DSG2
entrez
1829
canonical
uniprot
Q14126
canonical
ensembl
ENSG00000046604
resolver
ensp
ENSP00000261590
resolver
ensp
ENSP00000519063
resolver
ensp
ENSP00000519081
resolver
ensp
ENSP00000519082
resolver
ensp
ENSP00000519140
resolver
enst
ENST00000261590
resolver
enst
ENST00000713762
resolver
enst
ENST00000713779
resolver
enst
ENST00000713780
resolver
enst
ENST00000713835
resolver
genesymbol
DSG2
resolver
genesymbol_syn
CDHF5
resolver
hgnc
HGNC:3049
resolver
uniprot
A0AAQ5BGT2
resolver
uniprot
Q4KKU6
resolver
uniprot_entry
A0AAQ5BGT2_HUMAN
resolver
uniprot_entry
DSG2_HUMAN
resolver
uniprot_sec
Q4KKU6
resolver
amino_acid_sequence
MARSPGRAYALLLLLICFNVGSGLHLQVLSTRNENKLLPKHPHLVRQKRAWITAPVALREGEDLSKKNPIAKIHSDLAEERGLKITYKYTGKGITEPPFGIFVFNKDTGELNVTSILDREETPFFLLTGYALDARGNNVEKPLELRIKVLDINDNEPVFTQDVFVGSVEELSAAHTLVMKINATDADEPNTLNSKISYRIVSLEPAYPPVFYLNKDTGEIYTTSVTLDREEHSSYTLTVEARDGNGEVTDKPVKQAQVQIRILDVNDNIPVVENKVLEGMVEENQVNVEVTRIKVFDADEIGSDNWLANFTFASGNEGGYFHIETDAQTNEGIVTLIKEVDYEEMKNLDFSVIVANKAAFHKSIRSKYKPTPIPIKVKVKNVKEGIHFKSSVISIYVSESMDRSSKGQIIGNFQAFDEDTGLPAHARYVKLEDRDNWISVDSVTSEIKLAKLPDFESRYVQNGTYTVKIVAISEDYPRKTITGTVLINVEDINDNCPTLIEPVQTICHDAEYVNVTAEDLDGHPNSGPFSFSVIDKPPGMAEKWKIARQESTSVLLQQSEKKLGRSEIQFLISDNQGFSCPEKQVLTLTVCECLHGSGCREAQHDSYVGLGPAAIALMILAFLLLLLVPLLLLMCHCGKGAKGFTPIPGTIEMLHPWNNEGAPPEDKVVPSFLPVDQGGSLVGRNGVGGMAKEATMKGSSSASIVKGQHEMSEMDGRWEEHRSLLSGRATQFTGATGAIMTTETTKTARATGASRDMAGAQAAAVALNEEFLRNYFTDKAASYTEEDENHTAKDCLLVYSQEETESLNASIGCCSFIEGELDDRFLDDLGLKFKTLAEVCLGQKIDINKEIEQRQKPATETSMNTASHSLCEQTMVNSENTYSSGSSFPVPKSLQEANAEKVTQEIVTERSVSSRQAQKVATPLPDPMASRNVIATETSYVTGSTMPPTTVILGPSQPQSLIVTERVYAPASTLVDQPYANEGTVVVTERVIQPHGGGSNPLEGTQHLQDVPYVMVRERESFLAPSSGVQPTLAMPNIAVGQNVTVTERVLAPASTLQSSYQIPTENSMTARNTTVSGAGVPGPLPDFGLEESGHSNSTITTSSTRVTKHSTVQHSYS
uniprot
proteins
disease_involvement
DISEASE: Arrhythmogenic right ventricular dysplasia, familial, 10 (ARVD10) [MIM:610193]: A 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. {ECO:0000269|PubMed:16505173, ECO:0000269|PubMed:16773573, ECO:0000269|PubMed:19635863, ECO:0000269|PubMed:19863551, ECO:0000269|PubMed:20031617, ECO:0000269|PubMed:21062920, ECO:0000269|PubMed:30391969, ECO:0000269|PubMed:30454721, ECO:0000269|PubMed:31845994, ECO:0000269|PubMed:33917638, ECO:0000269|PubMed:38375917}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Cardiomyopathy, dilated, 1BB (CMD1BB) [MIM:612877]: A disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death. {ECO:0000269|PubMed:18678517}. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: A component of desmosome cell-cell junctions which are required for positive regulation of cellular adhesion (PubMed:17559062, PubMed:38395410). Involved in the interaction of plaque proteins and intermediate filaments mediating cell-cell adhesion. Required for proliferation and viability of embryonic stem cells in the blastocyst, thereby crucial for progression of post-implantation embryonic development (By similarity). Maintains pluripotency by regulating epithelial to mesenchymal transition/mesenchymal to epithelial transition (EMT/MET) via interacting with and sequestering CTNNB1 to sites of cell-cell contact, thereby reducing translocation of CTNNB1 to the nucleus and subsequent transcription of CTNNB1/TCF-target genes (PubMed:29910125). Promotes pluripotency and the multi-lineage differentiation potential of hematopoietic stem cells (PubMed:27338829). Plays a role in endothelial cell sprouting and elongation via mediating the junctional-association of cortical actin fibers and CDH5 (PubMed:27338829). Promotes cardiomyocyte cell homeostasis and desmosome junction formation at intercalated disks, as a result plays a role in the maintenance of cardiac conduction and heart chamber integrity (By similarity). Positively regulates pancreatic islet development and maintenance of endothelial cell barrier integrity in the pancreas, therefore involved in the controlled release of insulin from islet cells into the circulation in response to glucose (By similarity). Plays a role in limiting inflammatory infiltration and the apoptotic response to injury in kidney tubular epithelial cells, potentially via its role in maintaining cell-cell adhesion and the epithelial barrier (PubMed:38395410). Acts as a positive modulator of CSK and EGFR activation via sequestering them away from lipid rafts, this is independent of its role in desmosome cell junctions (PubMed:26918609). Also disrupts the localization of CAV1 to lipid rafts resulting in its distribution throughout the cytoplasm (PubMed:26918609). {ECO:0000250|UniProtKB:O55111, ECO:0000269|PubMed:17559062, ECO:0000269|PubMed:26918609, ECO:0000269|PubMed:27338829, ECO:0000269|PubMed:29910125, ECO:0000269|PubMed:38395410}.; FUNCTION: (Microbial infection) Required for fiber protein-mediated Human Adenovirus 55 and 14a infection; via its interaction with fiber protein. {ECO:0000269|PubMed:32581096}.
uniprot
proteins
mass_dalton
122294
uniprot
proteins
mutagenesis
MUTAGEN 112; /note="N->Q: Abolishes glycosylation, reduces localization to the plasma membrane."; /evidence="ECO:0000269|PubMed:30885746"; MUTAGEN 154; /note="D->E: Abolishes glycosylation. Increases size of glycosylation at ASN-182. Increase in cell-cell adhesion strength."; /evidence="ECO:0000269|PubMed:30885746"; MUTAGEN 182; /note="N->Q: Abolishes glycosylation, reduces localization to the plasma membrane."; /evidence="ECO:0000269|PubMed:30885746"; MUTAGEN 187; /note="D->G: Increase in cell-cell adhesion strength."; /evidence="ECO:0000269|PubMed:30885746"; MUTAGEN 309; /note="N->Q: Abolishes glycosylation."; /evidence="ECO:0000269|PubMed:30885746"; MUTAGEN 462; /note="N->Q: Abolishes glycosylation, reduces localization to the plasma membrane."; /evidence="ECO:0000269|PubMed:30885746"; MUTAGEN 514; /note="N->Q: Abolishes glycosylation, reduces localization to the plasma membrane."; /evidence="ECO:0000269|PubMed:30885746
uniprot
proteins
post_translational_modification
PTM: (Microbial infection) Proteolytically cleaved by H.pylori HtrA at the cell membrane; cleavage is facilitated by host MMP and ADAM family members. {ECO:0000269|PubMed:34742300}.; PTM: Cleaved by CASP3 in response to apoptosis which results in a loss of full length DSG2 at cell-cell adhesion junctions and a decrease in intercellular adhesion. {ECO:0000269|PubMed:17559062}.; PTM: N-glycosylated; promotes localization to the plasma membrane and cell-cell adhesion junction strength (PubMed:30885746). Not required for interaction with human adenovirus B 3 fiber protein (PubMed:29849084). {ECO:0000269|PubMed:29849084, ECO:0000269|PubMed:30885746}.; PTM: Palmitoylated by ZDHHC5 at the plasma membrane. {ECO:0000269|PubMed:31402609}.
uniprot
proteins
pubmed
11790773
uniprot
proteins
pubmed
12754519
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16335952
uniprot
proteins
pubmed
16505173
uniprot
proteins
pubmed
16773573
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17559062
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18678517
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
19139490
uniprot
proteins
pubmed
19159218
uniprot
proteins
pubmed
19349973
uniprot
proteins
pubmed
1935985
uniprot
proteins
pubmed
19635863
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
19863551
uniprot
proteins
pubmed
20031617
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20859650
uniprot
proteins
pubmed
21062920
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24220297
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25208567
uniprot
proteins
pubmed
26918609
uniprot
proteins
pubmed
27338829
uniprot
proteins
pubmed
29849084
uniprot
proteins
pubmed
29910125
uniprot
proteins
pubmed
29999492
uniprot
proteins
pubmed
30391969
uniprot
proteins
pubmed
30454721
uniprot
proteins
pubmed
30862836
uniprot
proteins
pubmed
30885746
uniprot
proteins
pubmed
31402609
uniprot
proteins
pubmed
31845994
uniprot
proteins
pubmed
32581096
uniprot
proteins
pubmed
33596089
uniprot
proteins
pubmed
33917638
uniprot
proteins
pubmed
34742300
uniprot
proteins
pubmed
36309486
uniprot
proteins
pubmed
38375917
uniprot
proteins
pubmed
38395410
uniprot
proteins
pubmed
8143788
uniprot
proteins
sequence_length
1118
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17559062, ECO:0000269|PubMed:26918609, ECO:0000269|PubMed:27338829, ECO:0000269|PubMed:30885746, ECO:0000269|PubMed:31402609, ECO:0000269|PubMed:36309486}; Single-pass type I membrane protein. Cell junction, desmosome {ECO:0000269|PubMed:20859650, ECO:0000269|PubMed:25208567, ECO:0000269|PubMed:29999492, ECO:0000269|PubMed:31402609, ECO:0000269|PubMed:31845994, ECO:0000269|PubMed:33596089, ECO:0000269|PubMed:38375917}. Cytoplasm {ECO:0000269|PubMed:17559062, ECO:0000269|PubMed:27338829, ECO:0000269|PubMed:38375917}. Note=Localized to intercalated disks in the heart (PubMed:31845994). Localizes to the cytoplasm following cleavage by CASP3 in response to apoptosis (PubMed:17559062). Glycosylation promotes localization to the plasma membrane (PubMed:30885746). {ECO:0000269|PubMed:17559062, ECO:0000269|PubMed:30885746, ECO:0000269|PubMed:31845994}.; SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:34742300}. Note=(Microbial infection) Proteolytically cleaved at the cell membrane upon H.pylori infection. {ECO:0000269|PubMed:34742300}.
uniprot
proteins
transmembrane_region
TRANSMEM 610..634; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins