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P12830

- CADH1_HUMAN

UniProt

P12830 - CADH1_HUMAN

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Protein

Cadherin-1

Gene

CDH1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Cadherins are calcium-dependent cell adhesion proteins. 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. Has a potent invasive suppressor role. It is a ligand for integrin alpha-E/beta-7.1 Publication
E-Cad/CTF2 promotes non-amyloidogenic degradation of Abeta precursors. Has a strong inhibitory effect on APP C99 and C83 production.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi257 – 2571Calcium 1
Metal bindingi257 – 2571Calcium 2
Metal bindingi288 – 2881Calcium 3
Sitei700 – 7012Cleavage; by a metalloproteinase
Sitei731 – 7322Cleavage; by gamma-secretase/PS1
Sitei750 – 7512Cleavage; by caspase-3

GO - Molecular functioni

  1. ankyrin binding Source: BHF-UCL
  2. beta-catenin binding Source: BHF-UCL
  3. calcium ion binding Source: Ensembl
  4. cell adhesion molecule binding Source: UniProtKB
  5. gamma-catenin binding Source: BHF-UCL
  6. glycoprotein binding Source: UniProt
  7. GTPase activating protein binding Source: UniProtKB

GO - Biological processi

  1. adherens junction organization Source: UniProtKB
  2. apoptotic process Source: Reactome
  3. calcium-dependent cell-cell adhesion Source: Ensembl
  4. cell-cell junction organization Source: Reactome
  5. cell junction assembly Source: Reactome
  6. cellular component disassembly involved in execution phase of apoptosis Source: Reactome
  7. cellular response to amino acid stimulus Source: Ensembl
  8. cellular response to indole-3-methanol Source: UniProtKB
  9. cellular response to lithium ion Source: UniProtKB
  10. cochlea development Source: Ensembl
  11. epithelial cell morphogenesis Source: Ensembl
  12. establishment of protein localization to plasma membrane Source: UniProt
  13. extracellular matrix disassembly Source: Reactome
  14. extracellular matrix organization Source: Reactome
  15. homophilic cell adhesion Source: UniProtKB
  16. intestinal epithelial cell development Source: Ensembl
  17. negative regulation of canonical Wnt signaling pathway Source: Ensembl
  18. negative regulation of cell-cell adhesion Source: UniProtKB
  19. negative regulation of epithelial cell proliferation Source: Ensembl
  20. neuron projection development Source: Ensembl
  21. pituitary gland development Source: Ensembl
  22. positive regulation of transcription, DNA-templated Source: BHF-UCL
  23. positive regulation of transcription factor import into nucleus Source: BHF-UCL
  24. protein homooligomerization Source: Ensembl
  25. protein localization to plasma membrane Source: BHF-UCL
  26. protein metabolic process Source: Ensembl
  27. regulation of branching involved in salivary gland morphogenesis Source: Ensembl
  28. regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: Ensembl
  29. regulation of immune response Source: Reactome
  30. regulation of neuron migration Source: Ensembl
  31. regulation of protein localization to cell surface Source: Ensembl
  32. regulation of water loss via skin Source: Ensembl
  33. response to drug Source: Ensembl
  34. response to toxic substance Source: Ensembl
  35. salivary gland cavitation Source: Ensembl
  36. sensory perception of sound Source: Ensembl
  37. single organismal cell-cell adhesion Source: BHF-UCL
  38. synapse assembly Source: Ensembl
  39. tight junction assembly Source: Ensembl
  40. trophectodermal cell differentiation Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_11152. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
REACT_118572. Degradation of the extracellular matrix.
REACT_13552. Integrin cell surface interactions.
REACT_13579. Apoptotic cleavage of cell adhesion proteins.
REACT_19195. Adherens junctions interactions.

Names & Taxonomyi

Protein namesi
Recommended name:
Cadherin-1
Alternative name(s):
CAM 120/80
Epithelial cadherin
Short name:
E-cadherin
Uvomorulin
CD_antigen: CD324
Cleaved into the following 3 chains:
Gene namesi
Name:CDH1
Synonyms:CDHE, UVO
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 16

Organism-specific databases

HGNCiHGNC:1748. CDH1.

Subcellular locationi

Cell junction. Cell membrane; Single-pass type I membrane protein. Endosome. Golgi apparatustrans-Golgi network
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.

GO - Cellular componenti

  1. actin cytoskeleton Source: BHF-UCL
  2. aggresome Source: HPA
  3. apical junction complex Source: UniProtKB
  4. apical part of cell Source: Ensembl
  5. axon terminus Source: Ensembl
  6. basolateral plasma membrane Source: Ensembl
  7. catenin complex Source: BHF-UCL
  8. cell-cell adherens junction Source: BHF-UCL
  9. cell junction Source: UniProtKB
  10. cell surface Source: Ensembl
  11. cytoplasm Source: HPA
  12. cytoplasmic side of plasma membrane Source: UniProtKB
  13. endosome Source: UniProtKB-KW
  14. extracellular region Source: Reactome
  15. extracellular vesicular exosome Source: UniProtKB
  16. focal adhesion Source: HPA
  17. integral component of membrane Source: BHF-UCL
  18. lateral loop Source: Ensembl
  19. lateral plasma membrane Source: BHF-UCL
  20. node of Ranvier Source: Ensembl
  21. perinuclear region of cytoplasm Source: BHF-UCL
  22. plasma membrane Source: HPA
  23. Schmidt-Lanterman incisure Source: Ensembl
  24. trans-Golgi network Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Endosome, Golgi apparatus, Membrane

Pathology & Biotechi

Involvement in diseasei

Hereditary diffuse gastric cancer (HDGC) [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.2 Publications
Note: The disease is caused by mutations 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.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti244 – 2441D → G in HDGC. 1 Publication
VAR_008712
Natural varianti487 – 4871V → A in HDGC. 1 Publication
VAR_008713
Natural varianti832 – 8321V → M in HDGC. 2 Publications
Corresponds to variant rs35572355 [ dbSNP | Ensembl ].
VAR_023358
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 variations affecting the gene represented in this entry.
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.1 Publication
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.
Breast cancer, lobular (LBC) [MIM:137215]: A type of breast cancer that begins in the milk-producing glands (lobules) of the breast.1 Publication
Note: The gene represented in this entry may be involved in disease pathogenesis.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi637 – 6371N → Q: CDH1 becomes a substrate for ERAD and is retro-translocated from ER to cytoplasm. 1 Publication
Mutagenesisi754 – 7541Y → F: Abolishes binding to CBLL1. 1 Publication
Mutagenesisi759 – 7613GGG → AAA: Binds to CTNNB1 but abolishes interaction of CTNNB1 with PSEN1. Abolishes gamma-secretase cleavage. 2 Publications

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi137215. phenotype.
167000. phenotype.
608089. phenotype.
Orphaneti1991. Cleft lip with or without cleft palate.
26106. Familial gastric cancer.
36273. Gastric linitis plastica.
PharmGKBiPA26282.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Sequence AnalysisAdd
BLAST
Propeptidei23 – 154132Sequence AnalysisPRO_0000003715Add
BLAST
Chaini155 – 882728Cadherin-1PRO_0000003716Add
BLAST
Chaini701 – 882182E-Cad/CTF1PRO_0000236067Add
BLAST
Chaini732 – 882151E-Cad/CTF2PRO_0000236068Add
BLAST
Chaini751 – 882132E-Cad/CTF3PRO_0000236069Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi163 – 163Interchain
Glycosylationi558 – 5581N-linked (GlcNAc...)1 Publication
Glycosylationi570 – 5701N-linked (GlcNAc...)1 Publication
Glycosylationi622 – 6221N-linked (GlcNAc...)1 Publication
Glycosylationi637 – 6371N-linked (GlcNAc...)1 Publication
Modified residuei753 – 7531Phosphotyrosine; by SRC1 Publication
Modified residuei754 – 7541Phosphotyrosine; by SRC1 Publication
Modified residuei755 – 7551Phosphotyrosine; by SRC1 Publication
Modified residuei838 – 8381PhosphoserineBy similarity
Modified residuei840 – 8401PhosphoserineBy similarity
Modified residuei846 – 8461PhosphoserineBy similarity

Post-translational modificationi

During apoptosis or with calcium influx, cleaved by a membrane-bound metalloproteinase (ADAM10), PS1/gamma-secretase and caspase-3 to produce fragments of about 38 kDa (E-CAD/CTF1), 33 kDa (E-CAD/CTF2) and 29 kDa (E-CAD/CTF3), respectively. Processing by the metalloproteinase, induced by calcium influx, causes disruption of cell-cell adhesion and the subsequent release of beta-catenin into the cytoplasm. The residual membrane-tethered cleavage product is rapidly degraded via an intracellular proteolytic pathway. Cleavage by caspase-3 releases the cytoplasmic tail resulting in disintegration of the actin microfilament system. The gamma-secretase-mediated cleavage promotes disassembly of adherens junctions.3 Publications
N-glycosylation at Asn-637 is essential for expression, folding and trafficking.1 Publication
Ubiquitinated by a SCF complex containing SKP2, which requires prior phosphorylation by CK1/CSNK1A1. Ubiquitinated by CBLL1/HAKAI, requires prior phosphorylation at Tyr-754.3 Publications

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP12830.
PaxDbiP12830.
PRIDEiP12830.

PTM databases

PhosphoSiteiP12830.

Miscellaneous databases

PMAP-CutDBP12830.

Expressioni

Tissue specificityi

Non-neural epithelial tissues.

Inductioni

Expression is repressed by MACROD1.1 Publication

Gene expression databases

BgeeiP12830.
CleanExiHS_CDH1.
ExpressionAtlasiP12830. baseline and differential.
GenevestigatoriP12830.

Organism-specific databases

HPAiCAB000087.
CAB028364.
HPA004812.

Interactioni

Subunit structurei

Homodimer; disulfide-linked. Component of an E-cadherin/ catenin adhesion complex composed of at least E-cadherin/CDH1, beta-catenin/CTNNB1 or gamma-catenin/JUP, and potentially alpha-catenin/CTNNA1; the complex is located to adherens junctions. The stable association of CTNNA1 is controversial as CTNNA1 was shown not to bind to F-actin when assembled in the complex. Alternatively, the CTNNA1-containing complex may be linked to F-actin by other proteins such as LIMA1. Interaction with PSEN1, cleaves CDH1 resulting in the disassociation of cadherin-based adherens junctions (CAJs). Interacts with AJAP1, CTNND1 and DLGAP5 (By similarity). Interacts with TBC1D2. Interacts with LIMA1. Interacts with CAV1. Interacts with the TRPV4 and CTNNB1 complex (By similarity). Interacts with PIP5K1C. Interacts with RAB8B (By similarity). Interacts with RAPGEF2 (By similarity). Interacts with DDR1; this stabilizes CDH1 at the cell surface and inhibits its internalization.By similarity11 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Cbll1Q9JIY221EBI-727477,EBI-7644904From a different organism.
CDC27P302602EBI-727477,EBI-994813
CTNNB1P3522210EBI-727477,EBI-491549
EGFRP005333EBI-727477,EBI-297353
FGFR1P113623EBI-727477,EBI-1028277
PPP1CAP621362EBI-727477,EBI-357253
PRKD1Q151397EBI-727477,EBI-1181072
SRCP129312EBI-727477,EBI-621482
TNS3Q68CZ22EBI-727477,EBI-1220488

Protein-protein interaction databases

BioGridi107434. 100 interactions.
DIPiDIP-477N.
IntActiP12830. 46 interactions.
MINTiMINT-119105.
STRINGi9606.ENSP00000261769.

