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P11531 (DMD_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 149. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dystrophin
Gene names
Name:Dmd
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length3678 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.9

Subunit structure

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. Ref.10 Ref.11 Ref.12 Ref.13 Ref.15 Ref.16

Subcellular location

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. Ref.15

Tissue specificity

Differentially expressed during skeletal muscle, heart, and brain development. Also expressed in retina. Ref.9

Sequence similarities

Contains 2 CH (calponin-homology) domains.

Contains 24 spectrin repeats.

Contains 1 WW domain.

Contains 1 ZZ-type zinc finger.

Ontologies

Keywords
   Cellular componentCell junction
Cell membrane
Cytoplasm
Cytoskeleton
Membrane
Postsynaptic cell membrane
Synapse
   Coding sequence diversityAlternative splicing
   DomainRepeat
Zinc-finger
   LigandActin-binding
Calcium
Metal-binding
Zinc
   PTMPhosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcardiac muscle cell action potential

Inferred from mutant phenotype PubMed 20080623PubMed 21677768. Source: BHF-UCL

cellular protein complex assembly

Inferred from mutant phenotype PubMed 19198614PubMed 20080623. Source: BHF-UCL

cellular protein localization

Inferred from mutant phenotype PubMed 7545544. Source: BHF-UCL

establishment of blood-nerve barrier

Inferred from mutant phenotype PubMed 12673830. Source: MGI

establishment of glial blood-brain barrier

Inferred from mutant phenotype PubMed 12673830. Source: MGI

muscle cell cellular homeostasis

Inferred from mutant phenotype PubMed 6583703. Source: MGI

muscle fiber development

Inferred from genetic interaction PubMed 8007658. Source: MGI

muscle organ development

Inferred from mutant phenotype PubMed 14645204. Source: MGI

myotube cell development

Inferred from mutant phenotype PubMed 19535499. Source: MGI

negative regulation of peptidyl-cysteine S-nitrosylation

Inferred from mutant phenotype PubMed 19198614PubMed 20080623. Source: BHF-UCL

negative regulation of peptidyl-serine phosphorylation

Inferred from mutant phenotype PubMed 23263329. Source: BHF-UCL

neurotransmitter receptor metabolic process

Inferred from mutant phenotype PubMed 9334395. Source: MGI

nucleus localization

Inferred from mutant phenotype PubMed 19535499. Source: MGI

olfactory nerve structural organization

Inferred from mutant phenotype PubMed 18586242. Source: MGI

positive regulation of cell-matrix adhesion

Inferred from mutant phenotype PubMed 12370193. Source: BHF-UCL

positive regulation of sodium ion transmembrane transporter activity

Inferred from mutant phenotype PubMed 21677768. Source: BHF-UCL

regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion

Inferred from mutant phenotype PubMed 20080623. Source: BHF-UCL

regulation of gene expression

Inferred from mutant phenotype PubMed 22000014. Source: MGI

regulation of heart rate

Inferred from mutant phenotype PubMed 20080623. Source: BHF-UCL

regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum

Inferred from mutant phenotype PubMed 20080623PubMed 23263329. Source: BHF-UCL

regulation of ryanodine-sensitive calcium-release channel activity

Inferred from mutant phenotype PubMed 20080623. Source: BHF-UCL

regulation of skeletal muscle contraction

Inferred from mutant phenotype PubMed 19198614. Source: BHF-UCL

regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion

Inferred from mutant phenotype PubMed 19198614. Source: BHF-UCL

regulation of transcription, DNA-templated

Inferred from mutant phenotype PubMed 7919967. Source: MGI

regulation of voltage-gated calcium channel activity

Inferred from mutant phenotype PubMed 21677768. Source: BHF-UCL

skeletal muscle tissue development

Inferred from mutant phenotype PubMed 16371353. Source: MGI

   Cellular_componentZ disc

Inferred from direct assay PubMed 7890770. Source: MGI

cell-substrate junction

Inferred from direct assay PubMed 7890770. Source: MGI

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

dystrophin-associated glycoprotein complex

Inferred from direct assay PubMed 7890770. Source: MGI

membrane raft

Inferred from direct assay PubMed 11259414. Source: MGI

neuron projection terminus

Inferred from direct assay PubMed 12115694. Source: MGI

plasma membrane

Inferred from direct assay PubMed 14627610. Source: MGI

postsynaptic membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

protein complex

Inferred from sequence orthology PubMed 18468998. Source: MGI

sarcolemma

Inferred from direct assay PubMed 11115849PubMed 11259414PubMed 16371353PubMed 16810681PubMed 7890770PubMed 8663016. Source: MGI

synapse

Inferred from direct assay PubMed 10995443. Source: MGI

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

nitric-oxide synthase binding

Inferred from physical interaction PubMed 7545544. Source: BHF-UCL

protein binding

Inferred from physical interaction Ref.11. Source: IntAct

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Snta1Q612342EBI-295928,EBI-295952

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: At least 11 isoforms are produced.
Isoform 1 (identifier: P11531-1)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 36783678Dystrophin
PRO_0000076076

Regions

Domain1 – 240240Actin-binding
Domain15 – 119105CH 1
Domain134 – 237104CH 2
Repeat341 – 449109Spectrin 1
Repeat450 – 558109Spectrin 2
Repeat561 – 669109Spectrin 3
Repeat721 – 830110Spectrin 4
Repeat832 – 936105Spectrin 5
Repeat945 – 1047103Spectrin 6
Repeat1050 – 1156107Spectrin 7
Repeat1159 – 1265107Spectrin 8
Repeat1268 – 1369102Spectrin 9
Repeat1370 – 146596Spectrin 10
Repeat1470 – 1570101Spectrin 11
Repeat1573 – 1678106Spectrin 12
Repeat1681 – 1780100Spectrin 13
Repeat1781 – 187696Spectrin 14
Repeat1879 – 1981103Spectrin 15
Repeat1994 – 2103110Spectrin 16
Repeat2106 – 2210105Spectrin 17
Repeat2213 – 2318106Spectrin 18
Repeat2319 – 241698Spectrin 19
Repeat2468 – 2570103Spectrin 20
Repeat2573 – 2679107Spectrin 21
Repeat2682 – 2795114Spectrin 22
Repeat2801 – 2923123Spectrin 23
Repeat2928 – 3033106Spectrin 24
Domain3048 – 308134WW
Zinc finger3300 – 334748ZZ-type
Region63 – 7210ANK2- and ANK-3 binding
Region1417 – 1915499Interaction with SYNM
Region3051 – 3401351Interaction with SYNM
Region3459 – 351153Binds to SNTB1 By similarity

Amino acid modifications

Modified residue34761Phosphoserine By similarity
Modified residue36051Phosphoserine By similarity
Modified residue36061Phosphoserine By similarity
Modified residue36101Phosphoserine By similarity
Modified residue36161Phosphoserine Ref.14
Modified residue36171Phosphoserine Ref.14
Modified residue36591Phosphoserine By similarity

Experimental info

Sequence conflict4631D → H in AAA37530. Ref.5
Sequence conflict6771S → F in AAA37530. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: 53487B1E27104228

FASTA3,678425,832
        10         20         30         40         50         60 
MLWWEEVEDC YEREDVQKKT FTKWINAQFS KFGKQHIDNL FSDLQDGKRL LDLLEGLTGQ 

        70         80         90        100        110        120 
KLPKEKGSTR VHALNNVNKA LRVLQKNNVD LVNIGSTDIV DGNHKLTLGL IWNIILHWQV 

       130        140        150        160        170        180 
KNVMKTIMAG LQQTNSEKIL LSWVRQSTRN YPQVNVINFT SSWSDGLALN ALIHSHRPDL 

       190        200        210        220        230        240 
FDWNSVVSQH SATQRLEHAF NIAKCQLGIE KLLDPEDVAT TYPDKKSILM YITSLFQVLP 

       250        260        270        280        290        300 
QQVSIEAIQE VEMLPRTSSK VTREEHFQLH HQMHYSQQIT VSLAQGYEQT SSSPKPRFKS 

       310        320        330        340        350        360 
YAFTQAAYVA TSDSTQSPYP SQHLEAPRDK SLDSSLMETE VNLDSYQTAL EEVLSWLLSA 

       370        380        390        400        410        420 
EDTLRAQGEI SNDVEEVKEQ FHAHEGFMMD LTSHQGLVGN VLQLGSQLVG KGKLSEDEEA 

       430        440        450        460        470        480 
EVQEQMNLLN SRWECLRVAS MEKQSKLHKV LMDLQNQKLK ELDDWLTKTE ERTKKMEEEP 

       490        500        510        520        530        540 
FGPDLEDLKC QVQQHKVLQE DLEQEQVRVN SLTHMVVVVD ESSGDHATAA LEEQLKVLGD 

       550        560        570        580        590        600 
RWANICRWTE DRWIVLQDIL LKWQHFTEEQ CLFSTWLSEK EDAMKNIQTS GFKDQNEMMS 

       610        620        630        640        650        660 
SLHKISTLKI DLEKKKPTME KLSSLNQDLL SALKNKSVTQ KMEIWMENFA QRWDNLTQKL 

       670        680        690        700        710        720 
EKSSAQISQA VTTTQPSLTQ TTVMETVTMV TTREQIMVKH AQEELPPPPP QKKRQITVDS 

       730        740        750        760        770        780 
ELRKRLDVDI TELHSWITRS EAVLQSSEFA VYRKEGNISD LQEKVNAIAR EKAEKFRKLQ 

       790        800        810        820        830        840 
DASRSAQALV EQMANEGVNA ESIRQASEQL NSRWTEFCQL LSERVNWLEY QTNIITFYNQ 

       850        860        870        880        890        900 
LQQLEQMTTT AENLLKTQST TLSEPTAIKS QLKICKDEVN RLSALQPQIE QLKIQSLQLK 

       910        920        930        940        950        960 
EKGQGPMFLD ADFVAFTNHF NHIFDGVRAK EKELQTIFDT LPPMRYQETM SSIRTWIQQS 

       970        980        990       1000       1010       1020 
ESKLSVPYLS VTEYEIMEER LGKLQALQSS LKEQQNGFNY LSDTVKEMAK KAPSEICQKY 

      1030       1040       1050       1060       1070       1080 
LSEFEEIEGH WKKLSSQLVE SCQKLEEHMN KLRKFQNHIK TLQKWMAEVD VFLKEEWPAL 

      1090       1100       1110       1120       1130       1140 
GDAEILKKQL KQCRLLVGDI QTIQPSLNSV NEGGQKIKSE AELEFASRLE TELRELNTQW 

      1150       1160       1170       1180       1190       1200 
DHICRQVYTR KEALKAGLDK TVSLQKDLSE MHEWMTQAEE EYLERDFEYK TPDELQTAVE 

      1210       1220       1230       1240       1250       1260 
EMKRAKEEAL QKETKVKLLT ETVNSVIAHA PPSAQEALKK ELETLTTNYQ WLCTRLNGKC 

      1270       1280       1290       1300       1310       1320 
KTLEEVWACW HELLSYLEKA NKWLNEVELK LKTMENVPAG PEEITEVLES LENLMHHSEE 

      1330       1340       1350       1360       1370       1380 
NPNQIRLLAQ TLTDGGVMDE LINEELETFN SRWRELHEEA VRKQKLLEQS IQSAQEIEKS 

      1390       1400       1410       1420       1430       1440 
LHLIQESLEF IDKQLAAYIT DKVDAAQMPQ EAQKIQSDLT SHEISLEEMK KHNQGKDANQ 

      1450       1460       1470       1480       1490       1500 
RVLSQIDVAQ KKLQDVSMKF RLFQKPANFE QRLEESKMIL DEVKMHLPAL ETKSVEQEVI 

      1510       1520       1530       1540       1550       1560 
QSQLSHCVNL YKSLSEVKSE VEMVIKTGRQ IVQKKQTENP KELDERVTAL KLHYNELGAK 

      1570       1580       1590       1600       1610       1620 
VTERKQQLEK CLKLSRKMRK EMNVLTEWLA ATDTELTKRS AVEGMPSNLD SEVAWGKATQ 

      1630       1640       1650       1660       1670       1680 
KEIEKQKAHL KSVTELGESL KMVLGKKETL VEDKLSLLNS NWIAVTSRVE EWLNLLLEYQ 

      1690       1700       1710       1720       1730       1740 
KHMETFDQNI EQITKWIIHA DELLDESEKK KPQQKEDILK RLKAEMNDMR PKVDSTRDQA 

      1750       1760       1770       1780       1790       1800 
AKLMANRGDH CRKVVEPQIS ELNRRFAAIS HRIKTGKASI PLKELEQFNS DIQKLLEPLE 

      1810       1820       1830       1840       1850       1860 
AEIQQGVNLK EEDFNKDMSE DNEGTVNELL QRGDNLQQRI TDERKREEIK IKQQLLQTKH 

      1870       1880       1890       1900       1910       1920 
NALKDLRSQR RKKALEISHQ WYQYKRQADD LLKCLDEIEK KLASLPEPRD ERKLKEIDRE 

      1930       1940       1950       1960       1970       1980 
LQKKKEELNA VRRQAEGLSE NGAAMAVEPT QIQLSKRWRQ IESNFAQFRR LNFAQIHTLH 

      1990       2000       2010       2020       2030       2040 
EETMVVTTED MPLDVSYVPS TYLTEISHIL QALSEVDHLL NTPELCAKDF EDLFKQEESL 

      2050       2060       2070       2080       2090       2100 
KNIKDNLQQI SGRIDIIHKK KTAALQSATS MEKVKVQEAV AQMDFQGEKL HRMYKERQGR 

      2110       2120       2130       2140       2150       2160 
FDRSVEKWRH FHYDMKVFNQ WLNEVEQFFK KTQNPENWEH AKYKWYLKEL QDGIGQRQAV 

      2170       2180       2190       2200       2210       2220 
VRTLNATGEE IIQQSSKTDV NILQEKLGSL SLRWHDICKE LAERRKRIEE QKNVLSEFQR 

      2230       2240       2250       2260       2270       2280 
DLNEFVLWLE EADNIAITPL GDEQQLKEQL EQVKLLAEEL PLRQGILKQL NETGGAVLVS 

      2290       2300       2310       2320       2330       2340 
APIRPEEQDK LEKKLKQTNL QWIKVSRALP EKQGELEVHL KDFRQLEEQL DHLLLWLSPI 

      2350       2360       2370       2380       2390       2400 
RNQLEIYNQP SQAGPFDIKE IEVTVHGKQA DVERLLSKGQ HLYKEKPSTQ PVKRKLEDLR 

      2410       2420       2430       2440       2450       2460 
SEWEAVNHLL RELRTKQPDR APGLSTTGAS ASQTVTLVTQ SVVTKETVIS KLEMPSSLLL 

      2470       2480       2490       2500       2510       2520 
EVPALADFNR AWTELTDWLS LLDRVIKSQR VMVGDLEDIN EMIIKQKATL QDLEQRRPQL 

      2530       2540       2550       2560       2570       2580 
EELITAAQNL KNKTSNQEAR TIITDRIERI QIQWDEVQEQ LQNRRQQLNE MLKDSTQWLE 

      2590       2600       2610       2620       2630       2640 
AKEEAEQVIG QVRGKLDSWK EGPHTVDAIQ KKITETKQLA KDLRQRQISV DVANDLALKL 

      2650       2660       2670       2680       2690       2700 
LRDYSADDTR KVHMITENIN TSWGNIHKRV SEQEAALEET HRLLQQFPLD LEKFLSWITE 

      2710       2720       2730       2740       2750       2760 
AETTANVLQD ASRKEKLLED SRGVRELMKP WQDLQGEIET HTDIYHNLDE NGQKILRSLE 

      2770       2780       2790       2800       2810       2820 
GSDEAPLLQR RLDNMNFKWS ELQKKSLNIR SHLEASSDQW KRLHLSLQEL LVWLQLKDDE 

      2830       2840       2850       2860       2870       2880 
LSRQAPIGGD FPAVQKQNDI HRAFKRELKT KEPVIMSTLE TVRIFLTEQP LEGLEKLYQE 

      2890       2900       2910       2920       2930       2940 
PRELPPEERA QNVTRLLRKQ AEEVNAEWDK LNLRSADWQR KIDEALERLQ ELQEAADELD 

      2950       2960       2970       2980       2990       3000 
LKLRQAEVIK GSWQPVGDLL IDSLQDHLEK VKALRGEIAP LKENVNRVND LAHQLTTLGI 

      3010       3020       3030       3040       3050       3060 
QLSPYNLSTL EDLNTRWRLL QVAVEDRVRQ LHEAHRDFGP ASQHFLSTSV QGPWERAISP 

      3070       3080       3090       3100       3110       3120 
NKVPYYINHE TQTTCWDHPK MTELYQSLAD LNNVRFSAYR TAMKLRRLQK ALCLDLLSLS 

      3130       3140       3150       3160       3170       3180 
AACDALDQHN LKQNDQPMDI LQIINCLTTI YDRLEQEHNN LVNVPLCVDM CLNWLLNVYD 

      3190       3200       3210       3220       3230       3240 
TGRTGRIRVL SFKTGIISLC KAHLEDKYRY LFKQVASSTG FCDQRRLGLL LHDSIQIPRQ 

      3250       3260       3270       3280       3290       3300 
LGEVASFGGS NIEPSVRSCF QFANNKPEIE AALFLDWMRL EPQSMVWLPV LHRVAAAETA 

      3310       3320       3330       3340       3350       3360 
KHQAKCNICK ECPIIGFRYR SLKHFNYDIC QSCFFSGRVA KGHKMHYPMV EYCTPTTSGE 

      3370       3380       3390       3400       3410       3420 
DVRDFAKVLK NKFRTKRYFA KHPRMGYLPV QTVLEGDNME TPVTLINFWP VDSAPASSPQ 

      3430       3440       3450       3460       3470       3480 
LSHDDTHSRI EHYASRLAEM ENSNGSYLND SISPNESIDD EHLLIQHYCQ SLNQDSPLSQ 

      3490       3500       3510       3520       3530       3540 
PRSPAQILIS LESEERGELE RILADLEEEN RNLQAEYDRL KQQHEHKGLS PLPSPPEMMP 

      3550       3560       3570       3580       3590       3600 
TSPQSPRDAE LIAEAKLLRQ HKGRLEARMQ ILEDHNKQLE SQLHRLRQLL EQPQAEAKVN 

      3610       3620       3630       3640       3650       3660 
GTTVSSPSTS LQRSDSSQPM LLRVVGSQTS ESMGEEDLLS PPQDTSTGLE EVMEQLNNSF 

      3670 
PSSRGRNAPG KPMREDTM 

« Hide

References

« Hide 'large scale' references
[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]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
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]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M68859 mRNA. Translation: AAB02797.1.
AL645848 expand/collapse EMBL AC list , AL645477, AL645857, AL672146, AL731776, AL732449, AL806516, AL808024, AL833800, AL844151, BX000479, BX294443, CR352330, CR382328 Genomic DNA. Translation: CAM14696.1.
BX000479 expand/collapse EMBL AC list , AL645477, AL645848, AL645857, AL672146, AL731776, AL732449, AL806516, AL808024, AL833800, AL844151, BX294443, CR352330, CR382328 Genomic DNA. Translation: CAM14885.1.
AL808024 expand/collapse EMBL AC list , AL645477, AL645848, AL645857, AL672146, AL731776, AL732449, AL806516, AL833800, AL844151, BX000479, BX294443, CR352330, CR382328 Genomic DNA. Translation: CAM15174.1.
AL833800 expand/collapse EMBL AC list , AL645477, AL645848, AL645857, AL672146, AL731776, AL732449, AL806516, AL808024, AL844151, BX000479, BX294443, CR352330, CR382328 Genomic DNA. Translation: CAM15349.1.
AL645477 expand/collapse EMBL AC list , AL645848, AL645857, AL672146, AL731776, AL732449, AL806516, AL808024, AL833800, AL844151, BX000479, BX294443, CR352330, CR382328 Genomic DNA. Translation: CAM15656.1.
AL645857 expand/collapse EMBL AC list , AL645477, AL645848, AL672146, AL731776, AL732449, AL806516, AL808024, AL833800, AL844151, BX000479, BX294443, CR352330, CR382328 Genomic DNA. Translation: CAM16090.1.
AL732449 expand/collapse EMBL AC list , AL645477, AL645848, AL645857, AL672146, AL731776, AL806516, AL808024, AL833800, AL844151, BX000479, BX294443, CR352330, CR382328 Genomic DNA. Translation: CAM17038.1.
BX294443 expand/collapse EMBL AC list , AL645477, AL645848, AL645857, AL672146, AL731776, AL732449, AL806516, AL808024, AL833800, AL844151, BX000479, CR352330, CR382328 Genomic DNA. Translation: CAM20240.1.
CR382328 expand/collapse EMBL AC list , AL645477, AL645848, AL645857, AL672146, AL731776, AL732449, AL806516, AL808024, AL833800, AL844151, BX000479, BX294443, CR352330 Genomic DNA. Translation: CAM20576.1.
CR352330 expand/collapse EMBL AC list , AL645477, AL645848, AL645857, AL672146, AL731776, AL732449, AL806516, AL808024, AL833800, AL844151, BX000479, BX294443, CR382328 Genomic DNA. Translation: CAM22468.1.
AL672146 expand/collapse EMBL AC list , AL645477, AL645848, AL645857, AL731776, AL732449, AL806516, AL808024, AL833800, AL844151, BX000479, BX294443, CR352330, CR382328 Genomic DNA. Translation: CAM22949.1.
AL806516 expand/collapse EMBL AC list , AL645477, AL645848, AL645857, AL672146, AL731776, AL732449, AL808024, AL833800, AL844151, BX000479, BX294443, CR352330, CR382328 Genomic DNA. Translation: CAM24749.1.
AL731776 expand/collapse EMBL AC list , AL645477, AL645848, AL645857, AL672146, AL732449, AL806516, AL808024, AL833800, AL844151, BX000479, BX294443, CR352330, CR382328 Genomic DNA. Translation: CAM26197.1.
AL844151 expand/collapse EMBL AC list , 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.
CCDSCCDS41047.1. [P11531-1]
PIRS28916.
RefSeqNP_031894.1. NM_007868.5. [P11531-1]
UniGeneMm.275608.
Mm.416750.

3D structure databases

ProteinModelPortalP11531.
SMRP11531. Positions 9-246, 340-455, 3040-3299.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid199245. 19 interactions.
DIPDIP-32899N.
IntActP11531. 6 interactions.
MINTMINT-85369.

PTM databases

PhosphoSiteP11531.

Proteomic databases

MaxQBP11531.
PaxDbP11531.
PRIDEP11531.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000114000; ENSMUSP00000109633; ENSMUSG00000045103. [P11531-1]
GeneID13405.
KEGGmmu:13405.
UCSCuc009tri.2. mouse. [P11531-1]

Organism-specific databases

CTD1756.
MGIMGI:94909. Dmd.

Phylogenomic databases

eggNOGCOG5069.
GeneTreeENSGT00740000115262.
HOGENOMHOG000231173.
HOVERGENHBG005495.
InParanoidA2A9Z0.
KOK10366.
OMAEGPYTMD.
OrthoDBEOG7V765N.
TreeFamTF320178.

Gene expression databases

ArrayExpressP11531.
BgeeP11531.
CleanExMM_DMD.
GenevestigatorP11531.

Family and domain databases

Gene3D1.10.238.10. 2 hits.
1.10.418.10. 2 hits.
InterProIPR001589. 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]
PfamPF00307. 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]
PIRSFPIRSF002341. Dystrophin/utrophin. 1 hit.
SMARTSM00033. CH. 2 hits.
SM00150. SPEC. 22 hits.
SM00456. WW. 1 hit.
SM00291. ZnF_ZZ. 1 hit.
[Graphical view]
SUPFAMSSF47576. SSF47576. 1 hit.
SSF51045. SSF51045. 1 hit.
PROSITEPS00019. 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]
ProtoNetSearch...

Other

NextBio283803.
PROP11531.
SOURCESearch...

Entry information

Entry nameDMD_MOUSE
AccessionPrimary (citable) accession number: P11531
Secondary accession number(s): A2A9Z0, O35653, Q60703
Entry history
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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot