P11531 (DMD_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dystrophin

Gene names

Name:

Dmd

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	3678 AA.
Sequence status	Complete.
Protein existence	Evidence 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 membrane › sarcolemma; Peripheral membrane protein; Cytoplasmic side. Cytoplasm › cytoskeleton. Cell junction › synapse › postsynaptic 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 component	Cell junction Cell membrane Cytoplasm Cytoskeleton Membrane Postsynaptic cell membrane Synapse
Coding sequence diversity	Alternative splicing
Domain	Repeat Zinc-finger
Ligand	Actin-binding Calcium Metal-binding Zinc
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	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 homeostasis Inferred from mutant phenotype PubMed 6583703. Source: MGI muscle fiber development Inferred from genetic interaction PubMed 8007658. Source: MGI myotube cell development Inferred from mutant phenotype PubMed 19535499. Source: MGI 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 peptide biosynthetic process Inferred from electronic annotation. Source: Compara 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 cell action potential Inferred from mutant phenotype PubMed 20080623PubMed 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 heart rate Inferred from mutant phenotype PubMed 20080623. Source: BHF-UCL regulation of peptidyl-cysteine S-nitrosylation Inferred from mutant phenotype PubMed 19198614PubMed 20080623. 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 by regulation of release of sequestered calcium ion Inferred from mutant phenotype PubMed 19198614. Source: BHF-UCL regulation of transcription, DNA-dependent Inferred from mutant phenotype PubMed 7919967. Source: MGI regulation of voltage-gated calcium channel activity Inferred from mutant phenotype PubMed 21677768. Source: BHF-UCL
Cellular_component	Z disc Inferred from direct assay PubMed 7890770. Source: MGI cell surface Inferred from electronic annotation. Source: Compara cell-substrate junction Inferred from direct assay PubMed 7890770. Source: MGI costamere Inferred from electronic annotation. Source: Compara 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 postsynaptic membrane Inferred from electronic annotation. Source: UniProtKB-SubCell sarcolemma Inferred from direct assay PubMed 11115849PubMed 11259414PubMed 16371353PubMed 16810681PubMed 8663016. Source: MGI synapse Inferred from direct assay PubMed 10995443. Source: MGI
Molecular_function	calcium ion binding Inferred from electronic annotation. Source: InterPro structural constituent of muscle Inferred from electronic annotation. Source: Compara zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Snta1	Q61234	2	EBI-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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 3678	3678	Dystrophin		PRO_0000076076
Regions
	Domain	1 – 240	240	Actin-binding
	Domain	15 – 119	105	CH 1
	Domain	134 – 237	104	CH 2
	Repeat	341 – 449	109	Spectrin 1
	Repeat	450 – 558	109	Spectrin 2
	Repeat	561 – 669	109	Spectrin 3
	Repeat	721 – 830	110	Spectrin 4
	Repeat	832 – 936	105	Spectrin 5
	Repeat	945 – 1047	103	Spectrin 6
	Repeat	1050 – 1156	107	Spectrin 7
	Repeat	1159 – 1265	107	Spectrin 8
	Repeat	1268 – 1369	102	Spectrin 9
	Repeat	1370 – 1465	96	Spectrin 10
	Repeat	1470 – 1570	101	Spectrin 11
	Repeat	1573 – 1678	106	Spectrin 12
	Repeat	1681 – 1780	100	Spectrin 13
	Repeat	1781 – 1876	96	Spectrin 14
	Repeat	1879 – 1981	103	Spectrin 15
	Repeat	1994 – 2103	110	Spectrin 16
	Repeat	2106 – 2210	105	Spectrin 17
	Repeat	2213 – 2318	106	Spectrin 18
	Repeat	2319 – 2416	98	Spectrin 19
	Repeat	2468 – 2570	103	Spectrin 20
	Repeat	2573 – 2679	107	Spectrin 21
	Repeat	2682 – 2795	114	Spectrin 22
	Repeat	2801 – 2923	123	Spectrin 23
	Repeat	2928 – 3033	106	Spectrin 24
	Domain	3048 – 3081	34	WW
	Zinc finger	3300 – 3347	48	ZZ-type
	Region	63 – 72	10	ANK2- and ANK-3 binding
	Region	1417 – 1915	499	Interaction with SYNM
	Region	3051 – 3401	351	Interaction with SYNM
	Region	3459 – 3511	53	Binds to SNTB1 By similarity
Amino acid modifications
	Modified residue	3476	1	Phosphoserine By similarity
	Modified residue	3605	1	Phosphoserine By similarity
	Modified residue	3606	1	Phosphoserine By similarity
	Modified residue	3610	1	Phosphoserine By similarity
	Modified residue	3616	1	Phosphoserine By similarity
	Modified residue	3617	1	Phosphoserine Ref.14
	Modified residue	3659	1	Phosphoserine By similarity
Experimental info
	Sequence conflict	463	1	D → H in AAA37530. Ref.5
	Sequence conflict	677	1	S → F in AAA37530. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 27, 2011. Version 3. Checksum: 53487B1E27104228	FASTA	3,678	425,832
	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

References

	« Hide 'large scale' referencesShow '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. , 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, 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-3617, MASS SPECTROMETRY. 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 , 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.
IPI	IPI00474450.
PIR	S28916.
RefSeq	NP_031894.1. NM_007868.5.
UniGene	Mm.275608. Mm.416750.
3D structure databases
ProteinModelPortal	P11531.
SMR	P11531. Positions 9-246, 340-455, 3040-3299.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-32899N.
IntAct	P11531. 5 interactions.
MINT	MINT-85369.
PTM databases
PhosphoSite	P11531.
Proteomic databases
PaxDb	P11531.
PRIDE	P11531.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000114000; ENSMUSP00000109633; ENSMUSG00000045103.
GeneID	13405.
KEGG	mmu:13405.
UCSC	uc009tri.2. mouse.
Organism-specific databases
CTD	1756.
MGI	MGI:94909. Dmd.
Phylogenomic databases
eggNOG	COG5069.
GeneTree	ENSGT00550000074400.
HOGENOM	HOG000231173.
HOVERGEN	HBG005495.
InParanoid	A2A9Z0.
KO	K10366.
OrthoDB	EOG480HW7.
Gene expression databases
ArrayExpress	P11531.
Bgee	P11531.
CleanEx	MM_DMD.
Genevestigator	P11531.
Family and domain databases
Gene3D	1.10.238.10. 2 hits. 1.10.418.10. 2 hits.
InterPro	IPR001589. Actinin_actin-bd_CS. IPR001715. CH-domain. IPR016344. Dystrophin/utrophin. IPR011992. EF-hand-like_dom. 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]
Pfam	PF00307. CH. 2 hits. PF09068. efhand_1. 1 hit. PF09069. efhand_2. 1 hit. PF00435. Spectrin. 16 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]
SUPFAM	SSF47576. Calponin-homology. 1 hit. SSF51045. WW_Rsp5_WWP. 1 hit.
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	Search...
Other
NextBio	283803.
SOURCE	Search...

Entry information

Entry name

DMD_MOUSE

Accession

Primary (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:	May 29, 2013
This is version 137 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program