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Protein

Desmoplakin

Gene

DSP

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

Functioni

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.

GO - Molecular functioni

  • cell adhesive protein binding involved in bundle of His cell-Purkinje myocyte communication Source: BHF-UCL
  • poly(A) RNA binding Source: UniProtKB
  • protein binding, bridging Source: UniProtKB
  • protein kinase C binding Source: BHF-UCL
  • scaffold protein binding Source: BHF-UCL
  • structural constituent of cytoskeleton Source: ProtInc
  • structural molecule activity Source: UniProtKB

GO - Biological processi

  • adherens junction organization Source: Ensembl
  • bundle of His cell-Purkinje myocyte adhesion involved in cell communication Source: BHF-UCL
  • desmosome organization Source: BHF-UCL
  • epidermis development Source: ProtInc
  • intermediate filament organization Source: BHF-UCL
  • keratinocyte differentiation Source: UniProtKB
  • peptide cross-linking Source: UniProtKB
  • protein localization to adherens junction Source: BHF-UCL
  • regulation of heart rate by cardiac conduction Source: BHF-UCL
  • regulation of ventricular cardiac muscle cell action potential Source: BHF-UCL
  • ventricular compact myocardium morphogenesis Source: BHF-UCL
  • wound healing Source: Ensembl
Complete GO annotation...

Enzyme and pathway databases

BioCyciZFISH:ENSG00000096696-MONOMER.
ReactomeiR-HSA-351906. Apoptotic cleavage of cell adhesion proteins.
R-HSA-6798695. Neutrophil degranulation.
R-HSA-6805567. Keratinization.
R-HSA-6809371. Formation of the cornified envelope.
SIGNORiP15924.

Names & Taxonomyi

Protein namesi
Recommended name:
Desmoplakin
Short name:
DP
Alternative name(s):
250/210 kDa paraneoplastic pemphigus antigen
Gene namesi
Name:DSP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:3052. DSP.

Subcellular locationi

GO - Cellular componenti

  • basolateral plasma membrane Source: Ensembl
  • cornified envelope Source: UniProtKB
  • cytoplasm Source: UniProtKB-KW
  • desmosome Source: UniProtKB-SubCell
  • extracellular exosome Source: UniProtKB
  • extracellular matrix Source: BHF-UCL
  • fascia adherens Source: Ensembl
  • intercalated disc Source: UniProtKB
  • intermediate filament Source: Ensembl
  • nucleus Source: UniProtKB
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Involvement in diseasei

Keratoderma, palmoplantar, striate 2 (SPPK2)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:612908
Cardiomyopathy, dilated, with woolly hair and keratoderma (DCWHK)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal recessive cardiocutaneous syndrome characterized by a generalized striate keratoderma particularly affecting the palmoplantar epidermis, woolly hair, and dilated left ventricular cardiomyopathy.
See also OMIM:605676
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_072432564T → I in DCWHKTA. 1 PublicationCorresponds to variant rs606231295dbSNPEnsembl.1
Natural variantiVAR_072433597S → L in DCWHKTA. 1 PublicationCorresponds to variant rs606231294dbSNPEnsembl.1
Arrhythmogenic right ventricular dysplasia, familial, 8 (ARVD8)3 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:607450
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_015402299S → R in ARVD8. 3 PublicationsCorresponds to variant rs121912992dbSNPEnsembl.1
Natural variantiVAR_065693445I → V in ARVD8. 1
Natural variantiVAR_0238141255R → K in ARVD8. 2 PublicationsCorresponds to variant rs777407386dbSNPEnsembl.1
Natural variantiVAR_0238161775R → I in ARVD8. 2 PublicationsCorresponds to variant rs34738426dbSNPEnsembl.1
Skin fragility-woolly hair syndrome (SFWHS)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn 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.
See also OMIM:607655
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_015569287N → K in SFWHS. 1 PublicationCorresponds to variant rs121912993dbSNPEnsembl.1
Natural variantiVAR_0155702366R → C in SFWHS. 1 PublicationCorresponds to variant rs28931610dbSNPEnsembl.1
Epidermolysis bullosa, lethal acantholytic (EBLA)
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:609638
Cardiomyopathy, dilated, with woolly hair, keratoderma, and tooth agenesis (DCWHKTA)3 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA cardiocutaneous syndrome characterized by biventricular dilated cardiomyopathy, hyperkeratosis, woolly hair, palmoplantar keratoderma, and hypo/oligodontia.
See also OMIM:615821
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_072432564T → I in DCWHKTA. 1 PublicationCorresponds to variant rs606231295dbSNPEnsembl.1
Natural variantiVAR_072433597S → L in DCWHKTA. 1 PublicationCorresponds to variant rs606231294dbSNPEnsembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi2849S → G: Increases association with KRT5-KRT14, KRT8-KRT18 or VIM intermediate filaments. 1 Publication1

Keywords - Diseasei

Cardiomyopathy, Disease mutation, Epidermolysis bullosa, Palmoplantar keratoderma

Organism-specific databases

DisGeNETi1832.
MalaCardsiDSP.
MIMi605676. phenotype.
607450. phenotype.
607655. phenotype.
609638. phenotype.
612908. phenotype.
615821. phenotype.
OpenTargetsiENSG00000096696.
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.
2032. Idiopathic pulmonary fibrosis.
50942. Keratosis palmoplantaris striata.
158687. Lethal acantholytic epidermolysis bullosa.
293165. Skin fragility-woolly hair-palmoplantar keratoderma syndrome.
65282. Woolly hair-palmoplantar keratoderma-dilated cardiomyopathy syndrome.
PharmGKBiPA27505.

Polymorphism and mutation databases

BioMutaiDSP.
DMDMi115502381.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000781441 – 2871DesmoplakinAdd BLAST2871

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei22PhosphoserineCombined sources1
Modified residuei53PhosphoserineCombined sources1
Modified residuei56PhosphotyrosineBy similarity1
Modified residuei61PhosphothreonineBy similarity1
Modified residuei165PhosphoserineCombined sources1
Modified residuei166PhosphoserineCombined sources1
Modified residuei176PhosphoserineCombined sources1
Modified residuei1658PhosphoserineCombined sources1
Modified residuei1708PhosphoserineCombined sources1
Modified residuei2024PhosphoserineCombined sources1
Modified residuei2207PhosphoserineCombined sources1
Modified residuei2209PhosphoserineCombined sources1
Modified residuei2225PhosphoserineCombined sources1
Lipidationi2480Omega-hydroxyceramide glutamate esterSequence analysis1
Modified residuei2810PhosphoserineCombined sources1
Modified residuei2815PhosphoserineCombined sources1
Modified residuei2817PhosphotyrosineCombined sources1
Modified residuei2820PhosphoserineCombined sources1
Modified residuei2821PhosphoserineCombined sources1
Modified residuei2825PhosphoserineCombined sources1
Modified residuei2826Omega-N-methylarginineBy similarity1
Modified residuei2847Omega-N-methylarginineBy similarity1
Modified residuei2849PhosphoserineCombined sources1
Modified residuei2853PhosphothreonineCombined sources1
Modified residuei2868PhosphoserineCombined sources1

Post-translational modificationi

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.
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).1 Publication

Keywords - PTMi

Lipoprotein, Methylation, Phosphoprotein

Proteomic databases

EPDiP15924.
MaxQBiP15924.
PaxDbiP15924.
PeptideAtlasiP15924.
PRIDEiP15924.

PTM databases

iPTMnetiP15924.
PhosphoSitePlusiP15924.
SwissPalmiP15924.

Expressioni

Tissue specificityi

Isoform DPI is apparently an obligate constituent of all desmosomes. Isoform DPII resides predominantly in tissues and cells of stratified origin.

Gene expression databases

BgeeiENSG00000096696.
CleanExiHS_DSP.
GenevisibleiP15924. HS.

Organism-specific databases

HPAiCAB037324.
HPA045840.
HPA054950.

Interactioni

Subunit structurei

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. Interacts weakly with TMEM65 (By similarity).By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
MAPRE1Q156917EBI-355041,EBI-1004115
PKP1Q13835-22EBI-355041,EBI-9087684

GO - Molecular functioni

  • cell adhesive protein binding involved in bundle of His cell-Purkinje myocyte communication Source: BHF-UCL
  • protein binding, bridging Source: UniProtKB
  • protein kinase C binding Source: BHF-UCL
  • scaffold protein binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi108166. 86 interactors.
DIPiDIP-109N.
IntActiP15924. 51 interactors.
MINTiMINT-1157663.
STRINGi9606.ENSP00000369129.

Structurei

Secondary structure

12871
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi182 – 201Combined sources20
Helixi211 – 241Combined sources31
Helixi245 – 294Combined sources50
Helixi307 – 338Combined sources32
Helixi344 – 402Combined sources59
Helixi411 – 442Combined sources32
Helixi449 – 451Combined sources3
Beta strandi462 – 467Combined sources6
Beta strandi469 – 471Combined sources3
Beta strandi474 – 476Combined sources3
Beta strandi481 – 486Combined sources6
Beta strandi488 – 496Combined sources9
Beta strandi498 – 500Combined sources3
Beta strandi503 – 506Combined sources4
Helixi507 – 509Combined sources3
Helixi517 – 561Combined sources45
Helixi565 – 568Combined sources4
Turni573 – 575Combined sources3
Helixi576 – 594Combined sources19
Helixi602 – 624Combined sources23
Helixi1963 – 1965Combined sources3
Beta strandi1967 – 1969Combined sources3
Beta strandi1971 – 1976Combined sources6
Helixi1977 – 1982Combined sources6
Helixi1988 – 1996Combined sources9
Beta strandi1997 – 1999Combined sources3
Helixi2001 – 2005Combined sources5
Helixi2009 – 2012Combined sources4
Beta strandi2018 – 2021Combined sources4
Beta strandi2023 – 2027Combined sources5
Helixi2031 – 2036Combined sources6
Helixi2042 – 2054Combined sources13
Turni2061 – 2063Combined sources3
Helixi2069 – 2074Combined sources6
Helixi2083 – 2094Combined sources12
Turni2099 – 2101Combined sources3
Helixi2107 – 2112Combined sources6
Helixi2118 – 2129Combined sources12
Turni2130 – 2132Combined sources3
Beta strandi2133 – 2136Combined sources4
Turni2137 – 2140Combined sources4
Beta strandi2141 – 2143Combined sources3
Helixi2145 – 2150Combined sources6
Helixi2156 – 2161Combined sources6
Turni2165 – 2168Combined sources4
Beta strandi2175 – 2177Combined sources3
Helixi2183 – 2187Combined sources5
Beta strandi2190 – 2192Combined sources3
Turni2194 – 2196Combined sources3
Beta strandi2199 – 2201Combined sources3
Beta strandi2209 – 2211Combined sources3
Beta strandi2213 – 2218Combined sources6
Helixi2219 – 2224Combined sources6
Helixi2230 – 2237Combined sources8
Helixi2243 – 2249Combined sources7
Helixi2251 – 2254Combined sources4
Beta strandi2260 – 2265Combined sources6
Turni2266 – 2269Combined sources4
Beta strandi2270 – 2272Combined sources3
Helixi2274 – 2280Combined sources7
Helixi2285 – 2296Combined sources12
Beta strandi2301 – 2303Combined sources3
Turni2304 – 2307Combined sources4
Beta strandi2308 – 2310Combined sources3
Helixi2312 – 2317Combined sources6
Helixi2326 – 2332Combined sources7
Helixi2334 – 2337Combined sources4
Turni2342 – 2344Combined sources3
Beta strandi2346 – 2348Combined sources3
Helixi2350 – 2355Combined sources6
Helixi2361 – 2372Combined sources12
Turni2373 – 2375Combined sources3
Beta strandi2376 – 2379Combined sources4
Turni2380 – 2383Combined sources4
Beta strandi2384 – 2386Combined sources3
Helixi2390 – 2393Combined sources4
Helixi2399 – 2406Combined sources8
Turni2410 – 2412Combined sources3
Beta strandi2415 – 2417Combined sources3
Turni2418 – 2421Combined sources4
Beta strandi2422 – 2424Combined sources3
Helixi2426 – 2430Combined sources5
Turni2437 – 2439Combined sources3
Beta strandi2442 – 2446Combined sources5
Beta strandi2619 – 2624Combined sources6
Turni2625 – 2628Combined sources4
Beta strandi2629 – 2631Combined sources3
Helixi2633 – 2638Combined sources6
Helixi2644 – 2655Combined sources12
Turni2656 – 2658Combined sources3
Beta strandi2659 – 2661Combined sources3
Turni2663 – 2665Combined sources3
Helixi2671 – 2676Combined sources6
Helixi2682 – 2696Combined sources15
Helixi2709 – 2714Combined sources6
Helixi2720 – 2732Combined sources13
Helixi2739 – 2741Combined sources3
Helixi2747 – 2752Combined sources6
Helixi2758 – 2765Combined sources8
Helixi2767 – 2769Combined sources3
Turni2777 – 2779Combined sources3
Helixi2785 – 2791Combined sources7
Turni2796 – 2798Combined sources3
Beta strandi2801 – 2805Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1LM5X-ray1.80A/B2609-2822[»]
1LM7X-ray3.00A/B2209-2456[»]
3R6NX-ray2.95A/B178-627[»]
5DZZX-ray2.60A1960-2448[»]
ProteinModelPortaliP15924.
SMRiP15924.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP15924.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati178 – 271Spectrin 1Add BLAST94
Repeati272 – 375Spectrin 2Add BLAST104
Repeati376 – 446Spectrin 3aAdd BLAST71
Domaini447 – 515SH3Add BLAST69
Repeati516 – 545Spectrin 3bAdd BLAST30
Repeati546 – 627Spectrin 4Add BLAST82
Repeati654 – 769Spectrin 5Add BLAST116
Repeati770 – 883Spectrin 6Add BLAST114
Repeati2009 – 2045Plectin 1Add BLAST37
Repeati2046 – 2083Plectin 2Add BLAST38
Repeati2084 – 2121Plectin 3Add BLAST38
Repeati2122 – 2159Plectin 4Add BLAST38
Repeati2163 – 2197Plectin 5Add BLAST35
Repeati2198 – 2233Plectin 6Add BLAST36
Repeati2251 – 2288Plectin 7Add BLAST38
Repeati2289 – 2326Plectin 8Add BLAST38
Repeati2327 – 2364Plectin 9Add BLAST38
Repeati2365 – 2402Plectin 10Add BLAST38
Repeati2406 – 2440Plectin 11Add BLAST35
Repeati2456 – 2493Plectin 12Add BLAST38
Repeati2507 – 2544Plectin 13Add BLAST38
Repeati2610 – 2647Plectin 14Add BLAST38
Repeati2648 – 2685Plectin 15Add BLAST38
Repeati2724 – 2761Plectin 16Add BLAST38
Repeati2762 – 2799Plectin 17Add BLAST38

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 1056Globular 1Add BLAST1056
Regioni1 – 584Interaction with plakophilin 1 and junction plakoglobinAdd BLAST584
Regioni1057 – 1945Central fibrous rod domainAdd BLAST889
Regioni1946 – 2871Globular 2Add BLAST926
Regioni1960 – 22084.5 X 38 AA tandem repeats (Domain A)Add BLAST249
Regioni2244 – 24464.5 X 38 AA tandem repeats (Domain B)Add BLAST203
Regioni2609 – 28224.5 X 38 AA tandem repeats (Domain C)Add BLAST214
Regioni2824 – 28476 X 4 AA tandem repeats of G-S-R-[SR]Add BLAST24

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili1018 – 1945Sequence analysisAdd BLAST928

Domaini

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.
The N-terminal region is required for localization to the desmosomal plaque and interacts with the N-terminal region of plakophilin 1.
The three tandem plakin repeat regions in the C-terminus mediate binding to intermediate filaments.

Sequence similaritiesi

Belongs to the plakin or cytolinker family.Curated
Contains 17 plectin repeats.Curated
Contains 1 SH3 domain.Curated
Contains 6 spectrin repeats.Curated

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiENOG410IQBR. Eukaryota.
ENOG4111ACS. LUCA.
GeneTreeiENSGT00760000119163.
HOGENOMiHOG000112198.
HOVERGENiHBG081434.
InParanoidiP15924.
KOiK10381.
OMAiKRSMSFQ.
OrthoDBiEOG091G003R.
PhylomeDBiP15924.
TreeFamiTF106435.

Family and domain databases

Gene3Di3.90.1290.10. 5 hits.
InterProiIPR028462. Desmoplakin.
IPR001101. Plectin_repeat.
IPR018159. Spectrin/alpha-actinin.
[Graphical view]
PANTHERiPTHR11915:SF234. PTHR11915:SF234. 1 hit.
PfamiPF00681. Plectin. 8 hits.
[Graphical view]
SMARTiSM00250. PLEC. 18 hits.
SM00150. SPEC. 3 hits.
[Graphical view]
SUPFAMiSSF75399. SSF75399. 5 hits.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform DPI (identifier: P15924-1) [UniParc]FASTAAdd to basket
Also known as: DP1

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSCNGGSHPR INTLGRMIRA ESGPDLRYEV TSGGGGTSRM YYSRRGVITD
60 70 80 90 100
QNSDGYCQTG TMSRHQNQNT IQELLQNCSD CLMRAELIVQ PELKYGDGIQ
110 120 130 140 150
LTRSRELDEC FAQANDQMEI LDSLIREMRQ MGQPCDAYQK RLLQLQEQMR
160 170 180 190 200
ALYKAISVPR VRRASSKGGG GYTCQSGSGW DEFTKHVTSE CLGWMRQQRA
210 220 230 240 250
EMDMVAWGVD LASVEQHINS HRGIHNSIGD YRWQLDKIKA DLREKSAIYQ
260 270 280 290 300
LEEEYENLLK ASFERMDHLR QLQNIIQATS REIMWINDCE EEELLYDWSD
310 320 330 340 350
KNTNIAQKQE AFSIRMSQLE VKEKELNKLK QESDQLVLNQ HPASDKIEAY
360 370 380 390 400
MDTLQTQWSW ILQITKCIDV HLKENAAYFQ FFEEAQSTEA YLKGLQDSIR
410 420 430 440 450
KKYPCDKNMP LQHLLEQIKE LEKEREKILE YKRQVQNLVN KSKKIVQLKP
460 470 480 490 500
RNPDYRSNKP IILRALCDYK QDQKIVHKGD ECILKDNNER SKWYVTGPGG
510 520 530 540 550
VDMLVPSVGL IIPPPNPLAV DLSCKIEQYY EAILALWNQL YINMKSLVSW
560 570 580 590 600
HYCMIDIEKI RAMTIAKLKT MRQEDYMKTI ADLELHYQEF IRNSQGSEMF
610 620 630 640 650
GDDDKRKIQS QFTDAQKHYQ TLVIQLPGYP QHQTVTTTEI THHGTCQDVN
660 670 680 690 700
HNKVIETNRE NDKQETWMLM ELQKIRRQIE HCEGRMTLKN LPLADQGSSH
710 720 730 740 750
HITVKINELK SVQNDSQAIA EVLNQLKDML ANFRGSEKYC YLQNEVFGLF
760 770 780 790 800
QKLENINGVT DGYLNSLCTV RALLQAILQT EDMLKVYEAR LTEEETVCLD
810 820 830 840 850
LDKVEAYRCG LKKIKNDLNL KKSLLATMKT ELQKAQQIHS QTSQQYPLYD
860 870 880 890 900
LDLGKFGEKV TQLTDRWQRI DKQIDFRLWD LEKQIKQLRN YRDNYQAFCK
910 920 930 940 950
WLYDAKRRQD SLESMKFGDS NTVMRFLNEQ KNLHSEISGK RDKSEEVQKI
960 970 980 990 1000
AELCANSIKD YELQLASYTS GLETLLNIPI KRTMIQSPSG VILQEAADVH
1010 1020 1030 1040 1050
ARYIELLTRS GDYYRFLSEM LKSLEDLKLK NTKIEVLEEE LRLARDANSE
1060 1070 1080 1090 1100
NCNKNKFLDQ NLQKYQAECS QFKAKLASLE ELKRQAELDG KSAKQNLDKC
1110 1120 1130 1140 1150
YGQIKELNEK ITRLTYEIED EKRRRKSVED RFDQQKNDYD QLQKARQCEK
1160 1170 1180 1190 1200
ENLGWQKLES EKAIKEKEYE IERLRVLLQE EGTRKREYEN ELAKVRNHYN
1210 1220 1230 1240 1250
EEMSNLRNKY ETEINITKTT IKEISMQKED DSKNLRNQLD RLSRENRDLK
1260 1270 1280 1290 1300
DEIVRLNDSI LQATEQRRRA EENALQQKAC GSEIMQKKQH LEIELKQVMQ
1310 1320 1330 1340 1350
QRSEDNARHK QSLEEAAKTI QDKNKEIERL KAEFQEEAKR RWEYENELSK
1360 1370 1380 1390 1400
VRNNYDEEII SLKNQFETEI NITKTTIHQL TMQKEEDTSG YRAQIDNLTR
1410 1420 1430 1440 1450
ENRSLSEEIK RLKNTLTQTT ENLRRVEEDI QQQKATGSEV SQRKQQLEVE
1460 1470 1480 1490 1500
LRQVTQMRTE ESVRYKQSLD DAAKTIQDKN KEIERLKQLI DKETNDRKCL
1510 1520 1530 1540 1550
EDENARLQRV QYDLQKANSS ATETINKLKV QEQELTRLRI DYERVSQERT
1560 1570 1580 1590 1600
VKDQDITRFQ NSLKELQLQK QKVEEELNRL KRTASEDSCK RKKLEEELEG
1610 1620 1630 1640 1650
MRRSLKEQAI KITNLTQQLE QASIVKKRSE DDLRQQRDVL DGHLREKQRT
1660 1670 1680 1690 1700
QEELRRLSSE VEALRRQLLQ EQESVKQAHL RNEHFQKAIE DKSRSLNESK
1710 1720 1730 1740 1750
IEIERLQSLT ENLTKEHLML EEELRNLRLE YDDLRRGRSE ADSDKNATIL
1760 1770 1780 1790 1800
ELRSQLQISN NRTLELQGLI NDLQRERENL RQEIEKFQKQ ALEASNRIQE
1810 1820 1830 1840 1850
SKNQCTQVVQ ERESLLVKIK VLEQDKARLQ RLEDELNRAK STLEAETRVK
1860 1870 1880 1890 1900
QRLECEKQQI QNDLNQWKTQ YSRKEEAIRK IESEREKSER EKNSLRSEIE
1910 1920 1930 1940 1950
RLQAEIKRIE ERCRRKLEDS TRETQSQLET ERSRYQREID KLRQRPYGSH
1960 1970 1980 1990 2000
RETQTECEWT VDTSKLVFDG LRKKVTAMQL YECQLIDKTT LDKLLKGKKS
2010 2020 2030 2040 2050
VEEVASEIQP FLRGAGSIAG ASASPKEKYS LVEAKRKKLI SPESTVMLLE
2060 2070 2080 2090 2100
AQAATGGIID PHRNEKLTVD SAIARDLIDF DDRQQIYAAE KAITGFDDPF
2110 2120 2130 2140 2150
SGKTVSVSEA IKKNLIDRET GMRLLEAQIA SGGVVDPVNS VFLPKDVALA
2160 2170 2180 2190 2200
RGLIDRDLYR SLNDPRDSQK NFVDPVTKKK VSYVQLKERC RIEPHTGLLL
2210 2220 2230 2240 2250
LSVQKRSMSF QGIRQPVTVT ELVDSGILRP STVNELESGQ ISYDEVGERI
2260 2270 2280 2290 2300
KDFLQGSSCI AGIYNETTKQ KLGIYEAMKI GLVRPGTALE LLEAQAATGF
2310 2320 2330 2340 2350
IVDPVSNLRL PVEEAYKRGL VGIEFKEKLL SAERAVTGYN DPETGNIISL
2360 2370 2380 2390 2400
FQAMNKELIE KGHGIRLLEA QIATGGIIDP KESHRLPVDI AYKRGYFNEE
2410 2420 2430 2440 2450
LSEILSDPSD DTKGFFDPNT EENLTYLQLK ERCIKDEETG LCLLPLKEKK
2460 2470 2480 2490 2500
KQVQTSQKNT LRKRRVVIVD PETNKEMSVQ EAYKKGLIDY ETFKELCEQE
2510 2520 2530 2540 2550
CEWEEITITG SDGSTRVVLV DRKTGSQYDI QDAIDKGLVD RKFFDQYRSG
2560 2570 2580 2590 2600
SLSLTQFADM ISLKNGVGTS SSMGSGVSDD VFSSSRHESV SKISTISSVR
2610 2620 2630 2640 2650
NLTIRSSSFS DTLEESSPIA AIFDTENLEK ISITEGIERG IVDSITGQRL
2660 2670 2680 2690 2700
LEAQACTGGI IHPTTGQKLS LQDAVSQGVI DQDMATRLKP AQKAFIGFEG
2710 2720 2730 2740 2750
VKGKKKMSAA EAVKEKWLPY EAGQRFLEFQ YLTGGLVDPE VHGRISTEEA
2760 2770 2780 2790 2800
IRKGFIDGRA AQRLQDTSSY AKILTCPKTK LKISYKDAIN RSMVEDITGL
2810 2820 2830 2840 2850
RLLEAASVSS KGLPSPYNMS SAPGSRSGSR SGSRSGSRSG SRSGSRRGSF
2860 2870
DATGNSSYSY SYSFSSSSIG H
Length:2,871
Mass (Da):331,774
Last modified:October 3, 2006 - v3
Checksum:i5770CC6B4F9F9F7B
GO
Isoform DPII (identifier: P15924-2) [UniParc]FASTAAdd to basket
Also known as: DP2

The sequence of this isoform differs from the canonical sequence as follows:
     1195-1793: Missing.

Show »
Length:2,272
Mass (Da):260,119
Checksum:i84F0CD39B48E1339
GO
Isoform DSPIa (identifier: P15924-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1351-1793: Missing.

Note: Minor isoform.
Show »
Length:2,428
Mass (Da):278,916
Checksum:iB26951DA08A0620C
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti905A → R in AAA85135 (PubMed:1731325).Curated1
Sequence conflicti1120D → R in AAA35766 (PubMed:1689290).Curated1
Sequence conflicti2687 – 2688RL → SV in AAA85135 (PubMed:1731325).Curated2
Sequence conflicti2687 – 2688RL → SV in AAA35766 (PubMed:1689290).Curated2

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_015569287N → K in SFWHS. 1 PublicationCorresponds to variant rs121912993dbSNPEnsembl.1
Natural variantiVAR_015402299S → R in ARVD8. 3 PublicationsCorresponds to variant rs121912992dbSNPEnsembl.1
Natural variantiVAR_033862305I → F.2 PublicationsCorresponds to variant rs17604693dbSNPEnsembl.1
Natural variantiVAR_065693445I → V in ARVD8. 1
Natural variantiVAR_072432564T → I in DCWHKTA. 1 PublicationCorresponds to variant rs606231295dbSNPEnsembl.1
Natural variantiVAR_072433597S → L in DCWHKTA. 1 PublicationCorresponds to variant rs606231294dbSNPEnsembl.1
Natural variantiVAR_0238141255R → K in ARVD8. 2 PublicationsCorresponds to variant rs777407386dbSNPEnsembl.1
Natural variantiVAR_0656941505A → V.1 PublicationCorresponds to variant rs375919492dbSNPEnsembl.1
Natural variantiVAR_0204681512Y → C.2 PublicationsCorresponds to variant rs2076299dbSNPEnsembl.1
Natural variantiVAR_0656951526N → K.2 PublicationsCorresponds to variant rs28763966dbSNPEnsembl.1
Natural variantiVAR_0656961537R → C.2 PublicationsCorresponds to variant rs28763967dbSNPEnsembl.1
Natural variantiVAR_0238151738R → Q.2 PublicationsCorresponds to variant rs6929069dbSNPEnsembl.1
Natural variantiVAR_0238161775R → I in ARVD8. 2 PublicationsCorresponds to variant rs34738426dbSNPEnsembl.1
Natural variantiVAR_0656971833E → V.2 PublicationsCorresponds to variant rs78652302dbSNPEnsembl.1
Natural variantiVAR_0155702366R → C in SFWHS. 1 PublicationCorresponds to variant rs28931610dbSNPEnsembl.1
Natural variantiVAR_0181582375G → R in a case of recessive arrhythmogenic right ventricular cardiomyopathy with skin abnormalities and woolly hair. 1 PublicationCorresponds to variant rs376923069dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0050701195 – 1793Missing in isoform DPII. 1 PublicationAdd BLAST599
Alternative sequenceiVSP_0537691351 – 1793Missing in isoform DSPIa. 1 PublicationAdd BLAST443

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M77830 mRNA. Translation: AAA85135.1.
HM151899 mRNA. Translation: ADI58529.1.
AL031058 Genomic DNA. Translation: CAA19927.1.
BC140802 mRNA. Translation: AAI40803.1.
J05211 mRNA. Translation: AAA35766.1.
AF139065 mRNA. Translation: AAF19785.1.
CCDSiCCDS4501.1. [P15924-1]
CCDS47368.1. [P15924-2]
PIRiA38194.
RefSeqiNP_001008844.1. NM_001008844.2. [P15924-2]
NP_001305963.1. NM_001319034.1. [P15924-3]
NP_004406.2. NM_004415.3. [P15924-1]
UniGeneiHs.519873.

Genome annotation databases

EnsembliENST00000379802; ENSP00000369129; ENSG00000096696. [P15924-1]
ENST00000418664; ENSP00000396591; ENSG00000096696. [P15924-2]
GeneIDi1832.
KEGGihsa:1832.
UCSCiuc003mxp.2. human. [P15924-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Desmoplakin entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M77830 mRNA. Translation: AAA85135.1.
HM151899 mRNA. Translation: ADI58529.1.
AL031058 Genomic DNA. Translation: CAA19927.1.
BC140802 mRNA. Translation: AAI40803.1.
J05211 mRNA. Translation: AAA35766.1.
AF139065 mRNA. Translation: AAF19785.1.
CCDSiCCDS4501.1. [P15924-1]
CCDS47368.1. [P15924-2]
PIRiA38194.
RefSeqiNP_001008844.1. NM_001008844.2. [P15924-2]
NP_001305963.1. NM_001319034.1. [P15924-3]
NP_004406.2. NM_004415.3. [P15924-1]
UniGeneiHs.519873.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1LM5X-ray1.80A/B2609-2822[»]
1LM7X-ray3.00A/B2209-2456[»]
3R6NX-ray2.95A/B178-627[»]
5DZZX-ray2.60A1960-2448[»]
ProteinModelPortaliP15924.
SMRiP15924.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108166. 86 interactors.
DIPiDIP-109N.
IntActiP15924. 51 interactors.
MINTiMINT-1157663.
STRINGi9606.ENSP00000369129.

PTM databases

iPTMnetiP15924.
PhosphoSitePlusiP15924.
SwissPalmiP15924.

Polymorphism and mutation databases

BioMutaiDSP.
DMDMi115502381.

Proteomic databases

EPDiP15924.
MaxQBiP15924.
PaxDbiP15924.
PeptideAtlasiP15924.
PRIDEiP15924.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000379802; ENSP00000369129; ENSG00000096696. [P15924-1]
ENST00000418664; ENSP00000396591; ENSG00000096696. [P15924-2]
GeneIDi1832.
KEGGihsa:1832.
UCSCiuc003mxp.2. human. [P15924-1]

Organism-specific databases

CTDi1832.
DisGeNETi1832.
GeneCardsiDSP.
GeneReviewsiDSP.
HGNCiHGNC:3052. DSP.
HPAiCAB037324.
HPA045840.
HPA054950.
MalaCardsiDSP.
MIMi125647. gene.
605676. phenotype.
607450. phenotype.
607655. phenotype.
609638. phenotype.
612908. phenotype.
615821. phenotype.
neXtProtiNX_P15924.
OpenTargetsiENSG00000096696.
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.
2032. Idiopathic pulmonary fibrosis.
50942. Keratosis palmoplantaris striata.
158687. Lethal acantholytic epidermolysis bullosa.
293165. Skin fragility-woolly hair-palmoplantar keratoderma syndrome.
65282. Woolly hair-palmoplantar keratoderma-dilated cardiomyopathy syndrome.
PharmGKBiPA27505.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IQBR. Eukaryota.
ENOG4111ACS. LUCA.
GeneTreeiENSGT00760000119163.
HOGENOMiHOG000112198.
HOVERGENiHBG081434.
InParanoidiP15924.
KOiK10381.
OMAiKRSMSFQ.
OrthoDBiEOG091G003R.
PhylomeDBiP15924.
TreeFamiTF106435.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000096696-MONOMER.
ReactomeiR-HSA-351906. Apoptotic cleavage of cell adhesion proteins.
R-HSA-6798695. Neutrophil degranulation.
R-HSA-6805567. Keratinization.
R-HSA-6809371. Formation of the cornified envelope.
SIGNORiP15924.

Miscellaneous databases

ChiTaRSiDSP. human.
EvolutionaryTraceiP15924.
GeneWikiiDesmoplakin.
GenomeRNAii1832.
PROiP15924.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000096696.
CleanExiHS_DSP.
GenevisibleiP15924. HS.

Family and domain databases

Gene3Di3.90.1290.10. 5 hits.
InterProiIPR028462. Desmoplakin.
IPR001101. Plectin_repeat.
IPR018159. Spectrin/alpha-actinin.
[Graphical view]
PANTHERiPTHR11915:SF234. PTHR11915:SF234. 1 hit.
PfamiPF00681. Plectin. 8 hits.
[Graphical view]
SMARTiSM00250. PLEC. 18 hits.
SM00150. SPEC. 3 hits.
[Graphical view]
SUPFAMiSSF75399. SSF75399. 5 hits.
ProtoNetiSearch...

Entry informationi

Entry nameiDESP_HUMAN
AccessioniPrimary (citable) accession number: P15924
Secondary accession number(s): B2RTT2
, D7RX09, O75993, Q14189, Q9UHN4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: October 3, 2006
Last modified: November 30, 2016
This is version 208 of the entry and version 3 of the sequence. [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 6
    Human chromosome 6: 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
  6. SIMILARITY comments
    Index of protein domains and families

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.