P12830 (CADH1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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:

1. E-Cad/CTF1
2. E-Cad/CTF2
3. E-Cad/CTF3

Gene names

Name:	CDH1
Synonyms:	CDHE, UVO

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	882 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 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.28 Ref.30 Ref.31
Subcellular location	Cell junction. Cell membrane; Single-pass type I membrane protein. Endosome. Golgi apparatus › trans-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.31
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.33 Ref.34
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 germline mutations CDH1 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.46 Ref.51 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.
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 process	Cell adhesion
Cellular component	Cell junction Cell membrane Endosome Golgi apparatus Membrane
Coding sequence diversity	Polymorphism
Disease	Disease mutation
Domain	Repeat Signal Transmembrane Transmembrane helix
Ligand	Calcium Metal-binding
PTM	Cleavage on pair of basic residues Disulfide bond Glycoprotein Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	adherens junction organization Traceable author statement. Source: Reactome cell junction assembly 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: Compara 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: Compara homophilic cell adhesion Non-traceable author statement Ref.14. Source: UniProtKB negative regulation of cell-cell adhesion Inferred from mutant phenotype PubMed 19653274. Source: UniProtKB neuron projection development Inferred from electronic annotation. Source: Compara pituitary gland development Inferred from electronic annotation. Source: Compara positive regulation of transcription factor import into nucleus Inferred from direct assay PubMed 16338932. Source: BHF-UCL positive regulation of transcription, DNA-dependent Inferred from direct assay PubMed 16338932. Source: BHF-UCL protein homooligomerization Inferred from electronic annotation. Source: Compara protein localization to plasma membrane Inferred from direct assay PubMed 17620337. Source: BHF-UCL protein metabolic process Inferred from electronic annotation. Source: Compara regulation of branching involved in salivary gland morphogenesis Inferred from electronic annotation. Source: Compara regulation of cysteine-type endopeptidase activity involved in apoptotic process Inferred from electronic annotation. Source: Compara regulation of immune response Traceable author statement. Source: Reactome regulation of protein localization to cell surface Inferred from electronic annotation. Source: Compara regulation of water loss via skin Inferred from electronic annotation. Source: Compara response to drug Inferred from electronic annotation. Source: Compara response to toxic substance Inferred from electronic annotation. Source: Compara salivary gland cavitation Inferred from electronic annotation. Source: Compara sensory perception of sound Inferred from electronic annotation. Source: Compara synapse assembly Inferred from electronic annotation. Source: Compara tight junction assembly Inferred from electronic annotation. Source: Compara trophectodermal cell differentiation Inferred from electronic annotation. Source: Compara
Cellular_component	Golgi apparatus Inferred from electronic annotation. Source: UniProtKB-SubCell Schmidt-Lanterman incisure Inferred from electronic annotation. Source: Compara 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: Compara axon terminus Inferred from electronic annotation. Source: Compara basolateral plasma membrane Inferred from electronic annotation. Source: Compara catenin complex Inferred from direct assay PubMed 18593713. Source: BHF-UCL cell surface Inferred from electronic annotation. Source: Compara cell-cell adherens junction Inferred from direct assay PubMed 16338932PubMed 20086044. Source: BHF-UCL endosome Inferred from electronic annotation. Source: UniProtKB-SubCell focal adhesion Inferred from direct assay. Source: HPA integral to membrane Inferred from direct assay PubMed 16338932. Source: BHF-UCL internal side of plasma membrane Inferred from direct assay PubMed 20189993. Source: UniProtKB lateral loop Inferred from electronic annotation. Source: Compara lateral plasma membrane Inferred from direct assay PubMed 16338932PubMed 17620337. Source: BHF-UCL node of Ranvier Inferred from electronic annotation. Source: Compara perinuclear region of cytoplasm Inferred from direct assay PubMed 16338932. Source: BHF-UCL trans-Golgi network Inferred from mutant phenotype PubMed 17620337. Source: BHF-UCL
Molecular_function	beta-catenin binding Inferred from direct assay PubMed 17620337. Source: BHF-UCL calcium ion binding Inferred from electronic annotation. Source: Compara cell adhesion molecule binding Non-traceable author statement PubMed 16338932. Source: BHF-UCL
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CDC27	P30260	2	EBI-727477,EBI-994813
CTNNB1	P35222	6	EBI-727477,EBI-491549
FGFR1	P11362	2	EBI-727477,EBI-1028277
PPP1CA	P62136	2	EBI-727477,EBI-357253
PRKD1	Q15139	7	EBI-727477,EBI-1181072
SRC	P12931	2	EBI-727477,EBI-621482
TNS3	Q68CZ2	2	EBI-727477,EBI-1220488

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 22

22

Potential

Propeptide

23 – 154

132

Potential

PRO_0000003715

Chain

155 – 882

728

Cadherin-1

PRO_0000003716

Chain

701 – 882

182

E-Cad/CTF1

PRO_0000236067

Chain

732 – 882

151

E-Cad/CTF2

PRO_0000236068

Chain

751 – 882

132

E-Cad/CTF3

PRO_0000236069

Regions

Topological domain

155 – 709

555

Extracellular Potential

Transmembrane

710 – 730

21

Helical; Potential

Topological domain

731 – 882

152

Cytoplasmic Potential

Domain

155 – 262

108

Cadherin 1

Domain

263 – 375

113

Cadherin 2

Domain

376 – 486

111

Cadherin 3

Domain

487 – 593

107

Cadherin 4

Domain

594 – 697

104

Cadherin 5

Region

758 – 769

12

Required for binding CTNND1 and PSEN1

Region

811 – 882

72

Required for binding alpha, beta and gamma catenins

Compositional bias

838 – 851

14

Ser-rich

Sites

Metal binding

257

1

Calcium 1

Metal binding

257

1

Calcium 2

Metal binding

288

1

Calcium 3

Site

700 – 701

2

Cleavage; by a metalloproteinase

Site

731 – 732

2

Cleavage; by gamma-secretase/PS1

Site

750 – 751

2

Cleavage; by caspase-3

Amino acid modifications

Modified residue

753

1

Phosphotyrosine; by SRC Ref.35

Modified residue

754

1

Phosphotyrosine; by SRC Ref.35

Modified residue

755

1

Phosphotyrosine; by SRC Ref.35

Modified residue

838

1

Phosphoserine By similarity

Modified residue

840

1

Phosphoserine By similarity

Modified residue

846

1

Phosphoserine By similarity

Glycosylation

558

1

N-linked (GlcNAc...) Ref.27

Glycosylation

570

1

N-linked (GlcNAc...) Ref.27

Glycosylation

622

1

N-linked (GlcNAc...) Ref.27

Glycosylation

637

1

N-linked (GlcNAc...) Ref.27

Disulfide bond

163

Interchain Ref.20

Natural variations

Natural variant

72

1

D → N.
Corresponds to variant rs35606263 [ dbSNP | Ensembl ].

VAR_048500

Natural variant

123

1

H → Y in a gastric cancer sample.

VAR_001306

Natural variant

193

1

T → P in a diffuse gastric cancer sample. Ref.42

VAR_001307

Natural variant

244

1

D → G in HDGC. Ref.46

VAR_008712

Natural variant

270

1

S → A May contribute to prostate cancer. Ref.48

VAR_013970

Natural variant

274 – 277

4

Missing Found in gastric carcinoma cell lines.

VAR_001308

Natural variant

282

1

M → I in a breast cancer sample; somatic mutation. Ref.53

VAR_033026

Natural variant

315

1

N → S in lobular breast carcinoma. Ref.40

VAR_001309

Natural variant

336

1

E → D. Ref.45

VAR_001310

Natural variant

340

1

T → 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.47 Ref.50 Ref.52

VAR_013971

Natural variant

370

1

D → A in a diffuse gastric cancer sample. Ref.14

VAR_001311

Natural variant

393

1

I → N.
Corresponds to variant rs34466743 [ dbSNP | Ensembl ].

VAR_048501

Natural variant

400

1

Missing in a gastric carcinoma sample; loss of heterozygosity. Ref.43

VAR_001312

Natural variant

418 – 423

6

Missing in a gastric carcinoma sample.

VAR_001313

Natural variant

463

1

E → Q in a gastric carcinoma sample.

VAR_001314

Natural variant

470

1

T → I. Ref.45

VAR_001315

Natural variant

473

1

V → D in a diffuse gastric cancer sample. Ref.14

VAR_001317

Natural variant

473

1

V → I.
Corresponds to variant rs36087757 [ dbSNP | Ensembl ].

VAR_048502

Natural variant

478

1

L → P. Ref.6
Corresponds to variant rs35520415 [ dbSNP | Ensembl ].

VAR_023357

Natural variant

487

1

V → A in HDGC. Ref.46

VAR_008713

Natural variant

592

1

A → T in a thyroid cancer sample; may play a role in colorectal carcinogenesis. Ref.44 Ref.49
Corresponds to variant rs35187787 [ dbSNP | Ensembl ].

VAR_001318

Natural variant

598

1

R → Q in a gastric cancer sample.

VAR_001319

Natural variant

617

1

A → 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.41 Ref.52
Corresponds to variant rs33935154 [ dbSNP | Ensembl ].

VAR_001320

Natural variant

630

1

L → V.
Corresponds to variant rs2276331 [ dbSNP | Ensembl ].

VAR_021868

Natural variant

634

1

A → 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.52

VAR_055431

Natural variant

695

1

C → R.
Corresponds to variant rs9282655 [ dbSNP | Ensembl ].

VAR_021869

Natural variant

711

1

L → V Detected in an endometrial cancer sample. Ref.41

VAR_001321

Natural variant

777

1

D → N in a breast cancer sample; somatic mutation. Ref.53

VAR_033027

Natural variant

832

1

V → M in HDGC. Ref.6 Ref.51
Corresponds to variant rs35572355 [ dbSNP | Ensembl ].

VAR_023358

Natural variant

838

1

S → G in an ovarian carcinoma sample; somatic mutation; loss of heterozygosity. Ref.41

VAR_001322

Natural variant

880

1

E → K. Ref.6
Corresponds to variant rs34507583 [ dbSNP | Ensembl ].

VAR_023359

Experimental info

Mutagenesis

637

1

N → Q: CDH1 becomes a substrate for ERAD and is retro-translocated from ER to cytoplasm. Ref.27

Mutagenesis

754

1

Y → F: Abolishes binding to CBLL1. Ref.35

Mutagenesis

759 – 761

3

GGG → AAA: Binds to CTNNB1 but abolishes interaction of CTNNB1 with PSEN1. Abolishes gamma-secretase cleavage. Ref.15 Ref.23

Sequence conflict

10

1

A → G in AAA61259. Ref.3

Sequence conflict

29

1

H → L in AAA61259. Ref.3

Sequence conflict

47

1

E → R in AAA61259. Ref.3

Sequence conflict

70 – 71

2

SL → P in AAA61259. Ref.3

Sequence conflict

483

1

A → G in AAA61259. Ref.3

Sequence conflict

530

1

A → R in AAA61259. Ref.3

Sequence conflict

543

1

S → F in CAA79356. Ref.2

Sequence conflict

615

1

I → H in AAA61259. Ref.3

Sequence conflict

634 – 636

3

ASA → RVP in AAA61259. Ref.3

Sequence conflict

868

1

R → P in AAA61259. Ref.3

Sequence conflict

882

1

D → H in AAA61259. Ref.3

Secondary structure

1

.

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882

Helix Strand Turn

Details...

Beta strand

163 – 166

4

Beta strand

169 – 177

9

Helix

181 – 184

4

Beta strand

189 – 195

7

Turn

196 – 198

3

Beta strand

199 – 201

3

Beta strand

204 – 207

4

Turn

209 – 211

3

Beta strand

213 – 216

4

Turn

222 – 224

3

Beta strand

227 – 235

9

Beta strand

241 – 243

3

Beta strand

246 – 253

8

Beta strand

261 – 272

12

Beta strand

280 – 283

4

Turn

292 – 294

3

Beta strand

301 – 309

9

Beta strand

316 – 319

4

Turn

321 – 323

3

Beta strand

325 – 328

4

Turn

335 – 337

3

Beta strand

340 – 348

9

Turn

349 – 353

5

Beta strand

356 – 366

11

Helix

769 – 771

3

Sequences

	Sequence		Length	Mass (Da)
	P12830 [UniParc]. Last modified July 1, 1993. Version 3. Checksum: E427118043A13C67	FASTA	882	97,456
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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]	"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.
[28]	"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.
[29]	"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.
[30]	"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.
[31]	"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.
[32]	"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].
[33]	"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.
[34]	"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.
[35]	"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.
[36]	"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.
[37]	"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.
[38]	"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.
[39]	"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.
[40]	"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.
[41]	"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.
[42]	"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.
[43]	"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.
[44]	"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.
[45]	"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.
[46]	"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.
[47]	"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.
[48]	"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.
[49]	"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.
[50]	"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.
[51]	"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.
[52]	"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.
[53]	"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.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

GeneReviews

NIEHS-SNPs

Wikipedia

E-cadherin entry

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 , 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.

IPI

IPI00025861.

PIR

IJHUCE. S37654.

RefSeq

NP_004351.1. NM_004360.3.

UniGene

Hs.461086.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1O6S	X-ray	1.80	B	156-255	[»]
2O72	X-ray	2.00	A	155-367	[»]
2OMT	X-ray	2.00	B	156-255	[»]
2OMU	X-ray	1.80	B	156-255	[»]
2OMV	X-ray	1.90	B	156-255	[»]
2OMX	X-ray	1.70	B	156-258	[»]
2OMY	X-ray	1.70	B	156-255	[»]
2OMZ	X-ray	1.60	B	156-255	[»]
3FF7	X-ray	1.80	A/B	155-253	[»]
3FF8	X-ray	2.00	A/B	155-254	[»]
3L6X	X-ray	2.40	B	756-773	[»]
3L6Y	X-ray	3.00	B/D/F	756-773	[»]

ProteinModelPortal

P12830.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-477N.

IntAct

P12830. 38 interactions.

MINT

MINT-119105.

STRING

9606.ENSP00000261769.

PTM databases

PhosphoSite

P12830.

Polymorphism databases

DMDM

399166.

Proteomic databases

PaxDb

P12830.

PRIDE

P12830.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000261769; ENSP00000261769; ENSG00000039068.

GeneID

999.

KEGG

hsa:999.

UCSC

uc002ewg.1. human.

Organism-specific databases

CTD

999.

GeneCards

GC16P068771.

HGNC

HGNC:1748. CDH1.

HPA

CAB000087.
CAB028364.
HPA004812.

MIM

137215. phenotype.
167000. phenotype.
192090. gene.
608089. phenotype.

neXtProt

NX_P12830.

Orphanet

26106. Familial gastric cancer.
36273. Gastric linitis plastica.

PharmGKB

PA26282.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG328838.

HOGENOM

HOG000231254.

HOVERGEN

HBG106438.

KO

K05689.

OrthoDB

EOG4GF3DT.

PhylomeDB

P12830.

Enzyme and pathway databases

Pathway_Interaction_DB

a6b1_a6b4_integrin_pathway. a6b1 and a6b4 Integrin signaling.
arf6_traffickingpathway. Arf6 trafficking events.
fgf_pathway. FGF signaling pathway.

Reactome

REACT_111102. Signal Transduction.
REACT_111155. Cell-Cell communication.
REACT_578. Apoptosis.
REACT_6900. Immune System.

Gene expression databases

ArrayExpress

P12830.

Bgee

P12830.

CleanEx

HS_CDH1.

Genevestigator

P12830.

GermOnline

ENSG00000039068. Homo sapiens.

Family and domain databases

Gene3D

2.60.40.60. 6 hits.
4.10.900.10. 1 hit.

InterPro

IPR002126. Cadherin.
IPR015919. Cadherin-like.
IPR020894. Cadherin_CS.
IPR000233. Cadherin_cytoplasmic-dom.
IPR014868. Cadherin_pro_dom.
IPR027397. Catenin_binding_dom.
[Graphical view]

Pfam

PF00028. Cadherin. 5 hits.
PF01049. Cadherin_C. 1 hit.
PF08758. Cadherin_pro. 1 hit.
[Graphical view]

PRINTS

PR00205. CADHERIN.

SMART

SM00112. CA. 4 hits.
SM01055. Cadherin_pro. 1 hit.
[Graphical view]

SUPFAM

SSF49313. Cadherin. 6 hits.

PROSITE

PS00232. CADHERIN_1. 3 hits.
PS50268. CADHERIN_2. 5 hits.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

CDH1. human.

EvolutionaryTrace

P12830.

GenomeRNAi

999.

NextBio

4200.

PMAP-CutDB

P12830.

SOURCE

Search...

Entry information

Entry name

CADH1_HUMAN

Accession

Primary (citable) accession number: P12830
Secondary accession number(s): A8K1U7 , Q13799, Q14216, Q15855, Q16194, Q4PJ14

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	July 1, 1993
Last modified:	May 29, 2013
This is version 174 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.