Dystrophin - wikipedia Dystrophin DMD Available structures PDB Ortholog search : PDBe RCSB List of PDB id codes 1DXX, 1EG3, 1EG4, 3UUN Identifiers Aliases DMD, BMD, CMD3B, DXS142, DXS164, DXS206, DXS230, DXS239, DXS268, DXS269, DXS270, DXS272, MRX85, dystrophin External IDs OMIM : 300377 MGI : 94909 HomoloGene : 20856 GeneCards : DMD Gene location ( Human ) Chr. X chromosome ( human ) Band Xp21. 2 - p21. 1 Start 31,097,677 bp End 33,339,441 bp Gene location ( Mouse ) Chr. X chromosome ( mouse ) Band X C1 X 38.38 cM Start 82,948,870 bp End 85,206,141 bp RNA expression pattern More reference expression data Gene ontology Molecular function nitric - oxide synthase binding dystroglycan binding vinculin binding myosin binding zinc ion binding metal ion binding protein binding actin binding structural constituent of muscle structural constituent of cytoskeleton Cellular component cytoplasm cytosol postsynaptic membrane lateral plasma membrane membrane filopodium cell - substrate junction plasma membrane synapse dystrophin - associated glycoprotein complex protein complex cell surface cell junction Z disc actin cytoskeleton membrane raft sarcolemma costamere syntrophin complex neuron projection terminus cytoskeleton nucleus filopodium membrane Biological process response to muscle stretch regulation of ryanodine - sensitive calcium - release channel activity cardiac muscle cell action potential regulation of voltage - gated calcium channel activity cardiac muscle contraction muscle cell cellular homeostasis negative regulation of peptidyl - cysteine S - nitrosylation regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion peptide biosynthetic process muscle organ development cellular protein complex assembly regulation of heart rate cellular protein localization muscle fiber development positive regulation of neuron differentiation negative regulation of peptidyl - serine phosphorylation positive regulation of neuron projection development muscle filament sliding positive regulation of sodium ion transmembrane transporter activity regulation of cellular response to growth factor stimulus regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum motile cilium assembly regulation of skeletal muscle contraction regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion cytoskeleton organization Sources : Amigo / QuickGO Orthologs Species Human Mouse Entrez 1756 13405 Ensembl ENSG00000198947 ENSMUSG00000045103 UniProt P11532 P11531 RefSeq ( mRNA ) NM_000109 NM_004006 NM_004007 NM_004009 NM_004010 NM_004011 NM_004012 NM_004013 NM_004014 NM_004015 NM_004016 NM_004017 NM_004018 NM_004019 NM_004020 NM_004021 NM_004022 NM_004023 NM_007868 NM_001314034 NM_001314035 NM_001314036 NM_001314037 NM_001314038 RefSeq ( protein ) NP_000100 NP_003997 NP_004000 NP_004001 NP_004002 NP_004003 NP_004004 NP_004005 NP_004006 NP_004007 NP_004008 NP_004009 NP_004010 NP_004011 NP_004012 NP_004013 NP_004014 NP_001300963 NP_001300964 NP_001300965 NP_001300966 NP_001300967 NP_031894 Location ( UCSC ) Chr X : 31.1 -- 33.34 Mb Chr X : 82.95 -- 85.21 Mb PubMed search Wikidata View / Edit Human View / Edit Mouse In human, the DMD gene is located on the short ( p ) arm of the X chromosome between positions 21.2 and 21.1 Dystrophin is a rod - shaped cytoplasmic protein, and a vital part of a protein complex that connects the cytoskeleton of a muscle fiber to the surrounding extracellular matrix through the cell membrane. This complex is variously known as the costamere or the dystrophin - associated protein complex. Many muscle proteins, such as α - dystrobrevin, syncoilin, synemin, sarcoglycan, dystroglycan, and sarcospan, colocalize with dystrophin at the costamere. The DMD gene, encoding the dystrophin protein, is one of the longest human genes known, covering 2.3 megabases ( 0.08 % of the human genome ) at locus Xp21. The primary transcript in muscle measures about 2,100 kilobases and takes 16 hours to transcribe ; the mature mRNA measures 14.0 kilobases. The 79 - exon muscle transcript codes for a protein of 3685 amino acid residues. Contents 1 Function 2 Pathology 3 Interactions 4 Neanderthal admixture 5 References 5.1 Other sources 6 Further reading 7 External links Function Dystrophin is a protein located between the sarcolemma and the outermost layer of myofilaments in the muscle fiber ( myofiber ). It is a cohesive protein, linking actin filaments to another support protein that resides on the inside surface of each muscle fiber 's plasma membrane ( sarcolemma ). This support protein on the inside surface of the sarcolemma in turn links to two other consecutive proteins for a total of three linking proteins. The final linking protein is attached to the fibrous endomysium of the entire muscle fiber. Dystrophin supports muscle fiber strength, and the absence of dystrophin reduces muscle stiffness, increases sarcolemmal deformability, and compromises the mechanical stability of costameres and their connections to nearby myofibrils ; as shown in recent studies where biomechanical properties of the sarcolemma and its links through costameres to the contractile apparatus were measured, and helps to prevent muscle fiber injury. Movement of thin filaments ( actin ) creates a pulling force on the extracellular connective tissue that eventually becomes the tendon of the muscle. Pathology Dystrophin deficiency has been definitively established as one of the root causes of the general class of myopathies collectively referred to as muscular dystrophy. The large cytosolic protein was first identified in 1987 by Louis M. Kunkel, after the 1986 discovery of the mutated gene that causes Duchenne muscular dystrophy ( DMD ). Normal skeletal muscle tissue contains only small amounts of dystrophin ( about 0.002 % of total muscle protein ), but its absence ( or abnormal expression ) leads to the development of a severe and currently incurable constellation of symptoms most readily characterized by several aberrant intracellular signaling pathways that ultimately yield pronounced myofiber necrosis as well as progressive muscle weakness and fatigability. Most DMD patients become wheelchair - dependent early in life, and the gradual development of cardiac hypertrophy -- a result of severe myocardial fibrosis -- typically results in premature death in the first two or three decades of life. Variants ( mutations ) in the DMD gene that lead to the production of too little or a defective, internally shortened but partially functional dystrophin protein, result in a display of a much milder dystrophic phenotype in affected patients, resulting in the disease known as Becker 's muscular dystrophy ( BMD ). In some cases the patient 's phenotype is such that experts may decide differently on whether a patient should be diagnosed with DMD or BMD. The theory currently most commonly used to predict whether a variant will result in a DMD or BMD phenotype, is the reading frame rule. Though its role in airway smooth muscle is not well established, recent research indicates that dystrophin along with other subunits of dystrophin glycoprotein complex is associated with phenotype maturation. Interactions Dystrophin has been shown to interact with : DTNA, SNTA1, and SNTB1. Neanderthal admixture A variant of the DMD gene, which is on the X chromosome, named B006, appears to be an introgression from a Neanderthal - modern human mating. References ^ Jump up to : GRCh38 : Ensembl release 89 : ENSG00000198947 - Ensembl, May 2017 ^ Jump up to : GRCm38 : Ensembl release 89 : ENSMUSG00000045103 - Ensembl, May 2017 Jump up ^ `` Human PubMed Reference : ''. Jump up ^ `` Mouse PubMed Reference : ''. Jump up ^ Tennyson CN, Klamut HJ, Worton RG ( 1995 ). `` The human dystrophin gene requires 16 hours to be transcribed and is cotranscriptionally spliced ''. Nature Genetics. 9 ( 2 ) : 184 -- 90. doi : 10.1038 / ng0295 - 184. PMID 7719347. Jump up ^ NCBI Sequence Viewer v2. 0 Jump up ^ Strachan T and Read AP, 1999. Human molecular genetics, BIOS Scientific, New York, USA Jump up ^ NCBI Sequence Viewer v2. 0 Jump up ^ García - Pelagio KP, Bloch RJ, Ortega A, González - Serratos H ( 2011 ). `` Biomechanics of the sarcolemma and costameres in single skeletal muscle fibers from normal and dystrophin - null mice ''. J Muscle Res Cell Motil. 31 ( 5 -- 6 ) : 323 -- 336. doi : 10.1007 / s10974 - 011 - 9238 - 9. PMC 4326082. PMID 21312057. Jump up ^ Hoffman EP, Brown RH, Kunkel LM ( 1987 ). `` Dystrophin : the protein product of the Duchenne muscular dystrophy locus ''. Cell. 51 ( 6 ) : 919 -- 28. doi : 10.1016 / 0092 - 8674 ( 87 ) 90579 - 4. PMID 3319190. Jump up ^ Monaco AP, Neve RL, Colletti - Feener C, Bertelson CJ, Kurnit DM, Kunkel LM ( 1986 ). `` Isolation of candidate cDNAs for portions of the Duchenne muscular dystrophy gene ''. Nature. 323 ( 6089 ) : 646 -- 50. Bibcode : 1986Natur. 323... 646M. doi : 10.1038 / 323646a0. PMID 3773991. Jump up ^ Hoffman, EP ; Brown RH, Jr ; Kunkel, LM ( 24 December 1987 ). `` Dystrophin : the protein product of the Duchenne muscular dystrophy locus ''. Cell. 51 ( 6 ) : 919 -- 28. doi : 10.1016 / 0092 - 8674 ( 87 ) 90579 - 4. PMID 3319190. Jump up ^ Aartsma - Rus A, Van Deutekom JC, Fokkema IF, Van Ommen GJ, Den Dunnen JT ( 2006 ). `` Entries in the Leiden Duchenne muscular dystrophy mutation database : an overview of mutation types and paradoxical cases that confirm the reading - frame rule ''. Muscle Nerve. 34 ( 2 ) : 135 -- 44. doi : 10.1002 / mus. 20586. PMID 16770791. Jump up ^ Sharma P, Tran T, Stelmack GL, McNeill K, Gosens R, Mutawe MM, Unruh H, Gerthoffer WT, Halayko AJ ( 2008 ). `` Expression of the dystrophin - glycoprotein complex is a marker for human airway smooth muscle phenotype maturation ''. Am. J. Physiol. Lung Cell Mol. Physiol. 294 ( 1 ) : L57 -- 68. doi : 10.1152 / ajplung. 00378.2007. PMID 17993586. Jump up ^ Sadoulet - Puccio HM, Rajala M, Kunkel LM ( 1997 ). `` Dystrobrevin and dystrophin : an interaction through coiled - coil motifs ''. Proc. Natl. Acad. Sci. U.S.A. 94 ( 23 ) : 12413 -- 8. Bibcode : 1997PNAS... 9412413S. doi : 10.1073 / pnas. 94.23. 12413. PMC 24974. PMID 9356463. Jump up ^ Ahn AH, Freener CA, Gussoni E, Yoshida M, Ozawa E, Kunkel LM ( 1996 ). `` 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 ( 5 ) : 2724 -- 30. doi : 10.1074 / jbc. 271.5. 2724. PMID 8576247. Jump up ^ Yang B, Jung D, Rafael JA, Chamberlain JS, Campbell KP ( 1995 ). `` Identification of alpha - syntrophin binding to syntrophin triplet, dystrophin, and utrophin ''. J. Biol. Chem. 270 ( 10 ) : 4975 -- 8. doi : 10.1074 / jbc. 270.10. 4975. PMID 7890602. Jump up ^ Gee SH, Madhavan R, Levinson SR, Caldwell JH, Sealock R, Froehner SC ( 1998 ). `` Interaction of muscle and brain sodium channels with multiple members of the syntrophin family of dystrophin - associated proteins ''. J. Neurosci. 18 ( 1 ) : 128 -- 37. PMID 9412493. Jump up ^ Ahn AH, Kunkel LM ( 1995 ). `` Syntrophin binds to an alternatively spliced exon of dystrophin ''. J. Cell Biol. 128 ( 3 ) : 363 -- 71. doi : 10.1083 / jcb. 128.3. 363. PMC 2120343. PMID 7844150. Jump up ^ Khan, Razib ( January 25, 2011 ). `` Neandertal admixture, revisiting results after shaken priors ''. Discover Magazine. Retrieved March 27, 2013. Other sources Saladin, Kenneth. Anatomy and Physiology : The Unity of Form and Function, 6th ed. McGraw - Hill. New York, 2012. `` DMD. '' Genetics Home Reference. U.S. National Library of Medicine, 2 Dec. 2012. Web. 09 Dec. 2012. Further reading Roberts RG, Gardner RJ, Bobrow M ( 1994 ). `` Searching for the 1 in 2,400,000 : a review of dystrophin gene point mutations ''. Hum. Mutat. 4 ( 1 ) : 1 -- 11. doi : 10.1002 / humu. 1380040102. PMID 7951253. Tinsley JM, Blake DJ, Zuellig RA, Davies KE ( 1994 ). `` Increasing complexity of the dystrophin - associated protein complex ''. Proc. Natl. Acad. Sci. U.S.A. 91 ( 18 ) : 8307 -- 13. Bibcode : 1994PNAS... 91.8307 T. doi : 10.1073 / pnas. 91.18. 8307. PMC 44595. PMID 8078878. Blake DJ, Weir A, Newey SE, Davies KE ( 2002 ). `` Function and genetics of dystrophin and dystrophin - related proteins in muscle ''. Physiol. Rev. 82 ( 2 ) : 291 -- 329. doi : 10.1152 / physrev. 00028.2001. PMID 11917091. Röper K, Gregory SL, Brown NH ( 2003 ). `` The ' spectraplakins ' : cytoskeletal giants with characteristics of both spectrin and plakin families ''. J. Cell Sci. 115 ( Pt 22 ) : 4215 -- 25. doi : 10.1242 / jcs. 00157. PMID 12376554. Muntoni F, Torelli S, Ferlini A ( 2003 ). `` Dystrophin and mutations : one gene, several proteins, multiple phenotypes ''. Lancet Neurology. 2 ( 12 ) : 731 -- 40. doi : 10.1016 / S1474 - 4422 ( 03 ) 00585 - 4. PMID 14636778. Haenggi T, Fritschy JM ( 2006 ). `` Role of dystrophin and utrophin for assembly and function of the dystrophin glycoprotein complex in non-muscle tissue ''. Cell. Mol. Life Sci. 63 ( 14 ) : 1614 -- 31. doi : 10.1007 / s00018 - 005 - 5461 - 0. PMID 16710609. External links GeneReviews / NCBI / NIH / UW entry on Dystrophinopathies Dystrophin at the US National Library of Medicine Medical Subject Headings ( MeSH ) LOVD mutation database : DMD, DMD ( whole exon changes ) PDB gallery 1dxx : N - TERMINAL ACTIN - BINDING DOMAIN OF HUMAN DYSTROPHIN 1eg3 : STRUCTURE OF A DYSTROPHIN WW DOMAIN FRAGMENT IN COMPLEX WITH A BETA - DYSTROGLYCAN PEPTIDE 1eg4 : STRUCTURE OF A DYSTROPHIN WW DOMAIN FRAGMENT IN COMPLEX WITH A BETA - DYSTROGLYCAN PEPTIDE Protein : cell membrane proteins ( other than Cell surface receptor, enzymes, and cytoskeleton ) Arrestin SAG ARRB1 ARRB2 ARR3 Membrane - spanning 4A MS4A1 MS4A2 MS4A3 MS4A4A MS4A4E MS4A5 MS4A6A MS4A6E MS4A7 MS4A8B MS4A9 MS4A10 MS4A12 MS4A13 MS4A14 MS4A15 MS4A18 Myelin Myelin basic protein PMP2 Myelin proteolipid protein PLP1 Myelin oligodendrocyte glycoprotein Myelin - associated glycoprotein Myelin protein zero Pulmonary surfactant Pulmonary surfactant - associated protein B Pulmonary surfactant - associated protein C Tetraspanin TSPAN1 TSPAN2 TSPAN3 TSPAN4 TSPAN5 TSPAN6 TSPAN7 TSPAN8 TSPAN9 TSPAN10 TSPAN11 TSPAN12 TSPAN13 TSPAN14 TSPAN15 TSPAN16 TSPAN17 TSPAN18 TSPAN19 TSPAN20 TSPAN21 TSPAN22 TSPAN23 TSPAN24 TSPAN25 TSPAN26 TSPAN27 TSPAN28 TSPAN29 TSPAN30 TSPAN31 TSPAN32 TSPAN33 TSPAN34 Other / ungrouped Calnexin LDL - receptor - related protein - associated protein Neurofibromin 2 Presenilin PSEN1 PSEN2 HFE Phospholipid transfer proteins Dysferlin STRC OTOF see also other cell membrane protein disorders Proteins of the cytoskeleton Human Microfilaments and ABPs Myofilament Actins A1 A2 C1 G1 G2 Myosins MYO1A MYO1B MYO1C MYO1D MYO1E MYO1F MYO1G MYO1H ) II MYH1 MYH2 MYH3 MYH4 MYH6 MYH7 MYH7B MYH8 MYH9 MYH10 MYH11 MYH13 MYH14 MYH15 MYH16 III MYO3A MYO3B V MYO5A MYO5B MYO5C VI MYO6 VII MYO7A MYO7B IX MYO9A MYO9B X MYO10 XV MYO15A XVIII MYO18A MYO18B LC MYL1 MYL2 MYL3 MYL4 MYL5 MYL6 MYL6B MYL7 MYL9 MYLIP MYLK MYLK2 MYLL1 Other Tropomodulin Troponin Tropomyosin Actinin Arp2 / 3 complex actin depolymerizing factors Cofilin Destrin Gelsolin Profilin Titin Other Wiskott - Aldrich syndrome protein Fibrillin Filamin FLNA FLNB FLNC Espin TRIOBP Intermediate filaments Type 1 / 2 ( Keratin, Cytokeratin ) Epithelial keratins ( soft alpha - keratins ) type I / chromosome 17 10 12 13 14 15 16 17 19 20 chromosome 12 18 none 21 type II / chromosome 12 2A 5 6A 6B 7 8 9 Hair keratins ( hard alpha - keratins ) type I / chromosome 17 31 32 33A 33B 34 35 36 37 38 type II / chromosome 12 81 82 83 84 85 86 Ungrouped alpha chromosome 17 23 24 25 26 27 28 39 40 chromosome 12 71 72 73 74 75 76 77 78 79 80 Not alpha Beta - keratin Type 3 Desmin GFAP Peripherin Vimentin Type 4 Internexin Nestin Neurofilament NEFL NEFM NEFH Synemin Syncoilin Type 5 Nuclear lamins : A / C B1 B2 Microtubules and MAPs Kinesins KIF1A KIF1B KIF2A KIF2C KIF3B KIF3C KIF4A KIF4B KIF5A KIF5B KIF5C KIF6 KIF7 KIF9 KIF11 KIF12 KIF13A KIF13B KIF14 KIF15 KIF16B KIF17 KIF18A KIF18B KIF19 KIF20A KIF20B KIF21A KIF21B KIF22 KIF23 KIF24 KIF25 KIF26A KIF26B KIF27 KIFC1 KIFC2 KIFC3 Dyneins axonemal : DNAH1 DNAH2 DNAH3 DNAH5 DNAH6 DNAH7 DNAH8 DNAH9 DNAH10 DNAH11 DNAH12 DNAH13 DNAH14 DNAH17 DNAI1 DNAI2 DNALI1 DNAL1 DNAL4 cytoplasmic : DYNC1H1 DYNC2H1 DYNC1I1 DYNC1I2 DYNC1LI1 DYNC1LI2 DYNC2LI1 DYNLL1 DYNLL2 DYNLRB1 DYNLRB2 DYNLT1 DYNLT3 Other Tau protein Dynactin DCTN1 Tubulins TUBA1A TUBA1B TUBA1C TUBA3C TUBA3D TUBA3E TUBA4A TUBA8 Stathmin Tektin TEKT1 TEKT2 TEKT3 TEKT4 TEKT5 Dynamin DNM1 DNM2 DNM3 Catenins Alpha catenin Beta catenin APC Plakoglobin ( gamma catenin ) Delta catenin GAN Membrane Dystrophin Dystroglycan Utrophin Ankyrin ANK1 ANK2 ANK3 Spectrin SPTA1 SPTAN1 SPTB SPTBN1 SPTBN2 SPTBN4 SPTBN5 Other Plakins Corneodesmosin Desmoplakin Dystonin Envoplakin MACF1 Periplakin Plectin Talin TLN1 Vinculin Plakophilin PKP1 PKP2 Nonhuman Major sperm proteins Prokaryotic cytoskeleton Crescentin FtsZ MreB See also : cytoskeletal defects Muscle tissue Smooth muscle Calmodulin Vascular smooth muscle Striated muscle Skeletal muscle Costamere / DAPC Membrane / extracellular DAP : Sarcoglycan SGCA SGCB SGCD SGCE SGCG SGCZ Dystroglycan Sarcospan Laminin, alpha 2 Intracellular Dystrophin Dystrobrevin Syntrophin B1 B2 G1 G2 Syncoilin Dysbindin Synemin / desmuslin related : NOS1 Caveolin 3 Sarcomere / ( a, i, and h bands ; z and m lines ) Myofilament thin filament / actin thick filament / myosin elastic filament / titin nebulin Tropomyosin Troponin Connective tissue Epimysium Fascicle Perimysium Endomysium Connective tissue in skeletal muscle General Neuromuscular junction Motor unit Muscle spindle Excitation -- contraction coupling Sliding filament mechanism Cardiac muscle Myocardium Intercalated disc Nebulette Both Fiber Muscle fiber intrafusal extrafusal Myofibril Microfilament / Myofilament Sarcomere Cells Myoblast / Myocyte Myosatellite cell Other Desmin Sarcoplasm Sarcolemma T - tubule Sarcoplasmic reticulum Other / ungrouped Myotilin Telethonin Dysferlin Fukutin Fukutin - related protein Retrieved from `` https://en.wikipedia.org/w/index.php?title=Dystrophin&oldid=809380402 '' Categories : Genes on human chromosome X Cytoskeleton Muscular dystrophy Cell adhesion proteins Talk Contents About Wikipedia Čeština Cymraeg Deutsch Español Français Galego Italiano עברית Nederlands 日本 語 Norsk Polski Português Русский Svenska Українська Edit links This page was last edited on 8 November 2017, at 19 : 08. 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Question: the dmd mutation is found where in the human genome
Answer: at locus Xp21