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UniProtKB - Q14126 (DSG2_HUMAN)

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Protein

Desmoglein-2

Gene

DSG2

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

Functioni

Component of intercellular desmosome junctions. Involved in the interaction of plaque proteins and intermediate filaments mediating cell-cell adhesion.

GO - Molecular functioni

  • calcium ion binding Source: InterPro
  • cell adhesion molecule binding Source: BHF-UCL
  • cell adhesive protein binding involved in bundle of His cell-Purkinje myocyte communication Source: BHF-UCL
Complete GO annotation...

GO - Biological processi

  • bundle of His cell-Purkinje myocyte adhesion involved in cell communication Source: BHF-UCL
  • cell adhesion Source: UniProtKB
  • cornification Source: Reactome
  • desmosome organization Source: BHF-UCL
  • homophilic cell adhesion via plasma membrane adhesion molecules Source: BHF-UCL
  • keratinization Source: Reactome
  • maternal process involved in female pregnancy Source: Ensembl
  • Purkinje myocyte development Source: BHF-UCL
  • regulation of heart rate by cardiac conduction Source: BHF-UCL
  • regulation of ventricular cardiac muscle cell action potential Source: BHF-UCL
  • response to progesterone Source: Ensembl
Complete GO annotation...

Keywordsi

Biological processCell adhesion
LigandCalcium, Metal-binding

Enzyme and pathway databases

ReactomeiR-HSA-351906. Apoptotic cleavage of cell adhesion proteins.
R-HSA-6805567. Keratinization.
R-HSA-6809371. Formation of the cornified envelope.

Names & Taxonomyi

Protein namesi
Recommended name:
Desmoglein-2
Alternative name(s):
Cadherin family member 5
HDGC
Gene namesi
Name:DSG2
Synonyms:CDHF5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 18

Organism-specific databases

HGNCiHGNC:3049. DSG2.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini50 – 609ExtracellularSequence analysisAdd BLAST560
Transmembranei610 – 634HelicalSequence analysisAdd BLAST25
Topological domaini635 – 1118CytoplasmicSequence analysisAdd BLAST484

GO - Cellular componenti

  • apical plasma membrane Source: Ensembl
  • cell-cell junction Source: ProtInc
  • cell surface Source: UniProtKB
  • cornified envelope Source: Reactome
  • desmosome Source: BHF-UCL
  • extracellular exosome Source: UniProtKB
  • integral component of membrane Source: UniProtKB-KW
  • intercalated disc Source: BHF-UCL
  • lateral plasma membrane Source: Ensembl
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane

Pathology & Biotechi

Involvement in diseasei

Arrhythmogenic right ventricular dysplasia, familial, 10 (ARVD10)4 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA congenital heart disease characterized by infiltration of adipose and fibrous tissue into the right ventricle and loss of myocardial cells, resulting in ventricular and supraventricular arrhythmias.
See also OMIM:610193
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02936546R → Q in ARVD10. 2 PublicationsCorresponds to variant dbSNP:rs121913008Ensembl.1
Natural variantiVAR_02936649R → H in ARVD10. 4 PublicationsCorresponds to variant dbSNP:rs121913006Ensembl.1
Natural variantiVAR_06238756V → M Associated with CMD1BB and ARVD10 although it may not be sufficient by itself to result in cardiomyopathy. 2 PublicationsCorresponds to variant dbSNP:rs121913013Ensembl.1
Natural variantiVAR_065686335T → A in ARVD10. 1 PublicationCorresponds to variant dbSNP:rs191564916Ensembl.1
Natural variantiVAR_029367507C → Y in ARVD10. 2 PublicationsCorresponds to variant dbSNP:rs121913009Ensembl.1
Natural variantiVAR_029368812G → C in ARVD10. 2 PublicationsCorresponds to variant dbSNP:rs121913010Ensembl.1
Cardiomyopathy, dilated 1BB (CMD1BB)1 Publication
Disease susceptibility is associated with variations affecting the gene represented in this entry.
Disease descriptionA disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death.
See also OMIM:612877
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_06238756V → M Associated with CMD1BB and ARVD10 although it may not be sufficient by itself to result in cardiomyopathy. 2 PublicationsCorresponds to variant dbSNP:rs121913013Ensembl.1

Keywords - Diseasei

Cardiomyopathy, Disease mutation

Organism-specific databases

DisGeNETi1829.
MalaCardsiDSG2.
MIMi610193. phenotype.
612877. phenotype.
OpenTargetsiENSG00000046604.
Orphaneti293899. Familial isolated arrhythmogenic ventricular dysplasia, biventricular form.
293888. Familial isolated arrhythmogenic ventricular dysplasia, left dominant form.
293910. Familial isolated arrhythmogenic ventricular dysplasia, right dominant form.
154. Familial isolated dilated cardiomyopathy.
PharmGKBiPA27502.

Polymorphism and mutation databases

BioMutaiDSG2.
DMDMi148876773.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 23Sequence analysisAdd BLAST23
PropeptideiPRO_000000384524 – 49Sequence analysisAdd BLAST26
ChainiPRO_000000384650 – 1118Desmoglein-2Add BLAST1069

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi112N-linked (GlcNAc...) asparagine2 Publications1
Glycosylationi182N-linked (GlcNAc...) asparagine3 Publications1
Glycosylationi309N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi462N-linked (GlcNAc...) (complex) asparagine2 Publications1
Glycosylationi514N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei680PhosphoserineCombined sources1
Modified residuei700PhosphoserineCombined sources1
Modified residuei703PhosphoserineCombined sources1
Modified residuei723PhosphoserineCombined sources1
Modified residuei726PhosphoserineCombined sources1
Modified residuei804PhosphothreonineCombined sources1
Modified residuei806PhosphoserineCombined sources1
Modified residuei810PhosphoserineCombined sources1
Modified residuei815PhosphoserineCombined sources1
Modified residuei922PhosphothreonineCombined sources1
Modified residuei1118PhosphoserineCombined sources1

Keywords - PTMi

Cleavage on pair of basic residues, Glycoprotein, Phosphoprotein

Proteomic databases

EPDiQ14126.
MaxQBiQ14126.
PaxDbiQ14126.
PeptideAtlasiQ14126.
PRIDEiQ14126.

PTM databases

iPTMnetiQ14126.
PhosphoSitePlusiQ14126.
SwissPalmiQ14126.

Miscellaneous databases

PMAP-CutDBiQ14126.

Expressioni

Tissue specificityi

All of the tissues tested and carcinomas.

Gene expression databases

BgeeiENSG00000046604.
CleanExiHS_DSG2.
ExpressionAtlasiQ14126. baseline and differential.
GenevisibleiQ14126. HS.

Organism-specific databases

HPAiCAB025122.
HPA004896.

Interactioni

GO - Molecular functioni

  • cell adhesion molecule binding Source: BHF-UCL
  • cell adhesive protein binding involved in bundle of His cell-Purkinje myocyte communication Source: BHF-UCL
Complete GO annotation...

Protein-protein interaction databases

BioGridi108163. 47 interactors.
DIPiDIP-46250N.
IntActiQ14126. 34 interactors.
MINTiMINT-4990532.
STRINGi9606.ENSP00000261590.

Structurei

Secondary structure

11118
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi56 – 59Combined sources4
Helixi65 – 67Combined sources3
Turni76 – 82Combined sources7
Beta strandi86 – 91Combined sources6
Turni92 – 94Combined sources3
Beta strandi95 – 98Combined sources4
Beta strandi100 – 104Combined sources5
Turni106 – 108Combined sources3
Beta strandi110 – 113Combined sources4
Turni119 – 121Combined sources3
Beta strandi123 – 132Combined sources10
Beta strandi134 – 136Combined sources3
Beta strandi138 – 140Combined sources3
Beta strandi143 – 150Combined sources8
Beta strandi158 – 160Combined sources3
Beta strandi162 – 169Combined sources8
Beta strandi177 – 180Combined sources4
Turni192 – 194Combined sources3
Beta strandi197 – 205Combined sources9
Beta strandi211 – 213Combined sources3
Turni215 – 217Combined sources3
Beta strandi219 – 222Combined sources4
Turni229 – 231Combined sources3
Beta strandi233 – 242Combined sources10
Beta strandi257 – 263Combined sources7
Beta strandi278 – 282Combined sources5
Beta strandi289 – 296Combined sources8
Turni304 – 306Combined sources3
Beta strandi307 – 315Combined sources9
Beta strandi321 – 326Combined sources6
Turni327 – 330Combined sources4
Beta strandi331 – 336Combined sources6
Turni342 – 345Combined sources4
Beta strandi350 – 358Combined sources9
Turni362 – 366Combined sources5
Beta strandi373 – 380Combined sources8
Beta strandi391 – 400Combined sources10
Turni401 – 403Combined sources3
Beta strandi409 – 412Combined sources4
Turni418 – 420Combined sources3
Beta strandi426 – 431Combined sources6
Beta strandi438 – 440Combined sources3
Turni442 – 444Combined sources3
Beta strandi446 – 451Combined sources6
Beta strandi464 – 477Combined sources14
Beta strandi480 – 490Combined sources11
Beta strandi498 – 500Combined sources3
Beta strandi502 – 507Combined sources6
Beta strandi513 – 518Combined sources6
Beta strandi525 – 528Combined sources4
Helixi540 – 543Combined sources4
Beta strandi544 – 549Combined sources6
Beta strandi551 – 560Combined sources10
Beta strandi564 – 570Combined sources7
Beta strandi575 – 577Combined sources3
Beta strandi584 – 591Combined sources8
Beta strandi595 – 598Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2YQGNMR-A47-162[»]
5ERDX-ray2.90A/B50-602[»]
5J5JX-ray3.29A152-601[»]
ProteinModelPortaliQ14126.
SMRiQ14126.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ14126.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini50 – 160Cadherin 1PROSITE-ProRule annotationAdd BLAST111
Domaini161 – 273Cadherin 2PROSITE-ProRule annotationAdd BLAST113
Domaini274 – 388Cadherin 3PROSITE-ProRule annotationAdd BLAST115
Domaini389 – 503Cadherin 4PROSITE-ProRule annotationAdd BLAST115
Repeati881 – 912Desmoglein repeat 1Add BLAST32
Repeati913 – 942Desmoglein repeat 2Add BLAST30
Repeati943 – 968Desmoglein repeat 3Add BLAST26
Repeati969 – 992Desmoglein repeat 4Add BLAST24
Repeati993 – 1021Desmoglein repeat 5Add BLAST29
Repeati1022 – 1051Desmoglein repeat 6Add BLAST30

Domaini

Three calcium ions are usually bound at the interface of each cadherin domain and rigidify the connections, imparting a strong curvature to the full-length ectodomain.By similarity

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3594. Eukaryota.
ENOG410XQHI. LUCA.
GeneTreeiENSGT00760000118906.
HOGENOMiHOG000236266.
HOVERGENiHBG005532.
InParanoidiQ14126.
KOiK07597.
OMAiVMVRERE.
OrthoDBiEOG091G01F3.
PhylomeDBiQ14126.
TreeFamiTF331809.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
4.10.900.10. 1 hit.
InterProiView protein in InterPro
IPR002126. Cadherin.
IPR015919. Cadherin-like.
IPR020894. Cadherin_CS.
IPR027397. Catenin_binding_dom.
IPR009123. Desmoglein.
IPR009122. Desmosomal_cadherin.
IPR013783. Ig-like_fold.
PANTHERiPTHR24025. PTHR24025. 1 hit.
PfamiView protein in Pfam
PF00028. Cadherin. 3 hits.
PRINTSiPR00205. CADHERIN.
PR01818. DESMOCADHERN.
PR01819. DESMOGLEIN.
SMARTiView protein in SMART
SM00112. CA. 4 hits.
SUPFAMiSSF49313. SSF49313. 5 hits.
PROSITEiView protein in PROSITE
PS00232. CADHERIN_1. 3 hits.
PS50268. CADHERIN_2. 4 hits.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q14126-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARSPGRAYA LLLLLICFNV GSGLHLQVLS TRNENKLLPK HPHLVRQKRA 
        60         70         80         90        100
WITAPVALRE GEDLSKKNPI AKIHSDLAEE RGLKITYKYT GKGITEPPFG 
       110        120        130        140        150
IFVFNKDTGE LNVTSILDRE ETPFFLLTGY ALDARGNNVE KPLELRIKVL 
       160        170        180        190        200
DINDNEPVFT QDVFVGSVEE LSAAHTLVMK INATDADEPN TLNSKISYRI 
       210        220        230        240        250
VSLEPAYPPV FYLNKDTGEI YTTSVTLDRE EHSSYTLTVE ARDGNGEVTD 
       260        270        280        290        300
KPVKQAQVQI RILDVNDNIP VVENKVLEGM VEENQVNVEV TRIKVFDADE 
       310        320        330        340        350
IGSDNWLANF TFASGNEGGY FHIETDAQTN EGIVTLIKEV DYEEMKNLDF 
       360        370        380        390        400
SVIVANKAAF HKSIRSKYKP TPIPIKVKVK NVKEGIHFKS SVISIYVSES 
       410        420        430        440        450
MDRSSKGQII GNFQAFDEDT GLPAHARYVK LEDRDNWISV DSVTSEIKLA 
       460        470        480        490        500
KLPDFESRYV QNGTYTVKIV AISEDYPRKT ITGTVLINVE DINDNCPTLI 
       510        520        530        540        550
EPVQTICHDA EYVNVTAEDL DGHPNSGPFS FSVIDKPPGM AEKWKIARQE 
       560        570        580        590        600
STSVLLQQSE KKLGRSEIQF LISDNQGFSC PEKQVLTLTV CECLHGSGCR 
       610        620        630        640        650
EAQHDSYVGL GPAAIALMIL AFLLLLLVPL LLLMCHCGKG AKGFTPIPGT 
       660        670        680        690        700
IEMLHPWNNE GAPPEDKVVP SFLPVDQGGS LVGRNGVGGM AKEATMKGSS 
       710        720        730        740        750
SASIVKGQHE MSEMDGRWEE HRSLLSGRAT QFTGATGAIM TTETTKTARA 
       760        770        780        790        800
TGASRDMAGA QAAAVALNEE FLRNYFTDKA ASYTEEDENH TAKDCLLVYS 
       810        820        830        840        850
QEETESLNAS IGCCSFIEGE LDDRFLDDLG LKFKTLAEVC LGQKIDINKE 
       860        870        880        890        900
IEQRQKPATE TSMNTASHSL CEQTMVNSEN TYSSGSSFPV PKSLQEANAE 
       910        920        930        940        950
KVTQEIVTER SVSSRQAQKV ATPLPDPMAS RNVIATETSY VTGSTMPPTT 
       960        970        980        990       1000
VILGPSQPQS LIVTERVYAP ASTLVDQPYA NEGTVVVTER VIQPHGGGSN 
      1010       1020       1030       1040       1050
PLEGTQHLQD VPYVMVRERE SFLAPSSGVQ PTLAMPNIAV GQNVTVTERV 
      1060       1070       1080       1090       1100
LAPASTLQSS YQIPTENSMT ARNTTVSGAG VPGPLPDFGL EESGHSNSTI 
      1110 
TTSSTRVTKH STVQHSYS
Length:1,118
Mass (Da):122,294
Last modified:May 29, 2007 - v2
Checksum:iE1481AA1686DB80A
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti4 – 10SPGRAYA → TRDRVR in CAA81226 (PubMed:8143788).Curated7
Sequence conflicti593C → V in CAA81226 (PubMed:8143788).Curated1
Sequence conflicti643G → A in CAA81226 (PubMed:8143788).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02936546R → Q in ARVD10. 2 PublicationsCorresponds to variant dbSNP:rs121913008Ensembl.1
Natural variantiVAR_02936649R → H in ARVD10. 4 PublicationsCorresponds to variant dbSNP:rs121913006Ensembl.1
Natural variantiVAR_06238756V → M Associated with CMD1BB and ARVD10 although it may not be sufficient by itself to result in cardiomyopathy. 2 PublicationsCorresponds to variant dbSNP:rs121913013Ensembl.1
Natural variantiVAR_04850889Y → C. Corresponds to variant dbSNP:rs2230232Ensembl.1
Natural variantiVAR_062388158V → G1 PublicationCorresponds to variant dbSNP:rs191143292Ensembl.1
Natural variantiVAR_048509293I → V2 PublicationsCorresponds to variant dbSNP:rs2230234Ensembl.1
Natural variantiVAR_065686335T → A in ARVD10. 1 PublicationCorresponds to variant dbSNP:rs191564916Ensembl.1
Natural variantiVAR_029367507C → Y in ARVD10. 2 PublicationsCorresponds to variant dbSNP:rs121913009Ensembl.1
Natural variantiVAR_048510515V → I. Corresponds to variant dbSNP:rs2230235Ensembl.1
Natural variantiVAR_062389713E → K2 PublicationsCorresponds to variant dbSNP:rs79241126Ensembl.1
Natural variantiVAR_048511773R → K2 PublicationsCorresponds to variant dbSNP:rs2278792Ensembl.1
Natural variantiVAR_029368812G → C in ARVD10. 2 PublicationsCorresponds to variant dbSNP:rs121913010Ensembl.1
Natural variantiVAR_048512863M → L. Corresponds to variant dbSNP:rs16962093Ensembl.1
Natural variantiVAR_048513903T → I. Corresponds to variant dbSNP:rs34065672Ensembl.1
Natural variantiVAR_062390920V → G2 PublicationsCorresponds to variant dbSNP:rs142841727Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z26317 mRNA. Translation: CAA81226.1.
BC099655 mRNA. Translation: AAH99655.1.
BC099656 mRNA. Translation: AAH99656.1.
BC099657 mRNA. Translation: AAH99657.1.
CCDSiCCDS42423.1.
PIRiS38673.
RefSeqiNP_001934.2. NM_001943.4.
UniGeneiHs.412597.

