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P15924

- DESP_HUMAN

UniProt

P15924 - DESP_HUMAN

Protein

Desmoplakin

Gene

DSP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 183 (01 Oct 2014)
      Sequence version 3 (03 Oct 2006)
      Previous versions | rss
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    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

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

    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

    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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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.3 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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 – 28712871DesmoplakinPRO_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 esterSequence Analysis
    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.4 Publications
    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, 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

    1
    2871
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP15924.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati178 – 27194Spectrin 1Add
    BLAST
    Repeati272 – 375104Spectrin 2Add
    BLAST
    Repeati376 – 44671Spectrin 3aAdd
    BLAST
    Domaini447 – 51569SH3Add
    BLAST
    Repeati516 – 54530Spectrin 3bAdd
    BLAST
    Repeati546 – 62782Spectrin 4Add
    BLAST
    Repeati654 – 769116Spectrin 5Add
    BLAST
    Repeati770 – 883114Spectrin 6Add
    BLAST
    Repeati2009 – 204537Plectin 1Add
    BLAST
    Repeati2046 – 208338Plectin 2Add
    BLAST
    Repeati2084 – 212138Plectin 3Add
    BLAST
    Repeati2122 – 215938Plectin 4Add
    BLAST
    Repeati2163 – 219735Plectin 5Add
    BLAST
    Repeati2198 – 223336Plectin 6Add
    BLAST
    Repeati2251 – 228838Plectin 7Add
    BLAST
    Repeati2289 – 232638Plectin 8Add
    BLAST
    Repeati2327 – 236438Plectin 9Add
    BLAST
    Repeati2365 – 240238Plectin 10Add
    BLAST
    Repeati2406 – 244035Plectin 11Add
    BLAST
    Repeati2456 – 249338Plectin 12Add
    BLAST
    Repeati2507 – 254438Plectin 13Add
    BLAST
    Repeati2610 – 264738Plectin 14Add
    BLAST
    Repeati2648 – 268538Plectin 15Add
    BLAST
    Repeati2724 – 276138Plectin 16Add
    BLAST
    Repeati2762 – 279938Plectin 17Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 10561056Globular 1Add
    BLAST
    Regioni1 – 584584Interacts with plakophilin 1 and junction plakoglobinAdd
    BLAST
    Regioni1057 – 1945889Central fibrous rod domainAdd
    BLAST
    Regioni1946 – 2871926Globular 2Add
    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 – 1945928Sequence AnalysisAdd
    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.
    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

    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti905 – 9051A → R in AAA85135. (PubMed:1731325)Curated
    Sequence conflicti1120 – 11201D → R in AAA35766. (PubMed:1689290)Curated
    Sequence conflicti2687 – 26882RL → SV in AAA85135. (PubMed:1731325)Curated
    Sequence conflicti2687 – 26882RL → SV in AAA35766. (PubMed:1689290)Curated

    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. 1 PublicationVSP_005070Add
    BLAST
    Alternative sequencei1351 – 1793443Missing in isoform DSPIa. 1 PublicationVSP_053769Add
    BLAST

    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

    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: October 1, 2014
    This is version 183 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