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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-type
Add
BLAST

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. nitric-oxide synthase binding Source: BHF-UCL
  3. protein binding Source: IntAct
  4. zinc ion binding Source: InterPro
Complete GO annotation...

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

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; Peripheral membrane protein; Cytoplasmic side. Cytoplasmcytoskeleton. Cell junctionsynapsepostsynaptic cell membrane
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.1 Publication

GO - Cellular componenti

  1. Z disc Source: MGI
  2. cell-substrate junction Source: MGI
  3. cytoskeleton Source: UniProtKB-SubCell
  4. dystrophin-associated glycoprotein complex Source: MGI
  5. membrane raft Source: MGI
  6. neuron projection terminus Source: MGI
  7. plasma membrane Source: MGI
  8. postsynaptic membrane Source: UniProtKB-SubCell
  9. protein complex Source: MGI
  10. sarcolemma Source: MGI
  11. synapse 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 – 36783678Dystrophin
PRO_0000076076Add
BLAST

Amino acid modifications

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

ArrayExpressiP11531.
BgeeiP11531.
CleanExiMM_DMD.
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.6 Publications

Binary interactionsi

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

Protein-protein interaction databases

BioGridi199245. 19 interactions.
DIPiDIP-32899N.
IntActiP11531. 6 interactions.
MINTiMINT-85369.

Structurei

3D structure databases

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 240240Actin-binding
Add
BLAST
Domaini15 – 119105CH 1
Add
BLAST
Domaini134 – 237104CH 2
Add
BLAST
Repeati341 – 449109Spectrin 1
Add
BLAST
Repeati450 – 558109Spectrin 2
Add
BLAST
Repeati561 – 669109Spectrin 3
Add
BLAST
Repeati721 – 830110Spectrin 4
Add
BLAST
Repeati832 – 936105Spectrin 5
Add
BLAST
Repeati945 – 1047103Spectrin 6
Add
BLAST
Repeati1050 – 1156107Spectrin 7
Add
BLAST
Repeati1159 – 1265107Spectrin 8
Add
BLAST
Repeati1268 – 1369102Spectrin 9
Add
BLAST
Repeati1370 – 146596Spectrin 10
Add
BLAST
Repeati1470 – 1570101Spectrin 11
Add
BLAST
Repeati1573 – 1678106Spectrin 12
Add
BLAST
Repeati1681 – 1780100Spectrin 13
Add
BLAST
Repeati1781 – 187696Spectrin 14
Add
BLAST
Repeati1879 – 1981103Spectrin 15
Add
BLAST
Repeati1994 – 2103110Spectrin 16
Add
BLAST
Repeati2106 – 2210105Spectrin 17
Add
BLAST
Repeati2213 – 2318106Spectrin 18
Add
BLAST
Repeati2319 – 241698Spectrin 19
Add
BLAST
Repeati2468 – 2570103Spectrin 20
Add
BLAST
Repeati2573 – 2679107Spectrin 21
Add
BLAST
Repeati2682 – 2795114Spectrin 22
Add
BLAST
Repeati2801 – 2923123Spectrin 23
Add
BLAST
Repeati2928 – 3033106Spectrin 24
Add
BLAST
Domaini3048 – 308134WW
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni63 – 7210ANK2- and ANK-3 binding
Regioni1417 – 1915499Interaction with SYNM
Add
BLAST
Regioni3051 – 3401351Interaction with SYNM
Add
BLAST
Regioni3459 – 351153Binds to SNTB1 By similarity
Add
BLAST

Sequence similaritiesi

Contains 24 spectrin repeats.
Contains 1 WW domain.

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG5069.
GeneTreeiENSGT00740000115262.
HOGENOMiHOG000231173.
HOVERGENiHBG005495.
InParanoidiA2A9Z0.
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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MLWWEEVEDC YEREDVQKKT FTKWINAQFS KFGKQHIDNL FSDLQDGKRL     50
LDLLEGLTGQ KLPKEKGSTR VHALNNVNKA LRVLQKNNVD LVNIGSTDIV 100
DGNHKLTLGL IWNIILHWQV KNVMKTIMAG LQQTNSEKIL LSWVRQSTRN 150
YPQVNVINFT SSWSDGLALN ALIHSHRPDL FDWNSVVSQH SATQRLEHAF 200
NIAKCQLGIE KLLDPEDVAT TYPDKKSILM YITSLFQVLP QQVSIEAIQE 250
VEMLPRTSSK VTREEHFQLH HQMHYSQQIT VSLAQGYEQT SSSPKPRFKS 300
YAFTQAAYVA TSDSTQSPYP SQHLEAPRDK SLDSSLMETE VNLDSYQTAL 350
EEVLSWLLSA EDTLRAQGEI SNDVEEVKEQ FHAHEGFMMD LTSHQGLVGN 400
VLQLGSQLVG KGKLSEDEEA EVQEQMNLLN SRWECLRVAS MEKQSKLHKV 450
LMDLQNQKLK ELDDWLTKTE ERTKKMEEEP FGPDLEDLKC QVQQHKVLQE 500
DLEQEQVRVN SLTHMVVVVD ESSGDHATAA LEEQLKVLGD RWANICRWTE 550
DRWIVLQDIL LKWQHFTEEQ CLFSTWLSEK EDAMKNIQTS GFKDQNEMMS 600
SLHKISTLKI DLEKKKPTME KLSSLNQDLL SALKNKSVTQ KMEIWMENFA 650
QRWDNLTQKL EKSSAQISQA VTTTQPSLTQ TTVMETVTMV TTREQIMVKH 700
AQEELPPPPP QKKRQITVDS ELRKRLDVDI TELHSWITRS EAVLQSSEFA 750
VYRKEGNISD LQEKVNAIAR EKAEKFRKLQ DASRSAQALV EQMANEGVNA 800
ESIRQASEQL NSRWTEFCQL LSERVNWLEY QTNIITFYNQ LQQLEQMTTT 850
AENLLKTQST TLSEPTAIKS QLKICKDEVN RLSALQPQIE QLKIQSLQLK 900
EKGQGPMFLD ADFVAFTNHF NHIFDGVRAK EKELQTIFDT LPPMRYQETM 950
SSIRTWIQQS ESKLSVPYLS VTEYEIMEER LGKLQALQSS LKEQQNGFNY 1000
LSDTVKEMAK KAPSEICQKY LSEFEEIEGH WKKLSSQLVE SCQKLEEHMN 1050
KLRKFQNHIK TLQKWMAEVD VFLKEEWPAL GDAEILKKQL KQCRLLVGDI 1100
QTIQPSLNSV NEGGQKIKSE AELEFASRLE TELRELNTQW DHICRQVYTR 1150
KEALKAGLDK TVSLQKDLSE MHEWMTQAEE EYLERDFEYK TPDELQTAVE 1200
EMKRAKEEAL QKETKVKLLT ETVNSVIAHA PPSAQEALKK ELETLTTNYQ 1250
WLCTRLNGKC KTLEEVWACW HELLSYLEKA NKWLNEVELK LKTMENVPAG 1300
PEEITEVLES LENLMHHSEE NPNQIRLLAQ TLTDGGVMDE LINEELETFN 1350
SRWRELHEEA VRKQKLLEQS IQSAQEIEKS LHLIQESLEF IDKQLAAYIT 1400
DKVDAAQMPQ EAQKIQSDLT SHEISLEEMK KHNQGKDANQ RVLSQIDVAQ 1450
KKLQDVSMKF RLFQKPANFE QRLEESKMIL DEVKMHLPAL ETKSVEQEVI 1500
QSQLSHCVNL YKSLSEVKSE VEMVIKTGRQ IVQKKQTENP KELDERVTAL 1550
KLHYNELGAK VTERKQQLEK CLKLSRKMRK EMNVLTEWLA ATDTELTKRS 1600
AVEGMPSNLD SEVAWGKATQ KEIEKQKAHL KSVTELGESL KMVLGKKETL 1650
VEDKLSLLNS NWIAVTSRVE EWLNLLLEYQ KHMETFDQNI EQITKWIIHA 1700
DELLDESEKK KPQQKEDILK RLKAEMNDMR PKVDSTRDQA AKLMANRGDH 1750
CRKVVEPQIS ELNRRFAAIS HRIKTGKASI PLKELEQFNS DIQKLLEPLE 1800
AEIQQGVNLK EEDFNKDMSE DNEGTVNELL QRGDNLQQRI TDERKREEIK 1850
IKQQLLQTKH NALKDLRSQR RKKALEISHQ WYQYKRQADD LLKCLDEIEK 1900
KLASLPEPRD ERKLKEIDRE LQKKKEELNA VRRQAEGLSE NGAAMAVEPT 1950
QIQLSKRWRQ IESNFAQFRR LNFAQIHTLH EETMVVTTED MPLDVSYVPS 2000
TYLTEISHIL QALSEVDHLL NTPELCAKDF EDLFKQEESL KNIKDNLQQI 2050
SGRIDIIHKK KTAALQSATS MEKVKVQEAV AQMDFQGEKL HRMYKERQGR 2100
FDRSVEKWRH FHYDMKVFNQ WLNEVEQFFK KTQNPENWEH AKYKWYLKEL 2150
QDGIGQRQAV VRTLNATGEE IIQQSSKTDV NILQEKLGSL SLRWHDICKE 2200
LAERRKRIEE QKNVLSEFQR DLNEFVLWLE EADNIAITPL GDEQQLKEQL 2250
EQVKLLAEEL PLRQGILKQL NETGGAVLVS APIRPEEQDK LEKKLKQTNL 2300
QWIKVSRALP EKQGELEVHL KDFRQLEEQL DHLLLWLSPI RNQLEIYNQP 2350
SQAGPFDIKE IEVTVHGKQA DVERLLSKGQ HLYKEKPSTQ PVKRKLEDLR 2400
SEWEAVNHLL RELRTKQPDR APGLSTTGAS ASQTVTLVTQ SVVTKETVIS 2450
KLEMPSSLLL EVPALADFNR AWTELTDWLS LLDRVIKSQR VMVGDLEDIN 2500
EMIIKQKATL QDLEQRRPQL EELITAAQNL KNKTSNQEAR TIITDRIERI 2550
QIQWDEVQEQ LQNRRQQLNE MLKDSTQWLE AKEEAEQVIG QVRGKLDSWK 2600
EGPHTVDAIQ KKITETKQLA KDLRQRQISV DVANDLALKL LRDYSADDTR 2650
KVHMITENIN TSWGNIHKRV SEQEAALEET HRLLQQFPLD LEKFLSWITE 2700
AETTANVLQD ASRKEKLLED SRGVRELMKP WQDLQGEIET HTDIYHNLDE 2750
NGQKILRSLE GSDEAPLLQR RLDNMNFKWS ELQKKSLNIR SHLEASSDQW 2800
KRLHLSLQEL LVWLQLKDDE LSRQAPIGGD FPAVQKQNDI HRAFKRELKT 2850
KEPVIMSTLE TVRIFLTEQP LEGLEKLYQE PRELPPEERA QNVTRLLRKQ 2900
AEEVNAEWDK LNLRSADWQR KIDEALERLQ ELQEAADELD LKLRQAEVIK 2950
GSWQPVGDLL IDSLQDHLEK VKALRGEIAP LKENVNRVND LAHQLTTLGI 3000
QLSPYNLSTL EDLNTRWRLL QVAVEDRVRQ LHEAHRDFGP ASQHFLSTSV 3050
QGPWERAISP NKVPYYINHE TQTTCWDHPK MTELYQSLAD LNNVRFSAYR 3100
TAMKLRRLQK ALCLDLLSLS AACDALDQHN LKQNDQPMDI LQIINCLTTI 3150
YDRLEQEHNN LVNVPLCVDM CLNWLLNVYD TGRTGRIRVL SFKTGIISLC 3200
KAHLEDKYRY LFKQVASSTG FCDQRRLGLL LHDSIQIPRQ LGEVASFGGS 3250
NIEPSVRSCF QFANNKPEIE AALFLDWMRL EPQSMVWLPV LHRVAAAETA 3300
KHQAKCNICK ECPIIGFRYR SLKHFNYDIC QSCFFSGRVA KGHKMHYPMV 3350
EYCTPTTSGE DVRDFAKVLK NKFRTKRYFA KHPRMGYLPV QTVLEGDNME 3400
TPVTLINFWP VDSAPASSPQ LSHDDTHSRI EHYASRLAEM ENSNGSYLND 3450
SISPNESIDD EHLLIQHYCQ SLNQDSPLSQ PRSPAQILIS LESEERGELE 3500
RILADLEEEN RNLQAEYDRL KQQHEHKGLS PLPSPPEMMP TSPQSPRDAE 3550
LIAEAKLLRQ HKGRLEARMQ ILEDHNKQLE SQLHRLRQLL EQPQAEAKVN 3600
GTTVSSPSTS LQRSDSSQPM LLRVVGSQTS ESMGEEDLLS PPQDTSTGLE 3650
EVMEQLNNSF PSSRGRNAPG KPMREDTM 3678
Length:3,678
Mass (Da):425,832
Last modified:July 27, 2011 - v3
Checksum:i53487B1E27104228
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti463 – 4631D → H in AAA37530. 1 Publication
Sequence conflicti677 – 6771S → F in AAA37530. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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...

Protein-protein interaction databases

BioGridi 199245. 19 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 ENSGT00740000115262.
HOGENOMi HOG000231173.
HOVERGENi HBG005495.
InParanoidi A2A9Z0.
KOi K10366.
OMAi EGPYTMD.
OrthoDBi EOG7V765N.
TreeFami TF320178.

Miscellaneous databases

NextBioi 283803.
PROi P11531.
SOURCEi Search...

Gene expression databases

ArrayExpressi P11531.
Bgeei P11531.
CleanExi MM_DMD.
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: July 9, 2014
This is version 149 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

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