Genome annotation databases

EnsembliENST00000261590; ENSP00000261590; ENSG00000046604.
GeneIDi1829.
KEGGihsa:1829.
UCSCiuc002kwu.5. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z26317 mRNA. Translation: CAA81226.1.
BC099655 mRNA. Translation: AAH99655.1.
BC099656 mRNA. Translation: AAH99656.1.
BC099657 mRNA. Translation: AAH99657.1.
CCDSiCCDS42423.1.
PIRiS38673.
RefSeqiNP_001934.2. NM_001943.4.
UniGeneiHs.412597.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2YQGNMR-A47-162[»]
5ERDX-ray2.90A/B50-602[»]
5J5JX-ray3.29A152-601[»]
ProteinModelPortaliQ14126.
SMRiQ14126.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108163. 47 interactors.
DIPiDIP-46250N.
IntActiQ14126. 34 interactors.
MINTiMINT-4990532.
STRINGi9606.ENSP00000261590.

PTM databases

iPTMnetiQ14126.
PhosphoSitePlusiQ14126.
SwissPalmiQ14126.

Polymorphism and mutation databases

BioMutaiDSG2.
DMDMi148876773.

Proteomic databases

EPDiQ14126.
MaxQBiQ14126.
PaxDbiQ14126.
PeptideAtlasiQ14126.
PRIDEiQ14126.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000261590; ENSP00000261590; ENSG00000046604.
GeneIDi1829.
KEGGihsa:1829.
UCSCiuc002kwu.5. human.

Organism-specific databases

CTDi1829.
DisGeNETi1829.
GeneCardsiDSG2.
GeneReviewsiDSG2.
H-InvDBiHIX0039840.
HGNCiHGNC:3049. DSG2.
HPAiCAB025122.
HPA004896.
MalaCardsiDSG2.
MIMi125671. gene.
610193. phenotype.
612877. phenotype.
neXtProtiNX_Q14126.
OpenTargetsiENSG00000046604.
Orphaneti293899. Familial isolated arrhythmogenic ventricular dysplasia, biventricular form.
293888. Familial isolated arrhythmogenic ventricular dysplasia, left dominant form.
293910. Familial isolated arrhythmogenic ventricular dysplasia, right dominant form.
154. Familial isolated dilated cardiomyopathy.
PharmGKBiPA27502.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3594. Eukaryota.
ENOG410XQHI. LUCA.
GeneTreeiENSGT00760000118906.
HOGENOMiHOG000236266.
HOVERGENiHBG005532.
InParanoidiQ14126.
KOiK07597.
OMAiVMVRERE.
OrthoDBiEOG091G01F3.
PhylomeDBiQ14126.
TreeFamiTF331809.

Enzyme and pathway databases

ReactomeiR-HSA-351906. Apoptotic cleavage of cell adhesion proteins.
R-HSA-6805567. Keratinization.
R-HSA-6809371. Formation of the cornified envelope.

Miscellaneous databases

ChiTaRSiDSG2. human.
EvolutionaryTraceiQ14126.
GeneWikiiDesmoglein_2.
GenomeRNAii1829.
PMAP-CutDBiQ14126.
PROiPR:Q14126.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000046604.
CleanExiHS_DSG2.
ExpressionAtlasiQ14126. baseline and differential.
GenevisibleiQ14126. HS.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
4.10.900.10. 1 hit.
InterProiView protein in InterPro
IPR002126. Cadherin.
IPR015919. Cadherin-like.
IPR020894. Cadherin_CS.
IPR027397. Catenin_binding_dom.
IPR009123. Desmoglein.
IPR009122. Desmosomal_cadherin.
IPR013783. Ig-like_fold.
PANTHERiPTHR24025. PTHR24025. 1 hit.
PfamiView protein in Pfam
PF00028. Cadherin. 3 hits.
PRINTSiPR00205. CADHERIN.
PR01818. DESMOCADHERN.
PR01819. DESMOGLEIN.
SMARTiView protein in SMART
SM00112. CA. 4 hits.
SUPFAMiSSF49313. SSF49313. 5 hits.
PROSITEiView protein in PROSITE
PS00232. CADHERIN_1. 3 hits.
PS50268. CADHERIN_2. 4 hits.
ProtoNetiSearch...

Entry informationi

Entry nameiDSG2_HUMAN
AccessioniPrimary (citable) accession number: Q14126
Secondary accession number(s): Q4KKU6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 29, 2007
Last modified: May 10, 2017
This is version 167 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 18
    Human chromosome 18: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

Similar proteinsi

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