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UniProtKB - P12830 (CADH1_HUMAN)

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Protein

Cadherin-1

Gene

CDH1

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

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

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 Source: BHF-UCL
  • calcium ion binding Source: InterPro
  • cell adhesion molecule binding Source: UniProtKB
  • gamma-catenin binding Source: BHF-UCL
  • GTPase activating protein binding Source: UniProtKB
  • identical protein binding Source: IntAct
View the complete GO annotation on QuickGO ...

GO - Biological processi

  • adherens junction organization Source: UniProtKB
  • cell-cell adhesion Source: BHF-UCL
  • cellular response to indole-3-methanol Source: UniProtKB
  • cellular response to lithium ion Source: UniProtKB
  • entry of bacterium into host cell 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 protein import into nucleus Source: BHF-UCL
  • positive regulation of transcription, DNA-templated Source: BHF-UCL
  • protein localization to plasma membrane Source: BHF-UCL
  • response to toxic substance Source: Ensembl
  • synapse assembly Source: Ensembl
View the complete GO annotation on QuickGO ...

Keywordsi

Biological processCell adhesion
LigandCalcium, Metal-binding

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

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:
E-Cad/CTF1
E-Cad/CTF2
E-Cad/CTF3
Gene namesi
Name:CDH1
Synonyms:CDHE, UVO
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 16

Organism-specific databases

EuPathDBiHostDB:ENSG00000039068.18
HGNCiHGNC:1748 CDH1
MIMi192090 gene
neXtProtiNX_P12830

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
Topological domaini155 – 709ExtracellularSequence analysisAdd BLAST555
Transmembranei710 – 730HelicalSequence analysisAdd BLAST21
Topological domaini731 – 882CytoplasmicSequence analysisAdd BLAST152

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 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
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

DisGeNETi999
GeneReviewsiCDH1
MalaCardsiCDH1
MIMi119580 phenotype
137215 phenotype
167000 phenotype
608089 phenotype
OpenTargetsiENSG00000039068
Orphaneti1991 Cleft lip with or without cleft palate
26106 Familial gastric cancer
36273 Gastric linitis plastica
PharmGKBiPA26282

Chemistry databases

ChEMBLiCHEMBL2321609

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...) asparagine1 Publication1
Glycosylationi570N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi622N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi637N-linked (GlcNAc...) asparagine1 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
ProteomicsDBi52879
TopDownProteomicsiP12830-2 [P12830-2]

PTM databases

iPTMnetiP12830
PhosphoSitePlusiP12830

Miscellaneous databases

PMAP-CutDBiP12830

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 (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

Binary interactionsi

Show more details

GO - Molecular functioni

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

Protein-protein interaction databases

BioGridi107434, 629 interactors
CORUMiP12830
DIPiDIP-477N
ELMiP12830
IntActiP12830, 83 interactors
MINTiP12830
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

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

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3594 Eukaryota
ENOG410XQHI LUCA
GeneTreeiENSGT00760000118906
HOGENOMiHOG000231254
HOVERGENiHBG106438
InParanoidiP12830
KOiK05689
PhylomeDBiP12830
TreeFamiTF316817

Family and domain databases

Gene3Di4.10.900.10, 1 hit
InterProiView protein in InterPro
IPR002126 Cadherin
IPR015919 Cadherin-like
IPR020894 Cadherin_CS
IPR000233 Cadherin_cytoplasmic-dom
IPR014868 Cadherin_pro_dom
IPR027397 Catenin_binding_dom_sf
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

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 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
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

Similar proteinsi

Entry informationi

Entry nameiCADH1_HUMAN
AccessioniPrimary (citable) accession number: P12830
Secondary accession number(s): A8K1U7
, Q13799, Q14216, Q15855, Q16194, Q4PJ14, Q9UII8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: July 1, 1993
Last modified: July 18, 2018
This is version 229 of the entry and version 3 of the sequence. See 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

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