Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Desmoplakin (DP) (250/210 kDa paraneoplastic pemphigus antigen)

 DESP_HUMAN              Reviewed;        2871 AA.
P15924; B2RTT2; D7RX09; O75993; Q14189; Q9UHN4;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
03-OCT-2006, sequence version 3.
30-AUG-2017, entry version 214.
RecName: Full=Desmoplakin;
Short=DP;
AltName: Full=250/210 kDa paraneoplastic pemphigus antigen;
Name=DSP;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM DPI).
TISSUE=Foreskin;
PubMed=1731325; DOI=10.1073/pnas.89.2.544;
Virata M.L.A., Wagner R.M., Parry D.A.D., Green K.J.;
"Molecular structure of the human desmoplakin I and II amino
terminus.";
Proc. Natl. Acad. Sci. U.S.A. 89:544-548(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM DSPIA).
PubMed=20524011; DOI=10.1007/s00441-010-0989-1;
Cabral R.M., Wan H., Cole C.L., Abrams D.J., Kelsell D.P., South A.P.;
"Identification and characterization of DSPIa, a novel isoform of
human desmoplakin.";
Cell Tissue Res. 341:121-129(2010).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
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.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM DPII).
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 1120-2871 (ISOFORM DPI).
TISSUE=Foreskin;
PubMed=1689290;
Green K.J., Parry D.A.D., Steinert P.M., Virata M.L.A., Wagner R.M.,
Angst B.D., Nilles L.A.;
"Structure of the human desmoplakins. Implications for function in the
desmosomal plaque.";
J. Biol. Chem. 265:2603-2612(1990).
[6]
ERRATUM.
PubMed=2391353;
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. 265:11406-11407(1990).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 2854-2871.
TISSUE=Skin;
PubMed=10594734; DOI=10.1046/j.1523-1747.1999.00783.x;
Whittock N.V., Ashton G.H., Dopping-Hepenstal P.J., Gratian M.J.,
Keane F.M., Eady R.A.J., McGrath J.A.;
"Striate palmoplantar keratoderma resulting from desmoplakin
haploinsufficiency.";
J. Invest. Dermatol. 113:940-946(1999).
[8]
CHARACTERIZATION.
PubMed=9348293; DOI=10.1083/jcb.139.3.773;
Kowalczyk A.P., Bornslaeger E.A., Borgwardt J.E., Palka H.L.,
Dhaliwal A.S., Corcoran C.M., Denning M.F., Green K.J.;
"The amino-terminal domain of desmoplakin binds to plakoglobin and
clusters desmosomal cadherin-plakoglobin complexes.";
J. Cell Biol. 139:773-784(1997).
[9]
INVOLVEMENT IN SPPK2.
PubMed=9887343; DOI=10.1093/hmg/8.1.143;
Armstrong D.K., McKenna K.E., Purkis P.E., Green K.J., Eady R.A.J.,
Leigh I.M., Hughes A.E.;
"Haploinsufficiency of desmoplakin causes a striate subtype of
palmoplantar keratoderma.";
Hum. Mol. Genet. 8:143-148(1999).
[10]
ERRATUM.
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. 8:943-943(1999).
[11]
INVOLVEMENT IN DCWHK.
PubMed=11063735; DOI=10.1093/hmg/9.18.2761;
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.;
"Recessive mutation in desmoplakin disrupts desmoplakin-intermediate
filament interactions and causes dilated cardiomyopathy, woolly hair
and keratoderma.";
Hum. Mol. Genet. 9:2761-2766(2000).
[12]
INTERACTION WITH COL17A1.
PubMed=12482924; DOI=10.1242/jcs.00241;
Koster J., Geerts D., Favre B., Borradori L., Sonnenberg A.;
"Analysis of the interactions between BP180, BP230, plectin and the
integrin alpha6beta4 important for hemidesmosome assembly.";
J. Cell Sci. 116:387-399(2003).
[13]
ASSOCIATION WITH KERATIN FILAMENTS, MUTAGENESIS OF SER-2849, AND
SUBCELLULAR LOCATION.
PubMed=12802069; DOI=10.1091/mbc.E02-08-0548;
Fontao L., Favre B., Riou S., Geerts D., Jaunin F., Saurat J.H.,
Green K.J., Sonnenberg A., Borradori L.;
"Interaction of the bullous pemphigoid antigen 1 (BP230) and
desmoplakin with intermediate filaments is mediated by distinct
sequences within their COOH terminus.";
Mol. Biol. Cell 14:1978-1992(2003).
[14]
INVOLVEMENT IN DCWHKTA.
PubMed=16628197; DOI=10.1038/sj.jid.5700291;
Norgett E.E., Lucke T.W., Bowers B., Munro C.S., Leigh I.M.,
Kelsell D.P.;
"Early death from cardiomyopathy in a family with autosomal dominant
striate palmoplantar keratoderma and woolly hair associated with a
novel insertion mutation in desmoplakin.";
J. Invest. Dermatol. 126:1651-1654(2006).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2825, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[17]
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, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2024; SER-2207;
SER-2209; SER-2815 AND SER-2825, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
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.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[22]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[23]
INTERACTION WITH DSC2, AND VARIANT VAL-1833.
PubMed=21062920; DOI=10.1093/cvr/cvq353;
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.;
"Mechanistic insights into arrhythmogenic right ventricular
cardiomyopathy caused by desmocollin-2 mutations.";
Cardiovasc. Res. 90:77-87(2011).
[24]
INVOLVEMENT IN DCWHKTA, AND VARIANT DCWHKTA LEU-597.
PubMed=20940358; DOI=10.1177/0022034510383984;
Chalabreysse L., Senni F., Bruyere P., Aime B., Ollagnier C.,
Bozio A., Bouvagnet P.;
"A new hypo/oligodontia syndrome: Carvajal/Naxos syndrome secondary to
desmoplakin-dominant mutations.";
J. Dent. Res. 90:58-64(2011).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22; SER-2209; SER-2820
AND SER-2825, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[26]
INTERACTION WITH PKP2.
PubMed=22781308; DOI=10.1161/CIRCGENETICS.111.961854;
Kirchner F., Schuetz A., Boldt L.H., Martens K., Dittmar G.,
Haverkamp W., Thierfelder L., Heinemann U., Gerull B.;
"Molecular insights into arrhythmogenic right ventricular
cardiomyopathy caused by plakophilin-2 missense mutations.";
Circ. Cardiovasc. Genet. 5:400-411(2012).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22; SER-165; SER-1658;
SER-1708; SER-2024; SER-2209; SER-2810; TYR-2817; SER-2820 AND
SER-2825, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22; SER-53; SER-165;
SER-166; SER-1708; SER-2209 AND SER-2225, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[29]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 2209-2456, X-RAY
CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 2609-2822, AND DOMAIN PLAKIN
REPEATS.
PubMed=12101406; DOI=10.1038/nsb818;
Choi H.J., Park-Snyder S., Pascoe L.T., Green K.J., Weis W.I.;
"Structures of two intermediate filament-binding fragments of
desmoplakin reveal a unique repeat motif structure.";
Nat. Struct. Biol. 9:612-620(2002).
[30]
X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF 178-627, DOMAIN SPECTRIN
REPEATS, AND DOMAIN SH3.
PubMed=21536047; DOI=10.1016/j.jmb.2011.04.046;
Choi H.J., Weis W.I.;
"Crystal structure of a rigid four-spectrin-repeat fragment of the
human desmoplakin plakin domain.";
J. Mol. Biol. 409:800-812(2011).
[31]
VARIANT ARVD8 ARG-299.
PubMed=12373648; DOI=10.1086/344208;
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.;
"Mutation in human desmoplakin domain binding to plakoglobin causes a
dominant form of arrhythmogenic right ventricular cardiomyopathy.";
Am. J. Hum. Genet. 71:1200-1206(2002).
[32]
VARIANTS SFWHS LYS-287 AND CYS-2366.
PubMed=11841538; DOI=10.1046/j.0022-202x.2001.01664.x;
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.;
"Compound heterozygosity for non-sense and mis-sense mutations in
desmoplakin underlies skin fragility/woolly hair syndrome.";
J. Invest. Dermatol. 118:232-238(2002).
[33]
VARIANT ARRHYTHMOGENIC CARDIOMYOPATHY ARG-2375.
PubMed=12875771; DOI=10.1016/S0735-1097(03)00628-4;
Alcalai R., Metzger S., Rosenheck S., Meiner V., Chajek-Shaul T.;
"A recessive mutation in desmoplakin causes arrhythmogenic right
ventricular dysplasia, skin disorder, and woolly hair.";
J. Am. Coll. Cardiol. 42:319-327(2003).
[34]
INVOLVEMENT IN LETHAL ACANTHOLYTIC EPIDERMOLYSIS BULLOSA.
PubMed=16175511; DOI=10.1086/496901;
Jonkman M.F., Pasmooij A.M.G., Pasmans S.G.M.A., van den Berg M.P.,
Ter Horst H.J., Timmer A., Pas H.H.;
"Loss of desmoplakin tail causes lethal acantholytic epidermolysis
bullosa.";
Am. J. Hum. Genet. 77:653-660(2005).
[35]
VARIANTS ARVD8 ARG-299; LYS-1255 AND ILE-1775.
PubMed=15941723; DOI=10.1093/eurheartj/ehi341;
Bauce B., Basso C., Rampazzo A., Beffagna G., Daliento L., Frigo G.,
Malacrida S., Settimo L., Danieli G., Thiene G., Nava A.;
"Clinical profile of four families with arrhythmogenic right
ventricular cardiomyopathy caused by dominant desmoplakin mutations.";
Eur. Heart J. 26:1666-1675(2005).
[36]
VARIANTS ARVD8 ARG-299; LYS-1255 AND ILE-1775, AND VARIANTS PHE-305;
VAL-1505; CYS-1512; LYS-1526; CYS-1537 AND GLN-1738.
PubMed=20031617; DOI=10.1161/CIRCGENETICS.109.858217;
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.;
"Comprehensive desmosome mutation analysis in North Americans with
arrhythmogenic right ventricular dysplasia/cardiomyopathy.";
Circ. Cardiovasc. Genet. 2:428-435(2009).
[37]
VARIANTS PHE-305; CYS-1512; LYS-1526; CYS-1537; CYS-1537; GLN-1738 AND
VAL-1833.
PubMed=19863551; DOI=10.1111/j.1399-0004.2009.01282.x;
Barahona-Dussault C., Benito B., Campuzano O., Iglesias A.,
Leung T.L., Robb L., Talajic M., Brugada R.;
"Role of genetic testing in arrhythmogenic right ventricular
cardiomyopathy/dysplasia.";
Clin. Genet. 77:37-48(2010).
[38]
VARIANT DCWHKTA ILE-564.
PubMed=22795705; DOI=10.1016/j.ijcard.2012.06.068;
Boule S., Fressart V., Laux D., Mallet A., Simon F., de Groote P.,
Bonnet D., Klug D., Charron P.;
"Expanding the phenotype associated with a desmoplakin dominant
mutation: Carvajal/Naxos syndrome associated with leukonychia and
oligodontia.";
Int. J. Cardiol. 161:50-52(2012).
-!- FUNCTION: Major high molecular weight protein of desmosomes.
Involved in the organization of the desmosomal cadherin-
plakoglobin complexes into discrete plasma membrane domains and in
the anchoring of intermediate filaments to the desmosomes.
-!- SUBUNIT: Homodimer. Interacts with COL17A1 (via cytoplasmic
region). Associates (via C-terminal) with KRT5-KRT14 (via rod
region), KRT8-KRT18 and VIM intermediate filaments. Interacts with
DSC2. Interacts with PKP2. Interacts weakly with TMEM65 (By
similarity). {ECO:0000250|UniProtKB:E9Q557,
ECO:0000269|PubMed:12482924, ECO:0000269|PubMed:21062920,
ECO:0000269|PubMed:22781308}.
-!- INTERACTION:
Q15691:MAPRE1; NbExp=7; IntAct=EBI-355041, EBI-1004115;
Q13835-2:PKP1; NbExp=2; IntAct=EBI-355041, EBI-9087684;
-!- SUBCELLULAR LOCATION: Cell junction, desmosome
{ECO:0000269|PubMed:12802069}. Cytoplasm, cytoskeleton
{ECO:0000269|PubMed:12802069}. Cell membrane
{ECO:0000250|UniProtKB:E9Q557}. Note=Innermost portion of the
desmosomal plaque. Colocalizes with epidermal KRT5-KRT14 and
simple KRT8-KRT18 keratins and VIM intermediate filaments network
(PubMed:12802069). Localizes at the intercalated disk in
cardiomyocytes (By similarity). {ECO:0000250|UniProtKB:E9Q557,
ECO:0000269|PubMed:12802069}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=DPI; Synonyms=DP1;
IsoId=P15924-1; Sequence=Displayed;
Name=DPII; Synonyms=DP2;
IsoId=P15924-2; Sequence=VSP_005070;
Name=DSPIa;
IsoId=P15924-3; Sequence=VSP_053769;
Note=Minor isoform.;
-!- TISSUE SPECIFICITY: Isoform DPI is apparently an obligate
constituent of all desmosomes. Isoform DPII resides predominantly
in tissues and cells of stratified origin.
-!- DOMAIN: Its association with epidermal and simple keratins is
dependent on the tertiary structure induced by heterodimerization
of these intermediate filaments proteins and most likely involves
recognition sites located in the rod domain of these keratins.
-!- DOMAIN: The N-terminal region is required for localization to the
desmosomal plaque and interacts with the N-terminal region of
plakophilin 1.
-!- DOMAIN: The three tandem plakin repeat regions in the C-terminus
mediate binding to intermediate filaments.
-!- PTM: Ser-2849 is probably phosphorylated by a cAMP-dependent
protein kinase. Phosphorylation on Ser-2849 probably affects its
association with epidermal, simple cytokeratins and VIM
intermediate filaments.
-!- DISEASE: Keratoderma, palmoplantar, striate 2 (SPPK2)
[MIM:612908]: A dermatological disorder characterized by
thickening of the skin on the palms (linear pattern) and the soles
(island-like pattern) and flexor aspect of the fingers.
Abnormalities of the nails, the teeth and the hair are rarely
present. {ECO:0000269|PubMed:9887343}. Note=The disease is caused
by mutations affecting the gene represented in this entry.
-!- DISEASE: Cardiomyopathy, dilated, with woolly hair and keratoderma
(DCWHK) [MIM:605676]: An autosomal recessive cardiocutaneous
syndrome characterized by a generalized striate keratoderma
particularly affecting the palmoplantar epidermis, woolly hair,
and dilated left ventricular cardiomyopathy.
{ECO:0000269|PubMed:11063735}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Arrhythmogenic right ventricular dysplasia, familial, 8
(ARVD8) [MIM:607450]: A congenital heart disease characterized by
infiltration of adipose and fibrous tissue into the right
ventricle and loss of myocardial cells, resulting in ventricular
and supraventricular arrhythmias. {ECO:0000269|PubMed:12373648,
ECO:0000269|PubMed:15941723, ECO:0000269|PubMed:20031617}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Skin fragility-woolly hair syndrome (SFWHS) [MIM:607655]:
An autosomal recessive genodermatosis characterized by skin
fragility with blistering, focal and diffuse palmoplantar
keratoderma, hyperkeratotic plaques on the trunk and limbs, and
woolly hair with varying degrees of alopecia.
{ECO:0000269|PubMed:11841538}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Epidermolysis bullosa, lethal acantholytic (EBLA)
[MIM:609638]: A form of epidermolysis bullosa characterized by
severe fragility of skin and mucous membranes. The phenotype is
lethal in the neonatal period because of immense transcutaneous
fluid loss. Typical features include universal alopecia, neonatal
teeth, and nail loss. Histopathology of the skin shows suprabasal
clefting and acantholysis throughout the spinous layer, mimicking
pemphigus. Note=The disease is caused by mutations affecting the
gene represented in this entry.
-!- DISEASE: Cardiomyopathy, dilated, with woolly hair, keratoderma,
and tooth agenesis (DCWHKTA) [MIM:615821]: A cardiocutaneous
syndrome characterized by biventricular dilated cardiomyopathy,
hyperkeratosis, woolly hair, palmoplantar keratoderma, and
hypo/oligodontia. {ECO:0000269|PubMed:16628197,
ECO:0000269|PubMed:20940358, ECO:0000269|PubMed:22795705}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the plakin or cytolinker family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Wikipedia; Note=Desmoplakin entry;
URL="https://en.wikipedia.org/wiki/Desmoplakin";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M77830; AAA85135.1; -; mRNA.
EMBL; HM151899; ADI58529.1; -; mRNA.
EMBL; AL031058; CAA19927.1; -; Genomic_DNA.
EMBL; BC140802; AAI40803.1; -; mRNA.
EMBL; J05211; AAA35766.1; -; mRNA.
EMBL; AF139065; AAF19785.1; -; mRNA.
CCDS; CCDS4501.1; -. [P15924-1]
CCDS; CCDS47368.1; -. [P15924-2]
PIR; A38194; A38194.
RefSeq; NP_001008844.1; NM_001008844.2. [P15924-2]
RefSeq; NP_001305963.1; NM_001319034.1. [P15924-3]
RefSeq; NP_004406.2; NM_004415.3. [P15924-1]
UniGene; Hs.519873; -.
PDB; 1LM5; X-ray; 1.80 A; A/B=2609-2822.
PDB; 1LM7; X-ray; 3.00 A; A/B=2209-2456.
PDB; 3R6N; X-ray; 2.95 A; A/B=178-627.
PDB; 5DZZ; X-ray; 2.60 A; A=1960-2448.
PDBsum; 1LM5; -.
PDBsum; 1LM7; -.
PDBsum; 3R6N; -.
PDBsum; 5DZZ; -.
ProteinModelPortal; P15924; -.
SMR; P15924; -.
BioGrid; 108166; 100.
DIP; DIP-109N; -.
IntAct; P15924; 51.
MINT; MINT-1157663; -.
STRING; 9606.ENSP00000369129; -.
iPTMnet; P15924; -.
PhosphoSitePlus; P15924; -.
SwissPalm; P15924; -.
BioMuta; DSP; -.
DMDM; 115502381; -.
EPD; P15924; -.
MaxQB; P15924; -.
PaxDb; P15924; -.
PeptideAtlas; P15924; -.
PRIDE; P15924; -.
Ensembl; ENST00000379802; ENSP00000369129; ENSG00000096696. [P15924-1]
Ensembl; ENST00000418664; ENSP00000396591; ENSG00000096696. [P15924-2]
GeneID; 1832; -.
KEGG; hsa:1832; -.
UCSC; uc003mxp.2; human. [P15924-1]
CTD; 1832; -.
DisGeNET; 1832; -.
GeneCards; DSP; -.
GeneReviews; DSP; -.
HGNC; HGNC:3052; DSP.
HPA; CAB037324; -.
HPA; HPA045840; -.
HPA; HPA054950; -.
MalaCards; DSP; -.
MIM; 125647; gene.
MIM; 605676; phenotype.
MIM; 607450; phenotype.
MIM; 607655; phenotype.
MIM; 609638; phenotype.
MIM; 612908; phenotype.
MIM; 615821; phenotype.
neXtProt; NX_P15924; -.
OpenTargets; ENSG00000096696; -.
Orphanet; 293899; Familial isolated arrhythmogenic ventricular dysplasia, biventricular form.
Orphanet; 293888; Familial isolated arrhythmogenic ventricular dysplasia, left dominant form.
Orphanet; 293910; Familial isolated arrhythmogenic ventricular dysplasia, right dominant form.
Orphanet; 2032; Idiopathic pulmonary fibrosis.
Orphanet; 50942; Keratosis palmoplantaris striata.
Orphanet; 158687; Lethal acantholytic epidermolysis bullosa.
Orphanet; 293165; Skin fragility-woolly hair-palmoplantar keratoderma syndrome.
Orphanet; 65282; Woolly hair-palmoplantar keratoderma-dilated cardiomyopathy syndrome.
PharmGKB; PA27505; -.
eggNOG; ENOG410IQBR; Eukaryota.
eggNOG; ENOG4111ACS; LUCA.
GeneTree; ENSGT00760000119163; -.
HOGENOM; HOG000112198; -.
HOVERGEN; HBG081434; -.
InParanoid; P15924; -.
KO; K10381; -.
OMA; KRSMSFQ; -.
OrthoDB; EOG091G003R; -.
PhylomeDB; P15924; -.
TreeFam; TF106435; -.
Reactome; R-HSA-351906; Apoptotic cleavage of cell adhesion proteins.
Reactome; R-HSA-6798695; Neutrophil degranulation.
Reactome; R-HSA-6805567; Keratinization.
Reactome; R-HSA-6809371; Formation of the cornified envelope.
SIGNOR; P15924; -.
ChiTaRS; DSP; human.
EvolutionaryTrace; P15924; -.
GeneWiki; Desmoplakin; -.
GenomeRNAi; 1832; -.
PRO; PR:P15924; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000096696; -.
CleanEx; HS_DSP; -.
Genevisible; P15924; HS.
GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl.
GO; GO:0001533; C:cornified envelope; IDA:UniProtKB.
GO; GO:0030057; C:desmosome; IEA:UniProtKB-SubCell.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0031012; C:extracellular matrix; IDA:BHF-UCL.
GO; GO:0005916; C:fascia adherens; IEA:Ensembl.
GO; GO:0101003; C:ficolin-1-rich granule membrane; TAS:Reactome.
GO; GO:0014704; C:intercalated disc; IDA:BHF-UCL.
GO; GO:0005882; C:intermediate filament; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0050839; F:cell adhesion molecule binding; IEA:InterPro.
GO; GO:0086083; F:cell adhesive protein binding involved in bundle of His cell-Purkinje myocyte communication; IC:BHF-UCL.
GO; GO:0030674; F:protein binding, bridging; IDA:UniProtKB.
GO; GO:0005080; F:protein kinase C binding; IPI:BHF-UCL.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0097110; F:scaffold protein binding; IPI:BHF-UCL.
GO; GO:0005200; F:structural constituent of cytoskeleton; TAS:ProtInc.
GO; GO:0005198; F:structural molecule activity; IDA:UniProtKB.
GO; GO:0034332; P:adherens junction organization; IEA:Ensembl.
GO; GO:0086073; P:bundle of His cell-Purkinje myocyte adhesion involved in cell communication; IMP:BHF-UCL.
GO; GO:0070268; P:cornification; TAS:Reactome.
GO; GO:0002934; P:desmosome organization; ISS:BHF-UCL.
GO; GO:0008544; P:epidermis development; TAS:ProtInc.
GO; GO:0045109; P:intermediate filament organization; ISS:BHF-UCL.
GO; GO:0031424; P:keratinization; TAS:Reactome.
GO; GO:0030216; P:keratinocyte differentiation; IDA:UniProtKB.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0018149; P:peptide cross-linking; IDA:UniProtKB.
GO; GO:0071896; P:protein localization to adherens junction; ISS:BHF-UCL.
GO; GO:0086091; P:regulation of heart rate by cardiac conduction; IMP:BHF-UCL.
GO; GO:0098911; P:regulation of ventricular cardiac muscle cell action potential; IMP:BHF-UCL.
GO; GO:0003223; P:ventricular compact myocardium morphogenesis; ISS:BHF-UCL.
GO; GO:0042060; P:wound healing; IEA:Ensembl.
Gene3D; 3.90.1290.10; -; 4.
InterPro; IPR028462; Desmoplakin.
InterPro; IPR001101; Plectin_repeat.
InterPro; IPR018159; Spectrin/alpha-actinin.
PANTHER; PTHR11915:SF367; PTHR11915:SF367; 1.
Pfam; PF00681; Plectin; 8.
SMART; SM00250; PLEC; 18.
SMART; SM00150; SPEC; 3.
SUPFAM; SSF75399; SSF75399; 5.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cardiomyopathy; Cell junction;
Cell membrane; Coiled coil; Complete proteome; Cytoplasm;
Cytoskeleton; Disease mutation; Epidermolysis bullosa; Membrane;
Methylation; Palmoplantar keratoderma; Phosphoprotein; Polymorphism;
Reference proteome; Repeat.
CHAIN 1 2871 Desmoplakin.
/FTId=PRO_0000078144.
REPEAT 178 271 Spectrin 1.
REPEAT 272 375 Spectrin 2.
REPEAT 376 446 Spectrin 3a.
DOMAIN 447 515 SH3.
REPEAT 516 545 Spectrin 3b.
REPEAT 546 627 Spectrin 4.
REPEAT 654 769 Spectrin 5.
REPEAT 770 883 Spectrin 6.
REPEAT 2009 2045 Plectin 1.
REPEAT 2046 2083 Plectin 2.
REPEAT 2084 2121 Plectin 3.
REPEAT 2122 2159 Plectin 4.
REPEAT 2163 2197 Plectin 5.
REPEAT 2198 2233 Plectin 6.
REPEAT 2251 2288 Plectin 7.
REPEAT 2289 2326 Plectin 8.
REPEAT 2327 2364 Plectin 9.
REPEAT 2365 2402 Plectin 10.
REPEAT 2406 2440 Plectin 11.
REPEAT 2456 2493 Plectin 12.
REPEAT 2507 2544 Plectin 13.
REPEAT 2610 2647 Plectin 14.
REPEAT 2648 2685 Plectin 15.
REPEAT 2724 2761 Plectin 16.
REPEAT 2762 2799 Plectin 17.
REGION 1 1056 Globular 1.
REGION 1 584 Interaction with plakophilin 1 and
junction plakoglobin.
REGION 1057 1945 Central fibrous rod domain.
REGION 1946 2871 Globular 2.
REGION 1960 2208 4.5 X 38 AA tandem repeats (Domain A).
REGION 2244 2446 4.5 X 38 AA tandem repeats (Domain B).
REGION 2609 2822 4.5 X 38 AA tandem repeats (Domain C).
REGION 2824 2847 6 X 4 AA tandem repeats of G-S-R-[SR].
COILED 1018 1945 {ECO:0000255}.
MOD_RES 22 22 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 53 53 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 56 56 Phosphotyrosine.
{ECO:0000250|UniProtKB:E9Q557}.
MOD_RES 61 61 Phosphothreonine.
{ECO:0000250|UniProtKB:E9Q557}.
MOD_RES 165 165 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 166 166 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:24275569}.
MOD_RES 176 176 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1658 1658 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1708 1708 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 2024 2024 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 2207 2207 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 2209 2209 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 2225 2225 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 2810 2810 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 2815 2815 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 2817 2817 Phosphotyrosine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 2820 2820 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 2821 2821 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 2825 2825 Phosphoserine.
{ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 2826 2826 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:E9Q557}.
MOD_RES 2847 2847 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:E9Q557}.
MOD_RES 2849 2849 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 2853 2853 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 2868 2868 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
VAR_SEQ 1195 1793 Missing (in isoform DPII).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_005070.
VAR_SEQ 1351 1793 Missing (in isoform DSPIa).
{ECO:0000303|PubMed:20524011}.
/FTId=VSP_053769.
VARIANT 287 287 N -> K (in SFWHS; dbSNP:rs121912993).
{ECO:0000269|PubMed:11841538}.
/FTId=VAR_015569.
VARIANT 299 299 S -> R (in ARVD8; unknown pathological
significance; dbSNP:rs121912992).
{ECO:0000269|PubMed:12373648,
ECO:0000269|PubMed:15941723,
ECO:0000269|PubMed:20031617}.
/FTId=VAR_015402.
VARIANT 305 305 I -> F (in dbSNP:rs17604693).
{ECO:0000269|PubMed:19863551,
ECO:0000269|PubMed:20031617}.
/FTId=VAR_033862.
VARIANT 445 445 I -> V (in ARVD8).
/FTId=VAR_065693.
VARIANT 564 564 T -> I (in DCWHKTA; dbSNP:rs606231295).
{ECO:0000269|PubMed:22795705}.
/FTId=VAR_072432.
VARIANT 597 597 S -> L (in DCWHKTA; dbSNP:rs606231294).
{ECO:0000269|PubMed:20940358}.
/FTId=VAR_072433.
VARIANT 1255 1255 R -> K (in ARVD8; dbSNP:rs777407386).
{ECO:0000269|PubMed:15941723,
ECO:0000269|PubMed:20031617}.
/FTId=VAR_023814.
VARIANT 1505 1505 A -> V (in dbSNP:rs375919492).
{ECO:0000269|PubMed:20031617}.
/FTId=VAR_065694.
VARIANT 1512 1512 Y -> C (in dbSNP:rs2076299).
{ECO:0000269|PubMed:19863551,
ECO:0000269|PubMed:20031617}.
/FTId=VAR_020468.
VARIANT 1526 1526 N -> K (in dbSNP:rs28763966).
{ECO:0000269|PubMed:19863551,
ECO:0000269|PubMed:20031617}.
/FTId=VAR_065695.
VARIANT 1537 1537 R -> C (in dbSNP:rs28763967).
{ECO:0000269|PubMed:19863551,
ECO:0000269|PubMed:20031617}.
/FTId=VAR_065696.
VARIANT 1738 1738 R -> Q (in dbSNP:rs6929069).
{ECO:0000269|PubMed:19863551,
ECO:0000269|PubMed:20031617}.
/FTId=VAR_023815.
VARIANT 1775 1775 R -> I (in ARVD8; unknown pathological
significance; dbSNP:rs34738426).
{ECO:0000269|PubMed:15941723,
ECO:0000269|PubMed:20031617}.
/FTId=VAR_023816.
VARIANT 1833 1833 E -> V (in dbSNP:rs78652302).
{ECO:0000269|PubMed:19863551,
ECO:0000269|PubMed:21062920}.
/FTId=VAR_065697.
VARIANT 2366 2366 R -> C (in SFWHS; dbSNP:rs28931610).
{ECO:0000269|PubMed:11841538}.
/FTId=VAR_015570.
VARIANT 2375 2375 G -> R (in a case of recessive
arrhythmogenic right ventricular
cardiomyopathy with skin abnormalities
and woolly hair; dbSNP:rs376923069).
{ECO:0000269|PubMed:12875771}.
/FTId=VAR_018158.
MUTAGEN 2849 2849 S->G: Increases association with KRT5-
KRT14, KRT8-KRT18 or VIM intermediate
filaments. {ECO:0000269|PubMed:12802069}.
CONFLICT 905 905 A -> R (in Ref. 1; AAA85135).
{ECO:0000305}.
CONFLICT 1120 1120 D -> R (in Ref. 5; AAA35766).
{ECO:0000305}.
CONFLICT 2687 2688 RL -> SV (in Ref. 1; AAA85135 and 5;
AAA35766). {ECO:0000305}.
HELIX 182 201 {ECO:0000244|PDB:3R6N}.
HELIX 211 241 {ECO:0000244|PDB:3R6N}.
HELIX 245 294 {ECO:0000244|PDB:3R6N}.
HELIX 307 338 {ECO:0000244|PDB:3R6N}.
HELIX 344 402 {ECO:0000244|PDB:3R6N}.
HELIX 411 442 {ECO:0000244|PDB:3R6N}.
HELIX 449 451 {ECO:0000244|PDB:3R6N}.
STRAND 462 467 {ECO:0000244|PDB:3R6N}.
STRAND 469 471 {ECO:0000244|PDB:3R6N}.
STRAND 474 476 {ECO:0000244|PDB:3R6N}.
STRAND 481 486 {ECO:0000244|PDB:3R6N}.
STRAND 488 496 {ECO:0000244|PDB:3R6N}.
STRAND 498 500 {ECO:0000244|PDB:3R6N}.
STRAND 503 506 {ECO:0000244|PDB:3R6N}.
HELIX 507 509 {ECO:0000244|PDB:3R6N}.
HELIX 517 561 {ECO:0000244|PDB:3R6N}.
HELIX 565 568 {ECO:0000244|PDB:3R6N}.
TURN 573 575 {ECO:0000244|PDB:3R6N}.
HELIX 576 594 {ECO:0000244|PDB:3R6N}.
HELIX 602 624 {ECO:0000244|PDB:3R6N}.
HELIX 1963 1965 {ECO:0000244|PDB:5DZZ}.
STRAND 1967 1969 {ECO:0000244|PDB:5DZZ}.
STRAND 1971 1976 {ECO:0000244|PDB:5DZZ}.
HELIX 1977 1982 {ECO:0000244|PDB:5DZZ}.
HELIX 1988 1996 {ECO:0000244|PDB:5DZZ}.
STRAND 1997 1999 {ECO:0000244|PDB:5DZZ}.
HELIX 2001 2005 {ECO:0000244|PDB:5DZZ}.
HELIX 2009 2012 {ECO:0000244|PDB:5DZZ}.
STRAND 2018 2021 {ECO:0000244|PDB:5DZZ}.
STRAND 2023 2027 {ECO:0000244|PDB:5DZZ}.
HELIX 2031 2036 {ECO:0000244|PDB:5DZZ}.
HELIX 2042 2054 {ECO:0000244|PDB:5DZZ}.
TURN 2061 2063 {ECO:0000244|PDB:5DZZ}.
HELIX 2069 2074 {ECO:0000244|PDB:5DZZ}.
HELIX 2083 2094 {ECO:0000244|PDB:5DZZ}.
TURN 2099 2101 {ECO:0000244|PDB:5DZZ}.
HELIX 2107 2112 {ECO:0000244|PDB:5DZZ}.
HELIX 2118 2129 {ECO:0000244|PDB:5DZZ}.
TURN 2130 2132 {ECO:0000244|PDB:5DZZ}.
STRAND 2133 2136 {ECO:0000244|PDB:5DZZ}.
TURN 2137 2140 {ECO:0000244|PDB:5DZZ}.
STRAND 2141 2143 {ECO:0000244|PDB:5DZZ}.
HELIX 2145 2150 {ECO:0000244|PDB:5DZZ}.
HELIX 2156 2161 {ECO:0000244|PDB:5DZZ}.
TURN 2165 2168 {ECO:0000244|PDB:5DZZ}.
STRAND 2175 2177 {ECO:0000244|PDB:5DZZ}.
HELIX 2183 2187 {ECO:0000244|PDB:5DZZ}.
STRAND 2190 2192 {ECO:0000244|PDB:5DZZ}.
TURN 2194 2196 {ECO:0000244|PDB:5DZZ}.
STRAND 2199 2201 {ECO:0000244|PDB:5DZZ}.
STRAND 2209 2211 {ECO:0000244|PDB:5DZZ}.
STRAND 2213 2218 {ECO:0000244|PDB:5DZZ}.
HELIX 2219 2224 {ECO:0000244|PDB:5DZZ}.
HELIX 2230 2237 {ECO:0000244|PDB:5DZZ}.
HELIX 2243 2249 {ECO:0000244|PDB:5DZZ}.
HELIX 2251 2254 {ECO:0000244|PDB:5DZZ}.
STRAND 2260 2265 {ECO:0000244|PDB:5DZZ}.
TURN 2266 2269 {ECO:0000244|PDB:5DZZ}.
STRAND 2270 2272 {ECO:0000244|PDB:5DZZ}.
HELIX 2274 2280 {ECO:0000244|PDB:5DZZ}.
HELIX 2285 2296 {ECO:0000244|PDB:5DZZ}.
STRAND 2301 2303 {ECO:0000244|PDB:5DZZ}.
TURN 2304 2307 {ECO:0000244|PDB:5DZZ}.
STRAND 2308 2310 {ECO:0000244|PDB:5DZZ}.
HELIX 2312 2317 {ECO:0000244|PDB:5DZZ}.
HELIX 2326 2332 {ECO:0000244|PDB:5DZZ}.
HELIX 2334 2337 {ECO:0000244|PDB:5DZZ}.
TURN 2342 2344 {ECO:0000244|PDB:5DZZ}.
STRAND 2346 2348 {ECO:0000244|PDB:5DZZ}.
HELIX 2350 2355 {ECO:0000244|PDB:5DZZ}.
HELIX 2361 2372 {ECO:0000244|PDB:5DZZ}.
TURN 2373 2375 {ECO:0000244|PDB:5DZZ}.
STRAND 2376 2379 {ECO:0000244|PDB:5DZZ}.
TURN 2380 2383 {ECO:0000244|PDB:5DZZ}.
STRAND 2384 2386 {ECO:0000244|PDB:5DZZ}.
HELIX 2390 2393 {ECO:0000244|PDB:5DZZ}.
HELIX 2399 2406 {ECO:0000244|PDB:5DZZ}.
TURN 2410 2412 {ECO:0000244|PDB:5DZZ}.
STRAND 2415 2417 {ECO:0000244|PDB:5DZZ}.
TURN 2418 2421 {ECO:0000244|PDB:5DZZ}.
STRAND 2422 2424 {ECO:0000244|PDB:5DZZ}.
HELIX 2426 2430 {ECO:0000244|PDB:5DZZ}.
TURN 2437 2439 {ECO:0000244|PDB:5DZZ}.
STRAND 2442 2446 {ECO:0000244|PDB:5DZZ}.
STRAND 2619 2624 {ECO:0000244|PDB:1LM5}.
TURN 2625 2628 {ECO:0000244|PDB:1LM5}.
STRAND 2629 2631 {ECO:0000244|PDB:1LM5}.
HELIX 2633 2638 {ECO:0000244|PDB:1LM5}.
HELIX 2644 2655 {ECO:0000244|PDB:1LM5}.
TURN 2656 2658 {ECO:0000244|PDB:1LM5}.
STRAND 2659 2661 {ECO:0000244|PDB:1LM5}.
TURN 2663 2665 {ECO:0000244|PDB:1LM5}.
HELIX 2671 2676 {ECO:0000244|PDB:1LM5}.
HELIX 2682 2696 {ECO:0000244|PDB:1LM5}.
HELIX 2709 2714 {ECO:0000244|PDB:1LM5}.
HELIX 2720 2732 {ECO:0000244|PDB:1LM5}.
HELIX 2739 2741 {ECO:0000244|PDB:1LM5}.
HELIX 2747 2752 {ECO:0000244|PDB:1LM5}.
HELIX 2758 2765 {ECO:0000244|PDB:1LM5}.
HELIX 2767 2769 {ECO:0000244|PDB:1LM5}.
TURN 2777 2779 {ECO:0000244|PDB:1LM5}.
HELIX 2785 2791 {ECO:0000244|PDB:1LM5}.
TURN 2796 2798 {ECO:0000244|PDB:1LM5}.
STRAND 2801 2805 {ECO:0000244|PDB:1LM5}.
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


Related products :

Catalog number Product name Quantity
EIAAB10960 250_210 kDa paraneoplastic pemphigus antigen,Desmoplakin,DP,DSP,Homo sapiens,Human
EIAAB30564 190 kDa paraneoplastic pemphigus antigen,195 kDa cornified envelope precursor protein,Homo sapiens,Human,KIAA0568,Periplakin,PPL
EIAAB13426 210 kDa cornified envelope precursor protein,210 kDa paraneoplastic pemphigus antigen,Envoplakin,EVPL,Homo sapiens,Human,p210
E02P0692 Rat paraneoplastic pemphigus 96 Tests/kit
E06P0692 Goat paraneoplastic pemphigus 96 Tests/kit
E05P0692 Guinea paraneoplastic pemphigus 96 Tests/kit
E01P0692 Human paraneoplastic pemphigus 96 Tests/kit
E11P0692 Bovine paraneoplastic pemphigus 96 Tests/kit
E13P0692 Anserine paraneoplastic pemphigus 96 Tests/kit
E02P0692 Rat anti-paraneoplastic pemphigus 96 Tests/kit
E08P0692 Canine paraneoplastic pemphigus 96 Tests/kit
E04P0692 Rabbit paraneoplastic pemphigus 96 Tests/kit
E03P0692 Mouse paraneoplastic pemphigus 96 Tests/kit
E12411521 Rat Paraneoplastic pemphigus(PNP) ELISA Kit 1
E07P0692 Porcine paraneoplastic pemphigus 96 Tests/kit
EIAAB12771 ELAVL3,ELAV-like protein 3,Homo sapiens,Hu-antigen C,HuC,HUC,Human,Paraneoplastic cerebellar degeneration-associated antigen,Paraneoplastic limbic encephalitis antigen 21,PLE21
E03P0692 Mouse anti-paraneoplastic pemphigus 96 Tests/kit
E04P0692 Rabbit anti-paraneoplastic pemphigus 96 Tests/kit
E0560Hu Human Paraneoplastic pemphigus,PNP ELISA Kit 48T
E07P0692 Porcine anti-paraneoplastic pemphigus 96 Tests/kit
E0560Hu Human Paraneoplastic pemphigus,PNP ELISA Kit 96T
E01P0692 Human Anti-paraneoplastic pemphigus 96 Tests/kit
CSB-E09086h Human Paraneoplastic pemphigus,PNP ELISA Kit 96tests
201-12-0561 Human Paraneoplastic pemphigus,PNP ELISA Kit 48T
E12531417 Mouse Paraneoplastic pemphigus(PNP) ELISA Kit 1


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur