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MitoProteome Human Mitochondrial Protein Database
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Related Proteins
MT000193
UniProt Annotations
Entry Information
Gene Name
desmoplakin
Protein Entry
DESP_HUMAN
UniProt ID
P15924
Species
Human
Comments
Comment type
Description
Alternative Products
Event=Alternative splicing; Named isoforms=3; Name=DPI; Synonyms=DP1; IsoId=P15924-1; Sequence=Displayed; Name=DPII; Synonyms=DP2; IsoId=P15924-2; Sequence=VSP_005070; Name=DSPIa; IsoId=P15924-3; Sequence=VSP_053769; Note=Minor isoform.;
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:20031617}. Note=The disease is caused by mutations 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}. Note=The disease is caused by mutations 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. Note=The disease is caused by mutations affecting the gene represented in this entry.
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:9887343}. Note=The disease is caused by mutations affecting the gene represented in this entry.
Disease
Skin fragility-woolly hair syndrome (SFWHS) [MIM:607655]: An autosomal recessive genodermatosis characterized by skin fragility with blistering, focal and diffuse palmoplantar keratoderma, hyperkeratotic plaques on the trunk and limbs, and woolly hair with varying degrees of alopecia. {ECO:0000269|PubMed:11841538}. Note=The disease is caused by mutations affecting the gene represented in this entry.
Domain
Its association with epidermal and simple keratins is dependent on the tertiary structure induced by heterodimerization of these intermediate filaments proteins and most likely involves recognition sites located in the rod domain of these keratins.
Domain
The N-terminal region is required for localization to the desmosomal plaque and interacts with the N-terminal region of plakophilin 1.
Domain
The three tandem plakin repeat regions in the C-terminus mediate binding to intermediate filaments.
Function
Major high molecular weight protein of desmosomes. Involved in the organization of the desmosomal cadherin- plakoglobin complexes into discrete plasma membrane domains and in the anchoring of intermediate filaments to the desmosomes.
Interaction
Q13835-2:PKP1; NbExp=2; IntAct=EBI-355041, EBI-9087684;
Ptm
Ser-2849 is probably phosphorylated by a cAMP-dependent protein kinase. Phosphorylation on Ser-2849 probably affects its association with epidermal, simple cytokeratins and VIM intermediate filaments. {ECO:0000269|PubMed:18220336, ECO:0000269|PubMed:18669648, ECO:0000269|PubMed:20068231, ECO:0000269|PubMed:21406692}.
Ptm
Substrate of transglutaminase. Some glutamines and lysines are cross-linked to other desmoplakin molecules, to other proteins such as keratin, envoplakin, periplakin and involucrin, and to lipids like omega-hydroxyceramide (PubMed:9651377). {ECO:0000269|PubMed:9651377}.
Similarity
Belongs to the plakin or cytolinker family. {ECO:0000305}.
Similarity
Contains 17 plectin repeats. {ECO:0000305}.
Similarity
Contains 1 SH3 domain. {ECO:0000305}.
Similarity
Contains 6 spectrin repeats. {ECO:0000305}.
Subcellular Location
Cell junction, desmosome {ECO:0000269|PubMed:12802069}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:12802069}. Note=Innermost portion of the desmosomal plaque. Colocalizes with epidermal KRT5-KRT14 and simple KRT8-KRT18 keratins and VIM intermediate filaments network.
Subunit
Homodimer. Interacts with COL17A1 (via cytoplasmic region). Associates (via C-terminal) with KRT5-KRT14 (via rod region), KRT8-KRT18 and VIM intermediate filaments. Interacts with DSC2. Interacts with PKP2. {ECO:0000269|PubMed:12482924, ECO:0000269|PubMed:21062920, ECO:0000269|PubMed:22781308}.
Tissue Specificity
Isoform DPI is apparently an obligate constituent of all desmosomes. Isoform DPII resides predominantly in tissues and cells of stratified origin.
Web Resource
Name=Wikipedia; Note=Desmoplakin entry; URL="http://en.wikipedia.org/wiki/Desmoplakin";
MitoProteome Human Mitochondrial Protein Database
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