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UniProtKB - P12830 (CADH1_HUMAN)

Entry version 235 (13 Feb 2019)
Sequence version 3 (01 Jul 1993)
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Protein

Cadherin-1

Gene

CDH1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Cadherins are calcium-dependent cell adhesion proteins (PubMed:11976333). They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. CDH1 is involved in mechanisms regulating cell-cell adhesions, mobility and proliferation of epithelial cells (PubMed:11976333). Has a potent invasive suppressor role. It is a ligand for integrin alpha-E/beta-7.2 Publications
E-Cad/CTF2 promotes non-amyloidogenic degradation of Abeta precursors. Has a strong inhibitory effect on APP C99 and C83 production.1 Publication
(Microbial infection) Serves as a receptor for Listeria monocytogenes; internalin A (InlA) binds to this protein and promotes uptake of the bacteria.3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi257Calcium 11
Metal bindingi257Calcium 21
Metal bindingi288Calcium 31

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

  • ankyrin binding Source: BHF-UCL
  • beta-catenin binding Source: BHF-UCL
  • cadherin binding Source: BHF-UCL
  • calcium ion binding Source: GO_Central
  • cell adhesion molecule binding Source: UniProtKB
  • cytoskeletal protein binding Source: GO_Central
  • gamma-catenin binding Source: BHF-UCL
  • GTPase activating protein binding Source: UniProtKB
  • identical protein binding Source: IntAct
  • protein homodimerization activity Source: GO_Central
View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Biological processCell adhesion
LigandCalcium, Metal-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-1474228 Degradation of the extracellular matrix
R-HSA-198933 Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell
R-HSA-216083 Integrin cell surface interactions
R-HSA-351906 Apoptotic cleavage of cell adhesion proteins
R-HSA-418990 Adherens junctions interactions
R-HSA-5626467 RHO GTPases activate IQGAPs
R-HSA-8876493 InlA-mediated entry of Listeria monocytogenes into host cells

SIGNOR Signaling Network Open Resource

More...SIGNORi		P12830

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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:
E-Cad/CTF1
E-Cad/CTF2
E-Cad/CTF3
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:CDH1
Synonyms:CDHE, UVO
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 16

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...EuPathDBi		HostDB:ENSG00000039068.18

Human Gene Nomenclature Database

More...HGNCi		HGNC:1748 CDH1

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		192090 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P12830

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini155 – 709ExtracellularSequence analysisAdd BLAST555
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei710 – 730HelicalSequence analysisAdd BLAST21
Topological domaini731 – 882CytoplasmicSequence analysisAdd BLAST152

Keywords - Cellular componenti

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

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Hereditary diffuse gastric cancer (HDGC)2 Publications
Disease susceptibility is associated with variations affecting the gene represented in this entry. Heterozygous CDH1 germline mutations are responsible for familial cases of diffuse gastric cancer. Somatic mutations has also been found in patients with sporadic diffuse gastric cancer and lobular breast cancer.
Disease descriptionA 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.
See also OMIM:137215
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_008712244D → G in HDGC. 1 PublicationCorresponds to variant dbSNP:rs1064794231Ensembl.1
Natural variantiVAR_008713487V → A in HDGC. 1 Publication1
Natural variantiVAR_023358832V → M in HDGC. 2 PublicationsCorresponds to variant dbSNP:rs35572355EnsemblClinVar.1
Endometrial cancer (ENDMC)
Disease susceptibility is associated with variations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:608089
Ovarian cancer (OC)1 Publication
Disease susceptibility is associated with variations affecting the gene represented in this entry.
Disease descriptionThe 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.
See also OMIM:167000
Breast cancer, lobular (LBC)1 Publication
The gene represented in this entry may be involved in disease pathogenesis.
Disease descriptionA type of breast cancer that begins in the milk-producing glands (lobules) of the breast.
See also OMIM:137215
Blepharocheilodontic syndrome 1 (BCDS1)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of blepharocheilodontic syndrome, a rare autosomal dominant disorder. It is characterized by lower eyelid ectropion, upper eyelid distichiasis, euryblepharon, bilateral cleft lip and palate, and features of ectodermal dysplasia, including hair anomalies, conical teeth and tooth agenesis. An additional rare manifestation is imperforate anus. There is considerable phenotypic variability among affected individuals.
See also OMIM:119580
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_079392254D → Y in BCDS1; abolishes protein abundance; loss of cell membrane localization. 1 Publication1
Natural variantiVAR_079393257D → V in BCDS1; slightly decreases protein abundance; loss of cell membrane localization. 1 Publication1
Natural variantiVAR_079394454Missing in BCDS1; decreases protein abundance; loss of cell membrane localization. 1 Publication1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi156W → A or S: No longer binds L.monocytogenes InlA. 1 Publication1
Mutagenesisi156W → D: Protein is partially unfolded, no longer binds L.monocytogenes InlA. 1 Publication1
Mutagenesisi170P → A, E or V: No longer binds L.monocytogenes InlA. 1 Publication1
Mutagenesisi170P → E: No longer adheres to L.monocytogenes InlA coated beads, nor do cells take up InlA coated beads. 1 Publication1
Mutagenesisi637N → Q: CDH1 becomes a substrate for ERAD and is retro-translocated from ER to cytoplasm. 1 Publication1
Mutagenesisi754Y → F: Abolishes binding to CBLL1. 1 Publication1
Mutagenesisi759 – 761GGG → AAA: Binds to CTNNB1 but abolishes interaction of CTNNB1 with PSEN1. Abolishes gamma-secretase cleavage. 2 Publications3

Keywords - Diseasei

Disease mutation, Ectodermal dysplasia

Organism-specific databases

DisGeNET

More...DisGeNETi		999

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

More...GeneReviewsi		CDH1

MalaCards human disease database

More...MalaCardsi		CDH1
MIMi119580 phenotype
137215 phenotype
167000 phenotype
608089 phenotype

Open Targets

More...OpenTargetsi		ENSG00000039068

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...Orphaneti		1997 Blepharo-cheilo-odontic syndrome
199306 Cleft lip/palate
26106 Hereditary diffuse gastric cancer

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA26282

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL2321609

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		CDH1

Domain mapping of disease mutations (DMDM)

More...DMDMi		399166

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 22Sequence analysisAdd BLAST22
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_000000371523 – 154Sequence analysisAdd BLAST132
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000003716155 – 882Cadherin-1Add BLAST728
ChainiPRO_0000236067701 – 882E-Cad/CTF1Add BLAST182
ChainiPRO_0000236068732 – 882E-Cad/CTF2Add BLAST151
ChainiPRO_0000236069751 – 882E-Cad/CTF3Add BLAST132

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi163Interchain
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi280O-linked (Man...) serineBy similarity1
Glycosylationi285O-linked (Man...) threonineBy similarity1
Glycosylationi358O-linked (Man...) threonineBy similarity1
Glycosylationi470O-linked (Man...) threonineBy similarity1
Glycosylationi472O-linked (Man...) threonineBy similarity1
Glycosylationi509O-linked (Man...) threonineBy similarity1
Glycosylationi558N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi570N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi576O-linked (Man...) threonineBy similarity1
Glycosylationi578O-linked (Man...) threonineBy similarity1
Glycosylationi580O-linked (Man...) threonineBy similarity1
Glycosylationi622N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi637N-linked (GlcNAc...) asparagine1 Publication1
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei753Phosphotyrosine; by SRC1 Publication1
Modified residuei754Phosphotyrosine; by SRC1 Publication1
Modified residuei755Phosphotyrosine; by SRC1 Publication1
Modified residuei770PhosphoserineCombined sources1
Modified residuei793PhosphoserineCombined sources1
Modified residuei838PhosphoserineBy similarity1
Modified residuei840PhosphoserineBy similarity1
Modified residuei846PhosphoserineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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. Addition of bisecting N-acetylglucosamine by MGAT3 modulates its cell membrane location (PubMed:19403558).2 Publications
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
O-glycosylated. O-manosylated by TMTC1, TMTC2, TMTC3 or TMTC4. Thr-285 and Thr-509 are O-mannosylated by TMTC2 or TMTC4 but not TMTC1 or TMTC3.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei700 – 701Cleavage; by a metalloproteinase2
Sitei731 – 732Cleavage; by gamma-secretase/PS12
Sitei750 – 751Cleavage; by caspase-32

Keywords - PTMi

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

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P12830

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P12830

MaxQB - The MaxQuant DataBase

More...MaxQBi		P12830

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P12830

PeptideAtlas

More...PeptideAtlasi		P12830

PRoteomics IDEntifications database

More...PRIDEi		P12830

ProteomicsDB human proteome resource

More...ProteomicsDBi		52879

Consortium for Top Down Proteomics

More...TopDownProteomicsi		P12830-2 [P12830-2]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P12830

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		P12830

Miscellaneous databases

CutDB - Proteolytic event database

More...PMAP-CutDBi		P12830

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Non-neural epithelial tissues.

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Expression is repressed by MACROD1.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000039068 Expressed in 185 organ(s), highest expression level in jejunal mucosa

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P12830 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P12830 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		CAB000087
CAB028364
CAB072855
CAB072856
CAB072857
HPA004812

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer; disulfide-linked (PubMed:11856755). 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 (PubMed:16126725, PubMed:7982500). Interacts with the TRPV4 and CTNNB1 complex (By similarity). Interacts with CTNND1 (PubMed:15240885). The stable association of CTNNA1 is controversial as CTNNA1 was shown not to bind to F-actin when assembled in the complex (By similarity). Alternatively, the CTNNA1-containing complex may be linked to F-actin by other proteins such as LIMA1 (By similarity). Interaction with PSEN1, cleaves CDH1 resulting in the disassociation of cadherin-based adherens junctions (CAJs) (PubMed:11226248, PubMed:16126725). Interacts with AJAP1 and DLGAP5 (PubMed:14699157, PubMed:14595118). Interacts with TBC1D2 (PubMed:20116244). Interacts with LIMA1 (PubMed:18093941). Interacts with CAV1. Interacts with PIP5K1C (PubMed:17261850). Interacts with RAB8B (By similarity). Interacts with RAPGEF2 (By similarity). Interacts with DDR1; this stabilizes CDH1 at the cell surface and inhibits its internalization (PubMed:20432435). Interacts with KLRG1 (PubMed:19604491).By similarity13 Publications
(Microbial infection) Interacts with L.monocytogenes InlA (PubMed:12526809, PubMed:17540170, PubMed:17715295). The formation of the complex between InlA and cadherin-1 is calcium-dependent (PubMed:12526809).3 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		107434, 631 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		P12830

Database of interacting proteins

More...DIPi		DIP-477N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...ELMi		P12830

Protein interaction database and analysis system

More...IntActi		P12830, 81 interactors

Molecular INTeraction database

More...MINTi		P12830

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000261769

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1882
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB 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[»]
4ZT1X-ray1.92A/B157-367[»]
4ZTEX-ray2.13A/B157-367[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		P12830

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P12830

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P12830

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini155 – 262Cadherin 1PROSITE-ProRule annotationAdd BLAST108
Domaini263 – 375Cadherin 2PROSITE-ProRule annotationAdd BLAST113
Domaini376 – 486Cadherin 3PROSITE-ProRule annotationAdd BLAST111
Domaini487 – 593Cadherin 4PROSITE-ProRule annotationAdd BLAST107
Domaini594 – 697Cadherin 5PROSITE-ProRule annotationAdd BLAST104

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni758 – 769Required for binding CTNND1 and PSEN1Add BLAST12
Regioni811 – 882Required for binding alpha, beta and gamma cateninsAdd BLAST72

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi838 – 851Ser-richAdd BLAST14

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG3594 Eukaryota
ENOG410XQHI LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00940000157175

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000231254

The HOVERGEN Database of Homologous Vertebrate Genes

More...HOVERGENi		HBG106438

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P12830

KEGG Orthology (KO)

More...KOi		K05689

Database of Orthologous Groups

More...OrthoDBi		182239at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P12830

TreeFam database of animal gene trees

More...TreeFami		TF316817

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		4.10.900.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR039808 Cadherin
IPR002126 Cadherin-like_dom
IPR015919 Cadherin-like_sf
IPR020894 Cadherin_CS
IPR000233 Cadherin_cytoplasmic-dom
IPR014868 Cadherin_pro_dom
IPR027397 Catenin_binding_dom_sf

The PANTHER Classification System

More...PANTHERi		PTHR24027 PTHR24027, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00028 Cadherin, 5 hits
PF01049 Cadherin_C, 1 hit
PF08758 Cadherin_pro, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00205 CADHERIN

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00112 CA, 4 hits
SM01055 Cadherin_pro, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF49313 SSF49313, 6 hits

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00232 CADHERIN_1, 3 hits
PS50268 CADHERIN_2, 5 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 6 potential isoforms that are computationally mapped.Show allAlign All

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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> 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

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 6 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A087WXI5A0A087WXI5_HUMAN
Cadherin-1
CDH1
903Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
H3BNC6H3BNC6_HUMAN
Cadherin-1
CDH1
537Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
H3BVI7H3BVI7_HUMAN
Cadherin-1
CDH1
414Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A087WU43A0A087WU43_HUMAN
Cadherin-1
CDH1
647Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A087WX17A0A087WX17_HUMAN
Cadherin-1
CDH1
647Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
J3QKP1J3QKP1_HUMAN
Cadherin-1
CDH1
155Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti10A → G in AAA61259 (PubMed:8185635).Curated1
Sequence conflicti29H → L in AAA61259 (PubMed:8185635).Curated1
Sequence conflicti47E → R in AAA61259 (PubMed:8185635).Curated1
Sequence conflicti70 – 71SL → P in AAA61259 (PubMed:8185635).Curated2
Sequence conflicti483A → G in AAA61259 (PubMed:8185635).Curated1
Sequence conflicti530A → R in AAA61259 (PubMed:8185635).Curated1
Sequence conflicti543S → F in CAA79356 (PubMed:8127895).Curated1
Sequence conflicti615I → H in AAA61259 (PubMed:8185635).Curated1
Sequence conflicti634 – 636ASA → RVP in AAA61259 (PubMed:8185635).Curated3
Sequence conflicti868R → P in AAA61259 (PubMed:8185635).Curated1
Sequence conflicti882D → H in AAA61259 (PubMed:8185635).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04850072D → N. Corresponds to variant dbSNP:rs35606263EnsemblClinVar.1
Natural variantiVAR_001306123H → Y in a gastric cancer sample. 1
Natural variantiVAR_001307193T → P in a diffuse gastric cancer sample. 1 Publication1
Natural variantiVAR_008712244D → G in HDGC. 1 PublicationCorresponds to variant dbSNP:rs1064794231Ensembl.1
Natural variantiVAR_079392254D → Y in BCDS1; abolishes protein abundance; loss of cell membrane localization. 1 Publication1
Natural variantiVAR_079393257D → V in BCDS1; slightly decreases protein abundance; loss of cell membrane localization. 1 Publication1
Natural variantiVAR_013970270S → A May contribute to prostate cancer. 1 PublicationCorresponds to variant dbSNP:rs587776399EnsemblClinVar.1
Natural variantiVAR_001308274 – 277Missing Found in gastric carcinoma cell lines. 1 Publication4
Natural variantiVAR_033026282M → I in a breast cancer sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs200932258EnsemblClinVar.1
Natural variantiVAR_001309315N → S in lobular breast carcinoma. 1 Publication1
Natural variantiVAR_001310336E → D1 PublicationCorresponds to variant dbSNP:rs267606712EnsemblClinVar.1
Natural variantiVAR_013971340T → 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. 3 PublicationsCorresponds to variant dbSNP:rs116093741EnsemblClinVar.1
Natural variantiVAR_001311370D → A in a diffuse gastric cancer sample. 1 Publication1
Natural variantiVAR_048501393I → N. Corresponds to variant dbSNP:rs34466743EnsemblClinVar.1
Natural variantiVAR_001312400Missing in a gastric carcinoma sample; loss of heterozygosity. 1 Publication1
Natural variantiVAR_001313418 – 423Missing in a gastric carcinoma sample. 1 Publication6
Natural variantiVAR_079394454Missing in BCDS1; decreases protein abundance; loss of cell membrane localization. 1 Publication1
Natural variantiVAR_001314463E → Q in a gastric carcinoma sample. 1
Natural variantiVAR_001315470T → I1 PublicationCorresponds to variant dbSNP:rs370864592EnsemblClinVar.1
Natural variantiVAR_001317473V → D in a diffuse gastric cancer sample. 1 Publication1
Natural variantiVAR_048502473V → I. Corresponds to variant dbSNP:rs36087757EnsemblClinVar.1
Natural variantiVAR_023357478L → P1 PublicationCorresponds to variant dbSNP:rs35520415EnsemblClinVar.1
Natural variantiVAR_008713487V → A in HDGC. 1 Publication1
Natural variantiVAR_001318592A → T in a thyroid cancer sample; may play a role in colorectal carcinogenesis. 2 PublicationsCorresponds to variant dbSNP:rs35187787EnsemblClinVar.1
Natural variantiVAR_001319598R → Q in a gastric cancer sample. Corresponds to variant dbSNP:rs780759537EnsemblClinVar.1
Natural variantiVAR_001320617A → 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 PublicationsCorresponds to variant dbSNP:rs33935154EnsemblClinVar.1
Natural variantiVAR_021868630L → V. Corresponds to variant dbSNP:rs2276331EnsemblClinVar.1
Natural variantiVAR_055431634A → 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 PublicationCorresponds to variant dbSNP:rs121964878EnsemblClinVar.1
Natural variantiVAR_021869695C → R. Corresponds to variant dbSNP:rs9282655Ensembl.1
Natural variantiVAR_001321711L → V Detected in an endometrial cancer sample. 1 PublicationCorresponds to variant dbSNP:rs121964871EnsemblClinVar.1
Natural variantiVAR_033027777D → N in a breast cancer sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs372989292EnsemblClinVar.1
Natural variantiVAR_023358832V → M in HDGC. 2 PublicationsCorresponds to variant dbSNP:rs35572355EnsemblClinVar.1
Natural variantiVAR_001322838S → G in an ovarian carcinoma sample; somatic mutation; loss of heterozygosity. 1 PublicationCorresponds to variant dbSNP:rs121964872EnsemblClinVar.1
Natural variantiVAR_023359880E → K1 PublicationCorresponds to variant dbSNP:rs34507583EnsemblClinVar.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_055586380 – 440Missing in isoform 2. 1 PublicationAdd BLAST61

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
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

The Consensus CDS (CCDS) project

More...CCDSi		CCDS10869.1 [P12830-1]
CCDS82005.1 [P12830-2]

Protein sequence database of the Protein Information Resource

More...PIRi		S37654 IJHUCE

NCBI Reference Sequences

More...RefSeqi		NP_001304113.1, NM_001317184.1 [P12830-2]
NP_001304114.1, NM_001317185.1
NP_001304115.1, NM_001317186.1
NP_004351.1, NM_004360.4 [P12830-1]

UniGene gene-oriented nucleotide sequence clusters

More...UniGenei		Hs.461086

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000261769; ENSP00000261769; ENSG00000039068 [P12830-1]
ENST00000422392; ENSP00000414946; ENSG00000039068 [P12830-2]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		999

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:999

UCSC genome browser

More...UCSCi		uc002ewg.2 human [P12830-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

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

E-cadherin entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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]
CCDS82005.1 [P12830-2]
PIRiS37654 IJHUCE
RefSeqiNP_001304113.1, NM_001317184.1 [P12830-2]
NP_001304114.1, NM_001317185.1
NP_001304115.1, NM_001317186.1
NP_004351.1, NM_004360.4 [P12830-1]
UniGeneiHs.461086

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4ZT1X-ray1.92A/B157-367[»]
4ZTEX-ray2.13A/B157-367[»]
ProteinModelPortaliP12830
SMRiP12830
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107434, 631 interactors
CORUMiP12830
DIPiDIP-477N
ELMiP12830
IntActiP12830, 81 interactors
MINTiP12830
STRINGi9606.ENSP00000261769

Chemistry databases

ChEMBLiCHEMBL2321609

PTM databases

iPTMnetiP12830
PhosphoSitePlusiP12830

Polymorphism and mutation databases

BioMutaiCDH1
DMDMi399166

Proteomic databases

EPDiP12830
jPOSTiP12830
MaxQBiP12830
PaxDbiP12830
PeptideAtlasiP12830
PRIDEiP12830
ProteomicsDBi52879
TopDownProteomicsiP12830-2 [P12830-2]

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		999
DisGeNETi999
EuPathDBiHostDB:ENSG00000039068.18

GeneCards: human genes, protein and diseases

More...GeneCardsi		CDH1
GeneReviewsiCDH1
HGNCiHGNC:1748 CDH1
HPAiCAB000087
CAB028364
CAB072855
CAB072856
CAB072857
HPA004812
MalaCardsiCDH1
MIMi119580 phenotype
137215 phenotype
167000 phenotype
192090 gene
608089 phenotype
neXtProtiNX_P12830
OpenTargetsiENSG00000039068
Orphaneti1997 Blepharo-cheilo-odontic syndrome
199306 Cleft lip/palate
26106 Hereditary diffuse gastric cancer
PharmGKBiPA26282

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG3594 Eukaryota
ENOG410XQHI LUCA
GeneTreeiENSGT00940000157175
HOGENOMiHOG000231254
HOVERGENiHBG106438
InParanoidiP12830
KOiK05689
OrthoDBi182239at2759
PhylomeDBiP12830
TreeFamiTF316817

Enzyme and pathway databases

ReactomeiR-HSA-1474228 Degradation of the extracellular matrix
R-HSA-198933 Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell
R-HSA-216083 Integrin cell surface interactions
R-HSA-351906 Apoptotic cleavage of cell adhesion proteins
R-HSA-418990 Adherens junctions interactions
R-HSA-5626467 RHO GTPases activate IQGAPs
R-HSA-8876493 InlA-mediated entry of Listeria monocytogenes into host cells
SIGNORiP12830

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		CDH1 human
EvolutionaryTraceiP12830

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		CDH1_(gene)

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		999
PMAP-CutDBiP12830

Protein Ontology

More...PROi		PR:P12830

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000039068 Expressed in 185 organ(s), highest expression level in jejunal mucosa
ExpressionAtlasiP12830 baseline and differential
GenevisibleiP12830 HS

Family and domain databases

Gene3Di4.10.900.10, 1 hit
InterProiView protein in InterPro
IPR039808 Cadherin
IPR002126 Cadherin-like_dom
IPR015919 Cadherin-like_sf
IPR020894 Cadherin_CS
IPR000233 Cadherin_cytoplasmic-dom
IPR014868 Cadherin_pro_dom
IPR027397 Catenin_binding_dom_sf
PANTHERiPTHR24027 PTHR24027, 1 hit
PfamiView protein in Pfam
PF00028 Cadherin, 5 hits
PF01049 Cadherin_C, 1 hit
PF08758 Cadherin_pro, 1 hit
PRINTSiPR00205 CADHERIN
SMARTiView protein in SMART
SM00112 CA, 4 hits
SM01055 Cadherin_pro, 1 hit
SUPFAMiSSF49313 SSF49313, 6 hits
PROSITEiView protein in PROSITE
PS00232 CADHERIN_1, 3 hits
PS50268 CADHERIN_2, 5 hits

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCADH1_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P12830
Secondary accession number(s): A8K1U7
, Q13799, Q14216, Q15855, Q16194, Q4PJ14, Q9UII8
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: July 1, 1993
Last modified: February 13, 2019
This is version 235 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

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

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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