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P12830

- CADH1_HUMAN

UniProt

P12830 - CADH1_HUMAN

Protein

Cadherin-1

Gene

CDH1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 188 (01 Oct 2014)
      Sequence version 3 (01 Jul 1993)
      Previous versions | rss
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    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: BHF-UCL
    5. gamma-catenin binding Source: BHF-UCL
    6. glycoprotein binding Source: UniProt
    7. GTPase activating protein binding Source: UniProtKB
    8. protein binding Source: UniProtKB

    GO - Biological processi

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

    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-SubCell
    14. extracellular region Source: Reactome
    15. extracellular vesicular exosome Source: UniProt
    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

    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.

    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 SRC2 Publications
    Modified residuei754 – 7541Phosphotyrosine; by SRC2 Publications
    Modified residuei755 – 7551Phosphotyrosine; by SRC2 Publications
    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

    ArrayExpressiP12830.
    BgeeiP12830.
    CleanExiHS_CDH1.
    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
    EGFRP005332EBI-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.
    HOGENOMiHOG000231254.
    HOVERGENiHBG106438.
    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

    MGPWSRSLSA LLLLLQVSSW LCQEPEPCHP GFDAESYTFT VPRRHLERGR    50
    VLGRVNFEDC TGRQRTAYFS LDTRFKVGTD GVITVKRPLR FHNPQIHFLV 100
    YAWDSTYRKF STKVTLNTVG HHHRPPPHQA SVSGIQAELL TFPNSSPGLR 150
    RQKRDWVIPP ISCPENEKGP FPKNLVQIKS NKDKEGKVFY SITGQGADTP 200
    PVGVFIIERE TGWLKVTEPL DRERIATYTL FSHAVSSNGN AVEDPMEILI 250
    TVTDQNDNKP EFTQEVFKGS VMEGALPGTS VMEVTATDAD DDVNTYNAAI 300
    AYTILSQDPE LPDKNMFTIN RNTGVISVVT TGLDRESFPT YTLVVQAADL 350
    QGEGLSTTAT AVITVTDTND NPPIFNPTTY KGQVPENEAN VVITTLKVTD 400
    ADAPNTPAWE AVYTILNDDG GQFVVTTNPV NNDGILKTAK GLDFEAKQQY 450
    ILHVAVTNVV PFEVSLTTST ATVTVDVLDV NEAPIFVPPE KRVEVSEDFG 500
    VGQEITSYTA QEPDTFMEQK ITYRIWRDTA NWLEINPDTG AISTRAELDR 550
    EDFEHVKNST YTALIIATDN GSPVATGTGT LLLILSDVND NAPIPEPRTI 600
    FFCERNPKPQ VINIIDADLP PNTSPFTAEL THGASANWTI QYNDPTQESI 650
    ILKPKMALEV GDYKINLKLM DNQNKDQVTT LEVSVCDCEG AAGVCRKAQP 700
    VEAGLQIPAI LGILGGILAL LILILLLLLF LRRRAVVKEP LLPPEDDTRD 750
    NVYYYDEEGG GEEDQDFDLS QLHRGLDARP EVTRNDVAPT LMSVPRYLPR 800
    PANPDEIGNF IDENLKAADT DPTAPPYDSL LVFDYEGSGS EAASLSSLNS 850
    SESDKDQDYD YLNEWGNRFK KLADMYGGGE DD 882
    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.
    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.
    PIRiS37654. IJHUCE.
    RefSeqiNP_004351.1. NM_004360.3.
    UniGeneiHs.461086.

    Genome annotation databases

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

    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.
    PIRi S37654. IJHUCE.
    RefSeqi NP_004351.1. NM_004360.3.
    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.

    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.
    HOGENOMi HOG000231254.
    HOVERGENi HBG106438.
    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

    ArrayExpressi P12830.
    Bgeei P12830.
    CleanExi HS_CDH1.
    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

    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 1, 2014
    This is version 188 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