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P11532

- DMD_HUMAN

UniProt

P11532 - DMD_HUMAN

Protein

Dystrophin

Gene

DMD

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 188 (01 Oct 2014)
      Sequence version 3 (30 Nov 2010)
      Previous versions | rss
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    Functioni

    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.1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri3307 – 335448ZZ-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. actin binding Source: UniProtKB
    2. calcium ion binding Source: InterPro
    3. dystroglycan binding Source: UniProtKB
    4. myosin binding Source: BHF-UCL
    5. nitric-oxide synthase binding Source: BHF-UCL
    6. protein binding Source: IntAct
    7. structural constituent of cytoskeleton Source: ProtInc
    8. structural constituent of muscle Source: UniProtKB
    9. vinculin binding Source: BHF-UCL
    10. zinc ion binding Source: InterPro

    GO - Biological processi

    1. cardiac muscle cell action potential Source: BHF-UCL
    2. cardiac muscle contraction Source: BHF-UCL
    3. cellular protein complex assembly Source: BHF-UCL
    4. cellular protein localization Source: BHF-UCL
    5. extracellular matrix organization Source: Reactome
    6. motile cilium assembly Source: BHF-UCL
    7. muscle filament sliding Source: Reactome
    8. muscle organ development Source: ProtInc
    9. negative regulation of peptidyl-cysteine S-nitrosylation Source: BHF-UCL
    10. negative regulation of peptidyl-serine phosphorylation Source: BHF-UCL
    11. peptide biosynthetic process Source: UniProtKB
    12. positive regulation of neuron differentiation Source: BHF-UCL
    13. positive regulation of neuron projection development Source: BHF-UCL
    14. positive regulation of sodium ion transmembrane transporter activity Source: BHF-UCL
    15. regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion Source: BHF-UCL
    16. regulation of cellular response to growth factor stimulus Source: BHF-UCL
    17. regulation of heart rate Source: BHF-UCL
    18. regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum Source: BHF-UCL
    19. regulation of ryanodine-sensitive calcium-release channel activity Source: BHF-UCL
    20. regulation of skeletal muscle contraction Source: BHF-UCL
    21. regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion Source: BHF-UCL
    22. regulation of voltage-gated calcium channel activity Source: BHF-UCL

    Keywords - Ligandi

    Actin-binding, Calcium, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_163874. Non-integrin membrane-ECM interactions.
    REACT_16969. Striated Muscle Contraction.
    SignaLinkiP11532.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dystrophin
    Gene namesi
    Name:DMD
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:2928. DMD.

    Subcellular locationi

    Cell membranesarcolemma; Peripheral membrane protein; Cytoplasmic side. Cytoplasmcytoskeleton. Cell junctionsynapsepostsynaptic cell membrane By similarity
    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 the presence of ANK2 By similarity.By similarity

    GO - Cellular componenti

    1. cell junction Source: UniProtKB-KW
    2. cell surface Source: UniProtKB
    3. costamere Source: UniProtKB
    4. cytoskeleton Source: ProtInc
    5. cytosol Source: Reactome
    6. dystrophin-associated glycoprotein complex Source: UniProtKB
    7. filopodium Source: BHF-UCL
    8. filopodium membrane Source: BHF-UCL
    9. membrane raft Source: BHF-UCL
    10. nucleus Source: BHF-UCL
    11. plasma membrane Source: BHF-UCL
    12. postsynaptic membrane Source: UniProtKB-SubCell
    13. protein complex Source: MGI
    14. sarcolemma Source: BHF-UCL
    15. syntrophin complex Source: BHF-UCL

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Cytoplasm, Cytoskeleton, Membrane, Postsynaptic cell membrane, Synapse

    Pathology & Biotechi

    Involvement in diseasei

    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.5 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti54 – 541L → R in DMD. 1 Publication
    VAR_005147
    Natural varianti645 – 6451D → G in DMD. 1 Publication
    VAR_023541
    Natural varianti773 – 7731K → E in DMD.
    VAR_005154
    Natural varianti2305 – 236662Missing in DMD.
    VAR_005166Add
    BLAST
    Natural varianti3313 – 33131C → F in DMD; results in highly reduced protein levels and expression at the sarcolemma. 1 Publication
    VAR_023545
    Natural varianti3335 – 33351D → H in DMD; does not affect protein stability; does not affect protein expression at the sarcolemma; interaction with DAG1 is reduced. 1 Publication
    VAR_023546
    Natural varianti3340 – 33401C → Y in DMD; results in highly reduced protein levels and expression at the sarcolemma. 1 Publication
    VAR_023547
    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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti32 – 6231Missing in BMD.
    VAR_005146Add
    BLAST
    Natural varianti168 – 1681A → D in BMD.
    VAR_005149
    Natural varianti171 – 1711A → P in BMD. 1 Publication
    VAR_023539
    Natural varianti231 – 2311Y → N in BMD.
    VAR_005150
    Natural varianti495 – 53440Missing in BMD.
    VAR_005152Add
    BLAST
    Natural varianti2921 – 29211H → R in BMD.
    Corresponds to variant rs1800279 [ dbSNP | Ensembl ].
    VAR_005170
    Natural varianti3421 – 34211A → V in BMD.
    VAR_005172
    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.3 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti18 – 181K → N in CMD3B. 1 Publication
    VAR_023537
    Natural varianti279 – 2791T → A in CMD3B. 1 Publication
    VAR_023540
    Natural varianti1672 – 16721N → K in CMD3B. 1 Publication
    Corresponds to variant rs16990264 [ dbSNP | Ensembl ].
    VAR_023542
    Natural varianti3228 – 32281F → L in CMD3B. 1 Publication
    VAR_023544

    Keywords - Diseasei

    Cardiomyopathy, Disease mutation

    Organism-specific databases

    MIMi300376. phenotype.
    302045. phenotype.
    310200. phenotype.
    Orphaneti98895. Becker muscular dystrophy.
    98896. Duchenne muscular dystrophy.
    154. Familial isolated dilated cardiomyopathy.
    206546. Symptomatic form of muscular dystrophy of Duchenne and Becker in female carriers.
    PharmGKBiPA27378.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 36853685DystrophinPRO_0000076075Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei3483 – 34831Phosphoserine1 Publication
    Modified residuei3612 – 36121Phosphoserine1 Publication
    Modified residuei3613 – 36131Phosphoserine2 Publications
    Modified residuei3617 – 36171Phosphoserine1 Publication
    Modified residuei3623 – 36231Phosphoserine2 Publications
    Modified residuei3624 – 36241PhosphoserineBy similarity
    Modified residuei3666 – 36661Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP11532.
    PaxDbiP11532.
    PRIDEiP11532.

    PTM databases

    PhosphoSiteiP11532.

    Expressioni

    Tissue specificityi

    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.3 Publications

    Developmental stagei

    Isoform 5 is expressed in embryonic neural tissue from the sixth week of development. Isoform 9 is detected in all embryonic tissues examined.1 Publication

    Gene expression databases

    ArrayExpressiP11532.
    BgeeiP11532.
    CleanExiHS_DMD.
    GenevestigatoriP11532.

    Organism-specific databases

    HPAiCAB000119.
    HPA002725.
    HPA023885.

    Interactioni

    Subunit structurei

    Interacts with SYNM By similarity. Interacts with the syntrophins SNTA1, SNTB1, SNTB2, SNTG1 and SNTG2. Interacts with KRT19. 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. 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.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ANK2Q014842EBI-1018651,EBI-941975
    Ank3Q3T1J52EBI-1018651,EBI-2133962From a different organism.
    KRT19P087272EBI-295827,EBI-742756
    SNTB1Q138843EBI-295827,EBI-295843

    Protein-protein interaction databases

    BioGridi108096. 28 interactions.
    IntActiP11532. 14 interactions.
    MINTiMINT-109755.
    STRINGi9606.ENSP00000354923.

    Structurei

    Secondary structure

    1
    3685
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi14 – 3118
    Turni40 – 467
    Helixi48 – 5811
    Helixi70 – 8617
    Helixi96 – 1005
    Helixi104 – 11815
    Turni119 – 1213
    Helixi122 – 13110
    Helixi136 – 14813
    Beta strandi158 – 1603
    Helixi161 – 1633
    Helixi167 – 17610
    Helixi178 – 1803
    Helixi183 – 1875
    Helixi192 – 20514
    Helixi215 – 2184
    Beta strandi219 – 2224
    Helixi225 – 23612
    Beta strandi243 – 2453
    Helixi339 – 36527
    Helixi372 – 40938
    Helixi414 – 45239
    Helixi3050 – 30545
    Beta strandi3061 – 30655
    Beta strandi3071 – 30755
    Turni3076 – 30794
    Beta strandi3080 – 30845
    Helixi3086 – 30949
    Helixi3095 – 30984
    Helixi3104 – 311815
    Helixi3121 – 31233
    Helixi3126 – 313510
    Beta strandi3143 – 31464
    Helixi3147 – 316418
    Beta strandi3165 – 31684
    Helixi3171 – 318616
    Beta strandi3192 – 31954
    Helixi3196 – 320510
    Beta strandi3207 – 32093
    Helixi3211 – 322212
    Helixi3231 – 324717
    Helixi3251 – 32544
    Helixi3260 – 326910
    Turni3270 – 32723
    Helixi3278 – 32869
    Turni3290 – 32934
    Helixi3294 – 330411

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1DXXX-ray2.60A/B/C/D1-246[»]
    1EG3X-ray2.00A3046-3306[»]
    1EG4X-ray2.00A3046-3306[»]
    3UUNX-ray2.30A/B338-456[»]
    ProteinModelPortaliP11532.
    SMRiP11532. Positions 9-246, 338-453, 3047-3306.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP11532.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 240240Actin-bindingAdd
    BLAST
    Domaini15 – 119105CH 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini134 – 237104CH 2PROSITE-ProRule annotationAdd
    BLAST
    Repeati339 – 447109Spectrin 1Add
    BLAST
    Repeati448 – 556109Spectrin 2Add
    BLAST
    Repeati559 – 667109Spectrin 3Add
    BLAST
    Repeati719 – 828110Spectrin 4Add
    BLAST
    Repeati830 – 934105Spectrin 5Add
    BLAST
    Repeati943 – 1045103Spectrin 6Add
    BLAST
    Repeati1048 – 1154107Spectrin 7Add
    BLAST
    Repeati1157 – 1263107Spectrin 8Add
    BLAST
    Repeati1266 – 1367102Spectrin 9Add
    BLAST
    Repeati1368 – 146396Spectrin 10Add
    BLAST
    Repeati1468 – 1568101Spectrin 11Add
    BLAST
    Repeati1571 – 1676106Spectrin 12Add
    BLAST
    Repeati1679 – 1778100Spectrin 13Add
    BLAST
    Repeati1779 – 187496Spectrin 14Add
    BLAST
    Repeati1877 – 1979103Spectrin 15Add
    BLAST
    Repeati1992 – 2101110Spectrin 16Add
    BLAST
    Repeati2104 – 2208105Spectrin 17Add
    BLAST
    Repeati2211 – 2318108Spectrin 18Add
    BLAST
    Repeati2319 – 2423105Spectrin 19Add
    BLAST
    Repeati2475 – 2577103Spectrin 20Add
    BLAST
    Repeati2580 – 2686107Spectrin 21Add
    BLAST
    Repeati2689 – 2802114Spectrin 22Add
    BLAST
    Repeati2808 – 2930123Spectrin 23Add
    BLAST
    Repeati2935 – 3040106Spectrin 24Add
    BLAST
    Domaini3055 – 308834WWPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni63 – 7210ANK2- and ANK-3 bindingBy similarity
    Regioni1415 – 1913499Interaction with SYNMBy similarityAdd
    BLAST
    Regioni3058 – 3408351Interaction with SYNMBy similarityAdd
    BLAST
    Regioni3466 – 351853Binds to SNTB1Add
    BLAST

    Sequence similaritiesi

    Contains 2 CH (calponin-homology) domains.PROSITE-ProRule annotation
    Contains 24 spectrin repeats.Curated
    Contains 1 WW domain.PROSITE-ProRule annotation
    Contains 1 ZZ-type zinc finger.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri3307 – 335448ZZ-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG5069.
    HOGENOMiHOG000231175.
    HOVERGENiHBG005495.
    InParanoidiP11532.
    KOiK10366.
    OrthoDBiEOG7V765N.
    PhylomeDBiP11532.
    TreeFamiTF320178.

    Family and domain databases

    Gene3Di1.10.238.10. 2 hits.
    1.10.418.10. 2 hits.
    InterProiIPR001589. Actinin_actin-bd_CS.
    IPR001715. CH-domain.
    IPR016344. Dystrophin/utrophin.
    IPR011992. EF-hand-dom_pair.
    IPR015153. EF-hand_dom_typ1.
    IPR015154. EF-hand_dom_typ2.
    IPR018159. Spectrin/alpha-actinin.
    IPR002017. Spectrin_repeat.
    IPR001202. WW_dom.
    IPR000433. Znf_ZZ.
    [Graphical view]
    PfamiPF00307. CH. 2 hits.
    PF09068. EF-hand_2. 1 hit.
    PF09069. EF-hand_3. 1 hit.
    PF00435. Spectrin. 17 hits.
    PF00397. WW. 1 hit.
    PF00569. ZZ. 1 hit.
    [Graphical view]
    PIRSFiPIRSF002341. Dystrophin/utrophin. 1 hit.
    SMARTiSM00033. CH. 2 hits.
    SM00150. SPEC. 22 hits.
    SM00456. WW. 1 hit.
    SM00291. ZnF_ZZ. 1 hit.
    [Graphical view]
    SUPFAMiSSF47576. SSF47576. 1 hit.
    SSF51045. SSF51045. 1 hit.
    PROSITEiPS00019. ACTININ_1. 1 hit.
    PS00020. ACTININ_2. 1 hit.
    PS50021. CH. 2 hits.
    PS01159. WW_DOMAIN_1. 1 hit.
    PS50020. WW_DOMAIN_2. 1 hit.
    PS01357. ZF_ZZ_1. 1 hit.
    PS50135. ZF_ZZ_2. 1 hit.
    [Graphical view]

    Sequences (10)i

    Sequence statusi: Complete.

    This entry describes 10 isoformsi produced by alternative splicing. Align

    Note: Additional isoforms seem to exist.

    Isoform 4 (identifier: P11532-1) [UniParc]FASTAAdd to Basket

    Also known as: Dystrophin-4

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MLWWEEVEDC YEREDVQKKT FTKWVNAQFS KFGKQHIENL FSDLQDGRRL     50
    LDLLEGLTGQ KLPKEKGSTR VHALNNVNKA LRVLQNNNVD LVNIGSTDIV 100
    DGNHKLTLGL IWNIILHWQV KNVMKNIMAG LQQTNSEKIL LSWVRQSTRN 150
    YPQVNVINFT TSWSDGLALN ALIHSHRPDL FDWNSVVCQQ SATQRLEHAF 200
    NIARYQLGIE KLLDPEDVDT TYPDKKSILM YITSLFQVLP QQVSIEAIQE 250
    VEMLPRPPKV TKEEHFQLHH QMHYSQQITV SLAQGYERTS SPKPRFKSYA 300
    YTQAAYVTTS DPTRSPFPSQ HLEAPEDKSF GSSLMESEVN LDRYQTALEE 350
    VLSWLLSAED TLQAQGEISN DVEVVKDQFH THEGYMMDLT AHQGRVGNIL 400
    QLGSKLIGTG KLSEDEETEV QEQMNLLNSR WECLRVASME KQSNLHRVLM 450
    DLQNQKLKEL NDWLTKTEER TRKMEEEPLG PDLEDLKRQV QQHKVLQEDL 500
    EQEQVRVNSL THMVVVVDES SGDHATAALE EQLKVLGDRW ANICRWTEDR 550
    WVLLQDILLK WQRLTEEQCL FSAWLSEKED AVNKIHTTGF KDQNEMLSSL 600
    QKLAVLKADL EKKKQSMGKL YSLKQDLLST LKNKSVTQKT EAWLDNFARC 650
    WDNLVQKLEK STAQISQAVT TTQPSLTQTT VMETVTTVTT REQILVKHAQ 700
    EELPPPPPQK KRQITVDSEI RKRLDVDITE LHSWITRSEA VLQSPEFAIF 750
    RKEGNFSDLK EKVNAIEREK AEKFRKLQDA SRSAQALVEQ MVNEGVNADS 800
    IKQASEQLNS RWIEFCQLLS ERLNWLEYQN NIIAFYNQLQ QLEQMTTTAE 850
    NWLKIQPTTP SEPTAIKSQL KICKDEVNRL SDLQPQIERL KIQSIALKEK 900
    GQGPMFLDAD FVAFTNHFKQ VFSDVQAREK ELQTIFDTLP PMRYQETMSA 950
    IRTWVQQSET KLSIPQLSVT DYEIMEQRLG ELQALQSSLQ EQQSGLYYLS 1000
    TTVKEMSKKA PSEISRKYQS EFEEIEGRWK KLSSQLVEHC QKLEEQMNKL 1050
    RKIQNHIQTL KKWMAEVDVF LKEEWPALGD SEILKKQLKQ CRLLVSDIQT 1100
    IQPSLNSVNE GGQKIKNEAE PEFASRLETE LKELNTQWDH MCQQVYARKE 1150
    ALKGGLEKTV SLQKDLSEMH EWMTQAEEEY LERDFEYKTP DELQKAVEEM 1200
    KRAKEEAQQK EAKVKLLTES VNSVIAQAPP VAQEALKKEL ETLTTNYQWL 1250
    CTRLNGKCKT LEEVWACWHE LLSYLEKANK WLNEVEFKLK TTENIPGGAE 1300
    EISEVLDSLE NLMRHSEDNP NQIRILAQTL TDGGVMDELI NEELETFNSR 1350
    WRELHEEAVR RQKLLEQSIQ SAQETEKSLH LIQESLTFID KQLAAYIADK 1400
    VDAAQMPQEA QKIQSDLTSH EISLEEMKKH NQGKEAAQRV LSQIDVAQKK 1450
    LQDVSMKFRL FQKPANFEQR LQESKMILDE VKMHLPALET KSVEQEVVQS 1500
    QLNHCVNLYK SLSEVKSEVE MVIKTGRQIV QKKQTENPKE LDERVTALKL 1550
    HYNELGAKVT ERKQQLEKCL KLSRKMRKEM NVLTEWLAAT DMELTKRSAV 1600
    EGMPSNLDSE VAWGKATQKE IEKQKVHLKS ITEVGEALKT VLGKKETLVE 1650
    DKLSLLNSNW IAVTSRAEEW LNLLLEYQKH METFDQNVDH ITKWIIQADT 1700
    LLDESEKKKP QQKEDVLKRL KAELNDIRPK VDSTRDQAAN LMANRGDHCR 1750
    KLVEPQISEL NHRFAAISHR IKTGKASIPL KELEQFNSDI QKLLEPLEAE 1800
    IQQGVNLKEE DFNKDMNEDN EGTVKELLQR GDNLQQRITD ERKREEIKIK 1850
    QQLLQTKHNA LKDLRSQRRK KALEISHQWY QYKRQADDLL KCLDDIEKKL 1900
    ASLPEPRDER KIKEIDRELQ KKKEELNAVR RQAEGLSEDG AAMAVEPTQI 1950
    QLSKRWREIE SKFAQFRRLN FAQIHTVREE TMMVMTEDMP LEISYVPSTY 2000
    LTEITHVSQA LLEVEQLLNA PDLCAKDFED LFKQEESLKN IKDSLQQSSG 2050
    RIDIIHSKKT AALQSATPVE RVKLQEALSQ LDFQWEKVNK MYKDRQGRFD 2100
    RSVEKWRRFH YDIKIFNQWL TEAEQFLRKT QIPENWEHAK YKWYLKELQD 2150
    GIGQRQTVVR TLNATGEEII QQSSKTDASI LQEKLGSLNL RWQEVCKQLS 2200
    DRKKRLEEQK NILSEFQRDL NEFVLWLEEA DNIASIPLEP GKEQQLKEKL 2250
    EQVKLLVEEL PLRQGILKQL NETGGPVLVS APISPEEQDK LENKLKQTNL 2300
    QWIKVSRALP EKQGEIEAQI KDLGQLEKKL EDLEEQLNHL LLWLSPIRNQ 2350
    LEIYNQPNQE GPFDVKETEI AVQAKQPDVE EILSKGQHLY KEKPATQPVK 2400
    RKLEDLSSEW KAVNRLLQEL RAKQPDLAPG LTTIGASPTQ TVTLVTQPVV 2450
    TKETAISKLE MPSSLMLEVP ALADFNRAWT ELTDWLSLLD QVIKSQRVMV 2500
    GDLEDINEMI IKQKATMQDL EQRRPQLEEL ITAAQNLKNK TSNQEARTII 2550
    TDRIERIQNQ WDEVQEHLQN RRQQLNEMLK DSTQWLEAKE EAEQVLGQAR 2600
    AKLESWKEGP YTVDAIQKKI TETKQLAKDL RQWQTNVDVA NDLALKLLRD 2650
    YSADDTRKVH MITENINASW RSIHKRVSER EAALEETHRL LQQFPLDLEK 2700
    FLAWLTEAET TANVLQDATR KERLLEDSKG VKELMKQWQD LQGEIEAHTD 2750
    VYHNLDENSQ KILRSLEGSD DAVLLQRRLD NMNFKWSELR KKSLNIRSHL 2800
    EASSDQWKRL HLSLQELLVW LQLKDDELSR QAPIGGDFPA VQKQNDVHRA 2850
    FKRELKTKEP VIMSTLETVR IFLTEQPLEG LEKLYQEPRE LPPEERAQNV 2900
    TRLLRKQAEE VNTEWEKLNL HSADWQRKID ETLERLQELQ EATDELDLKL 2950
    RQAEVIKGSW QPVGDLLIDS LQDHLEKVKA LRGEIAPLKE NVSHVNDLAR 3000
    QLTTLGIQLS PYNLSTLEDL NTRWKLLQVA VEDRVRQLHE AHRDFGPASQ 3050
    HFLSTSVQGP WERAISPNKV PYYINHETQT TCWDHPKMTE LYQSLADLNN 3100
    VRFSAYRTAM KLRRLQKALC LDLLSLSAAC DALDQHNLKQ NDQPMDILQI 3150
    INCLTTIYDR LEQEHNNLVN VPLCVDMCLN WLLNVYDTGR TGRIRVLSFK 3200
    TGIISLCKAH LEDKYRYLFK QVASSTGFCD QRRLGLLLHD SIQIPRQLGE 3250
    VASFGGSNIE PSVRSCFQFA NNKPEIEAAL FLDWMRLEPQ SMVWLPVLHR 3300
    VAAAETAKHQ AKCNICKECP IIGFRYRSLK HFNYDICQSC FFSGRVAKGH 3350
    KMHYPMVEYC TPTTSGEDVR DFAKVLKNKF RTKRYFAKHP RMGYLPVQTV 3400
    LEGDNMETPV TLINFWPVDS APASSPQLSH DDTHSRIEHY ASRLAEMENS 3450
    NGSYLNDSIS PNESIDDEHL LIQHYCQSLN QDSPLSQPRS PAQILISLES 3500
    EERGELERIL ADLEEENRNL QAEYDRLKQQ HEHKGLSPLP SPPEMMPTSP 3550
    QSPRDAELIA EAKLLRQHKG RLEARMQILE DHNKQLESQL HRLRQLLEQP 3600
    QAEAKVNGTT VSSPSTSLQR SDSSQPMLLR VVGSQTSDSM GEEDLLSPPQ 3650
    DTSTGLEEVM EQLNNSFPSS RGRNTPGKPM REDTM 3685
    Length:3,685
    Mass (Da):426,750
    Last modified:November 30, 2010 - v3
    Checksum:i24FF7E83F1E6BF8D
    GO
    Isoform 1 (identifier: P11532-2) [UniParc]FASTAAdd to Basket

    Also known as: Dystrophin-1

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MTEIILLIFFPAYFLN
         2-1357: Missing.

    Show »
    Length:2,344
    Mass (Da):271,391
    Checksum:i50AF557D10DD0B23
    GO
    Isoform 2 (identifier: P11532-3) [UniParc]FASTAAdd to Basket

    Also known as: Dystrophin-2

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MSARKLRNLSYKK
         2-1357: Missing.

    Show »
    Length:2,341
    Mass (Da):271,040
    Checksum:i5A695D20AE07D801
    GO
    Isoform 3 (identifier: P11532-4) [UniParc]FASTAAdd to Basket

    Also known as: Dystrophin-3

    The sequence of this isoform differs from the canonical sequence as follows:
         1-11: MLWWEEVEDCY → MED

    Show »
    Length:3,677
    Mass (Da):425,640
    Checksum:i234A6D63F4910420
    GO
    Isoform 5 (identifier: P11532-5) [UniParc]FASTAAdd to Basket

    Also known as: Dp71ab

    The sequence of this isoform differs from the canonical sequence as follows:
         1-3068: Missing.
         3069-3075: KVPYYIN → MREQLKG
         3409-3421: Missing.
         3673-3685: RNTPGKPMREDTM → HNVGSLFHMADDLGRAMESLVSVMTDEEGAE

    Note: Contains a phosphothreonine at position 340. Contains a phosphoserine at position 348. Contains a phosphoserine at position 344.

    Show »
    Length:622
    Mass (Da):70,750
    Checksum:i75D44165427FAB8B
    GO
    Isoform 6 (identifier: P11532-6) [UniParc]FASTAAdd to Basket

    Also known as: Dp71b

    The sequence of this isoform differs from the canonical sequence as follows:
         1-3068: Missing.
         3069-3075: KVPYYIN → MREQLKG
         3673-3685: RNTPGKPMREDTM → HNVGSLFHMADDLGRAMESLVSVMTDEEGAE

    Note: No experimental confirmation available.

    Show »
    Length:635
    Mass (Da):72,191
    Checksum:i5EB1E49C45CF34EC
    GO
    Isoform 7 (identifier: P11532-7) [UniParc]FASTAAdd to Basket

    Also known as: Dp71

    The sequence of this isoform differs from the canonical sequence as follows:
         1-3068: Missing.
         3069-3075: KVPYYIN → MREQLKG

    Show »
    Length:617
    Mass (Da):70,375
    Checksum:i660C9D904AF403B9
    GO
    Isoform 8 (identifier: P11532-8) [UniParc]FASTAAdd to Basket

    Also known as: Dp71a

    The sequence of this isoform differs from the canonical sequence as follows:
         1-3068: Missing.
         3069-3075: KVPYYIN → MREQLKG
         3409-3421: Missing.

    Note: No experimental confirmation available. Contains a phosphothreonine at position 340. Contains a phosphoserine at position 348. Contains a phosphoserine at position 344.

    Show »
    Length:604
    Mass (Da):68,934
    Checksum:i08BDA0A428FAA9F4
    GO
    Isoform 9 (identifier: P11532-9) [UniParc]FASTAAdd to Basket

    Also known as: Dp60, Dp71delta110

    The sequence of this isoform differs from the canonical sequence as follows:
         1-3068: Missing.
         3069-3075: KVPYYIN → MREQLKG
         3409-3518: Missing.
         3673-3685: RNTPGKPMREDTM → HNVGSLFHMADDLGRAMESLVSVMTDEEGAE

    Show »
    Length:525
    Mass (Da):59,769
    Checksum:iD597517BCE4D9FD1
    GO
    Isoform 10 (identifier: P11532-10) [UniParc]FASTAAdd to Basket

    Also known as: Dp71c

    The sequence of this isoform differs from the canonical sequence as follows:
         1-3068: Missing.
         3069-3075: KVPYYIN → MREQLKG
         3409-3518: Missing.

    Show »
    Length:507
    Mass (Da):57,953
    Checksum:i3F4518D23592BF1D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti664 – 6641Q → QM in CAA29544. (PubMed:3428261)Curated
    Sequence conflicti2361 – 23611G → E in CAA38589. 1 PublicationCurated
    Sequence conflicti3542 – 35421P → T in AAH70078. (PubMed:15489334)Curated
    Sequence conflicti3546 – 35461M → V in AAH70078. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti18 – 181K → N in CMD3B. 1 Publication
    VAR_023537
    Natural varianti32 – 6231Missing in BMD.
    VAR_005146Add
    BLAST
    Natural varianti54 – 541L → R in DMD. 1 Publication
    VAR_005147
    Natural varianti118 – 1181W → R in a patient with Becker muscular dystrophy. 1 Publication
    VAR_065764
    Natural varianti133 – 1331Q → P.1 Publication
    Corresponds to variant rs1800256 [ dbSNP | Ensembl ].
    VAR_005148
    Natural varianti165 – 1651D → V in one patient with Becker muscular dystrophy. 1 Publication
    VAR_023538
    Natural varianti168 – 1681A → D in BMD.
    VAR_005149
    Natural varianti171 – 1711A → P in BMD. 1 Publication
    VAR_023539
    Natural varianti231 – 2311Y → N in BMD.
    VAR_005150
    Natural varianti279 – 2791T → A in CMD3B. 1 Publication
    VAR_023540
    Natural varianti334 – 3341L → F in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_036353
    Natural varianti365 – 3651Q → H.1 Publication
    Corresponds to variant rs1800266 [ dbSNP | Ensembl ].
    VAR_005151
    Natural varianti409 – 4091T → S.
    Corresponds to variant rs34155804 [ dbSNP | Ensembl ].
    VAR_057642
    Natural varianti495 – 53440Missing in BMD.
    VAR_005152Add
    BLAST
    Natural varianti573 – 5731A → V.
    Corresponds to variant rs5972599 [ dbSNP | Ensembl ].
    VAR_057643
    Natural varianti623 – 6231L → I.1 Publication
    Corresponds to variant rs1800259 [ dbSNP | Ensembl ].
    VAR_005153
    Natural varianti645 – 6451D → G in DMD. 1 Publication
    VAR_023541
    Natural varianti666 – 6661S → L.
    Corresponds to variant rs34563188 [ dbSNP | Ensembl ].
    VAR_062110
    Natural varianti715 – 7151T → S.
    Corresponds to variant rs16998350 [ dbSNP | Ensembl ].
    VAR_057644
    Natural varianti773 – 7731K → E in DMD.
    VAR_005154
    Natural varianti784 – 7841A → G.1 Publication
    Corresponds to variant rs1800260 [ dbSNP | Ensembl ].
    VAR_005155
    Natural varianti882 – 8821D → G.3 Publications
    Corresponds to variant rs228406 [ dbSNP | Ensembl ].
    VAR_005156
    Natural varianti1136 – 11361T → S.
    Corresponds to variant rs3827462 [ dbSNP | Ensembl ].
    VAR_057645
    Natural varianti1197 – 11971V → F.1 Publication
    Corresponds to variant rs1800262 [ dbSNP | Ensembl ].
    VAR_005157
    Natural varianti1219 – 12191E → Q in a breast cancer sample; somatic mutation. 1 Publication
    VAR_036354
    Natural varianti1245 – 12451T → I.
    Corresponds to variant rs1800269 [ dbSNP | Ensembl ].
    VAR_005158
    Natural varianti1278 – 12781A → P.
    Corresponds to variant rs1800270 [ dbSNP | Ensembl ].
    VAR_005159
    Natural varianti1377 – 13771K → N.1 Publication
    Corresponds to variant rs1800263 [ dbSNP | Ensembl ].
    VAR_005160
    Natural varianti1388 – 13881F → V.
    Corresponds to variant rs28715870 [ dbSNP | Ensembl ].
    VAR_057646
    Natural varianti1469 – 14691Q → L.1 Publication
    Corresponds to variant rs1057872 [ dbSNP | Ensembl ].
    VAR_005161
    Natural varianti1470 – 14701R → H in a breast cancer sample; somatic mutation. 1 Publication
    VAR_036355
    Natural varianti1672 – 16721N → K in CMD3B. 1 Publication
    Corresponds to variant rs16990264 [ dbSNP | Ensembl ].
    VAR_023542
    Natural varianti1745 – 17451R → H.1 Publication
    Corresponds to variant rs1801187 [ dbSNP | Ensembl ].
    VAR_005162
    Natural varianti1844 – 18441R → S.1 Publication
    Corresponds to variant rs1801186 [ dbSNP | Ensembl ].
    VAR_005163
    Natural varianti2108 – 21081R → C.
    Corresponds to variant rs16990169 [ dbSNP | Ensembl ].
    VAR_057647
    Natural varianti2155 – 21551R → W.1 Publication
    Corresponds to variant rs1800273 [ dbSNP | Ensembl ].
    VAR_005164
    Natural varianti2164 – 21641A → V in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_036356
    Natural varianti2191 – 21911R → W.1 Publication
    VAR_005165
    Natural varianti2299 – 22991N → T.1 Publication
    VAR_023543
    Natural varianti2305 – 236662Missing in DMD.
    VAR_005166Add
    BLAST
    Natural varianti2366 – 23661K → Q.2 Publications
    Corresponds to variant rs1800275 [ dbSNP | Ensembl ].
    VAR_005167
    Natural varianti2910 – 29101E → V.1 Publication
    Corresponds to variant rs41305353 [ dbSNP | Ensembl ].
    VAR_005168
    Natural varianti2912 – 29121N → D.1 Publication
    Corresponds to variant rs1800278 [ dbSNP | Ensembl ].
    VAR_005169
    Natural varianti2921 – 29211H → R in BMD.
    Corresponds to variant rs1800279 [ dbSNP | Ensembl ].
    VAR_005170
    Natural varianti2937 – 29371Q → R.3 Publications
    Corresponds to variant rs1800280 [ dbSNP | Ensembl ].
    VAR_005171
    Natural varianti3228 – 32281F → L in CMD3B. 1 Publication
    VAR_023544
    Natural varianti3313 – 33131C → F in DMD; results in highly reduced protein levels and expression at the sarcolemma. 1 Publication
    VAR_023545
    Natural varianti3335 – 33351D → H in DMD; does not affect protein stability; does not affect protein expression at the sarcolemma; interaction with DAG1 is reduced. 1 Publication
    VAR_023546
    Natural varianti3340 – 33401C → Y in DMD; results in highly reduced protein levels and expression at the sarcolemma. 1 Publication
    VAR_023547
    Natural varianti3421 – 34211A → V in BMD.
    VAR_005172

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 30683068Missing in isoform 5, isoform 6, isoform 7, isoform 8, isoform 9 and isoform 10. 3 PublicationsVSP_017490Add
    BLAST
    Alternative sequencei1 – 1111MLWWEEVEDCY → MED in isoform 3. 1 PublicationVSP_006809Add
    BLAST
    Alternative sequencei1 – 11M → MTEIILLIFFPAYFLN in isoform 1. CuratedVSP_006806
    Alternative sequencei1 – 11M → MSARKLRNLSYKK in isoform 2. CuratedVSP_006808
    Alternative sequencei2 – 13571356Missing in isoform 1 and isoform 2. CuratedVSP_006807Add
    BLAST
    Alternative sequencei3069 – 30757KVPYYIN → MREQLKG in isoform 5, isoform 6, isoform 7, isoform 8, isoform 9 and isoform 10. 3 PublicationsVSP_017491
    Alternative sequencei3409 – 3518110Missing in isoform 9 and isoform 10. CuratedVSP_046319Add
    BLAST
    Alternative sequencei3409 – 342113Missing in isoform 5 and isoform 8. 3 PublicationsVSP_017492Add
    BLAST
    Alternative sequencei3673 – 368513RNTPG…REDTM → HNVGSLFHMADDLGRAMESL VSVMTDEEGAE in isoform 5, isoform 6 and isoform 9. 3 PublicationsVSP_017493Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M18533 mRNA. Translation: AAA53189.1.
    X14298 mRNA. Translation: CAA32479.1.
    M92650 mRNA. Translation: AAA52316.1.
    AL031542
    , AC004468, AC006061, AC078958, AC079143, AC079175, AC079177, AC079864, AC090632, AC093167, AC093193, AC096506, AL031643, AL096699, AL109609, AL139278, AL451144 Genomic DNA. Translation: CAI42229.1.
    AL031643
    , AC004468, AC006061, AC078958, AC079143, AC079175, AC079177, AC079864, AC090632, AC093167, AC093193, AC096506, AL031542, AL096699, AL109609, AL139278, AL451144 Genomic DNA. Translation: CAI43058.1.
    AL049643 Genomic DNA. No translation available.
    AL050305 Genomic DNA. No translation available.
    AL096699
    , AC004468, AC006061, AC078958, AC079143, AC079175, AC079177, AC079864, AC090632, AC093167, AC093193, AC096506, AL031542, AL031643, AL109609, AL139278, AL451144 Genomic DNA. Translation: CAI42225.1.
    AL109609
    , AC004468, AC006061, AC078958, AC079143, AC079175, AC079177, AC079864, AC090632, AC093167, AC093193, AC096506, AL031542, AL031643, AL096699, AL139278, AL451144 Genomic DNA. Translation: CAI42950.1.
    AL121880 Genomic DNA. No translation available.
    AL139278
    , AC004468, AC006061, AC078958, AC079143, AC079175, AC079177, AC079864, AC090632, AC093167, AC093193, AC096506, AL031542, AL031643, AL096699, AL109609, AL451144 Genomic DNA. Translation: CAI42991.1.
    AL139401 Genomic DNA. No translation available.
    AL451144
    , AC004468, AC006061, AC078958, AC079143, AC079175, AC079177, AC079864, AC090632, AC093167, AC093193, AC096506, AL031542, AL031643, AL096699, AL109609, AL139278 Genomic DNA. Translation: CAI39566.1.
    AL596023 Genomic DNA. No translation available.
    CH471074 Genomic DNA. Translation: EAW99065.1.
    BC028720 mRNA. Translation: AAH28720.1.
    BC070078 mRNA. Translation: AAH70078.1.
    BC094758 mRNA. Translation: AAH94758.1.
    U27203 Genomic DNA. Translation: AAA86115.1.
    U27203 Genomic DNA. Translation: AAA86116.1.
    X15148 mRNA. Translation: CAA33245.1.
    X06178 mRNA. Translation: CAA29544.1.
    X06179 mRNA. Translation: CAA29545.1.
    X13045 Genomic DNA. Translation: CAA31451.1.
    X13046 Genomic DNA. Translation: CAA31452.1.
    X13047 Genomic DNA. Translation: CAA31453.1.
    X13048 Genomic DNA. Translation: CAA31454.1.
    X15495 Genomic DNA. Translation: CAA33518.1.
    X54820 Genomic DNA. Translation: CAA38589.1.
    CCDSiCCDS14231.1. [P11532-6]
    CCDS14232.1. [P11532-5]
    CCDS14233.1. [P11532-1]
    CCDS14234.1. [P11532-7]
    PIRiA45255.
    RefSeqiNP_000100.2. NM_000109.3.
    NP_003997.1. NM_004006.2.
    NP_004000.1. NM_004009.3.
    NP_004001.1. NM_004010.3.
    NP_004002.2. NM_004011.3.
    NP_004003.1. NM_004012.3.
    NP_004004.1. NM_004013.2.
    NP_004005.1. NM_004014.2.
    NP_004006.1. NM_004015.2. [P11532-7]
    NP_004007.1. NM_004016.2. [P11532-6]
    NP_004008.1. NM_004017.2. [P11532-8]
    NP_004009.1. NM_004018.2. [P11532-5]
    NP_004010.1. NM_004019.2.
    NP_004011.2. NM_004020.3.
    NP_004012.1. NM_004021.2.
    NP_004013.1. NM_004022.2.
    NP_004014.1. NM_004023.2.
    UniGeneiHs.495912.

    Genome annotation databases

    EnsembliENST00000361471; ENSP00000354464; ENSG00000198947. [P11532-5]
    ENST00000378680; ENSP00000367951; ENSG00000198947. [P11532-9]
    ENST00000378702; ENSP00000367974; ENSG00000198947. [P11532-7]
    ENST00000378723; ENSP00000367997; ENSG00000198947. [P11532-6]
    GeneIDi1756.
    KEGGihsa:1756.
    UCSCiuc004dcn.1. human. [P11532-5]
    uc004dco.1. human. [P11532-6]
    uc004dcw.2. human. [P11532-3]
    uc004dcx.2. human. [P11532-1]
    uc004dcy.1. human. [P11532-4]

    Polymorphism databases

    DMDMi313104240.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    DMD

    Dystrophin Mutation Database

    SHMPD

    The Singapore human mutation and polymorphism database

    Wikipedia

    Dystrophin entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M18533 mRNA. Translation: AAA53189.1 .
    X14298 mRNA. Translation: CAA32479.1 .
    M92650 mRNA. Translation: AAA52316.1 .
    AL031542
    , AC004468 , AC006061 , AC078958 , AC079143 , AC079175 , AC079177 , AC079864 , AC090632 , AC093167 , AC093193 , AC096506 , AL031643 , AL096699 , AL109609 , AL139278 , AL451144 Genomic DNA. Translation: CAI42229.1 .
    AL031643
    , AC004468 , AC006061 , AC078958 , AC079143 , AC079175 , AC079177 , AC079864 , AC090632 , AC093167 , AC093193 , AC096506 , AL031542 , AL096699 , AL109609 , AL139278 , AL451144 Genomic DNA. Translation: CAI43058.1 .
    AL049643 Genomic DNA. No translation available.
    AL050305 Genomic DNA. No translation available.
    AL096699
    , AC004468 , AC006061 , AC078958 , AC079143 , AC079175 , AC079177 , AC079864 , AC090632 , AC093167 , AC093193 , AC096506 , AL031542 , AL031643 , AL109609 , AL139278 , AL451144 Genomic DNA. Translation: CAI42225.1 .
    AL109609
    , AC004468 , AC006061 , AC078958 , AC079143 , AC079175 , AC079177 , AC079864 , AC090632 , AC093167 , AC093193 , AC096506 , AL031542 , AL031643 , AL096699 , AL139278 , AL451144 Genomic DNA. Translation: CAI42950.1 .
    AL121880 Genomic DNA. No translation available.
    AL139278
    , AC004468 , AC006061 , AC078958 , AC079143 , AC079175 , AC079177 , AC079864 , AC090632 , AC093167 , AC093193 , AC096506 , AL031542 , AL031643 , AL096699 , AL109609 , AL451144 Genomic DNA. Translation: CAI42991.1 .
    AL139401 Genomic DNA. No translation available.
    AL451144
    , AC004468 , AC006061 , AC078958 , AC079143 , AC079175 , AC079177 , AC079864 , AC090632 , AC093167 , AC093193 , AC096506 , AL031542 , AL031643 , AL096699 , AL109609 , AL139278 Genomic DNA. Translation: CAI39566.1 .
    AL596023 Genomic DNA. No translation available.
    CH471074 Genomic DNA. Translation: EAW99065.1 .
    BC028720 mRNA. Translation: AAH28720.1 .
    BC070078 mRNA. Translation: AAH70078.1 .
    BC094758 mRNA. Translation: AAH94758.1 .
    U27203 Genomic DNA. Translation: AAA86115.1 .
    U27203 Genomic DNA. Translation: AAA86116.1 .
    X15148 mRNA. Translation: CAA33245.1 .
    X06178 mRNA. Translation: CAA29544.1 .
    X06179 mRNA. Translation: CAA29545.1 .
    X13045 Genomic DNA. Translation: CAA31451.1 .
    X13046 Genomic DNA. Translation: CAA31452.1 .
    X13047 Genomic DNA. Translation: CAA31453.1 .
    X13048 Genomic DNA. Translation: CAA31454.1 .
    X15495 Genomic DNA. Translation: CAA33518.1 .
    X54820 Genomic DNA. Translation: CAA38589.1 .
    CCDSi CCDS14231.1. [P11532-6 ]
    CCDS14232.1. [P11532-5 ]
    CCDS14233.1. [P11532-1 ]
    CCDS14234.1. [P11532-7 ]
    PIRi A45255.
    RefSeqi NP_000100.2. NM_000109.3.
    NP_003997.1. NM_004006.2.
    NP_004000.1. NM_004009.3.
    NP_004001.1. NM_004010.3.
    NP_004002.2. NM_004011.3.
    NP_004003.1. NM_004012.3.
    NP_004004.1. NM_004013.2.
    NP_004005.1. NM_004014.2.
    NP_004006.1. NM_004015.2. [P11532-7 ]
    NP_004007.1. NM_004016.2. [P11532-6 ]
    NP_004008.1. NM_004017.2. [P11532-8 ]
    NP_004009.1. NM_004018.2. [P11532-5 ]
    NP_004010.1. NM_004019.2.
    NP_004011.2. NM_004020.3.
    NP_004012.1. NM_004021.2.
    NP_004013.1. NM_004022.2.
    NP_004014.1. NM_004023.2.
    UniGenei Hs.495912.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1DXX X-ray 2.60 A/B/C/D 1-246 [» ]
    1EG3 X-ray 2.00 A 3046-3306 [» ]
    1EG4 X-ray 2.00 A 3046-3306 [» ]
    3UUN X-ray 2.30 A/B 338-456 [» ]
    ProteinModelPortali P11532.
    SMRi P11532. Positions 9-246, 338-453, 3047-3306.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108096. 28 interactions.
    IntActi P11532. 14 interactions.
    MINTi MINT-109755.
    STRINGi 9606.ENSP00000354923.

    PTM databases

    PhosphoSitei P11532.

    Polymorphism databases

    DMDMi 313104240.

    Proteomic databases

    MaxQBi P11532.
    PaxDbi P11532.
    PRIDEi P11532.

    Protocols and materials databases

    DNASUi 1756.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000361471 ; ENSP00000354464 ; ENSG00000198947 . [P11532-5 ]
    ENST00000378680 ; ENSP00000367951 ; ENSG00000198947 . [P11532-9 ]
    ENST00000378702 ; ENSP00000367974 ; ENSG00000198947 . [P11532-7 ]
    ENST00000378723 ; ENSP00000367997 ; ENSG00000198947 . [P11532-6 ]
    GeneIDi 1756.
    KEGGi hsa:1756.
    UCSCi uc004dcn.1. human. [P11532-5 ]
    uc004dco.1. human. [P11532-6 ]
    uc004dcw.2. human. [P11532-3 ]
    uc004dcx.2. human. [P11532-1 ]
    uc004dcy.1. human. [P11532-4 ]

    Organism-specific databases

    CTDi 1756.
    GeneCardsi GC0XM031047.
    GeneReviewsi DMD.
    HGNCi HGNC:2928. DMD.
    HPAi CAB000119.
    HPA002725.
    HPA023885.
    MIMi 300376. phenotype.
    300377. gene.
    302045. phenotype.
    310200. phenotype.
    neXtProti NX_P11532.
    Orphaneti 98895. Becker muscular dystrophy.
    98896. Duchenne muscular dystrophy.
    154. Familial isolated dilated cardiomyopathy.
    206546. Symptomatic form of muscular dystrophy of Duchenne and Becker in female carriers.
    PharmGKBi PA27378.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5069.
    HOGENOMi HOG000231175.
    HOVERGENi HBG005495.
    InParanoidi P11532.
    KOi K10366.
    OrthoDBi EOG7V765N.
    PhylomeDBi P11532.
    TreeFami TF320178.

    Enzyme and pathway databases

    Reactomei REACT_163874. Non-integrin membrane-ECM interactions.
    REACT_16969. Striated Muscle Contraction.
    SignaLinki P11532.

    Miscellaneous databases

    ChiTaRSi DMD. human.
    EvolutionaryTracei P11532.
    GeneWikii Dystrophin.
    GenomeRNAii 1756.
    NextBioi 7115.
    PROi P11532.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P11532.
    Bgeei P11532.
    CleanExi HS_DMD.
    Genevestigatori P11532.

    Family and domain databases

    Gene3Di 1.10.238.10. 2 hits.
    1.10.418.10. 2 hits.
    InterProi IPR001589. Actinin_actin-bd_CS.
    IPR001715. CH-domain.
    IPR016344. Dystrophin/utrophin.
    IPR011992. EF-hand-dom_pair.
    IPR015153. EF-hand_dom_typ1.
    IPR015154. EF-hand_dom_typ2.
    IPR018159. Spectrin/alpha-actinin.
    IPR002017. Spectrin_repeat.
    IPR001202. WW_dom.
    IPR000433. Znf_ZZ.
    [Graphical view ]
    Pfami PF00307. CH. 2 hits.
    PF09068. EF-hand_2. 1 hit.
    PF09069. EF-hand_3. 1 hit.
    PF00435. Spectrin. 17 hits.
    PF00397. WW. 1 hit.
    PF00569. ZZ. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF002341. Dystrophin/utrophin. 1 hit.
    SMARTi SM00033. CH. 2 hits.
    SM00150. SPEC. 22 hits.
    SM00456. WW. 1 hit.
    SM00291. ZnF_ZZ. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47576. SSF47576. 1 hit.
    SSF51045. SSF51045. 1 hit.
    PROSITEi PS00019. ACTININ_1. 1 hit.
    PS00020. ACTININ_2. 1 hit.
    PS50021. CH. 2 hits.
    PS01159. WW_DOMAIN_1. 1 hit.
    PS50020. WW_DOMAIN_2. 1 hit.
    PS01357. ZF_ZZ_1. 1 hit.
    PS50135. ZF_ZZ_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The complete sequence of dystrophin predicts a rod-shaped cytoskeletal protein."
      Koenig M., Monaco A.P., Kunkel L.M.
      Cell 53:219-228(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), VARIANTS GLY-882; LEU-1469 AND GLN-2366.
      Tissue: Muscle.
    2. "Two human cDNA molecules coding for the Duchenne muscular dystrophy (DMD) locus are highly homologous."
      Rosenthal A., Speer A., Billowitz H., Cross G.S., Forrest S.N., Davies K.E.
      Nucleic Acids Res. 17:5391-5391(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), VARIANTS PRO-133; ILE-623; GLY-784; GLY-882; PHE-1197; ASN-1377; HIS-1745 AND SER-1844.
    3. "A 71-kilodalton protein is a major product of the Duchenne muscular dystrophy gene in brain and other nonmuscle tissues."
      Lederfein D., Levy Z., Augier N., Mornet D., Morris G., Fuchs O., Yaffe D., Nudel U.
      Proc. Natl. Acad. Sci. U.S.A. 89:5346-5350(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), TISSUE SPECIFICITY.
      Tissue: Brain.
    4. "The DNA sequence of the human X chromosome."
      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.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ARG-2937.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 6 AND 8).
      Tissue: Brain, Placenta and Testis.
    7. White R.A.
      Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-1411 (ISOFORMS 1 AND 2).
      Tissue: Retina.
    8. "Complete cloning of the Duchenne muscular dystrophy (DMD) cDNA and preliminary genomic organization of the DMD gene in normal and affected individuals."
      Koenig M., Hoffman E.P., Bertelson C.J., Monaco A.P., Feener C., Kunkel L.M.
      Cell 50:509-517(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-497 (ISOFORM 4).
    9. "Alternative splicing of human dystrophin mRNA generates isoforms at the carboxy terminus."
      Feener C.A., Koenig M., Kunkel L.M.
      Nature 338:509-511(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-32 (ISOFORM 3), ALTERNATIVE SPLICING.
      Tissue: Brain.
    10. "Deletions of fetal and adult muscle cDNA in Duchenne and Becker muscular dystrophy patients."
      Cross G.S., Speer A., Rosenthal A., Forrest S.M., Smith T.J., Edwards Y., Flint T., Hill D., Davies K.E.
      EMBO J. 6:3277-3283(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 404-1137 (ISOFORMS 3/4/5), VARIANT GLY-882.
    11. "Deletion screening of the Duchenne muscular dystrophy locus via multiplex DNA amplification."
      Chamberlain J.S., Gibbs R.A., Ranier J.A., Nguyen P.N., Caskey C.T.
      Nucleic Acids Res. 16:11141-11156(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 665-722; 2098-2204 AND 2305-2366.
    12. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2147-2204.
    13. "Differences in introns flanking exon 48 of the DMD/BMD gene."
      Huth A., Will K., Speer A., Bauer D.
      Submitted (MAR-1991) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2305-2364.
    14. "Cloning and characterization of alternatively spliced isoforms of Dp71."
      Austin R.C., Howard P.L., D'Souza V.N., Klamut H.J., Ray P.N.
      Hum. Mol. Genet. 4:1475-1483(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3670-3685 (ISOFORMS 1/2/3/4 AND 5), TISSUE SPECIFICITY.
      Tissue: Amnion.
    15. "Detailed analysis of the repeat domain of dystrophin reveals four potential hinge segments that may confer flexibility."
      Koenig M., Kunkel L.M.
      J. Biol. Chem. 265:4560-4566(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: ANALYSIS OF THE DOMAIN STRUCTURE.
    16. "Identification and characterization of the dystrophin anchoring site on beta-dystroglycan."
      Jung D., Yang B., Meyer J., Chamberlain J.S., Campbell K.P.
      J. Biol. Chem. 270:27305-27310(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DAG1.
    17. "Syntrophin binds to an alternatively spliced exon of dystrophin."
      Ahn A.H., Kunkel L.M.
      J. Cell Biol. 128:363-371(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SNTB1.
    18. "The three human syntrophin genes are expressed in diverse tissues, have distinct chromosomal locations, and each bind to dystrophin and its relatives."
      Ahn A.H., Feener C.A., Gussoni E., Yoshida M., Ozawa E., Kunkel L.M.
      J. Biol. Chem. 271:2724-2730(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SNTA1 AND SNTB2.
    19. "A splice variant of Dp71 lacking the syntrophin binding site is expressed in early stages of human neural development."
      Ceccarini M., Rizzo G., Rosa G., Chelucci C., Macioce P., Petrucci T.C.
      Brain Res. Dev. Brain Res. 103:77-82(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING (ISOFORMS 5 AND 9), DEVELOPMENTAL STAGE.
      Tissue: Telencephalon.
    20. "Gamma1- and gamma2-syntrophins, two novel dystrophin-binding proteins localized in neuronal cells."
      Piluso G., Mirabella M., Ricci E., Belsito A., Abbondanza C., Servidei S., Puca A.A., Tonali P., Puca G.A., Nigro V.
      J. Biol. Chem. 275:15851-15860(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SNTG1 AND SNTG2.
    21. "Expression and synthesis of alternatively spliced variants of Dp71 in adult human brain."
      Austin R.C., Morris G.E., Howard P.L., Klamut H.J., Ray P.N.
      Neuromuscul. Disord. 10:187-193(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING (ISOFORMS 9 AND 10).
      Tissue: Brain.
    22. "The interaction of dystrophin with beta-dystroglycan is regulated by tyrosine phosphorylation."
      Ilsley J.L., Sudol M., Winder S.J.
      Cell. Signal. 13:625-632(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DAG1.
    23. "Specific interaction of the actin-binding domain of dystrophin with intermediate filaments containing keratin 19."
      Stone M.R., O'Neill A., Catino D., Bloch R.J.
      Mol. Biol. Cell 16:4280-4293(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH KRT19, TISSUE SPECIFICITY.
    24. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    25. "Role of dystrophin and utrophin for assembly and function of the dystrophin glycoprotein complex in non-muscle tissue."
      Haenggi T., Fritschy J.M.
      Cell. Mol. Life Sci. 63:1614-1631(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN THE DYSTROPHIN-ASSOCIATED GLYCOPROTEIN COMPLEX.
    26. Cited for: 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), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    27. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    28. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      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.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3612; SER-3613 AND SER-3623, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    29. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    30. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    31. "Structure of a WW domain containing fragment of dystrophin in complex with beta-dystroglycan."
      Huang X., Poy F., Zhang R., Joachimiak A., Sudol M., Eck M.J.
      Nat. Struct. Biol. 7:634-638(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 3046-3306 IN COMPLEX WITH DAG1.
    32. "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."
      Norwood F.L.M., Sutherland-Smith A.J., Keep N.H., Kendrick-Jones J.
      Structure 8:481-491(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-246.
    33. "Searching for the 1 in 2,400,000: a review of dystrophin gene point mutations."
      Roberts R.G., Gardner R.J., Bobrow M.
      Hum. Mutat. 4:1-11(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON DMD VARIANTS.
    34. "Microlesions and polymorphisms in the Duchenne/Becker muscular dystrophy gene."
      Rininsland F., Reiss J.
      Hum. Genet. 94:111-116(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON VARIANTS.
    35. "A missense mutation in the dystrophin gene in a Duchenne muscular dystrophy patient."
      Prior T.W., Papp A.C., Snyder P.J., Burghes A.H.M., Bartolo C., Sedra M.S., Western L.M., Mendell J.R.
      Nat. Genet. 4:357-360(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT DMD ARG-54.
    36. "Identification of a missense mutation, single base deletion and a polymorphism in the dystrophin exon 16."
      Prior T.W., Bartolo C., Papp A.C., Snyder P.J., Sedra M.S., Burghes A.H., Mendell J.R.
      Hum. Mol. Genet. 3:1173-1174(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT DMD GLY-645.
    37. "Novel small mutations along the DMD/BMD gene associated with different phenotypes."
      Nigro V., Nigro G., Esposito M.G., Comi L.I., Molinari A.M., Puca G.A., Politano L.
      Hum. Mol. Genet. 3:1907-1908(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS HIS-365; TRP-2191 AND ARG-2937.
    38. "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."
      Lenk U., Oexle K., Voit T., Ancker U., Hellner K.A., Speer A., Hubner C.
      Hum. Mol. Genet. 5:973-975(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT DMD TYR-3340.
    39. "Evidence for a dystrophin missense mutation as a cause of X-linked dilated cardiomyopathy."
      Ortiz-Lopez R., Li H., Su J., Goytia V., Towbin J.A.
      Circulation 95:2434-2440(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CMD3B ALA-279.
    40. "A dystrophin missense mutation showing persistence of dystrophin and dystrophin-associated proteins yet a severe phenotype."
      Goldberg L.R., Hausmanowa-Petrusewicz I., Fidzianska A., Duggan D.J., Steinberg L.S., Hoffman E.P.
      Ann. Neurol. 44:971-976(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT DMD HIS-3335.
    41. "Identification of point mutations in Turkish DMD/BMD families using multiplex-single stranded conformation analysis (SSCA)."
      Eraslan S., Kayserili H., Apak M.Y., Kirdar B.
      Eur. J. Hum. Genet. 7:765-770(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT BMD PRO-171.
    42. "Comprehensive mutation scanning of the dystrophin gene in patients with nonsyndromic X-linked dilated cardiomyopathy."
      Feng J., Yan J.Y., Buzin C.H., Sommer S.S., Towbin J.A.
      J. Am. Coll. Cardiol. 40:1120-1124(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CMD3B LYS-1672.
    43. "Mutations in the dystrophin gene are associated with sporadic dilated cardiomyopathy."
      Feng J., Yan J., Buzin C.H., Towbin J.A., Sommer S.S.
      Mol. Genet. Metab. 77:119-126(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS CMD3B ASN-18 AND LEU-3228, VARIANTS TRP-2155; THR-2299; GLN-2366; VAL-2910; ASP-2912 AND ARG-2937.
    44. Cited for: VARIANT DMD PHE-3313, VARIANT VAL-165.
    45. Cited for: VARIANTS [LARGE SCALE ANALYSIS] PHE-334; GLN-1219; HIS-1470 AND VAL-2164.
    46. "Clinical and molecular characterization of a cohort of patients with novel nucleotide alterations of the Dystrophin gene detected by direct sequencing."
      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.
      BMC Med. Genet. 12:37-37(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT ARG-118.
    47. Cited for: CHARACTERIZATION OF VARIANTS DMD PHE-3313; HIS-3335 AND TYR-3340.

    Entry informationi

    Entry nameiDMD_HUMAN
    AccessioniPrimary (citable) accession number: P11532
    Secondary accession number(s): E9PDN1
    , Q02295, Q14169, Q14170, Q5JYU0, Q6NSJ9, Q7KZ48, Q8N754, Q9UCW3, Q9UCW4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1989
    Last sequence update: November 30, 2010
    Last modified: October 1, 2014
    This is version 188 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    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.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3