Reviewed, UniProtKB/Swiss-Prot P11532 (DMD_HUMAN)

Names and origin

Protein names

Recommended name:
    Dystrophin

Gene names

Name:

DMD

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	3685 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	May play a role in anchoring the cytoskeleton to the plasma membrane.
Subunit structure	Interacts with the syntrophins SNTA1, SNTB1, SNTB2, SNTG1 and SNTG2. Interacts with KRT19. Interacts with SYNM By similarity.
Subcellular location	Cell membrane › sarcolemma; Peripheral membrane protein; Cytoplasmic side. Cytoplasm › cytoskeleton.
Tissue specificity	Expressed in muscle fibers accumulating in the costameres of myoplasm at the sarcolemma. Expressed in brain, muscle, kidney, lung and testis. Isoform 5 is expressed in heart, brain, liver, testis and hepatoma cells. Most tissues contain transcripts of multiple isoforms, however only isoform 5 is detected in heart and liver. Ref.12 Ref.16
Involvement in disease	Defects in DMD are the cause of Duchenne muscular dystrophy (DMD) [MIM:310200]. DMD is the 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. Ref.25 Ref.26 Ref.28 Ref.30 Defects in DMD are the cause of Becker muscular dystrophy (BMD) [MIM:300376]. BMD resembles DMD in hereditary and clinical features but is later in onset and more benign. Ref.31 Defects in DMD are a cause of cardiomyopathy dilated X-linked type 3B (CMD3B) [MIM:302045]; also known as X-linked dilated cardiomyopathy (XLCM). Dilated cardiomyopathy is a disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death. Ref.29 Ref.32 Ref.33
Miscellaneous	The DMD gene is the largest known gene in humans. It is 2.4 million base-pairs in size, comprises 79 exons and takes over 16 hours to be transcribed and cotranscriptionally spliced.
Sequence similarities	Contains 2 CH (calponin-homology) domains. Contains 22 spectrin repeats. Contains 1 WW domain. Contains 1 ZZ-type zinc finger.

Ontologies

Keywords
Cellular component	Cell membrane Cytoplasm Cytoskeleton Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Cardiomyopathy Disease mutation
Domain	Repeat Zinc-finger
Ligand	Actin-binding Calcium Metal-binding Zinc
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	muscle organ development Non-traceable author statement. Source: ProtInc peptide biosynthetic process Ref.16 Inferred from direct assay. Source: UniProtKB
Cellular component	cell surface Inferred from direct assay. Source: UniProtKB costamere Ref.16 Inferred from direct assay. Source: UniProtKB cytoskeleton Ref.1 Traceable author statement. Source: ProtInc dystrophin-associated glycoprotein complex Traceable author statement. Source: UniProtKB internal side of plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell sarcolemma Inferred from direct assay. Source: UniProtKB
Molecular function	actin binding Traceable author statement. Source: UniProtKB calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW nitric-oxide synthase binding Inferred from sequence or structural similarity. Source: UniProtKB structural constituent of cytoskeleton Ref.1 Traceable author statement. Source: ProtInc structural constituent of muscle Ref.16 Inferred from direct assay. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ANK2	Q01484	1	EBI-1018651,EBI-941975
Ank3	Q3T1J5	1	EBI-1018651,EBI-2133962	From a different organism.
Dtnb	O70585	1	EBI-295827,EBI-349714	From a different organism.
KRT19	P08727	1	EBI-295827,EBI-742756
SNTB1	Q13884	3	EBI-295827,EBI-295843
SNTB2	Q13425	1	EBI-295827,EBI-80411

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.

Isoform 4 (identifier: P11532-1)

Also known as: Dystrophin-4;

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

Isoform 1 (identifier: P11532-2)

Also known as: Dystrophin-1;

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

Isoform 2 (identifier: P11532-3)

Also known as: Dystrophin-2;

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

Isoform 3 (identifier: P11532-4)

Also known as: Dystrophin-3;

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

Isoform 5 (identifier: P11532-5)

Also known as: Dp71;

The sequence of this isoform differs from the canonical sequence as follows:
     1-3068: Missing.
     3069-3075: KVPYYIN → MREQLKG
     3410-3422: Missing.
     3673-3685: RNTPGKPMREDTM → HNVGSLFHMADDLGRAMESLVSVMTDEEGAE

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 3685

3685

Dystrophin

PRO_0000076075

Regions

Domain

1 – 240

240

Actin-binding

Domain

15 – 119

105

CH 1

Domain

134 – 237

104

CH 2

Repeat

339 – 447

109

Spectrin 1

Repeat

448 – 556

109

Spectrin 2

Repeat

559 – 667

109

Spectrin 3

Repeat

719 – 828

110

Spectrin 4

Repeat

830 – 934

105

Spectrin 5

Repeat

943 – 1045

103

Spectrin 6

Repeat

1048 – 1154

107

Spectrin 7

Repeat

1157 – 1263

107

Spectrin 8

Repeat

1266 – 1367

102

Spectrin 9

Repeat

1468 – 1568

101

Spectrin 10

Repeat

1571 – 1676

106

Spectrin 11

Repeat

1679 – 1780

102

Spectrin 12

Repeat

1877 – 1979

103

Spectrin 13

Repeat

2011 – 2101

91

Spectrin 14

Repeat

2104 – 2208

105

Spectrin 15

Repeat

2211 – 2318

108

Spectrin 16

Repeat

2475 – 2577

103

Spectrin 17

Repeat

2580 – 2686

107

Spectrin 18

Repeat

2689 – 2802

114

Spectrin 19

Repeat

2805 – 2907

103

Spectrin 20

Repeat

2909 – 2931

23

Spectrin 21

Repeat

2934 – 3040

107

Spectrin 22

Domain

3055 – 3088

34

WW

Zinc finger

3307 – 3354

48

ZZ-type

Region

1415 – 1913

499

Interaction with SYNM By similarity

Region

3058 – 3408

351

Interaction with SYNM By similarity

Region

3466 – 3518

53

Binds to SNTB1

Amino acid modifications

Modified residue

1590

1

Phosphothreonine Ref.17

Modified residue

3483

1

Phosphoserine Ref.20

Modified residue

3613

1

Phosphoserine Ref.20 Ref.19

Modified residue

3617

1

Phosphoserine Ref.20

Modified residue

3621

1

Phosphoserine Ref.18

Modified residue

3623

1

Phosphoserine Ref.20 Ref.18

Modified residue

3624

1

Phosphoserine By similarity

Modified residue

3652

1

Phosphothreonine Ref.20

Modified residue

3666

1

Phosphoserine Ref.20

Natural variations

Alternative sequence

1 – 3068

3068

Missing in isoform 5.

VSP_017490

Alternative sequence

1 – 11

11

MLWWEEVEDCY → MED in isoform 3.

VSP_006809

Alternative sequence

1

1

M → MTEIILLIFFPAYFLN in isoform 1.

VSP_006806

Alternative sequence

1

1

M → MSARKLRNLSYKK in isoform 2.

VSP_006808

Alternative sequence

2 – 1357

1356

Missing in isoform 1 and isoform 2.

VSP_006807

Alternative sequence

3069 – 3075

7

KVPYYIN → MREQLKG in isoform 5.

VSP_017491

Alternative sequence

3410 – 3422

13

Missing in isoform 5.

VSP_017492

Alternative sequence

3673 – 3685

13

RNTPG…REDTM → HNVGSLFHMADDLGRAMESL VSVMTDEEGAE in isoform 5.

VSP_017493

Natural variant

18

1

K → N in CMD3B. Ref.33

VAR_023537

Natural variant

32 – 62

31

Missing in BMD.

VAR_005146

Natural variant

54

1

L → R in DMD. Ref.25

VAR_005147

Natural variant

133

1

Q → P: dbSNP rs1800256. Ref.2

VAR_005148

Natural variant

165

1

D → V in one patient with Becker muscular dystrophy. Ref.34

VAR_023538

Natural variant

168

1

A → D in BMD.

VAR_005149

Natural variant

171

1

A → P in BMD. Ref.31

VAR_023539

Natural variant

231

1

Y → N in BMD.

VAR_005150

Natural variant

279

1

T → A in CMD3B. Ref.29

VAR_023540

Natural variant

334

1

L → F in a colorectal cancer sample; somatic mutation. Ref.35

VAR_036353

Natural variant

365

1

Q → H: dbSNP rs1800266. Ref.27

VAR_005151

Natural variant

409

1

T → S: dbSNP rs34155804.

VAR_057642

Natural variant

495 – 534

40

Missing in BMD.

VAR_005152

Natural variant

573

1

A → V: dbSNP rs5972599.

VAR_057643

Natural variant

623

1

L → I: dbSNP rs1800259. Ref.2

VAR_005153

Natural variant

645

1

D → G in DMD. Ref.26

VAR_023541

Natural variant

715

1

T → S: dbSNP rs16998350.

VAR_057644

Natural variant

773

1

K → E in DMD.

VAR_005154

Natural variant

784

1

A → G: dbSNP rs1800260. Ref.2

VAR_005155

Natural variant

882

1

G → D: dbSNP rs228406. Ref.4

VAR_005156

Natural variant

1136

1

T → S: dbSNP rs3827462.

VAR_057645

Natural variant

1197

1

V → F: dbSNP rs1800262. Ref.2

VAR_005157

Natural variant

1219

1

E → Q in a breast cancer sample; somatic mutation. Ref.35

VAR_036354

Natural variant

1245

1

T → I: dbSNP rs1800269.

VAR_005158

Natural variant

1278

1

A → P: dbSNP rs1800270.

VAR_005159

Natural variant

1377

1

K → N: dbSNP rs1800263. Ref.2

VAR_005160

Natural variant

1388

1

F → V: dbSNP rs28715870.

VAR_057646

Natural variant

1469

1

Q → L: dbSNP rs1057872. Ref.1

VAR_005161

Natural variant

1470

1

R → H in a breast cancer sample; somatic mutation. Ref.35

VAR_036355

Natural variant

1672

1

N → K in CMD3B. dbSNP rs16990264. Ref.32

VAR_023542

Natural variant

1745

1

R → H: dbSNP rs1801187. Ref.2

VAR_005162

Natural variant

1844

1

R → S: dbSNP rs1801186. Ref.2

VAR_005163

Natural variant

2108

1

R → C: dbSNP rs16990169.

VAR_057647

Natural variant

2155

1

R → W: dbSNP rs1800273. Ref.33

VAR_005164

Natural variant

2164

1

A → V in a colorectal cancer sample; somatic mutation. Ref.35

VAR_036356

Natural variant

2191

1

R → W

VAR_005165

Natural variant

2299

1

N → T

VAR_023543

Natural variant

2305 – 2366

62

Missing in DMD.

VAR_005166

Natural variant

2366

1

K → Q: dbSNP rs1800275. Ref.33 Ref.1

VAR_005167

Natural variant

2910

1

E → V

VAR_005168

Natural variant

2912

1

N → D: dbSNP rs1800278. Ref.33

VAR_005169

Natural variant

2921

1

H → R in BMD. dbSNP rs1800279.

VAR_005170

Natural variant

2937

1

Q → R: dbSNP rs1800280. Ref.33 Ref.27 Ref.4

VAR_005171

Natural variant

3228

1

F → L in CMD3B. Ref.33

VAR_023544

Natural variant

3313

1

C → F in one patient with Duchenne muscular dystrophy. Ref.34

VAR_023545

Natural variant

3335

1

D → H in DMD. Ref.30

VAR_023546

Natural variant

3340

1

C → Y in DMD. Ref.28

VAR_023547

Natural variant

3421

1

A → V in BMD.

VAR_005172

Experimental info

Sequence conflict

664

1

Q → QM in CAA29544. Ref.8

Sequence conflict

2361

1

G → E in CAA38589. Ref.11

Secondary structure

1

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3685

Helix Strand Turn

Details...

Helix

14 – 31

18

Turn

40 – 46

7

Helix

48 – 58

11

Helix

70 – 86

17

Helix

96 – 100

5

Helix

104 – 118

15

Turn

119 – 121

3

Helix

122 – 131

10

Helix

136 – 148

13

Beta strand

158 – 160

3

Helix

161 – 163

3

Helix

167 – 176

10

Helix

178 – 180

3

Helix

183 – 187

5

Helix

192 – 205

14

Helix

215 – 218

4

Beta strand

219 – 222

4

Helix

225 – 236

12

Beta strand

243 – 245

3

Helix

3050 – 3054

5

Beta strand

3061 – 3065

5

Beta strand

3071 – 3075

5

Turn

3076 – 3079

4

Beta strand

3080 – 3084

5

Helix

3086 – 3094

9

Helix

3095 – 3098

4

Helix

3104 – 3118

15

Helix

3121 – 3123

3

Helix

3126 – 3135

10

Beta strand

3143 – 3146

4

Helix

3147 – 3164

18

Helix

3171 – 3186

16

Beta strand

3192 – 3195

4

Helix

3196 – 3205

10

Beta strand

3207 – 3209

3

Helix

3211 – 3222

12

Helix

3231 – 3247

17

Helix

3251 – 3254

4

Helix

3260 – 3269

10

Turn

3270 – 3272

3

Helix

3278 – 3286

9

Turn

3290 – 3293

4

Helix

3294 – 3304

11

Sequences

	Sequence		Length	Mass (Da)
	Isoform 4 (Dystrophin-4) [UniParc]. Last modified September 27, 2005. Version 2. Checksum: 57F78E3EA917CC57	FASTA	3,685	426,692
	10 20 30 40 50 60 MLWWEEVEDC YEREDVQKKT FTKWVNAQFS KFGKQHIENL FSDLQDGRRL LDLLEGLTGQ 70 80 90 100 110 120 KLPKEKGSTR VHALNNVNKA LRVLQNNNVD LVNIGSTDIV DGNHKLTLGL IWNIILHWQV 130 140 150 160 170 180 KNVMKNIMAG LQQTNSEKIL LSWVRQSTRN YPQVNVINFT TSWSDGLALN ALIHSHRPDL 190 200 210 220 230 240 FDWNSVVCQQ SATQRLEHAF NIARYQLGIE KLLDPEDVDT TYPDKKSILM YITSLFQVLP 250 260 270 280 290 300 QQVSIEAIQE VEMLPRPPKV TKEEHFQLHH QMHYSQQITV SLAQGYERTS SPKPRFKSYA 310 320 330 340 350 360 YTQAAYVTTS DPTRSPFPSQ HLEAPEDKSF GSSLMESEVN LDRYQTALEE VLSWLLSAED 370 380 390 400 410 420 TLQAQGEISN DVEVVKDQFH THEGYMMDLT AHQGRVGNIL QLGSKLIGTG KLSEDEETEV 430 440 450 460 470 480 QEQMNLLNSR WECLRVASME KQSNLHRVLM DLQNQKLKEL NDWLTKTEER TRKMEEEPLG 490 500 510 520 530 540 PDLEDLKRQV QQHKVLQEDL EQEQVRVNSL THMVVVVDES SGDHATAALE EQLKVLGDRW 550 560 570 580 590 600 ANICRWTEDR WVLLQDILLK WQRLTEEQCL FSAWLSEKED AVNKIHTTGF KDQNEMLSSL 610 620 630 640 650 660 QKLAVLKADL EKKKQSMGKL YSLKQDLLST LKNKSVTQKT EAWLDNFARC WDNLVQKLEK 670 680 690 700 710 720 STAQISQAVT TTQPSLTQTT VMETVTTVTT REQILVKHAQ EELPPPPPQK KRQITVDSEI 730 740 750 760 770 780 RKRLDVDITE LHSWITRSEA VLQSPEFAIF RKEGNFSDLK EKVNAIEREK AEKFRKLQDA 790 800 810 820 830 840 SRSAQALVEQ MVNEGVNADS IKQASEQLNS RWIEFCQLLS ERLNWLEYQN NIIAFYNQLQ 850 860 870 880 890 900 QLEQMTTTAE NWLKIQPTTP SEPTAIKSQL KICKDEVNRL SGLQPQIERL KIQSIALKEK 910 920 930 940 950 960 GQGPMFLDAD FVAFTNHFKQ VFSDVQAREK ELQTIFDTLP PMRYQETMSA IRTWVQQSET 970 980 990 1000 1010 1020 KLSIPQLSVT DYEIMEQRLG ELQALQSSLQ EQQSGLYYLS TTVKEMSKKA PSEISRKYQS 1030 1040 1050 1060 1070 1080 EFEEIEGRWK KLSSQLVEHC QKLEEQMNKL RKIQNHIQTL KKWMAEVDVF LKEEWPALGD 1090 1100 1110 1120 1130 1140 SEILKKQLKQ CRLLVSDIQT IQPSLNSVNE GGQKIKNEAE PEFASRLETE LKELNTQWDH 1150 1160 1170 1180 1190 1200 MCQQVYARKE ALKGGLEKTV SLQKDLSEMH EWMTQAEEEY LERDFEYKTP DELQKAVEEM 1210 1220 1230 1240 1250 1260 KRAKEEAQQK EAKVKLLTES VNSVIAQAPP VAQEALKKEL ETLTTNYQWL CTRLNGKCKT 1270 1280 1290 1300 1310 1320 LEEVWACWHE LLSYLEKANK WLNEVEFKLK TTENIPGGAE EISEVLDSLE NLMRHSEDNP 1330 1340 1350 1360 1370 1380 NQIRILAQTL TDGGVMDELI NEELETFNSR WRELHEEAVR RQKLLEQSIQ SAQETEKSLH 1390 1400 1410 1420 1430 1440 LIQESLTFID KQLAAYIADK VDAAQMPQEA QKIQSDLTSH EISLEEMKKH NQGKEAAQRV 1450 1460 1470 1480 1490 1500 LSQIDVAQKK LQDVSMKFRL FQKPANFEQR LQESKMILDE VKMHLPALET KSVEQEVVQS 1510 1520 1530 1540 1550 1560 QLNHCVNLYK SLSEVKSEVE MVIKTGRQIV QKKQTENPKE LDERVTALKL HYNELGAKVT 1570 1580 1590 1600 1610 1620 ERKQQLEKCL KLSRKMRKEM NVLTEWLAAT DMELTKRSAV EGMPSNLDSE VAWGKATQKE 1630 1640 1650 1660 1670 1680 IEKQKVHLKS ITEVGEALKT VLGKKETLVE DKLSLLNSNW IAVTSRAEEW LNLLLEYQKH 1690 1700 1710 1720 1730 1740 METFDQNVDH ITKWIIQADT LLDESEKKKP QQKEDVLKRL KAELNDIRPK VDSTRDQAAN 1750 1760 1770 1780 1790 1800 LMANRGDHCR KLVEPQISEL NHRFAAISHR IKTGKASIPL KELEQFNSDI QKLLEPLEAE 1810 1820 1830 1840 1850 1860 IQQGVNLKEE DFNKDMNEDN EGTVKELLQR GDNLQQRITD ERKREEIKIK QQLLQTKHNA 1870 1880 1890 1900 1910 1920 LKDLRSQRRK KALEISHQWY QYKRQADDLL KCLDDIEKKL ASLPEPRDER KIKEIDRELQ 1930 1940 1950 1960 1970 1980 KKKEELNAVR RQAEGLSEDG AAMAVEPTQI QLSKRWREIE SKFAQFRRLN FAQIHTVREE 1990 2000 2010 2020 2030 2040 TMMVMTEDMP LEISYVPSTY LTEITHVSQA LLEVEQLLNA PDLCAKDFED LFKQEESLKN 2050 2060 2070 2080 2090 2100 IKDSLQQSSG RIDIIHSKKT AALQSATPVE RVKLQEALSQ LDFQWEKVNK MYKDRQGRFD 2110 2120 2130 2140 2150 2160 RSVEKWRRFH YDIKIFNQWL TEAEQFLRKT QIPENWEHAK YKWYLKELQD GIGQRQTVVR 2170 2180 2190 2200 2210 2220 TLNATGEEII QQSSKTDASI LQEKLGSLNL RWQEVCKQLS DRKKRLEEQK NILSEFQRDL 2230 2240 2250 2260 2270 2280 NEFVLWLEEA DNIASIPLEP GKEQQLKEKL EQVKLLVEEL PLRQGILKQL NETGGPVLVS 2290 2300 2310 2320 2330 2340 APISPEEQDK LENKLKQTNL QWIKVSRALP EKQGEIEAQI KDLGQLEKKL EDLEEQLNHL 2350 2360 2370 2380 2390 2400 LLWLSPIRNQ LEIYNQPNQE GPFDVKETEI AVQAKQPDVE EILSKGQHLY KEKPATQPVK 2410 2420 2430 2440 2450 2460 RKLEDLSSEW KAVNRLLQEL RAKQPDLAPG LTTIGASPTQ TVTLVTQPVV TKETAISKLE 2470 2480 2490 2500 2510 2520 MPSSLMLEVP ALADFNRAWT ELTDWLSLLD QVIKSQRVMV GDLEDINEMI IKQKATMQDL 2530 2540 2550 2560 2570 2580 EQRRPQLEEL ITAAQNLKNK TSNQEARTII TDRIERIQNQ WDEVQEHLQN RRQQLNEMLK 2590 2600 2610 2620 2630 2640 DSTQWLEAKE EAEQVLGQAR AKLESWKEGP YTVDAIQKKI TETKQLAKDL RQWQTNVDVA 2650 2660 2670 2680 2690 2700 NDLALKLLRD YSADDTRKVH MITENINASW RSIHKRVSER EAALEETHRL LQQFPLDLEK 2710 2720 2730 2740 2750 2760 FLAWLTEAET TANVLQDATR KERLLEDSKG VKELMKQWQD LQGEIEAHTD VYHNLDENSQ 2770 2780 2790 2800 2810 2820 KILRSLEGSD DAVLLQRRLD NMNFKWSELR KKSLNIRSHL EASSDQWKRL HLSLQELLVW 2830 2840 2850 2860 2870 2880 LQLKDDELSR QAPIGGDFPA VQKQNDVHRA FKRELKTKEP VIMSTLETVR IFLTEQPLEG 2890 2900 2910 2920 2930 2940 LEKLYQEPRE LPPEERAQNV TRLLRKQAEE VNTEWEKLNL HSADWQRKID ETLERLQELQ 2950 2960 2970 2980 2990 3000 EATDELDLKL RQAEVIKGSW QPVGDLLIDS LQDHLEKVKA LRGEIAPLKE NVSHVNDLAR 3010 3020 3030 3040 3050 3060 QLTTLGIQLS PYNLSTLEDL NTRWKLLQVA VEDRVRQLHE AHRDFGPASQ HFLSTSVQGP 3070 3080 3090 3100 3110 3120 WERAISPNKV PYYINHETQT TCWDHPKMTE LYQSLADLNN VRFSAYRTAM KLRRLQKALC 3130 3140 3150 3160 3170 3180 LDLLSLSAAC DALDQHNLKQ NDQPMDILQI INCLTTIYDR LEQEHNNLVN VPLCVDMCLN 3190 3200 3210 3220 3230 3240 WLLNVYDTGR TGRIRVLSFK TGIISLCKAH LEDKYRYLFK QVASSTGFCD QRRLGLLLHD 3250 3260 3270 3280 3290 3300 SIQIPRQLGE VASFGGSNIE PSVRSCFQFA NNKPEIEAAL FLDWMRLEPQ SMVWLPVLHR 3310 3320 3330 3340 3350 3360 VAAAETAKHQ AKCNICKECP IIGFRYRSLK HFNYDICQSC FFSGRVAKGH KMHYPMVEYC 3370 3380 3390 3400 3410 3420 TPTTSGEDVR DFAKVLKNKF RTKRYFAKHP RMGYLPVQTV LEGDNMETPV TLINFWPVDS 3430 3440 3450 3460 3470 3480 APASSPQLSH DDTHSRIEHY ASRLAEMENS NGSYLNDSIS PNESIDDEHL LIQHYCQSLN 3490 3500 3510 3520 3530 3540 QDSPLSQPRS PAQILISLES EERGELERIL ADLEEENRNL QAEYDRLKQQ HEHKGLSPLP 3550 3560 3570 3580 3590 3600 SPPEMMPTSP QSPRDAELIA EAKLLRQHKG RLEARMQILE DHNKQLESQL HRLRQLLEQP 3610 3620 3630 3640 3650 3660 QAEAKVNGTT VSSPSTSLQR SDSSQPMLLR VVGSQTSDSM GEEDLLSPPQ DTSTGLEEVM 3670 3680 EQLNNSFPSS RGRNTPGKPM REDTM
	Isoform 1 (Dystrophin-1). Checksum: 50AF557D10DD0B23	FASTA	2,344	271,391
	10 20 30 40 50 60 MTEIILLIFF PAYFLNAVRR QKLLEQSIQS AQETEKSLHL IQESLTFIDK QLAAYIADKV 70 80 90 100 110 120 DAAQMPQEAQ KIQSDLTSHE ISLEEMKKHN QGKEAAQRVL SQIDVAQKKL QDVSMKFRLF 130 140 150 160 170 180 QKPANFEQRL QESKMILDEV KMHLPALETK SVEQEVVQSQ LNHCVNLYKS LSEVKSEVEM 190 200 210 220 230 240 VIKTGRQIVQ KKQTENPKEL DERVTALKLH YNELGAKVTE RKQQLEKCLK LSRKMRKEMN 250 260 270 280 290 300 VLTEWLAATD MELTKRSAVE GMPSNLDSEV AWGKATQKEI EKQKVHLKSI TEVGEALKTV 310 320 330 340 350 360 LGKKETLVED KLSLLNSNWI AVTSRAEEWL NLLLEYQKHM ETFDQNVDHI TKWIIQADTL 370 380 390 400 410 420 LDESEKKKPQ QKEDVLKRLK AELNDIRPKV DSTRDQAANL MANRGDHCRK LVEPQISELN 430 440 450 460 470 480 HRFAAISHRI KTGKASIPLK ELEQFNSDIQ KLLEPLEAEI QQGVNLKEED FNKDMNEDNE 490 500 510 520 530 540 GTVKELLQRG DNLQQRITDE RKREEIKIKQ QLLQTKHNAL KDLRSQRRKK ALEISHQWYQ 550 560 570 580 590 600 YKRQADDLLK CLDDIEKKLA SLPEPRDERK IKEIDRELQK KKEELNAVRR QAEGLSEDGA 610 620 630 640 650 660 AMAVEPTQIQ LSKRWREIES KFAQFRRLNF AQIHTVREET MMVMTEDMPL EISYVPSTYL 670 680 690 700 710 720 TEITHVSQAL LEVEQLLNAP DLCAKDFEDL FKQEESLKNI KDSLQQSSGR IDIIHSKKTA 730 740 750 760 770 780 ALQSATPVER VKLQEALSQL DFQWEKVNKM YKDRQGRFDR SVEKWRRFHY DIKIFNQWLT 790 800 810 820 830 840 EAEQFLRKTQ IPENWEHAKY KWYLKELQDG IGQRQTVVRT LNATGEEIIQ QSSKTDASIL 850 860 870 880 890 900 QEKLGSLNLR WQEVCKQLSD RKKRLEEQKN ILSEFQRDLN EFVLWLEEAD NIASIPLEPG 910 920 930 940 950 960 KEQQLKEKLE QVKLLVEELP LRQGILKQLN ETGGPVLVSA PISPEEQDKL ENKLKQTNLQ 970 980 990 1000 1010 1020 WIKVSRALPE KQGEIEAQIK DLGQLEKKLE DLEEQLNHLL LWLSPIRNQL EIYNQPNQEG 1030 1040 1050 1060 1070 1080 PFDVKETEIA VQAKQPDVEE ILSKGQHLYK EKPATQPVKR KLEDLSSEWK AVNRLLQELR 1090 1100 1110 1120 1130 1140 AKQPDLAPGL TTIGASPTQT VTLVTQPVVT KETAISKLEM PSSLMLEVPA LADFNRAWTE 1150 1160 1170 1180 1190 1200 LTDWLSLLDQ VIKSQRVMVG DLEDINEMII KQKATMQDLE QRRPQLEELI TAAQNLKNKT 1210 1220 1230 1240 1250 1260 SNQEARTIIT DRIERIQNQW DEVQEHLQNR RQQLNEMLKD STQWLEAKEE AEQVLGQARA 1270 1280 1290 1300 1310 1320 KLESWKEGPY TVDAIQKKIT ETKQLAKDLR QWQTNVDVAN DLALKLLRDY SADDTRKVHM 1330 1340 1350 1360 1370 1380 ITENINASWR SIHKRVSERE AALEETHRLL QQFPLDLEKF LAWLTEAETT ANVLQDATRK 1390 1400 1410 1420 1430 1440 ERLLEDSKGV KELMKQWQDL QGEIEAHTDV YHNLDENSQK ILRSLEGSDD AVLLQRRLDN 1450 1460 1470 1480 1490 1500 MNFKWSELRK KSLNIRSHLE ASSDQWKRLH LSLQELLVWL QLKDDELSRQ APIGGDFPAV 1510 1520 1530 1540 1550 1560 QKQNDVHRAF KRELKTKEPV IMSTLETVRI FLTEQPLEGL EKLYQEPREL PPEERAQNVT 1570 1580 1590 1600 1610 1620 RLLRKQAEEV NTEWEKLNLH SADWQRKIDE TLERLQELQE ATDELDLKLR QAEVIKGSWQ 1630 1640 1650 1660 1670 1680 PVGDLLIDSL QDHLEKVKAL RGEIAPLKEN VSHVNDLARQ LTTLGIQLSP YNLSTLEDLN 1690 1700 1710 1720 1730 1740 TRWKLLQVAV EDRVRQLHEA HRDFGPASQH FLSTSVQGPW ERAISPNKVP YYINHETQTT 1750 1760 1770 1780 1790 1800 CWDHPKMTEL YQSLADLNNV RFSAYRTAMK LRRLQKALCL DLLSLSAACD ALDQHNLKQN 1810 1820 1830 1840 1850 1860 DQPMDILQII NCLTTIYDRL EQEHNNLVNV PLCVDMCLNW LLNVYDTGRT GRIRVLSFKT 1870 1880 1890 1900 1910 1920 GIISLCKAHL EDKYRYLFKQ VASSTGFCDQ RRLGLLLHDS IQIPRQLGEV ASFGGSNIEP 1930 1940 1950 1960 1970 1980 SVRSCFQFAN NKPEIEAALF LDWMRLEPQS MVWLPVLHRV AAAETAKHQA KCNICKECPI 1990 2000 2010 2020 2030 2040 IGFRYRSLKH FNYDICQSCF FSGRVAKGHK MHYPMVEYCT PTTSGEDVRD FAKVLKNKFR 2050 2060 2070 2080 2090 2100 TKRYFAKHPR MGYLPVQTVL EGDNMETPVT LINFWPVDSA PASSPQLSHD DTHSRIEHYA 2110 2120 2130 2140 2150 2160 SRLAEMENSN GSYLNDSISP NESIDDEHLL IQHYCQSLNQ DSPLSQPRSP AQILISLESE 2170 2180 2190 2200 2210 2220 ERGELERILA DLEEENRNLQ AEYDRLKQQH EHKGLSPLPS PPEMMPTSPQ SPRDAELIAE 2230 2240 2250 2260 2270 2280 AKLLRQHKGR LEARMQILED HNKQLESQLH RLRQLLEQPQ AEAKVNGTTV SSPSTSLQRS 2290 2300 2310 2320 2330 2340 DSSQPMLLRV VGSQTSDSMG EEDLLSPPQD TSTGLEEVME QLNNSFPSSR GRNTPGKPMR EDTM
	Isoform 2 (Dystrophin-2). Checksum: 5A695D20AE07D801	FASTA	2,341	271,040
	10 20 30 40 50 60 MSARKLRNLS YKKAVRRQKL LEQSIQSAQE TEKSLHLIQE SLTFIDKQLA AYIADKVDAA 70 80 90 100 110 120 QMPQEAQKIQ SDLTSHEISL EEMKKHNQGK EAAQRVLSQI DVAQKKLQDV SMKFRLFQKP 130 140 150 160 170 180 ANFEQRLQES KMILDEVKMH LPALETKSVE QEVVQSQLNH CVNLYKSLSE VKSEVEMVIK 190 200 210 220 230 240 TGRQIVQKKQ TENPKELDER VTALKLHYNE LGAKVTERKQ QLEKCLKLSR KMRKEMNVLT 250 260 270 280 290 300 EWLAATDMEL TKRSAVEGMP SNLDSEVAWG KATQKEIEKQ KVHLKSITEV GEALKTVLGK 310 320 330 340 350 360 KETLVEDKLS LLNSNWIAVT SRAEEWLNLL LEYQKHMETF DQNVDHITKW IIQADTLLDE 370 380 390 400 410 420 SEKKKPQQKE DVLKRLKAEL NDIRPKVDST RDQAANLMAN RGDHCRKLVE PQISELNHRF 430 440 450 460 470 480 AAISHRIKTG KASIPLKELE QFNSDIQKLL EPLEAEIQQG VNLKEEDFNK DMNEDNEGTV 490 500 510 520 530 540 KELLQRGDNL QQRITDERKR EEIKIKQQLL QTKHNALKDL RSQRRKKALE ISHQWYQYKR 550 560 570 580 590 600 QADDLLKCLD DIEKKLASLP EPRDERKIKE IDRELQKKKE ELNAVRRQAE GLSEDGAAMA 610 620 630 640 650 660 VEPTQIQLSK RWREIESKFA QFRRLNFAQI HTVREETMMV MTEDMPLEIS YVPSTYLTEI 670 680 690 700 710 720 THVSQALLEV EQLLNAPDLC AKDFEDLFKQ EESLKNIKDS LQQSSGRIDI IHSKKTAALQ 730 740 750 760 770 780 SATPVERVKL QEALSQLDFQ WEKVNKMYKD RQGRFDRSVE KWRRFHYDIK IFNQWLTEAE 790 800 810 820 830 840 QFLRKTQIPE NWEHAKYKWY LKELQDGIGQ RQTVVRTLNA TGEEIIQQSS KTDASILQEK 850 860 870 880 890 900 LGSLNLRWQE VCKQLSDRKK RLEEQKNILS EFQRDLNEFV LWLEEADNIA SIPLEPGKEQ 910 920 930 940 950 960 QLKEKLEQVK LLVEELPLRQ GILKQLNETG GPVLVSAPIS PEEQDKLENK LKQTNLQWIK 970 980 990 1000 1010 1020 VSRALPEKQG EIEAQIKDLG QLEKKLEDLE EQLNHLLLWL SPIRNQLEIY NQPNQEGPFD 1030 1040 1050 1060 1070 1080 VKETEIAVQA KQPDVEEILS KGQHLYKEKP ATQPVKRKLE DLSSEWKAVN RLLQELRAKQ 1090 1100 1110 1120 1130 1140 PDLAPGLTTI GASPTQTVTL VTQPVVTKET AISKLEMPSS LMLEVPALAD FNRAWTELTD 1150 1160 1170 1180 1190 1200 WLSLLDQVIK SQRVMVGDLE DINEMIIKQK ATMQDLEQRR PQLEELITAA QNLKNKTSNQ 1210 1220 1230 1240 1250 1260 EARTIITDRI ERIQNQWDEV QEHLQNRRQQ LNEMLKDSTQ WLEAKEEAEQ VLGQARAKLE 1270 1280 1290 1300 1310 1320 SWKEGPYTVD AIQKKITETK QLAKDLRQWQ TNVDVANDLA LKLLRDYSAD DTRKVHMITE 1330 1340 1350 1360 1370 1380 NINASWRSIH KRVSEREAAL EETHRLLQQF PLDLEKFLAW LTEAETTANV LQDATRKERL 1390 1400 1410 1420 1430 1440 LEDSKGVKEL MKQWQDLQGE IEAHTDVYHN LDENSQKILR SLEGSDDAVL LQRRLDNMNF 1450 1460 1470 1480 1490 1500 KWSELRKKSL NIRSHLEASS DQWKRLHLSL QELLVWLQLK DDELSRQAPI GGDFPAVQKQ 1510 1520 1530 1540 1550 1560 NDVHRAFKRE LKTKEPVIMS TLETVRIFLT EQPLEGLEKL YQEPRELPPE ERAQNVTRLL 1570 1580 1590 1600 1610 1620 RKQAEEVNTE WEKLNLHSAD WQRKIDETLE RLQELQEATD ELDLKLRQAE VIKGSWQPVG 1630 1640 1650 1660 1670 1680 DLLIDSLQDH LEKVKALRGE IAPLKENVSH VNDLARQLTT LGIQLSPYNL STLEDLNTRW 1690 1700 1710 1720 1730 1740 KLLQVAVEDR VRQLHEAHRD FGPASQHFLS TSVQGPWERA ISPNKVPYYI NHETQTTCWD 1750 1760 1770 1780 1790 1800 HPKMTELYQS LADLNNVRFS AYRTAMKLRR LQKALCLDLL SLSAACDALD QHNLKQNDQP 1810 1820 1830 1840 1850 1860 MDILQIINCL TTIYDRLEQE HNNLVNVPLC VDMCLNWLLN VYDTGRTGRI RVLSFKTGII 1870 1880 1890 1900 1910 1920 SLCKAHLEDK YRYLFKQVAS STGFCDQRRL GLLLHDSIQI PRQLGEVASF GGSNIEPSVR 1930 1940 1950 1960 1970 1980 SCFQFANNKP EIEAALFLDW MRLEPQSMVW LPVLHRVAAA ETAKHQAKCN ICKECPIIGF 1990 2000 2010 2020 2030 2040 RYRSLKHFNY DICQSCFFSG RVAKGHKMHY PMVEYCTPTT SGEDVRDFAK VLKNKFRTKR 2050 2060 2070 2080 2090 2100 YFAKHPRMGY LPVQTVLEGD NMETPVTLIN FWPVDSAPAS SPQLSHDDTH SRIEHYASRL 2110 2120 2130 2140 2150 2160 AEMENSNGSY LNDSISPNES IDDEHLLIQH YCQSLNQDSP LSQPRSPAQI LISLESEERG 2170 2180 2190 2200 2210 2220 ELERILADLE EENRNLQAEY DRLKQQHEHK GLSPLPSPPE MMPTSPQSPR DAELIAEAKL 2230 2240 2250 2260 2270 2280 LRQHKGRLEA RMQILEDHNK QLESQLHRLR QLLEQPQAEA KVNGTTVSSP STSLQRSDSS 2290 2300 2310 2320 2330 2340 QPMLLRVVGS QTSDSMGEED LLSPPQDTST GLEEVMEQLN NSFPSSRGRN TPGKPMREDT M
	Isoform 3 (Dystrophin-3). Checksum: 50429DDEAC6077FA	FASTA	3,677	425,582
	10 20 30 40 50 60 MEDEREDVQK KTFTKWVNAQ FSKFGKQHIE NLFSDLQDGR RLLDLLEGLT GQKLPKEKGS 70 80 90 100 110 120 TRVHALNNVN KALRVLQNNN VDLVNIGSTD IVDGNHKLTL GLIWNIILHW QVKNVMKNIM 130 140 150 160 170 180 AGLQQTNSEK ILLSWVRQST RNYPQVNVIN FTTSWSDGLA LNALIHSHRP DLFDWNSVVC 190 200 210 220 230 240 QQSATQRLEH AFNIARYQLG IEKLLDPEDV DTTYPDKKSI LMYITSLFQV LPQQVSIEAI 250 260 270 280 290 300 QEVEMLPRPP KVTKEEHFQL HHQMHYSQQI TVSLAQGYER TSSPKPRFKS YAYTQAAYVT 310 320 330 340 350 360 TSDPTRSPFP SQHLEAPEDK SFGSSLMESE VNLDRYQTAL EEVLSWLLSA EDTLQAQGEI 370 380 390 400 410 420 SNDVEVVKDQ FHTHEGYMMD LTAHQGRVGN ILQLGSKLIG TGKLSEDEET EVQEQMNLLN 430 440 450 460 470 480 SRWECLRVAS MEKQSNLHRV LMDLQNQKLK ELNDWLTKTE ERTRKMEEEP LGPDLEDLKR 490 500 510 520 530 540 QVQQHKVLQE DLEQEQVRVN SLTHMVVVVD ESSGDHATAA LEEQLKVLGD RWANICRWTE 550 560 570 580 590 600 DRWVLLQDIL LKWQRLTEEQ CLFSAWLSEK EDAVNKIHTT GFKDQNEMLS SLQKLAVLKA 610 620 630 640 650 660 DLEKKKQSMG KLYSLKQDLL STLKNKSVTQ KTEAWLDNFA RCWDNLVQKL EKSTAQISQA 670 680 690 700 710 720 VTTTQPSLTQ TTVMETVTTV TTREQILVKH AQEELPPPPP QKKRQITVDS EIRKRLDVDI 730 740 750 760 770 780 TELHSWITRS EAVLQSPEFA IFRKEGNFSD LKEKVNAIER EKAEKFRKLQ DASRSAQALV 790 800 810 820 830 840 EQMVNEGVNA DSIKQASEQL NSRWIEFCQL LSERLNWLEY QNNIIAFYNQ LQQLEQMTTT 850 860 870 880 890 900 AENWLKIQPT TPSEPTAIKS QLKICKDEVN RLSGLQPQIE RLKIQSIALK EKGQGPMFLD 910 920 930 940 950 960 ADFVAFTNHF KQVFSDVQAR EKELQTIFDT LPPMRYQETM SAIRTWVQQS ETKLSIPQLS 970 980 990 1000 1010 1020 VTDYEIMEQR LGELQALQSS LQEQQSGLYY LSTTVKEMSK KAPSEISRKY QSEFEEIEGR 1030 1040 1050 1060 1070 1080 WKKLSSQLVE HCQKLEEQMN KLRKIQNHIQ TLKKWMAEVD VFLKEEWPAL GDSEILKKQL 1090 1100 1110 1120 1130 1140 KQCRLLVSDI QTIQPSLNSV NEGGQKIKNE AEPEFASRLE TELKELNTQW DHMCQQVYAR 1150 1160 1170 1180 1190 1200 KEALKGGLEK TVSLQKDLSE MHEWMTQAEE EYLERDFEYK TPDELQKAVE EMKRAKEEAQ 1210 1220 1230 1240 1250 1260 QKEAKVKLLT ESVNSVIAQA PPVAQEALKK ELETLTTNYQ WLCTRLNGKC KTLEEVWACW 1270 1280 1290 1300 1310 1320 HELLSYLEKA NKWLNEVEFK LKTTENIPGG AEEISEVLDS LENLMRHSED NPNQIRILAQ 1330 1340 1350 1360 1370 1380 TLTDGGVMDE LINEELETFN SRWRELHEEA VRRQKLLEQS IQSAQETEKS LHLIQESLTF 1390 1400 1410 1420 1430 1440 IDKQLAAYIA DKVDAAQMPQ EAQKIQSDLT SHEISLEEMK KHNQGKEAAQ RVLSQIDVAQ 1450 1460 1470 1480 1490 1500 KKLQDVSMKF RLFQKPANFE QRLQESKMIL DEVKMHLPAL ETKSVEQEVV QSQLNHCVNL 1510 1520 1530 1540 1550 1560 YKSLSEVKSE VEMVIKTGRQ IVQKKQTENP KELDERVTAL KLHYNELGAK VTERKQQLEK 1570 1580 1590 1600 1610 1620 CLKLSRKMRK EMNVLTEWLA ATDMELTKRS AVEGMPSNLD SEVAWGKATQ KEIEKQKVHL 1630 1640 1650 1660 1670 1680 KSITEVGEAL KTVLGKKETL VEDKLSLLNS NWIAVTSRAE EWLNLLLEYQ KHMETFDQNV 1690 1700 1710 1720 1730 1740 DHITKWIIQA DTLLDESEKK KPQQKEDVLK RLKAELNDIR PKVDSTRDQA ANLMANRGDH 1750 1760 1770 1780 1790 1800 CRKLVEPQIS ELNHRFAAIS HRIKTGKASI PLKELEQFNS DIQKLLEPLE AEIQQGVNLK 1810 1820 1830 1840 1850 1860 EEDFNKDMNE DNEGTVKELL QRGDNLQQRI TDERKREEIK IKQQLLQTKH NALKDLRSQR 1870 1880 1890 1900 1910 1920 RKKALEISHQ WYQYKRQADD LLKCLDDIEK KLASLPEPRD ERKIKEIDRE LQKKKEELNA 1930 1940 1950 1960 1970 1980 VRRQAEGLSE DGAAMAVEPT QIQLSKRWRE IESKFAQFRR LNFAQIHTVR EETMMVMTED 1990 2000 2010 2020 2030 2040 MPLEISYVPS TYLTEITHVS QALLEVEQLL NAPDLCAKDF EDLFKQEESL KNIKDSLQQS 2050 2060 2070 2080 2090 2100 SGRIDIIHSK KTAALQSATP VERVKLQEAL SQLDFQWEKV NKMYKDRQGR FDRSVEKWRR 2110 2120 2130 2140 2150 2160 FHYDIKIFNQ WLTEAEQFLR KTQIPENWEH AKYKWYLKEL QDGIGQRQTV VRTLNATGEE 2170 2180 2190 2200 2210 2220 IIQQSSKTDA SILQEKLGSL NLRWQEVCKQ LSDRKKRLEE QKNILSEFQR DLNEFVLWLE 2230 2240 2250 2260 2270 2280 EADNIASIPL EPGKEQQLKE KLEQVKLLVE ELPLRQGILK QLNETGGPVL VSAPISPEEQ 2290 2300 2310 2320 2330 2340 DKLENKLKQT NLQWIKVSRA LPEKQGEIEA QIKDLGQLEK KLEDLEEQLN HLLLWLSPIR 2350 2360 2370 2380 2390 2400 NQLEIYNQPN QEGPFDVKET EIAVQAKQPD VEEILSKGQH LYKEKPATQP VKRKLEDLSS 2410 2420 2430 2440 2450 2460 EWKAVNRLLQ ELRAKQPDLA PGLTTIGASP TQTVTLVTQP VVTKETAISK LEMPSSLMLE 2470 2480 2490 2500 2510 2520 VPALADFNRA WTELTDWLSL LDQVIKSQRV MVGDLEDINE MIIKQKATMQ DLEQRRPQLE 2530 2540 2550 2560 2570 2580 ELITAAQNLK NKTSNQEART IITDRIERIQ NQWDEVQEHL QNRRQQLNEM LKDSTQWLEA 2590 2600 2610 2620 2630 2640 KEEAEQVLGQ ARAKLESWKE GPYTVDAIQK KITETKQLAK DLRQWQTNVD VANDLALKLL 2650 2660 2670 2680 2690 2700 RDYSADDTRK VHMITENINA SWRSIHKRVS EREAALEETH RLLQQFPLDL EKFLAWLTEA 2710 2720 2730 2740 2750 2760 ETTANVLQDA TRKERLLEDS KGVKELMKQW QDLQGEIEAH TDVYHNLDEN SQKILRSLEG 2770 2780 2790 2800 2810 2820 SDDAVLLQRR LDNMNFKWSE LRKKSLNIRS HLEASSDQWK RLHLSLQELL VWLQLKDDEL 2830 2840 2850 2860 2870 2880 SRQAPIGGDF PAVQKQNDVH RAFKRELKTK EPVIMSTLET VRIFLTEQPL EGLEKLYQEP 2890 2900 2910 2920 2930 2940 RELPPEERAQ NVTRLLRKQA EEVNTEWEKL NLHSADWQRK IDETLERLQE LQEATDELDL 2950 2960 2970 2980 2990 3000 KLRQAEVIKG SWQPVGDLLI DSLQDHLEKV KALRGEIAPL KENVSHVNDL ARQLTTLGIQ 3010 3020 3030 3040 3050 3060 LSPYNLSTLE DLNTRWKLLQ VAVEDRVRQL HEAHRDFGPA SQHFLSTSVQ GPWERAISPN 3070 3080 3090 3100 3110 3120 KVPYYINHET QTTCWDHPKM TELYQSLADL NNVRFSAYRT AMKLRRLQKA LCLDLLSLSA 3130 3140 3150 3160 3170 3180 ACDALDQHNL KQNDQPMDIL QIINCLTTIY DRLEQEHNNL VNVPLCVDMC LNWLLNVYDT 3190 3200 3210 3220 3230 3240 GRTGRIRVLS FKTGIISLCK AHLEDKYRYL FKQVASSTGF CDQRRLGLLL HDSIQIPRQL 3250 3260 3270 3280 3290 3300 GEVASFGGSN IEPSVRSCFQ FANNKPEIEA ALFLDWMRLE PQSMVWLPVL HRVAAAETAK 3310 3320 3330 3340 3350 3360 HQAKCNICKE CPIIGFRYRS LKHFNYDICQ SCFFSGRVAK GHKMHYPMVE YCTPTTSGED 3370 3380 3390 3400 3410 3420 VRDFAKVLKN KFRTKRYFAK HPRMGYLPVQ TVLEGDNMET PVTLINFWPV DSAPASSPQL 3430 3440 3450 3460 3470 3480 SHDDTHSRIE HYASRLAEME NSNGSYLNDS ISPNESIDDE HLLIQHYCQS LNQDSPLSQP 3490 3500 3510 3520 3530 3540 RSPAQILISL ESEERGELER ILADLEEENR NLQAEYDRLK QQHEHKGLSP LPSPPEMMPT 3550 3560 3570 3580 3590 3600 SPQSPRDAEL IAEAKLLRQH KGRLEARMQI LEDHNKQLES QLHRLRQLLE QPQAEAKVNG 3610 3620 3630 3640 3650 3660 TTVSSPSTSL QRSDSSQPML LRVVGSQTSD SMGEEDLLSP PQDTSTGLEE VMEQLNNSFP 3670 SSRGRNTPGK PMREDTM
	Isoform 5 (Dp71). Checksum: 75D44165427FAB8B	FASTA	622	70,750
	10 20 30 40 50 60 MREQLKGHET QTTCWDHPKM TELYQSLADL NNVRFSAYRT AMKLRRLQKA LCLDLLSLSA 70 80 90 100 110 120 ACDALDQHNL KQNDQPMDIL QIINCLTTIY DRLEQEHNNL VNVPLCVDMC LNWLLNVYDT 130 140 150 160 170 180 GRTGRIRVLS FKTGIISLCK AHLEDKYRYL FKQVASSTGF CDQRRLGLLL HDSIQIPRQL 190 200 210 220 230 240 GEVASFGGSN IEPSVRSCFQ FANNKPEIEA ALFLDWMRLE PQSMVWLPVL HRVAAAETAK 250 260 270 280 290 300 HQAKCNICKE CPIIGFRYRS LKHFNYDICQ SCFFSGRVAK GHKMHYPMVE YCTPTTSGED 310 320 330 340 350 360 VRDFAKVLKN KFRTKRYFAK HPRMGYLPVQ TVLEGDNMET PASSPQLSHD DTHSRIEHYA 370 380 390 400 410 420 SRLAEMENSN GSYLNDSISP NESIDDEHLL IQHYCQSLNQ DSPLSQPRSP AQILISLESE 430 440 450 460 470 480 ERGELERILA DLEEENRNLQ AEYDRLKQQH EHKGLSPLPS PPEMMPTSPQ SPRDAELIAE 490 500 510 520 530 540 AKLLRQHKGR LEARMQILED HNKQLESQLH RLRQLLEQPQ AEAKVNGTTV SSPSTSLQRS 550 560 570 580 590 600 DSSQPMLLRV VGSQTSDSMG EEDLLSPPQD TSTGLEEVME QLNNSFPSSR GHNVGSLFHM 610 620 ADDLGRAMES LVSVMTDEEG AE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The complete sequence of dystrophin predicts a rod-shaped cytoskeletal protein." Koenig M., Monaco A.P., Kunkel L.M. Cell 53:219-228(1988) [PubMed: 3282674] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), VARIANTS 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: 2668885] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), VARIANTS PRO-133; ILE-623; GLY-784; 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: 1319059] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5). 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: 15772651] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANTS ASP-882 AND ARG-2937.
[5]	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.
[6]	"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: 3607877] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-497 (ISOFORM 4).
[7]	"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: 2648158] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-32 (ISOFORM 3), ALTERNATIVE SPLICING. Tissue: Brain.
[8]	"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: 3428261] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 404-1137 (ISOFORMS 3/4/5).
[9]	"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: 3205741] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 665-722; 2098-2204 AND 2305-2366.
[10]	"High resolution deletion breakpoint mapping in the DMD gene by whole cosmid hybridization." Blonden L.A.J., den Dunnen J.T., van Paassen H.M.B., Wapenaar M.C., Grootscholten P.M., Ginjaar H.B., Bakker E., Pearson P.L., van Ommen G.J.B. Nucleic Acids Res. 17:5611-5621(1989) [PubMed: 2569720] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2147-2204.
[11]	"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.
[12]	"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: 8541829] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3670-3685 (ISOFORMS 1/2/3/4 AND 5), TISSUE SPECIFICITY. Tissue: Amnion.
[13]	"Syntrophin binds to an alternatively spliced exon of dystrophin." Ahn A.H., Kunkel L.M. J. Cell Biol. 128:363-371(1995) [PubMed: 7844150] [Abstract] Cited for: INTERACTION WITH SNTB1.
[14]	"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: 8576247] [Abstract] Cited for: INTERACTION WITH SNTA1 AND SNTB2.
[15]	"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: 10747910] [Abstract] Cited for: INTERACTION WITH SNTG1 AND SNTG2.
[16]	"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: 16000376] [Abstract] Cited for: INTERACTION WITH KRT19, TISSUE SPECIFICITY.
[17]	"Quantitative phosphoproteome analysis using a dendrimer conjugation chemistry and tandem mass spectrometry." Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J., Bodenmiller B., Watts J.D., Hood L., Aebersold R. Nat. Methods 2:591-598(2005) [PubMed: 16094384] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1590, MASS SPECTROMETRY. Tissue: T-cell.
[18]	"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3621 AND SER-3623, MASS SPECTROMETRY.
[19]	"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3613, MASS SPECTROMETRY.
[20]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3483; SER-3613; SER-3617; SER-3623; THR-3652 AND SER-3666, MASS SPECTROMETRY.
[21]	"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: 10932245] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 3046-3306.
[22]	"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: 10801490] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-246.
[23]	"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: 7951253] [Abstract] Cited for: REVIEW ON DMD VARIANTS.
[24]	"Microlesions and polymorphisms in the Duchenne/Becker muscular dystrophy gene." Rininsland F., Reiss J. Hum. Genet. 94:111-116(1994) [PubMed: 8045556] [Abstract] Cited for: REVIEW ON VARIANTS.
[25]	"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: 8401582] [Abstract] Cited for: VARIANT DMD ARG-54.
[26]	"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: 7981690] [Abstract] Cited for: VARIANT DMD GLY-645.
[27]	"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: 7849724] [Abstract] Cited for: VARIANTS HIS-365; TRP-2191 AND ARG-2937.
[28]	"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: 8817332] [Abstract] Cited for: VARIANT DMD TYR-3340.
[29]	"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: 9170407] [Abstract] Cited for: VARIANT CMD3B ALA-279.
[30]	"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: 9851445] [Abstract] Cited for: VARIANT DMD HIS-3335.
[31]	"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: 10573008] [Abstract] Cited for: VARIANT BMD PRO-171.
[32]	"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: 12354438] [Abstract] Cited for: VARIANT CMD3B LYS-1672.
[33]	"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: 12359139] [Abstract] Cited for: VARIANTS CMD3B ASN-18 AND LEU-3228, VARIANTS TRP-2155; THR-2299; GLN-2366; VAL-2910; ASP-2912 AND ARG-2937.
[34]	"Rapid direct sequence analysis of the dystrophin gene." Flanigan K.M., von Niederhausern A., Dunn D.M., Alder J., Mendell J.R., Weiss R.B. Am. J. Hum. Genet. 72:931-939(2003) [PubMed: 12632325] [Abstract] Cited for: VARIANTS VAL-165 AND PHE-3313.
[35]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed: 16959974] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] PHE-334; GLN-1219; HIS-1470 AND VAL-2164.
+	Additional computationally mapped references.

Web resources

DMD

Dystrophin Mutation Database

GeneReviews

SHMPD

The Singapore human mutation and polymorphism database

Wikipedia

Dystrophin entry

Cross-references

Sequence databases

EMBLGenBankDDBJ

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.
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.
AL139278 , AC004468, AC006061, AC078958, AC079143, AC079175, AC079177, AC079864, AC090632, AC093167, AC093193, AC096506, AL031542, AL031643, AL096699, AL109609, AL451144 Genomic DNA. Translation: CAI42991.1.
AL451144 , AC004468, AC006061, AC078958, AC079143, AC079175, AC079177, AC079864, AC090632, AC093167, AC093193, AC096506, AL031542, AL031643, AL096699, AL109609, AL139278 Genomic DNA. Translation: CAI39566.1.
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.

IPI

IPI00006091.
IPI00184813.
IPI00220577.
IPI00304638.
IPI00304639.

PIR

A45255.

RefSeq

NP_000100.2.
NP_003997.1.
NP_004000.1.
NP_004001.1.
NP_004002.2.
NP_004003.1.
NP_004004.1.
NP_004005.1.
NP_004008.1.
NP_004009.1.
NP_004010.1.
NP_004011.1.
NP_004012.1.
NP_004013.1.
NP_004014.1.

UniGene

Hs.495912

3D structure databases

PDBPDBe

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	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P11532. 11 interactions.

STRING

P11532.

PTM databases

PhosphoSite

P11532.

Proteomic databases

PRIDE

P11532.

Genome annotation databases

Ensembl

ENST00000288447; ENSP00000288447; ENSG00000198947; Homo sapiens. [Genome view]
ENST00000343523; ENSP00000340057; ENSG00000198947; Homo sapiens. [Genome view]
ENST00000357033; ENSP00000354923; ENSG00000198947; Homo sapiens. [Genome view]
ENST00000358062; ENSP00000350765; ENSG00000198947; Homo sapiens. [Genome view]
ENST00000359836; ENSP00000352894; ENSG00000198947; Homo sapiens. [Genome view]
ENST00000361471; ENSP00000354464; ENSG00000198947; Homo sapiens. [Genome view]
ENST00000378677; ENSP00000367948; ENSG00000198947; Homo sapiens. [Genome view]
ENST00000378680; ENSP00000367951; ENSG00000198947; Homo sapiens. [Genome view]
ENST00000378682; ENSP00000367953; ENSG00000198947; Homo sapiens. [Genome view]
ENST00000378684; ENSP00000367955; ENSG00000198947; Homo sapiens. [Genome view]
ENST00000378687; ENSP00000367958; ENSG00000198947; Homo sapiens. [Genome view]
ENST00000378702; ENSP00000367974; ENSG00000198947; Homo sapiens. [Genome view]
ENST00000378705; ENSP00000367977; ENSG00000198947; Homo sapiens. [Genome view]
ENST00000378707; ENSP00000367979; ENSG00000198947; Homo sapiens. [Genome view]
ENST00000378723; ENSP00000367997; ENSG00000198947; Homo sapiens. [Genome view]
ENST00000420596; ENSP00000399897; ENSG00000198947; Homo sapiens. [Genome view]
ENST00000445312; ENSP00000411636; ENSG00000198947; Homo sapiens. [Genome view]
ENST00000447523; ENSP00000395904; ENSG00000198947; Homo sapiens. [Genome view]
ENST00000448370; ENSP00000388559; ENSG00000198947; Homo sapiens. [Genome view]

GeneID

1756.

UCSC

uc004dcp.1. human.
uc004dcx.2. human.
uc004dcy.1. human.
uc004dda.1. human.

Organism-specific databases

CTD

1756.

GeneCards

GC0XM031047.

HGNC

HGNC:2928. DMD.

HPA

CAB000119.
HPA002725.
HPA023885.

MIM

300376. phenotype.
300377. gene.
302045. phenotype.
310200. phenotype.

Orphanet

154. Cardiomyopathy, familial dilated.
262. Duchenne and Becker muscular dystrophy.
98895. Muscular dystrophy, Becker type.
98896. Muscular dystrophy, Duchenne type.
215. Night blindness, stationary, congenital.

PharmGKB

PA27378.

GenAtlas

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Phylogenomic databases

HOGENOM

P11532.

HOVERGEN

P11532.

Enzyme and pathway databases

Reactome

REACT_17044. Muscle contraction.

Gene expression databases

ArrayExpress

P11532.

Bgee

P11532.

CleanEx

HS_DMD.

Genevestigator

P11532.

GermOnline

ENSG00000198947. Homo sapiens.

Family and domain databases

InterPro

IPR001589. Actinin_actin-bd_CS.
IPR001715. Calponin_act_bd.
IPR016344. Dystrophin/utrophin.
IPR015153. EF-hand_regn-1.
IPR015154. EF-hand_regn-2.
IPR011992. EF-Hand_type.
IPR018159. Spectrin/alpha-actinin.
IPR002017. Spectrin_repeat.
IPR001202. WW_Rsp5_WWP.
IPR000433. Znf_ZZ.
[Graphical view]

Gene3D

G3DSA:1.10.418.10. Calponin-homology. 2 hits.
G3DSA:1.10.238.10. EF-Hand_type. 2 hits.

Pfam

PF00307. CH. 2 hits.
PF09068. efhand_1. 1 hit.
PF09069. efhand_2. 1 hit.
PF00435. Spectrin. 19 hits.
PF00397. WW. 1 hit.
PF00569. ZZ. 1 hit.
[Graphical view]

PIRSF

PIRSF002341. Dystrophin/utrophin. 1 hit.

SMART

SM00033. CH. 2 hits.
SM00150. SPEC. 22 hits.
SM00456. WW. 1 hit.
SM00291. ZnF_ZZ. 1 hit.
[Graphical view]

PROSITE

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]

ProtoNet

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Other Resources

NextBio

7115.

SOURCE

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Entry information

Entry name

DMD_HUMAN

Accession

Primary (citable) accession number: P11532
Secondary accession number(s): Q02295 , Q14169, Q14170, Q5JYU0, Q7KZ48, Q9UCW3, Q9UCW4

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	September 27, 2005
Last modified:	November 3, 2009
This is version 134 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.