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P11531

- DMD_MOUSE

UniProt

P11531 - DMD_MOUSE

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Protein

Dystrophin

Gene

Dmd

Organism
Mus musculus (Mouse)
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 fingeri3300 – 334748ZZ-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. nitric-oxide synthase binding Source: BHF-UCL
  3. zinc ion binding Source: InterPro

GO - Biological processi

  1. cardiac muscle cell action potential Source: BHF-UCL
  2. cellular protein complex assembly Source: BHF-UCL
  3. cellular protein localization Source: BHF-UCL
  4. establishment of blood-nerve barrier Source: MGI
  5. establishment of glial blood-brain barrier Source: MGI
  6. muscle cell cellular homeostasis Source: MGI
  7. muscle fiber development Source: MGI
  8. muscle organ development Source: MGI
  9. myotube cell development Source: MGI
  10. negative regulation of peptidyl-cysteine S-nitrosylation Source: BHF-UCL
  11. negative regulation of peptidyl-serine phosphorylation Source: BHF-UCL
  12. neurotransmitter receptor metabolic process Source: MGI
  13. nucleus localization Source: MGI
  14. olfactory nerve structural organization Source: MGI
  15. positive regulation of cell-matrix adhesion Source: BHF-UCL
  16. positive regulation of sodium ion transmembrane transporter activity Source: BHF-UCL
  17. regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion Source: BHF-UCL
  18. regulation of gene expression Source: MGI
  19. regulation of heart rate Source: BHF-UCL
  20. regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum Source: BHF-UCL
  21. regulation of ryanodine-sensitive calcium-release channel activity Source: BHF-UCL
  22. regulation of skeletal muscle contraction Source: BHF-UCL
  23. regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion Source: BHF-UCL
  24. regulation of transcription, DNA-templated Source: MGI
  25. regulation of voltage-gated calcium channel activity Source: BHF-UCL
  26. skeletal muscle tissue development Source: MGI
Complete GO annotation...

Keywords - Ligandi

Actin-binding, Calcium, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_196607. Non-integrin membrane-ECM interactions.
REACT_232053. Striated Muscle Contraction.

Names & Taxonomyi

Protein namesi
Recommended name:
Dystrophin
Gene namesi
Name:Dmd
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome X

Organism-specific databases

MGIiMGI:94909. Dmd.

Subcellular locationi

Cell membranesarcolemma 1 Publication; Peripheral membrane protein 1 Publication; Cytoplasmic side 1 Publication. Cytoplasmcytoskeleton 1 Publication. Cell junctionsynapsepostsynaptic cell membrane 1 Publication
Note: In muscle cells, sarcolemma localization requires the presence of ANK2, while localization to costameres requires the presence of ANK3. Localizes to neuromuscular junctions (NMJs). In adult muscle, NMJ localization depends upon ANK2 presence, but not in newborn animals.

GO - Cellular componenti

  1. cell-substrate junction Source: MGI
  2. cytoskeleton Source: UniProtKB-KW
  3. dystrophin-associated glycoprotein complex Source: MGI
  4. membrane raft Source: MGI
  5. neuron projection terminus Source: MGI
  6. plasma membrane Source: MGI
  7. postsynaptic membrane Source: UniProtKB-KW
  8. protein complex Source: MGI
  9. sarcolemma Source: MGI
  10. synapse Source: MGI
  11. Z disc Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 36783678DystrophinPRO_0000076076Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei3476 – 34761PhosphoserineBy similarity
Modified residuei3605 – 36051PhosphoserineBy similarity
Modified residuei3606 – 36061PhosphoserineBy similarity
Modified residuei3610 – 36101PhosphoserineBy similarity
Modified residuei3616 – 36161Phosphoserine1 Publication
Modified residuei3617 – 36171Phosphoserine1 Publication
Modified residuei3659 – 36591PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP11531.
PaxDbiP11531.
PRIDEiP11531.

PTM databases

PhosphoSiteiP11531.

Expressioni

Tissue specificityi

Differentially expressed during skeletal muscle, heart, and brain development. Also expressed in retina.1 Publication

Gene expression databases

BgeeiP11531.
CleanExiMM_DMD.
ExpressionAtlasiP11531. baseline and differential.
GenevestigatoriP11531.

Interactioni

Subunit structurei

Interacts with SYNM. Interacts with the syntrophins 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 (By similarity). Interacts with SYNM; SNTA1 and SNTB1. Interacts with CMYA5. Directly interacts with ANK2 and ANK3; these interactions do not interfere with betaDAG1-binding and are necessary for proper localization in muscle cells.By similarity6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Snta1Q612342EBI-295928,EBI-295952

Protein-protein interaction databases

BioGridi199245. 20 interactions.
DIPiDIP-32899N.
IntActiP11531. 6 interactions.
MINTiMINT-85369.

Structurei

3D structure databases

ProteinModelPortaliP11531.
SMRiP11531. Positions 9-246, 340-455, 3040-3299.
ModBaseiSearch...
MobiDBiSearch...

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
Repeati341 – 449109Spectrin 1Add
BLAST
Repeati450 – 558109Spectrin 2Add
BLAST
Repeati561 – 669109Spectrin 3Add
BLAST
Repeati721 – 830110Spectrin 4Add
BLAST
Repeati832 – 936105Spectrin 5Add
BLAST
Repeati945 – 1047103Spectrin 6Add
BLAST
Repeati1050 – 1156107Spectrin 7Add
BLAST
Repeati1159 – 1265107Spectrin 8Add
BLAST
Repeati1268 – 1369102Spectrin 9Add
BLAST
Repeati1370 – 146596Spectrin 10Add
BLAST
Repeati1470 – 1570101Spectrin 11Add
BLAST
Repeati1573 – 1678106Spectrin 12Add
BLAST
Repeati1681 – 1780100Spectrin 13Add
BLAST
Repeati1781 – 187696Spectrin 14Add
BLAST
Repeati1879 – 1981103Spectrin 15Add
BLAST
Repeati1994 – 2103110Spectrin 16Add
BLAST
Repeati2106 – 2210105Spectrin 17Add
BLAST
Repeati2213 – 2318106Spectrin 18Add
BLAST
Repeati2319 – 241698Spectrin 19Add
BLAST
Repeati2468 – 2570103Spectrin 20Add
BLAST
Repeati2573 – 2679107Spectrin 21Add
BLAST
Repeati2682 – 2795114Spectrin 22Add
BLAST
Repeati2801 – 2923123Spectrin 23Add
BLAST
Repeati2928 – 3033106Spectrin 24Add
BLAST
Domaini3048 – 308134WWPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni63 – 7210ANK2- and ANK-3 binding
Regioni1417 – 1915499Interaction with SYNMAdd
BLAST
Regioni3051 – 3401351Interaction with SYNMAdd
BLAST
Regioni3459 – 351153Binds to SNTB1By similarityAdd
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 fingeri3300 – 334748ZZ-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG5069.
GeneTreeiENSGT00760000119237.
HOGENOMiHOG000231173.
HOVERGENiHBG005495.
InParanoidiP11531.
KOiK10366.
OMAiEGPYTMD.
OrthoDBiEOG7V765N.
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. 16 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]

Sequencei

Sequence statusi: Complete.

This entry describes 1 isoform i produced by alternative splicing. Align

Note: At least 11 isoforms are produced.

Isoform 1 (identifier: P11531-1) [UniParc]FASTAAdd to Basket

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.

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        10         20         30         40         50
MLWWEEVEDC YEREDVQKKT FTKWINAQFS KFGKQHIDNL FSDLQDGKRL
60 70 80 90 100
LDLLEGLTGQ KLPKEKGSTR VHALNNVNKA LRVLQKNNVD LVNIGSTDIV
110 120 130 140 150
DGNHKLTLGL IWNIILHWQV KNVMKTIMAG LQQTNSEKIL LSWVRQSTRN
160 170 180 190 200
YPQVNVINFT SSWSDGLALN ALIHSHRPDL FDWNSVVSQH SATQRLEHAF
210 220 230 240 250
NIAKCQLGIE KLLDPEDVAT TYPDKKSILM YITSLFQVLP QQVSIEAIQE
260 270 280 290 300
VEMLPRTSSK VTREEHFQLH HQMHYSQQIT VSLAQGYEQT SSSPKPRFKS
310 320 330 340 350
YAFTQAAYVA TSDSTQSPYP SQHLEAPRDK SLDSSLMETE VNLDSYQTAL
360 370 380 390 400
EEVLSWLLSA EDTLRAQGEI SNDVEEVKEQ FHAHEGFMMD LTSHQGLVGN
410 420 430 440 450
VLQLGSQLVG KGKLSEDEEA EVQEQMNLLN SRWECLRVAS MEKQSKLHKV
460 470 480 490 500
LMDLQNQKLK ELDDWLTKTE ERTKKMEEEP FGPDLEDLKC QVQQHKVLQE
510 520 530 540 550
DLEQEQVRVN SLTHMVVVVD ESSGDHATAA LEEQLKVLGD RWANICRWTE
560 570 580 590 600
DRWIVLQDIL LKWQHFTEEQ CLFSTWLSEK EDAMKNIQTS GFKDQNEMMS
610 620 630 640 650
SLHKISTLKI DLEKKKPTME KLSSLNQDLL SALKNKSVTQ KMEIWMENFA
660 670 680 690 700
QRWDNLTQKL EKSSAQISQA VTTTQPSLTQ TTVMETVTMV TTREQIMVKH
710 720 730 740 750
AQEELPPPPP QKKRQITVDS ELRKRLDVDI TELHSWITRS EAVLQSSEFA
760 770 780 790 800
VYRKEGNISD LQEKVNAIAR EKAEKFRKLQ DASRSAQALV EQMANEGVNA
810 820 830 840 850
ESIRQASEQL NSRWTEFCQL LSERVNWLEY QTNIITFYNQ LQQLEQMTTT
860 870 880 890 900
AENLLKTQST TLSEPTAIKS QLKICKDEVN RLSALQPQIE QLKIQSLQLK
910 920 930 940 950
EKGQGPMFLD ADFVAFTNHF NHIFDGVRAK EKELQTIFDT LPPMRYQETM
960 970 980 990 1000
SSIRTWIQQS ESKLSVPYLS VTEYEIMEER LGKLQALQSS LKEQQNGFNY
1010 1020 1030 1040 1050
LSDTVKEMAK KAPSEICQKY LSEFEEIEGH WKKLSSQLVE SCQKLEEHMN
1060 1070 1080 1090 1100
KLRKFQNHIK TLQKWMAEVD VFLKEEWPAL GDAEILKKQL KQCRLLVGDI
1110 1120 1130 1140 1150
QTIQPSLNSV NEGGQKIKSE AELEFASRLE TELRELNTQW DHICRQVYTR
1160 1170 1180 1190 1200
KEALKAGLDK TVSLQKDLSE MHEWMTQAEE EYLERDFEYK TPDELQTAVE
1210 1220 1230 1240 1250
EMKRAKEEAL QKETKVKLLT ETVNSVIAHA PPSAQEALKK ELETLTTNYQ
1260 1270 1280 1290 1300
WLCTRLNGKC KTLEEVWACW HELLSYLEKA NKWLNEVELK LKTMENVPAG
1310 1320 1330 1340 1350
PEEITEVLES LENLMHHSEE NPNQIRLLAQ TLTDGGVMDE LINEELETFN
1360 1370 1380 1390 1400
SRWRELHEEA VRKQKLLEQS IQSAQEIEKS LHLIQESLEF IDKQLAAYIT
1410 1420 1430 1440 1450
DKVDAAQMPQ EAQKIQSDLT SHEISLEEMK KHNQGKDANQ RVLSQIDVAQ
1460 1470 1480 1490 1500
KKLQDVSMKF RLFQKPANFE QRLEESKMIL DEVKMHLPAL ETKSVEQEVI
1510 1520 1530 1540 1550
QSQLSHCVNL YKSLSEVKSE VEMVIKTGRQ IVQKKQTENP KELDERVTAL
1560 1570 1580 1590 1600
KLHYNELGAK VTERKQQLEK CLKLSRKMRK EMNVLTEWLA ATDTELTKRS
1610 1620 1630 1640 1650
AVEGMPSNLD SEVAWGKATQ KEIEKQKAHL KSVTELGESL KMVLGKKETL
1660 1670 1680 1690 1700
VEDKLSLLNS NWIAVTSRVE EWLNLLLEYQ KHMETFDQNI EQITKWIIHA
1710 1720 1730 1740 1750
DELLDESEKK KPQQKEDILK RLKAEMNDMR PKVDSTRDQA AKLMANRGDH
1760 1770 1780 1790 1800
CRKVVEPQIS ELNRRFAAIS HRIKTGKASI PLKELEQFNS DIQKLLEPLE
1810 1820 1830 1840 1850
AEIQQGVNLK EEDFNKDMSE DNEGTVNELL QRGDNLQQRI TDERKREEIK
1860 1870 1880 1890 1900
IKQQLLQTKH NALKDLRSQR RKKALEISHQ WYQYKRQADD LLKCLDEIEK
1910 1920 1930 1940 1950
KLASLPEPRD ERKLKEIDRE LQKKKEELNA VRRQAEGLSE NGAAMAVEPT
1960 1970 1980 1990 2000
QIQLSKRWRQ IESNFAQFRR LNFAQIHTLH EETMVVTTED MPLDVSYVPS
2010 2020 2030 2040 2050
TYLTEISHIL QALSEVDHLL NTPELCAKDF EDLFKQEESL KNIKDNLQQI
2060 2070 2080 2090 2100
SGRIDIIHKK KTAALQSATS MEKVKVQEAV AQMDFQGEKL HRMYKERQGR
2110 2120 2130 2140 2150
FDRSVEKWRH FHYDMKVFNQ WLNEVEQFFK KTQNPENWEH AKYKWYLKEL
2160 2170 2180 2190 2200
QDGIGQRQAV VRTLNATGEE IIQQSSKTDV NILQEKLGSL SLRWHDICKE
2210 2220 2230 2240 2250
LAERRKRIEE QKNVLSEFQR DLNEFVLWLE EADNIAITPL GDEQQLKEQL
2260 2270 2280 2290 2300
EQVKLLAEEL PLRQGILKQL NETGGAVLVS APIRPEEQDK LEKKLKQTNL
2310 2320 2330 2340 2350
QWIKVSRALP EKQGELEVHL KDFRQLEEQL DHLLLWLSPI RNQLEIYNQP
2360 2370 2380 2390 2400
SQAGPFDIKE IEVTVHGKQA DVERLLSKGQ HLYKEKPSTQ PVKRKLEDLR
2410 2420 2430 2440 2450
SEWEAVNHLL RELRTKQPDR APGLSTTGAS ASQTVTLVTQ SVVTKETVIS
2460 2470 2480 2490 2500
KLEMPSSLLL EVPALADFNR AWTELTDWLS LLDRVIKSQR VMVGDLEDIN
2510 2520 2530 2540 2550
EMIIKQKATL QDLEQRRPQL EELITAAQNL KNKTSNQEAR TIITDRIERI
2560 2570 2580 2590 2600
QIQWDEVQEQ LQNRRQQLNE MLKDSTQWLE AKEEAEQVIG QVRGKLDSWK
2610 2620 2630 2640 2650
EGPHTVDAIQ KKITETKQLA KDLRQRQISV DVANDLALKL LRDYSADDTR
2660 2670 2680 2690 2700
KVHMITENIN TSWGNIHKRV SEQEAALEET HRLLQQFPLD LEKFLSWITE
2710 2720 2730 2740 2750
AETTANVLQD ASRKEKLLED SRGVRELMKP WQDLQGEIET HTDIYHNLDE
2760 2770 2780 2790 2800
NGQKILRSLE GSDEAPLLQR RLDNMNFKWS ELQKKSLNIR SHLEASSDQW
2810 2820 2830 2840 2850
KRLHLSLQEL LVWLQLKDDE LSRQAPIGGD FPAVQKQNDI HRAFKRELKT
2860 2870 2880 2890 2900
KEPVIMSTLE TVRIFLTEQP LEGLEKLYQE PRELPPEERA QNVTRLLRKQ
2910 2920 2930 2940 2950
AEEVNAEWDK LNLRSADWQR KIDEALERLQ ELQEAADELD LKLRQAEVIK
2960 2970 2980 2990 3000
GSWQPVGDLL IDSLQDHLEK VKALRGEIAP LKENVNRVND LAHQLTTLGI
3010 3020 3030 3040 3050
QLSPYNLSTL EDLNTRWRLL QVAVEDRVRQ LHEAHRDFGP ASQHFLSTSV
3060 3070 3080 3090 3100
QGPWERAISP NKVPYYINHE TQTTCWDHPK MTELYQSLAD LNNVRFSAYR
3110 3120 3130 3140 3150
TAMKLRRLQK ALCLDLLSLS AACDALDQHN LKQNDQPMDI LQIINCLTTI
3160 3170 3180 3190 3200
YDRLEQEHNN LVNVPLCVDM CLNWLLNVYD TGRTGRIRVL SFKTGIISLC
3210 3220 3230 3240 3250
KAHLEDKYRY LFKQVASSTG FCDQRRLGLL LHDSIQIPRQ LGEVASFGGS
3260 3270 3280 3290 3300
NIEPSVRSCF QFANNKPEIE AALFLDWMRL EPQSMVWLPV LHRVAAAETA
3310 3320 3330 3340 3350
KHQAKCNICK ECPIIGFRYR SLKHFNYDIC QSCFFSGRVA KGHKMHYPMV
3360 3370 3380 3390 3400
EYCTPTTSGE DVRDFAKVLK NKFRTKRYFA KHPRMGYLPV QTVLEGDNME
3410 3420 3430 3440 3450
TPVTLINFWP VDSAPASSPQ LSHDDTHSRI EHYASRLAEM ENSNGSYLND
3460 3470 3480 3490 3500
SISPNESIDD EHLLIQHYCQ SLNQDSPLSQ PRSPAQILIS LESEERGELE
3510 3520 3530 3540 3550
RILADLEEEN RNLQAEYDRL KQQHEHKGLS PLPSPPEMMP TSPQSPRDAE
3560 3570 3580 3590 3600
LIAEAKLLRQ HKGRLEARMQ ILEDHNKQLE SQLHRLRQLL EQPQAEAKVN
3610 3620 3630 3640 3650
GTTVSSPSTS LQRSDSSQPM LLRVVGSQTS ESMGEEDLLS PPQDTSTGLE
3660 3670
EVMEQLNNSF PSSRGRNAPG KPMREDTM
Length:3,678
Mass (Da):425,832
Last modified:July 27, 2011 - v3
Checksum:i53487B1E27104228
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti463 – 4631D → H in AAA37530. (PubMed:3659917)Curated
Sequence conflicti677 – 6771S → F in AAA37530. (PubMed:3659917)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M68859 mRNA. Translation: AAB02797.1.
AL645848
, AL645477, AL645857, AL672146, AL731776, AL732449, AL806516, AL808024, AL833800, AL844151, BX000479, BX294443, CR352330, CR382328 Genomic DNA. Translation: CAM14696.1.
BX000479
, AL645477, AL645848, AL645857, AL672146, AL731776, AL732449, AL806516, AL808024, AL833800, AL844151, BX294443, CR352330, CR382328 Genomic DNA. Translation: CAM14885.1.
AL808024
, AL645477, AL645848, AL645857, AL672146, AL731776, AL732449, AL806516, AL833800, AL844151, BX000479, BX294443, CR352330, CR382328 Genomic DNA. Translation: CAM15174.1.
AL833800
, AL645477, AL645848, AL645857, AL672146, AL731776, AL732449, AL806516, AL808024, AL844151, BX000479, BX294443, CR352330, CR382328 Genomic DNA. Translation: CAM15349.1.
AL645477
, AL645848, AL645857, AL672146, AL731776, AL732449, AL806516, AL808024, AL833800, AL844151, BX000479, BX294443, CR352330, CR382328 Genomic DNA. Translation: CAM15656.1.
AL645857
, AL645477, AL645848, AL672146, AL731776, AL732449, AL806516, AL808024, AL833800, AL844151, BX000479, BX294443, CR352330, CR382328 Genomic DNA. Translation: CAM16090.1.
AL732449
, AL645477, AL645848, AL645857, AL672146, AL731776, AL806516, AL808024, AL833800, AL844151, BX000479, BX294443, CR352330, CR382328 Genomic DNA. Translation: CAM17038.1.
BX294443
, AL645477, AL645848, AL645857, AL672146, AL731776, AL732449, AL806516, AL808024, AL833800, AL844151, BX000479, CR352330, CR382328 Genomic DNA. Translation: CAM20240.1.
CR382328
, AL645477, AL645848, AL645857, AL672146, AL731776, AL732449, AL806516, AL808024, AL833800, AL844151, BX000479, BX294443, CR352330 Genomic DNA. Translation: CAM20576.1.
CR352330
, AL645477, AL645848, AL645857, AL672146, AL731776, AL732449, AL806516, AL808024, AL833800, AL844151, BX000479, BX294443, CR382328 Genomic DNA. Translation: CAM22468.1.
AL672146
, AL645477, AL645848, AL645857, AL731776, AL732449, AL806516, AL808024, AL833800, AL844151, BX000479, BX294443, CR352330, CR382328 Genomic DNA. Translation: CAM22949.1.
AL806516
, AL645477, AL645848, AL645857, AL672146, AL731776, AL732449, AL808024, AL833800, AL844151, BX000479, BX294443, CR352330, CR382328 Genomic DNA. Translation: CAM24749.1.
AL731776
, AL645477, AL645848, AL645857, AL672146, AL732449, AL806516, AL808024, AL833800, AL844151, BX000479, BX294443, CR352330, CR382328 Genomic DNA. Translation: CAM26197.1.
AL844151
, AL645477, AL645848, AL645857, AL672146, AL731776, AL732449, AL806516, AL808024, AL833800, BX000479, BX294443, CR352330, CR382328 Genomic DNA. Translation: CAM26796.1.
X58153 Genomic DNA. Translation: CAA41157.1.
M18025 mRNA. Translation: AAA37530.1.
U56724 Genomic DNA. Translation: AAB01216.1.
U15218 mRNA. Translation: AAA87068.1.
CCDSiCCDS41047.1. [P11531-1]
PIRiS28916.
RefSeqiNP_031894.1. NM_007868.5. [P11531-1]
UniGeneiMm.275608.
Mm.416750.

Genome annotation databases

EnsembliENSMUST00000114000; ENSMUSP00000109633; ENSMUSG00000045103. [P11531-1]
GeneIDi13405.
KEGGimmu:13405.
UCSCiuc009tri.2. mouse. [P11531-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M68859 mRNA. Translation: AAB02797.1 .
AL645848
, AL645477 , AL645857 , AL672146 , AL731776 , AL732449 , AL806516 , AL808024 , AL833800 , AL844151 , BX000479 , BX294443 , CR352330 , CR382328 Genomic DNA. Translation: CAM14696.1 .
BX000479
, AL645477 , AL645848 , AL645857 , AL672146 , AL731776 , AL732449 , AL806516 , AL808024 , AL833800 , AL844151 , BX294443 , CR352330 , CR382328 Genomic DNA. Translation: CAM14885.1 .
AL808024
, AL645477 , AL645848 , AL645857 , AL672146 , AL731776 , AL732449 , AL806516 , AL833800 , AL844151 , BX000479 , BX294443 , CR352330 , CR382328 Genomic DNA. Translation: CAM15174.1 .
AL833800
, AL645477 , AL645848 , AL645857 , AL672146 , AL731776 , AL732449 , AL806516 , AL808024 , AL844151 , BX000479 , BX294443 , CR352330 , CR382328 Genomic DNA. Translation: CAM15349.1 .
AL645477
, AL645848 , AL645857 , AL672146 , AL731776 , AL732449 , AL806516 , AL808024 , AL833800 , AL844151 , BX000479 , BX294443 , CR352330 , CR382328 Genomic DNA. Translation: CAM15656.1 .
AL645857
, AL645477 , AL645848 , AL672146 , AL731776 , AL732449 , AL806516 , AL808024 , AL833800 , AL844151 , BX000479 , BX294443 , CR352330 , CR382328 Genomic DNA. Translation: CAM16090.1 .
AL732449
, AL645477 , AL645848 , AL645857 , AL672146 , AL731776 , AL806516 , AL808024 , AL833800 , AL844151 , BX000479 , BX294443 , CR352330 , CR382328 Genomic DNA. Translation: CAM17038.1 .
BX294443
, AL645477 , AL645848 , AL645857 , AL672146 , AL731776 , AL732449 , AL806516 , AL808024 , AL833800 , AL844151 , BX000479 , CR352330 , CR382328 Genomic DNA. Translation: CAM20240.1 .
CR382328
, AL645477 , AL645848 , AL645857 , AL672146 , AL731776 , AL732449 , AL806516 , AL808024 , AL833800 , AL844151 , BX000479 , BX294443 , CR352330 Genomic DNA. Translation: CAM20576.1 .
CR352330
, AL645477 , AL645848 , AL645857 , AL672146 , AL731776 , AL732449 , AL806516 , AL808024 , AL833800 , AL844151 , BX000479 , BX294443 , CR382328 Genomic DNA. Translation: CAM22468.1 .
AL672146
, AL645477 , AL645848 , AL645857 , AL731776 , AL732449 , AL806516 , AL808024 , AL833800 , AL844151 , BX000479 , BX294443 , CR352330 , CR382328 Genomic DNA. Translation: CAM22949.1 .
AL806516
, AL645477 , AL645848 , AL645857 , AL672146 , AL731776 , AL732449 , AL808024 , AL833800 , AL844151 , BX000479 , BX294443 , CR352330 , CR382328 Genomic DNA. Translation: CAM24749.1 .
AL731776
, AL645477 , AL645848 , AL645857 , AL672146 , AL732449 , AL806516 , AL808024 , AL833800 , AL844151 , BX000479 , BX294443 , CR352330 , CR382328 Genomic DNA. Translation: CAM26197.1 .
AL844151
, AL645477 , AL645848 , AL645857 , AL672146 , AL731776 , AL732449 , AL806516 , AL808024 , AL833800 , BX000479 , BX294443 , CR352330 , CR382328 Genomic DNA. Translation: CAM26796.1 .
X58153 Genomic DNA. Translation: CAA41157.1 .
M18025 mRNA. Translation: AAA37530.1 .
U56724 Genomic DNA. Translation: AAB01216.1 .
U15218 mRNA. Translation: AAA87068.1 .
CCDSi CCDS41047.1. [P11531-1 ]
PIRi S28916.
RefSeqi NP_031894.1. NM_007868.5. [P11531-1 ]
UniGenei Mm.275608.
Mm.416750.

3D structure databases

ProteinModelPortali P11531.
SMRi P11531. Positions 9-246, 340-455, 3040-3299.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 199245. 20 interactions.
DIPi DIP-32899N.
IntActi P11531. 6 interactions.
MINTi MINT-85369.

PTM databases

PhosphoSitei P11531.

Proteomic databases

MaxQBi P11531.
PaxDbi P11531.
PRIDEi P11531.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000114000 ; ENSMUSP00000109633 ; ENSMUSG00000045103 . [P11531-1 ]
GeneIDi 13405.
KEGGi mmu:13405.
UCSCi uc009tri.2. mouse. [P11531-1 ]

Organism-specific databases

CTDi 1756.
MGIi MGI:94909. Dmd.

Phylogenomic databases

eggNOGi COG5069.
GeneTreei ENSGT00760000119237.
HOGENOMi HOG000231173.
HOVERGENi HBG005495.
InParanoidi P11531.
KOi K10366.
OMAi EGPYTMD.
OrthoDBi EOG7V765N.
TreeFami TF320178.

Enzyme and pathway databases

Reactomei REACT_196607. Non-integrin membrane-ECM interactions.
REACT_232053. Striated Muscle Contraction.

Miscellaneous databases

ChiTaRSi Dmd. mouse.
NextBioi 283803.
PROi P11531.
SOURCEi Search...

Gene expression databases

Bgeei P11531.
CleanExi MM_DMD.
ExpressionAtlasi P11531. baseline and differential.
Genevestigatori P11531.

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. 16 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. "Human and murine dystrophin mRNA transcripts are differentially expressed during skeletal muscle, heart, and brain development."
    Bies R.D., Phelps S.F., Cortez M.D., Roberts R., Caskey C.T., Chamberlain J.S.
    Nucleic Acids Res. 20:1725-1731(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/10.
    Tissue: Skeletal muscle.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "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 1-201.
  4. "Sequence analysis of two exons from the murine dystrophin locus."
    Maconochie M.K., Brown S.D.M., Greenfield A.J.
    Mamm. Genome 2:64-68(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 120-176.
    Strain: 129/J.
  5. "Conservation of the Duchenne muscular dystrophy gene in mice and humans."
    Hoffman E.P., Monaco A.P., Feener C.C., Kunkel L.M.
    Science 238:347-350(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 300-1390.
  6. "PCR analysis of muscular dystrophy in mdx mice."
    Chamberlain J.S., Phelps S.F., Cox G.A., Maichele A.J., Greenwood A.D.
    Mol. Cell Biol. Hum. Dis. Ser. 3:167-189(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 986-1056.
    Strain: C57BL/10.
    Tissue: Skeletal muscle.
  7. Lubec G., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 1129-1134, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: OF1.
    Tissue: Hippocampus.
  8. "Characterization and cell type distribution of a novel, major transcript of the Duchenne muscular dystrophy gene."
    Rapaport D., Lederfein D., den Dunnen J.T., Grootscholten P.M., van Ommen G.J.B., Fuchs O., Nudel U., Yaffe D.
    Differentiation 49:187-193(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3069-3181.
  9. "A novel dystrophin isoform is required for normal retinal electrophysiology."
    D'Souza V.N., Nguyen T.M., Morris G.E., Karges W., Pillers D.-A.M., Ray P.N.
    Hum. Mol. Genet. 4:837-842(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING, FUNCTION, TISSUE SPECIFICITY.
    Strain: C57BL/10.
    Tissue: Retina.
  10. "Interactions between dystrophin glycoprotein complex proteins."
    Madhavan R., Jarrett H.W.
    Biochemistry 34:12204-12209(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SNTA1 IN THE DYSTROPHIN-ASSOCIATED GLYCOPROTEIN COMPLEX.
  11. "Differential association of syntrophin pairs with the dystrophin complex."
    Peters M.F., Adams M.E., Froehner S.C.
    J. Cell Biol. 138:81-93(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SNTB1 IN THE DYSTROPHIN-ASSOCIATED GLYCOPROTEIN COMPLEX.
  12. "Dystroglycan contributes to the formation of multiple dystrophin-like complexes in brain."
    Moukhles H., Carbonetto S.
    J. Neurochem. 78:824-834(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DAG1 IN THE DYSTROPHIN-ASSOCIATED GLYCOPROTEIN COMPLEX.
  13. "Interactions of intermediate filament protein synemin with dystrophin and utrophin."
    Bhosle R.C., Michele D.E., Campbell K.P., Li Z., Robson R.M.
    Biochem. Biophys. Res. Commun. 346:768-777(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SYNM.
  14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3616 AND SER-3617, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  15. "An ankyrin-based mechanism for functional organization of dystrophin and dystroglycan."
    Ayalon G., Davis J.Q., Scotland P.B., Bennett V.
    Cell 135:1189-1200(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ANK2 AND ANK3, SUBCELLULAR LOCATION.
  16. "Interactions with M-band titin and calpain 3 link myospryn (CMYA5) to tibial and limb-girdle muscular dystrophies."
    Sarparanta J., Blandin G., Charton K., Vihola A., Marchand S., Milic A., Hackman P., Ehler E., Richard I., Udd B.
    J. Biol. Chem. 285:30304-30315(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CMYA5.

Entry informationi

Entry nameiDMD_MOUSE
AccessioniPrimary (citable) accession number: P11531
Secondary accession number(s): A2A9Z0, O35653, Q60703
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: July 27, 2011
Last modified: November 26, 2014
This is version 152 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3