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P11532

- DMD_HUMAN

UniProt

P11532 - DMD_HUMAN

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Protein

Dystrophin

Gene

DMD

Organism
Homo sapiens (Human)
Status
Reviewed - 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.1 Publication

Regions

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

GO - Molecular functioni

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

GO - Biological processi

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

Keywords - Ligandi

Actin-binding, Calcium, Metal-binding, Zinc

Enzyme and pathway databases

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

Names & Taxonomyi

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

Organism-specific databases

HGNCiHGNC:2928. DMD.

Subcellular locationi

Cell membranesarcolemma; Peripheral membrane protein; Cytoplasmic side. Cytoplasmcytoskeleton. Cell junctionsynapsepostsynaptic cell membrane By similarity
Note: In muscle cells, sarcolemma localization requires the presence of ANK2, while localization to costameres requires the presence of ANK3. Localizes to neuromuscular junctions (NMJs) in the presence of ANK2 (By similarity).By similarity

GO - Cellular componenti

  1. cell junction Source: UniProtKB-KW
  2. cell surface Source: UniProtKB
  3. costamere Source: UniProtKB
  4. cytoskeleton Source: ProtInc
  5. cytosol Source: Reactome
  6. dystrophin-associated glycoprotein complex Source: UniProtKB
  7. filopodium Source: BHF-UCL
  8. filopodium membrane Source: BHF-UCL
  9. membrane raft Source: BHF-UCL
  10. nucleus Source: BHF-UCL
  11. plasma membrane Source: BHF-UCL
  12. postsynaptic membrane Source: UniProtKB-KW
  13. protein complex Source: MGI
  14. sarcolemma Source: BHF-UCL
  15. syntrophin complex 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) [MIM:310200]: Most common form of muscular dystrophy; a sex-linked recessive disorder. It typically presents in boys aged 3 to 7 year as proximal muscle weakness causing waddling gait, toe-walking, lordosis, frequent falls, and difficulty in standing up and climbing up stairs. The pelvic girdle is affected first, then the shoulder girdle. Progression is steady and most patients are confined to a wheelchair by age of 10 or 12. Flexion contractures and scoliosis ultimately occur. About 50% of patients have a lower IQ than their genetic expectations would suggest. There is no treatment.5 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti54 – 541L → R in DMD. 1 Publication
VAR_005147
Natural varianti645 – 6451D → G in DMD. 1 Publication
VAR_023541
Natural varianti773 – 7731K → E in DMD.
VAR_005154
Natural varianti2305 – 236662Missing in DMD.
VAR_005166Add
BLAST
Natural varianti3313 – 33131C → F in DMD; results in highly reduced protein levels and expression at the sarcolemma. 1 Publication
VAR_023545
Natural varianti3335 – 33351D → H in DMD; does not affect protein stability; does not affect protein expression at the sarcolemma; interaction with DAG1 is reduced. 1 Publication
VAR_023546
Natural varianti3340 – 33401C → Y in DMD; results in highly reduced protein levels and expression at the sarcolemma. 1 Publication
VAR_023547
Becker muscular dystrophy (BMD) [MIM:300376]: A neuromuscular disorder characterized by dystrophin deficiency. It appears between the age of 5 and 15 years with a proximal motor deficiency of variable progression. Heart involvement can be the initial sign. Becker muscular dystrophy has a more benign course than Duchenne muscular dystrophy.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti32 – 6231Missing in BMD.
VAR_005146Add
BLAST
Natural varianti168 – 1681A → D in BMD.
VAR_005149
Natural varianti171 – 1711A → P in BMD. 1 Publication
VAR_023539
Natural varianti231 – 2311Y → N in BMD.
VAR_005150
Natural varianti495 – 53440Missing in BMD.
VAR_005152Add
BLAST
Natural varianti2921 – 29211H → R in BMD.
Corresponds to variant rs1800279 [ dbSNP | Ensembl ].
VAR_005170
Natural varianti3421 – 34211A → V in BMD.
VAR_005172
Cardiomyopathy, dilated, X-linked 3B (CMD3B) [MIM:302045]: A disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death.3 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti18 – 181K → N in CMD3B. 1 Publication
VAR_023537
Natural varianti279 – 2791T → A in CMD3B. 1 Publication
VAR_023540
Natural varianti1672 – 16721N → K in CMD3B. 1 Publication
Corresponds to variant rs16990264 [ dbSNP | Ensembl ].
VAR_023542
Natural varianti3228 – 32281F → L in CMD3B. 1 Publication
VAR_023544

Keywords - Diseasei

Cardiomyopathy, Disease mutation

Organism-specific databases

MIMi300376. phenotype.
302045. phenotype.
310200. phenotype.
Orphaneti98895. Becker muscular dystrophy.
98896. Duchenne muscular dystrophy.
154. Familial isolated dilated cardiomyopathy.
206546. Symptomatic form of muscular dystrophy of Duchenne and Becker in female carriers.
777. X-linked non-syndromic intellectual disability.
PharmGKBiPA27378.

PTM / Processingi

Molecule processing

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

Amino acid modifications

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP11532.
PaxDbiP11532.
PRIDEiP11532.

PTM databases

PhosphoSiteiP11532.

Expressioni

Tissue specificityi

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

Developmental stagei

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

Gene expression databases

BgeeiP11532.
CleanExiHS_DMD.
ExpressionAtlasiP11532. baseline and differential.
GenevestigatoriP11532.

Organism-specific databases

HPAiCAB000119.
HPA002725.
HPA023885.

Interactioni

Subunit structurei

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

Binary interactionsi

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

Protein-protein interaction databases

BioGridi108096. 29 interactions.
IntActiP11532. 14 interactions.
MINTiMINT-109755.
STRINGi9606.ENSP00000354923.

Structurei

Secondary structure

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

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP11532.

Family & Domainsi

Domains and Repeats

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

Region

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

Sequence similaritiesi

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

Zinc finger

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

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG5069.
GeneTreeiENSGT00760000119237.
HOGENOMiHOG000231175.
HOVERGENiHBG005495.
InParanoidiP11532.
KOiK10366.
OrthoDBiEOG7V765N.
PhylomeDBiP11532.
TreeFamiTF320178.

Family and domain databases

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

Sequences (10)i

Sequence statusi: Complete.

This entry describes 10 isoformsi produced by alternative splicing. Align

Note: Additional isoforms seem to exist.

Isoform 4 (identifier: P11532) [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

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

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

Also known as: Dp71b

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

Note: No experimental confirmation available.

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

Also known as: Dp71

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

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

Also known as: Dp71a

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

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

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

Also known as: Dp60, Dp71delta110

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

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

Also known as: Dp71c

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

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

Experimental Info

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

Natural variant

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

Alternative sequence

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

Sequence databases

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

Genome annotation databases

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

Polymorphism databases

DMDMi313104240.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

DMD

Dystrophin Mutation Database

SHMPD

The Singapore human mutation and polymorphism database

Wikipedia

Dystrophin entry

Sequence databases

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

3D structure databases

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

Protein-protein interaction databases

BioGridi 108096. 29 interactions.
IntActi P11532. 14 interactions.
MINTi MINT-109755.
STRINGi 9606.ENSP00000354923.

PTM databases

PhosphoSitei P11532.

Polymorphism databases

DMDMi 313104240.

Proteomic databases

MaxQBi P11532.
PaxDbi P11532.
PRIDEi P11532.

Protocols and materials databases

DNASUi 1756.
Structural Biology Knowledgebase Search...

Genome annotation databases

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

Organism-specific databases

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

Phylogenomic databases

eggNOGi COG5069.
GeneTreei ENSGT00760000119237.
HOGENOMi HOG000231175.
HOVERGENi HBG005495.
InParanoidi P11532.
KOi K10366.
OrthoDBi EOG7V765N.
PhylomeDBi P11532.
TreeFami TF320178.

Enzyme and pathway databases

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

Miscellaneous databases

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

Gene expression databases

Bgeei P11532.
CleanExi HS_DMD.
ExpressionAtlasi P11532. baseline and differential.
Genevestigatori P11532.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "The complete sequence of dystrophin predicts a rod-shaped cytoskeletal protein."
    Koenig M., Monaco A.P., Kunkel L.M.
    Cell 53:219-228(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), VARIANTS GLY-882; LEU-1469 AND GLN-2366.
    Tissue: Muscle.
  2. "Two human cDNA molecules coding for the Duchenne muscular dystrophy (DMD) locus are highly homologous."
    Rosenthal A., Speer A., Billowitz H., Cross G.S., Forrest S.N., Davies K.E.
    Nucleic Acids Res. 17:5391-5391(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), VARIANTS PRO-133; ILE-623; GLY-784; GLY-882; PHE-1197; ASN-1377; HIS-1745 AND SER-1844.
  3. "A 71-kilodalton protein is a major product of the Duchenne muscular dystrophy gene in brain and other nonmuscle tissues."
    Lederfein D., Levy Z., Augier N., Mornet D., Morris G., Fuchs O., Yaffe D., Nudel U.
    Proc. Natl. Acad. Sci. U.S.A. 89:5346-5350(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), TISSUE SPECIFICITY.
    Tissue: Brain.
  4. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ARG-2937.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 6 AND 8).
    Tissue: Brain, Placenta and Testis.
  7. White R.A.
    Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-1411 (ISOFORMS 1 AND 2).
    Tissue: Retina.
  8. "Complete cloning of the Duchenne muscular dystrophy (DMD) cDNA and preliminary genomic organization of the DMD gene in normal and affected individuals."
    Koenig M., Hoffman E.P., Bertelson C.J., Monaco A.P., Feener C., Kunkel L.M.
    Cell 50:509-517(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-497 (ISOFORM 4).
  9. "Alternative splicing of human dystrophin mRNA generates isoforms at the carboxy terminus."
    Feener C.A., Koenig M., Kunkel L.M.
    Nature 338:509-511(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-32 (ISOFORM 3), ALTERNATIVE SPLICING.
    Tissue: Brain.
  10. "Deletions of fetal and adult muscle cDNA in Duchenne and Becker muscular dystrophy patients."
    Cross G.S., Speer A., Rosenthal A., Forrest S.M., Smith T.J., Edwards Y., Flint T., Hill D., Davies K.E.
    EMBO J. 6:3277-3283(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 404-1137 (ISOFORMS 3/4/5), VARIANT GLY-882.
  11. "Deletion screening of the Duchenne muscular dystrophy locus via multiplex DNA amplification."
    Chamberlain J.S., Gibbs R.A., Ranier J.A., Nguyen P.N., Caskey C.T.
    Nucleic Acids Res. 16:11141-11156(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 665-722; 2098-2204 AND 2305-2366.
  12. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2147-2204.
  13. "Differences in introns flanking exon 48 of the DMD/BMD gene."
    Huth A., Will K., Speer A., Bauer D.
    Submitted (MAR-1991) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2305-2364.
  14. "Cloning and characterization of alternatively spliced isoforms of Dp71."
    Austin R.C., Howard P.L., D'Souza V.N., Klamut H.J., Ray P.N.
    Hum. Mol. Genet. 4:1475-1483(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3670-3685 (ISOFORMS 1/2/3/4 AND 5), TISSUE SPECIFICITY.
    Tissue: Amnion.
  15. "Detailed analysis of the repeat domain of dystrophin reveals four potential hinge segments that may confer flexibility."
    Koenig M., Kunkel L.M.
    J. Biol. Chem. 265:4560-4566(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: ANALYSIS OF THE DOMAIN STRUCTURE.
  16. "Identification and characterization of the dystrophin anchoring site on beta-dystroglycan."
    Jung D., Yang B., Meyer J., Chamberlain J.S., Campbell K.P.
    J. Biol. Chem. 270:27305-27310(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DAG1.
  17. "Syntrophin binds to an alternatively spliced exon of dystrophin."
    Ahn A.H., Kunkel L.M.
    J. Cell Biol. 128:363-371(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SNTB1.
  18. "The three human syntrophin genes are expressed in diverse tissues, have distinct chromosomal locations, and each bind to dystrophin and its relatives."
    Ahn A.H., Feener C.A., Gussoni E., Yoshida M., Ozawa E., Kunkel L.M.
    J. Biol. Chem. 271:2724-2730(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SNTA1 AND SNTB2.
  19. "A splice variant of Dp71 lacking the syntrophin binding site is expressed in early stages of human neural development."
    Ceccarini M., Rizzo G., Rosa G., Chelucci C., Macioce P., Petrucci T.C.
    Brain Res. Dev. Brain Res. 103:77-82(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING (ISOFORMS 5 AND 9), DEVELOPMENTAL STAGE.
    Tissue: Telencephalon.
  20. "Gamma1- and gamma2-syntrophins, two novel dystrophin-binding proteins localized in neuronal cells."
    Piluso G., Mirabella M., Ricci E., Belsito A., Abbondanza C., Servidei S., Puca A.A., Tonali P., Puca G.A., Nigro V.
    J. Biol. Chem. 275:15851-15860(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SNTG1 AND SNTG2.
  21. "Expression and synthesis of alternatively spliced variants of Dp71 in adult human brain."
    Austin R.C., Morris G.E., Howard P.L., Klamut H.J., Ray P.N.
    Neuromuscul. Disord. 10:187-193(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING (ISOFORMS 9 AND 10).
    Tissue: Brain.
  22. "The interaction of dystrophin with beta-dystroglycan is regulated by tyrosine phosphorylation."
    Ilsley J.L., Sudol M., Winder S.J.
    Cell. Signal. 13:625-632(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DAG1.
  23. "Specific interaction of the actin-binding domain of dystrophin with intermediate filaments containing keratin 19."
    Stone M.R., O'Neill A., Catino D., Bloch R.J.
    Mol. Biol. Cell 16:4280-4293(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KRT19, TISSUE SPECIFICITY.
  24. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  25. "Role of dystrophin and utrophin for assembly and function of the dystrophin glycoprotein complex in non-muscle tissue."
    Haenggi T., Fritschy J.M.
    Cell. Mol. Life Sci. 63:1614-1631(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN THE DYSTROPHIN-ASSOCIATED GLYCOPROTEIN COMPLEX.
  26. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3483; SER-3613; SER-3617; SER-3623 AND SER-3666, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-340; SER-344 AND SER-348 (ISOFORMS 5 AND 8), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  27. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  28. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3612; SER-3613 AND SER-3623, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  29. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  30. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  31. "Structure of a WW domain containing fragment of dystrophin in complex with beta-dystroglycan."
    Huang X., Poy F., Zhang R., Joachimiak A., Sudol M., Eck M.J.
    Nat. Struct. Biol. 7:634-638(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 3046-3306 IN COMPLEX WITH DAG1.
  32. "The structure of the N-terminal actin-binding domain of human dystrophin and how mutations in this domain may cause Duchenne or Becker muscular dystrophy."
    Norwood F.L.M., Sutherland-Smith A.J., Keep N.H., Kendrick-Jones J.
    Structure 8:481-491(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-246.
  33. "Searching for the 1 in 2,400,000: a review of dystrophin gene point mutations."
    Roberts R.G., Gardner R.J., Bobrow M.
    Hum. Mutat. 4:1-11(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON DMD VARIANTS.
  34. "Microlesions and polymorphisms in the Duchenne/Becker muscular dystrophy gene."
    Rininsland F., Reiss J.
    Hum. Genet. 94:111-116(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON VARIANTS.
  35. "A missense mutation in the dystrophin gene in a Duchenne muscular dystrophy patient."
    Prior T.W., Papp A.C., Snyder P.J., Burghes A.H.M., Bartolo C., Sedra M.S., Western L.M., Mendell J.R.
    Nat. Genet. 4:357-360(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT DMD ARG-54.
  36. "Identification of a missense mutation, single base deletion and a polymorphism in the dystrophin exon 16."
    Prior T.W., Bartolo C., Papp A.C., Snyder P.J., Sedra M.S., Burghes A.H., Mendell J.R.
    Hum. Mol. Genet. 3:1173-1174(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT DMD GLY-645.
  37. "Novel small mutations along the DMD/BMD gene associated with different phenotypes."
    Nigro V., Nigro G., Esposito M.G., Comi L.I., Molinari A.M., Puca G.A., Politano L.
    Hum. Mol. Genet. 3:1907-1908(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS HIS-365; TRP-2191 AND ARG-2937.
  38. "A cysteine 3340 substitution in the dystroglycan-binding domain of dystrophin associated with Duchenne muscular dystrophy, mental retardation and absence of the ERG b-wave."
    Lenk U., Oexle K., Voit T., Ancker U., Hellner K.A., Speer A., Hubner C.
    Hum. Mol. Genet. 5:973-975(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT DMD TYR-3340.
  39. "Evidence for a dystrophin missense mutation as a cause of X-linked dilated cardiomyopathy."
    Ortiz-Lopez R., Li H., Su J., Goytia V., Towbin J.A.
    Circulation 95:2434-2440(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT CMD3B ALA-279.
  40. "A dystrophin missense mutation showing persistence of dystrophin and dystrophin-associated proteins yet a severe phenotype."
    Goldberg L.R., Hausmanowa-Petrusewicz I., Fidzianska A., Duggan D.J., Steinberg L.S., Hoffman E.P.
    Ann. Neurol. 44:971-976(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT DMD HIS-3335.
  41. "Identification of point mutations in Turkish DMD/BMD families using multiplex-single stranded conformation analysis (SSCA)."
    Eraslan S., Kayserili H., Apak M.Y., Kirdar B.
    Eur. J. Hum. Genet. 7:765-770(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT BMD PRO-171.
  42. "Comprehensive mutation scanning of the dystrophin gene in patients with nonsyndromic X-linked dilated cardiomyopathy."
    Feng J., Yan J.Y., Buzin C.H., Sommer S.S., Towbin J.A.
    J. Am. Coll. Cardiol. 40:1120-1124(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT CMD3B LYS-1672.
  43. "Mutations in the dystrophin gene are associated with sporadic dilated cardiomyopathy."
    Feng J., Yan J., Buzin C.H., Towbin J.A., Sommer S.S.
    Mol. Genet. Metab. 77:119-126(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS CMD3B ASN-18 AND LEU-3228, VARIANTS TRP-2155; THR-2299; GLN-2366; VAL-2910; ASP-2912 AND ARG-2937.
  44. Cited for: VARIANT DMD PHE-3313, VARIANT VAL-165.
  45. Cited for: VARIANTS [LARGE SCALE ANALYSIS] PHE-334; GLN-1219; HIS-1470 AND VAL-2164.
  46. "Clinical and molecular characterization of a cohort of patients with novel nucleotide alterations of the Dystrophin gene detected by direct sequencing."
    Magri F., Del Bo R., D'Angelo M.G., Govoni A., Ghezzi S., Gandossini S., Sciacco M., Ciscato P., Bordoni A., Tedeschi S., Fortunato F., Lucchini V., Cereda M., Corti S., Moggio M., Bresolin N., Comi G.P.
    BMC Med. Genet. 12:37-37(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT ARG-118.
  47. Cited for: CHARACTERIZATION OF VARIANTS DMD PHE-3313; HIS-3335 AND TYR-3340.

Entry informationi

Entry nameiDMD_HUMAN
AccessioniPrimary (citable) accession number: P11532
Secondary accession number(s): E9PDN1
, Q02295, Q14169, Q14170, Q5JYU0, Q6NSJ9, Q7KZ48, Q8N754, Q9UCW3, Q9UCW4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: November 30, 2010
Last modified: October 29, 2014
This is version 189 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

The DMD gene is the largest known gene in humans. It is 2.4 million base-pairs in size, comprises 79 exons and takes over 16 hours to be transcribed and cotranscriptionally spliced.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3