DSP
entrez
1832
canonical
uniprot
P15924
canonical
ensembl
ENSG00000096696
resolver
ensp
ENSP00000369129
resolver
ensp
ENSP00000396591
resolver
ensp
ENSP00000518230
resolver
ensp
ENSP00000519209
resolver
enst
ENST00000713910
resolver
genesymbol
DSP
resolver
hgnc
HGNC:3052
resolver
uniprot
A0AAQ5BH43
resolver
uniprot
B2RTT2
resolver
uniprot
B4DKX6
resolver
uniprot
D7RX09
resolver
uniprot
O75993
resolver
uniprot
Q14189
resolver
uniprot
Q9UHN4
resolver
uniprot_entry
A0AAQ5BH43_HUMAN
resolver
uniprot_entry
B4DKX6_HUMAN
resolver
uniprot_entry
DESP_HUMAN
resolver
uniprot_sec
B2RTT2
resolver
uniprot_sec
D7RX09
resolver
uniprot_sec
O75993
resolver
uniprot_sec
Q14189
resolver
uniprot_sec
Q9UHN4
resolver
amino_acid_sequence
MSCNGGSHPRINTLGRMIRAESGPDLRYEVTSGGGGTSRMYYSRRGVITDQNSDGYCQTGTMSRHQNQNTIQELLQNCSDCLMRAELIVQPELKYGDGIQLTRSRELDECFAQANDQMEILDSLIREMRQMGQPCDAYQKRLLQLQEQMRALYKAISVPRVRRASSKGGGGYTCQSGSGWDEFTKHVTSECLGWMRQQRAEMDMVAWGVDLASVEQHINSHRGIHNSIGDYRWQLDKIKADLREKSAIYQLEEEYENLLKASFERMDHLRQLQNIIQATSREIMWINDCEEEELLYDWSDKNTNIAQKQEAFSIRMSQLEVKEKELNKLKQESDQLVLNQHPASDKIEAYMDTLQTQWSWILQITKCIDVHLKENAAYFQFFEEAQSTEAYLKGLQDSIRKKYPCDKNMPLQHLLEQIKELEKEREKILEYKRQVQNLVNKSKKIVQLKPRNPDYRSNKPIILRALCDYKQDQKIVHKGDECILKDNNERSKWYVTGPGGVDMLVPSVGLIIPPPNPLAVDLSCKIEQYYEAILALWNQLYINMKSLVSWHYCMIDIEKIRAMTIAKLKTMRQEDYMKTIADLELHYQEFIRNSQGSEMFGDDDKRKIQSQFTDAQKHYQTLVIQLPGYPQHQTVTTTEITHHGTCQDVNHNKVIETNRENDKQETWMLMELQKIRRQIEHCEGRMTLKNLPLADQGSSHHITVKINELKSVQNDSQAIAEVLNQLKDMLANFRGSEKYCYLQNEVFGLFQKLENINGVTDGYLNSLCTVRALLQAILQTEDMLKVYEARLTEEETVCLDLDKVEAYRCGLKKIKNDLNLKKSLLATMKTELQKAQQIHSQTSQQYPLYDLDLGKFGEKVTQLTDRWQRIDKQIDFRLWDLEKQIKQLRNYRDNYQAFCKWLYDAKRRQDSLESMKFGDSNTVMRFLNEQKNLHSEISGKRDKSEEVQKIAELCANSIKDYELQLASYTSGLETLLNIPIKRTMIQSPSGVILQEAADVHARYIELLTRSGDYYRFLSEMLKSLEDLKLKNTKIEVLEEELRLARDANSENCNKNKFLDQNLQKYQAECSQFKAKLASLEELKRQAELDGKSAKQNLDKCYGQIKELNEKITRLTYEIEDEKRRRKSVEDRFDQQKNDYDQLQKARQCEKENLGWQKLESEKAIKEKEYEIERLRVLLQEEGTRKREYENELAKVRNHYNEEMSNLRNKYETEINITKTTIKEISMQKEDDSKNLRNQLDRLSRENRDLKDEIVRLNDSILQATEQRRRAEENALQQKACGSEIMQKKQHLEIELKQVMQQRSEDNARHKQSLEEAAKTIQDKNKEIERLKAEFQEEAKRRWEYENELSKVRNNYDEEIISLKNQFETEINITKTTIHQLTMQKEEDTSGYRAQIDNLTRENRSLSEEIKRLKNTLTQTTENLRRVEEDIQQQKATGSEVSQRKQQLEVELRQVTQMRTEESVRYKQSLDDAAKTIQDKNKEIERLKQLIDKETNDRKCLEDENARLQRVQYDLQKANSSATETINKLKVQEQELTRLRIDYERVSQERTVKDQDITRFQNSLKELQLQKQKVEEELNRLKRTASEDSCKRKKLEEELEGMRRSLKEQAIKITNLTQQLEQASIVKKRSEDDLRQQRDVLDGHLREKQRTQEELRRLSSEVEALRRQLLQEQESVKQAHLRNEHFQKAIEDKSRSLNESKIEIERLQSLTENLTKEHLMLEEELRNLRLEYDDLRRGRSEADSDKNATILELRSQLQISNNRTLELQGLINDLQRERENLRQEIEKFQKQALEASNRIQESKNQCTQVVQERESLLVKIKVLEQDKARLQRLEDELNRAKSTLEAETRVKQRLECEKQQIQNDLNQWKTQYSRKEEAIRKIESEREKSEREKNSLRSEIERLQAEIKRIEERCRRKLEDSTRETQSQLETERSRYQREIDKLRQRPYGSHRETQTECEWTVDTSKLVFDGLRKKVTAMQLYECQLIDKTTLDKLLKGKKSVEEVASEIQPFLRGAGSIAGASASPKEKYSLVEAKRKKLISPESTVMLLEAQAATGGIIDPHRNEKLTVDSAIARDLIDFDDRQQIYAAEKAITGFDDPFSGKTVSVSEAIKKNLIDRETGMRLLEAQIASGGVVDPVNSVFLPKDVALARGLIDRDLYRSLNDPRDSQKNFVDPVTKKKVSYVQLKERCRIEPHTGLLLLSVQKRSMSFQGIRQPVTVTELVDSGILRPSTVNELESGQISYDEVGERIKDFLQGSSCIAGIYNETTKQKLGIYEAMKIGLVRPGTALELLEAQAATGFIVDPVSNLRLPVEEAYKRGLVGIEFKEKLLSAERAVTGYNDPETGNIISLFQAMNKELIEKGHGIRLLEAQIATGGIIDPKESHRLPVDIAYKRGYFNEELSEILSDPSDDTKGFFDPNTEENLTYLQLKERCIKDEETGLCLLPLKEKKKQVQTSQKNTLRKRRVVIVDPETNKEMSVQEAYKKGLIDYETFKELCEQECEWEEITITGSDGSTRVVLVDRKTGSQYDIQDAIDKGLVDRKFFDQYRSGSLSLTQFADMISLKNGVGTSSSMGSGVSDDVFSSSRHESVSKISTISSVRNLTIRSSSFSDTLEESSPIAAIFDTENLEKISITEGIERGIVDSITGQRLLEAQACTGGIIHPTTGQKLSLQDAVSQGVIDQDMATRLKPAQKAFIGFEGVKGKKKMSAAEAVKEKWLPYEAGQRFLEFQYLTGGLVDPEVHGRISTEEAIRKGFIDGRAAQRLQDTSSYAKILTCPKTKLKISYKDAINRSMVEDITGLRLLEAASVSSKGLPSPYNMSSAPGSRSGSRSGSRSGSRSGSRSGSRRGSFDATGNSSYSYSYSFSSSSIGH
uniprot
proteins
disease_involvement
DISEASE: Keratoderma, palmoplantar, striate 2 (SPPK2) [MIM:612908]: A dermatological disorder characterized by thickening of the skin on the palms (linear pattern) and the soles (island-like pattern) and flexor aspect of the fingers. Abnormalities of the nails, the teeth and the hair are rarely present. {ECO:0000269|PubMed:29607617, ECO:0000269|PubMed:9887343}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Cardiomyopathy, dilated, with woolly hair and keratoderma (DCWHK) [MIM:605676]: An autosomal recessive cardiocutaneous syndrome characterized by a generalized striate keratoderma particularly affecting the palmoplantar epidermis, woolly hair, and dilated left ventricular cardiomyopathy. {ECO:0000269|PubMed:11063735, ECO:0000269|PubMed:11841538, ECO:0000269|PubMed:12875771, ECO:0000269|PubMed:22949226, ECO:0000269|PubMed:25227139, ECO:0000269|PubMed:32410525}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Arrhythmogenic right ventricular dysplasia, familial, 8 (ARVD8) [MIM:607450]: 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:12373648, ECO:0000269|PubMed:15941723, ECO:0000269|PubMed:16917092, ECO:0000269|PubMed:20031617, ECO:0000269|PubMed:25616123, ECO:0000269|PubMed:28527814, ECO:0000269|PubMed:30160835, ECO:0000269|PubMed:35470109}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Epidermolysis bullosa, lethal acantholytic (EBLA) [MIM:609638]: A form of epidermolysis bullosa characterized by severe fragility of skin and mucous membranes. The phenotype is lethal in the neonatal period because of immense transcutaneous fluid loss. Typical features include universal alopecia, neonatal teeth, and nail loss. Histopathology of the skin shows suprabasal clefting and acantholysis throughout the spinous layer, mimicking pemphigus. {ECO:0000269|PubMed:16175511, ECO:0000269|PubMed:28442525}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Erythroderma, congenital, with palmoplantar keratoderma, hypotrichosis, and hyper IgE (EPKHE) [MIM:615508]: A syndrome characterized by severe dermatitis, multiple allergies and metabolic wasting. Clinical features include erythroderma, yellowish papules and plaques arranged at the periphery of the palms, along the fingers and over weight-bearing areas of the feet, skin erosions and scaling, and hypotrichosis. Additionally, patients manifest severe food allergies, elevated immunoglobulin E (IgE) levels and recurrent infections with marked metabolic wasting. {ECO:0000269|PubMed:26073755}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Cardiomyopathy, dilated, with woolly hair, keratoderma, and tooth agenesis (DCWHKTA) [MIM:615821]: A cardiocutaneous syndrome characterized by biventricular dilated cardiomyopathy, hyperkeratosis, woolly hair, palmoplantar keratoderma, and hypo/oligodontia. {ECO:0000269|PubMed:16628197, ECO:0000269|PubMed:20940358, ECO:0000269|PubMed:22795705, ECO:0000269|PubMed:26604139, ECO:0000269|PubMed:30354334, ECO:0000269|PubMed:32808748, ECO:0000269|PubMed:35470109, ECO:0000269|PubMed:36768812}. Note=The disease is caused by 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:25733715). Critical for cell-cell adhesion in early stage blastocysts and progression through proamniotic cavity formation (By similarity). Not required for preimplantation morphogenic process in blastocysts (By similarity). Required for keratin filament anchoring at the desmosome junction and subsequent organization of the keratin intermediate filament network within the cytoplasm (By similarity). Required for anchoring of desmosomes to the microtubule architecture, via its interaction with NIN (By similarity). Promotes microtubule-mediated GJA1/CX43 trafficking to cell membranes via its interaction with MAPRE1/EB1, thereby facilitating gap junction intracellular communication (PubMed:25225338). Plays a key role in adhesion and organization of the dermal epithelial barrier (PubMed:26604139). Critical for the maintenance of the neural tube structure following formation and organization of the neuroepithelium (By similarity). Facilitates outgrowth and repair of motor neuron fibers in regenerating axons following injury, probably by promoting recruitment of a complex containing DSP, CDH2, VIM and JUP to the outgrowth tips (By similarity). Critical for the normal formation of heart and myocardial tissue during early embryogenesis (By similarity). Also required for development of vascular capillary structures and intact endothelial cell barriers (By similarity). Regulates profibrotic gene expression in cardiomyocytes via activation of the MAPK14/p38 MAPK signaling cascade and increase in TGFB1 protein abundance (By similarity). Maintains cardiac rhythmicity by ensuring correct cell-cell adhesion within the sinoatrial node, via stabilization of protein components of both desmosome and Gap junctions (By similarity). Involved in maintaining the protein stability and recruitment of GJA1 to functional gap junctions, via inhibition of KRAS-mediated MAPK1/MAPK3 phosphorylation of GJA1 (By similarity). Negative regulator of cell cycle progression and differentiation in keratinocytes, potentially via inhibition of MAPK and phosphoinositide-3-kinase (PI3K) signaling pathways (PubMed:17475244). Mediates the interaction between the desmosome and COP9 signalosome complex (CSN) protein complex (PubMed:28891468). As a result of this interaction, promotes keratinocyte differentiation via deneddylation of EGFR resulting in a reduction in EGFR protein stabilization and translocation away from the cell membrane (PubMed:28891468). Required for the maintenance of protein abundance of desmosome junction components DSG1, DSG2, DSC2, DSC3, PKP1, PKP2 and PKP3 (PubMed:17475244, PubMed:26073755). Required for the survival and maintenance of germ cells in the gonads during embryonic development (By similarity). Binds to telomere DNA (via C-terminus) and acts to prevent telomere damage and maintain telomere length via its interaction with TRF2 (PubMed:31595153). {ECO:0000250|UniProtKB:E9Q557, ECO:0000250|UniProtKB:F1LMV6, ECO:0000269|PubMed:17475244, ECO:0000269|PubMed:25225338, ECO:0000269|PubMed:25733715, ECO:0000269|PubMed:26073755, ECO:0000269|PubMed:26604139, ECO:0000269|PubMed:28891468, ECO:0000269|PubMed:31595153}.
uniprot
proteins
mass_dalton
331774
uniprot
proteins
mutagenesis
MUTAGEN 470; /note="K->E: No observable change in the secondary structure folding."; /evidence="ECO:0000269|PubMed:21756917"; MUTAGEN 808; /note="R->C: Reduced thermal stability of protein. No observable change in secondary structure folding."; /evidence="ECO:0000269|PubMed:21756917"; MUTAGEN 1122..1126; /note="Missing: Abolishes localization to the nucleus and binding to telomeres."; /evidence="ECO:0000269|PubMed:31595153"; MUTAGEN 2845; /note="S->A: Abolishes GSK3B phosphorylation of multiple downstream sites within the C-terminus and decreases interaction with GSK3B."; /evidence="ECO:0000269|PubMed:25733715"; MUTAGEN 2849; /note="S->G: Decreases cell-cell adhesion when under mechanical stress."; /evidence="ECO:0000269|PubMed:25733715"; MUTAGEN 2853; /note="T->A: No effect on GSK3B-mediated phosphorylation of multiple downstream sites within the C-terminus."; /evidence="ECO:0000269|PubMed:25733715
uniprot
proteins
post_translational_modification
PTM: Methylation by PRMT1 promotes GSK3B-mediated phosphorylation cascade of multiple serine residues at the C-terminus resulting in trafficking to desmosome cell-cell junctions. {ECO:0000269|PubMed:25733715}.; PTM: Phosphorylation by GSK3B occurs sequentially from Ser-2849 along multiple serine residue at the C-terminus. Hyperphosphorylation by GSK3B results in recruitment to desmosome cell-cell junction and promotion of intercellular adhesion (PubMed:25733715). Phosphorylation at Ser-2849 increases association with intermediate filament cytokeratin, potentially facilitating interaction between desmosome junctions and intermediate filament architecture (PubMed:33596089). {ECO:0000269|PubMed:25733715, ECO:0000269|PubMed:33596089}.
uniprot
proteins
protein_family
Plakin or cytolinker family
uniprot
proteins
pubmed
10594734
uniprot
proteins
pubmed
10852826
uniprot
proteins
pubmed
11063735
uniprot
proteins
pubmed
11790773
uniprot
proteins
pubmed
11841538
uniprot
proteins
pubmed
12101406
uniprot
proteins
pubmed
12373648
uniprot
proteins
pubmed
12482924
uniprot
proteins
pubmed
12875771
uniprot
proteins
pubmed
14574404
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15941723
uniprot
proteins
pubmed
16175511
uniprot
proteins
pubmed
16628197
uniprot
proteins
pubmed
1689290
uniprot
proteins
pubmed
16917092
uniprot
proteins
pubmed
1731325
uniprot
proteins
pubmed
17475244
uniprot
proteins
pubmed
18220336
uniprot
proteins
pubmed
18343367
uniprot
proteins
pubmed
18662195
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
19136012
uniprot
proteins
pubmed
19369195
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
19863551
uniprot
proteins
pubmed
20031617
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20524011
uniprot
proteins
pubmed
20859650
uniprot
proteins
pubmed
20940358
uniprot
proteins
pubmed
21062920
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
21536047
uniprot
proteins
pubmed
21756917
uniprot
proteins
pubmed
22781308
uniprot
proteins
pubmed
22795705
uniprot
proteins
pubmed
22949226
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23444369
uniprot
proteins
pubmed
2391353
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25208567
uniprot
proteins
pubmed
25225338
uniprot
proteins
pubmed
25227139
uniprot
proteins
pubmed
25616123
uniprot
proteins
pubmed
25733715
uniprot
proteins
pubmed
26073755
uniprot
proteins
pubmed
26604139
uniprot
proteins
pubmed
26808545
uniprot
proteins
pubmed
28442525
uniprot
proteins
pubmed
28527814
uniprot
proteins
pubmed
28891468
uniprot
proteins
pubmed
29034528
uniprot
proteins
pubmed
29607617
uniprot
proteins
pubmed
29878302
uniprot
proteins
pubmed
30160835
uniprot
proteins
pubmed
30354334
uniprot
proteins
pubmed
30479852
uniprot
proteins
pubmed
31595153
uniprot
proteins
pubmed
32410525
uniprot
proteins
pubmed
32808748
uniprot
proteins
pubmed
33596089
uniprot
proteins
pubmed
35348702
uniprot
proteins
pubmed
35470109
uniprot
proteins
pubmed
36768812
uniprot
proteins
pubmed
9348293
uniprot
proteins
pubmed
9887343
uniprot
proteins
sequence_length
2871
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell projection, axon {ECO:0000250|UniProtKB:E9Q557}. Cell junction, desmosome {ECO:0000269|PubMed:16917092, ECO:0000269|PubMed:18343367, ECO:0000269|PubMed:20859650, ECO:0000269|PubMed:25208567, ECO:0000269|PubMed:25733715, ECO:0000269|PubMed:26604139, ECO:0000269|PubMed:28891468}. Cell membrane {ECO:0000269|PubMed:16917092, ECO:0000269|PubMed:17475244, ECO:0000269|PubMed:25225338}. Cytoplasm {ECO:0000269|PubMed:17475244, ECO:0000269|PubMed:25208567, ECO:0000269|PubMed:25225338, ECO:0000269|PubMed:28891468, ECO:0000269|PubMed:29878302}. Nucleus {ECO:0000269|PubMed:31595153}. Note=Localizes to desmosome precursor particles in the cytoplasm (PubMed:25208567). Localizes to the cytoplasm in undifferentiated keratinocytes however becomes localizes to both lateral and tricellular cell-cell contacts as differentiation progresses and as epithelial sheet formation completes (By similarity). Localizes to the interface of the cortical keratin network and endodermal cell periphery in developing embryos (By similarity). {ECO:0000250|UniProtKB:E9Q557, ECO:0000269|PubMed:25208567}.
uniprot
proteins