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Protein

Cadherin-1

Gene

CDH1

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

Functioni

Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. CDH1 is involved in mechanisms regulating cell-cell adhesions, mobility and proliferation of epithelial cells. Has a potent invasive suppressor role. It is a ligand for integrin alpha-E/beta-7.1 Publication
E-Cad/CTF2 promotes non-amyloidogenic degradation of Abeta precursors. Has a strong inhibitory effect on APP C99 and C83 production.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi257Calcium 11
Metal bindingi257Calcium 21
Metal bindingi288Calcium 31

GO - Molecular functioni

  • ankyrin binding Source: BHF-UCL
  • beta-catenin binding Source: BHF-UCL
  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
  • calcium ion binding Source: InterPro
  • cell adhesion molecule binding Source: UniProtKB
  • gamma-catenin binding Source: BHF-UCL
  • glycoprotein binding Source: UniProtKB
  • GTPase activating protein binding Source: UniProtKB

GO - Biological processi

  • adherens junction organization Source: UniProtKB
  • cellular response to indole-3-methanol Source: UniProtKB
  • cellular response to lithium ion Source: UniProtKB
  • establishment of protein localization to plasma membrane Source: UniProtKB
  • extracellular matrix disassembly Source: Reactome
  • extracellular matrix organization Source: Reactome
  • homophilic cell adhesion via plasma membrane adhesion molecules Source: UniProtKB
  • negative regulation of cell-cell adhesion Source: UniProtKB
  • neuron projection development Source: Ensembl
  • pituitary gland development Source: Ensembl
  • positive regulation of transcription, DNA-templated Source: BHF-UCL
  • positive regulation of transcription factor import into nucleus Source: BHF-UCL
  • protein localization to plasma membrane Source: BHF-UCL
  • response to drug Source: Ensembl
  • response to toxic substance Source: Ensembl
  • single organismal cell-cell adhesion Source: BHF-UCL
  • synapse assembly Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000039068-MONOMER.
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.
SIGNORiP12830.

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
Proteomesi
  • UP000005640 Componenti: 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.

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini155 – 709ExtracellularSequence analysisAdd BLAST555
Transmembranei710 – 730HelicalSequence analysisAdd BLAST21
Topological domaini731 – 882CytoplasmicSequence analysisAdd BLAST152

GO - Cellular componenti

  • actin cytoskeleton Source: BHF-UCL
  • aggresome Source: HPA
  • apical junction complex Source: UniProtKB
  • catenin complex Source: BHF-UCL
  • cell-cell adherens junction Source: UniProtKB
  • cell junction Source: UniProtKB
  • cytoplasm Source: HPA
  • cytoplasmic side of plasma membrane Source: UniProtKB
  • endosome Source: UniProtKB-SubCell
  • extracellular exosome Source: UniProtKB
  • extracellular region Source: Reactome
  • flotillin complex Source: UniProtKB
  • focal adhesion Source: HPA
  • integral component of membrane Source: BHF-UCL
  • lamellipodium Source: UniProtKB
  • lateral plasma membrane Source: BHF-UCL
  • perinuclear region of cytoplasm Source: BHF-UCL
  • plasma membrane Source: HPA
  • trans-Golgi network Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Involvement in diseasei

Hereditary diffuse gastric cancer (HDGC)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
Natural variantiVAR_008712244D → G in HDGC. 1 Publication1
Natural variantiVAR_008713487V → A in HDGC. 1 Publication1
Natural variantiVAR_023358832V → M in HDGC. 2 PublicationsCorresponds to variant rs35572355dbSNPEnsembl.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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

Organism-specific databases

DisGeNETi999.
MalaCardsiCDH1.
MIMi137215. phenotype.
167000. phenotype.
608089. phenotype.
OpenTargetsiENSG00000039068.
Orphaneti1991. Cleft lip with or without cleft palate.
26106. Familial gastric cancer.
36273. Gastric linitis plastica.
PharmGKBiPA26282.

Polymorphism and mutation databases

BioMutaiCDH1.
DMDMi399166.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 22Sequence analysisAdd BLAST22
PropeptideiPRO_000000371523 – 154Sequence analysisAdd BLAST132
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
Disulfide bondi163Interchain
Glycosylationi558N-linked (GlcNAc...)1 Publication1
Glycosylationi570N-linked (GlcNAc...)1 Publication1
Glycosylationi622N-linked (GlcNAc...)1 Publication1
Glycosylationi637N-linked (GlcNAc...)1 Publication1
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

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

EPDiP12830.
MaxQBiP12830.
PaxDbiP12830.
PeptideAtlasiP12830.
PRIDEiP12830.
TopDownProteomicsiP12830-2. [P12830-2]

PTM databases

iPTMnetiP12830.
PhosphoSitePlusiP12830.

Miscellaneous databases

PMAP-CutDBP12830.

Expressioni

Tissue specificityi

Non-neural epithelial tissues.

Inductioni

Expression is repressed by MACROD1.1 Publication

Gene expression databases

BgeeiENSG00000039068.
CleanExiHS_CDH1.
ExpressionAtlasiP12830. baseline and differential.
GenevisibleiP12830. HS.

Organism-specific databases

HPAiCAB000087.
CAB028364.
CAB072855.
CAB072856.
CAB072857.
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
CTNNB1P3522211EBI-727477,EBI-491549
EGFRP005333EBI-727477,EBI-297353
FGFR1P113623EBI-727477,EBI-1028277
PPP1CAP621362EBI-727477,EBI-357253
PRKD1Q151397EBI-727477,EBI-1181072
SRCP129312EBI-727477,EBI-621482
TNS3Q68CZ22EBI-727477,EBI-1220488

GO - Molecular functioni

  • ankyrin binding Source: BHF-UCL
  • beta-catenin binding Source: BHF-UCL
  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
  • cell adhesion molecule binding Source: UniProtKB
  • gamma-catenin binding Source: BHF-UCL
  • GTPase activating protein binding Source: UniProtKB

Protein-protein interaction databases

BioGridi107434. 88 interactors.
DIPiDIP-477N.
IntActiP12830. 73 interactors.
MINTiMINT-119105.
STRINGi9606.ENSP00000261769.

Structurei

Secondary structure

1882
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi163 – 166Combined sources4
Beta strandi169 – 177Combined sources9
Helixi181 – 184Combined sources4
Beta strandi189 – 195Combined sources7
Turni196 – 198Combined sources3
Beta strandi199 – 201Combined sources3
Beta strandi204 – 207Combined sources4
Turni209 – 211Combined sources3
Beta strandi213 – 216Combined sources4
Turni222 – 224Combined sources3
Beta strandi227 – 235Combined sources9
Beta strandi241 – 243Combined sources3
Beta strandi246 – 253Combined sources8
Beta strandi261 – 263Combined sources3
Beta strandi265 – 272Combined sources8
Beta strandi279 – 283Combined sources5
Turni292 – 294Combined sources3
Beta strandi301 – 309Combined sources9
Beta strandi317 – 319Combined sources3
Turni321 – 323Combined sources3
Beta strandi325 – 328Combined sources4
Turni335 – 337Combined sources3
Beta strandi340 – 349Combined sources10
Helixi350 – 352Combined sources3
Beta strandi356 – 366Combined sources11
Helixi769 – 771Combined sources3

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...

Miscellaneous databases

EvolutionaryTraceiP12830.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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
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
Compositional biasi838 – 851Ser-richAdd BLAST14

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

eggNOGiKOG3594. Eukaryota.
ENOG410XQHI. LUCA.
GeneTreeiENSGT00760000118906.
HOGENOMiHOG000231254.
HOVERGENiHBG106438.
InParanoidiP12830.
KOiK05689.
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. AlignAdd to basket

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

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

« Hide

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

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

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

Sequence cautioni

The sequence AAA61259 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
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 rs35606263dbSNPEnsembl.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 Publication1
Natural variantiVAR_013970270S → A May contribute to prostate cancer. 1 PublicationCorresponds to variant rs587776399dbSNPEnsembl.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 rs200932258dbSNPEnsembl.1
Natural variantiVAR_001309315N → S in lobular breast carcinoma. 1 Publication1
Natural variantiVAR_001310336E → D.1 PublicationCorresponds to variant rs267606712dbSNPEnsembl.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 rs116093741dbSNPEnsembl.1
Natural variantiVAR_001311370D → A in a diffuse gastric cancer sample. 1 Publication1
Natural variantiVAR_048501393I → N.Corresponds to variant rs34466743dbSNPEnsembl.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_001314463E → Q in a gastric carcinoma sample. 1
Natural variantiVAR_001315470T → I.1 PublicationCorresponds to variant rs370864592dbSNPEnsembl.1
Natural variantiVAR_001317473V → D in a diffuse gastric cancer sample. 1 Publication1
Natural variantiVAR_048502473V → I.Corresponds to variant rs36087757dbSNPEnsembl.1
Natural variantiVAR_023357478L → P.1 PublicationCorresponds to variant rs35520415dbSNPEnsembl.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 rs35187787dbSNPEnsembl.1
Natural variantiVAR_001319598R → Q in a gastric cancer sample. Corresponds to variant rs780759537dbSNPEnsembl.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 rs33935154dbSNPEnsembl.1
Natural variantiVAR_021868630L → V.Corresponds to variant rs2276331dbSNPEnsembl.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 rs121964878dbSNPEnsembl.1
Natural variantiVAR_021869695C → R.Corresponds to variant rs9282655dbSNPEnsembl.1
Natural variantiVAR_001321711L → V Detected in an endometrial cancer sample. 1 PublicationCorresponds to variant rs121964871dbSNPEnsembl.1
Natural variantiVAR_033027777D → N in a breast cancer sample; somatic mutation. 1 PublicationCorresponds to variant rs372989292dbSNPEnsembl.1
Natural variantiVAR_023358832V → M in HDGC. 2 PublicationsCorresponds to variant rs35572355dbSNPEnsembl.1
Natural variantiVAR_001322838S → G in an ovarian carcinoma sample; somatic mutation; loss of heterozygosity. 1 PublicationCorresponds to variant rs121964872dbSNPEnsembl.1
Natural variantiVAR_023359880E → K.1 PublicationCorresponds to variant rs34507583dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_055586380 – 440Missing in isoform 2. 1 PublicationAdd BLAST61

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.

Genome annotation databases

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

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:
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. 88 interactors.
DIPiDIP-477N.
IntActiP12830. 73 interactors.
MINTiMINT-119105.
STRINGi9606.ENSP00000261769.

PTM databases

iPTMnetiP12830.
PhosphoSitePlusiP12830.

Polymorphism and mutation databases

BioMutaiCDH1.
DMDMi399166.

Proteomic databases

EPDiP12830.
MaxQBiP12830.
PaxDbiP12830.
PeptideAtlasiP12830.
PRIDEiP12830.
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

CTDi999.
DisGeNETi999.
GeneCardsiCDH1.
GeneReviewsiCDH1.
HGNCiHGNC:1748. CDH1.
HPAiCAB000087.
CAB028364.
CAB072855.
CAB072856.
CAB072857.
HPA004812.
MalaCardsiCDH1.
MIMi137215. phenotype.
167000. phenotype.
192090. gene.
608089. phenotype.
neXtProtiNX_P12830.
OpenTargetsiENSG00000039068.
Orphaneti1991. Cleft lip with or without cleft palate.
26106. Familial gastric cancer.
36273. Gastric linitis plastica.
PharmGKBiPA26282.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3594. Eukaryota.
ENOG410XQHI. LUCA.
GeneTreeiENSGT00760000118906.
HOGENOMiHOG000231254.
HOVERGENiHBG106438.
InParanoidiP12830.
KOiK05689.
PhylomeDBiP12830.
TreeFamiTF316817.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000039068-MONOMER.
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.
SIGNORiP12830.

Miscellaneous databases

ChiTaRSiCDH1. human.
EvolutionaryTraceiP12830.
GeneWikiiCDH1_(gene).
GenomeRNAii999.
PMAP-CutDBP12830.
PROiP12830.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000039068.
CleanExiHS_CDH1.
ExpressionAtlasiP12830. baseline and differential.
GenevisibleiP12830. HS.

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]
ProtoNetiSearch...

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: November 2, 2016
This is version 211 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.