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UniProtKB - Q91ZU6 (DYST_MOUSE)

UniProt

Q91ZU6 - DYST_MOUSE

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Protein

Dystonin

Gene

Dst

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Cytoskeletal linker protein. Acts as an integrator of intermediate filaments, actin and microtubule cytoskeleton networks. Required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. The proteins may self-aggregate to form filaments or a two-dimensional mesh. May regulate the organization and stability of the microtubule network of sensory neurons to allow axonal transport.
Isoform 5: plays a structural role in the assembly of hemidesmosomes of epithelial cells; anchors keratin-containing intermediate filaments to the inner plaque of hemidesmosomes. Required for the regulation of keratinocyte polarity and motility; mediates integrin ITGB4 regulation of RAC1 activity.
Isoform 6: required for bundling actin filaments around the nucleus.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi7032 – 7043121PROSITE-ProRule annotationAdd
BLAST
Calcium bindingi7068 – 7079122PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • axonogenesis Source: MGI
  • cell adhesion Source: UniProtKB-KW
  • cell cycle arrest Source: InterPro
  • intermediate filament cytoskeleton organization Source: UniProtKB
  • intracellular transport Source: UniProtKB
  • retrograde axonal transport Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Muscle protein

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Actin-binding, Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiR-MMU-2022090. Assembly of collagen fibrils and other multimeric structures.
R-MMU-446107. Type I hemidesmosome assembly.

Names & Taxonomyi

Protein namesi
Recommended name:
Dystonin
Alternative name(s):
Bullous pemphigoid antigen 1
Short name:
BPA
Dystonia musculorum protein
Hemidesmosomal plaque protein
Microtubule actin cross-linking factor 2
Gene namesi
Name:Dst
Synonyms:Bpag1, Macf2
OrganismiMus musculus (Mouse)Imported
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:104627. Dst.

Subcellular locationi

  • Cytoplasm › cytoskeleton
  • Cell projection › axon
  • Membrane

    • Note: Associates with axonal microtubules at the growing distal tip and intermediate filaments, but not with actin cytoskeleton, in sensory neurons (By similarity). Associates with intermediate filaments, acin and microtubule cytoskeletons. Localizes to actin stress fibers and to actin-rich ruffling at the cortex of cells.By similarity
Isoform 1 :
Isoform 2 :
Isoform 5 :
  • Cytoplasm › cytoskeleton
  • Cell junction › hemidesmosome

    • Note: Colocalizes with the epidermal KRT5-KRT14 intermediate filaments network of keratins. Colocalizes with ITGB4 at the leading edge of migrating keratinocytes (By similarity). Localizes to actin and intermediate filaments cytoskeletons.By similarity
Isoform 6 :
Isoform 7 :

GO - Cellular componenti

  • actin cytoskeleton Source: UniProtKB
  • axon cytoplasm Source: GOC
  • cell cortex Source: UniProtKB-SubCell
  • cytoplasm Source: UniProtKB
  • cytoplasmic, membrane-bounded vesicle Source: MGI
  • cytoplasmic side of plasma membrane Source: UniProtKB
  • endoplasmic reticulum membrane Source: UniProtKB
  • focal adhesion Source: UniProtKB
  • hemidesmosome Source: UniProtKB
  • H zone Source: UniProtKB
  • integral component of membrane Source: UniProtKB-KW
  • intercalated disc Source: UniProtKB
  • intermediate filament Source: UniProtKB-KW
  • membrane Source: UniProtKB
  • microtubule cytoskeleton Source: UniProtKB
  • microtubule plus-end Source: UniProtKB
  • nuclear envelope Source: UniProtKB
  • nucleus Source: UniProtKB
  • perinuclear endoplasmic reticulum Source: UniProtKB
  • perinuclear region of cytoplasm Source: UniProtKB
  • sarcolemma Source: UniProtKB
  • stress fiber Source: UniProtKB
  • Z disc Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Endoplasmic reticulum, Intermediate filament, Membrane, Microtubule, Nucleus

Pathology & Biotechi

Disruption phenotypei

Mice show progressive deterioration in motor function and sensory neurodegeneration. Exhibit axonal swellings packed with disorganized intermediate filaments (IFs) and microtubules. Show poorly defined Z lines and display a reduction in sarcomere length. Have increased accumulation of vesicles and severely disrupted retrograde axonal transport. In stratified epithelia, hemidesmosomes are normal but they lack the inner plate and have no cytoskeleton attached.4 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1385 – 13851R → A: Prevents isoform 6 from localizing to the nucleus; when associated with A-1386. 1 Publication
Mutagenesisi1386 – 13861R → A: Prevents isoform 6 from localizing to the nucleus; when associated with A-1385. 1 Publication

Chemistry

ChEMBLiCHEMBL2176789.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 73937393DystoninPRO_0000078141Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei236 – 2361PhosphoserineCombined sources
Modified residuei237 – 2371PhosphoserineCombined sources
Modified residuei1381 – 13811PhosphoserineCombined sources
Modified residuei2211 – 22111PhosphoserineCombined sources
Modified residuei2862 – 28621PhosphoserineBy similarity
Modified residuei3894 – 38941PhosphoserineBy similarity
Modified residuei4680 – 46801PhosphoserineCombined sources
Cross-linki5401 – 5401Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei5488 – 54881PhosphoserineCombined sources
Modified residuei7254 – 72541PhosphoserineBy similarity
Modified residuei7333 – 73331PhosphoserineCombined sources
Modified residuei7336 – 73361PhosphoserineCombined sources
Modified residuei7348 – 73481PhosphoserineCombined sources
Isoform 7 (identifier: Q91ZU6-8)
Modified residuei205 – 2051PhosphoserineCombined sources
Modified residuei208 – 2081PhosphoserineCombined sources

Keywords - PTMi

Isopeptide bond, Lipoprotein, Myristate, Palmitate, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ91ZU6.
PaxDbiQ91ZU6.
PeptideAtlasiQ91ZU6.
PRIDEiQ91ZU6.

2D gel databases

REPRODUCTION-2DPAGEIPI00230689.
IPI00230690.
IPI00284272.

PTM databases

iPTMnetiQ91ZU6.
PhosphoSiteiQ91ZU6.

Expressioni

Tissue specificityi

Isoform 1 and 2 are expressed in striated and heart muscle cells. Isoform 5 is expressed in the skin. Isoform 6 is expressed in sensory neural cells of the dorsal root ganglion and with low level in the skin (at protein level). Isoform 1 is expressed predominantly in the brain and spinal cord with low levels in the heart. Isoform 2 is predominantly expressed in muscle and heart and with low levels in the brain. Isoform 5 is expressed in the skin and with low levels in myoblast cells. Isoform 6 is expressed in neurons. Isoform 7 is expressed in lung and with low levels in the brain.9 Publications

Developmental stagei

Isoform 1 is the major form expressed in the dorsal root ganglia at 14.5 dpc. Isoform 2 is predominantly expressed in the myocardium, skeletal muscles, bone cartilage and epithelia of the tongue at 14.5 dpc. Isoform 5 is expressed at high levels in the epidermis and mucosal epithelia of the digestive tracts at 14.5 dpc.2 Publications

Gene expression databases

BgeeiENSMUSG00000026131.
CleanExiMM_DST.
ExpressionAtlasiQ91ZU6. baseline and differential.
GenevisibleiQ91ZU6. MM.

Interactioni

Subunit structurei

Homodimer. Interacts with MAPRE1; probably required for targeting to the growing microtubule plus ends. Isoform 2 interacts (via N-terminus) with ACTN2. Isoform 2 interacts (via N-terminus) with PLEC (via N-terminus). Isoform 5 interacts (via N-terminus) with COL17A1 (via cytoplasmic region). Isoform 5 interacts (via N-terminus) with ITGB4 isoform beta-4a (via cytoplasmic region). Isoform 5 interacts (via N-terminus) with ERBIN (via C-terminus). Isoform 5 associates (via C-terminal) with KRT5-KRT14 (via rod region) intermediate filaments of keratins (By similarity). Isoform 2 and isoform 6 can homodimerize (via N-terminus). Isoform 2 interacts (via N-terminus) with PLEC (via N-terminus). Interacts with the neuronal intermediate filament protein, PRPH. Interacts with DES. Interacts with SYNE3.By similarity4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PrphP218073EBI-446159,EBI-446227From a different organism.

GO - Molecular functioni

  • microtubule plus-end binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi199328. 1 interaction.
IntActiQ91ZU6. 6 interactions.
MINTiMINT-1861530.
STRINGi10090.ENSMUSP00000095392.

Structurei

Secondary structure

1
7393
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi590 – 5934Combined sources
Beta strandi594 – 5963Combined sources
Helixi600 – 6045Combined sources
Helixi608 – 62316Combined sources
Helixi631 – 65020Combined sources
Helixi652 – 66110Combined sources
Helixi662 – 6643Combined sources
Turni667 – 6693Combined sources
Helixi670 – 68617Combined sources
Turni687 – 6893Combined sources
Helixi690 – 72233Combined sources
Helixi744 – 76724Combined sources
Helixi773 – 79321Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2IAKX-ray3.00A580-803[»]
ProteinModelPortaliQ91ZU6.
SMRiQ91ZU6. Positions 31-255, 583-795.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ91ZU6.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini35 – 252218Actin-bindingAdd
BLAST
Domaini35 – 138104CH 1PROSITE-ProRule annotationCuratedAdd
BLAST
Domaini151 – 252102CH 2PROSITE-ProRule annotationCuratedAdd
BLAST
Repeati701 – 801101Spectrin 1Add
BLAST
Domaini889 – 94153SH3CuratedAdd
BLAST
Repeati1582 – 162443Plectin 1Add
BLAST
Repeati1657 – 170145Plectin 2Add
BLAST
Repeati1772 – 181544Plectin 3Add
BLAST
Repeati1816 – 184429Plectin 4Add
BLAST
Repeati1848 – 188942Plectin 5Add
BLAST
Repeati3850 – 393081Spectrin 2Add
BLAST
Repeati4002 – 408483Spectrin 3Add
BLAST
Repeati4445 – 4553109Spectrin 4Add
BLAST
Repeati4557 – 4662106Spectrin 5Add
BLAST
Repeati4780 – 4882103Spectrin 6Add
BLAST
Repeati5213 – 5320108Spectrin 7Add
BLAST
Repeati5327 – 5428102Spectrin 8Add
BLAST
Repeati5435 – 5537103Spectrin 9Add
BLAST
Repeati5651 – 5755105Spectrin 10Add
BLAST
Repeati5762 – 586099Spectrin 11Add
BLAST
Repeati6006 – 608681Spectrin 12Add
BLAST
Repeati6093 – 6195103Spectrin 13Add
BLAST
Repeati6201 – 6304104Spectrin 14Add
BLAST
Repeati6312 – 6414103Spectrin 15Add
BLAST
Repeati6419 – 6523105Spectrin 16Add
BLAST
Repeati6527 – 6633107Spectrin 17Add
BLAST
Repeati6640 – 6740101Spectrin 18Add
BLAST
Repeati6745 – 6848104Spectrin 19Add
BLAST
Domaini7019 – 705436EF-hand 1PROSITE-ProRule annotationAdd
BLAST
Domaini7055 – 709036EF-hand 2PROSITE-ProRule annotationAdd
BLAST
Domaini7095 – 717379GARPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1382 – 13887Nuclear localization signal; in isoform 6
Motifi7373 – 73764Microtubule tip localization signal

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi2367 – 242761Asp-richAdd
BLAST

Domaini

Its association with epidermal and simple keratins is dependent on the tertiary structure induced by heterodimerization of these intermedaite filaments proteins and most likely involves recognition sites located in the rod domain of these keratins.
The microtubule tip localization signal (MtLS) motif; mediates interaction with MAPRE1 and targeting to the growing microtubule plus ends.By similarity

Sequence similaritiesi

Belongs to the plakin or cytolinker family.Curated
Contains 1 actin-binding domain.Curated
Contains 2 CH (calponin-homology) domains.PROSITE-ProRule annotation
Contains 2 EF-hand domains.PROSITE-ProRule annotation
Contains 1 GAR domain.PROSITE-ProRule annotation
Contains 5 plectin repeats.Curated
Contains 1 SH3 domain.Curated
Contains 19 spectrin repeats.Curated

Keywords - Domaini

Coiled coil, Repeat, SH3 domain, Transmembrane

Phylogenomic databases

eggNOGiKOG0516. Eukaryota.
KOG0517. Eukaryota.
COG5069. LUCA.
GeneTreeiENSGT00760000119163.
HOVERGENiHBG031127.
InParanoidiQ91ZU6.
KOiK10382.
OMAiRKITEIQ.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
1.10.418.10. 2 hits.
3.30.920.20. 1 hit.
3.90.1290.10. 3 hits.
InterProiIPR001589. Actinin_actin-bd_CS.
IPR001715. CH-domain.
IPR029926. Dystonin.
IPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR003108. GAS_dom.
IPR001101. Plectin_repeat.
IPR018159. Spectrin/alpha-actinin.
IPR002017. Spectrin_repeat.
[Graphical view]
PANTHERiPTHR11915:SF38. PTHR11915:SF38. 7 hits.
PfamiPF00307. CH. 2 hits.
PF13499. EF-hand_7. 1 hit.
PF02187. GAS2. 1 hit.
PF00681. Plectin. 2 hits.
PF00435. Spectrin. 18 hits.
[Graphical view]
SMARTiSM00033. CH. 2 hits.
SM00054. EFh. 2 hits.
SM00243. GAS2. 1 hit.
SM00250. PLEC. 9 hits.
SM00150. SPEC. 33 hits.
[Graphical view]
SUPFAMiSSF143575. SSF143575. 1 hit.
SSF47473. SSF47473. 1 hit.
SSF47576. SSF47576. 1 hit.
SSF75399. SSF75399. 2 hits.
PROSITEiPS00019. ACTININ_1. 1 hit.
PS00020. ACTININ_2. 1 hit.
PS50021. CH. 2 hits.
PS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 2 hits.
PS51460. GAR. 1 hit.
[Graphical view]

Sequences (7)i

Sequence statusi: Complete.

This entry describes 7 isoformsi produced by alternative promoter usage and alternative splicing. AlignAdd to basket

Isoform 21 Publication (identifier: Q91ZU6-1) [UniParc]FASTAAdd to basket
Also known as: BPAG1-b, BPAG1a1, dystonin-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.

« Hide

        10         20         30         40         50
MAGYLSPAAY MYVEEQEYLQ AYEDVLERYK DERDKVQKKT FTKWINQHLM 
        60         70         80         90        100
KVRKHVNDLY EDLRDGHNLI SLLEVLSGDT LPREKGRMRF HRLQNVQIAL 
       110        120        130        140        150
DYLKRRQVKL VNIRNDDITD GNPKLTLGLI WTIILHFQIS DIHVTGESED 
       160        170        180        190        200
MSAKERLLLW TQQATEGYAG VRCENFTTCW RDGKLFNAII HKYRPDLIDM 
       210        220        230        240        250
NTVAVQSNLA NLEHAFYVAE KIGVIRLLDP EDVDVSSPDE KSVITYVSSL 
       260        270        280        290        300
YDAFPKVPEG GEGIGANDVE VKWIEYQNMV NYLIQWIRHH VVTMSERTFP 
       310        320        330        340        350
NNPLELKALY NQYLQFKEKE IPPKEMEKSK IKRLYKLLEI WIEFGRIKLL 
       360        370        380        390        400
QGYHPNDIEK EWGKLIIAML EREKALRPEV ERLDMLQQIA TRVQRDSVSC 
       410        420        430        440        450
EDKLILARNA LQSDSKRLES GVQFQNEAEI AGYILECENL LRQHVIDVQI 
       460        470        480        490        500
LIDGKYYQAD QLVQRVAKLR DEIMALRNEC SSVYSKGRML TTEQTKLMIS 
       510        520        530        540        550
GITQSLNSGF AQTLHPSLNS GLTQSLTPSL TSSSVTSGLS SGMTSRLTPS 
       560        570        580        590        600
VTPVYAPGFP SVVAPNFSLG VEPNSLQTLK LMQIRKPLLK SSLLDQNLTE 
       610        620        630        640        650
EEVNMKFVQD LLNWVDEMQV QLDRTEWGSD LPSVESHLEN HKNVHRAIEE 
       660        670        680        690        700
FESSLKEAKI SEIQMTAPLK LSYTDKLHRL ESQYAKLLNT SRNQERHLDT 
       710        720        730        740        750
LHNFVTRATN ELIWLNEKEE SEVAYDWSER NSSVARKKSY HAELMRELEQ 
       760        770        780        790        800
KEESIKAVQE IAEQLLLENH PARLTIEAYR AAMQTQWSWI LQLCQCVEQH 
       810        820        830        840        850
IQENSAYFEF FNDAKEATDY LRNLKDAIQR KYSCDRSSSI HKLEDLVQES 
       860        870        880        890        900
MEKEELLQYR SVVAGLMGRA KTVVQLKPRN PDNPLKTSIP IKAICDYRQI 
       910        920        930        940        950
EITIYKDDEC VLANNSHRAK WKVISPTGNE AMVPSVCFTV PPPNKEAVDF 
       960        970        980        990       1000
ANRIEQQYQS VLTLWHESHI NMKSVVSWHY LVNEIDRIRA SNVASIKTML 
      1010       1020       1030       1040       1050
PGEHQQVLSN LQSRLEDFLE DSQESQIFSG SDISQLEKEV SVCRKYYQEL 
      1060       1070       1080       1090       1100
LKSAEREEQE ESVYNLYISE VRNIRLRLES CEDRLIRQIR TPLERDDLHE 
      1110       1120       1130       1140       1150
SMLRITEQEK LKKELDRLKD DLGTITNKCE EFFSQAADSP SVPALRSELS 
      1160       1170       1180       1190       1200
VVIQSLSQIY SMSSTYIEKL KTVNLVLKNT QAAEALVKLY ETKLCEEEAV 
      1210       1220       1230       1240       1250
IADKNNIENL MSTLKQWRSE VDEKREVFHA LEDELQKAKA ISDEMFKTHK 
      1260       1270       1280       1290       1300
ERDLDFDWHK EKADQLVERW QSVHVQIDNR LRDLEGIGKS LKHYRDSYHP 
      1310       1320       1330       1340       1350
LDDWIQHIET TQRKIQENQP ENSKALALQL NQQKMLVSEI EVKQSKMDEC 
      1360       1370       1380       1390       1400
QKYSEQYSAA VKDYELQTMT YRAMVESQQK SPVKRRRIQS SADLVIQEFM 
      1410       1420       1430       1440       1450
DLRTRYTALV TLMTQYIKFA GDSLKRLEEE EKSLDEEKKQ HIEKAKELQK 
      1460       1470       1480       1490       1500
WVSNISKTLG DGEKAGKPLF SKQQMSSKEI STKKEQFSEA LQTTQIFLAK 
      1510       1520       1530       1540       1550
HGDKLTEEER SDLEKQVKTL QEGYNLLFSE SLKQQELQPS GESKVPEKPD 
      1560       1570       1580       1590       1600
KVIAGTINQT TGEVLSVFQA VLRGLIDYET GIRLLEAQLV ITGLISPELR 
      1610       1620       1630       1640       1650
KCFDLRDAES HGLIDEQVLR QLKELNRAKQ LISTASPTSI PVLDSLAQGM 
      1660       1670       1680       1690       1700
VSESMAIRVL EILLSAGPLL VPATGEHLTL QQAFQQNLIS SALFSKVLER 
      1710       1720       1730       1740       1750
QDTCKDLIDP CTSEKVSLTD MVQRSILQEN TRMWLLPVRP QEAGRITLKC 
      1760       1770       1780       1790       1800
GRSVSILRAA HEGLIDRETM FRLLGAQLLS GGLIDCNSGQ KMTVEEAVAE 
      1810       1820       1830       1840       1850
GVIDRDTASS ILTYQVQTGG IVHSNPAKRL TVDEAVQCEL ITSSSALLVL 
      1860       1870       1880       1890       1900
EAQRGYVGLI WPHSGEIFPT SSSLQQELIT NELASKILNG RQKIAALYIP 
      1910       1920       1930       1940       1950
ESSQVIGLDA AKQLGIIDNN TASVLKSVTL PDKMPDLGDL EDCKNAKRWL 
      1960       1970       1980       1990       2000
SFCKLQPSTV HDYRQEEGGS DGEEPVTAQS SEQTKKLFLS YLMVNSYMDA 
      2010       2020       2030       2040       2050
HTGQRLLLYD GDLDEAVGML LESCGTELGA DTSTRESLSV LTIPDAFPDC 
      2060       2070       2080       2090       2100
ALSEEKHECS AAAAGPDKCH YSHPGHKESL ENAKWDMNEA FCKMGNNDSN 
      2110       2120       2130       2140       2150
GELPRPENLA DTTVVQKGSE SPSRVRVPKP TSSSTQPEGS VLRPESGSIL 
      2160       2170       2180       2190       2200
KGCKSQSEPV TKKYPDGANH SHFLTSETSR PCDSNEREDE ENIQKGPSVF 
      2210       2220       2230       2240       2250
DYSPRLSALL SHDELRQSQG RFSDTSTPQN TGYLCEASTL SPSDQRVLAD 
      2260       2270       2280       2290       2300
QSTREKFQDQ FLGIAAISVS LQGAPCGQKP VDTECSSSQV HYHSEESMSD 
      2310       2320       2330       2340       2350
ASAESGATRQ TDESEKTGSK VEDNSCTMVP GGGSRNDNTS DCGPLSHKGA 
      2360       2370       2380       2390       2400
IDAGDYETSL LAGQQSDTAT DSDSDDYFYD TPLFEDEDHD SLILQGDDRD 
      2410       2420       2430       2440       2450
CLQPEDYDTS LQEENDRTPP PDDIFYDVMK EKENPEFPHG GMDESLGVEN 
      2460       2470       2480       2490       2500
KVCCPQGFPV GIEKPELYLA GEKEFNSGGS EQLVESVSES ENPPGLWDSE 
      2510       2520       2530       2540       2550
SDSLTEGEII GRKERLGASL TPDGHWRGDR EECDTSRESQ SDTDGVGSIQ 
      2560       2570       2580       2590       2600
SSESYRPYMS DGSDLDEEDN GGRSSEDSGD GRGGQGVADE GGEPQYQADP 
      2610       2620       2630       2640       2650
TQLYTAIRKE HGGETQNVSD MIPLDKTHSY SPLETQHGAG VFQPESAGRG 
      2660       2670       2680       2690       2700
GWDTERSSHP ELTTEADEED EASLSTHMAT KGVSLSNAEG TASEEIRLVQ 
      2710       2720       2730       2740       2750
GPDSTGILKA EDLENVSPEI SPSSDNIVRS EAELGGGASE DGHLSFTGSD 
      2760       2770       2780       2790       2800
RDQQGPGRGL VKGRDGQSDK LVDETSIREM GFQKEGVLMS SPEEGGEEER 
      2810       2820       2830       2840       2850
DLEPFPNGSA TESLNMGKSQ VPPLLTHTEE LSHRGAPHTT TMTTTMTLEG 
      2860       2870       2880       2890       2900
EAKNVQTGLT ESPVLLETLA EIFDTPASKV TRADLTSAVT ASEMKSQVKE 
      2910       2920       2930       2940       2950
DSLTGGPEKE TGPCTSLGHC DKCIHVDMLE PNEHTPSCAL VAPPTVKDNL 
      2960       2970       2980       2990       3000
CSVNNAGEKS VRPQEDWPPA AEVRLSDACV EESISEGKAG ILQFTPENSD 
      3010       3020       3030       3040       3050
STLSRLPHQS VAGWGKSADS VQARLPVSGV RHTSADTLDV GCPQLESSRE 
      3060       3070       3080       3090       3100
KASAEEEPHR ERALSLKPQE REHHMLGFVE DGRSILKSSL DKVHMNLQEV 
      3110       3120       3130       3140       3150
GDPSAGTGTK ISIQNLIRRA ILSELPNEVS NVPSHGISPI SNSSEVRAES 
      3160       3170       3180       3190       3200
GGDPFCITSF LHLLKQNQPP QETPGISELA KVLTQMDCDP EQRGLGSELL 
      3210       3220       3230       3240       3250
PPQLKNAFYK LLFDGYATEK DQAEALGQTS CAVPKMAEEK PHVCSDLRNK 
      3260       3270       3280       3290       3300
EGHHCPLNPQ AVGEAEVEPF SVHIAALPGG EKLGELCSEP PEHSESTSGS 
      3310       3320       3330       3340       3350
KERSSDSSSK EKCSNGLQQC LQHTEKMHEY LVLLQDMKPP LDNQASVESS 
      3360       3370       3380       3390       3400
LEALKSQLKQ LEAFELGLAP IAVFLRKDLK LAEEFLKSFP SDLPRRHHEE 
      3410       3420       3430       3440       3450
LSKSHQRLQN AFSSLSSVSS ERMKLIKLAI NSEMSKLAVR HEDFLHKLTS 
      3460       3470       3480       3490       3500
YSDWVSEKSR SVKAIQTVNV QDTELVKNSV KFLKNVLADL SHTKMQLETT 
      3510       3520       3530       3540       3550
AFDVQSFISD YAQDLSPSQS RQLLRLLNTT QKGFLDLQEL VTTEADRLEA 
      3560       3570       3580       3590       3600
LLQLEQELGH QKVVAERQQE YREKLQGLCD LLTQTENRLI SNQEAFVIGD 
      3610       3620       3630       3640       3650
GTVELQKYQS KQEELQRDMQ GSTQAMEEIV RNTELFLKES GDELSQADRA 
      3660       3670       3680       3690       3700
LIEQKLNEVK MKCAQLNLKA EQSRKELDKA VTTALKEETE KVAAVRQLEE 
      3710       3720       3730       3740       3750
SKTKIENLLN WLSNVEEDSE GVWTKHTQPM EQNGTYLHEG DSKLGAGEED 
      3760       3770       3780       3790       3800
EVNGNLLETD AEGHSEATKG NLNQQYEKVK AQHGKIMAQH QAVLLATQSA 
      3810       3820       3830       3840       3850
QVLLEKQGHY LSPEEKEKLQ KNTQELKVHY EKVLAECEKK VKLTHSLQEE 
      3860       3870       3880       3890       3900
LEKFDTDYSE FEHWLQQSEQ ELANLEAGAD DLSGLMDKLT RQKSFSEDVI 
      3910       3920       3930       3940       3950
SHKGDLRYIT ISGNRVIDAA KSCSKRDSDR IGKDSVETSA THREVQTKLD 
      3960       3970       3980       3990       4000
QVTDRFRSLY SKCSVLGNNL KDLVDQYQQY EDASCGLLSG LQACEAKASK 
      4010       4020       4030       4040       4050
HLREPIALDP KNLQRQLEET KALQGQISSQ QVAVEKLKKT AEVLLDAKGS 
      4060       4070       4080       4090       4100
LLPAKNDIQK TLDDIVGRYD DLSKCVNERN EKLQITLTRS LSVQDALDEM 
      4110       4120       4130       4140       4150
LDWMGSVESS LVKPGQVPLN STALQDLISK DTMLEQDITG RQSSINAMNE 
      4160       4170       4180       4190       4200
KVKTFIETTD PSTASSLQAK MKDLSARFSE ASQKHKEKLA KMVELKAKVE 
      4210       4220       4230       4240       4250
QFEKLSDKLQ TFLETQSQAL TEVAMPGKDV PELSQHMQES TAKFLEHRKD 
      4260       4270       4280       4290       4300
LEALHSLLKE ISSHGLPGDK ALVFEKTNNL SRKFKEMEDT IQEKKDALSS 
      4310       4320       4330       4340       4350
CQEQLSAFQT LAQSLKTWIK ETTKQVPVVK PSLGTEDLRK SLEETKKLQE 
      4360       4370       4380       4390       4400
KWNLKAPEIH KANNSGVSLC NLLSALISPA KAIAAAKSGG VILNGEGTDT 
      4410       4420       4430       4440       4450
NTQDFLANKG LTSIKKDMTD ISHSYEDLGL LLKDKIVELN TKLSKLQKAQ 
      4460       4470       4480       4490       4500
EESSAMMQWL EKMNKTASRW RQTPTPADTE SVKLQVEQNK SFEAELKQNV 
      4510       4520       4530       4540       4550
NKVQELKDKL SELLEENPEA PEAQSWKQAL AEMDTKWQEL NQLTMDRQQK 
      4560       4570       4580       4590       4600
LEESSNNLTQ FQTTEAQLKQ WLMEKELMVS VLGPLSIDPN MLNTQKQQVQ 
      4610       4620       4630       4640       4650
ILLQEFDTRK PQYEQLTAAG QGILSRPGED PSLHGIVNEQ LEAVTQKWDN 
      4660       4670       4680       4690       4700
LTGQLRDRCD WIDQAIVKST QYQSLLRSLS GTLTELDDKL SSGLTSGALP 
      4710       4720       4730       4740       4750
DAVNQQLEAA QRLKQEIEQQ APKIKEAQEV CEDLSALVKE EYLKAELSRQ 
      4760       4770       4780       4790       4800
LEGILKSFKD IEQKTENHVQ HLQSACASSH QFQQMSKDFQ AWLDAKKEEQ 
      4810       4820       4830       4840       4850
RDSPPISAKL DVLESLLNSQ KDFGKTFTEQ SNIYEKTISE GENLLLKTQG 
      4860       4870       4880       4890       4900
AEKAALQLQL NTMKTDWDRF RKQVKEREEK LKDSLEKALK YREQVETLRP 
      4910       4920       4930       4940       4950
WIDRCQHSLD GVTFSLDPTE SESSIAELKS LQKEMDHHFG MLELLNNTAN 
      4960       4970       4980       4990       5000
SLLSVCEVDK EAVTEENQSL MEKVNRVTEQ LQSKTVSLEN MAQKFKEFQE 
      5010       5020       5030       5040       5050
VSRDTQRQLQ DTKEQLEVHH SLGPQAYSNK HLSVLQAQQK SLQTLKQQVD 
      5060       5070       5080       5090       5100
EAKRLAQDLV VEAADSKGTS DVLLQAETLA EEHSELSQQV DEKCSFLETK 
      5110       5120       5130       5140       5150
LQGLGHFQNT IREMFSQFTE CDDELDGMAP VGRDAETLRK QKACMQTFLK 
      5160       5170       5180       5190       5200
KLEALMASND SANRTCKMML ATEETSPDLI GVKRDLEALS KQCNKLLDRA 
      5210       5220       5230       5240       5250
KTREEQVDGA TEKLEEFHRK LEEFSTLLQK AEEHEESQGP VGTETETINQ 
      5260       5270       5280       5290       5300
QLDVFKVFQK EEIEPLQVKQ QDVNWLGQGL IQSAAANTCT QGLEHDLDSV 
      5310       5320       5330       5340       5350
NSRWKTLNKK VAQRTSQLQE ALLHCGRFQD ALESLLSWMA DTEELVANQK 
      5360       5370       5380       5390       5400
PPSAEFKVVK AQIQEQKLLQ RLLEDRKSTV EVIKREGEKI AASAEPADRV 
      5410       5420       5430       5440       5450
KLTRQLSLLD SRWEALLSRA EARNRQLEGI SVVAQEFHET LEPLNEWLTA 
      5460       5470       5480       5490       5500
VEKKLANSEP IGTQAPKLEE QISQHKALQE DILLRKQSVD QALLNGLELL 
      5510       5520       5530       5540       5550
KQTTGDEVLI IQDKLEAIKA RYKDITKLSA DVAKTLEHAL QLAGQLQSMH 
      5560       5570       5580       5590       5600
KELCNWLDKV EVELLSYETQ GLKGEAASQV QERQKELKNE VRSNKALVDS 
      5610       5620       5630       5640       5650
LNEVSSALLE LVPWRAREGL EKTIAEDNER YRLVSDTITQ KVEEIDAAIL 
      5660       5670       5680       5690       5700
RSQQFEQAAD AELSWITETQ KKLMSLGDIR LEQDQTSAQL QVQKAFTMDI 
      5710       5720       5730       5740       5750
LRHKDIIDEL VTSGHKIMTT SSEEEKQSMK KKLDKVLKKY DAVCQINSER 
      5760       5770       5780       5790       5800
HLQLERAQSL VSQFWETYEE LWPWLTETQR IISQLPAPAL EYETLRRQQE 
      5810       5820       5830       5840       5850
EHRQLRELIA EHKPHIDKMN KTGPQLLELS PKEGIYIQEK YVAADTLYSQ 
      5860       5870       5880       5890       5900
IKEDVKKRAV VLDEAISQST QFHDKIDQIL ESLERIAERL RQPPSISAEV 
      5910       5920       5930       5940       5950
EKIKEQIGEN KSVSVDMEKL QPLYETLRQR GEEMIARSEG TEKDVSARAV 
      5960       5970       5980       5990       6000
QDKLDQMVFI WGSIHTLVEE REAKLLDVME LAEKFWCDHM SLVVTIKDTQ 
      6010       6020       6030       6040       6050
DFIRDLEDPG IDPSVVKQQQ EAAEAIREEI DGLQEELDMV ITLGSELIAA 
      6060       6070       6080       6090       6100
CGEPDKPIVK KSIDELNSAW DSLNKAWKDR VDRLEEAMQA AVQYQDGLQG 
      6110       6120       6130       6140       6150
IFDWVDIAGN KLATMSPIGT DLETVKQQIE ELKQFKSEAY QQQIEMERLN 
      6160       6170       6180       6190       6200
HQAELLLKKV TEEADKHTVQ DPLMELKLIW DSLDERIVSR QHKLEGALLA 
      6210       6220       6230       6240       6250
LGQFQHALDE LLAWLTHTKG LLSEQKPVGG DPKAIEIELA KHHVLQNDVL 
      6260       6270       6280       6290       6300
AHQSTVEAVN KAGNDLIESS EGEEASNLQY KLRILNQRWQ DILEKTDQRK 
      6310       6320       6330       6340       6350
QQLDSALRQA KGFHGEIEDL QQWLTDTERH LLASKPLGGL PETAKEQLNA 
      6360       6370       6380       6390       6400
HMEVCTAFAI KEETYKSLML RGQQMLARCP RSAETNIDQD ITNLKEKWES 
      6410       6420       6430       6440       6450
VKSKLNEKKT KLEEALHLAM NFHNSLQDFI NWLTQAEQTL NVASRPSLIL 
      6460       6470       6480       6490       6500
DTILFQIDEH KVFANEVNSH REQIIELDKT GTHLKYFSQK QDVVLIKNLL 
      6510       6520       6530       6540       6550
ISVQSRWEKV VQRLVERGRS LDEARKRAKQ FHEAWSKLME WLEESEKSLD 
      6560       6570       6580       6590       6600
SELEIANDPD KIKAQLVQHK EFQKSLGGKH SVYDTTNRTG RSLKEKTSLA 
      6610       6620       6630       6640       6650
DDNLKLDNML SELRDKWDTI CGKSVERQNK LEEALLFSGQ FTDALQALID 
      6660       6670       6680       6690       6700
WLYRVEPQLA EDQPVHGDID LVMNLIDNHK VFQKELGKRT SSVQALKRSA 
      6710       6720       6730       6740       6750
RELIEGSRDD SSWVRVQMQE LSTRWETVCA LSISKQTRLE SALQQAEEFH 
      6760       6770       6780       6790       6800
SVVHTLLEWL AEAEQTLRFH GALPDDEDAL RTLIEQHKEF MKRLEEKRAE 
      6810       6820       6830       6840       6850
LSKATGMGDA LLAVCHPDSI TTIKHWITII QARFEEVLAW AKQHQQRLAG 
      6860       6870       6880       6890       6900
ALAGLIAKQE LLETLLAWLQ WAETTLTEKD KEVIPQEIEE VKTLIAEHQT 
      6910       6920       6930       6940       6950
FMEEMTRKQP DVDKVTKTYK RRATDPPSLQ SHIPVLDKGR AGRKRFPASG 
      6960       6970       6980       6990       7000
FYPSGSQTQI ETKNPRVNLL VSKWQQVWLL ALERRRKLND ALDRLEELRE 
      7010       7020       7030       7040       7050
FANFDFDIWR KKYMRWMNHK KSRVMDFFRR IDKDQDGKIT RQEFIDGILS 
      7060       7070       7080       7090       7100
SKFPTSRLEM SAVADIFDRD GDGYIDYYEF VAALHPNKDA YKPITDADKI 
      7110       7120       7130       7140       7150
EDEVTRQVAK CKCAKRFQVE QIGDNKYRFF LGNQFGDSQQ LRLVRILRST 
      7160       7170       7180       7190       7200
VMVRVGGGWM ALDEFLVKND PCRVHHHGSK MLRSESNSSI TATQPTLAKG 
      7210       7220       7230       7240       7250
RTNMELREKF ILADGASQGM AAFRPRGRRS RPSSRGASPN RSTSASSHAC 
      7260       7270       7280       7290       7300
QAASPPVPAA ASTPKGTPIQ GSKLRLPGYL SGKGFHSGED SALITTAAAR 
      7310       7320       7330       7340       7350
VRTQFAESRK TPSRPGSRAG SKAGSRASSR RGSDASDFDI SEIQSVCSDV 
      7360       7370       7380       7390 
ETVPQTHRPV PRAGSRPSTA KPSKIPTPQR RSPASKLDKS SKR
Length:7,393
Mass (Da):834,218
Last modified:September 3, 2014 - v2
Checksum:iC3CDF88978C33EF1
GO
Isoform 11 Publication (identifier: Q91ZU6-2) [UniParc]FASTAAdd to basket
Also known as: BPAG1-a, BPAG1a2

The sequence of this isoform differs from the canonical sequence as follows:
     1549-3562: Missing.

Show »
Length:5,379
Mass (Da):615,214
Checksum:i083579C45EA0566F
GO
Isoform 3Curated (identifier: Q91ZU6-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     7129-7134: Missing.
     7174-7197: Missing.
     7265-7265: K → KILHPLTRNYGKPWLANSKMSTPCKAAECPDFPVSSAE

Note: No experimental confirmation available.Curated
Show »
Length:7,400
Mass (Da):834,953
Checksum:i80B5A7C7FDA19949
GO
Isoform 4Curated (identifier: Q91ZU6-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     7174-7197: Missing.
     7265-7265: K → KILHPLTRNYGKPWLANSKMSTPCKAAECPDFPVSSAE

Note: No experimental confirmation available.Curated
Show »
Length:7,406
Mass (Da):835,660
Checksum:iFA78FB01B169CFA7
GO
Isoform 5 (identifier: Q91ZU6-5) [UniParc]FASTAAdd to basket
Also known as: BPAG1-e

The sequence of this isoform differs from the canonical sequence as follows:
     1-381: MAGYLSPAAY...REKALRPEVE → MQSSSYSYRS...SFSNESLDGH
     1432-1432: K → MKRSKENSEH...GISNLYYSSQ
     1433-7393: Missing.

Show »
Length:2,639
Mass (Da):304,781
Checksum:i1FB46C15C1834D29
GO
Isoform 6 (identifier: Q91ZU6-6) [UniParc]FASTAAdd to basket
Also known as: BPAG1n, BPAG1-n1, BPAG1-n2, BPAG1a2, dystonin-2

The sequence of this isoform differs from the canonical sequence as follows:
     1-30: MAGYLSPAAYMYVEEQEYLQAYEDVLERYK → MIAAAFLVLL...PAERAVLRIA
     305-7393: Missing.

Note: Incomplete sequence. Transmembrane protein (helical transmembrane domain from amino acid 18 to 38).Curated
Show »
Length:482
Mass (Da):55,058
Checksum:iA40496BA1F6125BD
GO
Isoform 7 (identifier: Q91ZU6-8) [UniParc]FASTAAdd to basket
Also known as: BPAG1a3

The sequence of this isoform differs from the canonical sequence as follows:
     1-137: MAGYLSPAAY...GLIWTIILHF → MGNVCGCVRA...SKDAPRDDGC
     271-272: VK → KG
     273-7393: Missing.

Note: Incomplete sequence. Probably myristoylated on Gly-2. Probably S-palmitoylated on Cys-5 and Cys-7. Mutagenesis of Gly-2 to Ala inhibits cortical localization. Mutagenesis of Cys-5 to Ser inhibits cortical localization. Mutagenesis of Cys-7 to Ser inhibits cortical localization.Combined sources
Show »
Length:388
Mass (Da):42,618
Checksum:i7258EC5F1E2DA4E7
GO

Sequence cautioni

Isoform 6 : The sequence AAC52231 differs from that shown. Reason: Frameshift at position 51. Curated
The sequence AAK83382 differs from that shown.Many conflicts and frameshifts that might be strain-specific.Curated
The sequence AAK83383 differs from that shown.Many conflicts and frameshifts that might be strain-specific.Curated
The sequence AAK83384 differs from that shown.Many conflicts and frameshifts that might be strain-specific.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Isoform 6 (identifier: Q91ZU6-6)
Sequence conflicti101 – 1011E → K in AAC52231 (PubMed:7670468).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 381381MAGYL…RPEVE → MQSSSYSYRSSDSVFSNTTS TRTSLDSNENLLSVHCGPTL INSCISFSNESLDGH in isoform 5. 1 PublicationVSP_055459Add
BLAST
Alternative sequencei1 – 137137MAGYL…IILHF → MGNVCGCVRAEKEEPYFDPA KSPLSPEKYSPGRKYFRRKP CQKVVDDTEPVRQSSEREGK KGVSQPAGGQPAVSSGELPW EDPAASPTKEDAVQLGKRAA TEHGDQKPLPSSVDGYPHRV TVSSAQGRYSEVQVSIPDKI ISEEDSPPYCPETERHLDDV NSKHRTFLRKDNVSLSQTAA SSSPILCVTEKSLKNSALMG NLSRSCHSVLEQDSDERGHP FGVHRLQLTKRRCHSLSSGV SCVSKDAPRDDGC in isoform 7. 1 PublicationVSP_041542Add
BLAST
Alternative sequencei1 – 3030MAGYL…LERYK → MIAAAFLVLLRPYSIQCALF LLLLLLGTVATIVFFCCWHR KLQKGRHPMKSVFSGRSRSR DAALRSHHFRSEGFRASPRH IRRRVAAAAAARLEEVKPVV EVHHQSEQESSGRKRRIKKN SRVQPEFYHSVQGASTRRPS SGNASYRCSMSSSADFSDED DFSQKSGSASPAPGDTLPWN LPKHERSKRKIQGGSVLDPA ERAVLRIA in isoform 6. 1 PublicationVSP_041543Add
BLAST
Alternative sequencei271 – 2722VK → KG in isoform 7. 1 PublicationVSP_041544
Alternative sequencei273 – 73937121Missing in isoform 7. 1 PublicationVSP_041545Add
BLAST
Alternative sequencei305 – 73937089Missing in isoform 6. 1 PublicationVSP_041546Add
BLAST
Alternative sequencei1432 – 14321K → MKRSKENSEHGAYSDLLQRQ RATMVENSKLTGKISELETM VAELKKQKSRVEEELPKVKE AAENELRKQQRNVEDIALQK LRAESEAKQYRRELETIVRE KEAAERELERVRQLTAEAEA RRAAVEENLRNFRSQLQENT FTRQTLEDHLRRKDSSLSDL EQQKRALVEELQRKRDHEEE LLRLVKQMERDLAFQKQVAE KQLKEKQKVELEARRKITEI QFSCRESAAVAQARPQREQG RQKEEELKQQVDELTLANRK AEKEMRELKYELSAVQLEKA SSEEKARLLKDKLDETNNTL KCLKEDLERKDQAQERYSQQ LRDLGRQLNQTTDKAEEVRQ EANDLKKIKHTYQLELESLH QEKGKLQREVDRVTRAHALA ERNIQCLNSQVHASRDEKDL SEERRRLCQRKSDHLKEEFE RSHAQLLQNIQAEKENNDKI QKLNKELEKSNECAETLKQK VDELTRQNNETKLMMQRIQA ESKNIVREKQAIQQRCEVLR IQADGFKDQLRNTNEHLHKQ TKTEQDFHRKIKSLEDDLAQ SQNLVSEFKQKCDQQSMIIQ KTEKEVRSLSAELSASKEEK RREEQKAQLQRAQVQELNDR LKRVQDELHLKTIEEQMTHR KMILLQEESDKFKRSADEFR KKMEKLMESKVVTETDLSGI KHDFVSLQRENFRAQENAKL WETNIRELERQLQCYREKMQ QGPPVEANHYQKCRRLEEEL LAQRREVENLKQKMDQQIKE HEHQLLRLQCEIQKKSTTQD HTFASAFDTAGRECHHPAEI SPGNSGHLNLKTRLPLSRWT QEPHQTEGKWPHRAAEQLPK EVQFRQPGAPLDRESSQPCY SEYFSQTSTELQITFDDKNP ITRLSELETMREQALHPSRP PVTYQDDKLERELVKLLTPL EIAKNKQCGMHTEVTTLKQE KRLGSSAGGWMLEGCRTSGG LKGDFLKKSVEPEASPSLDL NQACSVRDEEFQFQGLRHTV TGRQLVEAKLLDMRTVEQLR LGLKTVEEVQRSLSKFLTKA TSIAGLYLESSKEKMSFTSA AQKIIIDKMIALAFLEAQAA TGFIIDPVSGQTYCVEDAVL HGIVDPEFRSRLLEAEKAVL GYSHASKTLSVFQAMENRML DRKKGKHILEAQIASGGVID PVRGVRVPPEMAVQQGLLNN AVLQFLHEPSSNTRVFPNPN NKQALYYSELLQICVFDVDC QCFLLPFGEREISNLNIEKT HKIAVVDTKTGAELTAFEAF QRNLIDKGIYLELSGQQYQW KEATFFDSYGHPSHMLTDTK TGLQFNISEAVEQGTLDKAL VQKYQEGLTTLTELADFLLS KVVPKKDLHSPIAGYWLTAS GERISLLKASRRNLVDRVTA LRCLEAQICTGGIIDPLTGK KYRVAEALHRGLVDEGFAQQ LRQCELVITGISHPVSNKMM SVVEAVNANIISKEMGMRCL EFQYLTGGLIEPKVFSRLTI EEALHVGIIDVLIATRLKDQ KSYVRDIMCPQTKRKLTYKE ALEKADFDFHTGLKLLEVSE PLGTGISNLYYSSQ in isoform 5. 1 PublicationVSP_055460
Alternative sequencei1433 – 73935961Missing in isoform 5. 1 PublicationVSP_055461Add
BLAST
Alternative sequencei1549 – 35622014Missing in isoform 1. 1 PublicationVSP_041549Add
BLAST
Alternative sequencei7129 – 71346Missing in isoform 3. 1 PublicationVSP_041550
Alternative sequencei7174 – 719724Missing in isoform 3 and isoform 4. 1 PublicationVSP_041551Add
BLAST
Alternative sequencei7265 – 72651K → KILHPLTRNYGKPWLANSKM STPCKAAECPDFPVSSAE in isoform 3 and isoform 4. 1 PublicationVSP_041552

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF396877 mRNA. Translation: AAK83382.1. Sequence problems.
AF396878 mRNA. Translation: AAK83383.1. Sequence problems.
AF396879 mRNA. Translation: AAK83384.1. Sequence problems.
AC123072 Genomic DNA. No translation available.
AC124386 Genomic DNA. No translation available.
AC127433 Genomic DNA. No translation available.
U22452 mRNA. Translation: AAC52230.1.
U25158 mRNA. Translation: AAC52231.1. Frameshift.
DQ023311 mRNA. Translation: AAY46942.1.
DQ463750 mRNA. Translation: ABF00406.1.
AK051626 mRNA. Translation: BAC34695.1.
AK037206 mRNA. Translation: BAC29753.1.
AF115383 mRNA. Translation: AAD22959.1.
AB085694 mRNA. Translation: BAB93448.1.
CCDSiCCDS35534.1. [Q91ZU6-1]
CCDS35535.1. [Q91ZU6-2]
CCDS69875.1. [Q91ZU6-5]
PIRiA60776.
I49290.
I49298.
RefSeqiNP_034211.2. NM_010081.2. [Q91ZU6-5]
NP_598594.2. NM_133833.3. [Q91ZU6-2]
NP_604443.2. NM_134448.3. [Q91ZU6-1]
UniGeneiMm.336625.
Mm.478284.
Mm.487428.

Genome annotation databases

EnsembliENSMUST00000097785; ENSMUSP00000095392; ENSMUSG00000026131. [Q91ZU6-1]
ENSMUST00000097786; ENSMUSP00000095393; ENSMUSG00000026131. [Q91ZU6-2]
ENSMUST00000183302; ENSMUSP00000138376; ENSMUSG00000026131. [Q91ZU6-5]
GeneIDi13518.
KEGGimmu:13518.
UCSCiuc007aoi.2. mouse. [Q91ZU6-1]
uc007aoj.2. mouse. [Q91ZU6-2]
uc007aok.1. mouse. [Q91ZU6-8]
uc007aol.2. mouse. [Q91ZU6-5]

Keywords - Coding sequence diversityi

Alternative promoter usage, Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF396877 mRNA. Translation: AAK83382.1. Sequence problems.
AF396878 mRNA. Translation: AAK83383.1. Sequence problems.
AF396879 mRNA. Translation: AAK83384.1. Sequence problems.
AC123072 Genomic DNA. No translation available.
AC124386 Genomic DNA. No translation available.
AC127433 Genomic DNA. No translation available.
U22452 mRNA. Translation: AAC52230.1.
U25158 mRNA. Translation: AAC52231.1. Frameshift.
DQ023311 mRNA. Translation: AAY46942.1.
DQ463750 mRNA. Translation: ABF00406.1.
AK051626 mRNA. Translation: BAC34695.1.
AK037206 mRNA. Translation: BAC29753.1.
AF115383 mRNA. Translation: AAD22959.1.
AB085694 mRNA. Translation: BAB93448.1.
CCDSiCCDS35534.1. [Q91ZU6-1]
CCDS35535.1. [Q91ZU6-2]
CCDS69875.1. [Q91ZU6-5]
PIRiA60776.
I49290.
I49298.
RefSeqiNP_034211.2. NM_010081.2. [Q91ZU6-5]
NP_598594.2. NM_133833.3. [Q91ZU6-2]
NP_604443.2. NM_134448.3. [Q91ZU6-1]
UniGeneiMm.336625.
Mm.478284.
Mm.487428.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2IAKX-ray3.00A580-803[»]
ProteinModelPortaliQ91ZU6.
SMRiQ91ZU6. Positions 31-255, 583-795.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199328. 1 interaction.
IntActiQ91ZU6. 6 interactions.
MINTiMINT-1861530.
STRINGi10090.ENSMUSP00000095392.

Chemistry

ChEMBLiCHEMBL2176789.

PTM databases

iPTMnetiQ91ZU6.
PhosphoSiteiQ91ZU6.

2D gel databases

REPRODUCTION-2DPAGEIPI00230689.
IPI00230690.
IPI00284272.

Proteomic databases

MaxQBiQ91ZU6.
PaxDbiQ91ZU6.
PeptideAtlasiQ91ZU6.
PRIDEiQ91ZU6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000097785; ENSMUSP00000095392; ENSMUSG00000026131. [Q91ZU6-1]
ENSMUST00000097786; ENSMUSP00000095393; ENSMUSG00000026131. [Q91ZU6-2]
ENSMUST00000183302; ENSMUSP00000138376; ENSMUSG00000026131. [Q91ZU6-5]
GeneIDi13518.
KEGGimmu:13518.
UCSCiuc007aoi.2. mouse. [Q91ZU6-1]
uc007aoj.2. mouse. [Q91ZU6-2]
uc007aok.1. mouse. [Q91ZU6-8]
uc007aol.2. mouse. [Q91ZU6-5]

Organism-specific databases

CTDi667.
MGIiMGI:104627. Dst.

Phylogenomic databases

eggNOGiKOG0516. Eukaryota.
KOG0517. Eukaryota.
COG5069. LUCA.
GeneTreeiENSGT00760000119163.
HOVERGENiHBG031127.
InParanoidiQ91ZU6.
KOiK10382.
OMAiRKITEIQ.

Enzyme and pathway databases

ReactomeiR-MMU-2022090. Assembly of collagen fibrils and other multimeric structures.
R-MMU-446107. Type I hemidesmosome assembly.

Miscellaneous databases

ChiTaRSiDst. mouse.
EvolutionaryTraceiQ91ZU6.
PROiQ91ZU6.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000026131.
CleanExiMM_DST.
ExpressionAtlasiQ91ZU6. baseline and differential.
GenevisibleiQ91ZU6. MM.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
1.10.418.10. 2 hits.
3.30.920.20. 1 hit.
3.90.1290.10. 3 hits.
InterProiIPR001589. Actinin_actin-bd_CS.
IPR001715. CH-domain.
IPR029926. Dystonin.
IPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR003108. GAS_dom.
IPR001101. Plectin_repeat.
IPR018159. Spectrin/alpha-actinin.
IPR002017. Spectrin_repeat.
[Graphical view]
PANTHERiPTHR11915:SF38. PTHR11915:SF38. 7 hits.
PfamiPF00307. CH. 2 hits.
PF13499. EF-hand_7. 1 hit.
PF02187. GAS2. 1 hit.
PF00681. Plectin. 2 hits.
PF00435. Spectrin. 18 hits.
[Graphical view]
SMARTiSM00033. CH. 2 hits.
SM00054. EFh. 2 hits.
SM00243. GAS2. 1 hit.
SM00250. PLEC. 9 hits.
SM00150. SPEC. 33 hits.
[Graphical view]
SUPFAMiSSF143575. SSF143575. 1 hit.
SSF47473. SSF47473. 1 hit.
SSF47576. SSF47576. 1 hit.
SSF75399. SSF75399. 2 hits.
PROSITEiPS00019. ACTININ_1. 1 hit.
PS00020. ACTININ_2. 1 hit.
PS50021. CH. 2 hits.
PS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 2 hits.
PS51460. GAR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDYST_MOUSE
AccessioniPrimary (citable) accession number: Q91ZU6
Secondary accession number(s): E9PXE5
, E9QL23, Q1KP04, Q3I6J6, Q60824, Q60845, Q8K5D4, Q91ZU7, Q91ZU8, Q9WU50, S4R1U5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 30, 2003
Last sequence update: September 3, 2014
Last modified: September 7, 2016
This is version 142 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.