Structurei

Secondary structure

1
882
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi163 – 1664
Beta strandi169 – 1779
Helixi181 – 1844
Beta strandi189 – 1957
Turni196 – 1983
Beta strandi199 – 2013
Beta strandi204 – 2074
Turni209 – 2113
Beta strandi213 – 2164
Turni222 – 2243
Beta strandi227 – 2359
Beta strandi241 – 2433
Beta strandi246 – 2538
Beta strandi261 – 27212
Beta strandi280 – 2834
Turni292 – 2943
Beta strandi301 – 3099
Beta strandi316 – 3194
Turni321 – 3233
Beta strandi325 – 3284
Turni335 – 3373
Beta strandi340 – 3489
Turni349 – 3535
Beta strandi356 – 36611
Helixi769 – 7713

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1O6SX-ray1.80B156-255[»]
2O72X-ray2.00A155-367[»]
2OMTX-ray2.00B156-255[»]
2OMUX-ray1.80B156-255[»]
2OMVX-ray1.90B156-255[»]
2OMXX-ray1.70B156-258[»]
2OMYX-ray1.70B156-254[»]
2OMZX-ray1.60B156-254[»]
3FF7X-ray1.80A/B155-253[»]
3FF8X-ray2.00A/B155-254[»]
3L6XX-ray2.40B756-773[»]
3L6YX-ray3.00B/D/F756-773[»]
ProteinModelPortaliP12830.
SMRiP12830. Positions 155-690, 782-875.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP12830.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini155 – 709555ExtracellularSequence AnalysisAdd
BLAST
Topological domaini731 – 882152CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei710 – 73021HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini155 – 262108Cadherin 1PROSITE-ProRule annotationAdd
BLAST
Domaini263 – 375113Cadherin 2PROSITE-ProRule annotationAdd
BLAST
Domaini376 – 486111Cadherin 3PROSITE-ProRule annotationAdd
BLAST
Domaini487 – 593107Cadherin 4PROSITE-ProRule annotationAdd
BLAST
Domaini594 – 697104Cadherin 5PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni758 – 76912Required for binding CTNND1 and PSEN1Add
BLAST
Regioni811 – 88272Required for binding alpha, beta and gamma cateninsAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi838 – 85114Ser-richAdd
BLAST

Domaini

Three calcium ions are usually bound at the interface of each cadherin domain and rigidify the connections, imparting a strong curvature to the full-length ectodomain.1 Publication

Sequence similaritiesi

Contains 5 cadherin domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG328838.
GeneTreeiENSGT00760000118906.
HOGENOMiHOG000231254.
HOVERGENiHBG106438.
InParanoidiP12830.
KOiK05689.
OMAiDFGVGQE.
OrthoDBiEOG7PS1DS.
PhylomeDBiP12830.
TreeFamiTF316817.

Family and domain databases

Gene3Di2.60.40.60. 6 hits.
4.10.900.10. 1 hit.
InterProiIPR002126. Cadherin.
IPR015919. Cadherin-like.
IPR020894. Cadherin_CS.
IPR000233. Cadherin_cytoplasmic-dom.
IPR014868. Cadherin_pro_dom.
IPR027397. Catenin_binding_dom.
[Graphical view]
PfamiPF00028. Cadherin. 5 hits.
PF01049. Cadherin_C. 1 hit.
PF08758. Cadherin_pro. 1 hit.
[Graphical view]
PRINTSiPR00205. CADHERIN.
SMARTiSM00112. CA. 4 hits.
SM01055. Cadherin_pro. 1 hit.
[Graphical view]
SUPFAMiSSF49313. SSF49313. 6 hits.
PROSITEiPS00232. CADHERIN_1. 3 hits.
PS50268. CADHERIN_2. 5 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P12830-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MGPWSRSLSA LLLLLQVSSW LCQEPEPCHP GFDAESYTFT VPRRHLERGR
60 70 80 90 100
VLGRVNFEDC TGRQRTAYFS LDTRFKVGTD GVITVKRPLR FHNPQIHFLV
110 120 130 140 150
YAWDSTYRKF STKVTLNTVG HHHRPPPHQA SVSGIQAELL TFPNSSPGLR
160 170 180 190 200
RQKRDWVIPP ISCPENEKGP FPKNLVQIKS NKDKEGKVFY SITGQGADTP
210 220 230 240 250
PVGVFIIERE TGWLKVTEPL DRERIATYTL FSHAVSSNGN AVEDPMEILI
260 270 280 290 300
TVTDQNDNKP EFTQEVFKGS VMEGALPGTS VMEVTATDAD DDVNTYNAAI
310 320 330 340 350
AYTILSQDPE LPDKNMFTIN RNTGVISVVT TGLDRESFPT YTLVVQAADL
360 370 380 390 400
QGEGLSTTAT AVITVTDTND NPPIFNPTTY KGQVPENEAN VVITTLKVTD
410 420 430 440 450
ADAPNTPAWE AVYTILNDDG GQFVVTTNPV NNDGILKTAK GLDFEAKQQY
460 470 480 490 500
ILHVAVTNVV PFEVSLTTST ATVTVDVLDV NEAPIFVPPE KRVEVSEDFG
510 520 530 540 550
VGQEITSYTA QEPDTFMEQK ITYRIWRDTA NWLEINPDTG AISTRAELDR
560 570 580 590 600
EDFEHVKNST YTALIIATDN GSPVATGTGT LLLILSDVND NAPIPEPRTI
610 620 630 640 650
FFCERNPKPQ VINIIDADLP PNTSPFTAEL THGASANWTI QYNDPTQESI
660 670 680 690 700
ILKPKMALEV GDYKINLKLM DNQNKDQVTT LEVSVCDCEG AAGVCRKAQP
710 720 730 740 750
VEAGLQIPAI LGILGGILAL LILILLLLLF LRRRAVVKEP LLPPEDDTRD
760 770 780 790 800
NVYYYDEEGG GEEDQDFDLS QLHRGLDARP EVTRNDVAPT LMSVPRYLPR
810 820 830 840 850
PANPDEIGNF IDENLKAADT DPTAPPYDSL LVFDYEGSGS EAASLSSLNS
860 870 880
SESDKDQDYD YLNEWGNRFK KLADMYGGGE DD
Length:882
Mass (Da):97,456
Last modified:July 1, 1993 - v3
Checksum:iE427118043A13C67
GO
Isoform 2 (identifier: P12830-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     380-440: Missing.

Show »
Length:821
Mass (Da):90,942
Checksum:i4EFF06672ACE35E9
GO

Sequence cautioni

The sequence AAA61259.1 differs from that shown. Reason: Frameshift at positions 16, 22, 25, 28, 31, 34, 52, 67, 73, 76, 94, 102, 633 and 636.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti10 – 101A → G in AAA61259. (PubMed:8185635)Curated
Sequence conflicti29 – 291H → L in AAA61259. (PubMed:8185635)Curated
Sequence conflicti47 – 471E → R in AAA61259. (PubMed:8185635)Curated
Sequence conflicti70 – 712SL → P in AAA61259. (PubMed:8185635)Curated
Sequence conflicti483 – 4831A → G in AAA61259. (PubMed:8185635)Curated
Sequence conflicti530 – 5301A → R in AAA61259. (PubMed:8185635)Curated
Sequence conflicti543 – 5431S → F in CAA79356. (PubMed:8127895)Curated
Sequence conflicti615 – 6151I → H in AAA61259. (PubMed:8185635)Curated
Sequence conflicti634 – 6363ASA → RVP in AAA61259. (PubMed:8185635)Curated
Sequence conflicti868 – 8681R → P in AAA61259. (PubMed:8185635)Curated
Sequence conflicti882 – 8821D → H in AAA61259. (PubMed:8185635)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti72 – 721D → N.
Corresponds to variant rs35606263 [ dbSNP | Ensembl ].
VAR_048500
Natural varianti123 – 1231H → Y in a gastric cancer sample.
VAR_001306
Natural varianti193 – 1931T → P in a diffuse gastric cancer sample. 1 Publication
VAR_001307
Natural varianti244 – 2441D → G in HDGC. 1 Publication
VAR_008712
Natural varianti270 – 2701S → A May contribute to prostate cancer. 1 Publication
VAR_013970
Natural varianti274 – 2774Missing Found in gastric carcinoma cell lines. 1 Publication
VAR_001308
Natural varianti282 – 2821M → I in a breast cancer sample; somatic mutation. 1 Publication
VAR_033026
Natural varianti315 – 3151N → S in lobular breast carcinoma. 1 Publication
VAR_001309
Natural varianti336 – 3361E → D.1 Publication
VAR_001310
Natural varianti340 – 3401T → A Found in gastric and colorectal cancer samples; cells exhibited decreased aggregation increased invasiveness and non-uniform migration in vitro compared to cells transfected with wild-type sequence. 2 Publications
VAR_013971
Natural varianti370 – 3701D → A in a diffuse gastric cancer sample. 1 Publication
VAR_001311
Natural varianti393 – 3931I → N.
Corresponds to variant rs34466743 [ dbSNP | Ensembl ].
VAR_048501
Natural varianti400 – 4001Missing in a gastric carcinoma sample; loss of heterozygosity. 1 Publication
VAR_001312
Natural varianti418 – 4236Missing in a gastric carcinoma sample. 1 Publication
VAR_001313
Natural varianti463 – 4631E → Q in a gastric carcinoma sample.
VAR_001314
Natural varianti470 – 4701T → I.1 Publication
VAR_001315
Natural varianti473 – 4731V → D in a diffuse gastric cancer sample. 1 Publication
VAR_001317
Natural varianti473 – 4731V → I.
Corresponds to variant rs36087757 [ dbSNP | Ensembl ].
VAR_048502
Natural varianti478 – 4781L → P.1 Publication
Corresponds to variant rs35520415 [ dbSNP | Ensembl ].
VAR_023357
Natural varianti487 – 4871V → A in HDGC. 1 Publication
VAR_008713
Natural varianti592 – 5921A → T in a thyroid cancer sample; may play a role in colorectal carcinogenesis. 2 Publications
Corresponds to variant rs35187787 [ dbSNP | Ensembl ].
VAR_001318
Natural varianti598 – 5981R → Q in a gastric cancer sample.
VAR_001319
Natural varianti617 – 6171A → T Detected in an endometrial cancer sample; loss of heterozygosity; cells exhibited an intermediate phenotype concerning aggregation invasiveness and migration in vitro compared to cells transfected with wild-type sequence. 3 Publications
Corresponds to variant rs33935154 [ dbSNP | Ensembl ].
VAR_001320
Natural varianti630 – 6301L → V.
Corresponds to variant rs2276331 [ dbSNP | Ensembl ].
VAR_021868
Natural varianti634 – 6341A → V Found in a gastric cancer sample; cells exhibited decreased aggregation increased invasiveness and non-uniform migration in vitro compared to cells transfected with wild-type sequence. 1 Publication
VAR_055431
Natural varianti695 – 6951C → R.
Corresponds to variant rs9282655 [ dbSNP | Ensembl ].
VAR_021869
Natural varianti711 – 7111L → V Detected in an endometrial cancer sample. 1 Publication
VAR_001321
Natural varianti777 – 7771D → N in a breast cancer sample; somatic mutation. 1 Publication
VAR_033027
Natural varianti832 – 8321V → M in HDGC. 2 Publications
Corresponds to variant rs35572355 [ dbSNP | Ensembl ].
VAR_023358
Natural varianti838 – 8381S → G in an ovarian carcinoma sample; somatic mutation; loss of heterozygosity. 1 Publication
VAR_001322
Natural varianti880 – 8801E → K.1 Publication
Corresponds to variant rs34507583 [ dbSNP | Ensembl ].
VAR_023359

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei380 – 44061Missing in isoform 2. 1 PublicationVSP_055586Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z13009 mRNA. Translation: CAA78353.1.
Z18923 mRNA. Translation: CAA79356.1.
L08599 mRNA. Translation: AAA61259.1. Frameshift.
AB025105 mRNA. Translation: BAA88956.1.
AK290012 mRNA. Translation: BAF82701.1.
AK312551 mRNA. Translation: BAG35448.1.
DQ090940 Genomic DNA. Translation: AAY68225.1.
AC099314 Genomic DNA. No translation available.
CH471092 Genomic DNA. Translation: EAW83243.1.
CH471092 Genomic DNA. Translation: EAW83244.1.
L34545 Genomic DNA. Translation: AAA21764.1.
D49685 Genomic DNA. Translation: BAA08537.1.
Z35402
, Z35403, Z35404, Z35405, Z35406, Z35407, Z35408, Z35409, Z35410, Z35411, Z35412, Z35413, Z35414, Z35415 Genomic DNA. Translation: CAA84586.1.
X12790 mRNA. Translation: CAA31279.1.
X52279 mRNA. Translation: CAA36522.1.
S72492, S72397, S72491 Genomic DNA. Translation: AAD14108.1.
CCDSiCCDS10869.1. [P12830-1]
PIRiS37654. IJHUCE.
RefSeqiNP_004351.1. NM_004360.3. [P12830-1]
UniGeneiHs.461086.

Genome annotation databases

EnsembliENST00000261769; ENSP00000261769; ENSG00000039068. [P12830-1]
ENST00000422392; ENSP00000414946; ENSG00000039068. [P12830-2]
GeneIDi999.
KEGGihsa:999.
UCSCiuc002ewg.1. human. [P12830-1]

Polymorphism databases

DMDMi399166.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology
NIEHS-SNPs
Wikipedia

E-cadherin entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z13009 mRNA. Translation: CAA78353.1 .
Z18923 mRNA. Translation: CAA79356.1 .
L08599 mRNA. Translation: AAA61259.1 . Frameshift.
AB025105 mRNA. Translation: BAA88956.1 .
AK290012 mRNA. Translation: BAF82701.1 .
AK312551 mRNA. Translation: BAG35448.1 .
DQ090940 Genomic DNA. Translation: AAY68225.1 .
AC099314 Genomic DNA. No translation available.
CH471092 Genomic DNA. Translation: EAW83243.1 .
CH471092 Genomic DNA. Translation: EAW83244.1 .
L34545 Genomic DNA. Translation: AAA21764.1 .
D49685 Genomic DNA. Translation: BAA08537.1 .
Z35402
, Z35403 , Z35404 , Z35405 , Z35406 , Z35407 , Z35408 , Z35409 , Z35410 , Z35411 , Z35412 , Z35413 , Z35414 , Z35415 Genomic DNA. Translation: CAA84586.1 .
X12790 mRNA. Translation: CAA31279.1 .
X52279 mRNA. Translation: CAA36522.1 .
S72492 , S72397 , S72491 Genomic DNA. Translation: AAD14108.1 .
CCDSi CCDS10869.1. [P12830-1 ]
PIRi S37654. IJHUCE.
RefSeqi NP_004351.1. NM_004360.3. [P12830-1 ]
UniGenei Hs.461086.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1O6S X-ray 1.80 B 156-255 [» ]
2O72 X-ray 2.00 A 155-367 [» ]
2OMT X-ray 2.00 B 156-255 [» ]
2OMU X-ray 1.80 B 156-255 [» ]
2OMV X-ray 1.90 B 156-255 [» ]
2OMX X-ray 1.70 B 156-258 [» ]
2OMY X-ray 1.70 B 156-254 [» ]
2OMZ X-ray 1.60 B 156-254 [» ]
3FF7 X-ray 1.80 A/B 155-253 [» ]
3FF8 X-ray 2.00 A/B 155-254 [» ]
3L6X X-ray 2.40 B 756-773 [» ]
3L6Y X-ray 3.00 B/D/F 756-773 [» ]
ProteinModelPortali P12830.
SMRi P12830. Positions 155-690, 782-875.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107434. 100 interactions.
DIPi DIP-477N.
IntActi P12830. 46 interactions.
MINTi MINT-119105.
STRINGi 9606.ENSP00000261769.

PTM databases

PhosphoSitei P12830.

Polymorphism databases

DMDMi 399166.

Proteomic databases

MaxQBi P12830.
PaxDbi P12830.
PRIDEi P12830.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000261769 ; ENSP00000261769 ; ENSG00000039068 . [P12830-1 ]
ENST00000422392 ; ENSP00000414946 ; ENSG00000039068 . [P12830-2 ]
GeneIDi 999.
KEGGi hsa:999.
UCSCi uc002ewg.1. human. [P12830-1 ]

Organism-specific databases

CTDi 999.
GeneCardsi GC16P068771.
GeneReviewsi CDH1.
HGNCi HGNC:1748. CDH1.
HPAi CAB000087.
CAB028364.
HPA004812.
MIMi 137215. phenotype.
167000. phenotype.
192090. gene.
608089. phenotype.
neXtProti NX_P12830.
Orphaneti 1991. Cleft lip with or without cleft palate.
26106. Familial gastric cancer.
36273. Gastric linitis plastica.
PharmGKBi PA26282.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG328838.
GeneTreei ENSGT00760000118906.
HOGENOMi HOG000231254.
HOVERGENi HBG106438.
InParanoidi P12830.
KOi K05689.
OMAi DFGVGQE.
OrthoDBi EOG7PS1DS.
PhylomeDBi P12830.
TreeFami TF316817.

Enzyme and pathway databases

Reactomei REACT_11152. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
REACT_118572. Degradation of the extracellular matrix.
REACT_13552. Integrin cell surface interactions.
REACT_13579. Apoptotic cleavage of cell adhesion proteins.
REACT_19195. Adherens junctions interactions.

Miscellaneous databases

ChiTaRSi CDH1. human.
EvolutionaryTracei P12830.
GeneWikii CDH1_(gene).
GenomeRNAii 999.
NextBioi 4200.
PMAP-CutDB P12830.
PROi P12830.
SOURCEi Search...

Gene expression databases

Bgeei P12830.
CleanExi HS_CDH1.
ExpressionAtlasi P12830. baseline and differential.
Genevestigatori P12830.

Family and domain databases

Gene3Di 2.60.40.60. 6 hits.
4.10.900.10. 1 hit.
InterProi IPR002126. Cadherin.
IPR015919. Cadherin-like.
IPR020894. Cadherin_CS.
IPR000233. Cadherin_cytoplasmic-dom.
IPR014868. Cadherin_pro_dom.
IPR027397. Catenin_binding_dom.
[Graphical view ]
Pfami PF00028. Cadherin. 5 hits.
PF01049. Cadherin_C. 1 hit.
PF08758. Cadherin_pro. 1 hit.
[Graphical view ]
PRINTSi PR00205. CADHERIN.
SMARTi SM00112. CA. 4 hits.
SM01055. Cadherin_pro. 1 hit.
[Graphical view ]
SUPFAMi SSF49313. SSF49313. 6 hits.
PROSITEi PS00232. CADHERIN_1. 3 hits.
PS50268. CADHERIN_2. 5 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and characterization of the human E-cadherin cDNA."
    Bussemakers M.J.G., Mees S.G.M., van Bokhoven A., Debruyne F.M.J., Schalken J.A.
    Mol. Biol. Rep. 17:123-128(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Pancreas.
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT 274-GLY--PRO-277 DEL.
  3. "Molecular cloning of human E-cadherin suggests a novel subdivision of the cadherin superfamily."
    Rimm D.L., Morrow J.S.
    Biochem. Biophys. Res. Commun. 200:1754-1761(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Liver.
  4. "Calcium influx triggers the sequential proteolysis of extracellular and cytoplasmic domains of E-cadherin, leading to loss of beta-catenin from cell-cell contacts."
    Ito K., Okamoto I., Araki N., Kawano Y., Nakao M., Fujiyama S., Tomita K., Mimori T., Saya H.
    Oncogene 18:7080-7090(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 586-591, PROTEOLYTIC PROCESSING, SUBCELLULAR LOCATION.
    Tissue: Epidermal carcinoma.
  5. "Mutant E-cadherin."
    Shibamoto S., Fukudome Y., Yanagihara K.
    Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  6. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Hippocampus and Tongue.
  7. NIEHS SNPs program
    Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS PRO-478; THR-617; MET-832 AND LYS-880.
  8. "The sequence and analysis of duplication-rich human chromosome 16."
    Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
    , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
    Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  10. "Transcriptional regulation of the human E-cadherin gene in human prostate cancer cell lines: characterization of the human E-cadherin gene promoter."
    Bussemakers M.J.G., Giroldi L.A., van Bokhoven A., Schalken J.A.
    Biochem. Biophys. Res. Commun. 203:1284-1290(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16.
  11. "Silencing of the E-cadherin invasion-suppressor gene by CpG methylation in human carcinomas."
    Yoshiura K., Kanai Y., Ochiai A., Shimoyama Y., Sugimura T., Hirohashi S.
    Proc. Natl. Acad. Sci. U.S.A. 92:7416-7419(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16.
    Tissue: Placenta.
  12. "Type I gamma phosphatidylinositol phosphate kinase modulates adherens junction and E-cadherin trafficking via a direct interaction with mu 1B adaptin."
    Ling K., Bairstow S.F., Carbonara C., Turbin D.A., Huntsman D.G., Anderson R.A.
    J. Cell Biol. 176:343-353(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PIP5K1C.
  13. "Cloning and characterization of the human invasion suppressor gene E-cadherin (CDH1)."
    Berx G., Staes K., van Hengel J., Molemans F., Bussemakers M.J.G., van Bokhoven A., van Roy F.
    Genomics 26:281-289(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 56-882.
    Tissue: Placenta.
  14. "Characterization and chromosomal localization of the gene encoding the human cell adhesion molecule uvomorulin."
    Mansouri A., Spurr N., Goodfellow P.N., Kemler R.
    Differentiation 38:67-71(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 172-311 (ISOFORM 1/2).
    Tissue: Liver.
  15. Frixen U.H.
    Submitted (MAR-1990) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 265-392 (ISOFORM 1).
    Tissue: Liver.
  16. "E-cadherin gene mutations provide clues to diffuse type gastric carcinomas."
    Becker K.-F., Atkinson M.J., Reich U., Becker I., Nekarda H., Siewert J.R., Hoefler H.
    Cancer Res. 54:3845-3852(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 337-476, VARIANTS ALA-370 AND ASP-473.
  17. "A presenilin-1/gamma-secretase cleavage releases the E-cadherin intracellular domain and regulates disassembly of adherens junctions."
    Marambaud P., Shioi J., Serban G., Georgakopoulos A., Sarner S., Nagy V., Baki L., Wen P., Efthimiopoulos S., Shao Z., Wisniewski T., Robakis N.K.
    EMBO J. 21:1948-1956(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 701-714 AND 732-742, PROTEOLYTIC PROCESSING BY GAMMA-SECRETASE/PS1 AND A MEMBRANE-BOUND METALLOPROTEINASE, MUTAGENESIS OF 759-GLY--GLY-761.
  18. "Uvomorulin-catenin complex formation is regulated by a specific domain in the cytoplasmic region of the cell adhesion molecule."
    Ozawa M., Ringwald M., Kemler R.
    Proc. Natl. Acad. Sci. U.S.A. 87:4246-4250(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN CATENIN-BINDING.
  19. "Distinct cadherin-catenin complexes in Ca(2+)-dependent cell-cell adhesion."
    Butz S., Kemler R.
    FEBS Lett. 355:195-200(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN AN E-CADHERIN/CATENIN ADHESION COMPLEX.
  20. "Cleavage and shedding of E-cadherin after induction of apoptosis."
    Steinhusen U., Weiske J., Badock V., Tauber R., Bommert K., Huber O.
    J. Biol. Chem. 276:4972-4980(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC PROCESSING.
  21. "Presenilin-1 binds cytoplasmic epithelial cadherin, inhibits cadherin/p120 association, and regulates stability and function of the cadherin/catenin adhesion complex."
    Baki L., Marambaud P., Efthimiopoulos S., Georgakopoulos A., Wen P., Cui W., Shioi J., Koo E., Ozawa M., Friedrich V.L., Robakis N.K.
    Proc. Natl. Acad. Sci. U.S.A. 98:2381-2386(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PSEN1.
  22. "Disulfide bond formation promotes the cis- and trans-dimerization of the E-cadherin-derived first repeat."
    Makagiansar I.T., Nguyen P.D., Ikesue A., Kuczera K., Dentler W., Urbauer J.L., Galeva N., Alterman M., Siahaan T.J.
    J. Biol. Chem. 277:16002-16010(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERCHAIN DISULFIDE BOND.
  23. "Human homolog of disc-large is required for adherens junction assembly and differentiation of human intestinal epithelial cells."
    Laprise P., Viel A., Rivard N.
    J. Biol. Chem. 279:10157-10166(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DLGAP5, SUBCELLULAR LOCATION.
  24. "Novel membrane protein shrew-1 targets to cadherin-mediated junctions in polarized epithelial cells."
    Bharti S., Handrow-Metzmacher H., Zickenheiner S., Zeitvogel A., Baumann R., Starzinski-Powitz A.
    Mol. Biol. Cell 15:397-406(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AJAP1.
    Tissue: Brain.
  25. "Cadherins mediate both the association between PS1 and beta-catenin and the effects of PS1 on beta-catenin stability."
    Serban G., Kouchi Z., Baki L., Georgakopoulos A., Litterst C.M., Shioi J., Robakis N.K.
    J. Biol. Chem. 280:36007-36012(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH WITH PSEN1 AND CTNNB1, MUTAGENESIS OF 759-GLY--GLY-761.
  26. "Rab11 in recycling endosomes regulates the sorting and basolateral transport of E-cadherin."
    Lock J.G., Stow J.L.
    Mol. Biol. Cell 16:1744-1755(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  27. "The cytoplasmic sequence of E-cadherin promotes non-amyloidogenic degradation of A beta precursors."
    Agiostratidou G., Muros R.M., Shioi J., Marambaud P., Robakis N.K.
    J. Neurochem. 96:1182-1188(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF E-CAD/CTF2.
  28. "Induction of the LRP16 gene by estrogen promotes the invasive growth of Ishikawa human endometrial cancer cells through the downregulation of E-cadherin."
    Meng Y.G., Han W.-D., Zhao Y.-L., Huang K., Si Y.-L., Wu Z.-Q., Mu Y.-M.
    Cell Res. 17:869-880(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  29. Cited for: INVOLVEMENT IN LBC.
  30. "Unglycosylation at Asn-633 made extracellular domain of E-cadherin folded incorrectly and arrested in endoplasmic reticulum, then sequentially 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) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT ASN-558; ASN-570; ASN-622 AND ASN-637, MUTAGENESIS OF ASN-637.
  31. "EPLIN mediates linkage of the cadherin catenin complex to F-actin and stabilizes the circumferential actin belt."
    Abe K., Takeichi M.
    Proc. Natl. Acad. Sci. U.S.A. 105:13-19(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LIMA1.
  32. "Structure and biochemistry of cadherins and catenins."
    Shapiro L., Weis W.I.
    Cold Spring Harb. Perspect. Biol. 1:A3053-A3053(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON CADHERINS.
  33. Cited for: INTERACTION WITH TBC1D2.
  34. "DDR1 regulates the stabilization of cell surface E-cadherin and E-cadherin-mediated cell aggregation."
    Eswaramoorthy R., Wang C.K., Chen W.C., Tang M.J., Ho M.L., Hwang C.C., Wang H.M., Wang C.Z.
    J. Cell. Physiol. 224:387-397(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH DDR1.
  35. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  36. "Slit-Robo signaling induces malignant transformation through Hakai-mediated E-cadherin degradation during colorectal epithelial cell carcinogenesis."
    Zhou W.J., Geng Z.H., Chi S., Zhang W., Niu X.F., Lan S.J., Ma L., Yang X., Wang L.J., Ding Y.Q., Geng J.G.
    Cell Res. 21:609-626(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION BY CBLL1.
  37. Cited for: UBIQUITINATION BY A SKP2-CONTAINING SCF COMPLEX, PHOSPHORYLATION BY CSNK1A1.
  38. Cited for: PHOSPHORYLATION AT TYR-753; TYR-754 AND TYR-755, MUTAGENESIS OF TYR-754.
  39. "Structure of internalin, a major invasion protein of Listeria monocytogenes, in complex with its human receptor E-cadherin."
    Schubert W.-D., Urbanke C., Ziehm T., Beier V., Machner M.P., Domann E., Wehland J., Chakraborty T., Heinz D.W.
    Cell 111:825-836(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 156-255 IN COMPLEX WITH LISTERIA INTERNALIN.
  40. "Mutations of the human E-cadherin (CDH1) gene."
    Berx G., Becker K.-F., Hoefler H., van Roy F.
    Hum. Mutat. 12:226-237(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON VARIANTS.
  41. "The crystal structure of human E-cadherin domains 1 and 2, and comparison with other cadherins in the context of adhesion mechanism."
    Parisini E., Higgins J.M., Liu J.H., Brenner M.B., Wang J.H.
    J. Mol. Biol. 373:401-411(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 155-367, CALCIUM-BINDING SITES.
  42. "Structure of natural killer cell receptor KLRG1 bound to E-cadherin reveals basis for MHC-independent missing self recognition."
    Li Y., Hofmann M., Wang Q., Teng L., Chlewicki L.K., Pircher H., Mariuzza R.A.
    Immunity 31:35-46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 155-253 IN COMPLEX WITH KLRG1.
  43. "Point mutation of the E-cadherin gene in invasive lobular carcinoma of the breast."
    Kanai Y., Oda T., Tsuda H., Ochiai A., Hirohashi S.
    Jpn. J. Cancer Res. 85:1035-1039(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT LOBULAR BREAST CARCINOMA SER-315.
  44. "Mutations of the E-cadherin gene in human gynecologic cancers."
    Risinger J.I., Berchuck A., Kohler M.F., Boyd J.
    Nat. Genet. 7:98-102(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS THR-617 AND VAL-711, VARIANT OVARIAN CANCER GLY-838.
  45. "E-cadherin gene mutations in signet ring cell carcinoma of the stomach."
    Muta H., Noguchi M., Kanai Y., Ochiai A., Nawata H., Hirohashi S.
    Jpn. J. Cancer Res. 87:843-848(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT PRO-193.
  46. "Inactivation of the E-cadherin gene in primary gastric carcinomas and gastric carcinoma cell lines."
    Tamura G., Sakata K., Nishizuka S., Maesawa C., Suzuki Y., Iwaya T., Terashima M., Saito K., Satodate R.
    Jpn. J. Cancer Res. 87:1153-1159(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS ASP-400 DEL AND 418-ASP--PHE-423 DEL.
  47. "E-cadherin gene alterations are rare events in thyroid tumors."
    Soares P., Berx G., van Roy F., Sobrinho-Simoes M.
    Int. J. Cancer 70:32-38(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT THYROID CANCER THR-592.
  48. Cited for: VARIANTS ASP-336 AND ILE-470.
  49. "Germline mutations of E-cadherin gene in Korean familial gastric cancer patients."
    Yoon K.-A., Ku J.-L., Yang H.-K., Kim W.H., Park S.Y., Park J.-G.
    J. Hum. Genet. 44:177-180(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS HDGC GLY-244 AND ALA-487.
  50. "The E-cadherin gene (CDH1) variants T340A and L599V in gastric and colorectal cancer patients in Korea."
    Kim H.C., Wheeler J.M.D., Kim J.C., Ilyas M., Beck N.E., Kim B.S., Park K.C., Bodmer W.F.
    Gut 47:262-267(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT ALA-340.
  51. "Association of E-cadherin germ-line alterations with prostate cancer."
    Ikonen T., Matikainen M., Mononen N., Hyytinen E.R., Helin H.J., Tommola S., Tammela T.L., Pukkala E., Schleutker J., Kallioniemi O.-P., Koivisto P.A.
    Clin. Cancer Res. 7:3465-3471(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT ALA-270.
  52. "A germline E-cadherin mutation in a family with gastric and colon cancer."
    Salahshor S., Hou H., Diep C.B., Loukola A., Zhang H., Liu T., Chen J., Iselius L., Rubio C., Lothe R.A., Aaltonen L., Sun X.F., Lindmark G., Lindblom A.
    Int. J. Mol. Med. 8:439-443(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT THR-592.
  53. "Screening E-cadherin in gastric cancer families reveals germline mutations only in hereditary diffuse gastric cancer kindred."
    Oliveira C., Bordin M.C., Grehan N., Huntsman D., Suriano G., Machado J.C., Kiviluoto T., Aaltonen L., Jackson C.E., Seruca R., Caldas C.
    Hum. Mutat. 19:510-517(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT ALA-340.
  54. "E-cadherin gene variants in gastric cancer families whose probands are diagnosed with diffuse gastric cancer."
    Yabuta T., Shinmura K., Tani M., Yamaguchi S., Yoshimura K., Katai H., Nakajima T., Mochiki E., Tsujinaka T., Takami M., Hirose K., Yamaguchi A., Takenoshita S., Yokota J.
    Int. J. Cancer 101:434-441(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT HDGC MET-832.
  55. "Identification of CDH1 germline missense mutations associated with functional inactivation of the E-cadherin protein in young gastric cancer probands."
    Suriano G., Oliveira C., Ferreira P., Machado J.C., Bordin M.C., De Wever O., Bruyneel E.A., Moguilevsky N., Grehan N., Porter T.R., Richards F.M., Hruban R.H., Roviello F., Huntsman D., Mareel M., Carneiro F., Caldas C., Seruca R.
    Hum. Mol. Genet. 12:575-582(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS THR-617 AND VAL-634, CHARACTERIZATION OF VARIANTS ALA-340; THR-617 AND VAL-634.
  56. "Somatic sequence alterations in twenty-one genes selected by expression profile analysis of breast carcinomas."
    Chanock S.J., Burdett L., Yeager M., Llaca V., Langeroed A., Presswalla S., Kaaresen R., Strausberg R.L., Gerhard D.S., Kristensen V., Perou C.M., Boerresen-Dale A.-L.
    Breast Cancer Res. 9:R5-R5(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS ILE-282 AND ASN-777.

Entry informationi

Entry nameiCADH1_HUMAN
AccessioniPrimary (citable) accession number: P12830
Secondary accession number(s): A8K1U7
, Q13799, Q14216, Q15855, Q16194, Q4PJ14, Q9UII8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: July 1, 1993
Last modified: October 29, 2014
This is version 189 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  2. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3