Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Dystrophin

Gene

DMD

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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.By similarity1 Publication

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri3307 – 3354ZZ-typePROSITE-ProRule annotationAdd BLAST48

GO - Molecular functioni

  • actin binding Source: UniProtKB
  • dystroglycan binding Source: UniProtKB
  • myosin binding Source: BHF-UCL
  • nitric-oxide synthase binding Source: BHF-UCL
  • structural constituent of cytoskeleton Source: ProtInc
  • structural constituent of muscle Source: UniProtKB
  • vinculin binding Source: BHF-UCL
  • zinc ion binding Source: InterPro

GO - Biological processi

  • cardiac muscle cell action potential Source: BHF-UCL
  • cardiac muscle contraction Source: BHF-UCL
  • cellular protein complex assembly Source: BHF-UCL
  • cellular protein localization Source: BHF-UCL
  • motile cilium assembly Source: BHF-UCL
  • muscle attachment Source: InterPro
  • muscle cell cellular homeostasis Source: BHF-UCL
  • muscle fiber development Source: BHF-UCL
  • muscle filament sliding Source: Reactome
  • muscle organ development Source: ProtInc
  • negative regulation of peptidyl-cysteine S-nitrosylation Source: BHF-UCL
  • negative regulation of peptidyl-serine phosphorylation Source: BHF-UCL
  • peptide biosynthetic process Source: UniProtKB
  • positive regulation of neuron differentiation Source: BHF-UCL
  • positive regulation of neuron projection development Source: BHF-UCL
  • positive regulation of sodium ion transmembrane transporter activity Source: BHF-UCL
  • regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion Source: BHF-UCL
  • regulation of cellular response to growth factor stimulus Source: BHF-UCL
  • regulation of heart rate Source: BHF-UCL
  • regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum Source: BHF-UCL
  • regulation of ryanodine-sensitive calcium-release channel activity Source: BHF-UCL
  • regulation of skeletal muscle contraction Source: BHF-UCL
  • regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion Source: BHF-UCL
  • regulation of voltage-gated calcium channel activity Source: BHF-UCL
  • response to muscle stretch Source: BHF-UCL
Complete GO annotation...

Keywords - Ligandi

Actin-binding, Calcium, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-HSA-3000171. Non-integrin membrane-ECM interactions.
R-HSA-390522. Striated Muscle Contraction.
SignaLinkiP11532.

Protein family/group databases

TCDBi8.A.66.1.2. the dystrophin (dystrophin) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Dystrophin
Gene namesi
Name:DMD
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:2928. DMD.

Subcellular locationi

  • Cell membranesarcolemma By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity
  • Cytoplasmcytoskeleton By similarity
  • 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 adult muscle, NMJ localization depends upon ANK2 presence, but not in newborn animals.By similarity

GO - Cellular componenti

  • cell-substrate junction Source: BHF-UCL
  • cell surface Source: UniProtKB
  • costamere Source: UniProtKB
  • cytoskeleton Source: ProtInc
  • cytosol Source: Reactome
  • dystrophin-associated glycoprotein complex Source: UniProtKB
  • filopodium Source: BHF-UCL
  • filopodium membrane Source: BHF-UCL
  • membrane raft Source: BHF-UCL
  • neuron projection terminus Source: BHF-UCL
  • nucleus Source: BHF-UCL
  • plasma membrane Source: BHF-UCL
  • postsynaptic membrane Source: UniProtKB-SubCell
  • protein complex Source: MGI
  • sarcolemma Source: BHF-UCL
  • synapse Source: BHF-UCL
  • syntrophin complex Source: BHF-UCL
  • Z disc Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Involvement in diseasei

Duchenne muscular dystrophy (DMD)5 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionMost 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.
See also OMIM:310200
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00514754L → R in DMD. 1 Publication1
Natural variantiVAR_023541645D → G in DMD. 1 Publication1
Natural variantiVAR_005154773K → E in DMD. 1
Natural variantiVAR_0051662305 – 2366Missing in DMD. Add BLAST62
Natural variantiVAR_0235453313C → F in DMD; results in highly reduced protein levels and expression at the sarcolemma. 2 Publications1
Natural variantiVAR_0235463335D → H in DMD; does not affect protein stability; does not affect protein expression at the sarcolemma; interaction with DAG1 is reduced. 2 Publications1
Natural variantiVAR_0235473340C → Y in DMD; results in highly reduced protein levels and expression at the sarcolemma. 2 Publications1
Becker muscular dystrophy (BMD)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:300376
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00514632 – 62Missing in BMD. Add BLAST31
Natural variantiVAR_005149168A → D in BMD. 1
Natural variantiVAR_023539171A → P in BMD. 1 Publication1
Natural variantiVAR_005150231Y → N in BMD. 1
Natural variantiVAR_005152495 – 534Missing in BMD. Add BLAST40
Natural variantiVAR_0051702921H → R in BMD. Corresponds to variant rs1800279dbSNPEnsembl.1
Natural variantiVAR_0051723421A → V in BMD. 1
Cardiomyopathy, dilated, X-linked 3B (CMD3B)4 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death.
See also OMIM:302045
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02353718K → N in CMD3B; decreased thermodynamic stability; accelerated unfolding, perturbed protein structure; no effect on anchoring function. 2 Publications1
Natural variantiVAR_023540279T → A in CMD3B. 1 Publication1
Natural variantiVAR_0235421672N → K in CMD3B. 1 PublicationCorresponds to variant rs16990264dbSNPEnsembl.1
Natural variantiVAR_0235443228F → L in CMD3B. 1 Publication1

Keywords - Diseasei

Cardiomyopathy, Disease mutation

Organism-specific databases

DisGeNETi1756.
MalaCardsiDMD.
MIMi300376. phenotype.
302045. phenotype.
310200. phenotype.
OpenTargetsiENSG00000198947.
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.
777. X-linked non-syndromic intellectual disability.
PharmGKBiPA27378.

Polymorphism and mutation databases

BioMutaiDMD.
DMDMi313104240.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000760751 – 3685DystrophinAdd BLAST3685

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei3483PhosphoserineCombined sources1
Modified residuei3490PhosphoserineCombined sources1
Modified residuei3500PhosphoserineCombined sources1
Modified residuei3612PhosphoserineCombined sources1
Modified residuei3613PhosphoserineCombined sources1
Modified residuei3617PhosphoserineCombined sources1
Modified residuei3623PhosphoserineCombined sources1
Modified residuei3624PhosphoserineCombined sources1
Modified residuei3666PhosphoserineCombined sources1
Isoform 5 (identifier: P11532-5)
Modified residuei340PhosphothreonineCombined sources1
Modified residuei344PhosphoserineCombined sources1
Modified residuei348PhosphoserineCombined sources1
Modified residuei616PhosphothreonineCombined sources1
Isoform 8 (identifier: P11532-8)
Modified residuei340PhosphothreonineCombined sources1
Modified residuei344PhosphoserineCombined sources1
Modified residuei348PhosphoserineCombined sources1
Isoform 9 (identifier: P11532-9)
Modified residuei519PhosphothreonineCombined sources1
Isoform 6 (identifier: P11532-6)
Modified residuei629PhosphothreonineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP11532.
MaxQBiP11532.
PaxDbiP11532.
PeptideAtlasiP11532.
PRIDEiP11532.

PTM databases

iPTMnetiP11532.
PhosphoSitePlusiP11532.
SwissPalmiP11532.

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

BgeeiENSG00000198947.
CleanExiHS_DMD.
ExpressionAtlasiP11532. baseline and differential.
GenevisibleiP11532. HS.

Organism-specific databases

HPAiCAB000119.
HPA002725.
HPA023885.

Interactioni

Subunit structurei

Interacts with SYNM (By similarity). Interacts with the syntrophins SNTA1, SNTB1, SNTB2, SNTG1 and SNTG2 (PubMed:7844150, PubMed:8576247). Interacts with KRT19 (PubMed:16000376). Component of the dystrophin-associated glycoprotein complex which is composed of three subcomplexes: a cytoplasmic complex comprised of DMD (or UTRN), DTNA and a number of syntrophins, such as SNTB1, SNTB2, SNTG1 and SNTG2, the transmembrane dystroglycan complex, and the sarcoglycan-sarcospan complex. Interacts with DAG1 (betaDAG1) with DMD; the interaction is inhibited by phosphorylation on the PPXY motif of DAG1 (PubMed:7592992, PubMed:11495720, PubMed:10932245). Interacts with CMYA5 (By similarity). Directly interacts with ANK2 and ANK3; these interactions do not interfere with betaDAG1-binding and are necessary for proper localization in muscle cells (By similarity). Identified in a dystroglycan complex that contains at least PRX, DRP2, UTRN, DMD and DAG1 (By similarity).By similarity6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ANK2Q014842EBI-1018651,EBI-941975
Ank3Q3T1J52EBI-1018651,EBI-2133962From a different organism.
CTNNAL1Q9UBT75EBI-295827,EBI-514206
DTNBO609413EBI-295827,EBI-740402
HAUS1Q96CS23EBI-295827,EBI-2514791
KRT19P087272EBI-295827,EBI-742756
SNTB1Q138843EBI-295827,EBI-295843

GO - Molecular functioni

  • actin binding Source: UniProtKB
  • dystroglycan binding Source: UniProtKB
  • myosin binding Source: BHF-UCL
  • nitric-oxide synthase binding Source: BHF-UCL
  • vinculin binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi108096. 51 interactors.
DIPiDIP-32593N.
IntActiP11532. 19 interactors.
MINTiMINT-109755.
STRINGi9606.ENSP00000354923.

Structurei

Secondary structure

13685
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi14 – 31Combined sources18
Turni40 – 46Combined sources7
Helixi48 – 58Combined sources11
Helixi70 – 86Combined sources17
Helixi96 – 100Combined sources5
Helixi104 – 118Combined sources15
Turni119 – 121Combined sources3
Helixi122 – 131Combined sources10
Helixi136 – 148Combined sources13
Beta strandi158 – 160Combined sources3
Helixi161 – 163Combined sources3
Helixi167 – 176Combined sources10
Helixi178 – 180Combined sources3
Helixi183 – 187Combined sources5
Helixi192 – 205Combined sources14
Helixi215 – 218Combined sources4
Beta strandi219 – 222Combined sources4
Helixi225 – 236Combined sources12
Beta strandi243 – 245Combined sources3
Helixi339 – 365Combined sources27
Helixi372 – 409Combined sources38
Helixi414 – 452Combined sources39
Helixi3050 – 3054Combined sources5
Beta strandi3061 – 3065Combined sources5
Beta strandi3071 – 3075Combined sources5
Turni3076 – 3079Combined sources4
Beta strandi3080 – 3084Combined sources5
Helixi3086 – 3094Combined sources9
Helixi3095 – 3098Combined sources4
Helixi3104 – 3118Combined sources15
Helixi3121 – 3123Combined sources3
Helixi3126 – 3135Combined sources10
Beta strandi3143 – 3146Combined sources4
Helixi3147 – 3164Combined sources18
Beta strandi3165 – 3168Combined sources4
Helixi3171 – 3186Combined sources16
Beta strandi3192 – 3195Combined sources4
Helixi3196 – 3205Combined sources10
Beta strandi3207 – 3209Combined sources3
Helixi3211 – 3222Combined sources12
Helixi3231 – 3247Combined sources17
Helixi3251 – 3254Combined sources4
Helixi3260 – 3269Combined sources10
Turni3270 – 3272Combined sources3
Helixi3278 – 3286Combined sources9
Turni3290 – 3293Combined sources4
Helixi3294 – 3304Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11532.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 240Actin-bindingAdd BLAST240
Domaini15 – 119CH 1PROSITE-ProRule annotationAdd BLAST105
Domaini134 – 237CH 2PROSITE-ProRule annotationAdd BLAST104
Repeati339 – 447Spectrin 1Add BLAST109
Repeati448 – 556Spectrin 2Add BLAST109
Repeati559 – 667Spectrin 3Add BLAST109
Repeati719 – 828Spectrin 4Add BLAST110
Repeati830 – 934Spectrin 5Add BLAST105
Repeati943 – 1045Spectrin 6Add BLAST103
Repeati1048 – 1154Spectrin 7Add BLAST107
Repeati1157 – 1263Spectrin 8Add BLAST107
Repeati1266 – 1367Spectrin 9Add BLAST102
Repeati1368 – 1463Spectrin 10Add BLAST96
Repeati1468 – 1568Spectrin 11Add BLAST101
Repeati1571 – 1676Spectrin 12Add BLAST106
Repeati1679 – 1778Spectrin 13Add BLAST100
Repeati1779 – 1874Spectrin 14Add BLAST96
Repeati1877 – 1979Spectrin 15Add BLAST103
Repeati1992 – 2101Spectrin 16Add BLAST110
Repeati2104 – 2208Spectrin 17Add BLAST105
Repeati2211 – 2318Spectrin 18Add BLAST108
Repeati2319 – 2423Spectrin 19Add BLAST105
Repeati2475 – 2577Spectrin 20Add BLAST103
Repeati2580 – 2686Spectrin 21Add BLAST107
Repeati2689 – 2802Spectrin 22Add BLAST114
Repeati2808 – 2930Spectrin 23Add BLAST123
Repeati2935 – 3040Spectrin 24Add BLAST106
Domaini3055 – 3088WWPROSITE-ProRule annotationAdd BLAST34

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni63 – 72ANK2- and ANK-3 bindingBy similarity10
Regioni1415 – 1913Interaction with SYNMBy similarityAdd BLAST499
Regioni3058 – 3408Interaction with SYNMBy similarityAdd BLAST351
Regioni3466 – 3518Binds to SNTB1Add BLAST53

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)DescriptionActionsGraphical viewLength
Zinc fingeri3307 – 3354ZZ-typePROSITE-ProRule annotationAdd BLAST48

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG4286. Eukaryota.
COG5069. LUCA.
GeneTreeiENSGT00760000119237.
HOGENOMiHOG000231175.
HOVERGENiHBG005495.
InParanoidiP11532.
KOiK10366.
PhylomeDBiP11532.
TreeFamiTF320178.

Family and domain databases

CDDicd00014. CH. 2 hits.
Gene3Di1.10.238.10. 2 hits.
1.10.418.10. 2 hits.
InterProiIPR001589. Actinin_actin-bd_CS.
IPR001715. CH-domain.
IPR016344. Dystrophin.
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]
SUPFAMiSSF47473. SSF47473. 2 hits.
SSF47576. 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. AlignAdd to basket

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

        10         20         30         40         50
MLWWEEVEDC YEREDVQKKT FTKWVNAQFS KFGKQHIENL FSDLQDGRRL
60 70 80 90 100
LDLLEGLTGQ KLPKEKGSTR VHALNNVNKA LRVLQNNNVD LVNIGSTDIV
110 120 130 140 150
DGNHKLTLGL IWNIILHWQV KNVMKNIMAG LQQTNSEKIL LSWVRQSTRN
160 170 180 190 200
YPQVNVINFT TSWSDGLALN ALIHSHRPDL FDWNSVVCQQ SATQRLEHAF
210 220 230 240 250
NIARYQLGIE KLLDPEDVDT TYPDKKSILM YITSLFQVLP QQVSIEAIQE
260 270 280 290 300
VEMLPRPPKV TKEEHFQLHH QMHYSQQITV SLAQGYERTS SPKPRFKSYA
310 320 330 340 350
YTQAAYVTTS DPTRSPFPSQ HLEAPEDKSF GSSLMESEVN LDRYQTALEE
360 370 380 390 400
VLSWLLSAED TLQAQGEISN DVEVVKDQFH THEGYMMDLT AHQGRVGNIL
410 420 430 440 450
QLGSKLIGTG KLSEDEETEV QEQMNLLNSR WECLRVASME KQSNLHRVLM
460 470 480 490 500
DLQNQKLKEL NDWLTKTEER TRKMEEEPLG PDLEDLKRQV QQHKVLQEDL
510 520 530 540 550
EQEQVRVNSL THMVVVVDES SGDHATAALE EQLKVLGDRW ANICRWTEDR
560 570 580 590 600
WVLLQDILLK WQRLTEEQCL FSAWLSEKED AVNKIHTTGF KDQNEMLSSL
610 620 630 640 650
QKLAVLKADL EKKKQSMGKL YSLKQDLLST LKNKSVTQKT EAWLDNFARC
660 670 680 690 700
WDNLVQKLEK STAQISQAVT TTQPSLTQTT VMETVTTVTT REQILVKHAQ
710 720 730 740 750
EELPPPPPQK KRQITVDSEI RKRLDVDITE LHSWITRSEA VLQSPEFAIF
760 770 780 790 800
RKEGNFSDLK EKVNAIEREK AEKFRKLQDA SRSAQALVEQ MVNEGVNADS
810 820 830 840 850
IKQASEQLNS RWIEFCQLLS ERLNWLEYQN NIIAFYNQLQ QLEQMTTTAE
860 870 880 890 900
NWLKIQPTTP SEPTAIKSQL KICKDEVNRL SDLQPQIERL KIQSIALKEK
910 920 930 940 950
GQGPMFLDAD FVAFTNHFKQ VFSDVQAREK ELQTIFDTLP PMRYQETMSA
960 970 980 990 1000
IRTWVQQSET KLSIPQLSVT DYEIMEQRLG ELQALQSSLQ EQQSGLYYLS
1010 1020 1030 1040 1050
TTVKEMSKKA PSEISRKYQS EFEEIEGRWK KLSSQLVEHC QKLEEQMNKL
1060 1070 1080 1090 1100
RKIQNHIQTL KKWMAEVDVF LKEEWPALGD SEILKKQLKQ CRLLVSDIQT
1110 1120 1130 1140 1150
IQPSLNSVNE GGQKIKNEAE PEFASRLETE LKELNTQWDH MCQQVYARKE
1160 1170 1180 1190 1200
ALKGGLEKTV SLQKDLSEMH EWMTQAEEEY LERDFEYKTP DELQKAVEEM
1210 1220 1230 1240 1250
KRAKEEAQQK EAKVKLLTES VNSVIAQAPP VAQEALKKEL ETLTTNYQWL
1260 1270 1280 1290 1300
CTRLNGKCKT LEEVWACWHE LLSYLEKANK WLNEVEFKLK TTENIPGGAE
1310 1320 1330 1340 1350
EISEVLDSLE NLMRHSEDNP NQIRILAQTL TDGGVMDELI NEELETFNSR
1360 1370 1380 1390 1400
WRELHEEAVR RQKLLEQSIQ SAQETEKSLH LIQESLTFID KQLAAYIADK
1410 1420 1430 1440 1450
VDAAQMPQEA QKIQSDLTSH EISLEEMKKH NQGKEAAQRV LSQIDVAQKK
1460 1470 1480 1490 1500
LQDVSMKFRL FQKPANFEQR LQESKMILDE VKMHLPALET KSVEQEVVQS
1510 1520 1530 1540 1550
QLNHCVNLYK SLSEVKSEVE MVIKTGRQIV QKKQTENPKE LDERVTALKL
1560 1570 1580 1590 1600
HYNELGAKVT ERKQQLEKCL KLSRKMRKEM NVLTEWLAAT DMELTKRSAV
1610 1620 1630 1640 1650
EGMPSNLDSE VAWGKATQKE IEKQKVHLKS ITEVGEALKT VLGKKETLVE
1660 1670 1680 1690 1700
DKLSLLNSNW IAVTSRAEEW LNLLLEYQKH METFDQNVDH ITKWIIQADT
1710 1720 1730 1740 1750
LLDESEKKKP QQKEDVLKRL KAELNDIRPK VDSTRDQAAN LMANRGDHCR
1760 1770 1780 1790 1800
KLVEPQISEL NHRFAAISHR IKTGKASIPL KELEQFNSDI QKLLEPLEAE
1810 1820 1830 1840 1850
IQQGVNLKEE DFNKDMNEDN EGTVKELLQR GDNLQQRITD ERKREEIKIK
1860 1870 1880 1890 1900
QQLLQTKHNA LKDLRSQRRK KALEISHQWY QYKRQADDLL KCLDDIEKKL
1910 1920 1930 1940 1950
ASLPEPRDER KIKEIDRELQ KKKEELNAVR RQAEGLSEDG AAMAVEPTQI
1960 1970 1980 1990 2000
QLSKRWREIE SKFAQFRRLN FAQIHTVREE TMMVMTEDMP LEISYVPSTY
2010 2020 2030 2040 2050
LTEITHVSQA LLEVEQLLNA PDLCAKDFED LFKQEESLKN IKDSLQQSSG
2060 2070 2080 2090 2100
RIDIIHSKKT AALQSATPVE RVKLQEALSQ LDFQWEKVNK MYKDRQGRFD
2110 2120 2130 2140 2150
RSVEKWRRFH YDIKIFNQWL TEAEQFLRKT QIPENWEHAK YKWYLKELQD
2160 2170 2180 2190 2200
GIGQRQTVVR TLNATGEEII QQSSKTDASI LQEKLGSLNL RWQEVCKQLS
2210 2220 2230 2240 2250
DRKKRLEEQK NILSEFQRDL NEFVLWLEEA DNIASIPLEP GKEQQLKEKL
2260 2270 2280 2290 2300
EQVKLLVEEL PLRQGILKQL NETGGPVLVS APISPEEQDK LENKLKQTNL
2310 2320 2330 2340 2350
QWIKVSRALP EKQGEIEAQI KDLGQLEKKL EDLEEQLNHL LLWLSPIRNQ
2360 2370 2380 2390 2400
LEIYNQPNQE GPFDVKETEI AVQAKQPDVE EILSKGQHLY KEKPATQPVK
2410 2420 2430 2440 2450
RKLEDLSSEW KAVNRLLQEL RAKQPDLAPG LTTIGASPTQ TVTLVTQPVV
2460 2470 2480 2490 2500
TKETAISKLE MPSSLMLEVP ALADFNRAWT ELTDWLSLLD QVIKSQRVMV
2510 2520 2530 2540 2550
GDLEDINEMI IKQKATMQDL EQRRPQLEEL ITAAQNLKNK TSNQEARTII
2560 2570 2580 2590 2600
TDRIERIQNQ WDEVQEHLQN RRQQLNEMLK DSTQWLEAKE EAEQVLGQAR
2610 2620 2630 2640 2650
AKLESWKEGP YTVDAIQKKI TETKQLAKDL RQWQTNVDVA NDLALKLLRD
2660 2670 2680 2690 2700
YSADDTRKVH MITENINASW RSIHKRVSER EAALEETHRL LQQFPLDLEK
2710 2720 2730 2740 2750
FLAWLTEAET TANVLQDATR KERLLEDSKG VKELMKQWQD LQGEIEAHTD
2760 2770 2780 2790 2800
VYHNLDENSQ KILRSLEGSD DAVLLQRRLD NMNFKWSELR KKSLNIRSHL
2810 2820 2830 2840 2850
EASSDQWKRL HLSLQELLVW LQLKDDELSR QAPIGGDFPA VQKQNDVHRA
2860 2870 2880 2890 2900
FKRELKTKEP VIMSTLETVR IFLTEQPLEG LEKLYQEPRE LPPEERAQNV
2910 2920 2930 2940 2950
TRLLRKQAEE VNTEWEKLNL HSADWQRKID ETLERLQELQ EATDELDLKL
2960 2970 2980 2990 3000
RQAEVIKGSW QPVGDLLIDS LQDHLEKVKA LRGEIAPLKE NVSHVNDLAR
3010 3020 3030 3040 3050
QLTTLGIQLS PYNLSTLEDL NTRWKLLQVA VEDRVRQLHE AHRDFGPASQ
3060 3070 3080 3090 3100
HFLSTSVQGP WERAISPNKV PYYINHETQT TCWDHPKMTE LYQSLADLNN
3110 3120 3130 3140 3150
VRFSAYRTAM KLRRLQKALC LDLLSLSAAC DALDQHNLKQ NDQPMDILQI
3160 3170 3180 3190 3200
INCLTTIYDR LEQEHNNLVN VPLCVDMCLN WLLNVYDTGR TGRIRVLSFK
3210 3220 3230 3240 3250
TGIISLCKAH LEDKYRYLFK QVASSTGFCD QRRLGLLLHD SIQIPRQLGE
3260 3270 3280 3290 3300
VASFGGSNIE PSVRSCFQFA NNKPEIEAAL FLDWMRLEPQ SMVWLPVLHR
3310 3320 3330 3340 3350
VAAAETAKHQ AKCNICKECP IIGFRYRSLK HFNYDICQSC FFSGRVAKGH
3360 3370 3380 3390 3400
KMHYPMVEYC TPTTSGEDVR DFAKVLKNKF RTKRYFAKHP RMGYLPVQTV
3410 3420 3430 3440 3450
LEGDNMETPV TLINFWPVDS APASSPQLSH DDTHSRIEHY ASRLAEMENS
3460 3470 3480 3490 3500
NGSYLNDSIS PNESIDDEHL LIQHYCQSLN QDSPLSQPRS PAQILISLES
3510 3520 3530 3540 3550
EERGELERIL ADLEEENRNL QAEYDRLKQQ HEHKGLSPLP SPPEMMPTSP
3560 3570 3580 3590 3600
QSPRDAELIA EAKLLRQHKG RLEARMQILE DHNKQLESQL HRLRQLLEQP
3610 3620 3630 3640 3650
QAEAKVNGTT VSSPSTSLQR SDSSQPMLLR VVGSQTSDSM GEEDLLSPPQ
3660 3670 3680
DTSTGLEEVM EQLNNSFPSS RGRNTPGKPM REDTM
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

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.Combined sources
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.Combined sources
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)DescriptionActionsGraphical viewLength
Sequence conflicti664Q → QM in CAA29544 (PubMed:3428261).Curated1
Sequence conflicti2361G → E in CAA38589 (Ref. 13) Curated1
Sequence conflicti3542P → T in AAH70078 (PubMed:15489334).Curated1
Sequence conflicti3546M → V in AAH70078 (PubMed:15489334).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02353718K → N in CMD3B; decreased thermodynamic stability; accelerated unfolding, perturbed protein structure; no effect on anchoring function. 2 Publications1
Natural variantiVAR_00514632 – 62Missing in BMD. Add BLAST31
Natural variantiVAR_00514754L → R in DMD. 1 Publication1
Natural variantiVAR_065764118W → R in a patient with Becker muscular dystrophy. 1 Publication1
Natural variantiVAR_005148133Q → P.1 PublicationCorresponds to variant rs1800256dbSNPEnsembl.1
Natural variantiVAR_023538165D → V in one patient with Becker muscular dystrophy. 1 Publication1
Natural variantiVAR_005149168A → D in BMD. 1
Natural variantiVAR_023539171A → P in BMD. 1 Publication1
Natural variantiVAR_005150231Y → N in BMD. 1
Natural variantiVAR_023540279T → A in CMD3B. 1 Publication1
Natural variantiVAR_036353334L → F in a colorectal cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_005151365Q → H.1 PublicationCorresponds to variant rs1800266dbSNPEnsembl.1
Natural variantiVAR_057642409T → S.Corresponds to variant rs34155804dbSNPEnsembl.1
Natural variantiVAR_005152495 – 534Missing in BMD. Add BLAST40
Natural variantiVAR_057643573A → V.Corresponds to variant rs5972599dbSNPEnsembl.1
Natural variantiVAR_005153623L → I.1 PublicationCorresponds to variant rs1800259dbSNPEnsembl.1
Natural variantiVAR_023541645D → G in DMD. 1 Publication1
Natural variantiVAR_062110666S → L.Corresponds to variant rs34563188dbSNPEnsembl.1
Natural variantiVAR_057644715T → S.Corresponds to variant rs16998350dbSNPEnsembl.1
Natural variantiVAR_005154773K → E in DMD. 1
Natural variantiVAR_005155784A → G.1 PublicationCorresponds to variant rs1800260dbSNPEnsembl.1
Natural variantiVAR_005156882D → G.3 PublicationsCorresponds to variant rs228406dbSNPEnsembl.1
Natural variantiVAR_0576451136T → S.Corresponds to variant rs3827462dbSNPEnsembl.1
Natural variantiVAR_0051571197V → F.1 PublicationCorresponds to variant rs1800262dbSNPEnsembl.1
Natural variantiVAR_0363541219E → Q in a breast cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_0051581245T → I.Corresponds to variant rs1800269dbSNPEnsembl.1
Natural variantiVAR_0051591278A → P.Corresponds to variant rs1800270dbSNPEnsembl.1
Natural variantiVAR_0051601377K → N.1 PublicationCorresponds to variant rs1800263dbSNPEnsembl.1
Natural variantiVAR_0576461388F → V.Corresponds to variant rs28715870dbSNPEnsembl.1
Natural variantiVAR_0051611469Q → L.1 PublicationCorresponds to variant rs1057872dbSNPEnsembl.1
Natural variantiVAR_0363551470R → H in a breast cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_0235421672N → K in CMD3B. 1 PublicationCorresponds to variant rs16990264dbSNPEnsembl.1
Natural variantiVAR_0051621745R → H.1 PublicationCorresponds to variant rs1801187dbSNPEnsembl.1
Natural variantiVAR_0051631844R → S.1 PublicationCorresponds to variant rs1801186dbSNPEnsembl.1
Natural variantiVAR_0576472108R → C.Corresponds to variant rs16990169dbSNPEnsembl.1
Natural variantiVAR_0051642155R → W.1 PublicationCorresponds to variant rs1800273dbSNPEnsembl.1
Natural variantiVAR_0363562164A → V in a colorectal cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_0051652191R → W.1 Publication1
Natural variantiVAR_0235432299N → T.1 Publication1
Natural variantiVAR_0051662305 – 2366Missing in DMD. Add BLAST62
Natural variantiVAR_0051672366K → Q.2 PublicationsCorresponds to variant rs1800275dbSNPEnsembl.1
Natural variantiVAR_0051682910E → V.1 PublicationCorresponds to variant rs41305353dbSNPEnsembl.1
Natural variantiVAR_0051692912N → D.1 PublicationCorresponds to variant rs1800278dbSNPEnsembl.1
Natural variantiVAR_0051702921H → R in BMD. Corresponds to variant rs1800279dbSNPEnsembl.1
Natural variantiVAR_0051712937Q → R.3 PublicationsCorresponds to variant rs1800280dbSNPEnsembl.1
Natural variantiVAR_0235443228F → L in CMD3B. 1 Publication1
Natural variantiVAR_0235453313C → F in DMD; results in highly reduced protein levels and expression at the sarcolemma. 2 Publications1
Natural variantiVAR_0235463335D → H in DMD; does not affect protein stability; does not affect protein expression at the sarcolemma; interaction with DAG1 is reduced. 2 Publications1
Natural variantiVAR_0235473340C → Y in DMD; results in highly reduced protein levels and expression at the sarcolemma. 2 Publications1
Natural variantiVAR_0051723421A → V in BMD. 1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0174901 – 3068Missing in isoform 5, isoform 6, isoform 7, isoform 8, isoform 9 and isoform 10. 3 PublicationsAdd BLAST3068
Alternative sequenceiVSP_0068091 – 11MLWWEEVEDCY → MED in isoform 3. 1 PublicationAdd BLAST11
Alternative sequenceiVSP_0068061M → MTEIILLIFFPAYFLN in isoform 1. Curated1
Alternative sequenceiVSP_0068081M → MSARKLRNLSYKK in isoform 2. Curated1
Alternative sequenceiVSP_0068072 – 1357Missing in isoform 1 and isoform 2. CuratedAdd BLAST1356
Alternative sequenceiVSP_0174913069 – 3075KVPYYIN → MREQLKG in isoform 5, isoform 6, isoform 7, isoform 8, isoform 9 and isoform 10. 3 Publications7
Alternative sequenceiVSP_0463193409 – 3518Missing in isoform 9 and isoform 10. CuratedAdd BLAST110
Alternative sequenceiVSP_0174923409 – 3421Missing in isoform 5 and isoform 8. 3 PublicationsAdd BLAST13
Alternative sequenceiVSP_0174933673 – 3685RNTPG…REDTM → HNVGSLFHMADDLGRAMESL VSVMTDEEGAE in isoform 5, isoform 6 and isoform 9. 3 PublicationsAdd BLAST13

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
UCSCiuc004dcm.2. human. [P11532-1]

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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108096. 51 interactors.
DIPiDIP-32593N.
IntActiP11532. 19 interactors.
MINTiMINT-109755.
STRINGi9606.ENSP00000354923.

Protein family/group databases

TCDBi8.A.66.1.2. the dystrophin (dystrophin) family.

PTM databases

iPTMnetiP11532.
PhosphoSitePlusiP11532.
SwissPalmiP11532.

Polymorphism and mutation databases

BioMutaiDMD.
DMDMi313104240.

Proteomic databases

EPDiP11532.
MaxQBiP11532.
PaxDbiP11532.
PeptideAtlasiP11532.
PRIDEiP11532.

Protocols and materials databases

DNASUi1756.
Structural Biology KnowledgebaseSearch...

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.
UCSCiuc004dcm.2. human. [P11532-1]

Organism-specific databases

CTDi1756.
DisGeNETi1756.
GeneCardsiDMD.
GeneReviewsiDMD.
HGNCiHGNC:2928. DMD.
HPAiCAB000119.
HPA002725.
HPA023885.
MalaCardsiDMD.
MIMi300376. phenotype.
300377. gene.
302045. phenotype.
310200. phenotype.
neXtProtiNX_P11532.
OpenTargetsiENSG00000198947.
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.
777. X-linked non-syndromic intellectual disability.
PharmGKBiPA27378.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4286. Eukaryota.
COG5069. LUCA.
GeneTreeiENSGT00760000119237.
HOGENOMiHOG000231175.
HOVERGENiHBG005495.
InParanoidiP11532.
KOiK10366.
PhylomeDBiP11532.
TreeFamiTF320178.

Enzyme and pathway databases

ReactomeiR-HSA-3000171. Non-integrin membrane-ECM interactions.
R-HSA-390522. Striated Muscle Contraction.
SignaLinkiP11532.

Miscellaneous databases

ChiTaRSiDMD. human.
EvolutionaryTraceiP11532.
GeneWikiiDystrophin.
GenomeRNAii1756.
PROiP11532.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000198947.
CleanExiHS_DMD.
ExpressionAtlasiP11532. baseline and differential.
GenevisibleiP11532. HS.

Family and domain databases

CDDicd00014. CH. 2 hits.
Gene3Di1.10.238.10. 2 hits.
1.10.418.10. 2 hits.
InterProiIPR001589. Actinin_actin-bd_CS.
IPR001715. CH-domain.
IPR016344. Dystrophin.
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]
SUPFAMiSSF47473. SSF47473. 2 hits.
SSF47576. 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]
ProtoNetiSearch...

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: November 30, 2016
This is version 212 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.