASE: Endometrial cancer (ENDMC) [MIM:608089]: A malignancy of endometrium, the mucous lining of the uterus. Most endometrial cancers are adenocarcinomas, cancers that begin in cells that make and release mucus and other fluids. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry.; DISEASE: Ovarian cancer (OC) [MIM:167000]: The term ovarian cancer defines malignancies originating from ovarian tissue. Although many histologic types of ovarian tumors have been described, epithelial ovarian carcinoma is the most common form. Ovarian cancers are often asymptomatic and the recognized signs and symptoms, even of late-stage disease, are vague. Consequently, most patients are diagnosed with advanced disease. {ECO:0000269|PubMed:8075649}. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry.; DISEASE: Breast cancer, lobular (LBC) [MIM:137215]: A type of breast cancer that begins in the milk-producing glands (lobules) of the breast. {ECO:0000269|PubMed:17660459}. Note=The gene represented in this entry may be involved in disease pathogenesis.; DISEASE: Blepharocheilodontic syndrome 1 (BCDS1) [MIM:119580]: A form of blepharocheilodontic syndrome, a rare autosomal dominant disorder. It is characterized by lower eyelid ectropion, upper eyelid distichiasis, euryblepharon, bilateral cleft lip and palate, and features of ectodermal dysplasia, including hair anomalies, conical teeth and tooth agenesis. An additional rare manifestation is imperforate anus. There is considerable phenotypic variability among affected individuals. {ECO:0000269|PubMed:28301459}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: 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 (PubMed:11976333). Promotes organization of radial actin fiber structure and cellular response to contractile forces, via its interaction with AMOTL2 which facilitates anchoring of radial actin fibers to CDH1 junction complexes at the cell membrane (By similarity). Plays a role in the early stages of desmosome cell-cell junction formation via facilitating the recruitment of DSG2 and DSP to desmosome plaques (PubMed:29999492). Has a potent invasive suppressor role. It is a ligand for integrin alpha-E/beta-7. {ECO:0000250|UniProtKB:F1PAA9, ECO:0000269|PubMed:11976333, ECO:0000269|PubMed:16417575, ECO:0000269|PubMed:29999492}.; FUNCTION: E-Cad/CTF2 promotes non-amyloidogenic degradation of Abeta precursors. Has a strong inhibitory effect on APP C99 and C83 production. {ECO:0000269|PubMed:16417575}.; FUNCTION: (Microbial infection) Serves as a receptor for Listeria monocytogenes; internalin A (InlA) binds to this protein and promotes uptake of the bacteria. {ECO:0000269|PubMed:10406800, ECO:0000269|PubMed:17540170, ECO:0000269|PubMed:8601315}.
uniprot
proteins
mass_dalton
97456
uniprot
proteins
mutagenesis
MUTAGEN 156; /note="W->A,S: No longer binds L.monocytogenes InlA."; /evidence="ECO:0000269|PubMed:12526809"; MUTAGEN 156; /note="W->D: Protein is partially unfolded, no longer binds L.monocytogenes InlA."; /evidence="ECO:0000269|PubMed:12526809"; MUTAGEN 170; /note="P->A,E,V: No longer binds L.monocytogenes InlA."; /evidence="ECO:0000269|PubMed:12526809"; MUTAGEN 170; /note="P->E: No longer adheres to L.monocytogenes InlA coated beads, nor do cells take up InlA coated beads."; /evidence="ECO:0000269|PubMed:10406800"; MUTAGEN 175; /note="L->D: Reduces localization to desmosome cell-cell junctions. Also reduces the localization of DSG2 and DSP to desmosome cell-cell junctions."; /evidence="ECO:0000269|PubMed:29999492"; MUTAGEN 637; /note="N->Q: CDH1 becomes a substrate for ERAD and is retro-translocated from ER to cytoplasm."; /evidence="ECO:0000269|PubMed:18491227"; MUTAGEN 754; /note="Y->F: Abolishes binding to CBLL1."; /evidence="ECO:0000269|PubMed:22252131"; MUTAGEN 759..761; /note="GGG->AAA: Binds to CTNNB1 but abolishes interaction of CTNNB1 with PSEN1. Abolishes gamma-secretase cleavage."; /evidence="ECO:0000269|PubMed:11953314, ECO:0000269|PubMed:16126725
uniprot
proteins
post_translational_modification
PTM: During apoptosis or with calcium influx, cleaved by a membrane-bound metalloproteinase (ADAM10), PS1/gamma-secretase and caspase-3 (PubMed:10597309, PubMed:11076937, PubMed:11953314). Processing by the metalloproteinase, induced by calcium influx, causes disruption of cell-cell adhesion and the subsequent release of beta-catenin into the cytoplasm (PubMed:10597309). The residual membrane-tethered cleavage product is rapidly degraded via an intracellular proteolytic pathway (PubMed:10597309). Cleavage by caspase-3 releases the cytoplasmic tail resulting in disintegration of the actin microfilament system (PubMed:11076937). The gamma-secretase-mediated cleavage promotes disassembly of adherens junctions (PubMed:11953314). During development of the cochlear organ of Corti, cleavage by ADAM10 at adherens junctions promotes pillar cell separation (By similarity). {ECO:0000250|UniProtKB:P09803, ECO:0000269|PubMed:10597309, ECO:0000269|PubMed:11076937, ECO:0000269|PubMed:11953314}.; PTM: N-glycosylation at Asn-637 is essential for expression, folding and trafficking. Addition of bisecting N-acetylglucosamine by MGAT3 modulates its cell membrane location (PubMed:19403558). {ECO:0000269|PubMed:18491227, ECO:0000269|PubMed:19403558}.; PTM: Ubiquitinated by a SCF complex containing SKP2, which requires prior phosphorylation by CK1/CSNK1A1. Ubiquitinated by CBLL1/HAKAI, requires prior phosphorylation at Tyr-754. {ECO:0000269|PubMed:21283129, ECO:0000269|PubMed:22252131, ECO:0000269|PubMed:22770219}.; PTM: O-glycosylated. O-manosylated by TMTC1, TMTC2, TMTC3 or TMTC4. Thr-285 and Thr-509 are O-mannosylated by TMTC2 or TMTC4 but not TMTC1 or TMTC3. {ECO:0000250|UniProtKB:P09803}.; PTM: (Microbial infection) Cleaved by S.pyogenes SpeB protease; leading to its degradation (PubMed:23532847). Degradation by SpeB promotes bacterial translocation across the host epithelial barrier (PubMed:23532847). Proteolytically cleaved by H.pylori HtrA at the cell membrane; cleavage is facilitated by host MMP and ADAM family members (PubMed:30936204, PubMed:34742300). {ECO:0000269|PubMed:23532847, ECO:0000269|PubMed:30936204, ECO:0000269|PubMed:34742300}.
uniprot
proteins
pubmed
10319582
uniprot
proteins
pubmed
10406800
uniprot
proteins
pubmed
10597309
uniprot
proteins
pubmed
10896919
uniprot
proteins
pubmed
11076937
uniprot
proteins
pubmed
11226248
uniprot
proteins
pubmed
11562785
uniprot
proteins
pubmed
11705864
uniprot
proteins
pubmed
11790773
uniprot
proteins
pubmed
11856755
uniprot
proteins
pubmed
11953314
uniprot
proteins
pubmed
11968083
uniprot
proteins
pubmed
11976333
uniprot
proteins
pubmed
12216071
uniprot
proteins
pubmed
12526809
uniprot
proteins
pubmed
12588804
uniprot
proteins
pubmed
14595118
uniprot
proteins
pubmed
14699157
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15240885
uniprot
proteins
pubmed
15616553
uniprot
proteins
pubmed
15689490
uniprot
proteins
pubmed
16126725
uniprot
proteins
pubmed
16417575
uniprot
proteins
pubmed
17224074
uniprot
proteins
pubmed
17261850
uniprot
proteins
pubmed
17540170
uniprot
proteins
pubmed
17660459
uniprot
proteins
pubmed
17715295
uniprot
proteins
pubmed
17850815
uniprot
proteins
pubmed
17893710
uniprot
proteins
pubmed
18093941
uniprot
proteins
pubmed
18343367
uniprot
proteins
pubmed
18491227
uniprot
proteins
pubmed
19403558
uniprot
proteins
pubmed
19604491
uniprot
proteins
pubmed
20066110
uniprot
proteins
pubmed
20116244
uniprot
proteins
pubmed
20432435
uniprot
proteins
pubmed
20859650
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21283129
uniprot
proteins
pubmed
22252131
uniprot
proteins
pubmed
22294297
uniprot
proteins
pubmed
22770219
uniprot
proteins
pubmed
2349235
uniprot
proteins
pubmed
23532847
uniprot
proteins
pubmed
24220297
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25208567
uniprot
proteins
pubmed
27760340
uniprot
proteins
pubmed
28169360
uniprot
proteins
pubmed
28301459
uniprot
proteins
pubmed
29999492
uniprot
proteins
pubmed
30936204
uniprot
proteins
pubmed
31473225
uniprot
proteins
pubmed
31835537
uniprot
proteins
pubmed
3263290
uniprot
proteins
pubmed
33596089
uniprot
proteins
pubmed
34742300
uniprot
proteins
pubmed
36309486
uniprot
proteins
pubmed
7543680
uniprot
proteins
pubmed
7601454
uniprot
proteins
pubmed
7961105
uniprot
proteins
pubmed
7982500
uniprot
proteins
pubmed
8033105
uniprot
proteins
pubmed
8075649
uniprot
proteins
pubmed
8093045
uniprot
proteins
pubmed
8127895
uniprot
proteins
pubmed
8185635
uniprot
proteins
pubmed
8459805
uniprot
proteins
pubmed
8601315
uniprot
proteins
pubmed
8797891
uniprot
proteins
pubmed
8985087
uniprot
proteins
pubmed
9045944
uniprot
proteins
pubmed
9537325
uniprot
proteins
pubmed
9744472
uniprot
proteins
sequence_length
882
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell junction, adherens junction {ECO:0000269|PubMed:18343367, ECO:0000269|PubMed:22294297, ECO:0000269|PubMed:27760340, ECO:0000269|PubMed:28169360}. Cell membrane {ECO:0000269|PubMed:19403558, ECO:0000269|PubMed:20859650, ECO:0000269|PubMed:28301459, ECO:0000269|PubMed:36309486}; Single-pass type I membrane protein. Endosome {ECO:0000269|PubMed:15689490}. Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:15689490}. Cytoplasm {ECO:0000269|PubMed:22294297}. Cell junction, desmosome {ECO:0000269|PubMed:25208567, ECO:0000269|PubMed:29999492, ECO:0000269|PubMed:33596089}. Note=Colocalizes with DLGAP5 at sites of cell-cell contact in intestinal epithelial cells. Anchored to actin microfilaments through association with alpha-, beta- and gamma-catenin. Sequential proteolysis induced by apoptosis or calcium influx, results in translocation from sites of cell-cell contact to the cytoplasm. Colocalizes with RAB11A endosomes during its transport from the Golgi apparatus to the plasma membrane. Recruited to desmosomes at the initial assembly phase and also accumulates progressively at mature desmosome cell-cell junctions (PubMed:25208567, PubMed:29999492). Localizes to cell-cell contacts as keratinocyte differentiation progresses (By similarity). {ECO:0000250|UniProtKB:P09803, ECO:0000269|PubMed:25208567, ECO:0000269|PubMed:29999492}.; SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:34742300}. Note=(Microbial infection) Proteolytically cleaved at the cell membrane upon H.pylori infection. {ECO:0000269|PubMed:34742300}.
uniprot
proteins
transmembrane_region
TRANSMEM 710..730; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins