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

Dystrophin

 DMD_HUMAN               Reviewed;        3685 AA.
P11532; E9PDN1; Q02295; Q14169; Q14170; Q5JYU0; Q6NSJ9; Q7KZ48;
Q8N754; Q9UCW3; Q9UCW4;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
30-NOV-2010, sequence version 3.
25-OCT-2017, entry version 221.
RecName: Full=Dystrophin;
Name=DMD;
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 4), AND VARIANTS GLY-882; LEU-1469
AND GLN-2366.
TISSUE=Muscle;
PubMed=3282674; DOI=10.1016/0092-8674(88)90383-2;
Koenig M., Monaco A.P., Kunkel L.M.;
"The complete sequence of dystrophin predicts a rod-shaped
cytoskeletal protein.";
Cell 53:219-228(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), AND VARIANTS PRO-133; ILE-623;
GLY-784; GLY-882; PHE-1197; ASN-1377; HIS-1745 AND SER-1844.
PubMed=2668885; DOI=10.1093/nar/17.13.5391;
Rosenthal A., Speer A., Billowitz H., Cross G.S., Forrest S.N.,
Davies K.E.;
"Two human cDNA molecules coding for the Duchenne muscular dystrophy
(DMD) locus are highly homologous.";
Nucleic Acids Res. 17:5391-5391(1989).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), AND TISSUE SPECIFICITY.
TISSUE=Brain;
PubMed=1319059; DOI=10.1073/pnas.89.12.5346;
Lederfein D., Levy Z., Augier N., Mornet D., Morris G., Fuchs O.,
Yaffe D., Nudel U.;
"A 71-kilodalton protein is a major product of the Duchenne muscular
dystrophy gene in brain and other nonmuscle tissues.";
Proc. Natl. Acad. Sci. U.S.A. 89:5346-5350(1992).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ARG-2937.
PubMed=15772651; DOI=10.1038/nature03440;
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 6 AND 8).
TISSUE=Brain, Placenta, and Testis;
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).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-1411 (ISOFORMS 1 AND 2).
TISSUE=Retina;
White R.A.;
Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-497 (ISOFORM 4).
PubMed=3607877; DOI=10.1016/0092-8674(87)90504-6;
Koenig M., Hoffman E.P., Bertelson C.J., Monaco A.P., Feener C.,
Kunkel L.M.;
"Complete cloning of the Duchenne muscular dystrophy (DMD) cDNA and
preliminary genomic organization of the DMD gene in normal and
affected individuals.";
Cell 50:509-517(1987).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-32 (ISOFORM 3), AND ALTERNATIVE
SPLICING.
TISSUE=Brain;
PubMed=2648158; DOI=10.1038/338509a0;
Feener C.A., Koenig M., Kunkel L.M.;
"Alternative splicing of human dystrophin mRNA generates isoforms at
the carboxy terminus.";
Nature 338:509-511(1989).
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 404-1137 (ISOFORMS 3/4/5), AND VARIANT
GLY-882.
PubMed=3428261;
Cross G.S., Speer A., Rosenthal A., Forrest S.M., Smith T.J.,
Edwards Y., Flint T., Hill D., Davies K.E.;
"Deletions of fetal and adult muscle cDNA in Duchenne and Becker
muscular dystrophy patients.";
EMBO J. 6:3277-3283(1987).
[11]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 665-722; 2098-2204 AND 2305-2366.
PubMed=3205741; DOI=10.1093/nar/16.23.11141;
Chamberlain J.S., Gibbs R.A., Ranier J.A., Nguyen P.N., Caskey C.T.;
"Deletion screening of the Duchenne muscular dystrophy locus via
multiplex DNA amplification.";
Nucleic Acids Res. 16:11141-11156(1988).
[12]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2147-2204.
PubMed=2569720; DOI=10.1093/nar/17.14.5611;
Blonden L.A.J., den Dunnen J.T., van Paassen H.M.B., Wapenaar M.C.,
Grootscholten P.M., Ginjaar H.B., Bakker E., Pearson P.L.,
van Ommen G.J.B.;
"High resolution deletion breakpoint mapping in the DMD gene by whole
cosmid hybridization.";
Nucleic Acids Res. 17:5611-5621(1989).
[13]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2305-2364.
Huth A., Will K., Speer A., Bauer D.;
"Differences in introns flanking exon 48 of the DMD/BMD gene.";
Submitted (MAR-1991) to the EMBL/GenBank/DDBJ databases.
[14]
NUCLEOTIDE SEQUENCE [MRNA] OF 3670-3685 (ISOFORMS 1/2/3/4 AND 5), AND
TISSUE SPECIFICITY.
TISSUE=Amnion;
PubMed=8541829; DOI=10.1093/hmg/4.9.1475;
Austin R.C., Howard P.L., D'Souza V.N., Klamut H.J., Ray P.N.;
"Cloning and characterization of alternatively spliced isoforms of
Dp71.";
Hum. Mol. Genet. 4:1475-1483(1995).
[15]
ANALYSIS OF THE DOMAIN STRUCTURE.
PubMed=2407739;
Koenig M., Kunkel L.M.;
"Detailed analysis of the repeat domain of dystrophin reveals four
potential hinge segments that may confer flexibility.";
J. Biol. Chem. 265:4560-4566(1990).
[16]
INTERACTION WITH DAG1.
PubMed=7592992; DOI=10.1074/jbc.270.45.27305;
Jung D., Yang B., Meyer J., Chamberlain J.S., Campbell K.P.;
"Identification and characterization of the dystrophin anchoring site
on beta-dystroglycan.";
J. Biol. Chem. 270:27305-27310(1995).
[17]
INTERACTION WITH SNTB1.
PubMed=7844150; DOI=10.1083/jcb.128.3.363;
Ahn A.H., Kunkel L.M.;
"Syntrophin binds to an alternatively spliced exon of dystrophin.";
J. Cell Biol. 128:363-371(1995).
[18]
INTERACTION WITH SNTA1 AND SNTB2.
PubMed=8576247; DOI=10.1074/jbc.271.5.2724;
Ahn A.H., Feener C.A., Gussoni E., Yoshida M., Ozawa E., Kunkel L.M.;
"The three human syntrophin genes are expressed in diverse tissues,
have distinct chromosomal locations, and each bind to dystrophin and
its relatives.";
J. Biol. Chem. 271:2724-2730(1996).
[19]
ALTERNATIVE SPLICING (ISOFORMS 5 AND 9), AND DEVELOPMENTAL STAGE.
TISSUE=Telencephalon;
PubMed=9370062; DOI=10.1016/S0165-3806(97)00122-3;
Ceccarini M., Rizzo G., Rosa G., Chelucci C., Macioce P.,
Petrucci T.C.;
"A splice variant of Dp71 lacking the syntrophin binding site is
expressed in early stages of human neural development.";
Brain Res. Dev. Brain Res. 103:77-82(1997).
[20]
INTERACTION WITH SNTG1 AND SNTG2.
PubMed=10747910; DOI=10.1074/jbc.M000439200;
Piluso G., Mirabella M., Ricci E., Belsito A., Abbondanza C.,
Servidei S., Puca A.A., Tonali P., Puca G.A., Nigro V.;
"Gamma1- and gamma2-syntrophins, two novel dystrophin-binding proteins
localized in neuronal cells.";
J. Biol. Chem. 275:15851-15860(2000).
[21]
ALTERNATIVE SPLICING (ISOFORMS 9 AND 10).
TISSUE=Brain;
PubMed=10734266; DOI=10.1016/S0960-8966(99)00105-4;
Austin R.C., Morris G.E., Howard P.L., Klamut H.J., Ray P.N.;
"Expression and synthesis of alternatively spliced variants of Dp71 in
adult human brain.";
Neuromuscul. Disord. 10:187-193(2000).
[22]
INTERACTION WITH DAG1.
PubMed=11495720; DOI=10.1016/S0898-6568(01)00188-7;
Ilsley J.L., Sudol M., Winder S.J.;
"The interaction of dystrophin with beta-dystroglycan is regulated by
tyrosine phosphorylation.";
Cell. Signal. 13:625-632(2001).
[23]
INTERACTION WITH KRT19, AND TISSUE SPECIFICITY.
PubMed=16000376; DOI=10.1091/mbc.E05-02-0112;
Stone M.R., O'Neill A., Catino D., Bloch R.J.;
"Specific interaction of the actin-binding domain of dystrophin with
intermediate filaments containing keratin 19.";
Mol. Biol. Cell 16:4280-4293(2005).
[24]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[25]
FUNCTION IN THE DYSTROPHIN-ASSOCIATED GLYCOPROTEIN COMPLEX.
PubMed=16710609; DOI=10.1007/s00018-005-5461-0;
Haenggi T., Fritschy J.M.;
"Role of dystrophin and utrophin for assembly and function of the
dystrophin glycoprotein complex in non-muscle tissue.";
Cell. Mol. Life Sci. 63:1614-1631(2006).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3483; SER-3613;
SER-3617; SER-3623 AND SER-3666, PHOSPHORYLATION [LARGE SCALE
ANALYSIS] AT THR-340; SER-344 AND SER-348 (ISOFORMS 5 AND 8), 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).
[27]
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).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3612; SER-3613 AND
SER-3623, 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).
[29]
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).
[30]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3612; SER-3623 AND
SER-3624, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
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).
[31]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3490; SER-3500;
SER-3623; SER-3624 AND SER-3666, PHOSPHORYLATION [LARGE SCALE
ANALYSIS] AT THR-616 (ISOFORM 5), PHOSPHORYLATION [LARGE SCALE
ANALYSIS] AT THR-629 (ISOFORM 6), PHOSPHORYLATION [LARGE SCALE
ANALYSIS] AT THR-519 (ISOFORM 9), 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).
[32]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 3046-3306 IN COMPLEX WITH
DAG1, AND INTERACTION WITH DAG1.
PubMed=10932245; DOI=10.1038/77923;
Huang X., Poy F., Zhang R., Joachimiak A., Sudol M., Eck M.J.;
"Structure of a WW domain containing fragment of dystrophin in complex
with beta-dystroglycan.";
Nat. Struct. Biol. 7:634-638(2000).
[33]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-246.
PubMed=10801490; DOI=10.1016/S0969-2126(00)00132-5;
Norwood F.L.M., Sutherland-Smith A.J., Keep N.H., Kendrick-Jones J.;
"The structure of the N-terminal actin-binding domain of human
dystrophin and how mutations in this domain may cause Duchenne or
Becker muscular dystrophy.";
Structure 8:481-491(2000).
[34]
REVIEW ON DMD VARIANTS.
PubMed=7951253; DOI=10.1002/humu.1380040102;
Roberts R.G., Gardner R.J., Bobrow M.;
"Searching for the 1 in 2,400,000: a review of dystrophin gene point
mutations.";
Hum. Mutat. 4:1-11(1994).
[35]
REVIEW ON VARIANTS.
PubMed=8045556; DOI=10.1007/BF00202854;
Rininsland F., Reiss J.;
"Microlesions and polymorphisms in the Duchenne/Becker muscular
dystrophy gene.";
Hum. Genet. 94:111-116(1994).
[36]
VARIANT DMD ARG-54.
PubMed=8401582; DOI=10.1038/ng0893-357;
Prior T.W., Papp A.C., Snyder P.J., Burghes A.H.M., Bartolo C.,
Sedra M.S., Western L.M., Mendell J.R.;
"A missense mutation in the dystrophin gene in a Duchenne muscular
dystrophy patient.";
Nat. Genet. 4:357-360(1993).
[37]
VARIANT DMD GLY-645.
PubMed=7981690; DOI=10.1093/hmg/3.7.1173;
Prior T.W., Bartolo C., Papp A.C., Snyder P.J., Sedra M.S.,
Burghes A.H., Mendell J.R.;
"Identification of a missense mutation, single base deletion and a
polymorphism in the dystrophin exon 16.";
Hum. Mol. Genet. 3:1173-1174(1994).
[38]
VARIANTS HIS-365; TRP-2191 AND ARG-2937.
PubMed=7849724; DOI=10.1093/hmg/3.10.1907;
Nigro V., Nigro G., Esposito M.G., Comi L.I., Molinari A.M.,
Puca G.A., Politano L.;
"Novel small mutations along the DMD/BMD gene associated with
different phenotypes.";
Hum. Mol. Genet. 3:1907-1908(1994).
[39]
VARIANT DMD TYR-3340.
PubMed=8817332; DOI=10.1093/hmg/5.7.973;
Lenk U., Oexle K., Voit T., Ancker U., Hellner K.A., Speer A.,
Hubner C.;
"A cysteine 3340 substitution in the dystroglycan-binding domain of
dystrophin associated with Duchenne muscular dystrophy, mental
retardation and absence of the ERG b-wave.";
Hum. Mol. Genet. 5:973-975(1996).
[40]
VARIANT CMD3B ALA-279.
PubMed=9170407; DOI=10.1161/01.CIR.95.10.2434;
Ortiz-Lopez R., Li H., Su J., Goytia V., Towbin J.A.;
"Evidence for a dystrophin missense mutation as a cause of X-linked
dilated cardiomyopathy.";
Circulation 95:2434-2440(1997).
[41]
VARIANT DMD HIS-3335.
PubMed=9851445; DOI=10.1002/ana.410440619;
Goldberg L.R., Hausmanowa-Petrusewicz I., Fidzianska A., Duggan D.J.,
Steinberg L.S., Hoffman E.P.;
"A dystrophin missense mutation showing persistence of dystrophin and
dystrophin-associated proteins yet a severe phenotype.";
Ann. Neurol. 44:971-976(1998).
[42]
VARIANT BMD PRO-171.
PubMed=10573008; DOI=10.1038/sj.ejhg.5200370;
Eraslan S., Kayserili H., Apak M.Y., Kirdar B.;
"Identification of point mutations in Turkish DMD/BMD families using
multiplex-single stranded conformation analysis (SSCA).";
Eur. J. Hum. Genet. 7:765-770(1999).
[43]
VARIANT CMD3B LYS-1672.
PubMed=12354438; DOI=10.1016/S0735-1097(02)02126-5;
Feng J., Yan J.Y., Buzin C.H., Sommer S.S., Towbin J.A.;
"Comprehensive mutation scanning of the dystrophin gene in patients
with nonsyndromic X-linked dilated cardiomyopathy.";
J. Am. Coll. Cardiol. 40:1120-1124(2002).
[44]
VARIANTS CMD3B ASN-18 AND LEU-3228, AND VARIANTS TRP-2155; THR-2299;
GLN-2366; VAL-2910; ASP-2912 AND ARG-2937.
PubMed=12359139; DOI=10.1016/S1096-7192(02)00153-1;
Feng J., Yan J., Buzin C.H., Towbin J.A., Sommer S.S.;
"Mutations in the dystrophin gene are associated with sporadic dilated
cardiomyopathy.";
Mol. Genet. Metab. 77:119-126(2002).
[45]
VARIANT DMD PHE-3313, AND VARIANT VAL-165.
PubMed=12632325; DOI=10.1086/374176;
Flanigan K.M., von Niederhausern A., Dunn D.M., Alder J.,
Mendell J.R., Weiss R.B.;
"Rapid direct sequence analysis of the dystrophin gene.";
Am. J. Hum. Genet. 72:931-939(2003).
[46]
VARIANTS [LARGE SCALE ANALYSIS] PHE-334; GLN-1219; HIS-1470 AND
VAL-2164.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
[47]
VARIANT ARG-118.
PubMed=21396098; DOI=10.1186/1471-2350-12-37;
Magri F., Del Bo R., D'Angelo M.G., Govoni A., Ghezzi S.,
Gandossini S., Sciacco M., Ciscato P., Bordoni A., Tedeschi S.,
Fortunato F., Lucchini V., Cereda M., Corti S., Moggio M.,
Bresolin N., Comi G.P.;
"Clinical and molecular characterization of a cohort of patients with
novel nucleotide alterations of the Dystrophin gene detected by direct
sequencing.";
BMC Med. Genet. 12:37-37(2011).
[48]
CHARACTERIZATION OF VARIANTS DMD PHE-3313; HIS-3335 AND TYR-3340.
PubMed=24302611; DOI=10.1002/humu.22479;
Vulin A., Wein N., Strandjord D.M., Johnson E.K., Findlay A.R.,
Maiti B., Howard M.T., Kaminoh Y.J., Taylor L.E., Simmons T.R.,
Ray W.C., Montanaro F., Ervasti J.M., Flanigan K.M.;
"The ZZ domain of dystrophin in DMD: making sense of missense
mutations.";
Hum. Mutat. 35:257-264(2014).
[49]
CHARACTERIZATION OF VARIANT CMD3B ASN-18.
PubMed=25340340; DOI=10.1371/journal.pone.0110439;
Singh S.M., Bandi S., Shah D.D., Armstrong G., Mallela K.M.;
"Missense mutation Lys18Asn in dystrophin that triggers X-linked
dilated cardiomyopathy decreases protein stability, increases protein
unfolding, and perturbs protein structure, but does not affect protein
function.";
PLoS ONE 9:E110439-E110439(2014).
-!- FUNCTION: Anchors the extracellular matrix to the cytoskeleton via
F-actin. Ligand for dystroglycan. Component of the dystrophin-
associated glycoprotein complex which accumulates at the
neuromuscular junction (NMJ) and at a variety of synapses in the
peripheral and central nervous systems and has a structural
function in stabilizing the sarcolemma. Also implicated in
signaling events and synaptic transmission.
{ECO:0000250|UniProtKB:P11531, ECO:0000269|PubMed:16710609}.
-!- SUBUNIT: Interacts with SYNM (By similarity). Interacts with the
syntrophins SNTA1, SNTB1, SNTB2, SNTG1 and SNTG2 (PubMed:7844150,
PubMed:8576247). Interacts with KRT19 (PubMed:16000376). Component
of the dystrophin-associated glycoprotein complex which is
composed of three subcomplexes: a cytoplasmic complex comprised of
DMD (or UTRN), DTNA and a number of syntrophins, such as SNTB1,
SNTB2, SNTG1 and SNTG2, the transmembrane dystroglycan complex,
and the sarcoglycan-sarcospan complex. Interacts with DAG1
(betaDAG1) with DMD; the interaction is inhibited by
phosphorylation on the PPXY motif of DAG1 (PubMed:7592992,
PubMed:11495720, PubMed:10932245). Interacts with CMYA5 (By
similarity). Directly interacts with ANK2 and ANK3; these
interactions do not interfere with betaDAG1-binding and are
necessary for proper localization in muscle cells (By similarity).
Identified in a dystroglycan complex that contains at least PRX,
DRP2, UTRN, DMD and DAG1 (By similarity).
{ECO:0000250|UniProtKB:P11531, ECO:0000269|PubMed:10932245,
ECO:0000269|PubMed:11495720, ECO:0000269|PubMed:16000376,
ECO:0000269|PubMed:7592992, ECO:0000269|PubMed:7844150,
ECO:0000269|PubMed:8576247}.
-!- INTERACTION:
Q01484:ANK2; NbExp=2; IntAct=EBI-1018651, EBI-941975;
Q3T1J5:Ank3 (xeno); NbExp=2; IntAct=EBI-1018651, EBI-2133962;
Q9UBT7:CTNNAL1; NbExp=3; IntAct=EBI-295827, EBI-514206;
O60941:DTNB; NbExp=3; IntAct=EBI-295827, EBI-740402;
Q96CS2:HAUS1; NbExp=3; IntAct=EBI-295827, EBI-2514791;
P41235-3:HNF4A; NbExp=3; IntAct=EBI-295827, EBI-12690684;
P08727:KRT19; NbExp=2; IntAct=EBI-295827, EBI-742756;
Q13884:SNTB1; NbExp=3; IntAct=EBI-295827, EBI-295843;
-!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma
{ECO:0000250|UniProtKB:P11531}; Peripheral membrane protein
{ECO:0000250|UniProtKB:P11531}; Cytoplasmic side
{ECO:0000250|UniProtKB:P11531}. Cytoplasm, cytoskeleton
{ECO:0000250|UniProtKB:P11531}. Cell junction, synapse,
postsynaptic cell membrane {ECO:0000250|UniProtKB:P11531}. Note=In
muscle cells, sarcolemma localization requires the presence of
ANK2, while localization to costameres requires the presence of
ANK3. Localizes to neuromuscular junctions (NMJs). In adult
muscle, NMJ localization depends upon ANK2 presence, but not in
newborn animals. {ECO:0000250|UniProtKB:P11531}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=10;
Comment=Additional isoforms seem to exist.;
Name=4; Synonyms=Dystrophin-4;
IsoId=P11532-1; Sequence=Displayed;
Name=1; Synonyms=Dystrophin-1;
IsoId=P11532-2; Sequence=VSP_006806, VSP_006807;
Name=2; Synonyms=Dystrophin-2;
IsoId=P11532-3; Sequence=VSP_006808, VSP_006807;
Name=3; Synonyms=Dystrophin-3;
IsoId=P11532-4; Sequence=VSP_006809;
Name=5; Synonyms=Dp71ab;
IsoId=P11532-5; Sequence=VSP_017490, VSP_017491, VSP_017492,
VSP_017493;
Note=Contains a phosphothreonine at position 340. Contains a
phosphoserine at position 348. Contains a phosphoserine at
position 344. Contains a phosphothreonine at position 616.
{ECO:0000244|PubMed:18669648, ECO:0000244|PubMed:24275569};
Name=6; Synonyms=Dp71b;
IsoId=P11532-6; Sequence=VSP_017490, VSP_017491, VSP_017493;
Note=No experimental confirmation available. Contains a
phosphothreonine at position 629. {ECO:0000244|PubMed:24275569};
Name=7; Synonyms=Dp71;
IsoId=P11532-7; Sequence=VSP_017490, VSP_017491;
Name=8; Synonyms=Dp71a;
IsoId=P11532-8; Sequence=VSP_017490, VSP_017491, VSP_017492;
Note=No experimental confirmation available. Contains a
phosphothreonine at position 340. Contains a phosphoserine at
position 348. Contains a phosphoserine at position 344.
{ECO:0000244|PubMed:18669648};
Name=9; Synonyms=Dp60, Dp71delta110;
IsoId=P11532-9; Sequence=VSP_017490, VSP_017491, VSP_046319,
VSP_017493;
Note=Contains a phosphothreonine at position 519.
{ECO:0000244|PubMed:24275569};
Name=10; Synonyms=Dp71c;
IsoId=P11532-10; Sequence=VSP_017490, VSP_017491, VSP_046319;
-!- TISSUE SPECIFICITY: Expressed in muscle fibers accumulating in the
costameres of myoplasm at the sarcolemma. Expressed in brain,
muscle, kidney, lung and testis. Isoform 5 is expressed in heart,
brain, liver, testis and hepatoma cells. Most tissues contain
transcripts of multiple isoforms, however only isoform 5 is
detected in heart and liver. {ECO:0000269|PubMed:1319059,
ECO:0000269|PubMed:16000376, ECO:0000269|PubMed:8541829}.
-!- DEVELOPMENTAL STAGE: Isoform 5 is expressed in embryonic neural
tissue from the sixth week of development. Isoform 9 is detected
in all embryonic tissues examined. {ECO:0000269|PubMed:9370062}.
-!- DISEASE: Duchenne muscular dystrophy (DMD) [MIM:310200]: Most
common form of muscular dystrophy; a sex-linked recessive
disorder. It typically presents in boys aged 3 to 7 year as
proximal muscle weakness causing waddling gait, toe-walking,
lordosis, frequent falls, and difficulty in standing up and
climbing up stairs. The pelvic girdle is affected first, then the
shoulder girdle. Progression is steady and most patients are
confined to a wheelchair by age of 10 or 12. Flexion contractures
and scoliosis ultimately occur. About 50% of patients have a lower
IQ than their genetic expectations would suggest. There is no
treatment. {ECO:0000269|PubMed:12632325,
ECO:0000269|PubMed:24302611, ECO:0000269|PubMed:7981690,
ECO:0000269|PubMed:8401582, ECO:0000269|PubMed:8817332,
ECO:0000269|PubMed:9851445}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Becker muscular dystrophy (BMD) [MIM:300376]: A
neuromuscular disorder characterized by dystrophin deficiency. It
appears between the age of 5 and 15 years with a proximal motor
deficiency of variable progression. Heart involvement can be the
initial sign. Becker muscular dystrophy has a more benign course
than Duchenne muscular dystrophy. {ECO:0000269|PubMed:10573008}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Cardiomyopathy, dilated, X-linked 3B (CMD3B)
[MIM:302045]: A disorder characterized by ventricular dilation and
impaired systolic function, resulting in congestive heart failure
and arrhythmia. Patients are at risk of premature death.
{ECO:0000269|PubMed:12354438, ECO:0000269|PubMed:12359139,
ECO:0000269|PubMed:25340340, ECO:0000269|PubMed:9170407}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- MISCELLANEOUS: The DMD gene is the largest known gene in humans.
It is 2.4 million base-pairs in size, comprises 79 exons and takes
over 16 hours to be transcribed and cotranscriptionally spliced.
-!- WEB RESOURCE: Name=DMD; Note=Dystrophin Mutation Database;
URL="http://www.dmd.nl/database.html";
-!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and
polymorphism database;
URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=DMD";
-!- WEB RESOURCE: Name=Wikipedia; Note=Dystrophin entry;
URL="https://en.wikipedia.org/wiki/Dystrophin";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M18533; AAA53189.1; -; mRNA.
EMBL; X14298; CAA32479.1; -; mRNA.
EMBL; M92650; AAA52316.1; -; mRNA.
EMBL; AL031542; CAI42229.1; -; Genomic_DNA.
EMBL; AC004468; CAI42229.1; JOINED; Genomic_DNA.
EMBL; AC006061; CAI42229.1; JOINED; Genomic_DNA.
EMBL; AC078958; CAI42229.1; JOINED; Genomic_DNA.
EMBL; AC079143; CAI42229.1; JOINED; Genomic_DNA.
EMBL; AC079175; CAI42229.1; JOINED; Genomic_DNA.
EMBL; AC079177; CAI42229.1; JOINED; Genomic_DNA.
EMBL; AC079864; CAI42229.1; JOINED; Genomic_DNA.
EMBL; AC090632; CAI42229.1; JOINED; Genomic_DNA.
EMBL; AC093167; CAI42229.1; JOINED; Genomic_DNA.
EMBL; AC093193; CAI42229.1; JOINED; Genomic_DNA.
EMBL; AC096506; CAI42229.1; JOINED; Genomic_DNA.
EMBL; AL031643; CAI42229.1; JOINED; Genomic_DNA.
EMBL; AL096699; CAI42229.1; JOINED; Genomic_DNA.
EMBL; AL109609; CAI42229.1; JOINED; Genomic_DNA.
EMBL; AL139278; CAI42229.1; JOINED; Genomic_DNA.
EMBL; AL451144; CAI42229.1; JOINED; Genomic_DNA.
EMBL; AL031643; CAI43058.1; -; Genomic_DNA.
EMBL; AC004468; CAI43058.1; JOINED; Genomic_DNA.
EMBL; AC006061; CAI43058.1; JOINED; Genomic_DNA.
EMBL; AC078958; CAI43058.1; JOINED; Genomic_DNA.
EMBL; AC079143; CAI43058.1; JOINED; Genomic_DNA.
EMBL; AC079175; CAI43058.1; JOINED; Genomic_DNA.
EMBL; AC079177; CAI43058.1; JOINED; Genomic_DNA.
EMBL; AC079864; CAI43058.1; JOINED; Genomic_DNA.
EMBL; AC090632; CAI43058.1; JOINED; Genomic_DNA.
EMBL; AC093167; CAI43058.1; JOINED; Genomic_DNA.
EMBL; AC093193; CAI43058.1; JOINED; Genomic_DNA.
EMBL; AC096506; CAI43058.1; JOINED; Genomic_DNA.
EMBL; AL031542; CAI43058.1; JOINED; Genomic_DNA.
EMBL; AL096699; CAI43058.1; JOINED; Genomic_DNA.
EMBL; AL109609; CAI43058.1; JOINED; Genomic_DNA.
EMBL; AL139278; CAI43058.1; JOINED; Genomic_DNA.
EMBL; AL451144; CAI43058.1; JOINED; Genomic_DNA.
EMBL; AL049643; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL050305; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL096699; CAI42225.1; -; Genomic_DNA.
EMBL; AC004468; CAI42225.1; JOINED; Genomic_DNA.
EMBL; AC006061; CAI42225.1; JOINED; Genomic_DNA.
EMBL; AC078958; CAI42225.1; JOINED; Genomic_DNA.
EMBL; AC079143; CAI42225.1; JOINED; Genomic_DNA.
EMBL; AC079175; CAI42225.1; JOINED; Genomic_DNA.
EMBL; AC079177; CAI42225.1; JOINED; Genomic_DNA.
EMBL; AC079864; CAI42225.1; JOINED; Genomic_DNA.
EMBL; AC090632; CAI42225.1; JOINED; Genomic_DNA.
EMBL; AC093167; CAI42225.1; JOINED; Genomic_DNA.
EMBL; AC093193; CAI42225.1; JOINED; Genomic_DNA.
EMBL; AC096506; CAI42225.1; JOINED; Genomic_DNA.
EMBL; AL031542; CAI42225.1; JOINED; Genomic_DNA.
EMBL; AL031643; CAI42225.1; JOINED; Genomic_DNA.
EMBL; AL109609; CAI42225.1; JOINED; Genomic_DNA.
EMBL; AL139278; CAI42225.1; JOINED; Genomic_DNA.
EMBL; AL451144; CAI42225.1; JOINED; Genomic_DNA.
EMBL; AL109609; CAI42950.1; -; Genomic_DNA.
EMBL; AC004468; CAI42950.1; JOINED; Genomic_DNA.
EMBL; AC006061; CAI42950.1; JOINED; Genomic_DNA.
EMBL; AC078958; CAI42950.1; JOINED; Genomic_DNA.
EMBL; AC079143; CAI42950.1; JOINED; Genomic_DNA.
EMBL; AC079175; CAI42950.1; JOINED; Genomic_DNA.
EMBL; AC079177; CAI42950.1; JOINED; Genomic_DNA.
EMBL; AC079864; CAI42950.1; JOINED; Genomic_DNA.
EMBL; AC090632; CAI42950.1; JOINED; Genomic_DNA.
EMBL; AC093167; CAI42950.1; JOINED; Genomic_DNA.
EMBL; AC093193; CAI42950.1; JOINED; Genomic_DNA.
EMBL; AC096506; CAI42950.1; JOINED; Genomic_DNA.
EMBL; AL031542; CAI42950.1; JOINED; Genomic_DNA.
EMBL; AL031643; CAI42950.1; JOINED; Genomic_DNA.
EMBL; AL096699; CAI42950.1; JOINED; Genomic_DNA.
EMBL; AL139278; CAI42950.1; JOINED; Genomic_DNA.
EMBL; AL451144; CAI42950.1; JOINED; Genomic_DNA.
EMBL; AL121880; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL139278; CAI42991.1; -; Genomic_DNA.
EMBL; AC004468; CAI42991.1; JOINED; Genomic_DNA.
EMBL; AC006061; CAI42991.1; JOINED; Genomic_DNA.
EMBL; AC078958; CAI42991.1; JOINED; Genomic_DNA.
EMBL; AC079143; CAI42991.1; JOINED; Genomic_DNA.
EMBL; AC079175; CAI42991.1; JOINED; Genomic_DNA.
EMBL; AC079177; CAI42991.1; JOINED; Genomic_DNA.
EMBL; AC079864; CAI42991.1; JOINED; Genomic_DNA.
EMBL; AC090632; CAI42991.1; JOINED; Genomic_DNA.
EMBL; AC093167; CAI42991.1; JOINED; Genomic_DNA.
EMBL; AC093193; CAI42991.1; JOINED; Genomic_DNA.
EMBL; AC096506; CAI42991.1; JOINED; Genomic_DNA.
EMBL; AL031542; CAI42991.1; JOINED; Genomic_DNA.
EMBL; AL031643; CAI42991.1; JOINED; Genomic_DNA.
EMBL; AL096699; CAI42991.1; JOINED; Genomic_DNA.
EMBL; AL109609; CAI42991.1; JOINED; Genomic_DNA.
EMBL; AL451144; CAI42991.1; JOINED; Genomic_DNA.
EMBL; AL139401; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL451144; CAI39566.1; -; Genomic_DNA.
EMBL; AC004468; CAI39566.1; JOINED; Genomic_DNA.
EMBL; AC006061; CAI39566.1; JOINED; Genomic_DNA.
EMBL; AC078958; CAI39566.1; JOINED; Genomic_DNA.
EMBL; AC079143; CAI39566.1; JOINED; Genomic_DNA.
EMBL; AC079175; CAI39566.1; JOINED; Genomic_DNA.
EMBL; AC079177; CAI39566.1; JOINED; Genomic_DNA.
EMBL; AC079864; CAI39566.1; JOINED; Genomic_DNA.
EMBL; AC090632; CAI39566.1; JOINED; Genomic_DNA.
EMBL; AC093167; CAI39566.1; JOINED; Genomic_DNA.
EMBL; AC093193; CAI39566.1; JOINED; Genomic_DNA.
EMBL; AC096506; CAI39566.1; JOINED; Genomic_DNA.
EMBL; AL031542; CAI39566.1; JOINED; Genomic_DNA.
EMBL; AL031643; CAI39566.1; JOINED; Genomic_DNA.
EMBL; AL096699; CAI39566.1; JOINED; Genomic_DNA.
EMBL; AL109609; CAI39566.1; JOINED; Genomic_DNA.
EMBL; AL139278; CAI39566.1; JOINED; Genomic_DNA.
EMBL; AL596023; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471074; EAW99065.1; -; Genomic_DNA.
EMBL; BC028720; AAH28720.1; -; mRNA.
EMBL; BC070078; AAH70078.1; -; mRNA.
EMBL; BC094758; AAH94758.1; -; mRNA.
EMBL; U27203; AAA86115.1; -; Genomic_DNA.
EMBL; U27203; AAA86116.1; -; Genomic_DNA.
EMBL; X15148; CAA33245.1; -; mRNA.
EMBL; X06178; CAA29544.1; -; mRNA.
EMBL; X06179; CAA29545.1; -; mRNA.
EMBL; X13045; CAA31451.1; -; Genomic_DNA.
EMBL; X13046; CAA31452.1; -; Genomic_DNA.
EMBL; X13047; CAA31453.1; -; Genomic_DNA.
EMBL; X13048; CAA31454.1; -; Genomic_DNA.
EMBL; X15495; CAA33518.1; -; Genomic_DNA.
EMBL; X54820; CAA38589.1; -; Genomic_DNA.
CCDS; CCDS14231.1; -. [P11532-6]
CCDS; CCDS14232.1; -. [P11532-5]
CCDS; CCDS14233.1; -. [P11532-1]
CCDS; CCDS14234.1; -. [P11532-7]
PIR; A45255; A45255.
RefSeq; NP_000100.2; NM_000109.3.
RefSeq; NP_003997.1; NM_004006.2.
RefSeq; NP_004000.1; NM_004009.3.
RefSeq; NP_004001.1; NM_004010.3.
RefSeq; NP_004002.2; NM_004011.3.
RefSeq; NP_004003.1; NM_004012.3.
RefSeq; NP_004004.1; NM_004013.2.
RefSeq; NP_004005.1; NM_004014.2.
RefSeq; NP_004006.1; NM_004015.2. [P11532-7]
RefSeq; NP_004007.1; NM_004016.2. [P11532-6]
RefSeq; NP_004008.1; NM_004017.2. [P11532-8]
RefSeq; NP_004009.1; NM_004018.2. [P11532-5]
RefSeq; NP_004010.1; NM_004019.2.
RefSeq; NP_004011.2; NM_004020.3.
RefSeq; NP_004012.1; NM_004021.2.
RefSeq; NP_004013.1; NM_004022.2.
RefSeq; NP_004014.1; NM_004023.2.
UniGene; Hs.495912; -.
PDB; 1DXX; X-ray; 2.60 A; A/B/C/D=1-246.
PDB; 1EG3; X-ray; 2.00 A; A=3046-3306.
PDB; 1EG4; X-ray; 2.00 A; A=3046-3306.
PDB; 3UUN; X-ray; 2.30 A; A/B=338-456.
PDBsum; 1DXX; -.
PDBsum; 1EG3; -.
PDBsum; 1EG4; -.
PDBsum; 3UUN; -.
ProteinModelPortal; P11532; -.
SMR; P11532; -.
BioGrid; 108096; 56.
DIP; DIP-32593N; -.
IntAct; P11532; 21.
MINT; MINT-109755; -.
STRING; 9606.ENSP00000354923; -.
TCDB; 8.A.66.1.2; the dystrophin (dystrophin) family.
iPTMnet; P11532; -.
PhosphoSitePlus; P11532; -.
SwissPalm; P11532; -.
BioMuta; DMD; -.
DMDM; 313104240; -.
EPD; P11532; -.
MaxQB; P11532; -.
PaxDb; P11532; -.
PeptideAtlas; P11532; -.
PRIDE; P11532; -.
DNASU; 1756; -.
Ensembl; ENST00000361471; ENSP00000354464; ENSG00000198947. [P11532-5]
Ensembl; ENST00000378680; ENSP00000367951; ENSG00000198947. [P11532-9]
Ensembl; ENST00000378702; ENSP00000367974; ENSG00000198947. [P11532-7]
Ensembl; ENST00000378723; ENSP00000367997; ENSG00000198947. [P11532-6]
GeneID; 1756; -.
KEGG; hsa:1756; -.
UCSC; uc004dcm.2; human. [P11532-1]
CTD; 1756; -.
DisGeNET; 1756; -.
EuPathDB; HostDB:ENSG00000198947.15; -.
GeneCards; DMD; -.
GeneReviews; DMD; -.
HGNC; HGNC:2928; DMD.
HPA; CAB000119; -.
HPA; HPA002725; -.
HPA; HPA023885; -.
MalaCards; DMD; -.
MIM; 300376; phenotype.
MIM; 300377; gene.
MIM; 302045; phenotype.
MIM; 310200; phenotype.
neXtProt; NX_P11532; -.
OpenTargets; ENSG00000198947; -.
Orphanet; 98895; Becker muscular dystrophy.
Orphanet; 98896; Duchenne muscular dystrophy.
Orphanet; 154; Familial isolated dilated cardiomyopathy.
Orphanet; 206546; Symptomatic form of muscular dystrophy of Duchenne and Becker in female carriers.
Orphanet; 777; X-linked non-syndromic intellectual disability.
PharmGKB; PA27378; -.
eggNOG; KOG4286; Eukaryota.
eggNOG; COG5069; LUCA.
GeneTree; ENSGT00760000119237; -.
HOGENOM; HOG000231175; -.
HOVERGEN; HBG005495; -.
InParanoid; P11532; -.
KO; K10366; -.
PhylomeDB; P11532; -.
TreeFam; TF320178; -.
Reactome; R-HSA-3000171; Non-integrin membrane-ECM interactions.
Reactome; R-HSA-390522; Striated Muscle Contraction.
SignaLink; P11532; -.
ChiTaRS; DMD; human.
EvolutionaryTrace; P11532; -.
GeneWiki; Dystrophin; -.
GenomeRNAi; 1756; -.
PRO; PR:P11532; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000198947; -.
CleanEx; HS_DMD; -.
ExpressionAtlas; P11532; baseline and differential.
Genevisible; P11532; HS.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0030055; C:cell-substrate junction; ISS:BHF-UCL.
GO; GO:0043034; C:costamere; IDA:UniProtKB.
GO; GO:0005856; C:cytoskeleton; TAS:ProtInc.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0016010; C:dystrophin-associated glycoprotein complex; IDA:UniProtKB.
GO; GO:0030175; C:filopodium; IDA:BHF-UCL.
GO; GO:0031527; C:filopodium membrane; IDA:BHF-UCL.
GO; GO:0045121; C:membrane raft; ISS:BHF-UCL.
GO; GO:0044306; C:neuron projection terminus; ISS:BHF-UCL.
GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
GO; GO:0005886; C:plasma membrane; TAS:BHF-UCL.
GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
GO; GO:0043234; C:protein complex; IDA:MGI.
GO; GO:0042383; C:sarcolemma; IDA:BHF-UCL.
GO; GO:0045202; C:synapse; ISS:BHF-UCL.
GO; GO:0016013; C:syntrophin complex; TAS:BHF-UCL.
GO; GO:0030018; C:Z disc; ISS:BHF-UCL.
GO; GO:0003779; F:actin binding; IDA:BHF-UCL.
GO; GO:0002162; F:dystroglycan binding; IPI:UniProtKB.
GO; GO:0017022; F:myosin binding; IDA:BHF-UCL.
GO; GO:0050998; F:nitric-oxide synthase binding; ISS:BHF-UCL.
GO; GO:0005200; F:structural constituent of cytoskeleton; TAS:ProtInc.
GO; GO:0008307; F:structural constituent of muscle; IDA:UniProtKB.
GO; GO:0017166; F:vinculin binding; IPI:BHF-UCL.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0086001; P:cardiac muscle cell action potential; ISS:BHF-UCL.
GO; GO:0060048; P:cardiac muscle contraction; IMP:BHF-UCL.
GO; GO:0043623; P:cellular protein complex assembly; ISS:BHF-UCL.
GO; GO:0034613; P:cellular protein localization; IMP:BHF-UCL.
GO; GO:0044458; P:motile cilium assembly; TAS:BHF-UCL.
GO; GO:0046716; P:muscle cell cellular homeostasis; ISS:BHF-UCL.
GO; GO:0048747; P:muscle fiber development; ISS:BHF-UCL.
GO; GO:0030049; P:muscle filament sliding; TAS:Reactome.
GO; GO:0007517; P:muscle organ development; NAS:ProtInc.
GO; GO:1902083; P:negative regulation of peptidyl-cysteine S-nitrosylation; ISS:BHF-UCL.
GO; GO:0033137; P:negative regulation of peptidyl-serine phosphorylation; ISS:BHF-UCL.
GO; GO:0043043; P:peptide biosynthetic process; IDA:UniProtKB.
GO; GO:0045666; P:positive regulation of neuron differentiation; IMP:BHF-UCL.
GO; GO:0010976; P:positive regulation of neuron projection development; IMP:BHF-UCL.
GO; GO:2000651; P:positive regulation of sodium ion transmembrane transporter activity; ISS:BHF-UCL.
GO; GO:0010881; P:regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion; ISS:BHF-UCL.
GO; GO:0090287; P:regulation of cellular response to growth factor stimulus; IMP:BHF-UCL.
GO; GO:0002027; P:regulation of heart rate; IMP:BHF-UCL.
GO; GO:0010880; P:regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; ISS:BHF-UCL.
GO; GO:0060314; P:regulation of ryanodine-sensitive calcium-release channel activity; ISS:BHF-UCL.
GO; GO:0014819; P:regulation of skeletal muscle contraction; ISS:BHF-UCL.
GO; GO:0014809; P:regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion; ISS:BHF-UCL.
GO; GO:1901385; P:regulation of voltage-gated calcium channel activity; ISS:BHF-UCL.
GO; GO:0035994; P:response to muscle stretch; ISS:BHF-UCL.
CDD; cd00014; CH; 2.
CDD; cd00201; WW; 1.
Gene3D; 1.10.418.10; -; 2.
InterPro; IPR001589; Actinin_actin-bd_CS.
InterPro; IPR036872; Calponin-like_dom_sf.
InterPro; IPR001715; CH-domain.
InterPro; IPR016344; Dystrophin.
InterPro; IPR035436; Dystrophin/utrophin.
InterPro; IPR011992; EF-hand-dom_pair.
InterPro; IPR015153; EF-hand_dom_typ1.
InterPro; IPR015154; EF-hand_dom_typ2.
InterPro; IPR018159; Spectrin/alpha-actinin.
InterPro; IPR002017; Spectrin_repeat.
InterPro; IPR001202; WW_dom.
InterPro; IPR036020; WW_dom_sf.
InterPro; IPR000433; Znf_ZZ.
PANTHER; PTHR44318:SF1; PTHR44318:SF1; 1.
Pfam; PF00307; CH; 2.
Pfam; PF09068; EF-hand_2; 1.
Pfam; PF09069; EF-hand_3; 1.
Pfam; PF00435; Spectrin; 17.
Pfam; PF00397; WW; 1.
Pfam; PF00569; ZZ; 1.
PIRSF; PIRSF002341; Dystrophin/utrophin; 1.
SMART; SM00033; CH; 2.
SMART; SM00150; SPEC; 22.
SMART; SM00456; WW; 1.
SMART; SM00291; ZnF_ZZ; 1.
SUPFAM; SSF47473; SSF47473; 2.
SUPFAM; SSF47576; SSF47576; 1.
SUPFAM; SSF51045; SSF51045; 1.
PROSITE; PS00019; ACTININ_1; 1.
PROSITE; PS00020; ACTININ_2; 1.
PROSITE; PS50021; CH; 2.
PROSITE; PS01159; WW_DOMAIN_1; 1.
PROSITE; PS50020; WW_DOMAIN_2; 1.
PROSITE; PS01357; ZF_ZZ_1; 1.
PROSITE; PS50135; ZF_ZZ_2; 1.
1: Evidence at protein level;
3D-structure; Actin-binding; Alternative splicing; Calcium;
Cardiomyopathy; Cell junction; Cell membrane; Complete proteome;
Cytoplasm; Cytoskeleton; Disease mutation; Membrane; Metal-binding;
Phosphoprotein; Polymorphism; Postsynaptic cell membrane;
Reference proteome; Repeat; Synapse; Zinc; Zinc-finger.
CHAIN 1 3685 Dystrophin.
/FTId=PRO_0000076075.
DOMAIN 15 119 Calponin-homology (CH) 1.
{ECO:0000255|PROSITE-ProRule:PRU00044}.
DOMAIN 134 240 Calponin-homology (CH) 2.
{ECO:0000255|PROSITE-ProRule:PRU00044}.
REPEAT 339 447 Spectrin 1.
REPEAT 448 556 Spectrin 2.
REPEAT 559 667 Spectrin 3.
REPEAT 719 828 Spectrin 4.
REPEAT 830 934 Spectrin 5.
REPEAT 943 1045 Spectrin 6.
REPEAT 1048 1154 Spectrin 7.
REPEAT 1157 1263 Spectrin 8.
REPEAT 1266 1367 Spectrin 9.
REPEAT 1368 1463 Spectrin 10.
REPEAT 1468 1568 Spectrin 11.
REPEAT 1571 1676 Spectrin 12.
REPEAT 1679 1778 Spectrin 13.
REPEAT 1779 1874 Spectrin 14.
REPEAT 1877 1979 Spectrin 15.
REPEAT 1992 2101 Spectrin 16.
REPEAT 2104 2208 Spectrin 17.
REPEAT 2211 2318 Spectrin 18.
REPEAT 2319 2423 Spectrin 19.
REPEAT 2475 2577 Spectrin 20.
REPEAT 2580 2686 Spectrin 21.
REPEAT 2689 2802 Spectrin 22.
REPEAT 2808 2930 Spectrin 23.
REPEAT 2935 3040 Spectrin 24.
DOMAIN 3055 3088 WW. {ECO:0000255|PROSITE-
ProRule:PRU00224}.
ZN_FING 3307 3354 ZZ-type. {ECO:0000255|PROSITE-
ProRule:PRU00228}.
REGION 1 240 Actin-binding.
REGION 63 72 ANK2- and ANK-3 binding. {ECO:0000250}.
REGION 1415 1913 Interaction with SYNM. {ECO:0000250}.
REGION 3058 3408 Interaction with SYNM. {ECO:0000250}.
REGION 3466 3518 Binds to SNTB1.
MOD_RES 3483 3483 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 3490 3490 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 3500 3500 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 3612 3612 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 3613 3613 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 3617 3617 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 3623 3623 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 3624 3624 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 3666 3666 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:24275569}.
VAR_SEQ 1 3068 Missing (in isoform 5, isoform 6, isoform
7, isoform 8, isoform 9 and isoform 10).
{ECO:0000303|PubMed:1319059,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:8541829}.
/FTId=VSP_017490.
VAR_SEQ 1 11 MLWWEEVEDCY -> MED (in isoform 3).
{ECO:0000303|PubMed:2648158}.
/FTId=VSP_006809.
VAR_SEQ 1 1 M -> MTEIILLIFFPAYFLN (in isoform 1).
{ECO:0000305}.
/FTId=VSP_006806.
VAR_SEQ 1 1 M -> MSARKLRNLSYKK (in isoform 2).
{ECO:0000305}.
/FTId=VSP_006808.
VAR_SEQ 2 1357 Missing (in isoform 1 and isoform 2).
{ECO:0000305}.
/FTId=VSP_006807.
VAR_SEQ 3069 3075 KVPYYIN -> MREQLKG (in isoform 5, isoform
6, isoform 7, isoform 8, isoform 9 and
isoform 10). {ECO:0000303|PubMed:1319059,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:8541829}.
/FTId=VSP_017491.
VAR_SEQ 3409 3518 Missing (in isoform 9 and isoform 10).
{ECO:0000305}.
/FTId=VSP_046319.
VAR_SEQ 3409 3421 Missing (in isoform 5 and isoform 8).
{ECO:0000303|PubMed:1319059,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:8541829}.
/FTId=VSP_017492.
VAR_SEQ 3673 3685 RNTPGKPMREDTM -> HNVGSLFHMADDLGRAMESLVSVM
TDEEGAE (in isoform 5, isoform 6 and
isoform 9). {ECO:0000303|PubMed:1319059,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:8541829}.
/FTId=VSP_017493.
VARIANT 18 18 K -> N (in CMD3B; decreased thermodynamic
stability; accelerated unfolding,
perturbed protein structure; no effect on
anchoring function).
{ECO:0000269|PubMed:12359139,
ECO:0000269|PubMed:25340340}.
/FTId=VAR_023537.
VARIANT 32 62 Missing (in BMD).
/FTId=VAR_005146.
VARIANT 54 54 L -> R (in DMD).
{ECO:0000269|PubMed:8401582}.
/FTId=VAR_005147.
VARIANT 118 118 W -> R (in a patient with Becker muscular
dystrophy).
{ECO:0000269|PubMed:21396098}.
/FTId=VAR_065764.
VARIANT 133 133 Q -> P (in dbSNP:rs1800256).
{ECO:0000269|PubMed:2668885}.
/FTId=VAR_005148.
VARIANT 165 165 D -> V (in one patient with Becker
muscular dystrophy).
{ECO:0000269|PubMed:12632325}.
/FTId=VAR_023538.
VARIANT 168 168 A -> D (in BMD).
/FTId=VAR_005149.
VARIANT 171 171 A -> P (in BMD).
{ECO:0000269|PubMed:10573008}.
/FTId=VAR_023539.
VARIANT 231 231 Y -> N (in BMD).
/FTId=VAR_005150.
VARIANT 279 279 T -> A (in CMD3B).
{ECO:0000269|PubMed:9170407}.
/FTId=VAR_023540.
VARIANT 334 334 L -> F (in a colorectal cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036353.
VARIANT 365 365 Q -> H (in dbSNP:rs1800266).
{ECO:0000269|PubMed:7849724}.
/FTId=VAR_005151.
VARIANT 409 409 T -> S (in dbSNP:rs34155804).
/FTId=VAR_057642.
VARIANT 495 534 Missing (in BMD).
/FTId=VAR_005152.
VARIANT 573 573 A -> V (in dbSNP:rs5972599).
/FTId=VAR_057643.
VARIANT 623 623 L -> I (in dbSNP:rs1800259).
{ECO:0000269|PubMed:2668885}.
/FTId=VAR_005153.
VARIANT 645 645 D -> G (in DMD).
{ECO:0000269|PubMed:7981690}.
/FTId=VAR_023541.
VARIANT 666 666 S -> L (in dbSNP:rs34563188).
/FTId=VAR_062110.
VARIANT 715 715 T -> S (in dbSNP:rs16998350).
/FTId=VAR_057644.
VARIANT 773 773 K -> E (in DMD).
/FTId=VAR_005154.
VARIANT 784 784 A -> G (in dbSNP:rs1800260).
{ECO:0000269|PubMed:2668885}.
/FTId=VAR_005155.
VARIANT 882 882 D -> G (in dbSNP:rs228406).
{ECO:0000269|PubMed:2668885,
ECO:0000269|PubMed:3282674,
ECO:0000269|PubMed:3428261}.
/FTId=VAR_005156.
VARIANT 1136 1136 T -> S (in dbSNP:rs3827462).
/FTId=VAR_057645.
VARIANT 1197 1197 V -> F (in dbSNP:rs1800262).
{ECO:0000269|PubMed:2668885}.
/FTId=VAR_005157.
VARIANT 1219 1219 E -> Q (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036354.
VARIANT 1245 1245 T -> I (in dbSNP:rs1800269).
/FTId=VAR_005158.
VARIANT 1278 1278 A -> P (in dbSNP:rs1800270).
/FTId=VAR_005159.
VARIANT 1377 1377 K -> N (in dbSNP:rs1800263).
{ECO:0000269|PubMed:2668885}.
/FTId=VAR_005160.
VARIANT 1388 1388 F -> V (in dbSNP:rs28715870).
/FTId=VAR_057646.
VARIANT 1469 1469 Q -> L (in dbSNP:rs1057872).
{ECO:0000269|PubMed:3282674}.
/FTId=VAR_005161.
VARIANT 1470 1470 R -> H (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036355.
VARIANT 1672 1672 N -> K (in CMD3B; dbSNP:rs16990264).
{ECO:0000269|PubMed:12354438}.
/FTId=VAR_023542.
VARIANT 1745 1745 R -> H (in dbSNP:rs1801187).
{ECO:0000269|PubMed:2668885}.
/FTId=VAR_005162.
VARIANT 1844 1844 R -> S (in dbSNP:rs1801186).
{ECO:0000269|PubMed:2668885}.
/FTId=VAR_005163.
VARIANT 2108 2108 R -> C (in dbSNP:rs16990169).
/FTId=VAR_057647.
VARIANT 2155 2155 R -> W (in dbSNP:rs1800273).
{ECO:0000269|PubMed:12359139}.
/FTId=VAR_005164.
VARIANT 2164 2164 A -> V (in a colorectal cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036356.
VARIANT 2191 2191 R -> W. {ECO:0000269|PubMed:7849724}.
/FTId=VAR_005165.
VARIANT 2299 2299 N -> T. {ECO:0000269|PubMed:12359139}.
/FTId=VAR_023543.
VARIANT 2305 2366 Missing (in DMD).
/FTId=VAR_005166.
VARIANT 2366 2366 K -> Q (in dbSNP:rs1800275).
{ECO:0000269|PubMed:12359139,
ECO:0000269|PubMed:3282674}.
/FTId=VAR_005167.
VARIANT 2910 2910 E -> V (in dbSNP:rs41305353).
{ECO:0000269|PubMed:12359139}.
/FTId=VAR_005168.
VARIANT 2912 2912 N -> D (in dbSNP:rs1800278).
{ECO:0000269|PubMed:12359139}.
/FTId=VAR_005169.
VARIANT 2921 2921 H -> R (in BMD; dbSNP:rs1800279).
/FTId=VAR_005170.
VARIANT 2937 2937 Q -> R (in dbSNP:rs1800280).
{ECO:0000269|PubMed:12359139,
ECO:0000269|PubMed:15772651,
ECO:0000269|PubMed:7849724}.
/FTId=VAR_005171.
VARIANT 3228 3228 F -> L (in CMD3B).
{ECO:0000269|PubMed:12359139}.
/FTId=VAR_023544.
VARIANT 3313 3313 C -> F (in DMD; results in highly reduced
protein levels and expression at the
sarcolemma).
{ECO:0000269|PubMed:12632325,
ECO:0000269|PubMed:24302611}.
/FTId=VAR_023545.
VARIANT 3335 3335 D -> H (in DMD; does not affect protein
stability; does not affect protein
expression at the sarcolemma; interaction
with DAG1 is reduced).
{ECO:0000269|PubMed:24302611,
ECO:0000269|PubMed:9851445}.
/FTId=VAR_023546.
VARIANT 3340 3340 C -> Y (in DMD; results in highly reduced
protein levels and expression at the
sarcolemma).
{ECO:0000269|PubMed:24302611,
ECO:0000269|PubMed:8817332}.
/FTId=VAR_023547.
VARIANT 3421 3421 A -> V (in BMD).
/FTId=VAR_005172.
CONFLICT 664 664 Q -> QM (in Ref. 10; CAA29544).
{ECO:0000305}.
CONFLICT 2361 2361 G -> E (in Ref. 13; CAA38589).
{ECO:0000305}.
CONFLICT 3542 3542 P -> T (in Ref. 6; AAH70078).
{ECO:0000305}.
CONFLICT 3546 3546 M -> V (in Ref. 6; AAH70078).
{ECO:0000305}.
HELIX 14 31 {ECO:0000244|PDB:1DXX}.
TURN 40 46 {ECO:0000244|PDB:1DXX}.
HELIX 48 58 {ECO:0000244|PDB:1DXX}.
HELIX 70 86 {ECO:0000244|PDB:1DXX}.
HELIX 96 100 {ECO:0000244|PDB:1DXX}.
HELIX 104 118 {ECO:0000244|PDB:1DXX}.
TURN 119 121 {ECO:0000244|PDB:1DXX}.
HELIX 122 131 {ECO:0000244|PDB:1DXX}.
HELIX 136 148 {ECO:0000244|PDB:1DXX}.
STRAND 158 160 {ECO:0000244|PDB:1DXX}.
HELIX 161 163 {ECO:0000244|PDB:1DXX}.
HELIX 167 176 {ECO:0000244|PDB:1DXX}.
HELIX 178 180 {ECO:0000244|PDB:1DXX}.
HELIX 183 187 {ECO:0000244|PDB:1DXX}.
HELIX 192 205 {ECO:0000244|PDB:1DXX}.
HELIX 215 218 {ECO:0000244|PDB:1DXX}.
STRAND 219 222 {ECO:0000244|PDB:1DXX}.
HELIX 225 236 {ECO:0000244|PDB:1DXX}.
STRAND 243 245 {ECO:0000244|PDB:1DXX}.
HELIX 339 365 {ECO:0000244|PDB:3UUN}.
HELIX 372 409 {ECO:0000244|PDB:3UUN}.
HELIX 414 452 {ECO:0000244|PDB:3UUN}.
HELIX 3050 3054 {ECO:0000244|PDB:1EG3}.
STRAND 3061 3065 {ECO:0000244|PDB:1EG3}.
STRAND 3071 3075 {ECO:0000244|PDB:1EG3}.
TURN 3076 3079 {ECO:0000244|PDB:1EG3}.
STRAND 3080 3084 {ECO:0000244|PDB:1EG3}.
HELIX 3086 3094 {ECO:0000244|PDB:1EG3}.
HELIX 3095 3098 {ECO:0000244|PDB:1EG3}.
HELIX 3104 3118 {ECO:0000244|PDB:1EG3}.
HELIX 3121 3123 {ECO:0000244|PDB:1EG3}.
HELIX 3126 3135 {ECO:0000244|PDB:1EG3}.
STRAND 3143 3146 {ECO:0000244|PDB:1EG3}.
HELIX 3147 3164 {ECO:0000244|PDB:1EG3}.
STRAND 3165 3168 {ECO:0000244|PDB:1EG4}.
HELIX 3171 3186 {ECO:0000244|PDB:1EG3}.
STRAND 3192 3195 {ECO:0000244|PDB:1EG3}.
HELIX 3196 3205 {ECO:0000244|PDB:1EG3}.
STRAND 3207 3209 {ECO:0000244|PDB:1EG3}.
HELIX 3211 3222 {ECO:0000244|PDB:1EG3}.
HELIX 3231 3247 {ECO:0000244|PDB:1EG3}.
HELIX 3251 3254 {ECO:0000244|PDB:1EG3}.
HELIX 3260 3269 {ECO:0000244|PDB:1EG3}.
TURN 3270 3272 {ECO:0000244|PDB:1EG3}.
HELIX 3278 3286 {ECO:0000244|PDB:1EG3}.
TURN 3290 3293 {ECO:0000244|PDB:1EG3}.
HELIX 3294 3304 {ECO:0000244|PDB:1EG3}.
SEQUENCE 3685 AA; 426750 MW; 24FF7E83F1E6BF8D CRC64;
MLWWEEVEDC YEREDVQKKT FTKWVNAQFS KFGKQHIENL FSDLQDGRRL LDLLEGLTGQ
KLPKEKGSTR VHALNNVNKA LRVLQNNNVD LVNIGSTDIV DGNHKLTLGL IWNIILHWQV
KNVMKNIMAG LQQTNSEKIL LSWVRQSTRN YPQVNVINFT TSWSDGLALN ALIHSHRPDL
FDWNSVVCQQ SATQRLEHAF NIARYQLGIE KLLDPEDVDT TYPDKKSILM YITSLFQVLP
QQVSIEAIQE VEMLPRPPKV TKEEHFQLHH QMHYSQQITV SLAQGYERTS SPKPRFKSYA
YTQAAYVTTS DPTRSPFPSQ HLEAPEDKSF GSSLMESEVN LDRYQTALEE VLSWLLSAED
TLQAQGEISN DVEVVKDQFH THEGYMMDLT AHQGRVGNIL QLGSKLIGTG KLSEDEETEV
QEQMNLLNSR WECLRVASME KQSNLHRVLM DLQNQKLKEL NDWLTKTEER TRKMEEEPLG
PDLEDLKRQV QQHKVLQEDL EQEQVRVNSL THMVVVVDES SGDHATAALE EQLKVLGDRW
ANICRWTEDR WVLLQDILLK WQRLTEEQCL FSAWLSEKED AVNKIHTTGF KDQNEMLSSL
QKLAVLKADL EKKKQSMGKL YSLKQDLLST LKNKSVTQKT EAWLDNFARC WDNLVQKLEK
STAQISQAVT TTQPSLTQTT VMETVTTVTT REQILVKHAQ EELPPPPPQK KRQITVDSEI
RKRLDVDITE LHSWITRSEA VLQSPEFAIF RKEGNFSDLK EKVNAIEREK AEKFRKLQDA
SRSAQALVEQ MVNEGVNADS IKQASEQLNS RWIEFCQLLS ERLNWLEYQN NIIAFYNQLQ
QLEQMTTTAE NWLKIQPTTP SEPTAIKSQL KICKDEVNRL SDLQPQIERL KIQSIALKEK
GQGPMFLDAD FVAFTNHFKQ VFSDVQAREK ELQTIFDTLP PMRYQETMSA IRTWVQQSET
KLSIPQLSVT DYEIMEQRLG ELQALQSSLQ EQQSGLYYLS TTVKEMSKKA PSEISRKYQS
EFEEIEGRWK KLSSQLVEHC QKLEEQMNKL RKIQNHIQTL KKWMAEVDVF LKEEWPALGD
SEILKKQLKQ CRLLVSDIQT IQPSLNSVNE GGQKIKNEAE PEFASRLETE LKELNTQWDH
MCQQVYARKE ALKGGLEKTV SLQKDLSEMH EWMTQAEEEY LERDFEYKTP DELQKAVEEM
KRAKEEAQQK EAKVKLLTES VNSVIAQAPP VAQEALKKEL ETLTTNYQWL CTRLNGKCKT
LEEVWACWHE LLSYLEKANK WLNEVEFKLK TTENIPGGAE EISEVLDSLE NLMRHSEDNP
NQIRILAQTL TDGGVMDELI NEELETFNSR WRELHEEAVR RQKLLEQSIQ SAQETEKSLH
LIQESLTFID KQLAAYIADK VDAAQMPQEA QKIQSDLTSH EISLEEMKKH NQGKEAAQRV
LSQIDVAQKK LQDVSMKFRL FQKPANFEQR LQESKMILDE VKMHLPALET KSVEQEVVQS
QLNHCVNLYK SLSEVKSEVE MVIKTGRQIV QKKQTENPKE LDERVTALKL HYNELGAKVT
ERKQQLEKCL KLSRKMRKEM NVLTEWLAAT DMELTKRSAV EGMPSNLDSE VAWGKATQKE
IEKQKVHLKS ITEVGEALKT VLGKKETLVE DKLSLLNSNW IAVTSRAEEW LNLLLEYQKH
METFDQNVDH ITKWIIQADT LLDESEKKKP QQKEDVLKRL KAELNDIRPK VDSTRDQAAN
LMANRGDHCR KLVEPQISEL NHRFAAISHR IKTGKASIPL KELEQFNSDI QKLLEPLEAE
IQQGVNLKEE DFNKDMNEDN EGTVKELLQR GDNLQQRITD ERKREEIKIK QQLLQTKHNA
LKDLRSQRRK KALEISHQWY QYKRQADDLL KCLDDIEKKL ASLPEPRDER KIKEIDRELQ
KKKEELNAVR RQAEGLSEDG AAMAVEPTQI QLSKRWREIE SKFAQFRRLN FAQIHTVREE
TMMVMTEDMP LEISYVPSTY LTEITHVSQA LLEVEQLLNA PDLCAKDFED LFKQEESLKN
IKDSLQQSSG RIDIIHSKKT AALQSATPVE RVKLQEALSQ LDFQWEKVNK MYKDRQGRFD
RSVEKWRRFH YDIKIFNQWL TEAEQFLRKT QIPENWEHAK YKWYLKELQD GIGQRQTVVR
TLNATGEEII QQSSKTDASI LQEKLGSLNL RWQEVCKQLS DRKKRLEEQK NILSEFQRDL
NEFVLWLEEA DNIASIPLEP GKEQQLKEKL EQVKLLVEEL PLRQGILKQL NETGGPVLVS
APISPEEQDK LENKLKQTNL QWIKVSRALP EKQGEIEAQI KDLGQLEKKL EDLEEQLNHL
LLWLSPIRNQ LEIYNQPNQE GPFDVKETEI AVQAKQPDVE EILSKGQHLY KEKPATQPVK
RKLEDLSSEW KAVNRLLQEL RAKQPDLAPG LTTIGASPTQ TVTLVTQPVV TKETAISKLE
MPSSLMLEVP ALADFNRAWT ELTDWLSLLD QVIKSQRVMV GDLEDINEMI IKQKATMQDL
EQRRPQLEEL ITAAQNLKNK TSNQEARTII TDRIERIQNQ WDEVQEHLQN RRQQLNEMLK
DSTQWLEAKE EAEQVLGQAR AKLESWKEGP YTVDAIQKKI TETKQLAKDL RQWQTNVDVA
NDLALKLLRD YSADDTRKVH MITENINASW RSIHKRVSER EAALEETHRL LQQFPLDLEK
FLAWLTEAET TANVLQDATR KERLLEDSKG VKELMKQWQD LQGEIEAHTD VYHNLDENSQ
KILRSLEGSD DAVLLQRRLD NMNFKWSELR KKSLNIRSHL EASSDQWKRL HLSLQELLVW
LQLKDDELSR QAPIGGDFPA VQKQNDVHRA FKRELKTKEP VIMSTLETVR IFLTEQPLEG
LEKLYQEPRE LPPEERAQNV TRLLRKQAEE VNTEWEKLNL HSADWQRKID ETLERLQELQ
EATDELDLKL RQAEVIKGSW QPVGDLLIDS LQDHLEKVKA LRGEIAPLKE NVSHVNDLAR
QLTTLGIQLS PYNLSTLEDL NTRWKLLQVA VEDRVRQLHE AHRDFGPASQ HFLSTSVQGP
WERAISPNKV PYYINHETQT TCWDHPKMTE LYQSLADLNN VRFSAYRTAM KLRRLQKALC
LDLLSLSAAC DALDQHNLKQ NDQPMDILQI INCLTTIYDR LEQEHNNLVN VPLCVDMCLN
WLLNVYDTGR TGRIRVLSFK TGIISLCKAH LEDKYRYLFK QVASSTGFCD QRRLGLLLHD
SIQIPRQLGE VASFGGSNIE PSVRSCFQFA NNKPEIEAAL FLDWMRLEPQ SMVWLPVLHR
VAAAETAKHQ AKCNICKECP IIGFRYRSLK HFNYDICQSC FFSGRVAKGH KMHYPMVEYC
TPTTSGEDVR DFAKVLKNKF RTKRYFAKHP RMGYLPVQTV LEGDNMETPV TLINFWPVDS
APASSPQLSH DDTHSRIEHY ASRLAEMENS NGSYLNDSIS PNESIDDEHL LIQHYCQSLN
QDSPLSQPRS PAQILISLES EERGELERIL ADLEEENRNL QAEYDRLKQQ HEHKGLSPLP
SPPEMMPTSP QSPRDAELIA EAKLLRQHKG RLEARMQILE DHNKQLESQL HRLRQLLEQP
QAEAKVNGTT VSSPSTSLQR SDSSQPMLLR VVGSQTSDSM GEEDLLSPPQ DTSTGLEEVM
EQLNNSFPSS RGRNTPGKPM REDTM


Related products :

Catalog number Product name Quantity
3586BP-50 Dystrophin Blocking Peptide target: Dystrophin 50 μg
MA1037 Monoclonal Antibodies: Dystrophin; reactive species: Human, mouse, rat, chicken.; Clone: DYS-48; Isotype: IgG2b; Specificity: Dystrophin 100?g
26-124 DTNB is dystrobrevin beta, a component of the dystrophin-associated protein complex (DPC). The DPC consists of dystrophin and several integral and peripheral membrane proteins, including dystroglycans 0.05 mg
LF-MA50038 anti-Dystrophin (DYS-48), Mouse monoclonal to Dystrophin, Isotype IgG2b, Host Mouse 200 ul
LF-PA41411 anti-Dystrophin, Rabbit polyclonal to Dystrophin, Isotype IgG, Host Rabbit 50 ug
MA1037 Monoclonal Anti-Dystrophin, Clone number: DYS-48, Ig type: mouse IgG2b, Immunogen: Recombinant human dystrophin fragment., Specificity: Human;mouse;rat;chicken. No cross reactivity with other proteins 100μg/vial
SCH-3990-5005 MOUSE ANTI HUMAN DYSTROPHIN (C_TERMINAL), Product Type Monoclonal Antibody, Specificity DYSTROPHIN , Target Species Human, Host Mouse, Format Lyophilized, Isotypes IgG1, Applications C, WB*, Cl 2.5 ml
3990-5005 MOUSE ANTI HUMAN DYSTROPHIN (C_TERMINAL), Product Type Monoclonal Antibody, Specificity DYSTROPHIN , Target Species Human, Host Mouse, Format Lyophilized, Isotypes IgG1, Applications C, WB*, Cl 2.5 ml
20-272-191044 Dystrophin - Mouse monoclonal [0.N.258] to Dystrophin; Monoclonal 0.25 ml
18-272-196332 Dystrophin - Rabbit polyclonal to Dystrophin; Polyclonal 0.5 ml
18-272-196333 Dystrophin prediluted - Rabbit polyclonal to Dystrophin prediluted; Polyclonal 7 ml
20-272-191045 Dystrophin - BSA and Azide free - Mouse monoclonal [0.N.258] to Dystrophin - BSA and Azide free; Monoclonal 0.05 mg
MC-087 Dystrophin 100
MC-083 Dystrophin 100
MC-087 Dystrophin 100 µg
MC-083 Dystrophin 100 µg
RP 152-05 Dystrophin; 0.5ml
Mob 387-05 Dystrophin; 0.5ml
BMMS-486-B1 Dystrophin 0.5mL
BMMS-486-B0 Dystrophin 0.1mL
GTX14451 Dystrophin 250 µl
DP152 Dystrophin 1 ml
BMMS-486-B Dystrophin 1mL
MC-087 Dystrophin 1808 100 µg
DP152-05 Dystrophin 0,5 ml


 

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