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P12830 (CADH1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 186. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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:

  1. E-Cad/CTF1
  2. E-Cad/CTF2
  3. E-Cad/CTF3
Gene names
Name:CDH1
Synonyms:CDHE, UVO
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length882 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.25

E-Cad/CTF2 promotes non-amyloidogenic degradation of Abeta precursors. Has a strong inhibitory effect on APP C99 and C83 production. Ref.25

Subunit structure

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. Ref.10 Ref.17 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.29 Ref.31 Ref.32

Subcellular location

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. Ref.4 Ref.21 Ref.24 Ref.32

Tissue specificity

Non-neural epithelial tissues.

Induction

Expression is repressed by MACROD1. Ref.26

Domain

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. Ref.16

Post-translational modification

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. Ref.4 Ref.15 Ref.18

N-glycosylation at Asn-637 is essential for expression, folding and trafficking.

Ubiquitinated by a SCF complex containing SKP2, which requires prior phosphorylation by CK1/CSNK1A1. Ubiquitinated by CBLL1/HAKAI, requires prior phosphorylation at Tyr-754. Ref.34 Ref.35

Involvement in disease

Hereditary diffuse gastric cancer (HDGC) [MIM:137215]: A cancer predisposition syndrome with increased susceptibility to diffuse gastric cancer. Diffuse gastric cancer is a malignant disease characterized by poorly differentiated infiltrating lesions resulting in thickening of the stomach. Malignant tumors start in the stomach, can spread to the esophagus or the small intestine, and can extend through the stomach wall to nearby lymph nodes and organs. It also can metastasize to other parts of the body.
Note: The disease is caused by mutations affecting the gene represented in this entry. Heterozygous CDH1 germline mutations are responsible for familial cases of diffuse gastric cancer. Somatic mutations has also been found in patients with sporadic diffuse gastric cancer and lobular breast cancer. Ref.47 Ref.52

Endometrial cancer (ENDMC) [MIM:608089]: A malignancy of endometrium, the mucous lining of the uterus. Most endometrial cancers are adenocarcinomas, cancers that begin in cells that make and release mucus and other fluids.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.

Ovarian cancer (OC) [MIM:167000]: The term ovarian cancer defines malignancies originating from ovarian tissue. Although many histologic types of ovarian tumors have been described, epithelial ovarian carcinoma is the most common form. Ovarian cancers are often asymptomatic and the recognized signs and symptoms, even of late-stage disease, are vague. Consequently, most patients are diagnosed with advanced disease.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.

Breast cancer, lobular (LBC) [MIM:137215]: A type of breast cancer that begins in the milk-producing glands (lobules) of the breast.
Note: The gene represented in this entry may be involved in disease pathogenesis. Ref.27

Sequence similarities

Contains 5 cadherin domains.

Sequence caution

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

Ontologies

Keywords
   Biological processCell adhesion
   Cellular componentCell junction
Cell membrane
Endosome
Golgi apparatus
Membrane
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
   DomainRepeat
Signal
Transmembrane
Transmembrane helix
   LigandCalcium
Metal-binding
   PTMCleavage on pair of basic residues
Disulfide bond
Glycoprotein
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processadherens junction organization

Traceable author statement. Source: Reactome

apoptotic process

Traceable author statement. Source: Reactome

cell junction assembly

Traceable author statement. Source: Reactome

cell-cell junction organization

Traceable author statement. Source: Reactome

cellular component disassembly involved in execution phase of apoptosis

Traceable author statement. Source: Reactome

cellular response to amino acid stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to indole-3-methanol

Inferred from direct assay PubMed 10868478. Source: UniProtKB

cellular response to lithium ion

Inferred from direct assay PubMed 12937339. Source: UniProtKB

cochlea development

Inferred from electronic annotation. Source: Ensembl

epithelial cell morphogenesis

Inferred from electronic annotation. Source: Ensembl

establishment of protein localization to plasma membrane

Inferred from mutant phenotype PubMed 20859650. Source: UniProt

extracellular matrix disassembly

Traceable author statement. Source: Reactome

extracellular matrix organization

Traceable author statement. Source: Reactome

homophilic cell adhesion

Non-traceable author statement Ref.14. Source: UniProtKB

intestinal epithelial cell development

Inferred from electronic annotation. Source: Ensembl

negative regulation of canonical Wnt signaling pathway

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell-cell adhesion

Inferred from mutant phenotype PubMed 19653274. Source: UniProtKB

negative regulation of epithelial cell proliferation

Inferred from electronic annotation. Source: Ensembl

neuron projection development

Inferred from electronic annotation. Source: Ensembl

pituitary gland development

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription factor import into nucleus

Inferred from direct assay PubMed 16338932. Source: BHF-UCL

positive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 16338932. Source: BHF-UCL

protein homooligomerization

Inferred from electronic annotation. Source: Ensembl

protein localization to plasma membrane

Inferred from direct assay PubMed 17620337. Source: BHF-UCL

protein metabolic process

Inferred from electronic annotation. Source: Ensembl

regulation of branching involved in salivary gland morphogenesis

Inferred from electronic annotation. Source: Ensembl

regulation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from electronic annotation. Source: Ensembl

regulation of immune response

Traceable author statement. Source: Reactome

regulation of protein localization to cell surface

Inferred from electronic annotation. Source: Ensembl

regulation of water loss via skin

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

response to toxic substance

Inferred from electronic annotation. Source: Ensembl

salivary gland cavitation

Inferred from electronic annotation. Source: Ensembl

sensory perception of sound

Inferred from electronic annotation. Source: Ensembl

single organismal cell-cell adhesion

Inferred from direct assay PubMed 16338932PubMed 18593713. Source: BHF-UCL

synapse assembly

Inferred from electronic annotation. Source: Ensembl

tight junction assembly

Inferred from electronic annotation. Source: Ensembl

trophectodermal cell differentiation

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentSchmidt-Lanterman incisure

Inferred from electronic annotation. Source: Ensembl

actin cytoskeleton

Inferred from direct assay PubMed 16338932. Source: BHF-UCL

aggresome

Inferred from direct assay. Source: HPA

apical junction complex

Inferred from direct assay PubMed 10460003. Source: UniProtKB

apical part of cell

Inferred from electronic annotation. Source: Ensembl

axon terminus

Inferred from electronic annotation. Source: Ensembl

basolateral plasma membrane

Inferred from electronic annotation. Source: Ensembl

catenin complex

Inferred from direct assay PubMed 18593713. Source: BHF-UCL

cell junction

Traceable author statement PubMed 17047063. Source: UniProtKB

cell surface

Inferred from electronic annotation. Source: Ensembl

cell-cell adherens junction

Inferred from direct assay PubMed 16338932PubMed 20086044. Source: BHF-UCL

cytoplasm

Inferred from direct assay. Source: HPA

cytoplasmic side of plasma membrane

Inferred from direct assay PubMed 20189993. Source: UniProtKB

endosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular region

Traceable author statement. Source: Reactome

focal adhesion

Inferred from direct assay. Source: HPA

integral component of membrane

Inferred from direct assay PubMed 16338932. Source: BHF-UCL

lateral loop

Inferred from electronic annotation. Source: Ensembl

lateral plasma membrane

Inferred from direct assay PubMed 16338932PubMed 17620337. Source: BHF-UCL

node of Ranvier

Inferred from electronic annotation. Source: Ensembl

perinuclear region of cytoplasm

Inferred from direct assay PubMed 16338932. Source: BHF-UCL

plasma membrane

Inferred from direct assay. Source: HPA

trans-Golgi network

Inferred from mutant phenotype PubMed 17620337. Source: BHF-UCL

   Molecular_functionGTPase activating protein binding

Inferred from physical interaction Ref.31. Source: UniProtKB

ankyrin binding

Inferred from physical interaction PubMed 17620337. Source: BHF-UCL

beta-catenin binding

Inferred from direct assay PubMed 17620337. Source: BHF-UCL

calcium ion binding

Inferred from electronic annotation. Source: Ensembl

cell adhesion molecule binding

Non-traceable author statement PubMed 16338932. Source: BHF-UCL

gamma-catenin binding

Inferred from physical interaction PubMed 1639850. Source: BHF-UCL

glycoprotein binding

Inferred from physical interaction PubMed 23086448. Source: UniProt

protein binding

Inferred from physical interaction PubMed 19038973PubMed 19822757. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Propeptide23 – 154132 Potential
PRO_0000003715
Chain155 – 882728Cadherin-1
PRO_0000003716
Chain701 – 882182E-Cad/CTF1
PRO_0000236067
Chain732 – 882151E-Cad/CTF2
PRO_0000236068
Chain751 – 882132E-Cad/CTF3
PRO_0000236069

Regions

Topological domain155 – 709555Extracellular Potential
Transmembrane710 – 73021Helical; Potential
Topological domain731 – 882152Cytoplasmic Potential
Domain155 – 262108Cadherin 1
Domain263 – 375113Cadherin 2
Domain376 – 486111Cadherin 3
Domain487 – 593107Cadherin 4
Domain594 – 697104Cadherin 5
Region758 – 76912Required for binding CTNND1 and PSEN1
Region811 – 88272Required for binding alpha, beta and gamma catenins
Compositional bias838 – 85114Ser-rich

Sites

Metal binding2571Calcium 1
Metal binding2571Calcium 2
Metal binding2881Calcium 3
Site700 – 7012Cleavage; by a metalloproteinase
Site731 – 7322Cleavage; by gamma-secretase/PS1
Site750 – 7512Cleavage; by caspase-3

Amino acid modifications

Modified residue7531Phosphotyrosine; by SRC Ref.36
Modified residue7541Phosphotyrosine; by SRC Ref.36
Modified residue7551Phosphotyrosine; by SRC Ref.36
Modified residue8381Phosphoserine By similarity
Modified residue8401Phosphoserine By similarity
Modified residue8461Phosphoserine By similarity
Glycosylation5581N-linked (GlcNAc...) Ref.28
Glycosylation5701N-linked (GlcNAc...) Ref.28
Glycosylation6221N-linked (GlcNAc...) Ref.28
Glycosylation6371N-linked (GlcNAc...) Ref.28
Disulfide bond163Interchain Ref.20

Natural variations

Natural variant721D → N.
Corresponds to variant rs35606263 [ dbSNP | Ensembl ].
VAR_048500
Natural variant1231H → Y in a gastric cancer sample.
VAR_001306
Natural variant1931T → P in a diffuse gastric cancer sample. Ref.43
VAR_001307
Natural variant2441D → G in HDGC. Ref.47
VAR_008712
Natural variant2701S → A May contribute to prostate cancer. Ref.49
VAR_013970
Natural variant274 – 2774Missing Found in gastric carcinoma cell lines.
VAR_001308
Natural variant2821M → I in a breast cancer sample; somatic mutation. Ref.54
VAR_033026
Natural variant3151N → S in lobular breast carcinoma. Ref.41
VAR_001309
Natural variant3361E → D. Ref.46
VAR_001310
Natural variant3401T → 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. Ref.48 Ref.51 Ref.53
VAR_013971
Natural variant3701D → A in a diffuse gastric cancer sample. Ref.14
VAR_001311
Natural variant3931I → N.
Corresponds to variant rs34466743 [ dbSNP | Ensembl ].
VAR_048501
Natural variant4001Missing in a gastric carcinoma sample; loss of heterozygosity. Ref.44
VAR_001312
Natural variant418 – 4236Missing in a gastric carcinoma sample.
VAR_001313
Natural variant4631E → Q in a gastric carcinoma sample.
VAR_001314
Natural variant4701T → I. Ref.46
VAR_001315
Natural variant4731V → D in a diffuse gastric cancer sample. Ref.14
VAR_001317
Natural variant4731V → I.
Corresponds to variant rs36087757 [ dbSNP | Ensembl ].
VAR_048502
Natural variant4781L → P. Ref.6
Corresponds to variant rs35520415 [ dbSNP | Ensembl ].
VAR_023357
Natural variant4871V → A in HDGC. Ref.47
VAR_008713
Natural variant5921A → T in a thyroid cancer sample; may play a role in colorectal carcinogenesis. Ref.45 Ref.50
Corresponds to variant rs35187787 [ dbSNP | Ensembl ].
VAR_001318
Natural variant5981R → Q in a gastric cancer sample.
VAR_001319
Natural variant6171A → 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. Ref.6 Ref.42 Ref.53
Corresponds to variant rs33935154 [ dbSNP | Ensembl ].
VAR_001320
Natural variant6301L → V.
Corresponds to variant rs2276331 [ dbSNP | Ensembl ].
VAR_021868
Natural variant6341A → 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. Ref.53
VAR_055431
Natural variant6951C → R.
Corresponds to variant rs9282655 [ dbSNP | Ensembl ].
VAR_021869
Natural variant7111L → V Detected in an endometrial cancer sample. Ref.42
VAR_001321
Natural variant7771D → N in a breast cancer sample; somatic mutation. Ref.54
VAR_033027
Natural variant8321V → M in HDGC. Ref.6 Ref.52
Corresponds to variant rs35572355 [ dbSNP | Ensembl ].
VAR_023358
Natural variant8381S → G in an ovarian carcinoma sample; somatic mutation; loss of heterozygosity. Ref.42
VAR_001322
Natural variant8801E → K. Ref.6
Corresponds to variant rs34507583 [ dbSNP | Ensembl ].
VAR_023359

Experimental info

Mutagenesis6371N → Q: CDH1 becomes a substrate for ERAD and is retro-translocated from ER to cytoplasm. Ref.28
Mutagenesis7541Y → F: Abolishes binding to CBLL1. Ref.36
Mutagenesis759 – 7613GGG → AAA: Binds to CTNNB1 but abolishes interaction of CTNNB1 with PSEN1. Abolishes gamma-secretase cleavage. Ref.15 Ref.23
Sequence conflict101A → G in AAA61259. Ref.3
Sequence conflict291H → L in AAA61259. Ref.3
Sequence conflict471E → R in AAA61259. Ref.3
Sequence conflict70 – 712SL → P in AAA61259. Ref.3
Sequence conflict4831A → G in AAA61259. Ref.3
Sequence conflict5301A → R in AAA61259. Ref.3
Sequence conflict5431S → F in CAA79356. Ref.2
Sequence conflict6151I → H in AAA61259. Ref.3
Sequence conflict634 – 6363ASA → RVP in AAA61259. Ref.3
Sequence conflict8681R → P in AAA61259. Ref.3
Sequence conflict8821D → H in AAA61259. Ref.3

Secondary structure

................................................ 882
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P12830 [UniParc].

Last modified July 1, 1993. Version 3.
Checksum: E427118043A13C67

FASTA88297,456
        10         20         30         40         50         60 
MGPWSRSLSA LLLLLQVSSW LCQEPEPCHP GFDAESYTFT VPRRHLERGR VLGRVNFEDC 

        70         80         90        100        110        120 
TGRQRTAYFS LDTRFKVGTD GVITVKRPLR FHNPQIHFLV YAWDSTYRKF STKVTLNTVG 

       130        140        150        160        170        180 
HHHRPPPHQA SVSGIQAELL TFPNSSPGLR RQKRDWVIPP ISCPENEKGP FPKNLVQIKS 

       190        200        210        220        230        240 
NKDKEGKVFY SITGQGADTP PVGVFIIERE TGWLKVTEPL DRERIATYTL FSHAVSSNGN 

       250        260        270        280        290        300 
AVEDPMEILI TVTDQNDNKP EFTQEVFKGS VMEGALPGTS VMEVTATDAD DDVNTYNAAI 

       310        320        330        340        350        360 
AYTILSQDPE LPDKNMFTIN RNTGVISVVT TGLDRESFPT YTLVVQAADL QGEGLSTTAT 

       370        380        390        400        410        420 
AVITVTDTND NPPIFNPTTY KGQVPENEAN VVITTLKVTD ADAPNTPAWE AVYTILNDDG 

       430        440        450        460        470        480 
GQFVVTTNPV NNDGILKTAK GLDFEAKQQY ILHVAVTNVV PFEVSLTTST ATVTVDVLDV 

       490        500        510        520        530        540 
NEAPIFVPPE KRVEVSEDFG VGQEITSYTA QEPDTFMEQK ITYRIWRDTA NWLEINPDTG 

       550        560        570        580        590        600 
AISTRAELDR EDFEHVKNST YTALIIATDN GSPVATGTGT LLLILSDVND NAPIPEPRTI 

       610        620        630        640        650        660 
FFCERNPKPQ VINIIDADLP PNTSPFTAEL THGASANWTI QYNDPTQESI ILKPKMALEV 

       670        680        690        700        710        720 
GDYKINLKLM DNQNKDQVTT LEVSVCDCEG AAGVCRKAQP VEAGLQIPAI LGILGGILAL 

       730        740        750        760        770        780 
LILILLLLLF LRRRAVVKEP LLPPEDDTRD NVYYYDEEGG GEEDQDFDLS QLHRGLDARP 

       790        800        810        820        830        840 
EVTRNDVAPT LMSVPRYLPR PANPDEIGNF IDENLKAADT DPTAPPYDSL LVFDYEGSGS 

       850        860        870        880 
EAASLSSLNS SESDKDQDYD YLNEWGNRFK KLADMYGGGE DD 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and characterization of the human E-cadherin cDNA."
Bussemakers M.J.G., Mees S.G.M., van Bokhoven A., Debruyne F.M.J., Schalken J.A.
Mol. Biol. Rep. 17:123-128(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Pancreas.
[2]"E-cadherin gene mutations in human gastric carcinoma cell lines."
Oda T., Kanai Y., Oyama T., Yoshiura K., Shimoyama Y., Birchmeier W., Sugimura T., Hirohashi S.
Proc. Natl. Acad. Sci. U.S.A. 91:1858-1862(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT 274-GLY--PRO-277 DEL.
[3]"Molecular cloning of human E-cadherin suggests a novel subdivision of the cadherin superfamily."
Rimm D.L., Morrow J.S.
Biochem. Biophys. Res. Commun. 200:1754-1761(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[4]"Calcium influx triggers the sequential proteolysis of extracellular and cytoplasmic domains of E-cadherin, leading to loss of beta-catenin from cell-cell contacts."
Ito K., Okamoto I., Araki N., Kawano Y., Nakao M., Fujiyama S., Tomita K., Mimori T., Saya H.
Oncogene 18:7080-7090(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 586-591, PROTEOLYTIC PROCESSING, SUBCELLULAR LOCATION.
Tissue: Epidermal carcinoma.
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Hippocampus and Tongue.
[6]NIEHS SNPs program
Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS PRO-478; THR-617; MET-832 AND LYS-880.
[7]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"Transcriptional regulation of the human E-cadherin gene in human prostate cancer cell lines: characterization of the human E-cadherin gene promoter."
Bussemakers M.J.G., Giroldi L.A., van Bokhoven A., Schalken J.A.
Biochem. Biophys. Res. Commun. 203:1284-1290(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16.
[9]"Silencing of the E-cadherin invasion-suppressor gene by CpG methylation in human carcinomas."
Yoshiura K., Kanai Y., Ochiai A., Shimoyama Y., Sugimura T., Hirohashi S.
Proc. Natl. Acad. Sci. U.S.A. 92:7416-7419(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16.
Tissue: Placenta.
[10]"Type I gamma phosphatidylinositol phosphate kinase modulates adherens junction and E-cadherin trafficking via a direct interaction with mu 1B adaptin."
Ling K., Bairstow S.F., Carbonara C., Turbin D.A., Huntsman D.G., Anderson R.A.
J. Cell Biol. 176:343-353(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PIP5K1C.
[11]"Cloning and characterization of the human invasion suppressor gene E-cadherin (CDH1)."
Berx G., Staes K., van Hengel J., Molemans F., Bussemakers M.J.G., van Bokhoven A., van Roy F.
Genomics 26:281-289(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 56-882.
Tissue: Placenta.
[12]"Characterization and chromosomal localization of the gene encoding the human cell adhesion molecule uvomorulin."
Mansouri A., Spurr N., Goodfellow P.N., Kemler R.
Differentiation 38:67-71(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 172-311.
Tissue: Liver.
[13]Frixen U.H.
Submitted (MAR-1990) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 265-392.
Tissue: Liver.
[14]"E-cadherin gene mutations provide clues to diffuse type gastric carcinomas."
Becker K.-F., Atkinson M.J., Reich U., Becker I., Nekarda H., Siewert J.R., Hoefler H.
Cancer Res. 54:3845-3852(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 337-476, VARIANTS ALA-370 AND ASP-473.
[15]"A presenilin-1/gamma-secretase cleavage releases the E-cadherin intracellular domain and regulates disassembly of adherens junctions."
Marambaud P., Shioi J., Serban G., Georgakopoulos A., Sarner S., Nagy V., Baki L., Wen P., Efthimiopoulos S., Shao Z., Wisniewski T., Robakis N.K.
EMBO J. 21:1948-1956(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 701-714 AND 732-742, PROTEOLYTIC PROCESSING BY GAMMA-SECRETASE/PS1 AND A MEMBRANE-BOUND METALLOPROTEINASE, MUTAGENESIS OF 759-GLY--GLY-761.
[16]"Uvomorulin-catenin complex formation is regulated by a specific domain in the cytoplasmic region of the cell adhesion molecule."
Ozawa M., Ringwald M., Kemler R.
Proc. Natl. Acad. Sci. U.S.A. 87:4246-4250(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: DOMAIN CATENIN-BINDING.
[17]"Distinct cadherin-catenin complexes in Ca(2+)-dependent cell-cell adhesion."
Butz S., Kemler R.
FEBS Lett. 355:195-200(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN AN E-CADHERIN/CATENIN ADHESION COMPLEX.
[18]"Cleavage and shedding of E-cadherin after induction of apoptosis."
Steinhusen U., Weiske J., Badock V., Tauber R., Bommert K., Huber O.
J. Biol. Chem. 276:4972-4980(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEOLYTIC PROCESSING.
[19]"Presenilin-1 binds cytoplasmic epithelial cadherin, inhibits cadherin/p120 association, and regulates stability and function of the cadherin/catenin adhesion complex."
Baki L., Marambaud P., Efthimiopoulos S., Georgakopoulos A., Wen P., Cui W., Shioi J., Koo E., Ozawa M., Friedrich V.L., Robakis N.K.
Proc. Natl. Acad. Sci. U.S.A. 98:2381-2386(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PSEN1.
[20]"Disulfide bond formation promotes the cis- and trans-dimerization of the E-cadherin-derived first repeat."
Makagiansar I.T., Nguyen P.D., Ikesue A., Kuczera K., Dentler W., Urbauer J.L., Galeva N., Alterman M., Siahaan T.J.
J. Biol. Chem. 277:16002-16010(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERCHAIN DISULFIDE BOND.
[21]"Human homolog of disc-large is required for adherens junction assembly and differentiation of human intestinal epithelial cells."
Laprise P., Viel A., Rivard N.
J. Biol. Chem. 279:10157-10166(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DLGAP5, SUBCELLULAR LOCATION.
[22]"Novel membrane protein shrew-1 targets to cadherin-mediated junctions in polarized epithelial cells."
Bharti S., Handrow-Metzmacher H., Zickenheiner S., Zeitvogel A., Baumann R., Starzinski-Powitz A.
Mol. Biol. Cell 15:397-406(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AJAP1.
Tissue: Brain.
[23]"Cadherins mediate both the association between PS1 and beta-catenin and the effects of PS1 on beta-catenin stability."
Serban G., Kouchi Z., Baki L., Georgakopoulos A., Litterst C.M., Shioi J., Robakis N.K.
J. Biol. Chem. 280:36007-36012(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH WITH PSEN1 AND CTNNB1, MUTAGENESIS OF 759-GLY--GLY-761.
[24]"Rab11 in recycling endosomes regulates the sorting and basolateral transport of E-cadherin."
Lock J.G., Stow J.L.
Mol. Biol. Cell 16:1744-1755(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[25]"The cytoplasmic sequence of E-cadherin promotes non-amyloidogenic degradation of A beta precursors."
Agiostratidou G., Muros R.M., Shioi J., Marambaud P., Robakis N.K.
J. Neurochem. 96:1182-1188(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF E-CAD/CTF2.
[26]"Induction of the LRP16 gene by estrogen promotes the invasive growth of Ishikawa human endometrial cancer cells through the downregulation of E-cadherin."
Meng Y.G., Han W.-D., Zhao Y.-L., Huang K., Si Y.-L., Wu Z.-Q., Mu Y.-M.
Cell Res. 17:869-880(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[27]"Germline E-cadherin mutations in familial lobular breast cancer."
Masciari S., Larsson N., Senz J., Boyd N., Kaurah P., Kandel M.J., Harris L.N., Pinheiro H.C., Troussard A., Miron P., Tung N., Oliveira C., Collins L., Schnitt S., Garber J.E., Huntsman D.
J. Med. Genet. 44:726-731(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN LBC.
[28]"Unglycosylation at Asn-633 made extracellular domain of E-cadherin folded incorrectly and arrested in endoplasmic reticulum, then sequentially degraded by ERAD."
Zhou F., Su J., Fu L., Yang Y., Zhang L., Wang L., Zhao H., Zhang D., Li Z., Zha X.
Glycoconj. J. 25:727-740(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-558; ASN-570; ASN-622 AND ASN-637, MUTAGENESIS OF ASN-637.
[29]"EPLIN mediates linkage of the cadherin catenin complex to F-actin and stabilizes the circumferential actin belt."
Abe K., Takeichi M.
Proc. Natl. Acad. Sci. U.S.A. 105:13-19(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LIMA1.
[30]"Structure and biochemistry of cadherins and catenins."
Shapiro L., Weis W.I.
Cold Spring Harb. Perspect. Biol. 1:A3053-A3053(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON CADHERINS.
[31]"Armus is a Rac1 effector that inactivates Rab7 and regulates E-cadherin degradation."
Frasa M.A., Maximiano F.C., Smolarczyk K., Francis R.E., Betson M.E., Lozano E., Goldenring J., Seabra M.C., Rak A., Ahmadian M.R., Braga V.M.
Curr. Biol. 20:198-208(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TBC1D2.
[32]"DDR1 regulates the stabilization of cell surface E-cadherin and E-cadherin-mediated cell aggregation."
Eswaramoorthy R., Wang C.K., Chen W.C., Tang M.J., Ho M.L., Hwang C.C., Wang H.M., Wang C.Z.
J. Cell. Physiol. 224:387-397(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH DDR1.
[33]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[34]"Slit-Robo signaling induces malignant transformation through Hakai-mediated E-cadherin degradation during colorectal epithelial cell carcinogenesis."
Zhou W.J., Geng Z.H., Chi S., Zhang W., Niu X.F., Lan S.J., Ma L., Yang X., Wang L.J., Ding Y.Q., Geng J.G.
Cell Res. 21:609-626(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION BY CBLL1.
[35]"Acetylation-dependent regulation of Skp2 function."
Inuzuka H., Gao D., Finley L.W., Yang W., Wan L., Fukushima H., Chin Y.R., Zhai B., Shaik S., Lau A.W., Wang Z., Gygi S.P., Nakayama K., Teruya-Feldstein J., Toker A., Haigis M.C., Pandolfi P.P., Wei W.
Cell 150:179-193(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION BY A SKP2-CONTAINING SCF COMPLEX, PHOSPHORYLATION BY CSNK1A1.
[36]"Structure of a novel phosphotyrosine-binding domain in Hakai that targets E-cadherin."
Mukherjee M., Chow S.Y., Yusoff P., Seetharaman J., Ng C., Sinniah S., Koh X.W., Asgar N.F., Li D., Yim D., Jackson R.A., Yew J., Qian J., Iyu A., Lim Y.P., Zhou X., Sze S.K., Guy G.R., Sivaraman J.
EMBO J. 31:1308-1319(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-753; TYR-754 AND TYR-755, MUTAGENESIS OF TYR-754.
[37]"Structure of internalin, a major invasion protein of Listeria monocytogenes, in complex with its human receptor E-cadherin."
Schubert W.-D., Urbanke C., Ziehm T., Beier V., Machner M.P., Domann E., Wehland J., Chakraborty T., Heinz D.W.
Cell 111:825-836(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 156-255 IN COMPLEX WITH LISTERIA INTERNALIN.
[38]"Mutations of the human E-cadherin (CDH1) gene."
Berx G., Becker K.-F., Hoefler H., van Roy F.
Hum. Mutat. 12:226-237(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON VARIANTS.
[39]"The crystal structure of human E-cadherin domains 1 and 2, and comparison with other cadherins in the context of adhesion mechanism."
Parisini E., Higgins J.M., Liu J.H., Brenner M.B., Wang J.H.
J. Mol. Biol. 373:401-411(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 155-367, CALCIUM-BINDING SITES.
[40]"Structure of natural killer cell receptor KLRG1 bound to E-cadherin reveals basis for MHC-independent missing self recognition."
Li Y., Hofmann M., Wang Q., Teng L., Chlewicki L.K., Pircher H., Mariuzza R.A.
Immunity 31:35-46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 155-253 IN COMPLEX WITH KLRG1.
[41]"Point mutation of the E-cadherin gene in invasive lobular carcinoma of the breast."
Kanai Y., Oda T., Tsuda H., Ochiai A., Hirohashi S.
Jpn. J. Cancer Res. 85:1035-1039(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LOBULAR BREAST CARCINOMA SER-315.
[42]"Mutations of the E-cadherin gene in human gynecologic cancers."
Risinger J.I., Berchuck A., Kohler M.F., Boyd J.
Nat. Genet. 7:98-102(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS THR-617 AND VAL-711, VARIANT OVARIAN CANCER GLY-838.
[43]"E-cadherin gene mutations in signet ring cell carcinoma of the stomach."
Muta H., Noguchi M., Kanai Y., Ochiai A., Nawata H., Hirohashi S.
Jpn. J. Cancer Res. 87:843-848(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PRO-193.
[44]"Inactivation of the E-cadherin gene in primary gastric carcinomas and gastric carcinoma cell lines."
Tamura G., Sakata K., Nishizuka S., Maesawa C., Suzuki Y., Iwaya T., Terashima M., Saito K., Satodate R.
Jpn. J. Cancer Res. 87:1153-1159(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ASP-400 DEL AND 418-ASP--PHE-423 DEL.
[45]"E-cadherin gene alterations are rare events in thyroid tumors."
Soares P., Berx G., van Roy F., Sobrinho-Simoes M.
Int. J. Cancer 70:32-38(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT THYROID CANCER THR-592.
[46]"E-cadherin germline mutations in familial gastric cancer."
Guilford P.J., Hopkins J.B.W., Harraway J., McLeod M., McLeod N., Harawira P., Taite H., Scoular R., Miller A., Reeve A.E.
Nature 392:402-405(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ASP-336 AND ILE-470.
[47]"Germline mutations of E-cadherin gene in Korean familial gastric cancer patients."
Yoon K.-A., Ku J.-L., Yang H.-K., Kim W.H., Park S.Y., Park J.-G.
J. Hum. Genet. 44:177-180(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HDGC GLY-244 AND ALA-487.
[48]"The E-cadherin gene (CDH1) variants T340A and L599V in gastric and colorectal cancer patients in Korea."
Kim H.C., Wheeler J.M.D., Kim J.C., Ilyas M., Beck N.E., Kim B.S., Park K.C., Bodmer W.F.
Gut 47:262-267(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ALA-340.
[49]"Association of E-cadherin germ-line alterations with prostate cancer."
Ikonen T., Matikainen M., Mononen N., Hyytinen E.R., Helin H.J., Tommola S., Tammela T.L., Pukkala E., Schleutker J., Kallioniemi O.-P., Koivisto P.A.
Clin. Cancer Res. 7:3465-3471(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ALA-270.
[50]"A germline E-cadherin mutation in a family with gastric and colon cancer."
Salahshor S., Hou H., Diep C.B., Loukola A., Zhang H., Liu T., Chen J., Iselius L., Rubio C., Lothe R.A., Aaltonen L., Sun X.F., Lindmark G., Lindblom A.
Int. J. Mol. Med. 8:439-443(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT THR-592.
[51]"Screening E-cadherin in gastric cancer families reveals germline mutations only in hereditary diffuse gastric cancer kindred."
Oliveira C., Bordin M.C., Grehan N., Huntsman D., Suriano G., Machado J.C., Kiviluoto T., Aaltonen L., Jackson C.E., Seruca R., Caldas C.
Hum. Mutat. 19:510-517(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ALA-340.
[52]"E-cadherin gene variants in gastric cancer families whose probands are diagnosed with diffuse gastric cancer."
Yabuta T., Shinmura K., Tani M., Yamaguchi S., Yoshimura K., Katai H., Nakajima T., Mochiki E., Tsujinaka T., Takami M., Hirose K., Yamaguchi A., Takenoshita S., Yokota J.
Int. J. Cancer 101:434-441(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HDGC MET-832.
[53]"Identification of CDH1 germline missense mutations associated with functional inactivation of the E-cadherin protein in young gastric cancer probands."
Suriano G., Oliveira C., Ferreira P., Machado J.C., Bordin M.C., De Wever O., Bruyneel E.A., Moguilevsky N., Grehan N., Porter T.R., Richards F.M., Hruban R.H., Roviello F., Huntsman D., Mareel M., Carneiro F., Caldas C., Seruca R.
Hum. Mol. Genet. 12:575-582(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS THR-617 AND VAL-634, CHARACTERIZATION OF VARIANTS ALA-340; THR-617 AND VAL-634.
[54]"Somatic sequence alterations in twenty-one genes selected by expression profile analysis of breast carcinomas."
Chanock S.J., Burdett L., Yeager M., Llaca V., Langeroed A., Presswalla S., Kaaresen R., Strausberg R.L., Gerhard D.S., Kristensen V., Perou C.M., Boerresen-Dale A.-L.
Breast Cancer Res. 9:R5-R5(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ILE-282 AND ASN-777.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z13009 mRNA. Translation: CAA78353.1.
Z18923 mRNA. Translation: CAA79356.1.
L08599 mRNA. Translation: AAA61259.1. Frameshift.
AK290012 mRNA. Translation: BAF82701.1.
AK312551 mRNA. Translation: BAG35448.1.
DQ090940 Genomic DNA. Translation: AAY68225.1.
CH471092 Genomic DNA. Translation: EAW83243.1.
L34545 Genomic DNA. Translation: AAA21764.1.
D49685 Genomic DNA. Translation: BAA08537.1.
Z35402 expand/collapse EMBL AC list , 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.
CCDSCCDS10869.1.
PIRIJHUCE. S37654.
RefSeqNP_004351.1. NM_004360.3.
UniGeneHs.461086.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP12830.
SMRP12830. Positions 155-690, 782-875.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107434. 97 interactions.
DIPDIP-477N.
IntActP12830. 43 interactions.
MINTMINT-119105.
STRING9606.ENSP00000261769.

PTM databases

PhosphoSiteP12830.

Polymorphism databases

DMDM399166.

Proteomic databases

MaxQBP12830.
PaxDbP12830.
PRIDEP12830.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000261769; ENSP00000261769; ENSG00000039068.
GeneID999.
KEGGhsa:999.
UCSCuc002ewg.1. human.

Organism-specific databases

CTD999.
GeneCardsGC16P068771.
GeneReviewsCDH1.
HGNCHGNC:1748. CDH1.
HPACAB000087.
CAB028364.
HPA004812.
MIM137215. phenotype.
167000. phenotype.
192090. gene.
608089. phenotype.
neXtProtNX_P12830.
Orphanet1991. Cleft lip with or without cleft palate.
26106. Familial gastric cancer.
36273. Gastric linitis plastica.
PharmGKBPA26282.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG328838.
HOGENOMHOG000231254.
HOVERGENHBG106438.
KOK05689.
OMADFGVGQE.
OrthoDBEOG7PS1DS.
PhylomeDBP12830.
TreeFamTF316817.

Enzyme and pathway databases

ReactomeREACT_111155. Cell-Cell communication.
REACT_118779. Extracellular matrix organization.
REACT_578. Apoptosis.
REACT_6900. Immune System.

Gene expression databases

ArrayExpressP12830.
BgeeP12830.
CleanExHS_CDH1.
GenevestigatorP12830.

Family and domain databases

Gene3D2.60.40.60. 6 hits.
4.10.900.10. 1 hit.
InterProIPR002126. Cadherin.
IPR015919. Cadherin-like.
IPR020894. Cadherin_CS.
IPR000233. Cadherin_cytoplasmic-dom.
IPR014868. Cadherin_pro_dom.
IPR027397. Catenin_binding_dom.
[Graphical view]
PfamPF00028. Cadherin. 5 hits.
PF01049. Cadherin_C. 1 hit.
PF08758. Cadherin_pro. 1 hit.
[Graphical view]
PRINTSPR00205. CADHERIN.
SMARTSM00112. CA. 4 hits.
SM01055. Cadherin_pro. 1 hit.
[Graphical view]
SUPFAMSSF49313. SSF49313. 6 hits.
PROSITEPS00232. CADHERIN_1. 3 hits.
PS50268. CADHERIN_2. 5 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCDH1. human.
EvolutionaryTraceP12830.
GeneWikiCDH1_(gene).
GenomeRNAi999.
NextBio4200.
PMAP-CutDBP12830.
PROP12830.
SOURCESearch...

Entry information

Entry nameCADH1_HUMAN
AccessionPrimary (citable) accession number: P12830
Secondary accession number(s): A8K1U7 expand/collapse secondary AC list , Q13799, Q14216, Q15855, Q16194, Q4PJ14
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: July 1, 1993
Last modified: July 9, 2014
This is version 186 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries