SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P15924

- DESP_HUMAN

UniProt

P15924 - DESP_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Desmoplakin
Gene
DSP
Organism
Homo sapiens (Human)
Status
Reviewed - 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

  1. poly(A) RNA binding Source: UniProtKB
  2. protein binding Source: UniProtKB
  3. protein binding, bridging Source: UniProtKB
  4. protein kinase C binding Source: BHF-UCL
  5. scaffold protein binding Source: BHF-UCL
  6. structural constituent of cytoskeleton Source: ProtInc
  7. structural molecule activity Source: UniProtKB

GO - Biological processi

  1. adherens junction organization Source: Ensembl
  2. apoptotic process Source: Reactome
  3. bundle of His cell to Purkinje myocyte communication Source: BHF-UCL
  4. cellular component disassembly involved in execution phase of apoptosis Source: Reactome
  5. desmosome organization Source: BHF-UCL
  6. epidermis development Source: ProtInc
  7. intermediate filament organization Source: BHF-UCL
  8. keratinocyte differentiation Source: UniProtKB
  9. peptide cross-linking Source: UniProtKB
  10. protein localization to adherens junction Source: BHF-UCL
  11. regulation of heart rate by cardiac conduction Source: BHF-UCL
  12. single organismal cell-cell adhesion Source: Ensembl
  13. ventricular cardiac muscle cell action potential Source: BHF-UCL
  14. ventricular compact myocardium morphogenesis Source: BHF-UCL
  15. wound healing Source: Ensembl
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_13579. Apoptotic cleavage of cell adhesion proteins.

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
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:3052. DSP.

Subcellular locationi

Cell junctiondesmosome. Cytoplasmcytoskeleton
Note: Innermost portion of the desmosomal plaque. Colocalizes with epidermal KRT5-KRT14 and simple KRT8-KRT18 keratins and VIM intermediate filaments network.1 Publication

GO - Cellular componenti

  1. basolateral plasma membrane Source: Ensembl
  2. cornified envelope Source: UniProtKB
  3. desmosome Source: UniProtKB-SubCell
  4. extracellular vesicular exosome Source: UniProt
  5. fascia adherens Source: Ensembl
  6. intercalated disc Source: BHF-UCL
  7. intermediate filament Source: Ensembl
  8. mitochondrion Source: Ensembl
  9. nucleus Source: UniProt
  10. plasma membrane Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasm, Cytoskeleton

Pathology & Biotechi

Involvement in diseasei

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
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.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
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.
Note: The disease is caused by mutations affecting the gene represented in this entry.3 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti299 – 2991S → R in ARVD8. 3 Publications
Corresponds to variant rs121912992 [ dbSNP | Ensembl ].
VAR_015402
Natural varianti445 – 4451I → V in ARVD8.
VAR_065693
Natural varianti1255 – 12551R → K in ARVD8. 2 Publications
VAR_023814
Natural varianti1775 – 17751R → I in ARVD8. 2 Publications
Corresponds to variant rs34738426 [ dbSNP | Ensembl ].
VAR_023816
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.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti287 – 2871N → K in SFWHS. 1 Publication
VAR_015569
Natural varianti2366 – 23661R → C in SFWHS. 1 Publication
Corresponds to variant rs28931610 [ dbSNP | Ensembl ].
VAR_015570
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.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi2849 – 28491S → G: Increases association with KRT5-KRT14, KRT8-KRT18 or VIM intermediate filaments. 1 Publication

Keywords - Diseasei

Cardiomyopathy, Disease mutation, Epidermolysis bullosa, Palmoplantar keratoderma

Organism-specific databases

MIMi605676. phenotype.
607450. phenotype.
607655. phenotype.
609638. phenotype.
612908. phenotype.
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.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 28712871Desmoplakin
PRO_0000078144Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei22 – 221Phosphoserine1 Publication
Modified residuei165 – 1651Phosphoserine1 Publication
Modified residuei166 – 1661Phosphoserine1 Publication
Modified residuei176 – 1761Phosphoserine1 Publication
Modified residuei2024 – 20241Phosphoserine2 Publications
Modified residuei2207 – 22071Phosphoserine1 Publication
Modified residuei2209 – 22091Phosphoserine3 Publications
Lipidationi2480 – 24801Omega-hydroxyceramide glutamate ester Reviewed prediction
Modified residuei2815 – 28151Phosphoserine2 Publications
Modified residuei2820 – 28201Phosphoserine1 Publication
Modified residuei2821 – 28211Phosphoserine1 Publication
Modified residuei2825 – 28251Phosphoserine4 Publications
Modified residuei2849 – 28491Phosphoserine1 Publication
Modified residuei2853 – 28531Phosphothreonine1 Publication
Modified residuei2868 – 28681Phosphoserine1 Publication

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 (1 Publication).

Keywords - PTMi

Lipoprotein, Phosphoprotein

Proteomic databases

MaxQBiP15924.
PaxDbiP15924.
PeptideAtlasiP15924.
PRIDEiP15924.

PTM databases

PhosphoSiteiP15924.

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

ArrayExpressiP15924.
BgeeiP15924.
CleanExiHS_DSP.
GenevestigatoriP15924.

Organism-specific databases

HPAiCAB037324.

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 PKP2.3 Publications

Binary interactionsi

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

Protein-protein interaction databases

BioGridi108166. 51 interactions.
DIPiDIP-109N.
IntActiP15924. 21 interactions.
MINTiMINT-1157663.
STRINGi9606.ENSP00000369129.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi182 – 20120
Helixi211 – 24131
Helixi245 – 29450
Helixi307 – 33832
Helixi344 – 40259
Helixi411 – 44232
Helixi449 – 4513
Beta strandi462 – 4676
Beta strandi469 – 4713
Beta strandi474 – 4763
Beta strandi481 – 4866
Beta strandi488 – 4969
Beta strandi498 – 5003
Beta strandi503 – 5064
Helixi507 – 5093
Helixi517 – 56145
Helixi565 – 5684
Turni573 – 5753
Helixi576 – 59419
Helixi602 – 62423
Beta strandi2213 – 22175
Helixi2219 – 22246
Helixi2230 – 22378
Helixi2246 – 22494
Helixi2251 – 22544
Beta strandi2260 – 22656
Turni2266 – 22694
Beta strandi2270 – 22734
Helixi2274 – 22785
Beta strandi2279 – 22835
Helixi2285 – 229612
Beta strandi2301 – 23033
Turni2304 – 23074
Beta strandi2308 – 23103
Helixi2312 – 23176
Turni2323 – 233311
Helixi2334 – 23374
Turni2342 – 23443
Helixi2350 – 23545
Turni2355 – 23573
Helixi2361 – 237212
Turni2373 – 23753
Beta strandi2376 – 23783
Turni2380 – 23823
Beta strandi2384 – 23863
Helixi2388 – 23936
Helixi2399 – 24068
Beta strandi2414 – 24174
Turni2418 – 24214
Beta strandi2422 – 24243
Helixi2426 – 24316
Turni2437 – 24393
Beta strandi2442 – 24465
Beta strandi2619 – 26246
Turni2625 – 26284
Beta strandi2629 – 26313
Helixi2633 – 26386
Helixi2644 – 265512
Turni2656 – 26583
Beta strandi2659 – 26613
Turni2663 – 26653
Helixi2671 – 26766
Helixi2682 – 269615
Helixi2709 – 27146
Helixi2720 – 273213
Helixi2739 – 27413
Helixi2747 – 27526
Helixi2758 – 27658
Helixi2767 – 27693
Turni2777 – 27793
Helixi2785 – 27917
Turni2796 – 27983
Beta strandi2801 – 28055

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LM5X-ray1.80A/B2609-2822[»]
1LM7X-ray3.00A/B2209-2456[»]
3R6NX-ray2.95A/B178-627[»]
ProteinModelPortaliP15924.
SMRiP15924. Positions 178-627, 2209-2448, 2613-2808.

Miscellaneous databases

EvolutionaryTraceiP15924.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati178 – 27194Spectrin 1
Add
BLAST
Repeati272 – 375104Spectrin 2
Add
BLAST
Repeati376 – 44671Spectrin 3a
Add
BLAST
Domaini447 – 51569SH3
Add
BLAST
Repeati516 – 54530Spectrin 3b
Add
BLAST
Repeati546 – 62782Spectrin 4
Add
BLAST
Repeati654 – 769116Spectrin 5
Add
BLAST
Repeati770 – 883114Spectrin 6
Add
BLAST
Repeati2009 – 204537Plectin 1
Add
BLAST
Repeati2046 – 208338Plectin 2
Add
BLAST
Repeati2084 – 212138Plectin 3
Add
BLAST
Repeati2122 – 215938Plectin 4
Add
BLAST
Repeati2163 – 219735Plectin 5
Add
BLAST
Repeati2198 – 223336Plectin 6
Add
BLAST
Repeati2251 – 228838Plectin 7
Add
BLAST
Repeati2289 – 232638Plectin 8
Add
BLAST
Repeati2327 – 236438Plectin 9
Add
BLAST
Repeati2365 – 240238Plectin 10
Add
BLAST
Repeati2406 – 244035Plectin 11
Add
BLAST
Repeati2456 – 249338Plectin 12
Add
BLAST
Repeati2507 – 254438Plectin 13
Add
BLAST
Repeati2610 – 264738Plectin 14
Add
BLAST
Repeati2648 – 268538Plectin 15
Add
BLAST
Repeati2724 – 276138Plectin 16
Add
BLAST
Repeati2762 – 279938Plectin 17
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 10561056Globular 1
Add
BLAST
Regioni1 – 584584Interacts with plakophilin 1 and junction plakoglobin
Add
BLAST
Regioni1057 – 1945889Central fibrous rod domain
Add
BLAST
Regioni1946 – 2871926Globular 2
Add
BLAST
Regioni1960 – 22082494.5 X 38 AA tandem repeats (Domain A)
Add
BLAST
Regioni2244 – 24462034.5 X 38 AA tandem repeats (Domain B)
Add
BLAST
Regioni2609 – 28222144.5 X 38 AA tandem repeats (Domain C)
Add
BLAST
Regioni2824 – 2847246 X 4 AA tandem repeats of G-S-R-[SR]
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1018 – 1945928 Reviewed prediction
Add
BLAST

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.2 Publications
The N-terminal region is required for localization to the desmosomal plaque and interacts with the N-terminal region of plakophilin 1.2 Publications
The three tandem plakin repeat regions in the C-terminus mediate binding to intermediate filaments.2 Publications

Sequence similaritiesi

Contains 17 plectin repeats.
Contains 1 SH3 domain.
Contains 6 spectrin repeats.

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiNOG12793.
HOGENOMiHOG000112198.
HOVERGENiHBG081434.
InParanoidiP15924.
KOiK10381.
OMAiKRSMSFQ.
OrthoDBiEOG7TQTZV.
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. Align

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

MSCNGGSHPR INTLGRMIRA ESGPDLRYEV TSGGGGTSRM YYSRRGVITD     50
QNSDGYCQTG TMSRHQNQNT IQELLQNCSD CLMRAELIVQ PELKYGDGIQ 100
LTRSRELDEC FAQANDQMEI LDSLIREMRQ MGQPCDAYQK RLLQLQEQMR 150
ALYKAISVPR VRRASSKGGG GYTCQSGSGW DEFTKHVTSE CLGWMRQQRA 200
EMDMVAWGVD LASVEQHINS HRGIHNSIGD YRWQLDKIKA DLREKSAIYQ 250
LEEEYENLLK ASFERMDHLR QLQNIIQATS REIMWINDCE EEELLYDWSD 300
KNTNIAQKQE AFSIRMSQLE VKEKELNKLK QESDQLVLNQ HPASDKIEAY 350
MDTLQTQWSW ILQITKCIDV HLKENAAYFQ FFEEAQSTEA YLKGLQDSIR 400
KKYPCDKNMP LQHLLEQIKE LEKEREKILE YKRQVQNLVN KSKKIVQLKP 450
RNPDYRSNKP IILRALCDYK QDQKIVHKGD ECILKDNNER SKWYVTGPGG 500
VDMLVPSVGL IIPPPNPLAV DLSCKIEQYY EAILALWNQL YINMKSLVSW 550
HYCMIDIEKI RAMTIAKLKT MRQEDYMKTI ADLELHYQEF IRNSQGSEMF 600
GDDDKRKIQS QFTDAQKHYQ TLVIQLPGYP QHQTVTTTEI THHGTCQDVN 650
HNKVIETNRE NDKQETWMLM ELQKIRRQIE HCEGRMTLKN LPLADQGSSH 700
HITVKINELK SVQNDSQAIA EVLNQLKDML ANFRGSEKYC YLQNEVFGLF 750
QKLENINGVT DGYLNSLCTV RALLQAILQT EDMLKVYEAR LTEEETVCLD 800
LDKVEAYRCG LKKIKNDLNL KKSLLATMKT ELQKAQQIHS QTSQQYPLYD 850
LDLGKFGEKV TQLTDRWQRI DKQIDFRLWD LEKQIKQLRN YRDNYQAFCK 900
WLYDAKRRQD SLESMKFGDS NTVMRFLNEQ KNLHSEISGK RDKSEEVQKI 950
AELCANSIKD YELQLASYTS GLETLLNIPI KRTMIQSPSG VILQEAADVH 1000
ARYIELLTRS GDYYRFLSEM LKSLEDLKLK NTKIEVLEEE LRLARDANSE 1050
NCNKNKFLDQ NLQKYQAECS QFKAKLASLE ELKRQAELDG KSAKQNLDKC 1100
YGQIKELNEK ITRLTYEIED EKRRRKSVED RFDQQKNDYD QLQKARQCEK 1150
ENLGWQKLES EKAIKEKEYE IERLRVLLQE EGTRKREYEN ELAKVRNHYN 1200
EEMSNLRNKY ETEINITKTT IKEISMQKED DSKNLRNQLD RLSRENRDLK 1250
DEIVRLNDSI LQATEQRRRA EENALQQKAC GSEIMQKKQH LEIELKQVMQ 1300
QRSEDNARHK QSLEEAAKTI QDKNKEIERL KAEFQEEAKR RWEYENELSK 1350
VRNNYDEEII SLKNQFETEI NITKTTIHQL TMQKEEDTSG YRAQIDNLTR 1400
ENRSLSEEIK RLKNTLTQTT ENLRRVEEDI QQQKATGSEV SQRKQQLEVE 1450
LRQVTQMRTE ESVRYKQSLD DAAKTIQDKN KEIERLKQLI DKETNDRKCL 1500
EDENARLQRV QYDLQKANSS ATETINKLKV QEQELTRLRI DYERVSQERT 1550
VKDQDITRFQ NSLKELQLQK QKVEEELNRL KRTASEDSCK RKKLEEELEG 1600
MRRSLKEQAI KITNLTQQLE QASIVKKRSE DDLRQQRDVL DGHLREKQRT 1650
QEELRRLSSE VEALRRQLLQ EQESVKQAHL RNEHFQKAIE DKSRSLNESK 1700
IEIERLQSLT ENLTKEHLML EEELRNLRLE YDDLRRGRSE ADSDKNATIL 1750
ELRSQLQISN NRTLELQGLI NDLQRERENL RQEIEKFQKQ ALEASNRIQE 1800
SKNQCTQVVQ ERESLLVKIK VLEQDKARLQ RLEDELNRAK STLEAETRVK 1850
QRLECEKQQI QNDLNQWKTQ YSRKEEAIRK IESEREKSER EKNSLRSEIE 1900
RLQAEIKRIE ERCRRKLEDS TRETQSQLET ERSRYQREID KLRQRPYGSH 1950
RETQTECEWT VDTSKLVFDG LRKKVTAMQL YECQLIDKTT LDKLLKGKKS 2000
VEEVASEIQP FLRGAGSIAG ASASPKEKYS LVEAKRKKLI SPESTVMLLE 2050
AQAATGGIID PHRNEKLTVD SAIARDLIDF DDRQQIYAAE KAITGFDDPF 2100
SGKTVSVSEA IKKNLIDRET GMRLLEAQIA SGGVVDPVNS VFLPKDVALA 2150
RGLIDRDLYR SLNDPRDSQK NFVDPVTKKK VSYVQLKERC RIEPHTGLLL 2200
LSVQKRSMSF QGIRQPVTVT ELVDSGILRP STVNELESGQ ISYDEVGERI 2250
KDFLQGSSCI AGIYNETTKQ KLGIYEAMKI GLVRPGTALE LLEAQAATGF 2300
IVDPVSNLRL PVEEAYKRGL VGIEFKEKLL SAERAVTGYN DPETGNIISL 2350
FQAMNKELIE KGHGIRLLEA QIATGGIIDP KESHRLPVDI AYKRGYFNEE 2400
LSEILSDPSD DTKGFFDPNT EENLTYLQLK ERCIKDEETG LCLLPLKEKK 2450
KQVQTSQKNT LRKRRVVIVD PETNKEMSVQ EAYKKGLIDY ETFKELCEQE 2500
CEWEEITITG SDGSTRVVLV DRKTGSQYDI QDAIDKGLVD RKFFDQYRSG 2550
SLSLTQFADM ISLKNGVGTS SSMGSGVSDD VFSSSRHESV SKISTISSVR 2600
NLTIRSSSFS DTLEESSPIA AIFDTENLEK ISITEGIERG IVDSITGQRL 2650
LEAQACTGGI IHPTTGQKLS LQDAVSQGVI DQDMATRLKP AQKAFIGFEG 2700
VKGKKKMSAA EAVKEKWLPY EAGQRFLEFQ YLTGGLVDPE VHGRISTEEA 2750
IRKGFIDGRA AQRLQDTSSY AKILTCPKTK LKISYKDAIN RSMVEDITGL 2800
RLLEAASVSS KGLPSPYNMS SAPGSRSGSR SGSRSGSRSG SRSGSRRGSF 2850
DATGNSSYSY SYSFSSSSIG H 2871
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

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti287 – 2871N → K in SFWHS. 1 Publication
VAR_015569
Natural varianti299 – 2991S → R in ARVD8. 3 Publications
Corresponds to variant rs121912992 [ dbSNP | Ensembl ].
VAR_015402
Natural varianti305 – 3051I → F.2 Publications
Corresponds to variant rs17604693 [ dbSNP | Ensembl ].
VAR_033862
Natural varianti445 – 4451I → V in ARVD8.
VAR_065693
Natural varianti1255 – 12551R → K in ARVD8. 2 Publications
VAR_023814
Natural varianti1505 – 15051A → V.1 Publication
VAR_065694
Natural varianti1512 – 15121Y → C.2 Publications
Corresponds to variant rs2076299 [ dbSNP | Ensembl ].
VAR_020468
Natural varianti1526 – 15261N → K.2 Publications
Corresponds to variant rs28763966 [ dbSNP | Ensembl ].
VAR_065695
Natural varianti1537 – 15371R → C.2 Publications
Corresponds to variant rs28763967 [ dbSNP | Ensembl ].
VAR_065696
Natural varianti1738 – 17381R → Q.2 Publications
Corresponds to variant rs6929069 [ dbSNP | Ensembl ].
VAR_023815
Natural varianti1775 – 17751R → I in ARVD8. 2 Publications
Corresponds to variant rs34738426 [ dbSNP | Ensembl ].
VAR_023816
Natural varianti1833 – 18331E → V.2 Publications
Corresponds to variant rs78652302 [ dbSNP | Ensembl ].
VAR_065697
Natural varianti2366 – 23661R → C in SFWHS. 1 Publication
Corresponds to variant rs28931610 [ dbSNP | Ensembl ].
VAR_015570
Natural varianti2375 – 23751G → R in a case of recessive arrhythmogenic right ventricular cardiomyopathy with skin abnormalities and woolly hair. 1 Publication
VAR_018158

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1195 – 1793599Missing in isoform DPII.
VSP_005070Add
BLAST
Alternative sequencei1351 – 1793443Missing in isoform DSPIa.
VSP_053769Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti905 – 9051A → R in AAA85135. 1 Publication
Sequence conflicti1120 – 11201D → R in AAA35766. 1 Publication
Sequence conflicti2687 – 26882RL → SV in AAA85135. 1 Publication
Sequence conflicti2687 – 26882RL → SV in AAA35766. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_001008844.1. [P15924-2]
NP_004406.2. NM_004415.2. [P15924-1]
UniGeneiHs.519873.

Genome annotation databases

EnsembliENST00000379802; ENSP00000369129; ENSG00000096696. [P15924-1]
ENST00000418664; ENSP00000396591; ENSG00000096696. [P15924-2]
GeneIDi1832.
KEGGihsa:1832.
UCSCiuc003mxp.1. human. [P15924-1]
uc003mxq.1. human. [P15924-2]

Polymorphism databases

DMDMi115502381.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Desmoplakin entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS4501.1. [P15924-1 ]
CCDS47368.1. [P15924-2 ]
PIRi A38194.
RefSeqi NP_001008844.1. NM_001008844.1. [P15924-2 ]
NP_004406.2. NM_004415.2. [P15924-1 ]
UniGenei Hs.519873.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1LM5 X-ray 1.80 A/B 2609-2822 [» ]
1LM7 X-ray 3.00 A/B 2209-2456 [» ]
3R6N X-ray 2.95 A/B 178-627 [» ]
ProteinModelPortali P15924.
SMRi P15924. Positions 178-627, 2209-2448, 2613-2808.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108166. 51 interactions.
DIPi DIP-109N.
IntActi P15924. 21 interactions.
MINTi MINT-1157663.
STRINGi 9606.ENSP00000369129.

PTM databases

PhosphoSitei P15924.

Polymorphism databases

DMDMi 115502381.

Proteomic databases

MaxQBi P15924.
PaxDbi P15924.
PeptideAtlasi P15924.
PRIDEi P15924.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000379802 ; ENSP00000369129 ; ENSG00000096696 . [P15924-1 ]
ENST00000418664 ; ENSP00000396591 ; ENSG00000096696 . [P15924-2 ]
GeneIDi 1832.
KEGGi hsa:1832.
UCSCi uc003mxp.1. human. [P15924-1 ]
uc003mxq.1. human. [P15924-2 ]

Organism-specific databases

CTDi 1832.
GeneCardsi GC06P007541.
GeneReviewsi DSP.
HGNCi HGNC:3052. DSP.
HPAi CAB037324.
MIMi 125647. gene.
605676. phenotype.
607450. phenotype.
607655. phenotype.
609638. phenotype.
612908. phenotype.
neXtProti NX_P15924.
Orphaneti 293899. 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.
PharmGKBi PA27505.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG12793.
HOGENOMi HOG000112198.
HOVERGENi HBG081434.
InParanoidi P15924.
KOi K10381.
OMAi KRSMSFQ.
OrthoDBi EOG7TQTZV.
PhylomeDBi P15924.
TreeFami TF106435.

Enzyme and pathway databases

Reactomei REACT_13579. Apoptotic cleavage of cell adhesion proteins.

Miscellaneous databases

ChiTaRSi DSP. human.
EvolutionaryTracei P15924.
GeneWikii Desmoplakin.
GenomeRNAii 1832.
NextBioi 35495766.
PROi P15924.
SOURCEi Search...

Gene expression databases

ArrayExpressi P15924.
Bgeei P15924.
CleanExi HS_DSP.
Genevestigatori P15924.

Family and domain databases

Gene3Di 3.90.1290.10. 5 hits.
InterProi IPR028462. Desmoplakin.
IPR001101. Plectin_repeat.
IPR018159. Spectrin/alpha-actinin.
[Graphical view ]
PANTHERi PTHR11915:SF234. PTHR11915:SF234. 1 hit.
Pfami PF00681. Plectin. 8 hits.
[Graphical view ]
SMARTi SM00250. PLEC. 18 hits.
SM00150. SPEC. 3 hits.
[Graphical view ]
SUPFAMi SSF75399. SSF75399. 5 hits.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular structure of the human desmoplakin I and II amino terminus."
    Virata M.L.A., Wagner R.M., Parry D.A.D., Green K.J.
    Proc. Natl. Acad. Sci. U.S.A. 89:544-548(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM DPI).
    Tissue: Foreskin.
  2. "Identification and characterization of DSPIa, a novel isoform of human desmoplakin."
    Cabral R.M., Wan H., Cole C.L., Abrams D.J., Kelsell D.P., South A.P.
    Cell Tissue Res. 341:121-129(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM DSPIA).
  3. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM DPII).
  5. "Structure of the human desmoplakins. Implications for function in the desmosomal plaque."
    Green K.J., Parry D.A.D., Steinert P.M., Virata M.L.A., Wagner R.M., Angst B.D., Nilles L.A.
    J. Biol. Chem. 265:2603-2612(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1120-2871 (ISOFORM DPI).
    Tissue: Foreskin.
  6. "Striate palmoplantar keratoderma resulting from desmoplakin haploinsufficiency."
    Whittock N.V., Ashton G.H., Dopping-Hepenstal P.J., Gratian M.J., Keane F.M., Eady R.A.J., McGrath J.A.
    J. Invest. Dermatol. 113:940-946(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2854-2871.
    Tissue: Skin.
  7. "The amino-terminal domain of desmoplakin binds to plakoglobin and clusters desmosomal cadherin-plakoglobin complexes."
    Kowalczyk A.P., Bornslaeger E.A., Borgwardt J.E., Palka H.L., Dhaliwal A.S., Corcoran C.M., Denning M.F., Green K.J.
    J. Cell Biol. 139:773-784(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  8. "Ceramides are bound to structural proteins of the human foreskin epidermal cornified cell envelope."
    Marekov L.N., Steinert P.M.
    J. Biol. Chem. 273:17763-17770(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: LIPIDATION.
  9. "Haploinsufficiency of desmoplakin causes a striate subtype of palmoplantar keratoderma."
    Armstrong D.K., McKenna K.E., Purkis P.E., Green K.J., Eady R.A.J., Leigh I.M., Hughes A.E.
    Hum. Mol. Genet. 8:143-148(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN SPPK2.
  10. "Recessive mutation in desmoplakin disrupts desmoplakin-intermediate filament interactions and causes dilated cardiomyopathy, woolly hair and keratoderma."
    Norgett E.E., Hatsell S.J., Carvajal-Huerta L., Cabezas J.-C.R., Common J., Purkis P.E., Whittock N.V., Leigh I.M., Stevens H.P., Kelsell D.P.
    Hum. Mol. Genet. 9:2761-2766(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN DCWHK.
  11. "Analysis of the interactions between BP180, BP230, plectin and the integrin alpha6beta4 important for hemidesmosome assembly."
    Koster J., Geerts D., Favre B., Borradori L., Sonnenberg A.
    J. Cell Sci. 116:387-399(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH COL17A1.
  12. "Interaction of the bullous pemphigoid antigen 1 (BP230) and desmoplakin with intermediate filaments is mediated by distinct sequences within their COOH terminus."
    Fontao L., Favre B., Riou S., Geerts D., Jaunin F., Saurat J.H., Green K.J., Sonnenberg A., Borradori L.
    Mol. Biol. Cell 14:1978-1992(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: ASSOCIATION WITH KERATIN FILAMENTS, MUTAGENESIS OF SER-2849, SUBCELLULAR LOCATION.
  13. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2825, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165; SER-166; SER-176; SER-2024; SER-2209; SER-2815; SER-2821; SER-2825; SER-2849; THR-2853 AND SER-2868, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  19. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2024; SER-2207; SER-2209; SER-2815 AND SER-2825, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "Mechanistic insights into arrhythmogenic right ventricular cardiomyopathy caused by desmocollin-2 mutations."
    Gehmlich K., Syrris P., Peskett E., Evans A., Ehler E., Asimaki A., Anastasakis A., Tsatsopoulou A., Vouliotis A.I., Stefanadis C., Saffitz J.E., Protonotarios N., McKenna W.J.
    Cardiovasc. Res. 90:77-87(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DSC2, VARIANT VAL-1833.
  22. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22; SER-2209; SER-2820 AND SER-2825, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "Molecular insights into arrhythmogenic right ventricular cardiomyopathy caused by plakophilin-2 missense mutations."
    Kirchner F., Schuetz A., Boldt L.H., Martens K., Dittmar G., Haverkamp W., Thierfelder L., Heinemann U., Gerull B.
    Circ. Cardiovasc. Genet. 5:400-411(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PKP2.
  24. "Structures of two intermediate filament-binding fragments of desmoplakin reveal a unique repeat motif structure."
    Choi H.J., Park-Snyder S., Pascoe L.T., Green K.J., Weis W.I.
    Nat. Struct. Biol. 9:612-620(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 2209-2456, X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 2609-2822, DOMAIN PLAKIN REPEATS.
  25. "Crystal structure of a rigid four-spectrin-repeat fragment of the human desmoplakin plakin domain."
    Choi H.J., Weis W.I.
    J. Mol. Biol. 409:800-812(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF 178-627, DOMAIN SPECTRIN REPEATS, DOMAIN SH3.
  26. "Mutation in human desmoplakin domain binding to plakoglobin causes a dominant form of arrhythmogenic right ventricular cardiomyopathy."
    Rampazzo A., Nava A., Malacrida S., Beffagna G., Bauce B., Rossi V., Zimbello R., Simionati B., Basso C., Thiene G., Towbin J.A., Danieli G.A.
    Am. J. Hum. Genet. 71:1200-1206(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT ARVD8 ARG-299.
  27. "Compound heterozygosity for non-sense and mis-sense mutations in desmoplakin underlies skin fragility/woolly hair syndrome."
    Whittock N.V., Wan H., Morley S.M., Garzon M.C., Kristal L., Hyde P., McLean W.H.I., Pulkkinen L., Uitto J., Christiano A.M., Eady R.A.J., McGrath J.A.
    J. Invest. Dermatol. 118:232-238(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS SFWHS LYS-287 AND CYS-2366.
  28. "A recessive mutation in desmoplakin causes arrhythmogenic right ventricular dysplasia, skin disorder, and woolly hair."
    Alcalai R., Metzger S., Rosenheck S., Meiner V., Chajek-Shaul T.
    J. Am. Coll. Cardiol. 42:319-327(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT ARRHYTHMOGENIC CARDIOMYOPATHY ARG-2375.
  29. Cited for: INVOLVEMENT IN LETHAL ACANTHOLYTIC EPIDERMOLYSIS BULLOSA.
  30. "Clinical profile of four families with arrhythmogenic right ventricular cardiomyopathy caused by dominant desmoplakin mutations."
    Bauce B., Basso C., Rampazzo A., Beffagna G., Daliento L., Frigo G., Malacrida S., Settimo L., Danieli G., Thiene G., Nava A.
    Eur. Heart J. 26:1666-1675(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS ARVD8 ARG-299; LYS-1255 AND ILE-1775.
  31. "Comprehensive desmosome mutation analysis in North Americans with arrhythmogenic right ventricular dysplasia/cardiomyopathy."
    den Haan A.D., Tan B.Y., Zikusoka M.N., Llado L.I., Jain R., Daly A., Tichnell C., James C., Amat-Alarcon N., Abraham T., Russell S.D., Bluemke D.A., Calkins H., Dalal D., Judge D.P.
    Circ. Cardiovasc. Genet. 2:428-435(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS ARVD8 ARG-299; LYS-1255 AND ILE-1775, VARIANTS PHE-305; VAL-1505; CYS-1512; LYS-1526; CYS-1537 AND GLN-1738.
  32. "Role of genetic testing in arrhythmogenic right ventricular cardiomyopathy/dysplasia."
    Barahona-Dussault C., Benito B., Campuzano O., Iglesias A., Leung T.L., Robb L., Talajic M., Brugada R.
    Clin. Genet. 77:37-48(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS PHE-305; CYS-1512; LYS-1526; CYS-1537; CYS-1537; GLN-1738 AND VAL-1833.

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: September 3, 2014
This is version 182 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

External Data

Dasty 3

Similar proteinsi