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Protein

Dystrophin

Gene

Dmd

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: 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.By similarity

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri3299 – 3346ZZ-typePROSITE-ProRule annotationAdd BLAST48

GO - Molecular functioni

  • integrin binding Source: RGD
  • lamin binding Source: RGD
  • PDZ domain binding Source: RGD
  • protein complex binding Source: RGD
  • structural constituent of cytoskeleton Source: InterPro
  • zinc ion binding Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Actin-binding, Calcium, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-RNO-390522. Striated Muscle Contraction.

Names & Taxonomyi

Protein namesi
Recommended name:
Dystrophin
Gene namesi
Name:Dmd
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome X

Organism-specific databases

RGDi2507. Dmd.

Subcellular locationi

  • Cell membranesarcolemma By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity
  • Cytoplasmcytoskeleton By similarity
  • Cell junctionsynapsepostsynaptic cell membrane By similarity

  • 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.By similarity

GO - Cellular componenti

  • cell-substrate junction Source: Ensembl
  • cytoskeleton Source: UniProtKB-SubCell
  • dystrophin-associated glycoprotein complex Source: RGD
  • membrane raft Source: RGD
  • myofibril Source: RGD
  • neuron projection terminus Source: Ensembl
  • nucleus Source: BHF-UCL
  • postsynaptic membrane Source: UniProtKB-SubCell
  • sarcolemma Source: RGD
  • Z disc Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000760771 – 3677DystrophinAdd BLAST3677

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei3475PhosphoserineBy similarity1
Modified residuei3482PhosphoserineBy similarity1
Modified residuei3492PhosphoserineBy similarity1
Modified residuei3604PhosphoserineBy similarity1
Modified residuei3605PhosphoserineBy similarity1
Modified residuei3609PhosphoserineBy similarity1
Modified residuei3615PhosphoserineCombined sources1
Modified residuei3616PhosphoserineCombined sources1
Modified residuei3658PhosphoserineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP11530.
PRIDEiP11530.

PTM databases

iPTMnetiP11530.

Expressioni

Tissue specificityi

Strongly expressed in skeletal muscle and weak expression observed in newborn brain which increases in adult brain.1 Publication

Gene expression databases

BgeeiENSRNOG00000003667.
ExpressionAtlasiP11530. baseline and differential.

Interactioni

Subunit structurei

Interacts with SYNM (By similarity). 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. Identified in a dystroglycan complex that contains at least PRX, DRP2, UTRN, DMD and DAG1 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Krt19Q632793EBI-706166,EBI-876985

GO - Molecular functioni

  • integrin binding Source: RGD
  • lamin binding Source: RGD
  • PDZ domain binding Source: RGD
  • protein complex binding Source: RGD

Protein-protein interaction databases

IntActiP11530. 4 interactors.
STRINGi10116.ENSRNOP00000029969.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 240Actin-bindingAdd BLAST240
Domaini15 – 119CH 1PROSITE-ProRule annotationAdd BLAST105
Domaini134 – 237CH 2PROSITE-ProRule annotationAdd BLAST104
Repeati342 – 447Spectrin 1Sequence analysisAdd BLAST106
Repeati451 – 557Spectrin 2Sequence analysisAdd BLAST107
Repeati560 – 668Spectrin 3Sequence analysisAdd BLAST109
Repeati728 – 828Spectrin 4Sequence analysisAdd BLAST101
Repeati831 – 935Spectrin 5Sequence analysisAdd BLAST105
Repeati944 – 1046Spectrin 6Sequence analysisAdd BLAST103
Repeati1049 – 1154Spectrin 7Sequence analysisAdd BLAST106
Repeati1163 – 1264Spectrin 8Sequence analysisAdd BLAST102
Repeati1268 – 1464Spectrin 9Sequence analysisAdd BLAST197
Repeati1469 – 1569Spectrin 10Sequence analysisAdd BLAST101
Repeati1573 – 1676Spectrin 11Sequence analysisAdd BLAST104
Repeati1680 – 1777Spectrin 12Sequence analysisAdd BLAST98
Repeati1779 – 1875Spectrin 13Sequence analysisAdd BLAST97
Repeati1878 – 1980Spectrin 14Sequence analysisAdd BLAST103
Repeati2001 – 2098Spectrin 15Sequence analysisAdd BLAST98
Repeati2106 – 2209Spectrin 16Sequence analysisAdd BLAST104
Repeati2215 – 2316Spectrin 17Sequence analysisAdd BLAST102
Repeati2317 – 2415Spectrin 18Sequence analysisAdd BLAST99
Repeati2465 – 2569Spectrin 19Sequence analysisAdd BLAST105
Repeati2576 – 2678Spectrin 20Sequence analysisAdd BLAST103
Repeati2682 – 2786Spectrin 21Sequence analysisAdd BLAST105
Repeati2800 – 2922Spectrin 22Sequence analysisAdd BLAST123
Repeati2927 – 3032Spectrin 23Sequence analysisAdd BLAST106
Domaini3047 – 3080WWPROSITE-ProRule annotationAdd BLAST34

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni63 – 72ANK2- and ANK-3 bindingBy similarity10
Regioni1416 – 1914Interaction with SYNMBy similarityAdd BLAST499
Regioni3050 – 3400Interaction with SYNMBy similarityAdd BLAST351
Regioni3458 – 3510Binds to SNTB1By similarityAdd BLAST53

Sequence similaritiesi

Contains 1 actin-binding domain.Curated
Contains 2 CH (calponin-homology) domains.PROSITE-ProRule annotation
Contains 23 spectrin repeats.Curated
Contains 1 WW domain.PROSITE-ProRule annotation
Contains 1 ZZ-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri3299 – 3346ZZ-typePROSITE-ProRule annotationAdd BLAST48

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG4286. Eukaryota.
COG5069. LUCA.
GeneTreeiENSGT00760000119237.
HOGENOMiHOG000231173.
InParanoidiF1M705.
OMAiLWLEEAD.
OrthoDBiEOG091G001Y.

Family and domain databases

CDDicd00014. CH. 2 hits.
Gene3Di1.10.238.10. 2 hits.
1.10.418.10. 2 hits.
InterProiIPR001589. Actinin_actin-bd_CS.
IPR001715. CH-domain.
IPR016344. Dystrophin.
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. 23 hits.
SM00456. WW. 1 hit.
SM00291. ZnF_ZZ. 1 hit.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 2 hits.
SSF47576. 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.

P11530-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLWWEEVEDC YEREDVQKKT FTKWINAQFS KFGKQHIDNL FSDLQDGKRL
60 70 80 90 100
LDLLEGLTGQ KLPKEKGSTR VHALNNVNKA LQVLQKNNVD LVNIGSTDIV
110 120 130 140 150
DGNHKLTLGL IWNIILHWQV KNVMKTIMAG LQQTNSEKIL LSWVRESTRN
160 170 180 190 200
YPQVNVLNFT SSWSDGLALN ALIHSHRPDL FDWNSVVSQQ SATQRLEHAF
210 220 230 240 250
NIAKCQLGIE KLLDPEDVAT TYPDKKSILM YITSLFQVLP QQVSIEAIRE
260 270 280 290 300
VEMLPRPSKV TREEHFQLHH QMHYSQQITV SLAQGYEQTS SSPKPRFKSY
310 320 330 340 350
AFTQAAYVAT SDSSQSPYPS QHLEAPGSKS FGSSLIETEV NLDSYQTALE
360 370 380 390 400
EVLSWLLSAE DTLRAQGEIS KDVEEVKEQF HAHEGFMMDL TSHQGLVGNV
410 420 430 440 450
LQLGSRLVGK GKLTEDEETE VQEQMNLLNS RWECLRVASM EKQSNLHKVL
460 470 480 490 500
MDLQNQKLKE LDDWLTKTEE RTKKMEEEPL GPDLEDLKCQ VQQHKVLQED
510 520 530 540 550
LEQEQVRVNS LTHMVVVVDE SSGDHATAAL EEQLKVLGDR WANICKWTED
560 570 580 590 600
RWILLQDILL KWQRFTEEQC LFSKWLSEKE DAMKNIQTSG FEDQNEMVSS
610 620 630 640 650
LQNISALKID LEKKKQSMEK LSSLNQDLLS ALKNKSVTQK MEMWMENFAQ
660 670 680 690 700
RWDNLTQKLE KSSAQISQAV TTTQPSLTQT TVMETVTMVT TREQIMVKHA
710 720 730 740 750
QEELPPPPPQ KKRQITVDSE IRKRLDVDIT ELHSWITRSE AVLQSSEFAV
760 770 780 790 800
YRKEGNISDL KEKVNAIARE KAEKFRKLQD ASRSAQALVE QMVNEGVNAE
810 820 830 840 850
SIRQASEQLN SRWTEFCQLL SERVNWLEYQ NNIITFYNQL QQLEQMTTTA
860 870 880 890 900
ENLLKTQPTT LSEPTAIKSQ LKICKDEVNR LSALQPQIER LKIQSLTLKE
910 920 930 940 950
KGQGPMFLDA DFVAFTNHFN YVFDGVRARE KELQTIFDTL PPMRYQETMS
960 970 980 990 1000
SIRTWIQQSE NKLSIPHLSV TEYEIMEERL GKLQALQSSL KEQQNGFNYL
1010 1020 1030 1040 1050
NATVKEIAKK APSEISQKYQ SEFEEVEGRW KKLSTQLVEH CQKLEEHMNK
1060 1070 1080 1090 1100
LRKFQNHKKT LQKWMAEVDV FLKEEWPALG DAEILKKQLK QCRLLVGDIQ
1110 1120 1130 1140 1150
TIQPSLNSVN EGGQKIKSEA EFEFASRLEK ELKELNTQWD HICRQVYTRK
1160 1170 1180 1190 1200
EALKAGLDKT VSLQKDLSEM HEWMTQAEEE YLERDFEYKT PDELQTAVEE
1210 1220 1230 1240 1250
MKRAKEEALQ KEAKVKLLTE TVNSVISQAP PAAQEALKKE LETLTTNYQW
1260 1270 1280 1290 1300
LCTRLNGKCK TLEEVWACWH ELLSYLEKAN KWLNEVELKL KATENVPAGA
1310 1320 1330 1340 1350
EEITEVLESL ENLMHHSEEN PNQIRLLAQT LTDGGVMDEL INEELETFNS
1360 1370 1380 1390 1400
RWRELHEEAV RKQKLLEQSI QSAQEIEKSL HLIQESLEFI DKQLAAYIAD
1410 1420 1430 1440 1450
KVDAAQMPQE AQKIQSDLTS HEISLEEMKK HNQGKDANQR VLSQIDVAQK
1460 1470 1480 1490 1500
KLQDVSIKFR LFQKPANFEQ RLEESKMILD EVKMHLPALE TKSVEQEVVQ
1510 1520 1530 1540 1550
SQLSHCVNLY KSLSEVKSEV EMVIKTGRQI VQKKQTENPK ELDERVTALK
1560 1570 1580 1590 1600
LHYNELGAKV TERKQQLEKC LKLSRKMRKE MNVLTEWLAA TDTELTKRSA
1610 1620 1630 1640 1650
VEGMPSNLDS EVAWGKATQK EIEKQKAHLK SVTELGDSLK TVLGKKETLV
1660 1670 1680 1690 1700
EDKLTLLNSN WIAVTSRVEE WLNLLLEYQK HMESFDQNVE HITKWIIHTD
1710 1720 1730 1740 1750
ELLDESEKRK PQQKEDILKR LKAEMNDIRP KVDATRDQAA KLMANRGDYC
1760 1770 1780 1790 1800
RKIVEPQISE LNRRFAAISH RIKTGKASIP LKELEQFNSD IQKLLEPLEA
1810 1820 1830 1840 1850
EIQQGVNLKE EDFNKDMSED NEGTVNELLQ RGDNLQQRIT DERKREEIKL
1860 1870 1880 1890 1900
KQQLLQTKHN ALKDLRSQRR KKALEISHQW YQYKSQADDL LKCLDEIEKK
1910 1920 1930 1940 1950
LASLPEPRDE RKIKEIDREL QKKKEELNAV RRQAESLSEN GAAMAVEPTQ
1960 1970 1980 1990 2000
IQLSKRWREI ESNFAQFRRL NFAQIHTLHE ETMVVTTEDM PLDVSYVPST
2010 2020 2030 2040 2050
YLTEISHILQ ALSEVEQLLN APELNAKDFE DLFKQEESLK NIKENLQQIS
2060 2070 2080 2090 2100
GRIDVIHKKK TAALQSATPM ERVKLQEAVS QMDFHWEKLN RMYKERQGRF
2110 2120 2130 2140 2150
DRSVEKWRHF HYDMKVFNQW LNDVEQFFKK TQNPENWEHA KYKWYLKELQ
2160 2170 2180 2190 2200
DGIGQRQAVV RTLNATGEEI IQQSSKTDAN ILQEKLGSLS LRWHEVCKEL
2210 2220 2230 2240 2250
AERRKRVEEQ KNVFSEFQRD LNEFVSWLEE ADNIATTPPG DEEQLKEKLE
2260 2270 2280 2290 2300
QVKLLTEELP LRQGILKQLN ETGGAVLVSA PIRPEEQDKL EKKLKQTNLQ
2310 2320 2330 2340 2350
WIKVSRALPE KQGELEVHIK DFRQFEEQLD HLLLWLSPIR NQLEIYNQPS
2360 2370 2380 2390 2400
QPGPFDLKET EVTVQAKQPD VERLLSKGQH LYKEKPSTQP VKRKLEDLRS
2410 2420 2430 2440 2450
EWEAVNHLLW ELRTKQPDRA PGLSTTGASA SQTVTVVTQP VDTKETVISK
2460 2470 2480 2490 2500
LEMPSSLLLE VPALADFNRA WTELTDWLSL LDRVIKSQRV MVGDLEDINE
2510 2520 2530 2540 2550
MIIKQKATLQ DLEQRRPQLE ELITAAQNLK NKTSNQEART IITDRIERIQ
2560 2570 2580 2590 2600
IQWDEVQEQL QNRRQQLNEM LKDSTQWLEA KEEAEQVIGQ ARGKLDSWKE
2610 2620 2630 2640 2650
GPHTMDAIQK KITETKQLAK DLRQRQINVD VANDLALKLL RDYSADDTRK
2660 2670 2680 2690 2700
VHMITENINT SWGNILKRVS EREAALEETQ RLLQQFPLDL EKFLAWITEA
2710 2720 2730 2740 2750
ETTANVLQDA SRKEKLLEDS RGVRELMKPW QDLQGEIEAH TDIYHNLDEN
2760 2770 2780 2790 2800
GQKILRSLEG SDEAPLLQRR LDNMNFKWSE LRKKSLNIRS HLEVSSDQWK
2810 2820 2830 2840 2850
RLHLSLQELL VWLQLKDDEL SRQAPIGGDF PAVQKQNDVH RAFKRELKTK
2860 2870 2880 2890 2900
EPVIMSTLET VRIFLTEQPL EGLEKLYQEP RELPPEERAQ NVTRLLRKQA
2910 2920 2930 2940 2950
EEVNTEWDKL NLHSADWQRK IDEALERLQE LQEAADELDL KLRQAEVIKG
2960 2970 2980 2990 3000
SWQPVGDLLI DSLQDHLEKV KALRGEIAPL KENVNHVNDL AHHLTTLGIQ
3010 3020 3030 3040 3050
LSPYNLSILE DLNTRWRLLQ VAVEDRVRQL HEAHRDFGPA SQHFLSTSVQ
3060 3070 3080 3090 3100
GPWERAISPN KVPYYINHET QTTCWDHPKM TELYQSLADL NNVRFSAYRT
3110 3120 3130 3140 3150
AMKLRRLQKA LCLDLLSLSA ACDALDQHNL KQNDQPMDIL QIINCLTTIY
3160 3170 3180 3190 3200
DRLEQEHNNL VNVPLCVDMC LNWLLNVYDT GRTGRIRVLS FKTGIISLCK
3210 3220 3230 3240 3250
AHLEDKYRYL FKQVASSTGF CDQRRLGLLL HDSIQIPRQL GEVASFGGSN
3260 3270 3280 3290 3300
IEPSVRSCFQ FANNKPEIEA ALFLDWMRLE PQSMVWLPVL HRVAAAETAK
3310 3320 3330 3340 3350
HQAKCNICKE CPIIGFRYRS LKHFNYDICQ SCFFSGRVAK GHKMHYPMVE
3360 3370 3380 3390 3400
YCTPTTSGED VRDFAKVLKN KFRTKRYFAK HPRMGYLPVQ TVLEGDNMET
3410 3420 3430 3440 3450
PVTLINFWPV DSAPASSPQL SHDDTHSRIE HYASRLAEME NSNGSYLNDS
3460 3470 3480 3490 3500
ISPNESIDDE HLLIQHYCQS LNQDSPLSQP RSPAQILISL ESEERGELER
3510 3520 3530 3540 3550
ILADLEEENR NLQAEYDRLK QQHEHKGLSP LPSPPEMMPT SPQSPRDAEL
3560 3570 3580 3590 3600
IAEAKLLRQH KGRLEARMQI LEDHNKQLES QLHRLRQLLE QPQAEAKVNG
3610 3620 3630 3640 3650
TTVSSPSTSL QRSDSSQPML LRVVGSQTSE SMGEEDLLSP PQDTSTGLEE
3660 3670
VMEQLNNSFP SSRGRNAPGK PMREDTM
Length:3,677
Mass (Da):425,828
Last modified:December 9, 2015 - v2
Checksum:i50526FA367B87FAB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR07073532 Genomic DNA. No translation available.
AC097383 Genomic DNA. No translation available.
AC111223 Genomic DNA. No translation available.
AC112800 Genomic DNA. No translation available.
AC113761 Genomic DNA. No translation available.
AC117871 Genomic DNA. No translation available.
AC125680 Genomic DNA. No translation available.
AC125768 Genomic DNA. No translation available.
AC131219 Genomic DNA. No translation available.
AC136037 Genomic DNA. No translation available.
X07000 Genomic DNA. Translation: CAA30057.1.
PIRiS01614.
RefSeqiXP_017457399.1. XM_017601910.1.
UniGeneiRn.10307.

Genome annotation databases

EnsembliENSRNOT00000035692; ENSRNOP00000029969; ENSRNOG00000046366.
GeneIDi24907.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR07073532 Genomic DNA. No translation available.
AC097383 Genomic DNA. No translation available.
AC111223 Genomic DNA. No translation available.
AC112800 Genomic DNA. No translation available.
AC113761 Genomic DNA. No translation available.
AC117871 Genomic DNA. No translation available.
AC125680 Genomic DNA. No translation available.
AC125768 Genomic DNA. No translation available.
AC131219 Genomic DNA. No translation available.
AC136037 Genomic DNA. No translation available.
X07000 Genomic DNA. Translation: CAA30057.1.
PIRiS01614.
RefSeqiXP_017457399.1. XM_017601910.1.
UniGeneiRn.10307.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP11530. 4 interactors.
STRINGi10116.ENSRNOP00000029969.

PTM databases

iPTMnetiP11530.

Proteomic databases

PaxDbiP11530.
PRIDEiP11530.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000035692; ENSRNOP00000029969; ENSRNOG00000046366.
GeneIDi24907.

Organism-specific databases

RGDi2507. Dmd.

Phylogenomic databases

eggNOGiKOG4286. Eukaryota.
COG5069. LUCA.
GeneTreeiENSGT00760000119237.
HOGENOMiHOG000231173.
InParanoidiF1M705.
OMAiLWLEEAD.
OrthoDBiEOG091G001Y.

Enzyme and pathway databases

ReactomeiR-RNO-390522. Striated Muscle Contraction.

Miscellaneous databases

PROiP11530.

Gene expression databases

BgeeiENSRNOG00000003667.
ExpressionAtlasiP11530. baseline and differential.

Family and domain databases

CDDicd00014. CH. 2 hits.
Gene3Di1.10.238.10. 2 hits.
1.10.418.10. 2 hits.
InterProiIPR001589. Actinin_actin-bd_CS.
IPR001715. CH-domain.
IPR016344. Dystrophin.
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. 23 hits.
SM00456. WW. 1 hit.
SM00291. ZnF_ZZ. 1 hit.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 2 hits.
SSF47576. 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]
ProtoNetiSearch...

Entry informationi

Entry nameiDMD_RAT
AccessioniPrimary (citable) accession number: P11530
Secondary accession number(s): F1M705
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: December 9, 2015
Last modified: November 30, 2016
This is version 104 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.