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P11532 (DMD_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 182. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dystrophin
Gene names
Name:DMD
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length3685 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Anchors the extracellular matrix to the cytoskeleton via F-actin. Ligand for dystroglycan. Component of the dystrophin-associated glycoprotein complex which accumulates at the neuromuscular junction (NMJ) and at a variety of synapses in the peripheral and central nervous systems and has a structural function in stabilizing the sarcolemma. Also implicated in signaling events and synaptic transmission. Ref.25

Subunit structure

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. Ref.16 Ref.17 Ref.18 Ref.20 Ref.22 Ref.23

Subcellular location

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.

Tissue specificity

Expressed in muscle fibers accumulating in the costameres of myoplasm at the sarcolemma. Expressed in brain, muscle, kidney, lung and testis. Isoform 5 is expressed in heart, brain, liver, testis and hepatoma cells. Most tissues contain transcripts of multiple isoforms, however only isoform 5 is detected in heart and liver. Ref.3 Ref.14 Ref.23

Developmental stage

Isoform 5 is expressed in embryonic neural tissue from the sixth week of development. Isoform 9 is detected in all embryonic tissues examined. Ref.19

Involvement in disease

Duchenne muscular dystrophy (DMD) [MIM:310200]: Most common form of muscular dystrophy; a sex-linked recessive disorder. It typically presents in boys aged 3 to 7 year as proximal muscle weakness causing waddling gait, toe-walking, lordosis, frequent falls, and difficulty in standing up and climbing up stairs. The pelvic girdle is affected first, then the shoulder girdle. Progression is steady and most patients are confined to a wheelchair by age of 10 or 12. Flexion contractures and scoliosis ultimately occur. About 50% of patients have a lower IQ than their genetic expectations would suggest. There is no treatment.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.35 Ref.36 Ref.38 Ref.40

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.41

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.39 Ref.42 Ref.43

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.

Sequence similarities

Contains 2 CH (calponin-homology) domains.

Contains 24 spectrin repeats.

Contains 1 WW domain.

Contains 1 ZZ-type zinc finger.

Ontologies

Keywords
   Cellular componentCell junction
Cell membrane
Cytoplasm
Cytoskeleton
Membrane
Postsynaptic cell membrane
Synapse
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseCardiomyopathy
Disease mutation
   DomainRepeat
Zinc-finger
   LigandActin-binding
Calcium
Metal-binding
Zinc
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcardiac muscle cell action potential

Inferred from sequence or structural similarity PubMed 20080623PubMed 21677768. Source: BHF-UCL

cardiac muscle contraction

Inferred from mutant phenotype PubMed 19027585. Source: BHF-UCL

cellular protein complex assembly

Inferred from sequence or structural similarity PubMed 19198614PubMed 20080623. Source: BHF-UCL

cellular protein localization

Inferred from mutant phenotype PubMed 7545544. Source: BHF-UCL

establishment of blood-nerve barrier

Inferred from electronic annotation. Source: Ensembl

establishment of glial blood-brain barrier

Inferred from electronic annotation. Source: Ensembl

extracellular matrix organization

Traceable author statement. Source: Reactome

motile cilium assembly

Traceable author statement PubMed 22105192. Source: BHF-UCL

muscle cell cellular homeostasis

Inferred from electronic annotation. Source: Ensembl

muscle fiber development

Inferred from electronic annotation. Source: Ensembl

muscle filament sliding

Traceable author statement. Source: Reactome

muscle organ development

Non-traceable author statement PubMed 1824797. Source: ProtInc

myotube cell development

Inferred from electronic annotation. Source: Ensembl

negative regulation of peptidyl-cysteine S-nitrosylation

Inferred from sequence or structural similarity PubMed 19198614PubMed 20080623. Source: BHF-UCL

negative regulation of peptidyl-serine phosphorylation

Inferred from sequence or structural similarity PubMed 23263329. Source: BHF-UCL

neurotransmitter receptor metabolic process

Inferred from electronic annotation. Source: Ensembl

nucleus localization

Inferred from electronic annotation. Source: Ensembl

olfactory nerve structural organization

Inferred from electronic annotation. Source: Ensembl

peptide biosynthetic process

Inferred from direct assay Ref.23. Source: UniProtKB

positive regulation of cell-matrix adhesion

Inferred from electronic annotation. Source: Ensembl

positive regulation of neuron differentiation

Inferred from mutant phenotype PubMed 15149856. Source: BHF-UCL

positive regulation of neuron projection development

Inferred from mutant phenotype PubMed 15149856. Source: BHF-UCL

positive regulation of sodium ion transmembrane transporter activity

Inferred from sequence or structural similarity PubMed 21677768. Source: BHF-UCL

regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion

Inferred from sequence or structural similarity PubMed 20080623. Source: BHF-UCL

regulation of cellular response to growth factor stimulus

Inferred from mutant phenotype PubMed 15149856. Source: BHF-UCL

regulation of heart rate

Inferred from mutant phenotype PubMed 19027585. Source: BHF-UCL

regulation of ryanodine-sensitive calcium-release channel activity

Inferred from sequence or structural similarity PubMed 20080623. Source: BHF-UCL

regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion

Inferred from sequence or structural similarity PubMed 19198614. Source: BHF-UCL

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: Ensembl

regulation of voltage-gated calcium channel activity

Inferred from sequence or structural similarity PubMed 21677768. Source: BHF-UCL

skeletal muscle tissue development

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentZ disc

Inferred from electronic annotation. Source: Ensembl

cell surface

Inferred from direct assay PubMed 10867799. Source: UniProtKB

cell-substrate junction

Inferred from electronic annotation. Source: Ensembl

costamere

Inferred from direct assay Ref.23. Source: UniProtKB

cytoskeleton

Traceable author statement Ref.1. Source: ProtInc

cytosol

Traceable author statement. Source: Reactome

dystrophin-associated glycoprotein complex

Traceable author statement PubMed 22105192. Source: BHF-UCL

filopodium

Inferred from direct assay PubMed 16803572. Source: BHF-UCL

membrane raft

Inferred from electronic annotation. Source: Ensembl

neuron projection terminus

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from direct assay PubMed 15149856. Source: BHF-UCL

postsynaptic membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

sarcolemma

Inferred from direct assay PubMed 7545544. Source: BHF-UCL

syntrophin complex

Traceable author statement PubMed 21164104. Source: BHF-UCL

   Molecular_functionactin binding

Traceable author statement PubMed 12376554. Source: UniProtKB

calcium ion binding

Inferred from electronic annotation. Source: InterPro

myosin binding

Inferred from direct assay PubMed 16803572. Source: BHF-UCL

nitric-oxide synthase binding

Inferred from sequence or structural similarity PubMed 7545544. Source: BHF-UCL

structural constituent of cytoskeleton

Traceable author statement Ref.1. Source: ProtInc

structural constituent of muscle

Inferred from direct assay Ref.23. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 10 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform 4 (identifier: P11532-1)

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.
Isoform 1 (identifier: P11532-2)

Also known as: Dystrophin-1;

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MTEIILLIFFPAYFLN
     2-1357: Missing.
Isoform 2 (identifier: P11532-3)

Also known as: Dystrophin-2;

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MSARKLRNLSYKK
     2-1357: Missing.
Isoform 3 (identifier: P11532-4)

Also known as: Dystrophin-3;

The sequence of this isoform differs from the canonical sequence as follows:
     1-11: MLWWEEVEDCY → MED
Isoform 5 (identifier: P11532-5)

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.
Isoform 6 (identifier: P11532-6)

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.
Isoform 7 (identifier: P11532-7)

Also known as: Dp71;

The sequence of this isoform differs from the canonical sequence as follows:
     1-3068: Missing.
     3069-3075: KVPYYIN → MREQLKG
Isoform 8 (identifier: P11532-8)

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.
Isoform 9 (identifier: P11532-9)

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
Isoform 10 (identifier: P11532-10)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 36853685Dystrophin
PRO_0000076075

Regions

Domain1 – 240240Actin-binding
Domain15 – 119105CH 1
Domain134 – 237104CH 2
Repeat339 – 447109Spectrin 1
Repeat448 – 556109Spectrin 2
Repeat559 – 667109Spectrin 3
Repeat719 – 828110Spectrin 4
Repeat830 – 934105Spectrin 5
Repeat943 – 1045103Spectrin 6
Repeat1048 – 1154107Spectrin 7
Repeat1157 – 1263107Spectrin 8
Repeat1266 – 1367102Spectrin 9
Repeat1368 – 146396Spectrin 10
Repeat1468 – 1568101Spectrin 11
Repeat1571 – 1676106Spectrin 12
Repeat1679 – 1778100Spectrin 13
Repeat1779 – 187496Spectrin 14
Repeat1877 – 1979103Spectrin 15
Repeat1992 – 2101110Spectrin 16
Repeat2104 – 2208105Spectrin 17
Repeat2211 – 2318108Spectrin 18
Repeat2319 – 2423105Spectrin 19
Repeat2475 – 2577103Spectrin 20
Repeat2580 – 2686107Spectrin 21
Repeat2689 – 2802114Spectrin 22
Repeat2808 – 2930123Spectrin 23
Repeat2935 – 3040106Spectrin 24
Domain3055 – 308834WW
Zinc finger3307 – 335448ZZ-type
Region63 – 7210ANK2- and ANK-3 binding By similarity
Region1415 – 1913499Interaction with SYNM By similarity
Region3058 – 3408351Interaction with SYNM By similarity
Region3466 – 351853Binds to SNTB1

Amino acid modifications

Modified residue34831Phosphoserine Ref.26
Modified residue36121Phosphoserine Ref.28
Modified residue36131Phosphoserine Ref.26 Ref.28
Modified residue36171Phosphoserine Ref.26
Modified residue36231Phosphoserine Ref.26 Ref.28
Modified residue36241Phosphoserine By similarity
Modified residue36661Phosphoserine Ref.26

Natural variations

Alternative sequence1 – 30683068Missing in isoform 5, isoform 6, isoform 7, isoform 8, isoform 9 and isoform 10.
VSP_017490
Alternative sequence1 – 1111MLWWEEVEDCY → MED in isoform 3.
VSP_006809
Alternative sequence11M → MTEIILLIFFPAYFLN in isoform 1.
VSP_006806
Alternative sequence11M → MSARKLRNLSYKK in isoform 2.
VSP_006808
Alternative sequence2 – 13571356Missing in isoform 1 and isoform 2.
VSP_006807
Alternative sequence3069 – 30757KVPYYIN → MREQLKG in isoform 5, isoform 6, isoform 7, isoform 8, isoform 9 and isoform 10.
VSP_017491
Alternative sequence3409 – 3518110Missing in isoform 9 and isoform 10.
VSP_046319
Alternative sequence3409 – 342113Missing in isoform 5 and isoform 8.
VSP_017492
Alternative sequence3673 – 368513RNTPG…REDTM → HNVGSLFHMADDLGRAMESL VSVMTDEEGAE in isoform 5, isoform 6 and isoform 9.
VSP_017493
Natural variant181K → N in CMD3B. Ref.43
VAR_023537
Natural variant32 – 6231Missing in BMD.
VAR_005146
Natural variant541L → R in DMD. Ref.35
VAR_005147
Natural variant1181W → R in a patient with Becker muscular dystrophy. Ref.46
VAR_065764
Natural variant1331Q → P. Ref.2
Corresponds to variant rs1800256 [ dbSNP | Ensembl ].
VAR_005148
Natural variant1651D → V in one patient with Becker muscular dystrophy. Ref.44
VAR_023538
Natural variant1681A → D in BMD.
VAR_005149
Natural variant1711A → P in BMD. Ref.41
VAR_023539
Natural variant2311Y → N in BMD.
VAR_005150
Natural variant2791T → A in CMD3B. Ref.39
VAR_023540
Natural variant3341L → F in a colorectal cancer sample; somatic mutation. Ref.45
VAR_036353
Natural variant3651Q → H. Ref.37
Corresponds to variant rs1800266 [ dbSNP | Ensembl ].
VAR_005151
Natural variant4091T → S.
Corresponds to variant rs34155804 [ dbSNP | Ensembl ].
VAR_057642
Natural variant495 – 53440Missing in BMD.
VAR_005152
Natural variant5731A → V.
Corresponds to variant rs5972599 [ dbSNP | Ensembl ].
VAR_057643
Natural variant6231L → I. Ref.2
Corresponds to variant rs1800259 [ dbSNP | Ensembl ].
VAR_005153
Natural variant6451D → G in DMD. Ref.36
VAR_023541
Natural variant6661S → L.
Corresponds to variant rs34563188 [ dbSNP | Ensembl ].
VAR_062110
Natural variant7151T → S.
Corresponds to variant rs16998350 [ dbSNP | Ensembl ].
VAR_057644
Natural variant7731K → E in DMD.
VAR_005154
Natural variant7841A → G. Ref.2
Corresponds to variant rs1800260 [ dbSNP | Ensembl ].
VAR_005155
Natural variant8821D → G. Ref.1 Ref.2 Ref.10
Corresponds to variant rs228406 [ dbSNP | Ensembl ].
VAR_005156
Natural variant11361T → S.
Corresponds to variant rs3827462 [ dbSNP | Ensembl ].
VAR_057645
Natural variant11971V → F. Ref.2
Corresponds to variant rs1800262 [ dbSNP | Ensembl ].
VAR_005157
Natural variant12191E → Q in a breast cancer sample; somatic mutation. Ref.45
VAR_036354
Natural variant12451T → I.
Corresponds to variant rs1800269 [ dbSNP | Ensembl ].
VAR_005158
Natural variant12781A → P.
Corresponds to variant rs1800270 [ dbSNP | Ensembl ].
VAR_005159
Natural variant13771K → N. Ref.2
Corresponds to variant rs1800263 [ dbSNP | Ensembl ].
VAR_005160
Natural variant13881F → V.
Corresponds to variant rs28715870 [ dbSNP | Ensembl ].
VAR_057646
Natural variant14691Q → L. Ref.1
Corresponds to variant rs1057872 [ dbSNP | Ensembl ].
VAR_005161
Natural variant14701R → H in a breast cancer sample; somatic mutation. Ref.45
VAR_036355
Natural variant16721N → K in CMD3B. Ref.42
Corresponds to variant rs16990264 [ dbSNP | Ensembl ].
VAR_023542
Natural variant17451R → H. Ref.2
Corresponds to variant rs1801187 [ dbSNP | Ensembl ].
VAR_005162
Natural variant18441R → S. Ref.2
Corresponds to variant rs1801186 [ dbSNP | Ensembl ].
VAR_005163
Natural variant21081R → C.
Corresponds to variant rs16990169 [ dbSNP | Ensembl ].
VAR_057647
Natural variant21551R → W. Ref.43
Corresponds to variant rs1800273 [ dbSNP | Ensembl ].
VAR_005164
Natural variant21641A → V in a colorectal cancer sample; somatic mutation. Ref.45
VAR_036356
Natural variant21911R → W. Ref.37
VAR_005165
Natural variant22991N → T. Ref.43
VAR_023543
Natural variant2305 – 236662Missing in DMD.
VAR_005166
Natural variant23661K → Q. Ref.1 Ref.43
Corresponds to variant rs1800275 [ dbSNP | Ensembl ].
VAR_005167
Natural variant29101E → V. Ref.43
Corresponds to variant rs41305353 [ dbSNP | Ensembl ].
VAR_005168
Natural variant29121N → D. Ref.43
Corresponds to variant rs1800278 [ dbSNP | Ensembl ].
VAR_005169
Natural variant29211H → R in BMD.
Corresponds to variant rs1800279 [ dbSNP | Ensembl ].
VAR_005170
Natural variant29371Q → R. Ref.4 Ref.37 Ref.43
Corresponds to variant rs1800280 [ dbSNP | Ensembl ].
VAR_005171
Natural variant32281F → L in CMD3B. Ref.43
VAR_023544
Natural variant33131C → F in one patient with Duchenne muscular dystrophy. Ref.44
VAR_023545
Natural variant33351D → H in DMD. Ref.40
VAR_023546
Natural variant33401C → Y in DMD. Ref.38
VAR_023547
Natural variant34211A → V in BMD.
VAR_005172

Experimental info

Sequence conflict6641Q → QM in CAA29544. Ref.10
Sequence conflict23611G → E in CAA38589. Ref.13
Sequence conflict35421P → T in AAH70078. Ref.6
Sequence conflict35461M → V in AAH70078. Ref.6

Secondary structure

................................................................................... 3685
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 4 (Dystrophin-4) [UniParc].

Last modified November 30, 2010. Version 3.
Checksum: 24FF7E83F1E6BF8D

FASTA3,685426,750
        10         20         30         40         50         60 
MLWWEEVEDC YEREDVQKKT FTKWVNAQFS KFGKQHIENL FSDLQDGRRL LDLLEGLTGQ 

        70         80         90        100        110        120 
KLPKEKGSTR VHALNNVNKA LRVLQNNNVD LVNIGSTDIV DGNHKLTLGL IWNIILHWQV 

       130        140        150        160        170        180 
KNVMKNIMAG LQQTNSEKIL LSWVRQSTRN YPQVNVINFT TSWSDGLALN ALIHSHRPDL 

       190        200        210        220        230        240 
FDWNSVVCQQ SATQRLEHAF NIARYQLGIE KLLDPEDVDT TYPDKKSILM YITSLFQVLP 

       250        260        270        280        290        300 
QQVSIEAIQE VEMLPRPPKV TKEEHFQLHH QMHYSQQITV SLAQGYERTS SPKPRFKSYA 

       310        320        330        340        350        360 
YTQAAYVTTS DPTRSPFPSQ HLEAPEDKSF GSSLMESEVN LDRYQTALEE VLSWLLSAED 

       370        380        390        400        410        420 
TLQAQGEISN DVEVVKDQFH THEGYMMDLT AHQGRVGNIL QLGSKLIGTG KLSEDEETEV 

       430        440        450        460        470        480 
QEQMNLLNSR WECLRVASME KQSNLHRVLM DLQNQKLKEL NDWLTKTEER TRKMEEEPLG 

       490        500        510        520        530        540 
PDLEDLKRQV QQHKVLQEDL EQEQVRVNSL THMVVVVDES SGDHATAALE EQLKVLGDRW 

       550        560        570        580        590        600 
ANICRWTEDR WVLLQDILLK WQRLTEEQCL FSAWLSEKED AVNKIHTTGF KDQNEMLSSL 

       610        620        630        640        650        660 
QKLAVLKADL EKKKQSMGKL YSLKQDLLST LKNKSVTQKT EAWLDNFARC WDNLVQKLEK 

       670        680        690        700        710        720 
STAQISQAVT TTQPSLTQTT VMETVTTVTT REQILVKHAQ EELPPPPPQK KRQITVDSEI 

       730        740        750        760        770        780 
RKRLDVDITE LHSWITRSEA VLQSPEFAIF RKEGNFSDLK EKVNAIEREK AEKFRKLQDA 

       790        800        810        820        830        840 
SRSAQALVEQ MVNEGVNADS IKQASEQLNS RWIEFCQLLS ERLNWLEYQN NIIAFYNQLQ 

       850        860        870        880        890        900 
QLEQMTTTAE NWLKIQPTTP SEPTAIKSQL KICKDEVNRL SDLQPQIERL KIQSIALKEK 

       910        920        930        940        950        960 
GQGPMFLDAD FVAFTNHFKQ VFSDVQAREK ELQTIFDTLP PMRYQETMSA IRTWVQQSET 

       970        980        990       1000       1010       1020 
KLSIPQLSVT DYEIMEQRLG ELQALQSSLQ EQQSGLYYLS TTVKEMSKKA PSEISRKYQS 

      1030       1040       1050       1060       1070       1080 
EFEEIEGRWK KLSSQLVEHC QKLEEQMNKL RKIQNHIQTL KKWMAEVDVF LKEEWPALGD 

      1090       1100       1110       1120       1130       1140 
SEILKKQLKQ CRLLVSDIQT IQPSLNSVNE GGQKIKNEAE PEFASRLETE LKELNTQWDH 

      1150       1160       1170       1180       1190       1200 
MCQQVYARKE ALKGGLEKTV SLQKDLSEMH EWMTQAEEEY LERDFEYKTP DELQKAVEEM 

      1210       1220       1230       1240       1250       1260 
KRAKEEAQQK EAKVKLLTES VNSVIAQAPP VAQEALKKEL ETLTTNYQWL CTRLNGKCKT 

      1270       1280       1290       1300       1310       1320 
LEEVWACWHE LLSYLEKANK WLNEVEFKLK TTENIPGGAE EISEVLDSLE NLMRHSEDNP 

      1330       1340       1350       1360       1370       1380 
NQIRILAQTL TDGGVMDELI NEELETFNSR WRELHEEAVR RQKLLEQSIQ SAQETEKSLH 

      1390       1400       1410       1420       1430       1440 
LIQESLTFID KQLAAYIADK VDAAQMPQEA QKIQSDLTSH EISLEEMKKH NQGKEAAQRV 

      1450       1460       1470       1480       1490       1500 
LSQIDVAQKK LQDVSMKFRL FQKPANFEQR LQESKMILDE VKMHLPALET KSVEQEVVQS 

      1510       1520       1530       1540       1550       1560 
QLNHCVNLYK SLSEVKSEVE MVIKTGRQIV QKKQTENPKE LDERVTALKL HYNELGAKVT 

      1570       1580       1590       1600       1610       1620 
ERKQQLEKCL KLSRKMRKEM NVLTEWLAAT DMELTKRSAV EGMPSNLDSE VAWGKATQKE 

      1630       1640       1650       1660       1670       1680 
IEKQKVHLKS ITEVGEALKT VLGKKETLVE DKLSLLNSNW IAVTSRAEEW LNLLLEYQKH 

      1690       1700       1710       1720       1730       1740 
METFDQNVDH ITKWIIQADT LLDESEKKKP QQKEDVLKRL KAELNDIRPK VDSTRDQAAN 

      1750       1760       1770       1780       1790       1800 
LMANRGDHCR KLVEPQISEL NHRFAAISHR IKTGKASIPL KELEQFNSDI QKLLEPLEAE 

      1810       1820       1830       1840       1850       1860 
IQQGVNLKEE DFNKDMNEDN EGTVKELLQR GDNLQQRITD ERKREEIKIK QQLLQTKHNA 

      1870       1880       1890       1900       1910       1920 
LKDLRSQRRK KALEISHQWY QYKRQADDLL KCLDDIEKKL ASLPEPRDER KIKEIDRELQ 

      1930       1940       1950       1960       1970       1980 
KKKEELNAVR RQAEGLSEDG AAMAVEPTQI QLSKRWREIE SKFAQFRRLN FAQIHTVREE 

      1990       2000       2010       2020       2030       2040 
TMMVMTEDMP LEISYVPSTY LTEITHVSQA LLEVEQLLNA PDLCAKDFED LFKQEESLKN 

      2050       2060       2070       2080       2090       2100 
IKDSLQQSSG RIDIIHSKKT AALQSATPVE RVKLQEALSQ LDFQWEKVNK MYKDRQGRFD 

      2110       2120       2130       2140       2150       2160 
RSVEKWRRFH YDIKIFNQWL TEAEQFLRKT QIPENWEHAK YKWYLKELQD GIGQRQTVVR 

      2170       2180       2190       2200       2210       2220 
TLNATGEEII QQSSKTDASI LQEKLGSLNL RWQEVCKQLS DRKKRLEEQK NILSEFQRDL 

      2230       2240       2250       2260       2270       2280 
NEFVLWLEEA DNIASIPLEP GKEQQLKEKL EQVKLLVEEL PLRQGILKQL NETGGPVLVS 

      2290       2300       2310       2320       2330       2340 
APISPEEQDK LENKLKQTNL QWIKVSRALP EKQGEIEAQI KDLGQLEKKL EDLEEQLNHL 

      2350       2360       2370       2380       2390       2400 
LLWLSPIRNQ LEIYNQPNQE GPFDVKETEI AVQAKQPDVE EILSKGQHLY KEKPATQPVK 

      2410       2420       2430       2440       2450       2460 
RKLEDLSSEW KAVNRLLQEL RAKQPDLAPG LTTIGASPTQ TVTLVTQPVV TKETAISKLE 

      2470       2480       2490       2500       2510       2520 
MPSSLMLEVP ALADFNRAWT ELTDWLSLLD QVIKSQRVMV GDLEDINEMI IKQKATMQDL 

      2530       2540       2550       2560       2570       2580 
EQRRPQLEEL ITAAQNLKNK TSNQEARTII TDRIERIQNQ WDEVQEHLQN RRQQLNEMLK 

      2590       2600       2610       2620       2630       2640 
DSTQWLEAKE EAEQVLGQAR AKLESWKEGP YTVDAIQKKI TETKQLAKDL RQWQTNVDVA 

      2650       2660       2670       2680       2690       2700 
NDLALKLLRD YSADDTRKVH MITENINASW RSIHKRVSER EAALEETHRL LQQFPLDLEK 

      2710       2720       2730       2740       2750       2760 
FLAWLTEAET TANVLQDATR KERLLEDSKG VKELMKQWQD LQGEIEAHTD VYHNLDENSQ 

      2770       2780       2790       2800       2810       2820 
KILRSLEGSD DAVLLQRRLD NMNFKWSELR KKSLNIRSHL EASSDQWKRL HLSLQELLVW 

      2830       2840       2850       2860       2870       2880 
LQLKDDELSR QAPIGGDFPA VQKQNDVHRA FKRELKTKEP VIMSTLETVR IFLTEQPLEG 

      2890       2900       2910       2920       2930       2940 
LEKLYQEPRE LPPEERAQNV TRLLRKQAEE VNTEWEKLNL HSADWQRKID ETLERLQELQ 

      2950       2960       2970       2980       2990       3000 
EATDELDLKL RQAEVIKGSW QPVGDLLIDS LQDHLEKVKA LRGEIAPLKE NVSHVNDLAR 

      3010       3020       3030       3040       3050       3060 
QLTTLGIQLS PYNLSTLEDL NTRWKLLQVA VEDRVRQLHE AHRDFGPASQ HFLSTSVQGP 

      3070       3080       3090       3100       3110       3120 
WERAISPNKV PYYINHETQT TCWDHPKMTE LYQSLADLNN VRFSAYRTAM KLRRLQKALC 

      3130       3140       3150       3160       3170       3180 
LDLLSLSAAC DALDQHNLKQ NDQPMDILQI INCLTTIYDR LEQEHNNLVN VPLCVDMCLN 

      3190       3200       3210       3220       3230       3240 
WLLNVYDTGR TGRIRVLSFK TGIISLCKAH LEDKYRYLFK QVASSTGFCD QRRLGLLLHD 

      3250       3260       3270       3280       3290       3300 
SIQIPRQLGE VASFGGSNIE PSVRSCFQFA NNKPEIEAAL FLDWMRLEPQ SMVWLPVLHR 

      3310       3320       3330       3340       3350       3360 
VAAAETAKHQ AKCNICKECP IIGFRYRSLK HFNYDICQSC FFSGRVAKGH KMHYPMVEYC 

      3370       3380       3390       3400       3410       3420 
TPTTSGEDVR DFAKVLKNKF RTKRYFAKHP RMGYLPVQTV LEGDNMETPV TLINFWPVDS 

      3430       3440       3450       3460       3470       3480 
APASSPQLSH DDTHSRIEHY ASRLAEMENS NGSYLNDSIS PNESIDDEHL LIQHYCQSLN 

      3490       3500       3510       3520       3530       3540 
QDSPLSQPRS PAQILISLES EERGELERIL ADLEEENRNL QAEYDRLKQQ HEHKGLSPLP 

      3550       3560       3570       3580       3590       3600 
SPPEMMPTSP QSPRDAELIA EAKLLRQHKG RLEARMQILE DHNKQLESQL HRLRQLLEQP 

      3610       3620       3630       3640       3650       3660 
QAEAKVNGTT VSSPSTSLQR SDSSQPMLLR VVGSQTSDSM GEEDLLSPPQ DTSTGLEEVM 

      3670       3680 
EQLNNSFPSS RGRNTPGKPM REDTM 

« Hide

Isoform 1 (Dystrophin-1) [UniParc].

Checksum: 50AF557D10DD0B23
Show »

FASTA2,344271,391
Isoform 2 (Dystrophin-2) [UniParc].

Checksum: 5A695D20AE07D801
Show »

FASTA2,341271,040
Isoform 3 (Dystrophin-3) [UniParc].

Checksum: 234A6D63F4910420
Show »

FASTA3,677425,640
Isoform 5 (Dp71ab) [UniParc].

Checksum: 75D44165427FAB8B
Show »

FASTA62270,750
Isoform 6 (Dp71b) [UniParc].

Checksum: 5EB1E49C45CF34EC
Show »

FASTA63572,191
Isoform 7 (Dp71) [UniParc].

Checksum: 660C9D904AF403B9
Show »

FASTA61770,375
Isoform 8 (Dp71a) [UniParc].

Checksum: 08BDA0A428FAA9F4
Show »

FASTA60468,934
Isoform 9 (Dp60) (Dp71delta110) [UniParc].

Checksum: D597517BCE4D9FD1
Show »

FASTA52559,769
Isoform 10 (Dp71c) [UniParc].

Checksum: 3F4518D23592BF1D
Show »

FASTA50757,953

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"High resolution deletion breakpoint mapping in the DMD gene by whole cosmid hybridization."
Blonden L.A.J., den Dunnen J.T., van Paassen H.M.B., Wapenaar M.C., Grootscholten P.M., Ginjaar H.B., Bakker E., Pearson P.L., van Ommen G.J.B.
Nucleic Acids Res. 17:5611-5621(1989) [PubMed] [Europe PMC] [Abstract]
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[30]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
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]"Rapid direct sequence analysis of the dystrophin gene."
Flanigan K.M., von Niederhausern A., Dunn D.M., Alder J., Mendell J.R., Weiss R.B.
Am. J. Hum. Genet. 72:931-939(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS VAL-165 AND PHE-3313.
[45]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Web resources

DMD

Dystrophin Mutation Database

GeneReviews
SHMPD

The Singapore human mutation and polymorphism database

Wikipedia

Dystrophin entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M18533 mRNA. Translation: AAA53189.1.
X14298 mRNA. Translation: CAA32479.1.
M92650 mRNA. Translation: AAA52316.1.
AL031542 expand/collapse EMBL AC list , AC004468, AC006061, AC078958, AC079143, AC079175, AC079177, AC079864, AC090632, AC093167, AC093193, AC096506, AL031643, AL096699, AL109609, AL139278, AL451144 Genomic DNA. Translation: CAI42229.1.
AL031643 expand/collapse EMBL AC list , 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 expand/collapse EMBL AC list , AC004468, AC006061, AC078958, AC079143, AC079175, AC079177, AC079864, AC090632, AC093167, AC093193, AC096506, AL031542, AL031643, AL109609, AL139278, AL451144 Genomic DNA. Translation: CAI42225.1.
AL109609 expand/collapse EMBL AC list , 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 expand/collapse EMBL AC list , 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 expand/collapse EMBL AC list , 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.
PIRA45255.
RefSeqNP_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.
NP_004007.1. NM_004016.2.
NP_004008.1. NM_004017.2.
NP_004009.1. NM_004018.2.
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.
UniGeneHs.495912.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DXXX-ray2.60A/B/C/D1-246[»]
1EG3X-ray2.00A3046-3306[»]
1EG4X-ray2.00A3046-3306[»]
3UUNX-ray2.30A/B338-456[»]
ProteinModelPortalP11532.
SMRP11532. Positions 9-246, 338-453, 3047-3306.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108096. 28 interactions.
IntActP11532. 14 interactions.
MINTMINT-109755.
STRING9606.ENSP00000354923.

PTM databases

PhosphoSiteP11532.

Polymorphism databases

DMDM76803557.

Proteomic databases

PaxDbP11532.
PRIDEP11532.

Protocols and materials databases

DNASU1756.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000361471; ENSP00000354464; ENSG00000198947. [P11532-5]
ENST00000378680; ENSP00000367951; ENSG00000198947. [P11532-9]
ENST00000378702; ENSP00000367974; ENSG00000198947. [P11532-7]
ENST00000378723; ENSP00000367997; ENSG00000198947. [P11532-6]
GeneID1756.
KEGGhsa:1756.
UCSCuc004dcn.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

CTD1756.
GeneCardsGC0XM031047.
HGNCHGNC:2928. DMD.
HPACAB000119.
HPA002725.
HPA023885.
MIM300376. phenotype.
300377. gene.
302045. phenotype.
310200. phenotype.
neXtProtNX_P11532.
Orphanet98895. Becker muscular dystrophy.
215. Congenital stationary night blindness.
98896. Duchenne muscular dystrophy.
154. Familial isolated dilated cardiomyopathy.
206546. Symptomatic form of muscular dystrophy of Duchenne and Becker in female carriers.
PharmGKBPA27378.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5069.
HOGENOMHOG000231175.
HOVERGENHBG005495.
InParanoidP11532.
KOK10366.
OrthoDBEOG7V765N.
TreeFamTF320178.

Enzyme and pathway databases

ReactomeREACT_118779. Extracellular matrix organization.
REACT_17044. Muscle contraction.
SignaLinkP11532.

Gene expression databases

ArrayExpressP11532.
BgeeP11532.
CleanExHS_DMD.
GenevestigatorP11532.

Family and domain databases

Gene3D1.10.238.10. 2 hits.
1.10.418.10. 2 hits.
InterProIPR001589. 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]
PfamPF00307. 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]
PIRSFPIRSF002341. Dystrophin/utrophin. 1 hit.
SMARTSM00033. CH. 2 hits.
SM00150. SPEC. 22 hits.
SM00456. WW. 1 hit.
SM00291. ZnF_ZZ. 1 hit.
[Graphical view]
SUPFAMSSF47576. SSF47576. 1 hit.
SSF51045. SSF51045. 1 hit.
PROSITEPS00019. 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]
ProtoNetSearch...

Other

ChiTaRSDMD. human.
EvolutionaryTraceP11532.
GeneWikiDystrophin.
GenomeRNAi1756.
NextBio7115.
PROP11532.
SOURCESearch...

Entry information

Entry nameDMD_HUMAN
AccessionPrimary (citable) accession number: P11532
Secondary accession number(s): E9PDN1 expand/collapse secondary AC list , Q02295, Q14169, Q14170, Q5JYU0, Q6NSJ9, Q7KZ48, Q8N754, Q9UCW3, Q9UCW4
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: November 30, 2010
Last modified: March 19, 2014
This is version 182 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM