ID DMD_HUMAN Reviewed; 3685 AA. AC P11532; A1L0U9; E7EQR9; E7EQS5; E7ESB2; E9PDN1; E9PDN5; F5GZY3; F8VX32; AC Q02295; Q14169; Q14170; Q5JYU0; Q6NSJ9; Q7KZ48; Q8N754; Q9UCW3; Q9UCW4; DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot. DT 30-NOV-2010, sequence version 3. DT 27-MAR-2024, entry version 263. DE RecName: Full=Dystrophin; GN Name=DMD; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS GLY-882; LEU-1469 AND RP GLN-2366. RC TISSUE=Muscle; RX PubMed=3282674; DOI=10.1016/0092-8674(88)90383-2; RA Koenig M., Monaco A.P., Kunkel L.M.; RT "The complete sequence of dystrophin predicts a rod-shaped cytoskeletal RT protein."; RL Cell 53:219-228(1988). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS PRO-133; ILE-623; RP GLY-784; GLY-882; PHE-1197; ASN-1377; HIS-1745 AND SER-1844. RX PubMed=2668885; DOI=10.1093/nar/17.13.5391; RA Rosenthal A., Speer A., Billowitz H., Cross G.S., Forrest S.N., RA Davies K.E.; RT "Two human cDNA molecules coding for the Duchenne muscular dystrophy (DMD) RT locus are highly homologous."; RL Nucleic Acids Res. 17:5391-5391(1989). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 15), AND TISSUE SPECIFICITY. RC TISSUE=Brain; RX PubMed=1319059; DOI=10.1073/pnas.89.12.5346; RA Lederfein D., Levy Z., Augier N., Mornet D., Morris G., Fuchs O., Yaffe D., RA Nudel U.; RT "A 71-kilodalton protein is a major product of the Duchenne muscular RT dystrophy gene in brain and other nonmuscle tissues."; RL Proc. Natl. Acad. Sci. U.S.A. 89:5346-5350(1992). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ARG-2937. RX PubMed=15772651; DOI=10.1038/nature03440; RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C., RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., RA Rogers J., Bentley D.R.; RT "The DNA sequence of the human X chromosome."; RL Nature 434:325-337(2005). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 6; 13 AND 14). RC TISSUE=Brain, Placenta, and Testis; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-1411 (ISOFORMS 4 AND 5). RC TISSUE=Retina; RA White R.A.; RL Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-497 (ISOFORM 1). RX PubMed=3607877; DOI=10.1016/0092-8674(87)90504-6; RA Koenig M., Hoffman E.P., Bertelson C.J., Monaco A.P., Feener C., RA Kunkel L.M.; RT "Complete cloning of the Duchenne muscular dystrophy (DMD) cDNA and RT preliminary genomic organization of the DMD gene in normal and affected RT individuals."; RL Cell 50:509-517(1987). RN [9] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-32 (ISOFORM 2), ALTERNATIVE PROMOTER USAGE, RP AND ALTERNATIVE SPLICING. RC TISSUE=Brain; RX PubMed=2648158; DOI=10.1038/338509a0; RA Feener C.A., Koenig M., Kunkel L.M.; RT "Alternative splicing of human dystrophin mRNA generates isoforms at the RT carboxy terminus."; RL Nature 338:509-511(1989). RN [10] RP NUCLEOTIDE SEQUENCE [MRNA] OF 404-1137, AND VARIANT GLY-882. RX PubMed=3428261; DOI=10.1002/j.1460-2075.1987.tb02646.x; RA Cross G.S., Speer A., Rosenthal A., Forrest S.M., Smith T.J., Edwards Y., RA Flint T., Hill D., Davies K.E.; RT "Deletions of fetal and adult muscle cDNA in Duchenne and Becker muscular RT dystrophy patients."; RL EMBO J. 6:3277-3283(1987). RN [11] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 665-722; 2098-2204 AND 2305-2366. RX PubMed=3205741; DOI=10.1093/nar/16.23.11141; RA Chamberlain J.S., Gibbs R.A., Ranier J.A., Nguyen P.N., Caskey C.T.; RT "Deletion screening of the Duchenne muscular dystrophy locus via multiplex RT DNA amplification."; RL Nucleic Acids Res. 16:11141-11156(1988). RN [12] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2147-2204. RX PubMed=2569720; DOI=10.1093/nar/17.14.5611; RA Blonden L.A.J., den Dunnen J.T., van Paassen H.M.B., Wapenaar M.C., RA Grootscholten P.M., Ginjaar H.B., Bakker E., Pearson P.L., RA van Ommen G.J.B.; RT "High resolution deletion breakpoint mapping in the DMD gene by whole RT cosmid hybridization."; RL Nucleic Acids Res. 17:5611-5621(1989). RN [13] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2305-2364. RA Huth A., Will K., Speer A., Bauer D.; RT "Differences in introns flanking exon 48 of the DMD/BMD gene."; RL Submitted (MAR-1991) to the EMBL/GenBank/DDBJ databases. RN [14] RP NUCLEOTIDE SEQUENCE [MRNA] OF 3670-3685, AND TISSUE SPECIFICITY. RC TISSUE=Amnion; RX PubMed=8541829; DOI=10.1093/hmg/4.9.1475; RA Austin R.C., Howard P.L., D'Souza V.N., Klamut H.J., Ray P.N.; RT "Cloning and characterization of alternatively spliced isoforms of Dp71."; RL Hum. Mol. Genet. 4:1475-1483(1995). RN [15] RP ANALYSIS OF THE DOMAIN STRUCTURE. RX PubMed=2407739; DOI=10.1016/s0021-9258(19)39599-7; RA Koenig M., Kunkel L.M.; RT "Detailed analysis of the repeat domain of dystrophin reveals four RT potential hinge segments that may confer flexibility."; RL J. Biol. Chem. 265:4560-4566(1990). RN [16] RP INTERACTION WITH DAG1. RX PubMed=7592992; DOI=10.1074/jbc.270.45.27305; RA Jung D., Yang B., Meyer J., Chamberlain J.S., Campbell K.P.; RT "Identification and characterization of the dystrophin anchoring site on RT beta-dystroglycan."; RL J. Biol. Chem. 270:27305-27310(1995). RN [17] RP INTERACTION WITH SNTB1. RX PubMed=7844150; DOI=10.1083/jcb.128.3.363; RA Ahn A.H., Kunkel L.M.; RT "Syntrophin binds to an alternatively spliced exon of dystrophin."; RL J. Cell Biol. 128:363-371(1995). RN [18] RP INTERACTION WITH SNTA1 AND SNTB2. RX PubMed=8576247; DOI=10.1074/jbc.271.5.2724; RA Ahn A.H., Feener C.A., Gussoni E., Yoshida M., Ozawa E., Kunkel L.M.; RT "The three human syntrophin genes are expressed in diverse tissues, have RT distinct chromosomal locations, and each bind to dystrophin and its RT relatives."; RL J. Biol. Chem. 271:2724-2730(1996). RN [19] RP ALTERNATIVE SPLICING (ISOFORMS 15 AND 16), AND DEVELOPMENTAL STAGE. RC TISSUE=Telencephalon; RX PubMed=9370062; DOI=10.1016/s0165-3806(97)00122-3; RA Ceccarini M., Rizzo G., Rosa G., Chelucci C., Macioce P., Petrucci T.C.; RT "A splice variant of Dp71 lacking the syntrophin binding site is expressed RT in early stages of human neural development."; RL Brain Res. Dev. Brain Res. 103:77-82(1997). RN [20] RP INTERACTION WITH SNTG1 AND SNTG2. RX PubMed=10747910; DOI=10.1074/jbc.m000439200; RA Piluso G., Mirabella M., Ricci E., Belsito A., Abbondanza C., Servidei S., RA Puca A.A., Tonali P., Puca G.A., Nigro V.; RT "Gamma1- and gamma2-syntrophins, two novel dystrophin-binding proteins RT localized in neuronal cells."; RL J. Biol. Chem. 275:15851-15860(2000). RN [21] RP ALTERNATIVE SPLICING (ISOFORM 16). RC TISSUE=Brain; RX PubMed=10734266; DOI=10.1016/s0960-8966(99)00105-4; RA Austin R.C., Morris G.E., Howard P.L., Klamut H.J., Ray P.N.; RT "Expression and synthesis of alternatively spliced variants of Dp71 in RT adult human brain."; RL Neuromuscul. Disord. 10:187-193(2000). RN [22] RP INTERACTION WITH DAG1. RX PubMed=11495720; DOI=10.1016/s0898-6568(01)00188-7; RA Ilsley J.L., Sudol M., Winder S.J.; RT "The interaction of dystrophin with beta-dystroglycan is regulated by RT tyrosine phosphorylation."; RL Cell. Signal. 13:625-632(2001). RN [23] RP REVIEW ON ALTERNATIVE PROMOTER USAGE. RX PubMed=14636778; DOI=10.1016/s1474-4422(03)00585-4; RA Muntoni F., Torelli S., Ferlini A.; RT "Dystrophin and mutations: one gene, several proteins, multiple RT phenotypes."; RL Lancet Neurol. 2:731-740(2003). RN [24] RP INTERACTION WITH KRT19, AND TISSUE SPECIFICITY. RX PubMed=16000376; DOI=10.1091/mbc.e05-02-0112; RA Stone M.R., O'Neill A., Catino D., Bloch R.J.; RT "Specific interaction of the actin-binding domain of dystrophin with RT intermediate filaments containing keratin 19."; RL Mol. Biol. Cell 16:4280-4293(2005). RN [25] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [26] RP FUNCTION IN THE DYSTROPHIN-ASSOCIATED GLYCOPROTEIN COMPLEX. RX PubMed=16710609; DOI=10.1007/s00018-005-5461-0; RA Haenggi T., Fritschy J.M.; RT "Role of dystrophin and utrophin for assembly and function of the RT dystrophin glycoprotein complex in non-muscle tissue."; RL Cell. Mol. Life Sci. 63:1614-1631(2006). RN [27] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3483; SER-3613; SER-3617; RP SER-3623 AND SER-3666, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-340; RP SER-344 AND SER-348 (ISOFORMS 13 AND 15), AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [28] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [29] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3612; SER-3613 AND SER-3623, RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [30] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [31] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3612; SER-3623 AND SER-3624, RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [32] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3490; SER-3500; SER-3623; RP SER-3624 AND SER-3666, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-616 RP (ISOFORM 15), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-629 (ISOFORM RP 14), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-519 (ISOFORM 16), AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [33] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 3046-3306 IN COMPLEX WITH DAG1, RP AND INTERACTION WITH DAG1. RX PubMed=10932245; DOI=10.1038/77923; RA Huang X., Poy F., Zhang R., Joachimiak A., Sudol M., Eck M.J.; RT "Structure of a WW domain containing fragment of dystrophin in complex with RT beta-dystroglycan."; RL Nat. Struct. Biol. 7:634-638(2000). RN [34] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-246. RX PubMed=10801490; DOI=10.1016/s0969-2126(00)00132-5; RA Norwood F.L.M., Sutherland-Smith A.J., Keep N.H., Kendrick-Jones J.; RT "The structure of the N-terminal actin-binding domain of human dystrophin RT and how mutations in this domain may cause Duchenne or Becker muscular RT dystrophy."; RL Structure 8:481-491(2000). RN [35] RP REVIEW ON DMD VARIANTS. RX PubMed=7951253; DOI=10.1002/humu.1380040102; RA Roberts R.G., Gardner R.J., Bobrow M.; RT "Searching for the 1 in 2,400,000: a review of dystrophin gene point RT mutations."; RL Hum. Mutat. 4:1-11(1994). RN [36] RP REVIEW ON VARIANTS. RX PubMed=8045556; DOI=10.1007/bf00202854; RA Rininsland F., Reiss J.; RT "Microlesions and polymorphisms in the Duchenne/Becker muscular dystrophy RT gene."; RL Hum. Genet. 94:111-116(1994). RN [37] RP VARIANT DMD ARG-54. RX PubMed=8401582; DOI=10.1038/ng0893-357; RA Prior T.W., Papp A.C., Snyder P.J., Burghes A.H.M., Bartolo C., Sedra M.S., RA Western L.M., Mendell J.R.; RT "A missense mutation in the dystrophin gene in a Duchenne muscular RT dystrophy patient."; RL Nat. Genet. 4:357-360(1993). RN [38] RP VARIANT DMD GLY-645. RX PubMed=7981690; DOI=10.1093/hmg/3.7.1173; RA Prior T.W., Bartolo C., Papp A.C., Snyder P.J., Sedra M.S., Burghes A.H., RA Mendell J.R.; RT "Identification of a missense mutation, single base deletion and a RT polymorphism in the dystrophin exon 16."; RL Hum. Mol. Genet. 3:1173-1174(1994). RN [39] RP VARIANTS HIS-365; TRP-2191 AND ARG-2937. RX PubMed=7849724; DOI=10.1093/hmg/3.10.1907; RA Nigro V., Nigro G., Esposito M.G., Comi L.I., Molinari A.M., Puca G.A., RA Politano L.; RT "Novel small mutations along the DMD/BMD gene associated with different RT phenotypes."; RL Hum. Mol. Genet. 3:1907-1908(1994). RN [40] RP VARIANT DMD TYR-3340. RX PubMed=8817332; DOI=10.1093/hmg/5.7.973; RA Lenk U., Oexle K., Voit T., Ancker U., Hellner K.A., Speer A., Hubner C.; RT "A cysteine 3340 substitution in the dystroglycan-binding domain of RT dystrophin associated with Duchenne muscular dystrophy, mental retardation RT and absence of the ERG b-wave."; RL Hum. Mol. Genet. 5:973-975(1996). RN [41] RP VARIANT CMD3B ALA-279. RX PubMed=9170407; DOI=10.1161/01.cir.95.10.2434; RA Ortiz-Lopez R., Li H., Su J., Goytia V., Towbin J.A.; RT "Evidence for a dystrophin missense mutation as a cause of X-linked dilated RT cardiomyopathy."; RL Circulation 95:2434-2440(1997). RN [42] RP VARIANT DMD HIS-3335. RX PubMed=9851445; DOI=10.1002/ana.410440619; RA Goldberg L.R., Hausmanowa-Petrusewicz I., Fidzianska A., Duggan D.J., RA Steinberg L.S., Hoffman E.P.; RT "A dystrophin missense mutation showing persistence of dystrophin and RT dystrophin-associated proteins yet a severe phenotype."; RL Ann. Neurol. 44:971-976(1998). RN [43] RP VARIANT BMD PRO-171. RX PubMed=10573008; DOI=10.1038/sj.ejhg.5200370; RA Eraslan S., Kayserili H., Apak M.Y., Kirdar B.; RT "Identification of point mutations in Turkish DMD/BMD families using RT multiplex-single stranded conformation analysis (SSCA)."; RL Eur. J. Hum. Genet. 7:765-770(1999). RN [44] RP VARIANT LYS-1672. RX PubMed=12354438; DOI=10.1016/s0735-1097(02)02126-5; RA Feng J., Yan J.Y., Buzin C.H., Sommer S.S., Towbin J.A.; RT "Comprehensive mutation scanning of the dystrophin gene in patients with RT nonsyndromic X-linked dilated cardiomyopathy."; RL J. Am. Coll. Cardiol. 40:1120-1124(2002). RN [45] RP VARIANTS CMD3B ASN-18 AND LEU-3228, AND VARIANTS TRP-2155; THR-2299; RP GLN-2366; VAL-2910; ASP-2912 AND ARG-2937. RX PubMed=12359139; DOI=10.1016/s1096-7192(02)00153-1; RA Feng J., Yan J., Buzin C.H., Towbin J.A., Sommer S.S.; RT "Mutations in the dystrophin gene are associated with sporadic dilated RT cardiomyopathy."; RL Mol. Genet. Metab. 77:119-126(2002). RN [46] RP VARIANT DMD PHE-3313, AND VARIANT VAL-165. RX PubMed=12632325; DOI=10.1086/374176; RA Flanigan K.M., von Niederhausern A., Dunn D.M., Alder J., Mendell J.R., RA Weiss R.B.; RT "Rapid direct sequence analysis of the dystrophin gene."; RL Am. J. Hum. Genet. 72:931-939(2003). RN [47] RP VARIANTS [LARGE SCALE ANALYSIS] PHE-334; GLN-1219; HIS-1470 AND VAL-2164. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). RN [48] RP VARIANT ARG-118. RX PubMed=21396098; DOI=10.1186/1471-2350-12-37; RA Magri F., Del Bo R., D'Angelo M.G., Govoni A., Ghezzi S., Gandossini S., RA Sciacco M., Ciscato P., Bordoni A., Tedeschi S., Fortunato F., Lucchini V., RA Cereda M., Corti S., Moggio M., Bresolin N., Comi G.P.; RT "Clinical and molecular characterization of a cohort of patients with novel RT nucleotide alterations of the Dystrophin gene detected by direct RT sequencing."; RL BMC Med. Genet. 12:37-37(2011). RN [49] RP CHARACTERIZATION OF VARIANTS DMD PHE-3313; HIS-3335 AND TYR-3340. RX PubMed=24302611; DOI=10.1002/humu.22479; RA Vulin A., Wein N., Strandjord D.M., Johnson E.K., Findlay A.R., Maiti B., RA Howard M.T., Kaminoh Y.J., Taylor L.E., Simmons T.R., Ray W.C., RA Montanaro F., Ervasti J.M., Flanigan K.M.; RT "The ZZ domain of dystrophin in DMD: making sense of missense mutations."; RL Hum. Mutat. 35:257-264(2014). RN [50] RP CHARACTERIZATION OF VARIANT CMD3B ASN-18. RX PubMed=25340340; DOI=10.1371/journal.pone.0110439; RA Singh S.M., Bandi S., Shah D.D., Armstrong G., Mallela K.M.; RT "Missense mutation Lys18Asn in dystrophin that triggers X-linked dilated RT cardiomyopathy decreases protein stability, increases protein unfolding, RT and perturbs protein structure, but does not affect protein function."; RL PLoS ONE 9:E110439-E110439(2014). CC -!- FUNCTION: Anchors the extracellular matrix to the cytoskeleton via F- CC actin. Ligand for dystroglycan. Component of the dystrophin-associated CC glycoprotein complex which accumulates at the neuromuscular junction CC (NMJ) and at a variety of synapses in the peripheral and central CC nervous systems and has a structural function in stabilizing the CC sarcolemma. Also implicated in signaling events and synaptic CC transmission. {ECO:0000250|UniProtKB:P11531, CC ECO:0000269|PubMed:16710609}. CC -!- SUBUNIT: Interacts with SYNM (By similarity). Interacts with the CC syntrophins SNTA1, SNTB1, SNTB2, SNTG1 and SNTG2 (PubMed:7844150, CC PubMed:8576247). Interacts with KRT19 (PubMed:16000376). Component of CC the dystrophin-associated glycoprotein complex which is composed of CC three subcomplexes: a cytoplasmic complex comprised of DMD (or UTRN), CC DTNA and a number of syntrophins, such as SNTB1, SNTB2, SNTG1 and CC SNTG2, the transmembrane dystroglycan complex, and the sarcoglycan- CC sarcospan complex. Interacts with DAG1 (betaDAG1) with DMD; the CC interaction is inhibited by phosphorylation on the PPXY motif of DAG1 CC (PubMed:7592992, PubMed:11495720, PubMed:10932245). Interacts with CC CMYA5 (By similarity). Directly interacts with ANK2 and ANK3; these CC interactions do not interfere with betaDAG1-binding and are necessary CC for proper localization in muscle cells (By similarity). Identified in CC a dystroglycan complex that contains at least PRX, DRP2, UTRN, DMD and CC DAG1 (By similarity). Interacts with DTNB (By similarity). Interacts CC with PGM5; the interaction is direct (By similarity). Interacts with CC NOS1; localizes NOS1 to sarcolemma in muscle cells (By similarity). CC {ECO:0000250|UniProtKB:P11530, ECO:0000250|UniProtKB:P11531, CC ECO:0000269|PubMed:10932245, ECO:0000269|PubMed:11495720, CC ECO:0000269|PubMed:16000376, ECO:0000269|PubMed:7592992, CC ECO:0000269|PubMed:7844150, ECO:0000269|PubMed:8576247}. CC -!- INTERACTION: CC P11532; Q9UBT7: CTNNAL1; NbExp=8; IntAct=EBI-295827, EBI-514206; CC P11532; Q9Y4J8: DTNA; NbExp=3; IntAct=EBI-295827, EBI-949471; CC P11532; O60941: DTNB; NbExp=4; IntAct=EBI-295827, EBI-740402; CC P11532; O60941-5: DTNB; NbExp=3; IntAct=EBI-295827, EBI-11984733; CC P11532; Q96CS2: HAUS1; NbExp=4; IntAct=EBI-295827, EBI-2514791; CC P11532; P41235-3: HNF4A; NbExp=3; IntAct=EBI-295827, EBI-12690684; CC P11532; P08727: KRT19; NbExp=2; IntAct=EBI-295827, EBI-742756; CC P11532; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-295827, EBI-79165; CC P11532; Q13424: SNTA1; NbExp=3; IntAct=EBI-295827, EBI-717191; CC P11532; Q13884: SNTB1; NbExp=4; IntAct=EBI-295827, EBI-295843; CC P11532; Q13425: SNTB2; NbExp=2; IntAct=EBI-295827, EBI-80411; CC P11532-5; Q01484: ANK2; NbExp=2; IntAct=EBI-1018651, EBI-941975; CC P11532-5; Q3T1J5: Ank3; Xeno; NbExp=2; IntAct=EBI-1018651, EBI-2133962; CC -!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma CC {ECO:0000250|UniProtKB:P11531}; Peripheral membrane protein CC {ECO:0000250|UniProtKB:P11531}; Cytoplasmic side CC {ECO:0000250|UniProtKB:P11531}. Cytoplasm, cytoskeleton CC {ECO:0000250|UniProtKB:P11531}. Postsynaptic cell membrane CC {ECO:0000250|UniProtKB:P11531}. Note=In muscle cells, sarcolemma CC localization requires the presence of ANK2, while localization to CC costameres requires the presence of ANK3. Localizes to neuromuscular CC junctions (NMJs). In adult muscle, NMJ localization depends upon ANK2 CC presence, but not in newborn animals. {ECO:0000250|UniProtKB:P11531}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=17; CC Name=1; Synonyms=Dystrophin-4, Dp427m; CC IsoId=P11532-1; Sequence=Displayed; CC Name=2; Synonyms=Dystrophin-3, Dp427c; CC IsoId=P11532-4; Sequence=VSP_006809; CC Name=3; Synonyms=Dp427p; CC IsoId=P11532-11; Sequence=VSP_060274; CC Name=4; Synonyms=Dystrophin-1, Dp260-1; CC IsoId=P11532-2; Sequence=VSP_006806, VSP_006807; CC Name=5; Synonyms=Dystrophin-2, Dp260-2; CC IsoId=P11532-3; Sequence=VSP_006808, VSP_006807; CC Name=6; Synonyms=Dp140; CC IsoId=P11532-12; Sequence=VSP_060275; CC Name=7; Synonyms=Dp140c; CC IsoId=P11532-13; Sequence=VSP_060275, VSP_046319; CC Name=8; Synonyms=Dp140b; CC IsoId=P11532-14; Sequence=VSP_060275, VSP_017493; CC Name=9; Synonyms=Dp140ab; CC IsoId=P11532-15; Sequence=VSP_060275, VSP_017492, VSP_017493; CC Name=10; Synonyms=Dp140bc; CC IsoId=P11532-16; Sequence=VSP_060275, VSP_046319, VSP_017493; CC Name=11; Synonyms=Dp116; CC IsoId=P11532-17; Sequence=VSP_060276, VSP_060277; CC Name=12; Synonyms=Dp71; CC IsoId=P11532-7; Sequence=VSP_017490, VSP_017491; CC Name=13; Synonyms=Dp71a; CC IsoId=P11532-8; Sequence=VSP_017490, VSP_017491, VSP_017492; CC Name=14; Synonyms=Dp71b; CC IsoId=P11532-6; Sequence=VSP_017490, VSP_017491, VSP_017493; CC Name=15; Synonyms=Dp71ab; CC IsoId=P11532-5; Sequence=VSP_017490, VSP_017491, VSP_017492, CC VSP_017493; CC Name=16; Synonyms=Dp60, Dp71delta110; CC IsoId=P11532-9; Sequence=VSP_017490, VSP_017491, VSP_046319, CC VSP_017493; CC Name=17; Synonyms=Dp40; CC IsoId=P11532-18; Sequence=VSP_017490, VSP_017491, VSP_060278; CC -!- TISSUE SPECIFICITY: Expressed in muscle fibers accumulating in the CC costameres of myoplasm at the sarcolemma. Expressed in brain, muscle, CC kidney, lung and testis. Most tissues contain transcripts of multiple CC isoforms. Isoform 15: Only isoform to be detected in heart and liver CC and is also expressed in brain, testis and hepatoma cells. CC {ECO:0000269|PubMed:1319059, ECO:0000269|PubMed:16000376, CC ECO:0000269|PubMed:8541829}. CC -!- DEVELOPMENTAL STAGE: Isoform 15: Expressed in embryonic neural tissue CC from the sixth week of development. Isoform 16: Detected in all CC embryonic tissues examined. {ECO:0000269|PubMed:9370062}. CC -!- DISEASE: Duchenne muscular dystrophy (DMD) [MIM:310200]: Most common CC form of muscular dystrophy; a sex-linked recessive disorder. It CC typically presents in boys aged 3 to 7 year as proximal muscle weakness CC causing waddling gait, toe-walking, lordosis, frequent falls, and CC difficulty in standing up and climbing up stairs. The pelvic girdle is CC affected first, then the shoulder girdle. Progression is steady and CC most patients are confined to a wheelchair by age of 10 or 12. Flexion CC contractures and scoliosis ultimately occur. About 50% of patients have CC a lower IQ than their genetic expectations would suggest. There is no CC treatment. {ECO:0000269|PubMed:12632325, ECO:0000269|PubMed:24302611, CC ECO:0000269|PubMed:7981690, ECO:0000269|PubMed:8401582, CC ECO:0000269|PubMed:8817332, ECO:0000269|PubMed:9851445}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- DISEASE: Becker muscular dystrophy (BMD) [MIM:300376]: A neuromuscular CC disorder characterized by dystrophin deficiency. It appears between the CC age of 5 and 15 years with a proximal motor deficiency of variable CC progression. Heart involvement can be the initial sign. Becker muscular CC dystrophy has a more benign course than Duchenne muscular dystrophy. CC {ECO:0000269|PubMed:10573008}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Cardiomyopathy, dilated, 3B (CMD3B) [MIM:302045]: A disorder CC characterized by ventricular dilation and impaired systolic function, CC resulting in congestive heart failure and arrhythmia. Patients are at CC risk of premature death. CMD3B is an X-linked disorder. CC {ECO:0000269|PubMed:12359139, ECO:0000269|PubMed:25340340, CC ECO:0000269|PubMed:9170407}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- MISCELLANEOUS: The DMD gene is the largest known gene in humans. It is CC 2.4 million base-pairs in size, comprises 79 exons and takes over 16 CC hours to be transcribed and cotranscriptionally spliced. CC -!- MISCELLANEOUS: [Isoform 1]: Produced by alternative promoter usage. CC -!- MISCELLANEOUS: [Isoform 2]: Produced by alternative promoter usage. CC {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 3]: Produced by alternative promoter usage. CC {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 4]: Produced by alternative promoter usage. CC {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 5]: Produced by alternative splicing of isoform CC 4. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 6]: Produced by alternative promoter usage. CC {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 7]: Produced by alternative splicing of isoform CC 6. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 8]: Produced by alternative splicing of isoform CC 6. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 9]: Produced by alternative splicing of isoform CC 6. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 10]: Produced by alternative splicing of CC isoform 6. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 11]: Produced by alternative promoter usage. CC {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 12]: Produced by alternative promoter usage. CC {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 13]: Produced by alternative splicing of CC isoform 12. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 14]: Produced by alternative splicing of CC isoform 12. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 15]: Produced by alternative splicing of CC isoform 12. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 16]: Produced by alternative splicing of CC isoform 12. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 17]: Produced by alternative splicing of CC isoform 12. {ECO:0000305}. CC -!- WEB RESOURCE: Name=DMD; Note=Dystrophin Mutation Database; CC URL="https://www.dmd.nl/database.html"; CC -!- WEB RESOURCE: Name=Wikipedia; Note=Dystrophin entry; CC URL="https://en.wikipedia.org/wiki/Dystrophin"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M18533; AAA53189.1; -; mRNA. DR EMBL; X14298; CAA32479.1; -; mRNA. DR EMBL; M92650; AAA52316.1; -; mRNA. DR EMBL; AC078957; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL031542; CAI42229.1; -; Genomic_DNA. DR EMBL; AC004468; CAI42229.1; JOINED; Genomic_DNA. DR EMBL; AC006061; CAI42229.1; JOINED; Genomic_DNA. DR EMBL; AC078958; CAI42229.1; JOINED; Genomic_DNA. DR EMBL; AC079143; CAI42229.1; JOINED; Genomic_DNA. DR EMBL; AC079175; CAI42229.1; JOINED; Genomic_DNA. DR EMBL; AC079177; CAI42229.1; JOINED; Genomic_DNA. DR EMBL; AC079864; CAI42229.1; JOINED; Genomic_DNA. DR EMBL; AC090632; CAI42229.1; JOINED; Genomic_DNA. DR EMBL; AC093167; CAI42229.1; JOINED; Genomic_DNA. DR EMBL; AC093193; CAI42229.1; JOINED; Genomic_DNA. DR EMBL; AC096506; CAI42229.1; JOINED; Genomic_DNA. DR EMBL; AL031643; CAI42229.1; JOINED; Genomic_DNA. DR EMBL; AL096699; CAI42229.1; JOINED; Genomic_DNA. DR EMBL; AL109609; CAI42229.1; JOINED; Genomic_DNA. DR EMBL; AL139278; CAI42229.1; JOINED; Genomic_DNA. DR EMBL; AL451144; CAI42229.1; JOINED; Genomic_DNA. DR EMBL; AL031643; CAI43058.1; -; Genomic_DNA. DR EMBL; AC004468; CAI43058.1; JOINED; Genomic_DNA. DR EMBL; AC006061; CAI43058.1; JOINED; Genomic_DNA. DR EMBL; AC078958; CAI43058.1; JOINED; Genomic_DNA. DR EMBL; AC079143; CAI43058.1; JOINED; Genomic_DNA. DR EMBL; AC079175; CAI43058.1; JOINED; Genomic_DNA. DR EMBL; AC079177; CAI43058.1; JOINED; Genomic_DNA. DR EMBL; AC079864; CAI43058.1; JOINED; Genomic_DNA. DR EMBL; AC090632; CAI43058.1; JOINED; Genomic_DNA. DR EMBL; AC093167; CAI43058.1; JOINED; Genomic_DNA. DR EMBL; AC093193; CAI43058.1; JOINED; Genomic_DNA. DR EMBL; AC096506; CAI43058.1; JOINED; Genomic_DNA. DR EMBL; AL031542; CAI43058.1; JOINED; Genomic_DNA. DR EMBL; AL096699; CAI43058.1; JOINED; Genomic_DNA. DR EMBL; AL109609; CAI43058.1; JOINED; Genomic_DNA. DR EMBL; AL139278; CAI43058.1; JOINED; Genomic_DNA. DR EMBL; AL451144; CAI43058.1; JOINED; Genomic_DNA. DR EMBL; AL049643; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL050305; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL096699; CAI42225.1; -; Genomic_DNA. DR EMBL; AC004468; CAI42225.1; JOINED; Genomic_DNA. DR EMBL; AC006061; CAI42225.1; JOINED; Genomic_DNA. DR EMBL; AC078958; CAI42225.1; JOINED; Genomic_DNA. DR EMBL; AC079143; CAI42225.1; JOINED; Genomic_DNA. DR EMBL; AC079175; CAI42225.1; JOINED; Genomic_DNA. DR EMBL; AC079177; CAI42225.1; JOINED; Genomic_DNA. DR EMBL; AC079864; CAI42225.1; JOINED; Genomic_DNA. DR EMBL; AC090632; CAI42225.1; JOINED; Genomic_DNA. DR EMBL; AC093167; CAI42225.1; JOINED; Genomic_DNA. DR EMBL; AC093193; CAI42225.1; JOINED; Genomic_DNA. DR EMBL; AC096506; CAI42225.1; JOINED; Genomic_DNA. DR EMBL; AL031542; CAI42225.1; JOINED; Genomic_DNA. DR EMBL; AL031643; CAI42225.1; JOINED; Genomic_DNA. DR EMBL; AL109609; CAI42225.1; JOINED; Genomic_DNA. DR EMBL; AL139278; CAI42225.1; JOINED; Genomic_DNA. DR EMBL; AL451144; CAI42225.1; JOINED; Genomic_DNA. DR EMBL; AL109609; CAI42950.1; -; Genomic_DNA. DR EMBL; AC004468; CAI42950.1; JOINED; Genomic_DNA. DR EMBL; AC006061; CAI42950.1; JOINED; Genomic_DNA. DR EMBL; AC078958; CAI42950.1; JOINED; Genomic_DNA. DR EMBL; AC079143; CAI42950.1; JOINED; Genomic_DNA. DR EMBL; AC079175; CAI42950.1; JOINED; Genomic_DNA. DR EMBL; AC079177; CAI42950.1; JOINED; Genomic_DNA. DR EMBL; AC079864; CAI42950.1; JOINED; Genomic_DNA. DR EMBL; AC090632; CAI42950.1; JOINED; Genomic_DNA. DR EMBL; AC093167; CAI42950.1; JOINED; Genomic_DNA. DR EMBL; AC093193; CAI42950.1; JOINED; Genomic_DNA. DR EMBL; AC096506; CAI42950.1; JOINED; Genomic_DNA. DR EMBL; AL031542; CAI42950.1; JOINED; Genomic_DNA. DR EMBL; AL031643; CAI42950.1; JOINED; Genomic_DNA. DR EMBL; AL096699; CAI42950.1; JOINED; Genomic_DNA. DR EMBL; AL139278; CAI42950.1; JOINED; Genomic_DNA. DR EMBL; AL451144; CAI42950.1; JOINED; Genomic_DNA. DR EMBL; AL121880; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL139278; CAI42991.1; -; Genomic_DNA. DR EMBL; AC004468; CAI42991.1; JOINED; Genomic_DNA. DR EMBL; AC006061; CAI42991.1; JOINED; Genomic_DNA. DR EMBL; AC078958; CAI42991.1; JOINED; Genomic_DNA. DR EMBL; AC079143; CAI42991.1; JOINED; Genomic_DNA. DR EMBL; AC079175; CAI42991.1; JOINED; Genomic_DNA. DR EMBL; AC079177; CAI42991.1; JOINED; Genomic_DNA. DR EMBL; AC079864; CAI42991.1; JOINED; Genomic_DNA. DR EMBL; AC090632; CAI42991.1; JOINED; Genomic_DNA. DR EMBL; AC093167; CAI42991.1; JOINED; Genomic_DNA. DR EMBL; AC093193; CAI42991.1; JOINED; Genomic_DNA. DR EMBL; AC096506; CAI42991.1; JOINED; Genomic_DNA. DR EMBL; AL031542; CAI42991.1; JOINED; Genomic_DNA. DR EMBL; AL031643; CAI42991.1; JOINED; Genomic_DNA. DR EMBL; AL096699; CAI42991.1; JOINED; Genomic_DNA. DR EMBL; AL109609; CAI42991.1; JOINED; Genomic_DNA. DR EMBL; AL451144; CAI42991.1; JOINED; Genomic_DNA. DR EMBL; AL139401; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL451144; CAI39566.1; -; Genomic_DNA. DR EMBL; AC004468; CAI39566.1; JOINED; Genomic_DNA. DR EMBL; AC006061; CAI39566.1; JOINED; Genomic_DNA. DR EMBL; AC078958; CAI39566.1; JOINED; Genomic_DNA. DR EMBL; AC079143; CAI39566.1; JOINED; Genomic_DNA. DR EMBL; AC079175; CAI39566.1; JOINED; Genomic_DNA. DR EMBL; AC079177; CAI39566.1; JOINED; Genomic_DNA. DR EMBL; AC079864; CAI39566.1; JOINED; Genomic_DNA. DR EMBL; AC090632; CAI39566.1; JOINED; Genomic_DNA. DR EMBL; AC093167; CAI39566.1; JOINED; Genomic_DNA. DR EMBL; AC093193; CAI39566.1; JOINED; Genomic_DNA. DR EMBL; AC096506; CAI39566.1; JOINED; Genomic_DNA. DR EMBL; AL031542; CAI39566.1; JOINED; Genomic_DNA. DR EMBL; AL031643; CAI39566.1; JOINED; Genomic_DNA. DR EMBL; AL096699; CAI39566.1; JOINED; Genomic_DNA. DR EMBL; AL109609; CAI39566.1; JOINED; Genomic_DNA. DR EMBL; AL139278; CAI39566.1; JOINED; Genomic_DNA. DR EMBL; AL596023; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471074; EAW99065.1; -; Genomic_DNA. DR EMBL; BC028720; AAH28720.1; -; mRNA. DR EMBL; BC070078; AAH70078.1; -; mRNA. DR EMBL; BC094758; AAH94758.1; -; mRNA. DR EMBL; BC127103; AAI27104.2; -; mRNA. DR EMBL; U27203; AAA86115.1; -; Genomic_DNA. DR EMBL; U27203; AAA86116.1; -; Genomic_DNA. DR EMBL; X15148; CAA33245.1; -; mRNA. DR EMBL; X06178; CAA29544.1; -; mRNA. DR EMBL; X06179; CAA29545.1; -; mRNA. DR EMBL; X13045; CAA31451.1; -; Genomic_DNA. DR EMBL; X13046; CAA31452.1; -; Genomic_DNA. DR EMBL; X13047; CAA31453.1; -; Genomic_DNA. DR EMBL; X13048; CAA31454.1; -; Genomic_DNA. DR EMBL; X15495; CAA33518.1; -; Genomic_DNA. DR EMBL; X54820; CAA38589.1; -; Genomic_DNA. DR CCDS; CCDS14229.1; -. [P11532-15] DR CCDS; CCDS14230.1; -. [P11532-16] DR CCDS; CCDS14231.1; -. [P11532-6] DR CCDS; CCDS14232.1; -. [P11532-5] DR CCDS; CCDS14233.1; -. [P11532-1] DR CCDS; CCDS14234.1; -. [P11532-7] DR CCDS; CCDS48091.1; -. [P11532-12] DR CCDS; CCDS55394.1; -. [P11532-13] DR CCDS; CCDS55395.1; -. [P11532-11] DR CCDS; CCDS94585.1; -. [P11532-8] DR CCDS; CCDS94586.1; -. [P11532-3] DR PIR; A45255; A45255. DR RefSeq; NP_000100.2; NM_000109.3. DR RefSeq; NP_003997.1; NM_004006.2. DR RefSeq; NP_004000.1; NM_004009.3. DR RefSeq; NP_004001.1; NM_004010.3. DR RefSeq; NP_004002.2; NM_004011.3. DR RefSeq; NP_004003.1; NM_004012.3. DR RefSeq; NP_004004.1; NM_004013.2. DR RefSeq; NP_004005.1; NM_004014.2. DR RefSeq; NP_004006.1; NM_004015.2. [P11532-7] DR RefSeq; NP_004007.1; NM_004016.2. [P11532-6] DR RefSeq; NP_004008.1; NM_004017.2. [P11532-8] DR RefSeq; NP_004009.1; NM_004018.2. [P11532-5] DR RefSeq; NP_004010.1; NM_004019.2. [P11532-18] DR RefSeq; NP_004011.2; NM_004020.3. DR RefSeq; NP_004012.1; NM_004021.2. DR RefSeq; NP_004013.1; NM_004022.2. DR RefSeq; NP_004014.1; NM_004023.2. DR PDB; 1DXX; X-ray; 2.60 A; A/B/C/D=1-246. DR PDB; 1EG3; X-ray; 2.00 A; A=3046-3306. DR PDB; 1EG4; X-ray; 2.00 A; A=3046-3306. DR PDB; 3UUN; X-ray; 2.30 A; A/B=338-456. DR PDBsum; 1DXX; -. DR PDBsum; 1EG3; -. DR PDBsum; 1EG4; -. DR PDBsum; 3UUN; -. DR SASBDB; P11532; -. DR SMR; P11532; -. DR BioGRID; 108096; 97. DR ComplexPortal; CPX-2424; Dystrophin glycoprotein complex, skeletal muscle variant. [P11532-1] DR ComplexPortal; CPX-2453; Dystrophin glycoprotein complex, CNS variant. [P11532-4] DR ComplexPortal; CPX-2454; Dystrophin glycoprotein complex, retinal outer plexiform layer variant. [P11532-2] DR ComplexPortal; CPX-2455; Dystrophin glycoprotein complex, retinal inner limiting membrane variant. [P11532-7] DR DIP; DIP-32593N; -. DR IntAct; P11532; 63. DR MINT; P11532; -. DR STRING; 9606.ENSP00000354923; -. DR DrugBank; DB15593; Golodirsen. DR DrugCentral; P11532; -. DR TCDB; 8.A.66.1.2; the dystrophin (dystrophin) family. DR CarbonylDB; P11532; -. DR GlyGen; P11532; 2 sites, 1 O-linked glycan (2 sites). DR iPTMnet; P11532; -. DR PhosphoSitePlus; P11532; -. DR SwissPalm; P11532; -. DR BioMuta; DMD; -. DR DMDM; 313104240; -. DR EPD; P11532; -. DR jPOST; P11532; -. DR MassIVE; P11532; -. DR MaxQB; P11532; -. DR PaxDb; 9606-ENSP00000354923; -. DR PeptideAtlas; P11532; -. DR ProteomicsDB; 17631; -. DR ProteomicsDB; 17635; -. DR ProteomicsDB; 17951; -. DR ProteomicsDB; 19709; -. DR ProteomicsDB; 19712; -. DR ProteomicsDB; 25166; -. DR ProteomicsDB; 29059; -. DR ProteomicsDB; 52788; -. [P11532-1] DR ProteomicsDB; 52789; -. [P11532-2] DR ProteomicsDB; 52790; -. [P11532-3] DR ProteomicsDB; 52791; -. [P11532-4] DR ProteomicsDB; 52792; -. [P11532-5] DR ProteomicsDB; 52793; -. [P11532-6] DR Pumba; P11532; -. DR Antibodypedia; 476; 704 antibodies from 38 providers. DR DNASU; 1756; -. DR Ensembl; ENST00000361471.8; ENSP00000354464.4; ENSG00000198947.18. [P11532-5] DR Ensembl; ENST00000378680.6; ENSP00000367951.2; ENSG00000198947.18. [P11532-9] DR Ensembl; ENST00000378702.8; ENSP00000367974.4; ENSG00000198947.18. [P11532-7] DR Ensembl; ENST00000378723.7; ENSP00000367997.3; ENSG00000198947.18. [P11532-6] DR Ensembl; ENST00000682600.1; ENSP00000507640.1; ENSG00000198947.18. [P11532-8] DR GeneID; 1756; -. DR KEGG; hsa:1756; -. DR UCSC; uc004dcm.2; human. [P11532-1] DR UCSC; uc004dcq.1; human. DR UCSC; uc004dcr.1; human. DR UCSC; uc004dct.1; human. DR UCSC; uc004dcu.2; human. DR UCSC; uc004dcv.1; human. DR UCSC; uc004dcy.2; human. DR AGR; HGNC:2928; -. DR CTD; 1756; -. DR DisGeNET; 1756; -. DR GeneCards; DMD; -. DR GeneReviews; DMD; -. DR HGNC; HGNC:2928; DMD. DR HPA; ENSG00000198947; Low tissue specificity. DR MalaCards; DMD; -. DR MIM; 300376; phenotype. DR MIM; 300377; gene. DR MIM; 302045; phenotype. DR MIM; 310200; phenotype. DR neXtProt; NX_P11532; -. DR OpenTargets; ENSG00000198947; -. DR Orphanet; 98895; Becker muscular dystrophy. DR Orphanet; 98896; Duchenne muscular dystrophy. DR Orphanet; 154; Familial isolated dilated cardiomyopathy. DR Orphanet; 206546; Symptomatic form of muscular dystrophy of Duchenne and Becker in female carriers. DR Orphanet; 777; X-linked non-syndromic intellectual disability. DR PharmGKB; PA27378; -. DR VEuPathDB; HostDB:ENSG00000198947; -. DR eggNOG; KOG4286; Eukaryota. DR GeneTree; ENSGT00940000154342; -. DR HOGENOM; CLU_001187_1_2_1; -. DR InParanoid; P11532; -. DR OrthoDB; 2880153at2759; -. DR PhylomeDB; P11532; -. DR TreeFam; TF320178; -. DR PathwayCommons; P11532; -. DR Reactome; R-HSA-3000171; Non-integrin membrane-ECM interactions. DR Reactome; R-HSA-390522; Striated Muscle Contraction. DR SignaLink; P11532; -. DR SIGNOR; P11532; -. DR BioGRID-ORCS; 1756; 10 hits in 785 CRISPR screens. DR ChiTaRS; DMD; human. DR EvolutionaryTrace; P11532; -. DR GeneWiki; Dystrophin; -. DR GenomeRNAi; 1756; -. DR Pharos; P11532; Tclin. DR PRO; PR:P11532; -. DR Proteomes; UP000005640; Chromosome X. DR RNAct; P11532; Protein. DR Bgee; ENSG00000198947; Expressed in trigeminal ganglion and 203 other cell types or tissues. DR ExpressionAtlas; P11532; baseline and differential. DR GO; GO:0009986; C:cell surface; IDA:UniProtKB. DR GO; GO:0030055; C:cell-substrate junction; ISS:BHF-UCL. DR GO; GO:0043034; C:costamere; IDA:UniProtKB. DR GO; GO:0005856; C:cytoskeleton; TAS:ProtInc. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0016010; C:dystrophin-associated glycoprotein complex; IDA:UniProtKB. DR GO; GO:0030175; C:filopodium; IDA:BHF-UCL. DR GO; GO:0031527; C:filopodium membrane; IDA:BHF-UCL. DR GO; GO:0045121; C:membrane raft; ISS:BHF-UCL. DR GO; GO:0044306; C:neuron projection terminus; ISS:BHF-UCL. DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL. DR GO; GO:0005886; C:plasma membrane; TAS:BHF-UCL. DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell. DR GO; GO:0032991; C:protein-containing complex; IDA:MGI. DR GO; GO:0042383; C:sarcolemma; IDA:BHF-UCL. DR GO; GO:0045202; C:synapse; ISS:BHF-UCL. DR GO; GO:0016013; C:syntrophin complex; TAS:BHF-UCL. DR GO; GO:0030018; C:Z disc; ISS:BHF-UCL. DR GO; GO:0003779; F:actin binding; IDA:BHF-UCL. DR GO; GO:0002162; F:dystroglycan binding; IPI:UniProtKB. DR GO; GO:0017022; F:myosin binding; IDA:BHF-UCL. DR GO; GO:0050998; F:nitric-oxide synthase binding; ISS:BHF-UCL. DR GO; GO:0005200; F:structural constituent of cytoskeleton; TAS:ProtInc. DR GO; GO:0008307; F:structural constituent of muscle; IDA:UniProtKB. DR GO; GO:0017166; F:vinculin binding; IPI:BHF-UCL. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0086001; P:cardiac muscle cell action potential; ISS:BHF-UCL. DR GO; GO:0060048; P:cardiac muscle contraction; IMP:BHF-UCL. DR GO; GO:0035633; P:maintenance of blood-brain barrier; NAS:ARUK-UCL. DR GO; GO:0044458; P:motile cilium assembly; TAS:BHF-UCL. DR GO; GO:0046716; P:muscle cell cellular homeostasis; ISS:BHF-UCL. DR GO; GO:0055001; P:muscle cell development; ISS:BHF-UCL. DR GO; GO:0007517; P:muscle organ development; NAS:ProtInc. DR GO; GO:1902083; P:negative regulation of peptidyl-cysteine S-nitrosylation; ISS:BHF-UCL. DR GO; GO:0033137; P:negative regulation of peptidyl-serine phosphorylation; ISS:BHF-UCL. DR GO; GO:0048666; P:neuron development; IBA:GO_Central. DR GO; GO:0043043; P:peptide biosynthetic process; IDA:UniProtKB. DR GO; GO:0045666; P:positive regulation of neuron differentiation; IMP:BHF-UCL. DR GO; GO:0010976; P:positive regulation of neuron projection development; IMP:BHF-UCL. DR GO; GO:2000651; P:positive regulation of sodium ion transmembrane transporter activity; ISS:BHF-UCL. DR GO; GO:0008104; P:protein localization; IMP:BHF-UCL. DR GO; GO:0065003; P:protein-containing complex assembly; ISS:BHF-UCL. DR GO; GO:0010881; P:regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion; ISS:BHF-UCL. DR GO; GO:0090287; P:regulation of cellular response to growth factor stimulus; IMP:BHF-UCL. DR GO; GO:0002027; P:regulation of heart rate; IMP:BHF-UCL. DR GO; GO:0090257; P:regulation of muscle system process; IBA:GO_Central. DR GO; GO:0010880; P:regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; ISS:BHF-UCL. DR GO; GO:0060314; P:regulation of ryanodine-sensitive calcium-release channel activity; ISS:BHF-UCL. DR GO; GO:0014819; P:regulation of skeletal muscle contraction; ISS:BHF-UCL. DR GO; GO:0014809; P:regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion; ISS:BHF-UCL. DR GO; GO:1901385; P:regulation of voltage-gated calcium channel activity; ISS:BHF-UCL. DR GO; GO:0035994; P:response to muscle stretch; ISS:BHF-UCL. DR GO; GO:0007519; P:skeletal muscle tissue development; IBA:GO_Central. DR GO; GO:0099536; P:synaptic signaling; IBA:GO_Central. DR CDD; cd21231; CH_DMD_rpt1; 1. DR CDD; cd21233; CH_DMD_rpt2; 1. DR CDD; cd16246; EFh_DMD; 1. DR CDD; cd00176; SPEC; 11. DR CDD; cd00201; WW; 1. DR CDD; cd02334; ZZ_dystrophin; 1. DR Gene3D; 1.20.58.60; -; 16. DR Gene3D; 2.20.70.10; -; 1. DR Gene3D; 3.30.60.90; -; 1. DR Gene3D; 1.10.418.10; Calponin-like domain; 2. DR Gene3D; 1.10.238.10; EF-hand; 2. DR IDEAL; IID00267; -. DR InterPro; IPR001589; Actinin_actin-bd_CS. DR InterPro; IPR001715; CH_dom. DR InterPro; IPR036872; CH_dom_sf. DR InterPro; IPR035436; Dystrophin/utrophin. DR InterPro; IPR011992; EF-hand-dom_pair. DR InterPro; IPR015153; EF-hand_dom_typ1. DR InterPro; IPR015154; EF-hand_dom_typ2. DR InterPro; IPR018159; Spectrin/alpha-actinin. DR InterPro; IPR002017; Spectrin_repeat. DR InterPro; IPR001202; WW_dom. DR InterPro; IPR036020; WW_dom_sf. DR InterPro; IPR000433; Znf_ZZ. DR InterPro; IPR043145; Znf_ZZ_sf. DR PANTHER; PTHR12268:SF25; DYSTROPHIN; 1. DR PANTHER; PTHR12268; E3 UBIQUITIN-PROTEIN LIGASE KCMF1; 1. DR Pfam; PF00307; CH; 2. DR Pfam; PF09068; EF-hand_2; 1. DR Pfam; PF09069; EF-hand_3; 1. DR Pfam; PF00435; Spectrin; 17. DR Pfam; PF00397; WW; 1. DR Pfam; PF00569; ZZ; 1. DR PIRSF; PIRSF002341; Dystrophin/utrophin; 1. DR SMART; SM00033; CH; 2. DR SMART; SM00150; SPEC; 22. DR SMART; SM00456; WW; 1. DR SMART; SM00291; ZnF_ZZ; 1. DR SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1. DR SUPFAM; SSF47473; EF-hand; 2. DR SUPFAM; SSF57850; RING/U-box; 1. DR SUPFAM; SSF46966; Spectrin repeat; 18. DR SUPFAM; SSF51045; WW domain; 1. DR PROSITE; PS00019; ACTININ_1; 1. DR PROSITE; PS00020; ACTININ_2; 1. DR PROSITE; PS50021; CH; 2. DR PROSITE; PS01159; WW_DOMAIN_1; 1. DR PROSITE; PS50020; WW_DOMAIN_2; 1. DR PROSITE; PS01357; ZF_ZZ_1; 1. DR PROSITE; PS50135; ZF_ZZ_2; 1. DR Genevisible; P11532; HS. PE 1: Evidence at protein level; KW 3D-structure; Actin-binding; Alternative promoter usage; KW Alternative splicing; Calcium; Cardiomyopathy; Cell membrane; Cytoplasm; KW Cytoskeleton; Disease variant; Membrane; Metal-binding; Phosphoprotein; KW Postsynaptic cell membrane; Reference proteome; Repeat; Synapse; Zinc; KW Zinc-finger. FT CHAIN 1..3685 FT /note="Dystrophin" FT /id="PRO_0000076075" FT DOMAIN 15..119 FT /note="Calponin-homology (CH) 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044" FT DOMAIN 134..240 FT /note="Calponin-homology (CH) 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044" FT REPEAT 339..447 FT /note="Spectrin 1" FT REPEAT 448..556 FT /note="Spectrin 2" FT REPEAT 559..667 FT /note="Spectrin 3" FT REPEAT 719..828 FT /note="Spectrin 4" FT REPEAT 830..934 FT /note="Spectrin 5" FT REPEAT 943..1045 FT /note="Spectrin 6" FT REPEAT 1048..1154 FT /note="Spectrin 7" FT REPEAT 1157..1263 FT /note="Spectrin 8" FT REPEAT 1266..1367 FT /note="Spectrin 9" FT REPEAT 1368..1463 FT /note="Spectrin 10" FT REPEAT 1468..1568 FT /note="Spectrin 11" FT REPEAT 1571..1676 FT /note="Spectrin 12" FT REPEAT 1679..1778 FT /note="Spectrin 13" FT REPEAT 1779..1874 FT /note="Spectrin 14" FT REPEAT 1877..1979 FT /note="Spectrin 15" FT REPEAT 1992..2101 FT /note="Spectrin 16" FT REPEAT 2104..2208 FT /note="Spectrin 17" FT REPEAT 2211..2318 FT /note="Spectrin 18" FT REPEAT 2319..2423 FT /note="Spectrin 19" FT REPEAT 2475..2577 FT /note="Spectrin 20" FT REPEAT 2580..2686 FT /note="Spectrin 21" FT REPEAT 2689..2802 FT /note="Spectrin 22" FT REPEAT 2808..2930 FT /note="Spectrin 23" FT REPEAT 2935..3040 FT /note="Spectrin 24" FT DOMAIN 3055..3088 FT /note="WW" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224" FT ZN_FING 3308..3364 FT /note="ZZ-type; degenerate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228" FT REGION 1..240 FT /note="Actin-binding" FT REGION 63..72 FT /note="ANK2- and ANK-3 binding" FT /evidence="ECO:0000250" FT REGION 1415..1913 FT /note="Interaction with SYNM" FT /evidence="ECO:0000250" FT REGION 3058..3408 FT /note="Interaction with SYNM" FT /evidence="ECO:0000250" FT REGION 3466..3518 FT /note="Binds to SNTB1" FT REGION 3528..3554 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 3603..3685 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 3603..3673 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 3313 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228" FT BINDING 3316 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228" FT BINDING 3337 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228" FT BINDING 3340 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228" FT MOD_RES 3483 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 3490 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 3500 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 3612 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 3613 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231" FT MOD_RES 3617 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 3623 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 3624 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 3666 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:24275569" FT VAR_SEQ 1..3068 FT /note="Missing (in isoform 12, isoform 13, isoform 14, FT isoform 15, isoform 16 and isoform 17)" FT /evidence="ECO:0000303|PubMed:1319059, FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:8541829" FT /id="VSP_017490" FT VAR_SEQ 1..2729 FT /note="Missing (in isoform 11)" FT /id="VSP_060276" FT VAR_SEQ 1..2460 FT /note="Missing (in isoform 6, isoform 7, isoform 8, isoform FT 9 and isoform 10)" FT /id="VSP_060275" FT VAR_SEQ 1..11 FT /note="MLWWEEVEDCY -> MED (in isoform 2)" FT /evidence="ECO:0000303|PubMed:2648158" FT /id="VSP_006809" FT VAR_SEQ 1..11 FT /note="MLWWEEVEDCY -> MSEVSSD (in isoform 3)" FT /id="VSP_060274" FT VAR_SEQ 1 FT /note="M -> MTEIILLIFFPAYFLN (in isoform 4)" FT /id="VSP_006806" FT VAR_SEQ 1 FT /note="M -> MSARKLRNLSYKK (in isoform 5)" FT /evidence="ECO:0000305" FT /id="VSP_006808" FT VAR_SEQ 2..1357 FT /note="Missing (in isoform 4 and isoform 5)" FT /id="VSP_006807" FT VAR_SEQ 2730..2739 FT /note="GVKELMKQWQ -> MLHRKTYHVK (in isoform 11)" FT /id="VSP_060277" FT VAR_SEQ 3069..3075 FT /note="KVPYYIN -> MREQLKG (in isoform 12, isoform 13, FT isoform 14, isoform 15, isoform 16 and isoform 17)" FT /evidence="ECO:0000303|PubMed:1319059, FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:8541829" FT /id="VSP_017491" FT VAR_SEQ 3409..3685 FT /note="Missing (in isoform 17)" FT /id="VSP_060278" FT VAR_SEQ 3409..3518 FT /note="Missing (in isoform 7, isoform 10 and isoform 16)" FT /id="VSP_046319" FT VAR_SEQ 3409..3421 FT /note="Missing (in isoform 9, isoform 13 and isoform 15)" FT /evidence="ECO:0000303|PubMed:1319059, FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:8541829" FT /id="VSP_017492" FT VAR_SEQ 3673..3685 FT /note="RNTPGKPMREDTM -> HNVGSLFHMADDLGRAMESLVSVMTDEEGAE (in FT isoform 8, isoform 9, isoform 10, isoform 14, isoform 15 FT and isoform 16)" FT /evidence="ECO:0000303|PubMed:1319059, FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:8541829" FT /id="VSP_017493" FT VARIANT 18 FT /note="K -> N (in CMD3B; decreased thermodynamic stability; FT accelerated unfolding, perturbed protein structure; no FT effect on anchoring function)" FT /evidence="ECO:0000269|PubMed:12359139, FT ECO:0000269|PubMed:25340340" FT /id="VAR_023537" FT VARIANT 32..62 FT /note="Missing (in BMD)" FT /id="VAR_005146" FT VARIANT 54 FT /note="L -> R (in DMD)" FT /evidence="ECO:0000269|PubMed:8401582" FT /id="VAR_005147" FT VARIANT 118 FT /note="W -> R (in a patient with Becker muscular FT dystrophy)" FT /evidence="ECO:0000269|PubMed:21396098" FT /id="VAR_065764" FT VARIANT 133 FT /note="Q -> P (in dbSNP:rs1800256)" FT /evidence="ECO:0000269|PubMed:2668885" FT /id="VAR_005148" FT VARIANT 165 FT /note="D -> V (in one patient with Becker muscular FT dystrophy)" FT /evidence="ECO:0000269|PubMed:12632325" FT /id="VAR_023538" FT VARIANT 168 FT /note="A -> D (in BMD)" FT /id="VAR_005149" FT VARIANT 171 FT /note="A -> P (in BMD)" FT /evidence="ECO:0000269|PubMed:10573008" FT /id="VAR_023539" FT VARIANT 231 FT /note="Y -> N (in BMD)" FT /id="VAR_005150" FT VARIANT 279 FT /note="T -> A (in CMD3B)" FT /evidence="ECO:0000269|PubMed:9170407" FT /id="VAR_023540" FT VARIANT 334 FT /note="L -> F (in a colorectal cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_036353" FT VARIANT 365 FT /note="Q -> H (in dbSNP:rs1800266)" FT /evidence="ECO:0000269|PubMed:7849724" FT /id="VAR_005151" FT VARIANT 409 FT /note="T -> S (in dbSNP:rs34155804)" FT /id="VAR_057642" FT VARIANT 495..534 FT /note="Missing (in BMD)" FT /id="VAR_005152" FT VARIANT 573 FT /note="A -> V (in dbSNP:rs5972599)" FT /id="VAR_057643" FT VARIANT 623 FT /note="L -> I (in dbSNP:rs1800259)" FT /evidence="ECO:0000269|PubMed:2668885" FT /id="VAR_005153" FT VARIANT 645 FT /note="D -> G (in DMD)" FT /evidence="ECO:0000269|PubMed:7981690" FT /id="VAR_023541" FT VARIANT 666 FT /note="S -> L (in dbSNP:rs34563188)" FT /id="VAR_062110" FT VARIANT 715 FT /note="T -> S (in dbSNP:rs16998350)" FT /id="VAR_057644" FT VARIANT 773 FT /note="K -> E (in DMD)" FT /id="VAR_005154" FT VARIANT 784 FT /note="A -> G (in dbSNP:rs1800260)" FT /evidence="ECO:0000269|PubMed:2668885" FT /id="VAR_005155" FT VARIANT 882 FT /note="D -> G (in dbSNP:rs228406)" FT /evidence="ECO:0000269|PubMed:2668885, FT ECO:0000269|PubMed:3282674, ECO:0000269|PubMed:3428261" FT /id="VAR_005156" FT VARIANT 1136 FT /note="T -> S (in dbSNP:rs3827462)" FT /id="VAR_057645" FT VARIANT 1197 FT /note="V -> F (in dbSNP:rs1800262)" FT /evidence="ECO:0000269|PubMed:2668885" FT /id="VAR_005157" FT VARIANT 1219 FT /note="E -> Q (in a breast cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_036354" FT VARIANT 1245 FT /note="T -> I (in dbSNP:rs1800269)" FT /id="VAR_005158" FT VARIANT 1278 FT /note="A -> P (in dbSNP:rs1800270)" FT /id="VAR_005159" FT VARIANT 1377 FT /note="K -> N (in dbSNP:rs1800263)" FT /evidence="ECO:0000269|PubMed:2668885" FT /id="VAR_005160" FT VARIANT 1388 FT /note="F -> V (in dbSNP:rs28715870)" FT /id="VAR_057646" FT VARIANT 1469 FT /note="Q -> L (in dbSNP:rs1057872)" FT /evidence="ECO:0000269|PubMed:3282674" FT /id="VAR_005161" FT VARIANT 1470 FT /note="R -> H (in a breast cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_036355" FT VARIANT 1672 FT /note="N -> K (in dbSNP:rs16990264)" FT /evidence="ECO:0000269|PubMed:12354438" FT /id="VAR_023542" FT VARIANT 1745 FT /note="R -> H (in dbSNP:rs1801187)" FT /evidence="ECO:0000269|PubMed:2668885" FT /id="VAR_005162" FT VARIANT 1844 FT /note="R -> S (in dbSNP:rs1801186)" FT /evidence="ECO:0000269|PubMed:2668885" FT /id="VAR_005163" FT VARIANT 2108 FT /note="R -> C (in dbSNP:rs16990169)" FT /id="VAR_057647" FT VARIANT 2155 FT /note="R -> W (in dbSNP:rs1800273)" FT /evidence="ECO:0000269|PubMed:12359139" FT /id="VAR_005164" FT VARIANT 2164 FT /note="A -> V (in a colorectal cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_036356" FT VARIANT 2191 FT /note="R -> W" FT /evidence="ECO:0000269|PubMed:7849724" FT /id="VAR_005165" FT VARIANT 2299 FT /note="N -> T" FT /evidence="ECO:0000269|PubMed:12359139" FT /id="VAR_023543" FT VARIANT 2305..2366 FT /note="Missing (in DMD)" FT /id="VAR_005166" FT VARIANT 2366 FT /note="K -> Q (in dbSNP:rs1800275)" FT /evidence="ECO:0000269|PubMed:12359139, FT ECO:0000269|PubMed:3282674" FT /id="VAR_005167" FT VARIANT 2910 FT /note="E -> V (in dbSNP:rs41305353)" FT /evidence="ECO:0000269|PubMed:12359139" FT /id="VAR_005168" FT VARIANT 2912 FT /note="N -> D (in dbSNP:rs1800278)" FT /evidence="ECO:0000269|PubMed:12359139" FT /id="VAR_005169" FT VARIANT 2921 FT /note="H -> R (in BMD; dbSNP:rs1800279)" FT /id="VAR_005170" FT VARIANT 2937 FT /note="Q -> R (in dbSNP:rs1800280)" FT /evidence="ECO:0000269|PubMed:12359139, FT ECO:0000269|PubMed:15772651, ECO:0000269|PubMed:7849724" FT /id="VAR_005171" FT VARIANT 3228 FT /note="F -> L (in CMD3B)" FT /evidence="ECO:0000269|PubMed:12359139" FT /id="VAR_023544" FT VARIANT 3313 FT /note="C -> F (in DMD; results in highly reduced protein FT levels and expression at the sarcolemma)" FT /evidence="ECO:0000269|PubMed:12632325, FT ECO:0000269|PubMed:24302611" FT /id="VAR_023545" FT VARIANT 3335 FT /note="D -> H (in DMD; does not affect protein stability; FT does not affect protein expression at the sarcolemma; FT interaction with DAG1 is reduced)" FT /evidence="ECO:0000269|PubMed:24302611, FT ECO:0000269|PubMed:9851445" FT /id="VAR_023546" FT VARIANT 3340 FT /note="C -> Y (in DMD; results in highly reduced protein FT levels and expression at the sarcolemma)" FT /evidence="ECO:0000269|PubMed:24302611, FT ECO:0000269|PubMed:8817332" FT /id="VAR_023547" FT VARIANT 3421 FT /note="A -> V (in BMD)" FT /id="VAR_005172" FT CONFLICT 664 FT /note="Q -> QM (in Ref. 10; CAA29544)" FT /evidence="ECO:0000305" FT CONFLICT 2361 FT /note="G -> E (in Ref. 13; CAA38589)" FT /evidence="ECO:0000305" FT CONFLICT 3542 FT /note="P -> T (in Ref. 6; AAH70078)" FT /evidence="ECO:0000305" FT CONFLICT 3546 FT /note="M -> V (in Ref. 6; AAH70078)" FT /evidence="ECO:0000305" FT HELIX 14..31 FT /evidence="ECO:0007829|PDB:1DXX" FT TURN 40..46 FT /evidence="ECO:0007829|PDB:1DXX" FT HELIX 48..58 FT /evidence="ECO:0007829|PDB:1DXX" FT HELIX 70..86 FT /evidence="ECO:0007829|PDB:1DXX" FT HELIX 96..100 FT /evidence="ECO:0007829|PDB:1DXX" FT HELIX 104..118 FT /evidence="ECO:0007829|PDB:1DXX" FT TURN 119..121 FT /evidence="ECO:0007829|PDB:1DXX" FT HELIX 122..131 FT /evidence="ECO:0007829|PDB:1DXX" FT HELIX 136..148 FT /evidence="ECO:0007829|PDB:1DXX" FT STRAND 158..160 FT /evidence="ECO:0007829|PDB:1DXX" FT HELIX 161..163 FT /evidence="ECO:0007829|PDB:1DXX" FT HELIX 167..176 FT /evidence="ECO:0007829|PDB:1DXX" FT HELIX 178..180 FT /evidence="ECO:0007829|PDB:1DXX" FT HELIX 183..187 FT /evidence="ECO:0007829|PDB:1DXX" FT HELIX 192..205 FT /evidence="ECO:0007829|PDB:1DXX" FT HELIX 215..218 FT /evidence="ECO:0007829|PDB:1DXX" FT STRAND 219..222 FT /evidence="ECO:0007829|PDB:1DXX" FT HELIX 225..236 FT /evidence="ECO:0007829|PDB:1DXX" FT STRAND 243..245 FT /evidence="ECO:0007829|PDB:1DXX" FT HELIX 339..365 FT /evidence="ECO:0007829|PDB:3UUN" FT HELIX 372..409 FT /evidence="ECO:0007829|PDB:3UUN" FT HELIX 414..452 FT /evidence="ECO:0007829|PDB:3UUN" FT HELIX 3050..3054 FT /evidence="ECO:0007829|PDB:1EG3" FT STRAND 3061..3065 FT /evidence="ECO:0007829|PDB:1EG3" FT STRAND 3071..3075 FT /evidence="ECO:0007829|PDB:1EG3" FT TURN 3076..3079 FT /evidence="ECO:0007829|PDB:1EG3" FT STRAND 3080..3084 FT /evidence="ECO:0007829|PDB:1EG3" FT HELIX 3086..3094 FT /evidence="ECO:0007829|PDB:1EG3" FT HELIX 3095..3098 FT /evidence="ECO:0007829|PDB:1EG3" FT HELIX 3104..3118 FT /evidence="ECO:0007829|PDB:1EG3" FT HELIX 3121..3123 FT /evidence="ECO:0007829|PDB:1EG3" FT HELIX 3126..3135 FT /evidence="ECO:0007829|PDB:1EG3" FT STRAND 3143..3146 FT /evidence="ECO:0007829|PDB:1EG3" FT HELIX 3147..3164 FT /evidence="ECO:0007829|PDB:1EG3" FT STRAND 3165..3168 FT /evidence="ECO:0007829|PDB:1EG4" FT HELIX 3171..3186 FT /evidence="ECO:0007829|PDB:1EG3" FT STRAND 3192..3195 FT /evidence="ECO:0007829|PDB:1EG3" FT HELIX 3196..3205 FT /evidence="ECO:0007829|PDB:1EG3" FT STRAND 3207..3209 FT /evidence="ECO:0007829|PDB:1EG3" FT HELIX 3211..3222 FT /evidence="ECO:0007829|PDB:1EG3" FT HELIX 3231..3247 FT /evidence="ECO:0007829|PDB:1EG3" FT HELIX 3251..3254 FT /evidence="ECO:0007829|PDB:1EG3" FT HELIX 3260..3269 FT /evidence="ECO:0007829|PDB:1EG3" FT TURN 3270..3272 FT /evidence="ECO:0007829|PDB:1EG3" FT HELIX 3278..3286 FT /evidence="ECO:0007829|PDB:1EG3" FT TURN 3290..3293 FT /evidence="ECO:0007829|PDB:1EG3" FT HELIX 3294..3304 FT /evidence="ECO:0007829|PDB:1EG3" FT MOD_RES P11532-5:340 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES P11532-5:344 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES P11532-5:348 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES P11532-5:616 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES P11532-6:629 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES P11532-8:340 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES P11532-8:344 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES P11532-8:348 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES P11532-9:519 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:24275569" SQ 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 //