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Q03001

- DYST_HUMAN

UniProt

Q03001 - DYST_HUMAN

Protein

Dystonin

Gene

DST

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 166 (01 Oct 2014)
      Sequence version 4 (20 Apr 2010)
      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.
    Isoform 3: 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.By similarity
    Isoform 7: regulates the organization and stability of the microtubule network of sensory neurons to allow axonal transport.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Calcium bindingi7210 – 7221121PROSITE-ProRule annotationAdd
    BLAST
    Calcium bindingi7246 – 7257122PROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

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

    GO - Biological processi

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

    Keywords - Molecular functioni

    Muscle protein

    Keywords - Biological processi

    Cell adhesion

    Keywords - Ligandi

    Actin-binding, Calcium, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_150180. Assembly of collagen fibrils and other multimeric structures.
    REACT_20537. Type I hemidesmosome assembly.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dystonin
    Alternative name(s):
    230 kDa bullous pemphigoid antigen
    230/240 kDa bullous pemphigoid antigen
    Bullous pemphigoid antigen 1
    Short name:
    BPA
    Short name:
    Bullous pemphigoid antigen
    Dystonia musculorum protein
    Hemidesmosomal plaque protein
    Gene namesi
    Name:DST
    Synonyms:BP230, BP240, BPAG1, DMH, DT, KIAA0728
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:1090. DST.

    Subcellular locationi

    Cytoplasmcytoskeleton 2 Publications
    Note: 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. Associated at the growing distal tip of microtubules.By similarity
    Isoform 1 : Cytoplasmcytoskeleton By similarity. CytoplasmmyofibrilsarcomereZ line. CytoplasmmyofibrilsarcomereH zone By similarity
    Note: Localizes to microtubules and actin microfilaments throughout the cytoplasm and at focal contact attachments at the plasma membrane.By similarity
    Isoform 2 : Cytoplasmcytoskeleton By similarity
    Note: Colocalizes both cortical and cytoplasmic actin filaments.By similarity
    Isoform 3 : Cytoplasmcytoskeleton. Cell junctionhemidesmosome
    Note: Localizes to actin and intermediate filaments cytoskeletons By similarity. Colocalizes with the epidermal KRT5-KRT14 intermediate filaments network of keratins. Colocalizes with ITGB4 at the leading edge of migrating keratinocytes.By similarity
    Isoform 6 : Nucleus By similarity. Nucleus envelope 1 Publication. Membrane 1 Publication; Single-pass membrane protein 1 Publication. Endoplasmic reticulum membrane By similarity; Single-pass membrane protein By similarity. Cytoplasmcytoskeleton 1 Publication
    Note: 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. Associates with actin cytoskeleton in sensory neurons.By similarity
    Isoform 7 : Cytoplasmcytoskeleton 1 Publication. Cell projectionaxon 1 Publication. Membrane 1 Publication
    Note: Associates with axonal microtubules and intermediate filaments, but not with actin cytoskeleton, in sensory neurons.
    Isoform 8 : Cytoplasmcytoskeleton By similarity. Cytoplasmcell cortex By similarity. Cell membrane By similarity; Lipid-anchor By similarity

    GO - Cellular componenti

    1. actin cytoskeleton Source: UniProtKB
    2. axon Source: UniProtKB
    3. basal plasma membrane Source: UniProtKB
    4. basement membrane Source: ProtInc
    5. cell cortex Source: UniProtKB-SubCell
    6. cell leading edge Source: UniProtKB
    7. cytoplasm Source: UniProtKB
    8. cytoplasmic membrane-bounded vesicle Source: MGI
    9. cytosol Source: Reactome
    10. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    11. extracellular vesicular exosome Source: UniProt
    12. hemidesmosome Source: UniProtKB
    13. H zone Source: UniProtKB-SubCell
    14. integral component of membrane Source: UniProtKB-KW
    15. intermediate filament Source: UniProtKB-KW
    16. intermediate filament cytoskeleton Source: UniProtKB
    17. microtubule cytoskeleton Source: HPA
    18. microtubule plus-end Source: UniProtKB
    19. neurofilament cytoskeleton Source: Ensembl
    20. nuclear envelope Source: UniProtKB-SubCell
    21. nucleus Source: UniProt
    22. Z disc Source: UniProtKB

    Keywords - Cellular componenti

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

    Pathology & Biotechi

    Involvement in diseasei

    Neuropathy, hereditary sensory and autonomic, 6 (HSAN6) [MIM:614653]: A form of hereditary sensory and autonomic neuropathy, a genetically and clinically heterogeneous group of disorders characterized by degeneration of dorsal root and autonomic ganglion cells, and by sensory and/or autonomic abnormalities. HSAN6 is a severe autosomal recessive disorder characterized by neonatal hypotonia, respiratory and feeding difficulties, lack of psychomotor development, and autonomic abnormalities including labile cardiovascular function, lack of corneal reflexes leading to corneal scarring, areflexia, and absent axonal flare response after intradermal histamine injection.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Epidermolysis bullosa simplex, autosomal recessive 2 (EBSB2) [MIM:615425]: A form of epidermolysis bullosa, a dermatologic disorder characterized by localized blistering on the dorsal, lateral and plantar surfaces of the feet. EBSB2 is characterized by trauma-induced blistering mainly occurring on the feet and ankles. Ultrastructural analysis of skin biopsy shows abnormal hemidesmosomes with poorly formed inner plaques.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi7548 – 75481K → Q: Loss of interaction with MAPRE1 and association with microtubule growing ends. 1 Publication
    Mutagenesisi7550 – 75501S → A or N: Loss of association with microtubule growing ends. 1 Publication
    Mutagenesisi7552 – 75521I → N: Loss of interaction with MAPRE1 and association with the growing microtubule plus ends; when associated with N-7553. 1 Publication
    Mutagenesisi7553 – 75531P → N: Loss of interaction with MAPRE1 and association with the growing microtubule plus ends; when associated with N-7552. 1 Publication
    Mutagenesisi7557 – 75571R → N: Loss of interaction with MAPRE1 and association with the growing microtubule plus ends.
    Mutagenesisi7558 – 75581K → N: Loss of interaction with MAPRE1 and association with the growing microtubule plus ends.

    Keywords - Diseasei

    Epidermolysis bullosa, Neuropathy

    Organism-specific databases

    MIMi614653. phenotype.
    615425. phenotype.
    Orphaneti89838. Autosomal recessive epidermolysis bullosa simplex.
    314381. Hereditary sensory and autonomic neuropathy type 6.
    PharmGKBiPA25399.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 75707570DystoninPRO_0000078138Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2919 – 29191Phosphoserine1 Publication
    Cross-linki5470 – 5470Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
    Modified residuei7432 – 74321Phosphoserine1 Publication

    Keywords - PTMi

    Isopeptide bond, Lipoprotein, Palmitate, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ03001.
    PaxDbiQ03001.
    PRIDEiQ03001.

    PTM databases

    PhosphoSiteiQ03001.

    Expressioni

    Tissue specificityi

    Isoform 1 is expressed in myoblasts (at protein level). Isoform 3 is expressed in the skin. Isoform 6 is expressed in the brain. Highly expressed in skeletal muscle and cultured keratinocytes.3 Publications

    Gene expression databases

    ArrayExpressiQ03001.
    BgeeiQ03001.
    CleanExiHS_DST.
    GenevestigatoriQ03001.

    Organism-specific databases

    HPAiHPA030200.

    Interactioni

    Subunit structurei

    Homodimer. Isoform 1 interacts (via N-terminus) with PLEC (via N-terminus). Interacts with the neuronal intermediate filament protein, PRPH. Interacts with DES. Interacts with SYNE3 By similarity. Isoform 1 and isoform 6 can homodimerize (via N-terminus). Isoform 1 interacts (via N-terminus) with ACTN2. Isoform 1 interacts (via N-terminus) with PLEC (via N-terminus). Isoform 3 interacts (via N-terminus) with COL17A1 (via cytoplasmic region). Isoform 3 interacts (via N-terminus) with ITGB4 isoform beta-4a (via cytoplasmic region). Isoform 3 interacts (via N-terminus) with ERBB2IP (via C-terminus). Isoform 3 associates (via C-terminal) with KRT5-KRT14 (via rod region) intermadiate filaments of keratins. Interacts with MAPRE1; probably required for targeting to the growing microtubule plus ends. Interacts with TMIGD2.By similarity6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    P299914EBI-310758,EBI-8826488From a different organism.
    APPL1Q9UKG13EBI-310758,EBI-741243
    DISC1Q9NRI55EBI-310758,EBI-529989
    MAPRE1Q156912EBI-310758,EBI-1004115
    Mapre1Q611663EBI-310758,EBI-2027055From a different organism.
    OPTNQ96CV92EBI-310758,EBI-748974

    Protein-protein interaction databases

    BioGridi107135. 36 interactions.
    DIPiDIP-33131N.
    IntActiQ03001. 34 interactions.
    MINTiMINT-119936.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3GJOX-ray2.50E/F/G/H7541-7570[»]
    ProteinModelPortaliQ03001.
    SMRiQ03001. Positions 31-255, 583-795.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ03001.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini35 – 252218Actin-bindingAdd
    BLAST
    Domaini35 – 138104CH 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini151 – 252102CH 2PROSITE-ProRule annotationAdd
    BLAST
    Repeati701 – 79797Spectrin 1Add
    BLAST
    Domaini890 – 94253SH3Add
    BLAST
    Repeati1584 – 162643Plectin 1Add
    BLAST
    Repeati1660 – 170344Plectin 2Add
    BLAST
    Repeati1774 – 181744Plectin 3Add
    BLAST
    Repeati1818 – 185538Plectin 4Add
    BLAST
    Repeati1856 – 189136Plectin 5Add
    BLAST
    Repeati3924 – 400077Spectrin 2Add
    BLAST
    Repeati4069 – 415385Spectrin 3Add
    BLAST
    Repeati4514 – 4622109Spectrin 4Add
    BLAST
    Repeati4626 – 4731106Spectrin 5Add
    BLAST
    Repeati4849 – 4952104Spectrin 6Add
    BLAST
    Repeati5281 – 5389109Spectrin 7Add
    BLAST
    Repeati5396 – 5497102Spectrin 8Add
    BLAST
    Repeati5504 – 5606103Spectrin 9Add
    BLAST
    Repeati5829 – 5933105Spectrin 10Add
    BLAST
    Repeati5940 – 6042103Spectrin 11Add
    BLAST
    Repeati6048 – 6154107Spectrin 12Add
    BLAST
    Repeati6184 – 626481Spectrin 13Add
    BLAST
    Repeati6270 – 6373104Spectrin 14Add
    BLAST
    Repeati6379 – 6481103Spectrin 15Add
    BLAST
    Repeati6490 – 6592103Spectrin 16Add
    BLAST
    Repeati6597 – 6700104Spectrin 17Add
    BLAST
    Repeati6705 – 6811107Spectrin 18Add
    BLAST
    Repeati6818 – 6918101Spectrin 19Add
    BLAST
    Repeati6923 – 7026104Spectrin 20Add
    BLAST
    Domaini7197 – 723236EF-hand 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini7233 – 726836EF-hand 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini7273 – 735179GARPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi1383 – 13897Nuclear localization signal; in isoform 6By similarity
    Motifi7550 – 75534Microtubule tip localization signal

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi2394 – 243138Asp-richAdd
    BLAST
    Compositional biasi2592 – 25998Poly-Asp

    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.

    Sequence similaritiesi

    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 20 spectrin repeats.Curated

    Keywords - Domaini

    Coiled coil, Repeat, SH3 domain, Transmembrane

    Phylogenomic databases

    eggNOGiCOG5069.
    HOVERGENiHBG031127.
    InParanoidiQ8WXK8.
    KOiK10382.
    OMAiRKITEIQ.
    PhylomeDBiQ03001.
    TreeFamiTF335163.

    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. 2 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. 19 hits.
    [Graphical view]
    SMARTiSM00033. CH. 2 hits.
    SM00054. EFh. 2 hits.
    SM00243. GAS2. 1 hit.
    SM00250. PLEC. 8 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 (8)i

    Sequence statusi: Complete.

    This entry describes 8 isoformsi produced by alternative promoter usage and alternative splicing. Align

    Isoform 1 (identifier: Q03001-7) [UniParc]FASTAAdd to Basket

    Also known as: BPAG1-b

    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.

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    MAGYLSPAAY LYVEEQEYLQ AYEDVLERYK DERDKVQKKT FTKWINQHLM     50
    KVRKHVNDLY EDLRDGHNLI SLLEVLSGDT LPREKGRMRF HRLQNVQIAL 100
    DYLKRRQVKL VNIRNDDITD GNPKLTLGLI WTIILHFQIS DIHVTGESED 150
    MSAKERLLLW TQQATEGYAG IRCENFTTCW RDGKLFNAII HKYRPDLIDM 200
    NTVAVQSNLA NLEHAFYVAE KIGVIRLLDP EDVDVSSPDE KSVITYVSSL 250
    YDAFPKVPEG GEGIGANDVE VKWIEYQNMV NYLIQWIRHH VTTMSERTFP 300
    NNPVELKALY NQYLQFKETE IPPKETEKSK IKRLYKLLEI WIEFGRIKLL 350
    QGYHPNDIEK EWGKLIIAML EREKALRPEV ERLEMLQQIA NRVQRDSVIC 400
    EDKLILAGNA LQSDSKRLES GVQFQNEAEI AGYILECENL LRQHVIDVQI 450
    LIDGKYYQAD QLVQRVAKLR DEIMALRNEC SSVYSKGRIL TTEQTKLMIS 500
    GITQSLNSGF AQTLHPSLTS GLTQSLTPSL TSSSMTSGLS SGMTSRLTPS 550
    VTPAYTPGFP SGLVPNFSSG VEPNSLQTLK LMQIRKPLLK SSLLDQNLTE 600
    EEINMKFVQD LLNWVDEMQV QLDRTEWGSD LPSVESHLEN HKNVHRAIEE 650
    FESSLKEAKI SEIQMTAPLK LTYAEKLHRL ESQYAKLLNT SRNQERHLDT 700
    LHNFVSRATN ELIWLNEKEE EEVAYDWSER NTNIARKKDY HAELMRELDQ 750
    KEENIKSVQE IAEQLLLENH PARLTIEAYR AAMQTQWSWI LQLCQCVEQH 800
    IKENTAYFEF FNDAKEATDY LRNLKDAIQR KYSCDRSSSI HKLEDLVQES 850
    MEEKEELLQY KSTIANLMGK AKTIIQLKPR NSDCPLKTSI PIKAICDYRQ 900
    IEITIYKDDE CVLANNSHRA KWKVISPTGN EAMVPSVCFT VPPPNKEAVD 950
    LANRIEQQYQ NVLTLWHESH INMKSVVSWH YLINEIDRIR ASNVASIKTM 1000
    LPGEHQQVLS NLQSRFEDFL EDSQESQVFS GSDITQLEKE VNVCKQYYQE 1050
    LLKSAEREEQ EESVYNLYIS EVRNIRLRLE NCEDRLIRQI RTPLERDDLH 1100
    ESVFRITEQE KLKKELERLK DDLGTITNKC EEFFSQAAAS SSVPTLRSEL 1150
    NVVLQNMNQV YSMSSTYIDK LKTVNLVLKN TQAAEALVKL YETKLCEEEA 1200
    VIADKNNIEN LISTLKQWRS EVDEKRQVFH ALEDELQKAK AISDEMFKTY 1250
    KERDLDFDWH KEKADQLVER WQNVHVQIDN RLRDLEGIGK SLKYYRDTYH 1300
    PLDDWIQQVE TTQRKIQENQ PENSKTLATQ LNQQKMLVSE IEMKQSKMDE 1350
    CQKYAEQYSA TVKDYELQTM TYRAMVDSQQ KSPVKRRRMQ SSADLIIQEF 1400
    MDLRTRYTAL VTLMTQYIKF AGDSLKRLEE EEKSLEEEKK EHVEKAKELQ 1450
    KWVSNISKTL KDAEKAGKPP FSKQKISSEE ISTKKEQLSE ALQTIQLFLA 1500
    KHGDKMTDEE RNELEKQVKT LQESYNLLFS ESLKQLQESQ TSGDVKVEEK 1550
    LDKVIAGTID QTTGEVLSVF QAVLRGLIDY DTGIRLLETQ LMISGLISPE 1600
    LRKCFDLKDA KSHGLIDEQI LCQLKELSKA KEIISAASPT TIPVLDALAQ 1650
    SMITESMAIK VLEILLSTGS LVIPATGEQL TLQKAFQQNL VSSALFSKVL 1700
    ERQNMCKDLI DPCTSEKVSL IDMVQRSTLQ ENTGMWLLPV RPQEGGRITL 1750
    KCGRNISILR AAHEGLIDRE TMFRLLSAQL LSGGLINSNS GQRMTVEEAV 1800
    REGVIDRDTA SSILTYQVQT GGIIQSNPAK RLTVDEAVQC DLITSSSALL 1850
    VLEAQRGYVG LIWPHSGEIF PTSSSLQQEL ITNELAYKIL NGRQKIAALY 1900
    IPESSQVIGL DAAKQLGIID NNTASILKNI TLPDKMPDLG DLEACKNARR 1950
    WLSFCKFQPS TVHDYRQEED VFDGEEPVTT QTSEETKKLF LSYLMINSYM 2000
    DANTGQRLLL YDGDLDEAVG MLLEGCHAEF DGNTAIKECL DVLSSSGVFL 2050
    NNASGREKDE CTATPSSFNK CHCGEPEHEE TPENRKCAID EEFNEMRNTV 2100
    INSEFSQSGK LASTISIDPK VNSSPSVCVP SLISYLTQTE LADISMLRSD 2150
    SENILTNYEN QSRVETNERA NECSHSKNIQ NFPSDLIENP IMKSKMSKFC 2200
    GVNETENEDN TNRDSPIFDY SPRLSALLSH DKLMHSQGSF NDTHTPESNG 2250
    NKCEAPALSF SDKTMLSGQR IGEKFQDQFL GIAAINISLP GEQYGQKSLN 2300
    MISSNPQVQY HNDKYISNTS GEDEKTHPGF QQMPEDKEDE SEIEEYSCAV 2350
    TPGGDTDNAI VSLTCATPLL DETISASDYE TSLLNDQQNN TGTDTDSDDD 2400
    FYDTPLFEDD DHDSLLLDGD DRDCLHPEDY DTLQEENDET ASPADVFYDV 2450
    SKENENSMVP QGAPVGSLSV KNKAHCLQDF LMDVEKDELD SGEKIHLNPV 2500
    GSDKVNGQSL ETGSERECTN ILEGDESDSL TDYDIVGGKE SFTASLKFDD 2550
    SGSWRGRKEE YVTGQEFHSD TDHLDSMQSE ESYGDYIYDS NDQDDDDDDG 2600
    IDEEGGGIRD ENGKPRCQNV AEDMDIQLCA SILNENSDEN ENINTMILLD 2650
    KMHSCSSLEK QQRVNVVQLA SPSENNLVTE KSNLPEYTTE IAGKSKENLL 2700
    NHEMVLKDVL PPIIKDTESE KTFGPASISH DNNNISSTSE LGTDLANTKV 2750
    KLIQGSELPE LTDSVKGKDE YFKNMTPKVD SSLDHIICTE PDLIGKPAEE 2800
    SHLSLIASVT DKDPQGNGSD LIKGRDGKSD ILIEDETSIQ KMYLGEGEVL 2850
    VEGLVEEENR HLKLLPGKNT RDSFKLINSQ FPFPQITNNE ELNQKGSLKK 2900
    ATVTLKDEPN NLQIIVSKSP VQFENLEEIF DTSVSKEISD DITSDITSWE 2950
    GNTHFEESFT DGPEKELDLF TYLKHCAKNI KAKDVAKPNE DVPSHVLITA 3000
    PPMKEHLQLG VNNTKEKSTS TQKDSPLNDM IQSNDLCSKE SISGGGTEIS 3050
    QFTPESIEAT LSILSRKHVE DVGKNDFLQS ERCANGLGND NSSNTLNTDY 3100
    SFLEINNKKE RIEQQLPKEQ ALSPRSQEKE VQIPELSQVF VEDVKDILKS 3150
    RLKEGHMNPQ EVEEPSACAD TKILIQNLIK RITTSQLVNE ASTVPSDSQM 3200
    SDSSGVSPMT NSSELKPESR DDPFCIGNLK SELLLNILKQ DQHSQKITGV 3250
    FELMRELTHM EYDLEKRGIT SKVLPLQLEN IFYKLLADGY SEKIEHVGDF 3300
    NQKACSTSEM MEEKPHILGD IKSKEGNYYS PNLETVKEIG LESSTVWAST 3350
    LPRDEKLKDL CNDFPSHLEC TSGSKEMASG DSSTEQFSSE LQQCLQHTEK 3400
    MHEYLTLLQD MKPPLDNQES LDNNLEALKN QLRQLETFEL GLAPIAVILR 3450
    KDMKLAEEFL KSLPSDFPRG HVEELSISHQ SLKTAFSSLS NVSSERTKQI 3500
    MLAIDSEMSK LAVSHEEFLH KLKSFSDWVS EKSKSVKDIE IVNVQDSEYV 3550
    KKRLEFLKNV LKDLGHTKMQ LETTAFDVQF FISEYAQDLS PNQSKQLLRL 3600
    LNTTQKCFLD VQESVTTQVE RLETQLHLEQ DLDDQKIVAE RQQEYKEKLQ 3650
    GICDLLTQTE NRLIGHQEAF MIGDGTVELK KYQSKQEELQ KDMQGSAQAL 3700
    AEVVKNTENF LKENGEKLSQ EDKALIEQKL NEAKIKCEQL NLKAEQSKKE 3750
    LDKVVTTAIK EETEKVAAVK QLEESKTKIE NLLDWLSNVD KDSERAGTKH 3800
    KQVIEQNGTH FQEGDGKSAI GEEDEVNGNL LETDVDGQVG TTQENLNQQY 3850
    QKVKAQHEKI ISQHQAVIIA TQSAQVLLEK QGQYLSPEEK EKLQKNMKEL 3900
    KVHYETALAE SEKKMKLTHS LQEELEKFDA DYTEFEHWLQ QSEQELENLE 3950
    AGADDINGLM TKLKRQKSFS EDVISHKGDL RYITISGNRV LEAAKSCSKR 4000
    DGGKVDTSAT HREVQRKLDH ATDRFRSLYS KCNVLGNNLK DLVDKYQHYE 4050
    DASCGLLAGL QACEATASKH LSEPIAVDPK NLQRQLEETK ALQGQISSQQ 4100
    VAVEKLKKTA EVLLDARGSL LPAKNDIQKT LDDIVGRYED LSKSVNERNE 4150
    KLQITLTRSL SVQDGLDEML DWMGNVESSL KEQGQVPLNS TALQDIISKN 4200
    IMLEQDIAGR QSSINAMNEK VKKFMETTDP STASSLQAKM KDLSARFSEA 4250
    SHKHKETLAK MEELKTKVEL FENLSEKLQT FLETKTQALT EVDVPGKDVT 4300
    ELSQYMQEST SEFLEHKKHL EVLHSLLKEI SSHGLPSDKA LVLEKTNNLS 4350
    KKFKEMEDTI KEKKEAVTSC QEQLDAFQVL VKSLKSWIKE TTKKVPIVQP 4400
    SFGAEDLGKS LEDTKKLQEK WSLKTPEIQK VNNSGISLCN LISAVTTPAK 4450
    AIAAVKSGGA VLNGEGTATN TEEFWANKGL TSIKKDMTDI SHGYEDLGLL 4500
    LKDKIAELNT KLSKLQKAQE ESSAMMQWLQ KMNKTATKWQ QTPAPTDTEA 4550
    VKTQVEQNKS FEAELKQNVN KVQELKDKLT ELLEENPDTP EAPRWKQMLT 4600
    EIDSKWQELN QLTIDRQQKL EESSNNLTQF QTVEAQLKQW LVEKELMVSV 4650
    LGPLSIDPNM LNTQRQQVQI LLQEFATRKP QYEQLTAAGQ GILSRPGEDP 4700
    SLRGIVKEQL AAVTQKWDSL TGQLSDRCDW IDQAIVKSTQ YQSLLRSLSD 4750
    KLSDLDNKLS SSLAVSTHPD AMNQQLETAQ KMKQEIQQEK KQIKVAQALC 4800
    EDLSALVKEE YLKAELSRQL EGILKSFKDV EQKAENHVQH LQSACASSHQ 4850
    FQQMSRDFQA WLDTKKEEQN KSHPISAKLD VLESLIKDHK DFSKTLTAQS 4900
    HMYEKTIAEG ENLLLKTQGS EKAALQLQLN TIKTNWDTFN KQVKERENKL 4950
    KESLEKALKY KEQVETLWPW IDKCQNNLEE IKFCLDPAEG ENSIAKLKSL 5000
    QKEMDQHFGM VELLNNTANS LLSVCEIDKE VVTDENKSLI QKVDMVTEQL 5050
    HSKKFCLENM TQKFKEFQEV SKESKRQLQC AKEQLDIHDS LGSQAYSNKY 5100
    LTMLQTQQKS LQALKHQVDL AKRLAQDLVV EASDSKGTSD VLLQVETIAQ 5150
    EHSTLSQQVD EKCSFLETKL QGIGHFQNTI REMFSQFAEF DDELDSMAPV 5200
    GRDAETLQKQ KETIKAFLKK LEALMASNDN ANKTCKMMLA TEETSPDLVG 5250
    IKRDLEALSK QCNKLLDRAQ AREEQVEGTI KRLEEFYSKL KEFSILLQKA 5300
    EEHEESQGPV GMETETINQQ LNMFKVFQKE EIEPLQGKQQ DVNWLGQGLI 5350
    QSAAKSTSTQ GLEHDLDDVN ARWKTLNKKV AQRAAQLQEA LLHCGRFQDA 5400
    LESLLSWMVD TEELVANQKP PSAEFKVVKA QIQEQKLLQR LLDDRKSTVE 5450
    VIKREGEKIA TTAEPADKVK ILKQLSLLDS RWEALLNKAE TRNRQLEGIS 5500
    VVAQQFHETL EPLNEWLTTI EKRLVNCEPI GTQASKLEEQ IAQHKALEDD 5550
    IINHNKHLHQ AVSIGQSLKV LSSREDKDMV QSKLDFSQVW YIEIQEKSHS 5600
    RSELLQQALC NAKIFGEDEV ELMNWLNEVH DKLSKLSVQD YSTEGLWKQQ 5650
    SELRVLQEDI LLRKQNVDQA LLNGLELLKQ TTGDEVLIIQ DKLEAIKARY 5700
    KDITKLSTDV AKTLEQALQL ARRLHSTHEE LCTWLDKVEV ELLSYETQVL 5750
    KGEEASQAQM RPKELKKEAK NNKALLDSLN EVSSALLELV PWRAREGLEK 5800
    MVAEDNERYR LVSDTITQKV EEIDAAILRS QQFDQAADAE LSWITETEKK 5850
    LMSLGDIRLE QDQTSAQLQV QKTFTMEILR HKDIIDDLVK SGHKIMTACS 5900
    EEEKQSMKKK LDKVLKNYDT ICQINSERYL QLERAQSLVN QFWETYEELW 5950
    PWLTETQSII SQLPAPALEY ETLRQQQEEH RQLRELIAEH KPHIDKMNKT 6000
    GPQLLELSPG EGFSIQEKYV AADTLYSQIK EDVKKRAVAL DEAISQSTQF 6050
    HDKIDQILES LERIVERLRQ PPSISAEVEK IKEQISENKN VSVDMEKLQP 6100
    LYETLKQRGE EMIARSGGTD KDISAKAVQD KLDQMVFIWE NIHTLVEERE 6150
    AKLLDVMELA EKFWCDHMSL IVTIKDTQDF IRDLEDPGID PSVVKQQQEA 6200
    AETIREEIDG LQEELDIVIN LGSELIAACG EPDKPIVKKS IDELNSAWDS 6250
    LNKAWKDRID KLEEAMQAAV QYQDGLQAVF DWVDIAGGKL ASMSPIGTDL 6300
    ETVKQQIEEL KQFKSEAYQQ QIEMERLNHQ AELLLKKVTE ESDKHTVQDP 6350
    LMELKLIWDS LEERIINRQH KLEGALLALG QFQHALDELL AWLTHTEGLL 6400
    SEQKPVGGDP KAIEIELAKH HVLQNDVLAH QSTVEAVNKA GNDLIESSAG 6450
    EEASNLQNKL EVLNQRWQNV LEKTEQRKQQ LDGALRQAKG FHGEIEDLQQ 6500
    WLTDTERHLL ASKPLGGLPE TAKEQLNVHM EVCAAFEAKE ETYKSLMQKG 6550
    QQMLARCPKS AETNIDQDIN NLKEKWESVE TKLNERKTKL EEALNLAMEF 6600
    HNSLQDFINW LTQAEQTLNV ASRPSLILDT VLFQIDEHKV FANEVNSHRE 6650
    QIIELDKTGT HLKYFSQKQD VVLIKNLLIS VQSRWEKVVQ RLVERGRSLD 6700
    DARKRAKQFH EAWSKLMEWL EESEKSLDSE LEIANDPDKI KTQLAQHKEF 6750
    QKSLGAKHSV YDTTNRTGRS LKEKTSLADD NLKLDDMLSE LRDKWDTICG 6800
    KSVERQNKLE EALLFSGQFT DALQALIDWL YRVEPQLAED QPVHGDIDLV 6850
    MNLIDNHKAF QKELGKRTSS VQALKRSARE LIEGSRDDSS WVKVQMQELS 6900
    TRWETVCALS ISKQTRLEAA LRQAEEFHSV VHALLEWLAE AEQTLRFHGV 6950
    LPDDEDALRT LIDQHKEFMK KLEEKRAELN KATTMGDTVL AICHPDSITT 7000
    IKHWITIIRA RFEEVLAWAK QHQQRLASAL AGLIAKQELL EALLAWLQWA 7050
    ETTLTDKDKE VIPQEIEEVK ALIAEHQTFM EEMTRKQPDV DKVTKTYKRR 7100
    AADPSSLQSH IPVLDKGRAG RKRFPASSLY PSGSQTQIET KNPRVNLLVS 7150
    KWQQVWLLAL ERRRKLNDAL DRLEELREFA NFDFDIWRKK YMRWMNHKKS 7200
    RVMDFFRRID KDQDGKITRQ EFIDGILSSK FPTSRLEMSA VADIFDRDGD 7250
    GYIDYYEFVA ALHPNKDAYK PITDADKIED EVTRQVAKCK CAKRFQVEQI 7300
    GDNKYRFFLG NQFGDSQQLR LVRILRSTVM VRVGGGWMAL DEFLVKNDPC 7350
    RVHHHGSKML RSESNSSITT TQPTIAKGRT NMELREKFIL ADGASQGMAA 7400
    FRPRGRRSRP SSRGASPNRS TSVSSQAAQA ASPQVPATTT PKGTPIQGSK 7450
    LRLPGYLSGK GFHSGEDSGL ITTAAARVRT QFADSKKTPS RPGSRAGSKA 7500
    GSRASSRRGS DASDFDISEI QSVCSDVETV PQTHRPTPRA GSRPSTAKPS 7550
    KIPTPQRKSP ASKLDKSSKR 7570

    Note: No experimental confirmation available. Derived from EST data.

    Length:7,570
    Mass (Da):860,662
    Last modified:April 20, 2010 - v4
    Checksum:i1EA992E53D1C243E
    GO
    Isoform 2 (identifier: Q03001-8) [UniParc]FASTAAdd to Basket

    Also known as: BPAG1-a, BPAG1eA, Dystonin-1, eA

    The sequence of this isoform differs from the canonical sequence as follows:
         1-381: MAGYLSPAAY...REKALRPEVE → MHSSSYSYRS...SFGSESFDGH
         1550-3635: Missing.
         7352-7375: Missing.
         7442-7442: K → KILHPLTRNYGKPWLTNSKMSTPCKAAECSDFPVPSAE

    Show »
    Length:5,171
    Mass (Da):591,036
    Checksum:iEF1B5C94E21ED130
    GO
    Isoform 3 (identifier: Q03001-3) [UniParc]FASTAAdd to Basket

    Also known as: BPAG1e, eBPAG1

    The sequence of this isoform differs from the canonical sequence as follows:
         1-381: MAGYLSPAAY...REKALRPEVE → MHSSSYSYRS...SFGSESFDGH
         1433-1433: K → IKRCKETSEH...TGISSLYYSS
         1434-7570: Missing.

    Note: Contains a phosphoserine at position 1565.By similarityCurated

    Show »
    Length:2,649
    Mass (Da):306,755
    Checksum:i5D0C62D26120E069
    GO
    Isoform 4 (identifier: Q03001-9) [UniParc]FASTAAdd to Basket

    Also known as: BPAG1eA, eB

    The sequence of this isoform differs from the canonical sequence as follows:
         1-381: MAGYLSPAAY...REKALRPEVE → MHSSSYSYRS...SFGSESFDGH
         3387-7570: Missing.

    Note: Incomplete sequence.

    Show »
    Length:3,060
    Mass (Da):345,032
    Checksum:i71C7175B93F7E1EC
    GO
    Isoform 5 (identifier: Q03001-10) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-3753: Missing.
         4184-4200: GQVPLNSTALQDIISKN → DVGTGYCRSSEQYKCHE
         4201-7570: Missing.

    Note: Incomplete sequence. No experimental confirmation available. Note=May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

    Show »
    Length:447
    Mass (Da):50,373
    Checksum:iD462C85D9FA1C903
    GO
    Isoform 6 (identifier: Q03001-11) [UniParc]FASTAAdd to Basket

    Also known as: BPAG1n1, BPAG1n2, Dystonin-2

    The sequence of this isoform differs from the canonical sequence as follows:
         1-30: MAGYLSPAAYLYVEEQEYLQAYEDVLERYK → MIAAAFLVLL...PAERAVLRIA
         47-7570: Missing.

    Note: Incomplete sequence. Transmembrane protein (helical transmembrane domain from amino acid 18 to 38).Curated

    Show »
    Length:224
    Mass (Da):25,379
    Checksum:i9AD0D616AC22B94E
    GO
    Isoform 7 (identifier: Q03001-12) [UniParc]FASTAAdd to Basket

    Also known as: BPAG1n3

    The sequence of this isoform differs from the canonical sequence as follows:
         1-138: MAGYLSPAAY...LIWTIILHFQ → MQHSIFSLKKKRCHSLYTSMSSVSKDTDGNE
         189-7570: Missing.

    Note: Incomplete sequence.

    Show »
    Length:81
    Mass (Da):9,221
    Checksum:i8C50813157B4E7D3
    GO
    Isoform 8 (identifier: Q03001-13) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-138: MAGYLSPAAY...LIWTIILHFQ → MGNVCGCVRA...SVSKDTDGNE
         778-789: AYRAAMQTQWSW → VKLESVMVLVEY
         790-7570: Missing.

    Note: Probably myristoylated on Gly-2. Probably S-palmitoylated on Cys-5 and Cys-7.By similarity

    Show »
    Length:905
    Mass (Da):102,868
    Checksum:iAB344F0B597C1961
    GO

    Sequence cautioni

    The sequence AAA35538.1 differs from that shown. Reason: Contaminating sequence. Sequence of unknown origin in the C-terminal part.
    Isoform 6 : The sequence AAC50244.1 differs from that shown. Reason: Frameshift at position 51.
    The sequence BAB70870.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAC04449.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAC04848.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence AAA57185.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence CAI14341.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence CAI14989.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence CAI16609.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence CAI16610.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence CAI20330.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence CAI20332.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence CAI22044.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence CAI22045.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti573 – 5731P → A in BAH12207. (PubMed:14702039)Curated
    Sequence conflicti1177 – 11771V → G in M69225. (PubMed:1717441)Curated
    Sequence conflicti1177 – 11771V → G in AAL62061. (PubMed:11751855)Curated
    Sequence conflicti1177 – 11771V → G in AAL62062. (PubMed:11751855)Curated
    Sequence conflicti1363 – 13631K → E in AAL62061. (PubMed:11751855)Curated
    Sequence conflicti4703 – 47031R → H in BAC04449. (PubMed:14702039)Curated
    Sequence conflicti4935 – 49351N → S in BAC04449. (PubMed:14702039)Curated
    Sequence conflicti5030 – 50301E → G in AAL62061. (PubMed:11751855)Curated
    Sequence conflicti5177 – 51771Q → R in AAL62061. (PubMed:11751855)Curated
    Sequence conflicti5225 – 52251M → I in BAB70870. (PubMed:14702039)Curated
    Sequence conflicti5299 – 52991K → R in AAL62061. (PubMed:11751855)Curated
    Sequence conflicti5823 – 58231I → V in AAL62061. (PubMed:11751855)Curated
    Sequence conflicti5882 – 58821K → R in AAL62061. (PubMed:11751855)Curated
    Sequence conflicti5986 – 59861L → S in AAL62061. (PubMed:11751855)Curated
    Sequence conflicti6080 – 60801K → E in BAC04848. (PubMed:14702039)Curated
    Sequence conflicti6186 – 61861D → G in AAL62061. (PubMed:11751855)Curated
    Sequence conflicti6440 – 64401A → G in AAL62061. (PubMed:11751855)Curated
    Isoform 6 (identifier: Q03001-11)
    Sequence conflicti48 – 481P → L in AAC50244. (PubMed:8575775)Curated
    Isoform 3 (identifier: Q03001-3)
    Sequence conflicti1644 – 16441R → T in M69225. (PubMed:1717441)By similarityCurated
    Sequence conflicti1943 – 19431G → R in CAA41528. (PubMed:2461961)By similarityCurated
    Sequence conflicti2364 – 23641S → T in M69225. (PubMed:1717441)By similarityCurated
    Sequence conflicti2495 – 24951G → V in M69225. (PubMed:1717441)By similarityCurated
    Sequence conflicti2543 – 25431N → K in M69225. (PubMed:1717441)By similarityCurated
    Sequence conflicti2621 – 26211A → P in M69225. (PubMed:1717441)By similarityCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti1319 – 13191N → K.
    Corresponds to variant rs35014998 [ dbSNP | Ensembl ].
    VAR_063045
    Natural varianti2332 – 23321Q → R.
    Corresponds to variant rs16888053 [ dbSNP | Ensembl ].
    VAR_063046
    Natural varianti3720 – 37201Q → R.
    Corresponds to variant rs4712138 [ dbSNP | Ensembl ].
    VAR_063047
    Natural varianti5138 – 51381T → A.1 Publication
    Corresponds to variant rs4715631 [ dbSNP | Ensembl ].
    VAR_063048

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 37533753Missing in isoform 5. 1 PublicationVSP_041524Add
    BLAST
    Alternative sequencei1 – 381381MAGYL…RPEVE → MHSSSYSYRSSDSVFSNTTS TRTSLDSNENLLLVHCGPTL INSCISFGSESFDGH in isoform 2, isoform 3 and isoform 4. 5 PublicationsVSP_041525Add
    BLAST
    Alternative sequencei1 – 138138MAGYL…ILHFQ → MQHSIFSLKKKRCHSLYTSM SSVSKDTDGNE in isoform 7. 1 PublicationVSP_041526Add
    BLAST
    Alternative sequencei1 – 138138MAGYL…ILHFQ → MGNVCGCVRAEKEEQYVDPA KTPLNPEKYSPGRKYFRRKP IKKTGGDKESVGANNENEGK KKSSSQPSKEQPAPLSRGLV QQESVTLNSALGDGIQQKKT EVVADSVKQKLLPSAVSSWS DCVNTSPAKDSETEVKVSEL DERISEKDSTPYCAKRKKHL DDVNTSEITFQEKTDVFSFR KAASLSSIPSGIERSLEKGG FPEDPPKSYSSIQEKQNTER FCPHATQHFQFKKKRCHSLY TSMSSVSKDTDGNE in isoform 8. 1 PublicationVSP_041527Add
    BLAST
    Alternative sequencei1 – 3030MAGYL…LERYK → MIAAAFLVLLRPYSIQCALF LLLLLLGTIATIVFFCCWHR KLQKGRHPMKSVFSGRSRSR DAVLRSHHFRSEGFRASPRH LRRRVAAAAAARLEEVKPVV EVHHQSEQETSVRKRRIKKS SRVQPEFYHSVQGASIRRPS SGNASYRCSMSSSADFSDED DFSQKSGSASPAPGDTLPWN LPKHERSKRKIQGGSVLDPA ERAVLRIA in isoform 6. 1 PublicationVSP_041528Add
    BLAST
    Alternative sequencei47 – 75707524Missing in isoform 6. 1 PublicationVSP_041529Add
    BLAST
    Alternative sequencei189 – 75707382Missing in isoform 7. 1 PublicationVSP_041530Add
    BLAST
    Alternative sequencei778 – 78912AYRAA…TQWSW → VKLESVMVLVEY in isoform 8. 1 PublicationVSP_041531Add
    BLAST
    Alternative sequencei790 – 75706781Missing in isoform 8. 1 PublicationVSP_041532Add
    BLAST
    Alternative sequencei1433 – 14331K → IKRCKETSEHGAYSDLLQRQ KATVLENSKLTGKISELERM VAELKKQKSRVEEELPKVRE AAENELRKQQRNVEDISLQK IRAESEAKQYRRELETIVRE KEAAERELERVRQLTIEAEA KRAAVEENLLNFRNQLEENT FTRRTLEDHLKRKDLSLNDL EQQKNKLMEELRRKRDNEEE LLKLIKQMEKDLAFQKQVAE KQLKEKQKIELEARRKITEI QYTCRENALPVCPITQATSC RAVTGLQQEHDKQKAEELKQ QVDELTAANRKAEQDMRELT YELNALQLEKTSSEEKARLL KDKLDETNNTLRCLKLELER KDQAEKGYSQQLRELGRQLN QTTGKAEEAMQEASDLKKIK RNYQLELESLNHEKGKLQRE VDRITRAHAVAEKNIQHLNS QIHSFRDEKELERLQICQRK SDHLKEQFEKSHEQLLQNIK AEKENNDKIQRLNEELEKSN ECAEMLKQKVEELTRQNNET KLMMQRIQAESENIVLEKQT IQQRCEALKIQADGFKDQLR STNEHLHKQTKTEQDFQRKI KCLEEDLAKSQNLVSEFKQK CDQQNIIIQNTKKEVRNLNA ELNASKEEKRRGEQKVQLQQ AQVQELNNRLKKVQDELHLK TIEEQMTHRKMVLFQEESGK FKQSAEEFRKKMEKLMESKV ITENDISGIRLDFVSLQQEN SRAQENAKLCETNIKELERQ LQQYREQMQQGQHMEANHYQ KCQKLEDELIAQKREVENLK QKMDQQIKEHEHQLVLLQCE IQKKSTAKDCTFKPDFEMTV KECQHSGELSSRNTGHLHPT PRSPLLRWTQEPQPLEEKWQ HRVVEQIPKEVQFQPPGAPL EKEKSQQCYSEYFSQTSTEL QITFDETNPITRLSEIEKIR DQALNNSRPPVRYQDNACEM ELVKVLTPLEIAKNKQYDMH TEVTTLKQEKNPVPSAEEWM LEGCRASGGLKKGDFLKKGL EPETFQNFDGDHACSVRDDE FKFQGLRHTVTARQLVEAKL LDMRTIEQLRLGLKTVEEVQ KTLNKFLTKATSIAGLYLES TKEKISFASAAERIIIDKMV ALAFLEAQAATGFIIDPISG QTYSVEDAVLKGVVDPEFRI RLLEAEKAAVGYSYSSKTLS VFQAMENRMLDRQKGKHILE AQIASGGVIDPVRGIRVPPE IALQQGLLNNAILQFLHEPS SNTRVFPNPNNKQALYYSEL LRMCVFDVESQCFLFPFGER NISNLNVKKTHRISVVDTKT GSELTVYEAFQRNLIEKSIY LELSGQQYQWKEAMFFESYG HSSHMLTDTKTGLHFNINEA IEQGTIDKALVKKYQEGLIT LTELADSLLSRLVPKKDLHS PVAGYWLTASGERISVLKAS RRNLVDRITALRCLEAQVST GGIIDPLTGKKYRVAEALHR GLVDEGFAQQLRQCELVITG IGHPITNKMMSVVEAVNANI INKEMGIRCLEFQYLTGGLI EPQVHSRLSIEEALQVGIID VLIATKLKDQKSYVRNIICP QTKRKLTYKEALEKADFDFH TGLKLLEVSEPLMTGISSLY YSS in isoform 3. 3 PublicationsVSP_041533
    Alternative sequencei1434 – 75706137Missing in isoform 3. 3 PublicationsVSP_041534Add
    BLAST
    Alternative sequencei1550 – 36352086Missing in isoform 2. 2 PublicationsVSP_041535Add
    BLAST
    Alternative sequencei3387 – 75704184Missing in isoform 4. 1 PublicationVSP_041536Add
    BLAST
    Alternative sequencei4184 – 420017GQVPL…IISKN → DVGTGYCRSSEQYKCHE in isoform 5. 1 PublicationVSP_041537Add
    BLAST
    Alternative sequencei4201 – 75703370Missing in isoform 5. 1 PublicationVSP_041538Add
    BLAST
    Alternative sequencei7352 – 737524Missing in isoform 2. 2 PublicationsVSP_041539Add
    BLAST
    Alternative sequencei7442 – 74421K → KILHPLTRNYGKPWLTNSKM STPCKAAECSDFPVPSAE in isoform 2. 2 PublicationsVSP_041540

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M69225 mRNA. No translation available.
    L11690 mRNA. Translation: AAA52288.1.
    AF400226 mRNA. Translation: AAL62061.1.
    AF400227 mRNA. Translation: AAL62062.1.
    AK055189 mRNA. Translation: BAB70870.1. Different initiation.
    AK094883 mRNA. Translation: BAC04449.1. Different initiation.
    AK096713 mRNA. Translation: BAC04848.1. Different initiation.
    AK295864 mRNA. Translation: BAH12207.1.
    AL049215 Genomic DNA. No translation available.
    AL512422
    , AL096710, AL137008, AL512448, AL590005 Genomic DNA. Translation: CAI14341.1. Sequence problems.
    AL590005
    , AL096710, AL137008, AL512422, AL512448 Genomic DNA. Translation: CAI14989.1. Sequence problems.
    AL512448
    , AL096710, AL137008, AL512422, AL590005 Genomic DNA. Translation: CAI16609.1. Sequence problems.
    AL512448, AL096710, AL137008 Genomic DNA. Translation: CAI16610.1. Sequence problems.
    AL137008
    , AL096710, AL512422, AL512448, AL590005 Genomic DNA. Translation: CAI20330.1. Sequence problems.
    AL137008, AL096710, AL512448 Genomic DNA. Translation: CAI20332.1. Sequence problems.
    AL096710
    , AL137008, AL512422, AL512448, AL590005 Genomic DNA. Translation: CAI22044.1. Sequence problems.
    AL096710, AL137008, AL512448 Genomic DNA. Translation: CAI22045.1. Sequence problems.
    AL096710 Genomic DNA. Translation: CAI22046.1.
    AL096710 Genomic DNA. Translation: CAI22047.1.
    U31850 mRNA. Translation: AAC50243.1.
    U31851 mRNA. Translation: AAC50244.1. Frameshift.
    AF165191 mRNA. Translation: AAD49334.1.
    AY032900 mRNA. Translation: AAK63130.1.
    AY032901 mRNA. Translation: AAK63131.1.
    M63618 mRNA. Translation: AAA35606.1.
    BC016991 mRNA. Translation: AAH16991.1.
    AB018271 mRNA. Translation: BAA34448.2.
    M22942 mRNA. Translation: AAA35538.1. Sequence problems.
    X58677 mRNA. Translation: CAA41528.1.
    U04850 Genomic DNA. Translation: AAA57184.1.
    U04850 Genomic DNA. Translation: AAA57185.1. Sequence problems.
    CCDSiCCDS47443.1. [Q03001-8]
    CCDS4959.1. [Q03001-3]
    PIRiI56317. A40937.
    RefSeqiNP_001138241.1. NM_001144769.2.
    NP_001138242.1. NM_001144770.1.
    NP_001714.1. NM_001723.5. [Q03001-3]
    NP_056363.2. NM_015548.4. [Q03001-8]
    NP_899236.1. NM_183380.3.
    UniGeneiHs.604915.
    Hs.669931.
    Hs.728928.
    Hs.735651.

    Genome annotation databases

    EnsembliENST00000244364; ENSP00000244364; ENSG00000151914. [Q03001-8]
    ENST00000370765; ENSP00000359801; ENSG00000151914. [Q03001-3]
    ENST00000439203; ENSP00000404924; ENSG00000151914. [Q03001-9]
    GeneIDi667.
    KEGGihsa:667.
    UCSCiuc003pcy.4. human. [Q03001-8]
    uc003pdc.4. human. [Q03001-3]
    uc003pde.2. human. [Q03001-13]
    uc021zax.1. human. [Q03001-9]
    uc021zay.2. human. [Q03001-7]

    Polymorphism databases

    DMDMi294862529.

    Keywords - Coding sequence diversityi

    Alternative promoter usage, Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M69225 mRNA. No translation available.
    L11690 mRNA. Translation: AAA52288.1 .
    AF400226 mRNA. Translation: AAL62061.1 .
    AF400227 mRNA. Translation: AAL62062.1 .
    AK055189 mRNA. Translation: BAB70870.1 . Different initiation.
    AK094883 mRNA. Translation: BAC04449.1 . Different initiation.
    AK096713 mRNA. Translation: BAC04848.1 . Different initiation.
    AK295864 mRNA. Translation: BAH12207.1 .
    AL049215 Genomic DNA. No translation available.
    AL512422
    , AL096710 , AL137008 , AL512448 , AL590005 Genomic DNA. Translation: CAI14341.1 . Sequence problems.
    AL590005
    , AL096710 , AL137008 , AL512422 , AL512448 Genomic DNA. Translation: CAI14989.1 . Sequence problems.
    AL512448
    , AL096710 , AL137008 , AL512422 , AL590005 Genomic DNA. Translation: CAI16609.1 . Sequence problems.
    AL512448 , AL096710 , AL137008 Genomic DNA. Translation: CAI16610.1 . Sequence problems.
    AL137008
    , AL096710 , AL512422 , AL512448 , AL590005 Genomic DNA. Translation: CAI20330.1 . Sequence problems.
    AL137008 , AL096710 , AL512448 Genomic DNA. Translation: CAI20332.1 . Sequence problems.
    AL096710
    , AL137008 , AL512422 , AL512448 , AL590005 Genomic DNA. Translation: CAI22044.1 . Sequence problems.
    AL096710 , AL137008 , AL512448 Genomic DNA. Translation: CAI22045.1 . Sequence problems.
    AL096710 Genomic DNA. Translation: CAI22046.1 .
    AL096710 Genomic DNA. Translation: CAI22047.1 .
    U31850 mRNA. Translation: AAC50243.1 .
    U31851 mRNA. Translation: AAC50244.1 . Frameshift.
    AF165191 mRNA. Translation: AAD49334.1 .
    AY032900 mRNA. Translation: AAK63130.1 .
    AY032901 mRNA. Translation: AAK63131.1 .
    M63618 mRNA. Translation: AAA35606.1 .
    BC016991 mRNA. Translation: AAH16991.1 .
    AB018271 mRNA. Translation: BAA34448.2 .
    M22942 mRNA. Translation: AAA35538.1 . Sequence problems.
    X58677 mRNA. Translation: CAA41528.1 .
    U04850 Genomic DNA. Translation: AAA57184.1 .
    U04850 Genomic DNA. Translation: AAA57185.1 . Sequence problems.
    CCDSi CCDS47443.1. [Q03001-8 ]
    CCDS4959.1. [Q03001-3 ]
    PIRi I56317. A40937.
    RefSeqi NP_001138241.1. NM_001144769.2.
    NP_001138242.1. NM_001144770.1.
    NP_001714.1. NM_001723.5. [Q03001-3 ]
    NP_056363.2. NM_015548.4. [Q03001-8 ]
    NP_899236.1. NM_183380.3.
    UniGenei Hs.604915.
    Hs.669931.
    Hs.728928.
    Hs.735651.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3GJO X-ray 2.50 E/F/G/H 7541-7570 [» ]
    ProteinModelPortali Q03001.
    SMRi Q03001. Positions 31-255, 583-795.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107135. 36 interactions.
    DIPi DIP-33131N.
    IntActi Q03001. 34 interactions.
    MINTi MINT-119936.

    PTM databases

    PhosphoSitei Q03001.

    Polymorphism databases

    DMDMi 294862529.

    Proteomic databases

    MaxQBi Q03001.
    PaxDbi Q03001.
    PRIDEi Q03001.

    Protocols and materials databases

    DNASUi 667.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000244364 ; ENSP00000244364 ; ENSG00000151914 . [Q03001-8 ]
    ENST00000370765 ; ENSP00000359801 ; ENSG00000151914 . [Q03001-3 ]
    ENST00000439203 ; ENSP00000404924 ; ENSG00000151914 . [Q03001-9 ]
    GeneIDi 667.
    KEGGi hsa:667.
    UCSCi uc003pcy.4. human. [Q03001-8 ]
    uc003pdc.4. human. [Q03001-3 ]
    uc003pde.2. human. [Q03001-13 ]
    uc021zax.1. human. [Q03001-9 ]
    uc021zay.2. human. [Q03001-7 ]

    Organism-specific databases

    CTDi 667.
    GeneCardsi GC06M056370.
    H-InvDB HIX0005976.
    HIX0164999.
    HGNCi HGNC:1090. DST.
    HPAi HPA030200.
    MIMi 113810. gene.
    614653. phenotype.
    615425. phenotype.
    neXtProti NX_Q03001.
    Orphaneti 89838. Autosomal recessive epidermolysis bullosa simplex.
    314381. Hereditary sensory and autonomic neuropathy type 6.
    PharmGKBi PA25399.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5069.
    HOVERGENi HBG031127.
    InParanoidi Q8WXK8.
    KOi K10382.
    OMAi RKITEIQ.
    PhylomeDBi Q03001.
    TreeFami TF335163.

    Enzyme and pathway databases

    Reactomei REACT_150180. Assembly of collagen fibrils and other multimeric structures.
    REACT_20537. Type I hemidesmosome assembly.

    Miscellaneous databases

    ChiTaRSi DST. human.
    EvolutionaryTracei Q03001.
    GeneWikii Dystonin.
    GenomeRNAii 667.
    NextBioi 2720.
    PROi Q03001.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q03001.
    Bgeei Q03001.
    CleanExi HS_DST.
    Genevestigatori Q03001.

    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. 2 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. 19 hits.
    [Graphical view ]
    SMARTi SM00033. CH. 2 hits.
    SM00054. EFh. 2 hits.
    SM00243. GAS2. 1 hit.
    SM00250. PLEC. 8 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. "Human bullous pemphigoid antigen (BPAG1). Amino acid sequences deduced from cloned cDNAs predict biologically important peptide segments and protein domains."
      Sawamura D., Li K., Chu M.-L., Uitto J.
      J. Biol. Chem. 266:17784-17790(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), DISEASE.
      Tissue: Keratinocyte.
    2. "Cloning of the 5' mRNA for the 230-kD bullous pemphigoid antigen by rapid amplification of cDNA ends."
      Elgart G.W., Stanley J.R.
      J. Invest. Dermatol. 101:244-246(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
      Tissue: Keratinocyte.
    3. "Novel alternative splicings of BPAG1 (bullous pemphigoid antigen 1) including the domain structure closely related to MACF (microtubule actin cross-linking factor)."
      Okumura M., Yamakawa H., Ohara O., Owaribe K.
      J. Biol. Chem. 277:6682-6687(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [MRNA] OF 1-3386 (ISOFORM 4), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: Keratinocyte.
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 8), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4114-6568 (ISOFORM 1), VARIANT ALA-5138.
      Tissue: Brain, Hippocampus, Placenta and Tongue.
    5. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "Cloning and characterization of the neural isoforms of human dystonin."
      Brown A., Dalpe G., Mathieu M., Kothary R.
      Genomics 29:777-780(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-461 (ISOFORM 1), NUCLEOTIDE SEQUENCE [MRNA] OF 1-46 (ISOFORM 6).
      Tissue: Fetal brain and Retina.
    7. "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: NUCLEOTIDE SEQUENCE [MRNA] OF 1-188 (ISOFORM 7), ALTERNATIVE SPLICING (ISOFORMS 6 AND 7), FUNCTION OF ISOFORMS 6 AND 7, SUBCELLULAR LOCATION (ISOFORMS 6 AND 7).
      Tissue: Fetal brain.
    8. Geerts D., Sonnenberg A.
      Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 208-308 (ISOFORM 1).
      Tissue: Pineal gland.
    9. "Comparison of molecularly cloned bullous pemphigoid antigen to desmoplakin I confirms that they define a new family of cell adhesion junction plaque proteins."
      Tanaka T., Parry D.A.D., Klaus-Kovtun V., Steinert P.M., Stanley J.R.
      J. Biol. Chem. 266:12555-12559(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 881-7570 (ISOFORM 3).
      Tissue: Keratinocyte.
    10. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3754-7570 (ISOFORM 5).
      Tissue: Duodenum.
    11. "Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 5:277-286(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5947-7570 (ISOFORM 2).
      Tissue: Brain.
    12. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
      Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
      DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION.
    13. "Isolation of complementary DNA for bullous pemphigoid antigen by use of patients' autoantibodies."
      Stanley J.R., Tanaka T., Mueller S., Klaus-Kovtun V., Roop D.
      J. Clin. Invest. 82:1864-1870(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
      Tissue: Keratinocyte.
    14. "The hemidesmosomal plaque. I. Characterization of a major constituent protein as a differentiation marker for certain forms of epithelia."
      Owaribe K., Kartenbeck J., Stumpp S., Magin T.M., Krieg T., Diaz L.A., Franke W.W.
      Differentiation 45:207-220(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
    15. "Identification of a second protein product of the gene encoding a human epidermal autoantigen."
      Hopkinson S.B., Jones J.C.
      Biochem. J. 300:851-857(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM 3).
    16. "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 3 AND 6), TISSUE SPECIFICITY.
    17. "The N terminus of the transmembrane protein BP180 interacts with the N-terminal domain of BP230, thereby mediating keratin cytoskeleton anchorage to the cell surface at the site of the hemidesmosome."
      Hopkinson S.B., Jones J.C.
      Mol. Biol. Cell 11:277-286(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING (ISOFORM 3), INTERACTION WITH COL17A1 AND ITGB4.
    18. "Structural analysis of the predicted coiled-coil rod domain of the cytoplasmic bullous pemphigoid antigen (BPAG1). Empirical localization of the N-terminal globular domain-rod boundary."
      Tang H.-Y., Chaffotte A.-F., Thacher S.M.
      J. Biol. Chem. 271:9716-9722(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: DOMAINS.
    19. "The hemidesmosomal protein bullous pemphigoid antigen 1 and the integrin beta 4 subunit bind to ERBIN. Molecular cloning of multiple alternative splice variants of ERBIN and analysis of their tissue expression."
      Favre B., Fontao L., Koster J., Shafaatian R., Jaunin F., Saurat J.-H., Sonnenberg A., Borradori L.
      J. Biol. Chem. 276:32427-32436(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ITGB4 AND ERBB2IP.
    20. "Analysis of the interactions between BP180, BP230, plectin and the integrin alpha6beta4 important for hemidesmosome assembly."
      Koster J., Geerts D., Favre B., Borradori L., Sonnenberg A.
      J. Cell Sci. 116:387-399(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING (ISOFORM 3), FUNCTION OF ISOFORM 3, INTERACTION WITH COL17A1 AND ITGB4, SUBCELLULAR LOCATION (ISOFORM 3).
    21. "Interaction of the bullous pemphigoid antigen 1 (BP230) and desmoplakin with intermediate filaments is mediated by distinct sequences within their COOH terminus."
      Fontao L., Favre B., Riou S., Geerts D., Jaunin F., Saurat J.H., Green K.J., Sonnenberg A., Borradori L.
      Mol. Biol. Cell 14:1978-1992(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING (ISOFORM 3), ASSOCIATION WITH KERATIN FILAMENTS, SUBCELLULAR LOCATION (ISOFORM 3).
    22. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7432, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    23. "BPAG1e maintains keratinocyte polarity through beta4 integrin-mediated modulation of Rac1 and cofilin activities."
      Hamill K.J., Hopkinson S.B., DeBiase P., Jones J.C.
      Mol. Biol. Cell 20:2954-2962(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING (ISOFORM 3), FUNCTION OF ISOFORM 3, SUBCELLULAR LOCATION (ISOFORM 3).
    24. "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 (ISOFORM 1), HOMODIMERIZATION, INTERACTION WITH ACTN2 AND PLEC, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    25. "A homozygous nonsense mutation within the dystonin gene coding for the coiled-coil domain of the epithelial isoform of BPAG1 underlies a new subtype of autosomal recessive epidermolysis bullosa simplex."
      Groves R.W., Liu L., Dopping-Hepenstal P.J., Markus H.S., Lovell P.A., Ozoemena L., Lai-Cheong J.E., Gawler J., Owaribe K., Hashimoto T., Mellerio J.E., Mee J.B., McGrath J.A.
      J. Invest. Dermatol. 130:1551-1557(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN EBSB2.
    26. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    27. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2919, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    28. "Hereditary sensory autonomic neuropathy caused by a mutation in dystonin."
      Edvardson S., Cinnamon Y., Jalas C., Shaag A., Maayan C., Axelrod F.B., Elpeleg O.
      Ann. Neurol. 71:569-572(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN HSAN6.
    29. Cited for: INVOLVEMENT IN EBSB2.
    30. "Identification of IGPR-1 as a novel adhesion molecule involved in angiogenesis."
      Rahimi N., Rezazadeh K., Mahoney J.E., Hartsough E., Meyer R.D.
      Mol. Biol. Cell 23:1646-1656(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TMIGD2.
    31. Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 7541-7570 IN COMPLEX WITH MAPRE1, DOMAIN MICROTUBULE TIP LOCALIZATION SIGNAL, MUTAGENESIS OF LYS-7548; SER-7550; ILE-7552; PRO-7553 AND 7557-ARG-LYS-7558.

    Entry informationi

    Entry nameiDYST_HUMAN
    AccessioniPrimary (citable) accession number: Q03001
    Secondary accession number(s): B7Z3H1
    , O94833, Q12825, Q13266, Q13267, Q13775, Q5TBT0, Q5TBT2, Q5TF23, Q5TF24, Q8N1T8, Q8N8J3, Q8WXK8, Q8WXK9, Q96AK9, Q96DQ5, Q96J76, Q96QT5, Q9H555, Q9UGD7, Q9UGD8, Q9UN10
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: April 20, 2010
    Last modified: October 1, 2014
    This is version 166 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3