Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P12830 (CADH1_HUMAN)

Last modified June 16, 2009. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Cadherin-1
Alternative name(s):
    Epithelial cadherin
      Short name=E-cadherin
    Uvomorulin
    CAM 120/80
    CD_antigen=CD324
Cleaved into the following 3 chains:
    1- Recommended name:
            E-Cad/CTF1
    2- Recommended name:
            E-Cad/CTF2
    3- Recommended name:
            E-Cad/CTF3
Gene names
Name: CDH1
Synonyms: CDHE, UVO
OrganismHomo sapiens (Human)
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.21

E-Cad/CTF2 promotes non-amyloidogenic degradation of Abeta precursors. Has a strong inhibitory effect on APP C99 and C83 production. Ref.21

Subunit structure

Homodimer; disulfide-linked. Interacts directly, via the cytoplasmic domain, with CTNNB1 or JUP to form the PSEN1/cadherin/catenin adhesion complex which connects to the actin skeleton through the actin binding of alpha-catenin. Interaction with PSEN1, cleaves CDH1 resulting in the disassociation of cadherin-based adherens junctions (CAJs). Interacts with AJAP1, CTNND1 and DLGAP5. Ref.16 Ref.17 Ref.18 Ref.19

Subcellular location

Cell junction. Cell membrane; Single-pass type I membrane protein. 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. Ref.18 Ref.4

Tissue specificity

Non-neural epithelial tissues.

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 disaaaembly of adherens junctions. Ref.4 Ref.12 Ref.15

Involvement in disease

Defects in CDH1 are involved in dysfunction of the cell-cell adhesion system, triggering cancer invasion (gastric, breast, ovary, endometrium and thyroid) and metastasis.

Defects in CDH1 are a cause of gastric cancer [MIM:137215]; also known as hereditary familial diffuse gastric cancer (HDGC).

Defects in CDH1 are a cause of susceptibility to endometrial cancer [MIM:608089].

Defects in CDH1 are associated with ovarian cancer [MIM:167000]. Ovarian cancer is the leading cause of death from gynecologic malignancy. It is characterized by advanced presentation with loco-regional dissemination in the peritoneal cavity and the rare incidence of visceral metastases. These typical features relate to the biology of the disease, which is a principal determinant of outcome.

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.

Binary interactions

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 – 73021 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

Site700 – 7012Cleavage; by a metalloproteinase
Site731 – 7322Cleavage; by gamma-secretase/PS1
Site750 – 7512Cleavage; by caspase-3

Amino acid modifications

Modified residue8381Phosphoserine By similarity
Modified residue8401Phosphoserine By similarity
Modified residue8461Phosphoserine By similarity
Glycosylation5581N-linked (GlcNAc...) Potential
Glycosylation6371N-linked (GlcNAc...) Potential
Disulfide bond163Interchain Ref.17

Natural variations

Natural variant721D → N: dbSNP rs35606263.
VAR_048500
Natural variant1231H → Y in diffuse gastric cancer.
VAR_001306
Natural variant1931T → P in diffuse gastric cancer. Ref.26
VAR_001307
Natural variant2441D → G in HDGC. Ref.30
VAR_008712
Natural variant2701S → A May contribute to prostate cancer. Ref.32
VAR_013970
Natural variant274 – 2774Missing in gastric adenocarcinoma. Ref.2
VAR_001308
Natural variant2821M → I in a breast cancer sample; somatic mutation. Ref.37
VAR_033026
Natural variant3151N → S in lobular breast carcinoma. Ref.24
VAR_001309
Natural variant3361E → D Ref.29
VAR_001310
Natural variant3401T → A in HDGC and colorectal cancer; cells exhibited decreased aggregation increased invasiveness and non-uniform migration in vitro compared to cells transfected with wild-type sequence.
VAR_013971
Natural variant3701D → A in diffuse gastric cancer. Ref.11
VAR_001311
Natural variant3931I → N: dbSNP rs34466743.
VAR_048501
Natural variant4001Missing in gastric carcinoma; loss of heterozygosity. Ref.27
VAR_001312
Natural variant418 – 4236Missing in gastric carcinoma. Ref.27
VAR_001313
Natural variant4631E → Q in diffuse gastric cancer.
VAR_001314
Natural variant4701T → I Ref.29
VAR_001315
Natural variant4731V → D in diffuse gastric cancer. Ref.11
VAR_001317
Natural variant4731V → I: dbSNP rs36087757. Ref.11
VAR_048502
Natural variant4781L → P: dbSNP rs35520415.
VAR_023357
Natural variant4871V → A in HDGC. Ref.30
VAR_008713
Natural variant5921A → T in thyroid cancer; may play a role in colorectal carcinogenesis. dbSNP rs35187787. Ref.28 Ref.33
VAR_001318
Natural variant5981R → Q in diffuse gastric cancer.
VAR_001319
Natural variant6171A → T in endometrial cancer; loss of heterozygosity; also found as a polymorphism; cells exhibited an intermediate phenotype concerning aggregation invasiveness and migration in vitro compared to cells transfected with wild-type sequence. dbSNP rs33935154. Ref.5 Ref.25
VAR_001320
Natural variant6301L → V: dbSNP rs2276331.
VAR_021868
Natural variant6341A → V in gastric cancer; cells exhibited decreased aggregation increased invasiveness and non-uniform migration in vitro compared to cells transfected with wild-type sequence.
VAR_055431
Natural variant6951C → R: dbSNP rs9282655.
VAR_021869
Natural variant7111L → V in endometrial cancer. Ref.25
VAR_001321
Natural variant7771D → N in a breast cancer sample; somatic mutation. Ref.37
VAR_033027
Natural variant8321V → M in HDGC. dbSNP rs35572355.
VAR_023358
Natural variant8381S → G in ovarian cancer; somatic mutation; loss of heterozygosity.
VAR_001322
Natural variant8801E → K: dbSNP rs34507583.
VAR_023359

Experimental info

Mutagenesis759 – 7613GGG → AAA: Binds to CTNNB1 but abolishes formation of the PSEN1/CTNNB1 complex; when associated with CTNNB1 D-431. Abolishes binding PSEN1. Abolishes gamma-secretase cleavage. Ref.12 Ref.20
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
P12830-1 [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

[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: 8459805] [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: 8127895] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT GASTRIC ADENOCARCINOMA 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: 8185635] [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: 10597309] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 586-591, PROTEOLYTIC PROCESSING, SUBCELLULAR LOCATION.
Tissue: Epidermal carcinoma.
[5]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.
[6]"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: 8093045] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16.
[7]"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: 7543680] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16.
Tissue: Placenta.
[8]"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: 7601454] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 56-882.
Tissue: Placenta.
[9]"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: 3263290] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 172-311.
Tissue: Liver.
[10]Frixen U.H.
Submitted (MAR-1990) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 265-392.
Tissue: Liver.
[11]"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: 8033105] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 337-476, VARIANTS DIFFUSE GASTRIC CANCER ALA-370 AND ASP-473.
[12]"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: 11953314] [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.
[13]"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: 2349235] [Abstract]
Cited for: DOMAIN CATENIN BINDING.
[14]"Presenilin-1 forms complexes with the cadherin/catenin cell-cell adhesion system and is recruited to intercellular and synaptic contacts."
Georgakopoulos A., Marambaud P., Efthimiopoulos S., Shioi J., Cui W., Li H.-C., Schutte M., Gordon R., Holstein G.R., Martinelli G., Mehta P., Friedrich V.L. Jr., Robakis N.K.
Mol. Cell 4:893-902(1999) [PubMed: 10635315] [Abstract]
Cited for: COMPONENT OF THE PSEN1/E-CADHERIN/CATENIN ADHESION COMPLEX WITH PSEN1; CDH1; CTNNA1 AND CTNNB1/CTNND1.
[15]"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: 11076937] [Abstract]
Cited for: PROTEOLYTIC PROCESSING.
[16]"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: 11226248] [Abstract]
Cited for: INTERACTION WITH PSEN1.
[17]"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: 11856755] [Abstract]
Cited for: INTERCHAIN DISULFIDE BOND.
[18]"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: 14699157] [Abstract]
Cited for: INTERACTION WITH DLGAP5, SUBCELLULAR LOCATION.
[19]"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: 14595118] [Abstract]
Cited for: INTERACTION WITH AJAP1.
Tissue: Brain.
[20]"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: 16126725] [Abstract]
Cited for: COMPONENT OF PSEN1/CATENIN/CADHERIN COMPLEX WITH PSEN1; CDH1 AND CTNNB1, MUTAGENESIS OF 759-GLY--GLY-761.
[21]"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: 16417575] [Abstract]
Cited for: FUNCTION OF E-CAD/CTF2.
[22]"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: 12526809] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 156-255 IN COMPLEX WITH LISTERIA INTERNALIN.
[23]"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: 9744472] [Abstract]
Cited for: REVIEW ON VARIANTS.
[24]"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: 7961105] [Abstract]
Cited for: VARIANT LOBULAR BREAST CARCINOMA SER-315.
[25]"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: 8075649] [Abstract]
Cited for: VARIANTS ENDOMETRIAL CANCER THR-617 AND VAL-711, VARIANT OVARIAN CANCER GLY-838.
[26]"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: 8797891] [Abstract]
Cited for: VARIANT DIFFUSE GASTRIC CANCER PRO-193.
[27]"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: 9045944] [Abstract]
Cited for: VARIANTS GASTRIC CARCINOMA ASP-400 DEL AND 418-ASP--PHE-423 DEL.
[28]"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: 8985087] [Abstract]
Cited for: VARIANT THYROID CANCER THR-592.
[29]"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: 9537325] [Abstract]
Cited for: VARIANTS ASP-336 AND ILE-470.
[30]"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: 10319582] [Abstract]
Cited for: VARIANTS HDGC GLY-244 AND ALA-487.
[31]"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: 10896919] [Abstract]
Cited for: VARIANT COLORECTAL CANCER ALA-340.
[32]"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: 11705864] [Abstract]
Cited for: VARIANT ALA-270.
[33]"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: 11562785] [Abstract]
Cited for: VARIANT THR-592.
[34]"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: 11968083] [Abstract]
Cited for: VARIANT HDGC ALA-340.
[35]"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: 12216071] [Abstract]
Cited for: VARIANT HDGC MET-832.
[36]"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: 12588804] [Abstract]
Cited for: VARIANTS GASTRIC CANCER THR-617 AND VAL-634, CHARACTERIZATION OF VARIANTS GASTRIC CANCER ALA-340; THR-617 AND VAL-634.
[37]"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: 17224074] [Abstract]
Cited for: VARIANTS ILE-282 AND ASN-777.
+Additional computationally mapped references.

Cross-references

Sequence databases

Z13009 mRNA. Translation: CAA78353.1.
Z18923 mRNA. Translation: CAA79356.1.
L08599 mRNA. Translation: AAA61259.1. Frameshift.
DQ090940 Genomic DNA. Translation: AAY68225.1.
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.
IPIIPI00025861.
PIRIJHUCE. S37654.
RefSeqNP_004351.1.
UniGeneHs.461086

3D structure databases

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-ray1.70B156-255[»]
2OMZX-ray1.60B156-255[»]
SMRP12830. Positions 802-877.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:477N.
IntActP12830. 30 interactions.

PTM databases

PhosphoSiteP12830.

Proteomic databases

PRIDEP12830.

Genome annotation databases

EnsemblENSG00000039068. Homo sapiens. [Contig view]
GeneID999.
KEGGhsa:999.
NMPDRfig|9606.3.peg.12460.

Organism-specific databases

GeneCardsGC16P067328.
H-InvDBHIX0038521.
HGNCHGNC:1748. CDH1.
HPACAB000087.
HPA004812.
MIM137215. phenotype.
167000. phenotype.
192090. gene.
608089. phenotype.
Orphanet26106. Gastric cancer, familial.
PharmGKBPA26282.
GenAtlasSearch...

Phylogenomic databases

HOVERGENP12830.

Enzyme and pathway databases

Pathway_Interaction_DBa6b1_a6b4_integrin_pathway. a6b1 and a6b4 Integrin signaling.
arf6_traffickingpathway. Arf6 trafficking events.
fgf_pathway. FGF signaling pathway.
ReactomeREACT_13552. Integrin cell surface interactions.
REACT_578. Apoptosis.
REACT_6900. Signaling in Immune system.

Gene expression databases

ArrayExpressP12830.
BgeeP12830.
CleanExHS_CDH1.
GermOnlineENSG00000039068. Homo sapiens.

Family and domain databases

InterProIPR002126. Cadherin.
IPR000233. Cadherin_C_term.
IPR014868. Cadherin_pro.
[Graphical view]
Gene3DG3DSA:2.60.40.60. Cadherin. 4 hits.
PfamPF00028. Cadherin. 5 hits.
PF01049. Cadherin_C. 1 hit.
PF08758. Cadherin_pro. 1 hit.
[Graphical view]
PRINTSPR00205. CADHERIN.
SMARTSM00112. CA. 4 hits.
[Graphical view]
PROSITEPS00232. CADHERIN_1. 3 hits.
PS50268. CADHERIN_2. 5 hits.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio4200.
PMAP-CutDBP12830.
SOURCESearch...

Entry information

Entry nameCADH1_HUMAN
AccessionPrimary (citable) accession number: P12830
Secondary accession number(s): Q13799 expand/collapse secondary AC list , Q14216, Q15855, Q16194, Q4PJ14
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: July 1, 1993
Last modified: June 16, 2009
This is version 125 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human cell differentiation molecules

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

Human chromosome 16

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents