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Q91ZU6

- DYST_MOUSE

UniProt

Q91ZU6 - DYST_MOUSE

Protein

Dystonin

Gene

Dst

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 2 (03 Sep 2014)
      Previous versions | rss
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    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

    1. calcium ion binding Source: InterPro
    2. microtubule binding Source: MGI
    3. microtubule plus-end binding Source: UniProtKB
    4. protein binding Source: UniProtKB
    5. protein homodimerization activity Source: UniProtKB

    GO - Biological processi

    1. axonogenesis Source: MGI
    2. cell adhesion Source: UniProtKB-KW
    3. cell cycle arrest Source: InterPro
    4. cell motility Source: Ensembl
    5. cytoplasmic microtubule organization Source: MGI
    6. hemidesmosome assembly Source: Ensembl
    7. intermediate filament cytoskeleton organization Source: UniProtKB
    8. intracellular transport Source: UniProtKB
    9. maintenance of cell polarity Source: Ensembl
    10. regulation of microtubule polymerization or depolymerization Source: MGI
    11. response to wounding Source: Ensembl
    12. retrograde axon cargo transport Source: MGI

    Keywords - Molecular functioni

    Muscle protein

    Keywords - Biological processi

    Cell adhesion

    Keywords - Ligandi

    Actin-binding, Calcium, Metal-binding

    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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Unplaced

    Organism-specific databases

    MGIiMGI:104627. Dst.

    Subcellular locationi

    Cytoplasmcytoskeleton. Cell projectionaxon. 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 : Cytoplasmcytoskeleton 1 Publication
    Note: Colocalizes both cortical and cytoplasmic actin filaments.
    Isoform 2 : Cell membranesarcolemma. CytoplasmmyofibrilsarcomereZ line. CytoplasmmyofibrilsarcomereH zone. Cytoplasmcytoskeleton
    Note: Localizes to microtubules and actin microfilaments throughout the cytoplasm and at focal contact attachments at the plasma membrane.
    Isoform 5 : Cytoplasmcytoskeleton. Cell junctionhemidesmosome
    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 : Nucleus. Nucleus envelope. Membrane; Single-pass membrane protein. Endoplasmic reticulum membrane; Single-pass membrane protein. Cytoplasmcytoskeleton
    Note: Associates with actin cytoskeleton in sensory neurons By similarity. Localizes to actin and intermediate filaments cytoskeletons. Localizes to central actin stress fibers around the nucleus and is excluded form focal contact sites in myoblast cells. Translocates to the nucleus.By similarity

    GO - Cellular componenti

    1. actin cytoskeleton Source: MGI
    2. axon Source: UniProtKB-SubCell
    3. cell cortex Source: UniProtKB-SubCell
    4. cell leading edge Source: Ensembl
    5. cytoplasm Source: UniProtKB
    6. cytoplasmic membrane-bounded vesicle Source: MGI
    7. cytoplasmic side of plasma membrane Source: UniProtKB
    8. endoplasmic reticulum membrane Source: UniProtKB
    9. focal adhesion Source: UniProtKB
    10. hemidesmosome Source: MGI
    11. H zone Source: UniProtKB
    12. integral component of membrane Source: UniProtKB-KW
    13. intercalated disc Source: UniProtKB
    14. intermediate filament Source: UniProtKB-KW
    15. membrane Source: UniProtKB
    16. microtubule cytoskeleton Source: MGI
    17. microtubule plus-end Source: UniProtKB
    18. neurofilament cytoskeleton Source: MGI
    19. nuclear envelope Source: UniProtKB
    20. nucleus Source: UniProtKB
    21. perinuclear endoplasmic reticulum Source: UniProtKB
    22. perinuclear region of cytoplasm Source: UniProtKB
    23. sarcolemma Source: UniProtKB
    24. stress fiber Source: UniProtKB
    25. Z disc Source: UniProtKB

    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. 2 Publications
    Mutagenesisi1386 – 13861R → A: Prevents isoform 6 from localizing to the nucleus; when associated with A-1385. 2 Publications

    PTM / Processingi

    Molecule processing

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

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2862 – 28621PhosphoserineBy similarity
    Modified residuei7254 – 72541PhosphoserineBy similarity

    Keywords - PTMi

    Lipoprotein, Myristate, Palmitate, Phosphoprotein

    Proteomic databases

    MaxQBiQ91ZU6.
    PaxDbiQ91ZU6.
    PRIDEiQ91ZU6.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00230689.
    IPI00230690.
    IPI00284272.

    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

    ArrayExpressiE9PXE5.
    BgeeiE9PXE5.
    CleanExiMM_DST.
    GenevestigatoriQ91ZU6.

    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 ERBB2IP (via C-terminus). Isoform 5 associates (via C-terminal) with KRT5-KRT14 (via rod region) intermadiate 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.

    Protein-protein interaction databases

    IntActiQ91ZU6. 5 interactions.
    MINTiMINT-1861530.
    STRINGi10090.ENSMUSP00000095392.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2IAKX-ray3.00A580-803[»]
    ProteinModelPortaliQ91ZU6.
    SMRiQ91ZU6. Positions 31-255, 268-479, 583-1051, 1553-1927, 4476-4570, 5208-5532, 6115-6480, 7098-7170.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ91ZU6.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini35 – 252218Actin-bindingAdd
    BLAST
    Domaini35 – 138104CH 1CuratedPROSITE-ProRule annotationAdd
    BLAST
    Domaini151 – 252102CH 2CuratedPROSITE-ProRule annotationAdd
    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

    eggNOGiCOG5069.
    HOVERGENiHBG031127.
    OrthoDBiEOG76738T.
    PhylomeDBiQ91ZU6.

    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.
    IPR011992. EF-hand-dom_pair.
    IPR018247. EF_Hand_1_Ca_BS.
    IPR002048. EF_hand_dom.
    IPR003108. GAS2_dom.
    IPR001101. Plectin_repeat.
    IPR018159. Spectrin/alpha-actinin.
    IPR002017. Spectrin_repeat.
    [Graphical view]
    PfamiPF00307. CH. 2 hits.
    PF13499. EF-hand_7. 1 hit.
    PF02187. GAS2. 1 hit.
    PF00681. Plectin. 5 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. 32 hits.
    [Graphical view]
    SUPFAMiSSF143575. SSF143575. 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. Align

    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

    MAGYLSPAAY MYVEEQEYLQ AYEDVLERYK DERDKVQKKT FTKWINQHLM     50
    KVRKHVNDLY EDLRDGHNLI SLLEVLSGDT LPREKGRMRF HRLQNVQIAL 100
    DYLKRRQVKL VNIRNDDITD GNPKLTLGLI WTIILHFQIS DIHVTGESED 150
    MSAKERLLLW TQQATEGYAG VRCENFTTCW RDGKLFNAII HKYRPDLIDM 200
    NTVAVQSNLA NLEHAFYVAE KIGVIRLLDP EDVDVSSPDE KSVITYVSSL 250
    YDAFPKVPEG GEGIGANDVE VKWIEYQNMV NYLIQWIRHH VVTMSERTFP 300
    NNPLELKALY NQYLQFKEKE IPPKEMEKSK IKRLYKLLEI WIEFGRIKLL 350
    QGYHPNDIEK EWGKLIIAML EREKALRPEV ERLDMLQQIA TRVQRDSVSC 400
    EDKLILARNA LQSDSKRLES GVQFQNEAEI AGYILECENL LRQHVIDVQI 450
    LIDGKYYQAD QLVQRVAKLR DEIMALRNEC SSVYSKGRML TTEQTKLMIS 500
    GITQSLNSGF AQTLHPSLNS GLTQSLTPSL TSSSVTSGLS SGMTSRLTPS 550
    VTPVYAPGFP SVVAPNFSLG VEPNSLQTLK LMQIRKPLLK SSLLDQNLTE 600
    EEVNMKFVQD LLNWVDEMQV QLDRTEWGSD LPSVESHLEN HKNVHRAIEE 650
    FESSLKEAKI SEIQMTAPLK LSYTDKLHRL ESQYAKLLNT SRNQERHLDT 700
    LHNFVTRATN ELIWLNEKEE SEVAYDWSER NSSVARKKSY HAELMRELEQ 750
    KEESIKAVQE IAEQLLLENH PARLTIEAYR AAMQTQWSWI LQLCQCVEQH 800
    IQENSAYFEF FNDAKEATDY LRNLKDAIQR KYSCDRSSSI HKLEDLVQES 850
    MEKEELLQYR SVVAGLMGRA KTVVQLKPRN PDNPLKTSIP IKAICDYRQI 900
    EITIYKDDEC VLANNSHRAK WKVISPTGNE AMVPSVCFTV PPPNKEAVDF 950
    ANRIEQQYQS VLTLWHESHI NMKSVVSWHY LVNEIDRIRA SNVASIKTML 1000
    PGEHQQVLSN LQSRLEDFLE DSQESQIFSG SDISQLEKEV SVCRKYYQEL 1050
    LKSAEREEQE ESVYNLYISE VRNIRLRLES CEDRLIRQIR TPLERDDLHE 1100
    SMLRITEQEK LKKELDRLKD DLGTITNKCE EFFSQAADSP SVPALRSELS 1150
    VVIQSLSQIY SMSSTYIEKL KTVNLVLKNT QAAEALVKLY ETKLCEEEAV 1200
    IADKNNIENL MSTLKQWRSE VDEKREVFHA LEDELQKAKA ISDEMFKTHK 1250
    ERDLDFDWHK EKADQLVERW QSVHVQIDNR LRDLEGIGKS LKHYRDSYHP 1300
    LDDWIQHIET TQRKIQENQP ENSKALALQL NQQKMLVSEI EVKQSKMDEC 1350
    QKYSEQYSAA VKDYELQTMT YRAMVESQQK SPVKRRRIQS SADLVIQEFM 1400
    DLRTRYTALV TLMTQYIKFA GDSLKRLEEE EKSLDEEKKQ HIEKAKELQK 1450
    WVSNISKTLG DGEKAGKPLF SKQQMSSKEI STKKEQFSEA LQTTQIFLAK 1500
    HGDKLTEEER SDLEKQVKTL QEGYNLLFSE SLKQQELQPS GESKVPEKPD 1550
    KVIAGTINQT TGEVLSVFQA VLRGLIDYET GIRLLEAQLV ITGLISPELR 1600
    KCFDLRDAES HGLIDEQVLR QLKELNRAKQ LISTASPTSI PVLDSLAQGM 1650
    VSESMAIRVL EILLSAGPLL VPATGEHLTL QQAFQQNLIS SALFSKVLER 1700
    QDTCKDLIDP CTSEKVSLTD MVQRSILQEN TRMWLLPVRP QEAGRITLKC 1750
    GRSVSILRAA HEGLIDRETM FRLLGAQLLS GGLIDCNSGQ KMTVEEAVAE 1800
    GVIDRDTASS ILTYQVQTGG IVHSNPAKRL TVDEAVQCEL ITSSSALLVL 1850
    EAQRGYVGLI WPHSGEIFPT SSSLQQELIT NELASKILNG RQKIAALYIP 1900
    ESSQVIGLDA AKQLGIIDNN TASVLKSVTL PDKMPDLGDL EDCKNAKRWL 1950
    SFCKLQPSTV HDYRQEEGGS DGEEPVTAQS SEQTKKLFLS YLMVNSYMDA 2000
    HTGQRLLLYD GDLDEAVGML LESCGTELGA DTSTRESLSV LTIPDAFPDC 2050
    ALSEEKHECS AAAAGPDKCH YSHPGHKESL ENAKWDMNEA FCKMGNNDSN 2100
    GELPRPENLA DTTVVQKGSE SPSRVRVPKP TSSSTQPEGS VLRPESGSIL 2150
    KGCKSQSEPV TKKYPDGANH SHFLTSETSR PCDSNEREDE ENIQKGPSVF 2200
    DYSPRLSALL SHDELRQSQG RFSDTSTPQN TGYLCEASTL SPSDQRVLAD 2250
    QSTREKFQDQ FLGIAAISVS LQGAPCGQKP VDTECSSSQV HYHSEESMSD 2300
    ASAESGATRQ TDESEKTGSK VEDNSCTMVP GGGSRNDNTS DCGPLSHKGA 2350
    IDAGDYETSL LAGQQSDTAT DSDSDDYFYD TPLFEDEDHD SLILQGDDRD 2400
    CLQPEDYDTS LQEENDRTPP PDDIFYDVMK EKENPEFPHG GMDESLGVEN 2450
    KVCCPQGFPV GIEKPELYLA GEKEFNSGGS EQLVESVSES ENPPGLWDSE 2500
    SDSLTEGEII GRKERLGASL TPDGHWRGDR EECDTSRESQ SDTDGVGSIQ 2550
    SSESYRPYMS DGSDLDEEDN GGRSSEDSGD GRGGQGVADE GGEPQYQADP 2600
    TQLYTAIRKE HGGETQNVSD MIPLDKTHSY SPLETQHGAG VFQPESAGRG 2650
    GWDTERSSHP ELTTEADEED EASLSTHMAT KGVSLSNAEG TASEEIRLVQ 2700
    GPDSTGILKA EDLENVSPEI SPSSDNIVRS EAELGGGASE DGHLSFTGSD 2750
    RDQQGPGRGL VKGRDGQSDK LVDETSIREM GFQKEGVLMS SPEEGGEEER 2800
    DLEPFPNGSA TESLNMGKSQ VPPLLTHTEE LSHRGAPHTT TMTTTMTLEG 2850
    EAKNVQTGLT ESPVLLETLA EIFDTPASKV TRADLTSAVT ASEMKSQVKE 2900
    DSLTGGPEKE TGPCTSLGHC DKCIHVDMLE PNEHTPSCAL VAPPTVKDNL 2950
    CSVNNAGEKS VRPQEDWPPA AEVRLSDACV EESISEGKAG ILQFTPENSD 3000
    STLSRLPHQS VAGWGKSADS VQARLPVSGV RHTSADTLDV GCPQLESSRE 3050
    KASAEEEPHR ERALSLKPQE REHHMLGFVE DGRSILKSSL DKVHMNLQEV 3100
    GDPSAGTGTK ISIQNLIRRA ILSELPNEVS NVPSHGISPI SNSSEVRAES 3150
    GGDPFCITSF LHLLKQNQPP QETPGISELA KVLTQMDCDP EQRGLGSELL 3200
    PPQLKNAFYK LLFDGYATEK DQAEALGQTS CAVPKMAEEK PHVCSDLRNK 3250
    EGHHCPLNPQ AVGEAEVEPF SVHIAALPGG EKLGELCSEP PEHSESTSGS 3300
    KERSSDSSSK EKCSNGLQQC LQHTEKMHEY LVLLQDMKPP LDNQASVESS 3350
    LEALKSQLKQ LEAFELGLAP IAVFLRKDLK LAEEFLKSFP SDLPRRHHEE 3400
    LSKSHQRLQN AFSSLSSVSS ERMKLIKLAI NSEMSKLAVR HEDFLHKLTS 3450
    YSDWVSEKSR SVKAIQTVNV QDTELVKNSV KFLKNVLADL SHTKMQLETT 3500
    AFDVQSFISD YAQDLSPSQS RQLLRLLNTT QKGFLDLQEL VTTEADRLEA 3550
    LLQLEQELGH QKVVAERQQE YREKLQGLCD LLTQTENRLI SNQEAFVIGD 3600
    GTVELQKYQS KQEELQRDMQ GSTQAMEEIV RNTELFLKES GDELSQADRA 3650
    LIEQKLNEVK MKCAQLNLKA EQSRKELDKA VTTALKEETE KVAAVRQLEE 3700
    SKTKIENLLN WLSNVEEDSE GVWTKHTQPM EQNGTYLHEG DSKLGAGEED 3750
    EVNGNLLETD AEGHSEATKG NLNQQYEKVK AQHGKIMAQH QAVLLATQSA 3800
    QVLLEKQGHY LSPEEKEKLQ KNTQELKVHY EKVLAECEKK VKLTHSLQEE 3850
    LEKFDTDYSE FEHWLQQSEQ ELANLEAGAD DLSGLMDKLT RQKSFSEDVI 3900
    SHKGDLRYIT ISGNRVIDAA KSCSKRDSDR IGKDSVETSA THREVQTKLD 3950
    QVTDRFRSLY SKCSVLGNNL KDLVDQYQQY EDASCGLLSG LQACEAKASK 4000
    HLREPIALDP KNLQRQLEET KALQGQISSQ QVAVEKLKKT AEVLLDAKGS 4050
    LLPAKNDIQK TLDDIVGRYD DLSKCVNERN EKLQITLTRS LSVQDALDEM 4100
    LDWMGSVESS LVKPGQVPLN STALQDLISK DTMLEQDITG RQSSINAMNE 4150
    KVKTFIETTD PSTASSLQAK MKDLSARFSE ASQKHKEKLA KMVELKAKVE 4200
    QFEKLSDKLQ TFLETQSQAL TEVAMPGKDV PELSQHMQES TAKFLEHRKD 4250
    LEALHSLLKE ISSHGLPGDK ALVFEKTNNL SRKFKEMEDT IQEKKDALSS 4300
    CQEQLSAFQT LAQSLKTWIK ETTKQVPVVK PSLGTEDLRK SLEETKKLQE 4350
    KWNLKAPEIH KANNSGVSLC NLLSALISPA KAIAAAKSGG VILNGEGTDT 4400
    NTQDFLANKG LTSIKKDMTD ISHSYEDLGL LLKDKIVELN TKLSKLQKAQ 4450
    EESSAMMQWL EKMNKTASRW RQTPTPADTE SVKLQVEQNK SFEAELKQNV 4500
    NKVQELKDKL SELLEENPEA PEAQSWKQAL AEMDTKWQEL NQLTMDRQQK 4550
    LEESSNNLTQ FQTTEAQLKQ WLMEKELMVS VLGPLSIDPN MLNTQKQQVQ 4600
    ILLQEFDTRK PQYEQLTAAG QGILSRPGED PSLHGIVNEQ LEAVTQKWDN 4650
    LTGQLRDRCD WIDQAIVKST QYQSLLRSLS GTLTELDDKL SSGLTSGALP 4700
    DAVNQQLEAA QRLKQEIEQQ APKIKEAQEV CEDLSALVKE EYLKAELSRQ 4750
    LEGILKSFKD IEQKTENHVQ HLQSACASSH QFQQMSKDFQ AWLDAKKEEQ 4800
    RDSPPISAKL DVLESLLNSQ KDFGKTFTEQ SNIYEKTISE GENLLLKTQG 4850
    AEKAALQLQL NTMKTDWDRF RKQVKEREEK LKDSLEKALK YREQVETLRP 4900
    WIDRCQHSLD GVTFSLDPTE SESSIAELKS LQKEMDHHFG MLELLNNTAN 4950
    SLLSVCEVDK EAVTEENQSL MEKVNRVTEQ LQSKTVSLEN MAQKFKEFQE 5000
    VSRDTQRQLQ DTKEQLEVHH SLGPQAYSNK HLSVLQAQQK SLQTLKQQVD 5050
    EAKRLAQDLV VEAADSKGTS DVLLQAETLA EEHSELSQQV DEKCSFLETK 5100
    LQGLGHFQNT IREMFSQFTE CDDELDGMAP VGRDAETLRK QKACMQTFLK 5150
    KLEALMASND SANRTCKMML ATEETSPDLI GVKRDLEALS KQCNKLLDRA 5200
    KTREEQVDGA TEKLEEFHRK LEEFSTLLQK AEEHEESQGP VGTETETINQ 5250
    QLDVFKVFQK EEIEPLQVKQ QDVNWLGQGL IQSAAANTCT QGLEHDLDSV 5300
    NSRWKTLNKK VAQRTSQLQE ALLHCGRFQD ALESLLSWMA DTEELVANQK 5350
    PPSAEFKVVK AQIQEQKLLQ RLLEDRKSTV EVIKREGEKI AASAEPADRV 5400
    KLTRQLSLLD SRWEALLSRA EARNRQLEGI SVVAQEFHET LEPLNEWLTA 5450
    VEKKLANSEP IGTQAPKLEE QISQHKALQE DILLRKQSVD QALLNGLELL 5500
    KQTTGDEVLI IQDKLEAIKA RYKDITKLSA DVAKTLEHAL QLAGQLQSMH 5550
    KELCNWLDKV EVELLSYETQ GLKGEAASQV QERQKELKNE VRSNKALVDS 5600
    LNEVSSALLE LVPWRAREGL EKTIAEDNER YRLVSDTITQ KVEEIDAAIL 5650
    RSQQFEQAAD AELSWITETQ KKLMSLGDIR LEQDQTSAQL QVQKAFTMDI 5700
    LRHKDIIDEL VTSGHKIMTT SSEEEKQSMK KKLDKVLKKY DAVCQINSER 5750
    HLQLERAQSL VSQFWETYEE LWPWLTETQR IISQLPAPAL EYETLRRQQE 5800
    EHRQLRELIA EHKPHIDKMN KTGPQLLELS PKEGIYIQEK YVAADTLYSQ 5850
    IKEDVKKRAV VLDEAISQST QFHDKIDQIL ESLERIAERL RQPPSISAEV 5900
    EKIKEQIGEN KSVSVDMEKL QPLYETLRQR GEEMIARSEG TEKDVSARAV 5950
    QDKLDQMVFI WGSIHTLVEE REAKLLDVME LAEKFWCDHM SLVVTIKDTQ 6000
    DFIRDLEDPG IDPSVVKQQQ EAAEAIREEI DGLQEELDMV ITLGSELIAA 6050
    CGEPDKPIVK KSIDELNSAW DSLNKAWKDR VDRLEEAMQA AVQYQDGLQG 6100
    IFDWVDIAGN KLATMSPIGT DLETVKQQIE ELKQFKSEAY QQQIEMERLN 6150
    HQAELLLKKV TEEADKHTVQ DPLMELKLIW DSLDERIVSR QHKLEGALLA 6200
    LGQFQHALDE LLAWLTHTKG LLSEQKPVGG DPKAIEIELA KHHVLQNDVL 6250
    AHQSTVEAVN KAGNDLIESS EGEEASNLQY KLRILNQRWQ DILEKTDQRK 6300
    QQLDSALRQA KGFHGEIEDL QQWLTDTERH LLASKPLGGL PETAKEQLNA 6350
    HMEVCTAFAI KEETYKSLML RGQQMLARCP RSAETNIDQD ITNLKEKWES 6400
    VKSKLNEKKT KLEEALHLAM NFHNSLQDFI NWLTQAEQTL NVASRPSLIL 6450
    DTILFQIDEH KVFANEVNSH REQIIELDKT GTHLKYFSQK QDVVLIKNLL 6500
    ISVQSRWEKV VQRLVERGRS LDEARKRAKQ FHEAWSKLME WLEESEKSLD 6550
    SELEIANDPD KIKAQLVQHK EFQKSLGGKH SVYDTTNRTG RSLKEKTSLA 6600
    DDNLKLDNML SELRDKWDTI CGKSVERQNK LEEALLFSGQ FTDALQALID 6650
    WLYRVEPQLA EDQPVHGDID LVMNLIDNHK VFQKELGKRT SSVQALKRSA 6700
    RELIEGSRDD SSWVRVQMQE LSTRWETVCA LSISKQTRLE SALQQAEEFH 6750
    SVVHTLLEWL AEAEQTLRFH GALPDDEDAL RTLIEQHKEF MKRLEEKRAE 6800
    LSKATGMGDA LLAVCHPDSI TTIKHWITII QARFEEVLAW AKQHQQRLAG 6850
    ALAGLIAKQE LLETLLAWLQ WAETTLTEKD KEVIPQEIEE VKTLIAEHQT 6900
    FMEEMTRKQP DVDKVTKTYK RRATDPPSLQ SHIPVLDKGR AGRKRFPASG 6950
    FYPSGSQTQI ETKNPRVNLL VSKWQQVWLL ALERRRKLND ALDRLEELRE 7000
    FANFDFDIWR KKYMRWMNHK KSRVMDFFRR IDKDQDGKIT RQEFIDGILS 7050
    SKFPTSRLEM SAVADIFDRD GDGYIDYYEF VAALHPNKDA YKPITDADKI 7100
    EDEVTRQVAK CKCAKRFQVE QIGDNKYRFF LGNQFGDSQQ LRLVRILRST 7150
    VMVRVGGGWM ALDEFLVKND PCRVHHHGSK MLRSESNSSI TATQPTLAKG 7200
    RTNMELREKF ILADGASQGM AAFRPRGRRS RPSSRGASPN RSTSASSHAC 7250
    QAASPPVPAA ASTPKGTPIQ GSKLRLPGYL SGKGFHSGED SALITTAAAR 7300
    VRTQFAESRK TPSRPGSRAG SKAGSRASSR RGSDASDFDI SEIQSVCSDV 7350
    ETVPQTHRPV PRAGSRPSTA KPSKIPTPQR RSPASKLDKS SKR 7393
    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.

    Show »
    Length:388
    Mass (Da):42,618
    Checksum:i7258EC5F1E2DA4E7
    GO

    Sequence cautioni

    The sequence AAK83382.1 differs from that shown. Reason: Many conflicts and frameshifts that might be strain-specific.
    The sequence AAK83383.1 differs from that shown. Reason: Many conflicts and frameshifts that might be strain-specific.
    The sequence AAK83384.1 differs from that shown. Reason: Many conflicts and frameshifts that might be strain-specific.
    Isoform 6 : The sequence AAC52231.1 differs from that shown. Reason: Frameshift at position 51.

    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:
    EMBL
    GenBank
    DDBJ
    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.
    PIRiA60776.
    I49290.
    I49298.
    UniGeneiMm.336625.
    Mm.478284.
    Mm.487428.

    Genome annotation databases

    UCSCiuc007aof.1. mouse. [Q91ZU6-6]

    Keywords - Coding sequence diversityi

    Alternative promoter usage, Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    PIRi A60776.
    I49290.
    I49298.
    UniGenei Mm.336625.
    Mm.478284.
    Mm.487428.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2IAK X-ray 3.00 A 580-803 [» ]
    ProteinModelPortali Q91ZU6.
    SMRi Q91ZU6. Positions 31-255, 268-479, 583-1051, 1553-1927, 4476-4570, 5208-5532, 6115-6480, 7098-7170.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q91ZU6. 5 interactions.
    MINTi MINT-1861530.
    STRINGi 10090.ENSMUSP00000095392.

    Chemistry

    ChEMBLi CHEMBL2176789.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00230689.
    IPI00230690.
    IPI00284272.

    Proteomic databases

    MaxQBi Q91ZU6.
    PaxDbi Q91ZU6.
    PRIDEi Q91ZU6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    UCSCi uc007aof.1. mouse. [Q91ZU6-6 ]

    Organism-specific databases

    CTDi 667.
    MGIi MGI:104627. Dst.

    Phylogenomic databases

    eggNOGi COG5069.
    HOVERGENi HBG031127.
    OrthoDBi EOG76738T.
    PhylomeDBi Q91ZU6.

    Miscellaneous databases

    ChiTaRSi DST. mouse.
    EvolutionaryTracei Q91ZU6.
    NextBioi 284082.
    PROi Q91ZU6.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi E9PXE5.
    Bgeei E9PXE5.
    CleanExi MM_DST.
    Genevestigatori Q91ZU6.

    Family and domain databases

    Gene3Di 1.10.238.10. 1 hit.
    1.10.418.10. 2 hits.
    3.30.920.20. 1 hit.
    3.90.1290.10. 3 hits.
    InterProi IPR001589. Actinin_actin-bd_CS.
    IPR001715. CH-domain.
    IPR011992. EF-hand-dom_pair.
    IPR018247. EF_Hand_1_Ca_BS.
    IPR002048. EF_hand_dom.
    IPR003108. GAS2_dom.
    IPR001101. Plectin_repeat.
    IPR018159. Spectrin/alpha-actinin.
    IPR002017. Spectrin_repeat.
    [Graphical view ]
    Pfami PF00307. CH. 2 hits.
    PF13499. EF-hand_7. 1 hit.
    PF02187. GAS2. 1 hit.
    PF00681. Plectin. 5 hits.
    PF00435. Spectrin. 18 hits.
    [Graphical view ]
    SMARTi SM00033. CH. 2 hits.
    SM00054. EFh. 2 hits.
    SM00243. GAS2. 1 hit.
    SM00250. PLEC. 9 hits.
    SM00150. SPEC. 32 hits.
    [Graphical view ]
    SUPFAMi SSF143575. SSF143575. 1 hit.
    SSF47576. SSF47576. 1 hit.
    SSF75399. SSF75399. 2 hits.
    PROSITEi PS00019. 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 ]
    ProtoNeti Search...

    Publicationsi

    1. "The BPAG1 locus: alternative splicing produces multiple isoforms with distinct cytoskeletal linker domains, including predominant isoforms in neurons and muscles."
      Leung C.L., Zheng M., Prater S.M., Liem R.K.H.
      J. Cell Biol. 154:691-697(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 5), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, ALTERNATIVE SPLICING.
      Strain: BALB/c.
      Tissue: Epithelium, Muscle and Neuron.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    3. "The mouse dystonia musculorum gene is a neural isoform of bullous pemphigoid antigen 1."
      Brown A., Bernier G., Mathieu M., Rossant J., Kothary R.
      Nat. Genet. 10:301-306(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-511 (ISOFORM 2), PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
      Tissue: Brain.
    4. "A Bpag1 isoform involved in cytoskeletal organization surrounding the nucleus."
      Young K.G., Pinheiro B., Kothary R.
      Exp. Cell Res. 312:121-134(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-304 (ISOFORM 6), ALTERNATIVE SPLICING (ISOFORMS 2 AND 6), SUBCELLULAR LOCATION (ISOFORMS 2 AND 6).
      Strain: C3H.
    5. "Dissecting the sequence specific functions of alternative N-terminal isoforms of mouse bullous pemphigoid antigen 1."
      Jefferson J.J., Leung C.L., Liem R.K.
      Exp. Cell Res. 312:2712-2725(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-270 (ISOFORM 7), ALTERNATIVE SPLICING (ISOFORMS 1; 6 AND 7), FUNCTION OF ISOFORMS 1; 6 AND 7, PALMITOYLATION, MYRISTOYLATION, MUTAGENESIS, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Strain: C57BL/6 X CBA.
    6. "Structural analysis of the plakin domain of bullous pemphigoid antigen1 (BPAG1) suggests that plakins are members of the spectrin superfamily."
      Jefferson J.J., Ciatto C., Shapiro L., Liem R.K.
      J. Mol. Biol. 366:244-257(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 580-584; 1043-1047 AND 1053-1057, X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 580-803.
    7. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 6697-7393 (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 6874-7393 (ISOFORM 4).
      Strain: C57BL/6J.
      Tissue: Fetal skin and Fetal spinal cord.
    8. "The intermediate filament protein peripherin is the specific interaction partner of mouse BPAG1-n (dystonin) in neurons."
      Leung C.L., Sun D., Liem R.K.
      J. Cell Biol. 144:435-446(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), FUNCTION, INTERACTION WITH PRPH.
      Strain: BALB/c.
    9. "Molecular network in NGF-mediated neural differentiation."
      Kubo Y., Ohba M., Iwashita S.
      Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
      Strain: Swiss Webster / NIH.
    10. "Gene targeting of BPAG1: abnormalities in mechanical strength and cell migration in stratified epithelia and neurologic degeneration."
      Guo L., Degenstein L., Dowling J., Yu Q.C., Wollmann R., Perman B., Fuchs E.
      Cell 81:233-243(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING (ISOFORM 5), DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION (ISOFORM 5), TISSUE SPECIFICITY.
    11. "An essential cytoskeletal linker protein connecting actin microfilaments to intermediate filaments."
      Yang Y., Dowling J., Yu Q.C., Kouklis P., Cleveland D.W., Fuchs E.
      Cell 86:655-665(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING (ISOFORMS 5 AND 6), SUBCELLULAR LOCATION (ISOFORMS 5 AND 6), TISSUE SPECIFICITY.
    12. "Integrators of the cytoskeleton that stabilize microtubules."
      Yang Y., Bauer C., Strasser G., Wollman R., Julien J.P., Fuchs E.
      Cell 98:229-238(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE.
    13. "Dystonin-deficient mice exhibit an intrinsic muscle weakness and an instability of skeletal muscle cytoarchitecture."
      Dalpe G., Mathieu M., Comtois A., Zhu E., Wasiak S., De Repentigny Y., Leclerc N., Kothary R.
      Dev. Biol. 210:367-380(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DES, DISRUPTION PHENOTYPE.
    14. "BPAG1n4 is essential for retrograde axonal transport in sensory neurons."
      Liu J.J., Ding J., Kowal A.S., Nardine T., Allen E., Delcroix J.D., Wu C., Mobley W., Fuchs E., Yang Y.
      J. Cell Biol. 163:223-229(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    15. "Bpag1 localization to actin filaments and to the nucleus is regulated by its N-terminus."
      Young K.G., Pool M., Kothary R.
      J. Cell Sci. 116:4543-4555(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING (ISOFORMS 2; 5 AND 6), HOMODIMERIZATION, MUTAGENESIS OF ARG-1385 AND ARG-1386, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    16. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
      Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
      Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain.
    17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    18. "Dystonin/Bpag1 is a necessary endoplasmic reticulum/nuclear envelope protein in sensory neurons."
      Young K.G., Kothary R.
      Exp. Cell Res. 314:2750-2761(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING (ISOFORM 6), INTERACTION WITH SYNE3, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    19. "BPAG1 isoform-b: complex distribution pattern in striated and heart muscle and association with plectin and alpha-actinin."
      Steiner-Champliaud M.F., Schneider Y., Favre B., Paulhe F., Praetzel-Wunder S., Faulkner G., Konieczny P., Raith M., Wiche G., Adebola A., Liem R.K., Langbein L., Sonnenberg A., Fontao L., Borradori L.
      Exp. Cell Res. 316:297-313(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), INTERACTION WITH PLEC, SUBCELLULAR LOCATION (ISOFORMS 1 AND 2), TISSUE SPECIFICITY.
    20. "Hearts of dystonia musculorum mice display normal morphological and histological features but show signs of cardiac stress."
      Boyer J.G., Bhanot K., Kothary R., Boudreau-Lariviere C.
      PLoS ONE 5:E9465-E9465(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING (ISOFORM 2), FUNCTION OF ISOFORM 2, SUBCELLULAR LOCATION (ISOFORM 2), TISSUE SPECIFICITY.

    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: October 1, 2014
    This is version 124 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

    External Data

    Dasty 3