DESP_HUMAN
ID DESP_HUMAN Reviewed; 2871 AA.
AC P15924; B2RTT2; D7RX09; O75993; Q14189; Q9UHN4;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 3.
DT 03-AUG-2022, entry version 251.
DE RecName: Full=Desmoplakin;
DE Short=DP;
DE AltName: Full=250/210 kDa paraneoplastic pemphigus antigen;
GN Name=DSP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM DPI).
RC TISSUE=Foreskin;
RX PubMed=1731325; DOI=10.1073/pnas.89.2.544;
RA Virata M.L.A., Wagner R.M., Parry D.A.D., Green K.J.;
RT "Molecular structure of the human desmoplakin I and II amino terminus.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:544-548(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM DSPIA).
RX PubMed=20524011; DOI=10.1007/s00441-010-0989-1;
RA Cabral R.M., Wan H., Cole C.L., Abrams D.J., Kelsell D.P., South A.P.;
RT "Identification and characterization of DSPIa, a novel isoform of human
RT desmoplakin.";
RL Cell Tissue Res. 341:121-129(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM DPII).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1120-2871 (ISOFORM DPI).
RC TISSUE=Foreskin;
RX PubMed=1689290; DOI=10.1016/s0021-9258(19)39844-8;
RA Green K.J., Parry D.A.D., Steinert P.M., Virata M.L.A., Wagner R.M.,
RA Angst B.D., Nilles L.A.;
RT "Structure of the human desmoplakins. Implications for function in the
RT desmosomal plaque.";
RL J. Biol. Chem. 265:2603-2612(1990).
RN [6]
RP ERRATUM OF PUBMED:1689290.
RX PubMed=2391353; DOI=10.1016/s0021-9258(19)38608-9;
RA Green K.J., Parry D.A.D., Steinert P.M., Virata M.L.A., Wagner R.M.,
RA Angst B.D., Nilles L.A.;
RL J. Biol. Chem. 265:11406-11407(1990).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2854-2871.
RC TISSUE=Skin;
RX PubMed=10594734; DOI=10.1046/j.1523-1747.1999.00783.x;
RA Whittock N.V., Ashton G.H., Dopping-Hepenstal P.J., Gratian M.J.,
RA Keane F.M., Eady R.A.J., McGrath J.A.;
RT "Striate palmoplantar keratoderma resulting from desmoplakin
RT haploinsufficiency.";
RL J. Invest. Dermatol. 113:940-946(1999).
RN [8]
RP CHARACTERIZATION.
RX PubMed=9348293; DOI=10.1083/jcb.139.3.773;
RA Kowalczyk A.P., Bornslaeger E.A., Borgwardt J.E., Palka H.L.,
RA Dhaliwal A.S., Corcoran C.M., Denning M.F., Green K.J.;
RT "The amino-terminal domain of desmoplakin binds to plakoglobin and clusters
RT desmosomal cadherin-plakoglobin complexes.";
RL J. Cell Biol. 139:773-784(1997).
RN [9]
RP INVOLVEMENT IN SPPK2.
RX PubMed=9887343; DOI=10.1093/hmg/8.1.143;
RA Armstrong D.K., McKenna K.E., Purkis P.E., Green K.J., Eady R.A.J.,
RA Leigh I.M., Hughes A.E.;
RT "Haploinsufficiency of desmoplakin causes a striate subtype of palmoplantar
RT keratoderma.";
RL Hum. Mol. Genet. 8:143-148(1999).
RN [10]
RP ERRATUM OF PUBMED:9887343.
RA Armstrong D.K., McKenna K.E., Purkis P.E., Green K.J., Eady R.A.J.,
RA Leigh I.M., Hughes A.E.;
RL Hum. Mol. Genet. 8:943-943(1999).
RN [11]
RP INVOLVEMENT IN DCWHK.
RX PubMed=11063735; DOI=10.1093/hmg/9.18.2761;
RA Norgett E.E., Hatsell S.J., Carvajal-Huerta L., Cabezas J.-C.R., Common J.,
RA Purkis P.E., Whittock N.V., Leigh I.M., Stevens H.P., Kelsell D.P.;
RT "Recessive mutation in desmoplakin disrupts desmoplakin-intermediate
RT filament interactions and causes dilated cardiomyopathy, woolly hair and
RT keratoderma.";
RL Hum. Mol. Genet. 9:2761-2766(2000).
RN [12]
RP INTERACTION WITH COL17A1.
RX PubMed=12482924; DOI=10.1242/jcs.00241;
RA Koster J., Geerts D., Favre B., Borradori L., Sonnenberg A.;
RT "Analysis of the interactions between BP180, BP230, plectin and the
RT integrin alpha6beta4 important for hemidesmosome assembly.";
RL J. Cell Sci. 116:387-399(2003).
RN [13]
RP ASSOCIATION WITH KERATIN FILAMENTS, MUTAGENESIS OF SER-2849, AND
RP SUBCELLULAR LOCATION.
RX PubMed=12802069; DOI=10.1091/mbc.e02-08-0548;
RA Fontao L., Favre B., Riou S., Geerts D., Jaunin F., Saurat J.H.,
RA Green K.J., Sonnenberg A., Borradori L.;
RT "Interaction of the bullous pemphigoid antigen 1 (BP230) and desmoplakin
RT with intermediate filaments is mediated by distinct sequences within their
RT COOH terminus.";
RL Mol. Biol. Cell 14:1978-1992(2003).
RN [14]
RP INVOLVEMENT IN DCWHKTA.
RX PubMed=16628197; DOI=10.1038/sj.jid.5700291;
RA Norgett E.E., Lucke T.W., Bowers B., Munro C.S., Leigh I.M., Kelsell D.P.;
RT "Early death from cardiomyopathy in a family with autosomal dominant
RT striate palmoplantar keratoderma and woolly hair associated with a novel
RT insertion mutation in desmoplakin.";
RL J. Invest. Dermatol. 126:1651-1654(2006).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2825, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165; SER-166; SER-176;
RP SER-2024; SER-2209; SER-2815; SER-2821; SER-2825; SER-2849; THR-2853 AND
RP SER-2868, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2024; SER-2207; SER-2209;
RP SER-2815 AND SER-2825, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [22]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [23]
RP INTERACTION WITH DSC2, AND VARIANT VAL-1833.
RX PubMed=21062920; DOI=10.1093/cvr/cvq353;
RA Gehmlich K., Syrris P., Peskett E., Evans A., Ehler E., Asimaki A.,
RA Anastasakis A., Tsatsopoulou A., Vouliotis A.I., Stefanadis C.,
RA Saffitz J.E., Protonotarios N., McKenna W.J.;
RT "Mechanistic insights into arrhythmogenic right ventricular cardiomyopathy
RT caused by desmocollin-2 mutations.";
RL Cardiovasc. Res. 90:77-87(2011).
RN [24]
RP INVOLVEMENT IN DCWHKTA, AND VARIANT DCWHKTA LEU-597.
RX PubMed=20940358; DOI=10.1177/0022034510383984;
RA Chalabreysse L., Senni F., Bruyere P., Aime B., Ollagnier C., Bozio A.,
RA Bouvagnet P.;
RT "A new hypo/oligodontia syndrome: Carvajal/Naxos syndrome secondary to
RT desmoplakin-dominant mutations.";
RL J. Dent. Res. 90:58-64(2011).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22; SER-2209; SER-2820 AND
RP SER-2825, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [26]
RP INTERACTION WITH PKP2.
RX PubMed=22781308; DOI=10.1161/circgenetics.111.961854;
RA Kirchner F., Schuetz A., Boldt L.H., Martens K., Dittmar G., Haverkamp W.,
RA Thierfelder L., Heinemann U., Gerull B.;
RT "Molecular insights into arrhythmogenic right ventricular cardiomyopathy
RT caused by plakophilin-2 missense mutations.";
RL Circ. Cardiovasc. Genet. 5:400-411(2012).
RN [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22; SER-165; SER-1658;
RP SER-1708; SER-2024; SER-2209; SER-2810; TYR-2817; SER-2820 AND SER-2825,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [28]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22; SER-53; SER-165; SER-166;
RP SER-1708; SER-2209 AND SER-2225, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [29]
RP TISSUE SPECIFICITY.
RX PubMed=29034528; DOI=10.1111/ced.13214;
RA Abreu-Velez A.M., Valencia-Yepes C.A., Upegui-Zapata Y.A.,
RA Upegui-Quiceno E., Mesa-Herrera N.R., Velazquez-Velez J.E., Howard M.S.;
RT "Patients with a new variant of endemic pemphigus foliaceus have
RT autoantibodies against arrector pili muscle, colocalizing with MYZAP,
RT p0071, desmoplakins 1 and 2 and ARVCF.";
RL Clin. Exp. Dermatol. 42:874-880(2017).
RN [30]
RP TISSUE SPECIFICITY.
RX PubMed=30479852; DOI=10.5826/dpc.0804a02;
RA Abreu-Velez A.M., Howard M.S., Padilla H.J.L., Tobon-Arroyave S.;
RT "Subclinical oral involvement in patients with endemic pemphigus
RT foliaceus.";
RL Dermatol. Pract. Concept. 8:252-261(2018).
RN [31]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 2209-2456, X-RAY CRYSTALLOGRAPHY
RP (1.8 ANGSTROMS) OF 2609-2822, AND DOMAIN PLAKIN REPEATS.
RX PubMed=12101406; DOI=10.1038/nsb818;
RA Choi H.J., Park-Snyder S., Pascoe L.T., Green K.J., Weis W.I.;
RT "Structures of two intermediate filament-binding fragments of desmoplakin
RT reveal a unique repeat motif structure.";
RL Nat. Struct. Biol. 9:612-620(2002).
RN [32]
RP X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF 178-627, DOMAIN SPECTRIN REPEATS,
RP AND DOMAIN SH3.
RX PubMed=21536047; DOI=10.1016/j.jmb.2011.04.046;
RA Choi H.J., Weis W.I.;
RT "Crystal structure of a rigid four-spectrin-repeat fragment of the human
RT desmoplakin plakin domain.";
RL J. Mol. Biol. 409:800-812(2011).
RN [33]
RP VARIANT ARVD8 ARG-299.
RX PubMed=12373648; DOI=10.1086/344208;
RA Rampazzo A., Nava A., Malacrida S., Beffagna G., Bauce B., Rossi V.,
RA Zimbello R., Simionati B., Basso C., Thiene G., Towbin J.A., Danieli G.A.;
RT "Mutation in human desmoplakin domain binding to plakoglobin causes a
RT dominant form of arrhythmogenic right ventricular cardiomyopathy.";
RL Am. J. Hum. Genet. 71:1200-1206(2002).
RN [34]
RP VARIANTS SFWHS LYS-287 AND CYS-2366.
RX PubMed=11841538; DOI=10.1046/j.0022-202x.2001.01664.x;
RA Whittock N.V., Wan H., Morley S.M., Garzon M.C., Kristal L., Hyde P.,
RA McLean W.H.I., Pulkkinen L., Uitto J., Christiano A.M., Eady R.A.J.,
RA McGrath J.A.;
RT "Compound heterozygosity for non-sense and mis-sense mutations in
RT desmoplakin underlies skin fragility/woolly hair syndrome.";
RL J. Invest. Dermatol. 118:232-238(2002).
RN [35]
RP VARIANT ARRHYTHMOGENIC CARDIOMYOPATHY ARG-2375.
RX PubMed=12875771; DOI=10.1016/s0735-1097(03)00628-4;
RA Alcalai R., Metzger S., Rosenheck S., Meiner V., Chajek-Shaul T.;
RT "A recessive mutation in desmoplakin causes arrhythmogenic right
RT ventricular dysplasia, skin disorder, and woolly hair.";
RL J. Am. Coll. Cardiol. 42:319-327(2003).
RN [36]
RP INVOLVEMENT IN LETHAL ACANTHOLYTIC EPIDERMOLYSIS BULLOSA.
RX PubMed=16175511; DOI=10.1086/496901;
RA Jonkman M.F., Pasmooij A.M.G., Pasmans S.G.M.A., van den Berg M.P.,
RA Ter Horst H.J., Timmer A., Pas H.H.;
RT "Loss of desmoplakin tail causes lethal acantholytic epidermolysis
RT bullosa.";
RL Am. J. Hum. Genet. 77:653-660(2005).
RN [37]
RP VARIANTS ARVD8 ARG-299; LYS-1255 AND ILE-1775.
RX PubMed=15941723; DOI=10.1093/eurheartj/ehi341;
RA Bauce B., Basso C., Rampazzo A., Beffagna G., Daliento L., Frigo G.,
RA Malacrida S., Settimo L., Danieli G., Thiene G., Nava A.;
RT "Clinical profile of four families with arrhythmogenic right ventricular
RT cardiomyopathy caused by dominant desmoplakin mutations.";
RL Eur. Heart J. 26:1666-1675(2005).
RN [38]
RP VARIANTS ARVD8 ARG-299; LYS-1255 AND ILE-1775, AND VARIANTS PHE-305;
RP VAL-1505; CYS-1512; LYS-1526; CYS-1537 AND GLN-1738.
RX PubMed=20031617; DOI=10.1161/circgenetics.109.858217;
RA den Haan A.D., Tan B.Y., Zikusoka M.N., Llado L.I., Jain R., Daly A.,
RA Tichnell C., James C., Amat-Alarcon N., Abraham T., Russell S.D.,
RA Bluemke D.A., Calkins H., Dalal D., Judge D.P.;
RT "Comprehensive desmosome mutation analysis in North Americans with
RT arrhythmogenic right ventricular dysplasia/cardiomyopathy.";
RL Circ. Cardiovasc. Genet. 2:428-435(2009).
RN [39]
RP VARIANTS PHE-305; CYS-1512; LYS-1526; CYS-1537; CYS-1537; GLN-1738 AND
RP VAL-1833.
RX PubMed=19863551; DOI=10.1111/j.1399-0004.2009.01282.x;
RA Barahona-Dussault C., Benito B., Campuzano O., Iglesias A., Leung T.L.,
RA Robb L., Talajic M., Brugada R.;
RT "Role of genetic testing in arrhythmogenic right ventricular
RT cardiomyopathy/dysplasia.";
RL Clin. Genet. 77:37-48(2010).
RN [40]
RP VARIANT DCWHKTA ILE-564.
RX PubMed=22795705; DOI=10.1016/j.ijcard.2012.06.068;
RA Boule S., Fressart V., Laux D., Mallet A., Simon F., de Groote P.,
RA Bonnet D., Klug D., Charron P.;
RT "Expanding the phenotype associated with a desmoplakin dominant mutation:
RT Carvajal/Naxos syndrome associated with leukonychia and oligodontia.";
RL Int. J. Cardiol. 161:50-52(2012).
CC -!- FUNCTION: Major high molecular weight protein of desmosomes. Involved
CC in the organization of the desmosomal cadherin-plakoglobin complexes
CC into discrete plasma membrane domains and in the anchoring of
CC intermediate filaments to the desmosomes.
CC -!- SUBUNIT: Homodimer. Interacts with COL17A1 (via cytoplasmic region).
CC Associates (via C-terminal) with KRT5-KRT14 (via rod region), KRT8-
CC KRT18 and VIM intermediate filaments. Interacts with DSC2. Interacts
CC with PKP2. Interacts weakly with TMEM65 (By similarity).
CC {ECO:0000250|UniProtKB:E9Q557, ECO:0000269|PubMed:12482924,
CC ECO:0000269|PubMed:21062920, ECO:0000269|PubMed:22781308}.
CC -!- INTERACTION:
CC P15924; Q02413: DSG1; NbExp=2; IntAct=EBI-355041, EBI-1045757;
CC P15924; P07332: FES; NbExp=2; IntAct=EBI-355041, EBI-1055635;
CC P15924; Q15691: MAPRE1; NbExp=7; IntAct=EBI-355041, EBI-1004115;
CC P15924; Q13835-2: PKP1; NbExp=2; IntAct=EBI-355041, EBI-9087684;
CC -!- SUBCELLULAR LOCATION: Cell junction, desmosome
CC {ECO:0000269|PubMed:12802069}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:12802069}. Cell membrane
CC {ECO:0000250|UniProtKB:E9Q557}. Note=Innermost portion of the
CC desmosomal plaque. Colocalizes with epidermal KRT5-KRT14 and simple
CC KRT8-KRT18 keratins and VIM intermediate filaments network
CC (PubMed:12802069). Localizes at the intercalated disk in cardiomyocytes
CC (By similarity). {ECO:0000250|UniProtKB:E9Q557,
CC ECO:0000269|PubMed:12802069}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=DPI; Synonyms=DP1;
CC IsoId=P15924-1; Sequence=Displayed;
CC Name=DPII; Synonyms=DP2;
CC IsoId=P15924-2; Sequence=VSP_005070;
CC Name=DSPIa;
CC IsoId=P15924-3; Sequence=VSP_053769;
CC -!- TISSUE SPECIFICITY: Expressed in oral mucosa (at protein level)
CC (PubMed:30479852). Expressed in arrector pili muscle (at protein level)
CC (PubMed:29034528). {ECO:0000269|PubMed:29034528,
CC ECO:0000269|PubMed:30479852}.
CC -!- TISSUE SPECIFICITY: [Isoform DPI]: Apparently an obligate constituent
CC of all desmosomes.
CC -!- TISSUE SPECIFICITY: [Isoform DPII]: Resides predominantly in tissues
CC and cells of stratified origin.
CC -!- DOMAIN: Its association with epidermal and simple keratins is dependent
CC on the tertiary structure induced by heterodimerization of these
CC intermediate filaments proteins and most likely involves recognition
CC sites located in the rod domain of these keratins.
CC -!- DOMAIN: The N-terminal region is required for localization to the
CC desmosomal plaque and interacts with the N-terminal region of
CC plakophilin 1.
CC -!- DOMAIN: The three tandem plakin repeat regions in the C-terminus
CC mediate binding to intermediate filaments.
CC -!- PTM: Ser-2849 is probably phosphorylated by a cAMP-dependent protein
CC kinase. Phosphorylation on Ser-2849 probably affects its association
CC with epidermal, simple cytokeratins and VIM intermediate filaments.
CC -!- DISEASE: Keratoderma, palmoplantar, striate 2 (SPPK2) [MIM:612908]: A
CC dermatological disorder characterized by thickening of the skin on the
CC palms (linear pattern) and the soles (island-like pattern) and flexor
CC aspect of the fingers. Abnormalities of the nails, the teeth and the
CC hair are rarely present. {ECO:0000269|PubMed:9887343}. Note=The disease
CC is caused by variants affecting the gene represented in this entry.
CC -!- DISEASE: Cardiomyopathy, dilated, with woolly hair and keratoderma
CC (DCWHK) [MIM:605676]: An autosomal recessive cardiocutaneous syndrome
CC characterized by a generalized striate keratoderma particularly
CC affecting the palmoplantar epidermis, woolly hair, and dilated left
CC ventricular cardiomyopathy. {ECO:0000269|PubMed:11063735}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Arrhythmogenic right ventricular dysplasia, familial, 8
CC (ARVD8) [MIM:607450]: A congenital heart disease characterized by
CC infiltration of adipose and fibrous tissue into the right ventricle and
CC loss of myocardial cells, resulting in ventricular and supraventricular
CC arrhythmias. {ECO:0000269|PubMed:12373648, ECO:0000269|PubMed:15941723,
CC ECO:0000269|PubMed:20031617}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Skin fragility-woolly hair syndrome (SFWHS) [MIM:607655]: An
CC autosomal recessive genodermatosis characterized by skin fragility with
CC blistering, focal and diffuse palmoplantar keratoderma, hyperkeratotic
CC plaques on the trunk and limbs, and woolly hair with varying degrees of
CC alopecia. {ECO:0000269|PubMed:11841538}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
CC -!- DISEASE: Epidermolysis bullosa, lethal acantholytic (EBLA)
CC [MIM:609638]: A form of epidermolysis bullosa characterized by severe
CC fragility of skin and mucous membranes. The phenotype is lethal in the
CC neonatal period because of immense transcutaneous fluid loss. Typical
CC features include universal alopecia, neonatal teeth, and nail loss.
CC Histopathology of the skin shows suprabasal clefting and acantholysis
CC throughout the spinous layer, mimicking pemphigus. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- DISEASE: Cardiomyopathy, dilated, with woolly hair, keratoderma, and
CC tooth agenesis (DCWHKTA) [MIM:615821]: A cardiocutaneous syndrome
CC characterized by biventricular dilated cardiomyopathy, hyperkeratosis,
CC woolly hair, palmoplantar keratoderma, and hypo/oligodontia.
CC {ECO:0000269|PubMed:16628197, ECO:0000269|PubMed:20940358,
CC ECO:0000269|PubMed:22795705}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: [Isoform DSPIa]: Minor isoform. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the plakin or cytolinker family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Desmoplakin entry;
CC URL="https://en.wikipedia.org/wiki/Desmoplakin";
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DR EMBL; M77830; AAA85135.1; -; mRNA.
DR EMBL; HM151899; ADI58529.1; -; mRNA.
DR EMBL; AL031058; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC140802; AAI40803.1; -; mRNA.
DR EMBL; J05211; AAA35766.1; -; mRNA.
DR EMBL; AF139065; AAF19785.1; -; mRNA.
DR CCDS; CCDS4501.1; -. [P15924-1]
DR CCDS; CCDS47368.1; -. [P15924-2]
DR PIR; A38194; A38194.
DR RefSeq; NP_001008844.1; NM_001008844.2. [P15924-2]
DR RefSeq; NP_001305963.1; NM_001319034.1. [P15924-3]
DR RefSeq; NP_004406.2; NM_004415.3. [P15924-1]
DR PDB; 1LM5; X-ray; 1.80 A; A/B=2609-2822.
DR PDB; 1LM7; X-ray; 3.00 A; A/B=2209-2456.
DR PDB; 3R6N; X-ray; 2.95 A; A/B=178-627.
DR PDB; 5DZZ; X-ray; 2.60 A; A=1960-2448.
DR PDBsum; 1LM5; -.
DR PDBsum; 1LM7; -.
DR PDBsum; 3R6N; -.
DR PDBsum; 5DZZ; -.
DR SASBDB; P15924; -.
DR SMR; P15924; -.
DR BioGRID; 108166; 251.
DR DIP; DIP-109N; -.
DR IntAct; P15924; 117.
DR MINT; P15924; -.
DR STRING; 9606.ENSP00000369129; -.
DR DrugBank; DB11638; Artenimol.
DR DrugBank; DB01593; Zinc.
DR DrugBank; DB14487; Zinc acetate.
DR CarbonylDB; P15924; -.
DR GlyGen; P15924; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P15924; -.
DR MetOSite; P15924; -.
DR PhosphoSitePlus; P15924; -.
DR SwissPalm; P15924; -.
DR BioMuta; DSP; -.
DR DMDM; 115502381; -.
DR CPTAC; CPTAC-498; -.
DR CPTAC; CPTAC-499; -.
DR EPD; P15924; -.
DR jPOST; P15924; -.
DR MassIVE; P15924; -.
DR MaxQB; P15924; -.
DR PaxDb; P15924; -.
DR PeptideAtlas; P15924; -.
DR PRIDE; P15924; -.
DR ProteomicsDB; 53244; -. [P15924-1]
DR ProteomicsDB; 53245; -. [P15924-2]
DR Antibodypedia; 24671; 335 antibodies from 39 providers.
DR DNASU; 1832; -.
DR Ensembl; ENST00000379802.8; ENSP00000369129.3; ENSG00000096696.15. [P15924-1]
DR Ensembl; ENST00000418664.2; ENSP00000396591.2; ENSG00000096696.15. [P15924-2]
DR GeneID; 1832; -.
DR KEGG; hsa:1832; -.
DR MANE-Select; ENST00000379802.8; ENSP00000369129.3; NM_004415.4; NP_004406.2.
DR UCSC; uc003mxp.2; human. [P15924-1]
DR CTD; 1832; -.
DR DisGeNET; 1832; -.
DR GeneCards; DSP; -.
DR GeneReviews; DSP; -.
DR HGNC; HGNC:3052; DSP.
DR HPA; ENSG00000096696; Group enriched (esophagus, skin, vagina).
DR MalaCards; DSP; -.
DR MIM; 125647; gene.
DR MIM; 605676; phenotype.
DR MIM; 607450; phenotype.
DR MIM; 607655; phenotype.
DR MIM; 609638; phenotype.
DR MIM; 612908; phenotype.
DR MIM; 615821; phenotype.
DR neXtProt; NX_P15924; -.
DR OpenTargets; ENSG00000096696; -.
DR Orphanet; 65282; Carvajal syndrome.
DR Orphanet; 476096; Erythrokeratodermia-cardiomyopathy syndrome.
DR Orphanet; 293899; Familial isolated arrhythmogenic ventricular dysplasia, biventricular form.
DR Orphanet; 293888; Familial isolated arrhythmogenic ventricular dysplasia, left dominant form.
DR Orphanet; 293910; Familial isolated arrhythmogenic ventricular dysplasia, right dominant form.
DR Orphanet; 154; Familial isolated dilated cardiomyopathy.
DR Orphanet; 2032; Idiopathic pulmonary fibrosis.
DR Orphanet; 158687; Lethal acantholytic erosive disorder.
DR Orphanet; 369992; Severe dermatitis-multiple allergies-metabolic wasting syndrome.
DR Orphanet; 293165; Skin fragility-woolly hair-palmoplantar keratoderma syndrome.
DR Orphanet; 50942; Striate palmoplantar keratoderma.
DR PharmGKB; PA27505; -.
DR VEuPathDB; HostDB:ENSG00000096696; -.
DR eggNOG; KOG0516; Eukaryota.
DR GeneTree; ENSGT00940000154843; -.
DR HOGENOM; CLU_000679_1_0_1; -.
DR InParanoid; P15924; -.
DR OMA; ALCKWIC; -.
DR PhylomeDB; P15924; -.
DR TreeFam; TF106435; -.
DR PathwayCommons; P15924; -.
DR Reactome; R-HSA-351906; Apoptotic cleavage of cell adhesion proteins.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-6805567; Keratinization.
DR Reactome; R-HSA-6809371; Formation of the cornified envelope.
DR Reactome; R-HSA-9696264; RND3 GTPase cycle.
DR Reactome; R-HSA-9696273; RND1 GTPase cycle.
DR SignaLink; P15924; -.
DR SIGNOR; P15924; -.
DR BioGRID-ORCS; 1832; 16 hits in 1083 CRISPR screens.
DR ChiTaRS; DSP; human.
DR EvolutionaryTrace; P15924; -.
DR GeneWiki; Desmoplakin; -.
DR GenomeRNAi; 1832; -.
DR Pharos; P15924; Tbio.
DR PRO; PR:P15924; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; P15924; protein.
DR Bgee; ENSG00000096696; Expressed in skin of hip and 173 other tissues.
DR Genevisible; P15924; HS.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl.
DR GO; GO:0001533; C:cornified envelope; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0030057; C:desmosome; IEA:UniProtKB-SubCell.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005916; C:fascia adherens; IEA:Ensembl.
DR GO; GO:0101003; C:ficolin-1-rich granule membrane; TAS:Reactome.
DR GO; GO:0014704; C:intercalated disc; IDA:BHF-UCL.
DR GO; GO:0005882; C:intermediate filament; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0086083; F:cell adhesive protein binding involved in bundle of His cell-Purkinje myocyte communication; IC:BHF-UCL.
DR GO; GO:0005080; F:protein kinase C binding; IPI:BHF-UCL.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0097110; F:scaffold protein binding; IPI:BHF-UCL.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; TAS:ProtInc.
DR GO; GO:0005198; F:structural molecule activity; IBA:GO_Central.
DR GO; GO:0034332; P:adherens junction organization; IEA:Ensembl.
DR GO; GO:0086073; P:bundle of His cell-Purkinje myocyte adhesion involved in cell communication; IMP:BHF-UCL.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0002934; P:desmosome organization; ISS:BHF-UCL.
DR GO; GO:0008544; P:epidermis development; TAS:ProtInc.
DR GO; GO:0090136; P:epithelial cell-cell adhesion; IMP:MGI.
DR GO; GO:0045104; P:intermediate filament cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0045109; P:intermediate filament organization; ISS:BHF-UCL.
DR GO; GO:0030216; P:keratinocyte differentiation; IDA:UniProtKB.
DR GO; GO:0018149; P:peptide cross-linking; IDA:UniProtKB.
DR GO; GO:0150105; P:protein localization to cell-cell junction; ISS:BHF-UCL.
DR GO; GO:0086091; P:regulation of heart rate by cardiac conduction; IMP:BHF-UCL.
DR GO; GO:0098911; P:regulation of ventricular cardiac muscle cell action potential; IMP:BHF-UCL.
DR GO; GO:0043588; P:skin development; IBA:GO_Central.
DR GO; GO:0003223; P:ventricular compact myocardium morphogenesis; ISS:BHF-UCL.
DR GO; GO:0042060; P:wound healing; IBA:GO_Central.
DR CDD; cd00176; SPEC; 1.
DR Gene3D; 3.90.1290.10; -; 3.
DR InterPro; IPR028462; Desmoplakin.
DR InterPro; IPR041615; Desmoplakin_SH3.
DR InterPro; IPR041573; Desmoplakin_Spectrin-like.
DR InterPro; IPR043197; Plakin.
DR InterPro; IPR035915; Plakin_repeat_sf.
DR InterPro; IPR001101; Plectin_repeat.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR018159; Spectrin/alpha-actinin.
DR PANTHER; PTHR23169; PTHR23169; 1.
DR PANTHER; PTHR23169:SF26; PTHR23169:SF26; 1.
DR Pfam; PF00681; Plectin; 8.
DR Pfam; PF17902; SH3_10; 1.
DR Pfam; PF18373; Spectrin_like; 1.
DR SMART; SM00250; PLEC; 18.
DR SMART; SM00150; SPEC; 3.
DR SUPFAM; SSF75399; SSF75399; 4.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cardiomyopathy; Cell junction;
KW Cell membrane; Coiled coil; Cytoplasm; Cytoskeleton; Disease variant;
KW Epidermolysis bullosa; Membrane; Methylation; Palmoplantar keratoderma;
KW Phosphoprotein; Reference proteome; Repeat; SH3 domain.
FT CHAIN 1..2871
FT /note="Desmoplakin"
FT /id="PRO_0000078144"
FT REPEAT 178..271
FT /note="Spectrin 1"
FT REPEAT 272..375
FT /note="Spectrin 2"
FT REPEAT 376..446
FT /note="Spectrin 3a"
FT DOMAIN 458..515
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REPEAT 516..545
FT /note="Spectrin 3b"
FT REPEAT 546..627
FT /note="Spectrin 4"
FT REPEAT 654..769
FT /note="Spectrin 5"
FT REPEAT 770..883
FT /note="Spectrin 6"
FT REPEAT 2009..2045
FT /note="Plectin 1"
FT REPEAT 2046..2083
FT /note="Plectin 2"
FT REPEAT 2084..2121
FT /note="Plectin 3"
FT REPEAT 2122..2159
FT /note="Plectin 4"
FT REPEAT 2163..2197
FT /note="Plectin 5"
FT REPEAT 2198..2233
FT /note="Plectin 6"
FT REPEAT 2251..2288
FT /note="Plectin 7"
FT REPEAT 2289..2326
FT /note="Plectin 8"
FT REPEAT 2327..2364
FT /note="Plectin 9"
FT REPEAT 2365..2402
FT /note="Plectin 10"
FT REPEAT 2406..2440
FT /note="Plectin 11"
FT REPEAT 2456..2493
FT /note="Plectin 12"
FT REPEAT 2507..2544
FT /note="Plectin 13"
FT REPEAT 2610..2647
FT /note="Plectin 14"
FT REPEAT 2648..2685
FT /note="Plectin 15"
FT REPEAT 2724..2761
FT /note="Plectin 16"
FT REPEAT 2762..2799
FT /note="Plectin 17"
FT REGION 1..1056
FT /note="Globular 1"
FT REGION 1..584
FT /note="Interaction with plakophilin 1 and junction
FT plakoglobin"
FT REGION 1057..1945
FT /note="Central fibrous rod domain"
FT REGION 1946..2871
FT /note="Globular 2"
FT REGION 1960..2208
FT /note="4.5 X 38 AA tandem repeats (Domain A)"
FT REGION 2244..2446
FT /note="4.5 X 38 AA tandem repeats (Domain B)"
FT REGION 2609..2822
FT /note="4.5 X 38 AA tandem repeats (Domain C)"
FT REGION 2810..2871
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2824..2847
FT /note="6 X 4 AA tandem repeats of G-S-R-[SR]"
FT COILED 1018..1945
FT /evidence="ECO:0000255"
FT COMPBIAS 2811..2871
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 56
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:E9Q557"
FT MOD_RES 61
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:E9Q557"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 166
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 176
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1658
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1708
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 2024
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 2207
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 2209
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 2225
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 2810
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 2815
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 2817
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 2820
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 2821
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 2825
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 2826
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:E9Q557"
FT MOD_RES 2847
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:E9Q557"
FT MOD_RES 2849
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 2853
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 2868
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VAR_SEQ 1195..1793
FT /note="Missing (in isoform DPII)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_005070"
FT VAR_SEQ 1351..1793
FT /note="Missing (in isoform DSPIa)"
FT /evidence="ECO:0000303|PubMed:20524011"
FT /id="VSP_053769"
FT VARIANT 287
FT /note="N -> K (in SFWHS; dbSNP:rs121912993)"
FT /evidence="ECO:0000269|PubMed:11841538"
FT /id="VAR_015569"
FT VARIANT 299
FT /note="S -> R (in ARVD8; unknown pathological significance;
FT dbSNP:rs121912992)"
FT /evidence="ECO:0000269|PubMed:12373648,
FT ECO:0000269|PubMed:15941723, ECO:0000269|PubMed:20031617"
FT /id="VAR_015402"
FT VARIANT 305
FT /note="I -> F (in dbSNP:rs17604693)"
FT /evidence="ECO:0000269|PubMed:19863551,
FT ECO:0000269|PubMed:20031617"
FT /id="VAR_033862"
FT VARIANT 445
FT /note="I -> V (in ARVD8; dbSNP:rs934142779)"
FT /id="VAR_065693"
FT VARIANT 564
FT /note="T -> I (in DCWHKTA; dbSNP:rs606231295)"
FT /evidence="ECO:0000269|PubMed:22795705"
FT /id="VAR_072432"
FT VARIANT 597
FT /note="S -> L (in DCWHKTA; dbSNP:rs606231294)"
FT /evidence="ECO:0000269|PubMed:20940358"
FT /id="VAR_072433"
FT VARIANT 1255
FT /note="R -> K (in ARVD8; dbSNP:rs777407386)"
FT /evidence="ECO:0000269|PubMed:15941723,
FT ECO:0000269|PubMed:20031617"
FT /id="VAR_023814"
FT VARIANT 1505
FT /note="A -> V (in dbSNP:rs375919492)"
FT /evidence="ECO:0000269|PubMed:20031617"
FT /id="VAR_065694"
FT VARIANT 1512
FT /note="Y -> C (in dbSNP:rs2076299)"
FT /evidence="ECO:0000269|PubMed:19863551,
FT ECO:0000269|PubMed:20031617"
FT /id="VAR_020468"
FT VARIANT 1526
FT /note="N -> K (in dbSNP:rs28763966)"
FT /evidence="ECO:0000269|PubMed:19863551,
FT ECO:0000269|PubMed:20031617"
FT /id="VAR_065695"
FT VARIANT 1537
FT /note="R -> C (in dbSNP:rs28763967)"
FT /evidence="ECO:0000269|PubMed:19863551,
FT ECO:0000269|PubMed:20031617"
FT /id="VAR_065696"
FT VARIANT 1738
FT /note="R -> Q (in dbSNP:rs6929069)"
FT /evidence="ECO:0000269|PubMed:19863551,
FT ECO:0000269|PubMed:20031617"
FT /id="VAR_023815"
FT VARIANT 1775
FT /note="R -> I (in ARVD8; unknown pathological significance;
FT dbSNP:rs34738426)"
FT /evidence="ECO:0000269|PubMed:15941723,
FT ECO:0000269|PubMed:20031617"
FT /id="VAR_023816"
FT VARIANT 1833
FT /note="E -> V (in dbSNP:rs78652302)"
FT /evidence="ECO:0000269|PubMed:19863551,
FT ECO:0000269|PubMed:21062920"
FT /id="VAR_065697"
FT VARIANT 2366
FT /note="R -> C (in SFWHS; dbSNP:rs28931610)"
FT /evidence="ECO:0000269|PubMed:11841538"
FT /id="VAR_015570"
FT VARIANT 2375
FT /note="G -> R (in a case of recessive arrhythmogenic right
FT ventricular cardiomyopathy with skin abnormalities and
FT woolly hair; dbSNP:rs376923069)"
FT /evidence="ECO:0000269|PubMed:12875771"
FT /id="VAR_018158"
FT MUTAGEN 2849
FT /note="S->G: Increases association with KRT5-KRT14, KRT8-
FT KRT18 or VIM intermediate filaments."
FT /evidence="ECO:0000269|PubMed:12802069"
FT CONFLICT 905
FT /note="A -> R (in Ref. 1; AAA85135)"
FT /evidence="ECO:0000305"
FT CONFLICT 1120
FT /note="D -> R (in Ref. 5; AAA35766)"
FT /evidence="ECO:0000305"
FT CONFLICT 2687..2688
FT /note="RL -> SV (in Ref. 1; AAA85135 and 5; AAA35766)"
FT /evidence="ECO:0000305"
FT HELIX 182..201
FT /evidence="ECO:0007829|PDB:3R6N"
FT HELIX 211..241
FT /evidence="ECO:0007829|PDB:3R6N"
FT HELIX 245..294
FT /evidence="ECO:0007829|PDB:3R6N"
FT HELIX 307..338
FT /evidence="ECO:0007829|PDB:3R6N"
FT HELIX 344..402
FT /evidence="ECO:0007829|PDB:3R6N"
FT HELIX 411..442
FT /evidence="ECO:0007829|PDB:3R6N"
FT HELIX 449..451
FT /evidence="ECO:0007829|PDB:3R6N"
FT STRAND 462..467
FT /evidence="ECO:0007829|PDB:3R6N"
FT STRAND 469..471
FT /evidence="ECO:0007829|PDB:3R6N"
FT STRAND 474..476
FT /evidence="ECO:0007829|PDB:3R6N"
FT STRAND 481..486
FT /evidence="ECO:0007829|PDB:3R6N"
FT STRAND 488..496
FT /evidence="ECO:0007829|PDB:3R6N"
FT STRAND 498..500
FT /evidence="ECO:0007829|PDB:3R6N"
FT STRAND 503..506
FT /evidence="ECO:0007829|PDB:3R6N"
FT HELIX 507..509
FT /evidence="ECO:0007829|PDB:3R6N"
FT HELIX 517..561
FT /evidence="ECO:0007829|PDB:3R6N"
FT HELIX 565..568
FT /evidence="ECO:0007829|PDB:3R6N"
FT TURN 573..575
FT /evidence="ECO:0007829|PDB:3R6N"
FT HELIX 576..594
FT /evidence="ECO:0007829|PDB:3R6N"
FT HELIX 602..624
FT /evidence="ECO:0007829|PDB:3R6N"
FT HELIX 1963..1965
FT /evidence="ECO:0007829|PDB:5DZZ"
FT STRAND 1967..1969
FT /evidence="ECO:0007829|PDB:5DZZ"
FT STRAND 1971..1976
FT /evidence="ECO:0007829|PDB:5DZZ"
FT HELIX 1977..1982
FT /evidence="ECO:0007829|PDB:5DZZ"
FT HELIX 1988..1996
FT /evidence="ECO:0007829|PDB:5DZZ"
FT STRAND 1997..1999
FT /evidence="ECO:0007829|PDB:5DZZ"
FT HELIX 2001..2005
FT /evidence="ECO:0007829|PDB:5DZZ"
FT HELIX 2009..2012
FT /evidence="ECO:0007829|PDB:5DZZ"
FT STRAND 2018..2021
FT /evidence="ECO:0007829|PDB:5DZZ"
FT STRAND 2023..2027
FT /evidence="ECO:0007829|PDB:5DZZ"
FT HELIX 2031..2036
FT /evidence="ECO:0007829|PDB:5DZZ"
FT HELIX 2042..2054
FT /evidence="ECO:0007829|PDB:5DZZ"
FT TURN 2061..2063
FT /evidence="ECO:0007829|PDB:5DZZ"
FT HELIX 2069..2074
FT /evidence="ECO:0007829|PDB:5DZZ"
FT HELIX 2083..2094
FT /evidence="ECO:0007829|PDB:5DZZ"
FT TURN 2099..2101
FT /evidence="ECO:0007829|PDB:5DZZ"
FT HELIX 2107..2112
FT /evidence="ECO:0007829|PDB:5DZZ"
FT HELIX 2118..2129
FT /evidence="ECO:0007829|PDB:5DZZ"
FT TURN 2130..2132
FT /evidence="ECO:0007829|PDB:5DZZ"
FT STRAND 2133..2136
FT /evidence="ECO:0007829|PDB:5DZZ"
FT TURN 2137..2140
FT /evidence="ECO:0007829|PDB:5DZZ"
FT STRAND 2141..2143
FT /evidence="ECO:0007829|PDB:5DZZ"
FT HELIX 2145..2150
FT /evidence="ECO:0007829|PDB:5DZZ"
FT HELIX 2156..2161
FT /evidence="ECO:0007829|PDB:5DZZ"
FT TURN 2165..2168
FT /evidence="ECO:0007829|PDB:5DZZ"
FT STRAND 2175..2177
FT /evidence="ECO:0007829|PDB:5DZZ"
FT HELIX 2183..2187
FT /evidence="ECO:0007829|PDB:5DZZ"
FT STRAND 2190..2192
FT /evidence="ECO:0007829|PDB:5DZZ"
FT TURN 2194..2196
FT /evidence="ECO:0007829|PDB:5DZZ"
FT STRAND 2199..2201
FT /evidence="ECO:0007829|PDB:5DZZ"
FT STRAND 2209..2211
FT /evidence="ECO:0007829|PDB:5DZZ"
FT STRAND 2213..2218
FT /evidence="ECO:0007829|PDB:5DZZ"
FT HELIX 2219..2224
FT /evidence="ECO:0007829|PDB:5DZZ"
FT HELIX 2230..2237
FT /evidence="ECO:0007829|PDB:5DZZ"
FT HELIX 2243..2249
FT /evidence="ECO:0007829|PDB:5DZZ"
FT HELIX 2251..2254
FT /evidence="ECO:0007829|PDB:5DZZ"
FT STRAND 2260..2265
FT /evidence="ECO:0007829|PDB:5DZZ"
FT TURN 2266..2269
FT /evidence="ECO:0007829|PDB:5DZZ"
FT STRAND 2270..2272
FT /evidence="ECO:0007829|PDB:5DZZ"
FT HELIX 2274..2280
FT /evidence="ECO:0007829|PDB:5DZZ"
FT HELIX 2285..2296
FT /evidence="ECO:0007829|PDB:5DZZ"
FT STRAND 2301..2303
FT /evidence="ECO:0007829|PDB:5DZZ"
FT TURN 2304..2307
FT /evidence="ECO:0007829|PDB:5DZZ"
FT STRAND 2308..2310
FT /evidence="ECO:0007829|PDB:5DZZ"
FT HELIX 2312..2317
FT /evidence="ECO:0007829|PDB:5DZZ"
FT HELIX 2326..2332
FT /evidence="ECO:0007829|PDB:5DZZ"
FT HELIX 2334..2337
FT /evidence="ECO:0007829|PDB:5DZZ"
FT TURN 2342..2344
FT /evidence="ECO:0007829|PDB:5DZZ"
FT STRAND 2346..2348
FT /evidence="ECO:0007829|PDB:5DZZ"
FT HELIX 2350..2355
FT /evidence="ECO:0007829|PDB:5DZZ"
FT HELIX 2361..2372
FT /evidence="ECO:0007829|PDB:5DZZ"
FT TURN 2373..2375
FT /evidence="ECO:0007829|PDB:5DZZ"
FT STRAND 2376..2379
FT /evidence="ECO:0007829|PDB:5DZZ"
FT TURN 2380..2383
FT /evidence="ECO:0007829|PDB:5DZZ"
FT STRAND 2384..2386
FT /evidence="ECO:0007829|PDB:5DZZ"
FT HELIX 2390..2393
FT /evidence="ECO:0007829|PDB:5DZZ"
FT HELIX 2399..2406
FT /evidence="ECO:0007829|PDB:5DZZ"
FT TURN 2410..2412
FT /evidence="ECO:0007829|PDB:5DZZ"
FT STRAND 2415..2417
FT /evidence="ECO:0007829|PDB:5DZZ"
FT TURN 2418..2421
FT /evidence="ECO:0007829|PDB:5DZZ"
FT STRAND 2422..2424
FT /evidence="ECO:0007829|PDB:5DZZ"
FT HELIX 2426..2430
FT /evidence="ECO:0007829|PDB:5DZZ"
FT TURN 2437..2439
FT /evidence="ECO:0007829|PDB:5DZZ"
FT STRAND 2442..2446
FT /evidence="ECO:0007829|PDB:5DZZ"
FT STRAND 2619..2624
FT /evidence="ECO:0007829|PDB:1LM5"
FT TURN 2625..2628
FT /evidence="ECO:0007829|PDB:1LM5"
FT STRAND 2629..2631
FT /evidence="ECO:0007829|PDB:1LM5"
FT HELIX 2633..2638
FT /evidence="ECO:0007829|PDB:1LM5"
FT HELIX 2644..2655
FT /evidence="ECO:0007829|PDB:1LM5"
FT TURN 2656..2658
FT /evidence="ECO:0007829|PDB:1LM5"
FT STRAND 2659..2661
FT /evidence="ECO:0007829|PDB:1LM5"
FT TURN 2663..2665
FT /evidence="ECO:0007829|PDB:1LM5"
FT HELIX 2671..2676
FT /evidence="ECO:0007829|PDB:1LM5"
FT HELIX 2682..2696
FT /evidence="ECO:0007829|PDB:1LM5"
FT HELIX 2709..2714
FT /evidence="ECO:0007829|PDB:1LM5"
FT HELIX 2720..2732
FT /evidence="ECO:0007829|PDB:1LM5"
FT HELIX 2739..2741
FT /evidence="ECO:0007829|PDB:1LM5"
FT HELIX 2747..2752
FT /evidence="ECO:0007829|PDB:1LM5"
FT HELIX 2758..2765
FT /evidence="ECO:0007829|PDB:1LM5"
FT HELIX 2767..2769
FT /evidence="ECO:0007829|PDB:1LM5"
FT TURN 2777..2779
FT /evidence="ECO:0007829|PDB:1LM5"
FT HELIX 2785..2791
FT /evidence="ECO:0007829|PDB:1LM5"
FT TURN 2796..2798
FT /evidence="ECO:0007829|PDB:1LM5"
FT STRAND 2801..2805
FT /evidence="ECO:0007829|PDB:1LM5"
SQ SEQUENCE 2871 AA; 331774 MW; 5770CC6B4F9F9F7B CRC64;
MSCNGGSHPR INTLGRMIRA ESGPDLRYEV TSGGGGTSRM YYSRRGVITD QNSDGYCQTG
TMSRHQNQNT IQELLQNCSD CLMRAELIVQ PELKYGDGIQ LTRSRELDEC FAQANDQMEI
LDSLIREMRQ MGQPCDAYQK RLLQLQEQMR ALYKAISVPR VRRASSKGGG GYTCQSGSGW
DEFTKHVTSE CLGWMRQQRA EMDMVAWGVD LASVEQHINS HRGIHNSIGD YRWQLDKIKA
DLREKSAIYQ LEEEYENLLK ASFERMDHLR QLQNIIQATS REIMWINDCE EEELLYDWSD
KNTNIAQKQE AFSIRMSQLE VKEKELNKLK QESDQLVLNQ HPASDKIEAY MDTLQTQWSW
ILQITKCIDV HLKENAAYFQ FFEEAQSTEA YLKGLQDSIR KKYPCDKNMP LQHLLEQIKE
LEKEREKILE YKRQVQNLVN KSKKIVQLKP RNPDYRSNKP IILRALCDYK QDQKIVHKGD
ECILKDNNER SKWYVTGPGG VDMLVPSVGL IIPPPNPLAV DLSCKIEQYY EAILALWNQL
YINMKSLVSW HYCMIDIEKI RAMTIAKLKT MRQEDYMKTI ADLELHYQEF IRNSQGSEMF
GDDDKRKIQS QFTDAQKHYQ TLVIQLPGYP QHQTVTTTEI THHGTCQDVN HNKVIETNRE
NDKQETWMLM ELQKIRRQIE HCEGRMTLKN LPLADQGSSH HITVKINELK SVQNDSQAIA
EVLNQLKDML ANFRGSEKYC YLQNEVFGLF QKLENINGVT DGYLNSLCTV RALLQAILQT
EDMLKVYEAR LTEEETVCLD LDKVEAYRCG LKKIKNDLNL KKSLLATMKT ELQKAQQIHS
QTSQQYPLYD LDLGKFGEKV TQLTDRWQRI DKQIDFRLWD LEKQIKQLRN YRDNYQAFCK
WLYDAKRRQD SLESMKFGDS NTVMRFLNEQ KNLHSEISGK RDKSEEVQKI AELCANSIKD
YELQLASYTS GLETLLNIPI KRTMIQSPSG VILQEAADVH ARYIELLTRS GDYYRFLSEM
LKSLEDLKLK NTKIEVLEEE LRLARDANSE NCNKNKFLDQ NLQKYQAECS QFKAKLASLE
ELKRQAELDG KSAKQNLDKC YGQIKELNEK ITRLTYEIED EKRRRKSVED RFDQQKNDYD
QLQKARQCEK ENLGWQKLES EKAIKEKEYE IERLRVLLQE EGTRKREYEN ELAKVRNHYN
EEMSNLRNKY ETEINITKTT IKEISMQKED DSKNLRNQLD RLSRENRDLK DEIVRLNDSI
LQATEQRRRA EENALQQKAC GSEIMQKKQH LEIELKQVMQ QRSEDNARHK QSLEEAAKTI
QDKNKEIERL KAEFQEEAKR RWEYENELSK VRNNYDEEII SLKNQFETEI NITKTTIHQL
TMQKEEDTSG YRAQIDNLTR ENRSLSEEIK RLKNTLTQTT ENLRRVEEDI QQQKATGSEV
SQRKQQLEVE LRQVTQMRTE ESVRYKQSLD DAAKTIQDKN KEIERLKQLI DKETNDRKCL
EDENARLQRV QYDLQKANSS ATETINKLKV QEQELTRLRI DYERVSQERT VKDQDITRFQ
NSLKELQLQK QKVEEELNRL KRTASEDSCK RKKLEEELEG MRRSLKEQAI KITNLTQQLE
QASIVKKRSE DDLRQQRDVL DGHLREKQRT QEELRRLSSE VEALRRQLLQ EQESVKQAHL
RNEHFQKAIE DKSRSLNESK IEIERLQSLT ENLTKEHLML EEELRNLRLE YDDLRRGRSE
ADSDKNATIL ELRSQLQISN NRTLELQGLI NDLQRERENL RQEIEKFQKQ ALEASNRIQE
SKNQCTQVVQ ERESLLVKIK VLEQDKARLQ RLEDELNRAK STLEAETRVK QRLECEKQQI
QNDLNQWKTQ YSRKEEAIRK IESEREKSER EKNSLRSEIE RLQAEIKRIE ERCRRKLEDS
TRETQSQLET ERSRYQREID KLRQRPYGSH RETQTECEWT VDTSKLVFDG LRKKVTAMQL
YECQLIDKTT LDKLLKGKKS VEEVASEIQP FLRGAGSIAG ASASPKEKYS LVEAKRKKLI
SPESTVMLLE AQAATGGIID PHRNEKLTVD SAIARDLIDF DDRQQIYAAE KAITGFDDPF
SGKTVSVSEA IKKNLIDRET GMRLLEAQIA SGGVVDPVNS VFLPKDVALA RGLIDRDLYR
SLNDPRDSQK NFVDPVTKKK VSYVQLKERC RIEPHTGLLL LSVQKRSMSF QGIRQPVTVT
ELVDSGILRP STVNELESGQ ISYDEVGERI KDFLQGSSCI AGIYNETTKQ KLGIYEAMKI
GLVRPGTALE LLEAQAATGF IVDPVSNLRL PVEEAYKRGL VGIEFKEKLL SAERAVTGYN
DPETGNIISL FQAMNKELIE KGHGIRLLEA QIATGGIIDP KESHRLPVDI AYKRGYFNEE
LSEILSDPSD DTKGFFDPNT EENLTYLQLK ERCIKDEETG LCLLPLKEKK KQVQTSQKNT
LRKRRVVIVD PETNKEMSVQ EAYKKGLIDY ETFKELCEQE CEWEEITITG SDGSTRVVLV
DRKTGSQYDI QDAIDKGLVD RKFFDQYRSG SLSLTQFADM ISLKNGVGTS SSMGSGVSDD
VFSSSRHESV SKISTISSVR NLTIRSSSFS DTLEESSPIA AIFDTENLEK ISITEGIERG
IVDSITGQRL LEAQACTGGI IHPTTGQKLS LQDAVSQGVI DQDMATRLKP AQKAFIGFEG
VKGKKKMSAA EAVKEKWLPY EAGQRFLEFQ YLTGGLVDPE VHGRISTEEA IRKGFIDGRA
AQRLQDTSSY AKILTCPKTK LKISYKDAIN RSMVEDITGL RLLEAASVSS KGLPSPYNMS
SAPGSRSGSR SGSRSGSRSG SRSGSRRGSF DATGNSSYSY SYSFSSSSIG H
