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Q91ZU6 (DYST_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Dst
Synonyms:Bpag1, Macf2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length7389 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.4 Ref.7 Ref.13 Ref.19

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. Ref.4 Ref.7 Ref.13 Ref.19

Isoform 6:required for bundling actin filaments around the nucleus. Ref.4 Ref.7 Ref.13 Ref.19

Subunit structure

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. Ref.7 Ref.12 Ref.14 Ref.17 Ref.18

Subcellular location

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. Ref.3 Ref.4 Ref.9 Ref.10 Ref.14 Ref.17 Ref.18 Ref.19

Isoform 1: Cytoplasmcytoskeleton. Note: Colocalizes both cortical and cytoplasmic actin filaments. Ref.3 Ref.4 Ref.9 Ref.10 Ref.14 Ref.17 Ref.18 Ref.19

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. Ref.3 Ref.4 Ref.9 Ref.10 Ref.14 Ref.17 Ref.18 Ref.19

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. Ref.3 Ref.4 Ref.9 Ref.10 Ref.14 Ref.17 Ref.18 Ref.19

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. Ref.3 Ref.4 Ref.9 Ref.10 Ref.14 Ref.17 Ref.18 Ref.19

Isoform 7: Cytoplasmcytoskeleton. Cytoplasmcell cortex. Cell membrane; Lipid-anchor Ref.3 Ref.4 Ref.9 Ref.10 Ref.14 Ref.17 Ref.18 Ref.19.

Tissue specificity

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. Ref.1 Ref.2 Ref.4 Ref.9 Ref.10 Ref.14 Ref.17 Ref.18 Ref.19

Developmental stage

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. Ref.1 Ref.2

Domain

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.

Disruption phenotype

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. Ref.9 Ref.11 Ref.12 Ref.13

Sequence similarities

Belongs to the plakin or cytolinker family. UniProtKB Q03001

Contains 1 actin-binding domain.

Contains 2 CH (calponin-homology) domains.

Contains 2 EF-hand domains.

Contains 1 GAR domain.

Contains 5 plectin repeats.

Contains 1 SH3 domain.

Contains 19 spectrin repeats.

Sequence caution

Isoform 6: The sequence AAC52231.1 differs from that shown. Reason: Frameshift at position 51.

Ontologies

Keywords
   Biological processCell adhesion
   Cellular componentCell junction
Cell membrane
Cell projection
Cytoplasm
Cytoskeleton
Endoplasmic reticulum
Intermediate filament
Membrane
Microtubule
Nucleus
   Coding sequence diversityAlternative promoter usage
Alternative splicing
   DomainCoiled coil
Repeat
SH3 domain
Transmembrane
   LigandActin-binding
Calcium
Metal-binding
   Molecular functionMuscle protein
   PTMLipoprotein
Myristate
Palmitate
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processaxonogenesis

Inferred from mutant phenotype PubMed 1634998. Source: MGI

cell adhesion

Inferred from electronic annotation. Source: UniProtKB-KW

cell cycle arrest

Inferred from electronic annotation. Source: InterPro

cytoplasmic microtubule organization

Inferred from mutant phenotype Ref.11. Source: MGI

intermediate filament cytoskeleton organization

Inferred from sequence or structural similarity. Source: UniProtKB

intracellular transport

Inferred from direct assay Ref.14. Source: UniProtKB

regulation of microtubule polymerization or depolymerization

Inferred from mutant phenotype Ref.11. Source: MGI

retrograde axon cargo transport

Inferred from mutant phenotype Ref.13. Source: MGI

   Cellular_componentH zone

Inferred from direct assay Ref.19. Source: UniProtKB

Z disc

Inferred from direct assay Ref.18Ref.19. Source: UniProtKB

actin cytoskeleton

Inferred from direct assay Ref.11. Source: MGI

axon

Inferred from electronic annotation. Source: UniProtKB-SubCell

cell cortex

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasm

Inferred from direct assay Ref.18. Source: UniProtKB

cytoplasmic membrane-bounded vesicle

Inferred from sequence orthology Ref.13. Source: MGI

cytoplasmic side of plasma membrane

Inferred from direct assay Ref.3. Source: UniProtKB

endoplasmic reticulum membrane

Inferred from direct assay Ref.17. Source: UniProtKB

focal adhesion

Inferred from direct assay Ref.14Ref.3. Source: UniProtKB

hemidesmosome

Inferred from direct assay PubMed 8707838. Source: MGI

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

intercalated disc

Inferred from direct assay Ref.18. Source: UniProtKB

intermediate filament

Inferred from electronic annotation. Source: UniProtKB-KW

membrane

Inferred from direct assay Ref.3. Source: UniProtKB

microtubule cytoskeleton

Inferred from direct assay Ref.11. Source: MGI

microtubule plus-end

Inferred from sequence or structural similarity. Source: UniProtKB

neurofilament cytoskeleton

Inferred from direct assay Ref.11. Source: MGI

nuclear envelope

Inferred from direct assay Ref.17. Source: UniProtKB

nucleus

Inferred from direct assay Ref.14Ref.3. Source: UniProtKB

perinuclear endoplasmic reticulum

Inferred from direct assay Ref.3. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from direct assay Ref.3. Source: UniProtKB

sarcolemma

Inferred from direct assay Ref.19. Source: UniProtKB

stress fiber

Inferred from direct assay Ref.14. Source: UniProtKB

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

microtubule binding

Inferred from direct assay Ref.11. Source: MGI

microtubule plus-end binding

Inferred from sequence or structural similarity. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.17Ref.18. Source: UniProtKB

protein homodimerization activity

Inferred from direct assay Ref.14. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PrphP218073EBI-446159,EBI-446227From a different organism.

Alternative products

This entry describes 7 isoforms produced by alternative promoter usage and alternative splicing. [Align] [Select]
Isoform 2 Ref.1 (identifier: Q91ZU6-1)

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.
Isoform 1 Ref.1 (identifier: Q91ZU6-2)

Also known as: BPAG1-a; BPAG1a2;

The sequence of this isoform differs from the canonical sequence as follows:
     1549-3557: Missing.
Isoform 3 (identifier: Q91ZU6-3)

The sequence of this isoform differs from the canonical sequence as follows:
     7125-7130: Missing.
     7170-7193: Missing.
     7261-7261: K → KILHPLTRNYGKPWLANSKMSTPCKAAECPDFPVSSAE
Note: No experimental confirmation available.
Isoform 4 (identifier: Q91ZU6-4)

The sequence of this isoform differs from the canonical sequence as follows:
     7170-7193: Missing.
     7261-7261: K → KILHPLTRNYGKPWLANSKMSTPCKAAECPDFPVSSAE
Note: No experimental confirmation available.
Isoform 5 Ref.1 (identifier: Q91ZU6-5)

Also known as: BPAG1-e;

The sequence of this isoform differs from the canonical sequence as follows:
     1-381: MAGYLSPAAY...REKALRPEVE → MRISCPFIVVPLINSCISFSNESLDGH
     1432-1432: K → MKRSKENSEH...GISNLYYSSQ
     1433-7389: Missing.
Isoform 6 (identifier: Q91ZU6-6)

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
     305-7389: Missing.
Note: Incomplete sequence. Transmembrane protein (helical transmembrane domain from amino acid 18 to 38).
Isoform 7 (identifier: Q91ZU6-8)

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
     273-7389: 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 73897389Dystonin
PRO_0000078141

Regions

Domain35 – 252218Actin-binding
Domain35 – 138104CH 1
Domain151 – 252102CH 2
Repeat701 – 801101Spectrin 1
Domain889 – 94153SH3
Repeat1582 – 162443Plectin 1
Repeat1657 – 170145Plectin 2
Repeat1772 – 181544Plectin 3
Repeat1816 – 184429Plectin 4
Repeat1848 – 188942Plectin 5
Repeat3845 – 392581Spectrin 2
Repeat3997 – 407983Spectrin 3
Repeat4440 – 4548109Spectrin 4
Repeat4552 – 4657106Spectrin 5
Repeat4775 – 4877103Spectrin 6
Repeat5208 – 5315108Spectrin 7
Repeat5322 – 5423102Spectrin 8
Repeat5430 – 5532103Spectrin 9
Repeat5647 – 5751105Spectrin 10
Repeat5758 – 585699Spectrin 11
Repeat6002 – 608281Spectrin 12
Repeat6089 – 6191103Spectrin 13
Repeat6197 – 6300104Spectrin 14
Repeat6308 – 6410103Spectrin 15
Repeat6415 – 6519105Spectrin 16
Repeat6523 – 6629107Spectrin 17
Repeat6636 – 6736101Spectrin 18
Repeat6741 – 6844104Spectrin 19
Domain7015 – 705036EF-hand 1
Domain7051 – 708636EF-hand 2
Domain7091 – 716979GAR
Calcium binding7028 – 7039121 Potential
Calcium binding7064 – 7075122 Potential
Motif1382 – 13887Nuclear localization signal; in isoform 6
Motif7369 – 73724Microtubule tip localization signal
Compositional bias2362 – 242261Asp-rich

Amino acid modifications

Modified residue28571Phosphoserine By similarity
Modified residue72501Phosphoserine By similarity

Natural variations

Alternative sequence1 – 381381MAGYL…RPEVE → MRISCPFIVVPLINSCISFS NESLDGH in isoform 5.
VSP_041541
Alternative sequence1 – 137137MAGYL…IILHF → MGNVCGCVRAEKEEPYFDPA KSPLSPEKYSPGRKYFRRKP CQKVVDDTEPVRQSSEREGK KGVSQPAGGQPAVSSGELPW EDPAASPTKEDAVQLGKRAA TEHGDQKPLPSSVDGYPHRV TVSSAQGRYSEVQVSIPDKI ISEEDSPPYCPETERHLDDV NSKHRTFLRKDNVSLSQTAA SSSPILCVTEKSLKNSALMG NLSRSCHSVLEQDSDERGHP FGVHRLQLTKRRCHSLSSGV SCVSKDAPRDDGC in isoform 7.
VSP_041542
Alternative sequence1 – 3030MAGYL…LERYK → MIAAAFLVLLRPYSIQCALF LLLLLLGTVATIVFFCCWHR KLQKGRHPMKSVFSGRSRSR DAALRSHHFRSEGFRASPRH IRRRVAAAAAARLEEVKPVV EVHHQSEQESSGRKRRIKKN SRVQPEFYHSVQGASTRRPS SGNASYRCSMSSSADFSDED DFSQKSGSASPAPGDTLPWN LPKHERSKRKIQGGSVLDPA ERAVLRIA in isoform 6.
VSP_041543
Alternative sequence271 – 2722VK → KG in isoform 7.
VSP_041544
Alternative sequence273 – 73897117Missing in isoform 7.
VSP_041545
Alternative sequence305 – 73897085Missing in isoform 6.
VSP_041546
Alternative sequence14321K → MKRSKENSEHGAYSDLLQRQ RATMVENSKLTGKISELETM VAELKKQKSRVEEELPKVKE AAENELRKQQRNVEDIALQK LRAESEAKQYRRELETIVRE KEAAERELERVRQLTAEAEA RRAAVEENLRNFRSQLQENT FTRQTLEDHLRRKDSSLSDL EQQKRALVEELQRKRDHEEE LLRLVKQMERDLAFQKQVAE KQLKEKQKVELEARRKITEI QFSCRESAAVAQARPQREQG RQKEEELKQQVDELTLANRK AEKEMRELKYELSAVQLEKA SSEEKARLLKDKLDETNNTL KCLKEDLERKDQAQERYSQQ LRDLGGQLNQTTDKAEEVRQ 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.
VSP_041547
Alternative sequence1433 – 73895957Missing in isoform 5.
VSP_041548
Alternative sequence1549 – 35572009Missing in isoform 1. Ref.1
VSP_041549
Alternative sequence7125 – 71306Missing in isoform 3.
VSP_041550
Alternative sequence7170 – 719324Missing in isoform 3 and isoform 4.
VSP_041551
Alternative sequence72611K → KILHPLTRNYGKPWLANSKM STPCKAAECPDFPVSSAE in isoform 3 and isoform 4.
VSP_041552

Experimental info

Mutagenesis13851R → A: Prevents isoform 6 from localizing to the nucleus; when associated with A-1386. Ref.14
Mutagenesis13861R → A: Prevents isoform 6 from localizing to the nucleus; when associated with A-1385. Ref.14
Sequence conflict61931T → A in AAK83383. Ref.1
Sequence conflict70971G → E in BAC29753. Ref.6
Sequence conflict70971G → E in BAC34695. Ref.6
Sequence conflict72411G → A in BAC29753. Ref.6
Sequence conflict72411G → A in BAC34695. Ref.6
Isoform 5:
Sequence conflict23251G → D in BAB93448. Ref.7
Sequence conflict24161A → T in BAB93448. Ref.7
Sequence conflict25301K → Q in BAB93448. Ref.7
Isoform 6:
Sequence conflict1011E → K in AAC52231. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 2 (BPAG1-b) (BPAG1a1) (dystonin-1) [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: BFED827ED8A88AAD

FASTA7,389833,638
        10         20         30         40         50         60 
MAGYLSPAAY MYVEEQEYLQ AYEDVLERYK DERDKVQKKT FTKWINQHLM KVRKHVNDLY 

        70         80         90        100        110        120 
EDLRDGHNLI SLLEVLSGDT LPREKGRMRF HRLQNVQIAL DYLKRRQVKL VNIRNDDITD 

       130        140        150        160        170        180 
GNPKLTLGLI WTIILHFQIS DIHVTGESED MSAKERLLLW TQQATEGYAG VRCENFTTCW 

       190        200        210        220        230        240 
RDGKLFNAII HKYRPDLIDM NTVAVQSNLA NLEHAFYVAE KIGVIRLLDP EDVDVSSPDE 

       250        260        270        280        290        300 
KSVITYVSSL YDAFPKVPEG GEGIGANDVE VKWIEYQNMV NYLIQWIRHH VVTMSERTFP 

       310        320        330        340        350        360 
NNPLELKALY NQYLQFKEKE IPPKEMEKSK IKRLYKLLEI WIEFGRIKLL QGYHPNDIEK 

       370        380        390        400        410        420 
EWGKLIIAML EREKALRPEV ERLDMLQQIA TRVQRDSVSC EDKLILARNA LQSDSKRLES 

       430        440        450        460        470        480 
GVQFQNEAEI AGYILECENL LRQHVIDVQI LIDGKYYQAD QLVQRVAKLR DEIMALRNEC 

       490        500        510        520        530        540 
SSVYSKGRML TTEQTKLMIS GITQSLNSGF AQTLHPSLNS GLTQSLTPSL TSSSVTSGLS 

       550        560        570        580        590        600 
SGMTSRLTPS VTPVYAPGFP SVVAPNFSLG VEPNSLQTLK LMQIRKPLLK SSLLDQNLTE 

       610        620        630        640        650        660 
EEVNMKFVQD LLNWVDEMQV QLDRTEWGSD LPSVESHLEN HKNVHRAIEE FESSLKEAKI 

       670        680        690        700        710        720 
SEIQMTAPLK LSYTDKLHRL ESQYAKLLNT SRNQERHLDT LHNFVTRATN ELIWLNEKEE 

       730        740        750        760        770        780 
SEVAYDWSER NSSVARKKSY HVELMRELEQ KEESIKAVQE IAEQLLLENH PARLTIEAYR 

       790        800        810        820        830        840 
AAMQTQWSWI LQLCQCVEQH IQENSAYFEF FNDAKEATDY LRNLKDAIQR KYSCDRSSSI 

       850        860        870        880        890        900 
HKLEDLVQES MEKEELLQYR SVVAGLMGRA KTVVQLKPRN PDNPLKTSIP IKAICDYRQI 

       910        920        930        940        950        960 
EITIYKDDEC VLANNSHRAK WKVISPTGNE AVVPSVCFTV PPPNKEAVDF ANRIEQQYQS 

       970        980        990       1000       1010       1020 
VLTLWHESHI NMKSVVSWHY LVNEIDRIRA SNVASIKTML PGEHQQVLSN LQSRLEDFLE 

      1030       1040       1050       1060       1070       1080 
DSQESQIFSG SDISQLEKEV SVCRKYYQEL LKSAEREEQE ESVYNLYISE VRNIRLRLES 

      1090       1100       1110       1120       1130       1140 
CEDRLIRQIR TPLERDDLHE SMLRITEQEK LKKELDRLKD DLGTITNKCE EFFSQAADSP 

      1150       1160       1170       1180       1190       1200 
SVPALRSELS VVIQSLSQIY SMSSTYIEKL KTVNLVLKNT QAAEALVKLY ETKLCEEEAV 

      1210       1220       1230       1240       1250       1260 
IADKNNIENL MSTLKQWRSE VDEKREVFHA LEDELQKAKA ISDEMFKTHK ERDLDFDWHK 

      1270       1280       1290       1300       1310       1320 
EKADQLVERW QSVHVQIDNR LRDLEGIGKS LKHYRDSYHP LDDWIQHIET TQRKIQENQP 

      1330       1340       1350       1360       1370       1380 
ENSKALALQL NQQKMLVSEI EVKQSKMDEC QKYSEQYSAA VKDYELQTMT YRAMVESQQK 

      1390       1400       1410       1420       1430       1440 
SPVKRRRIQS SADLVIQEFM DLRTRYTALV TLMTQYIKFA GDSLKRLEEE EKSLDEEKKQ 

      1450       1460       1470       1480       1490       1500 
HIEKAKELQK WVSNISKTLG DGEKAGKPLF SKQQMSSKEI STKKEQFSEA LQTTQIFLAK 

      1510       1520       1530       1540       1550       1560 
HGDKLTEEER SDLEKQVKTL QEGYNLLFSE SLKQQELQPS GESKVPEKPD KVIAGTINQT 

      1570       1580       1590       1600       1610       1620 
TGEVLSVFQA VLRGLIDYET GIRLLEAQLV ITGLISPELR KCFDLRDAES HGLIDEQVLR 

      1630       1640       1650       1660       1670       1680 
QLKELNRAKQ LISTASPTSI PVLDSLAQGM VSESMAIRVL EILLSAGPLL VPATGEHLTL 

      1690       1700       1710       1720       1730       1740 
QQAFQQNLIS SALFSKVLER QDTCKDLIDP CTSEKVSLTD MVQRSILQEN TRMWLLPVRP 

      1750       1760       1770       1780       1790       1800 
QEAGRITLKC GRSVSILRAA HEGLIDRETM FRLLGAQLLS GGLIDCNSGQ KMTVEEAVAE 

      1810       1820       1830       1840       1850       1860 
GVIDRDTASS ILTYQVQTGG IVHSNPAKRL TVDEAVQCEL ITSSSALLVL EAQRGYVGLI 

      1870       1880       1890       1900       1910       1920 
WPHSGEIFPT SSSLQQELIT NELASKILNG RQKIAALYIP ESSQVIGLDA AKQLGIIDNN 

      1930       1940       1950       1960       1970       1980 
TASVLKDVKL PDKMPDLGDL EDCKNAKRWL SFCKFQPSTV HDYRQEEGGS DGEEPVTAQS 

      1990       2000       2010       2020       2030       2040 
SEQTKKLFLS YLMVNSYMDA HTGQRLLLYD GDLDEAVSML LESCGAELGA DTSTRESLSV 

      2050       2060       2070       2080       2090       2100 
LTIPDAFPDC ALSEEKHECS ADKCHYSHPG HKESLENAKW DMNEAFCKMG NNDSNGELPR 

      2110       2120       2130       2140       2150       2160 
PENLADTTVV QKGSESPSRV RVPKPTSSST QPEGSVLRPE SGSILKGCKS QSEPVTKKYP 

      2170       2180       2190       2200       2210       2220 
DGTNHSHFLT SETSRPCDSN EREDEENIQK GPSVFDYSPR LSALLSHDEL RQSQGRFSDT 

      2230       2240       2250       2260       2270       2280 
STPQNTGYLC EASTLSPSDQ RVLADQSTRE KFQDRFLGIA AISVSLQGAP CGQKPVDTEC 

      2290       2300       2310       2320       2330       2340 
SSSQVHYHSE ESMSDASAES GATRQTDESE KTGSKVEDNS CTMVPGGGSR NDNTSDCGPL 

      2350       2360       2370       2380       2390       2400 
SHKGAIDAGD YETSLLAGQQ SDTATDSDSD DYFYDTPLFE DEDHDSLILQ GDDRDCLQPE 

      2410       2420       2430       2440       2450       2460 
DYDTSLQEEN DRTPPPDDIF YDVMKEKENP EFPHGGMDES LGVENKVCCP QGFPVGIEKP 

      2470       2480       2490       2500       2510       2520 
ELYLAGEKEF NSGGSEQLVE SVSESENPPG LWDSESDSLT EGEIIGRKER LGASLTPDGH 

      2530       2540       2550       2560       2570       2580 
WRGDREECDT SRESQSDTDG VGSIQSSESY RPYMSDGSDL DEEDNGGRSS EDSGDGRGGQ 

      2590       2600       2610       2620       2630       2640 
GVADEGGEPQ YQADPTQLYT AIRKEHGGET QNVSDMIPLD KTHSYSPLET QHGAGVFQPE 

      2650       2660       2670       2680       2690       2700 
SAGKGGWDTE RSSHPELTTE ADEEDEASLS THMATKGVSL SNAEGTASEE IRLVQGPDSS 

      2710       2720       2730       2740       2750       2760 
GILKAEDLEN VSPEISPSSD NIVRSEAELG GGASEDGHLS FTGSDRDQQG PGRGLVKGRD 

      2770       2780       2790       2800       2810       2820 
GQSDKLVDET SIREMGFQKE GVLMSSPEEG GEEERDLEPF PNGSATESLN MGKSQVPPLL 

      2830       2840       2850       2860       2870       2880 
THTEELSHRG APHTTTMTTT MTLEGEAKNV QTGLTESPVL LETLAEIFDT PASKVTRADL 

      2890       2900       2910       2920       2930       2940 
TSAVTASEMK SQVKEDSLTG GPEKETGPCT SLGHCDKCIH VDMLEPNEHT PSCALVAPPT 

      2950       2960       2970       2980       2990       3000 
VKDNLCSVNN AGEKSVRPQE DWPPAAEVRL SDACVEESIS EGKAGILQFT PENSDSTLSR 

      3010       3020       3030       3040       3050       3060 
LPHQSVAGWG KSADSVQARL PVSGVRHTSA DTLDVGCPQL ESSREKASAE EEPHRERALS 

      3070       3080       3090       3100       3110       3120 
LKPQEREHHM LGFVEDGRSI LKSSLDKVHM NLQEVGDPSA GTGTKISIQN LIRRAILSEL 

      3130       3140       3150       3160       3170       3180 
PNEVSNVPSH GISPISNSSE VRAESGGDPF CITSFLHLLK QNQPPQETPG ISELAKVLTQ 

      3190       3200       3210       3220       3230       3240 
MDCDPEQRGL GSELLPPQLK NAFYKLLFDG YATEKDQAEA LGQTSCAVPK MAEEKPHVCS 

      3250       3260       3270       3280       3290       3300 
DLRNKEGHHC PLNPQAVGEA EVEPFSVHIA ALPGGEKLGE LCSEPPEHSE STSGSKERSS 

      3310       3320       3330       3340       3350       3360 
DGSSKEKCSN GLQQCLQHTE KMHEYLVLLQ DMKPPLDNQA SVESSLEALK SQLKQLEAFE 

      3370       3380       3390       3400       3410       3420 
LGLAPIAVFL RKDLKLAEEF LKSFPSDLPR RHHEELSKSH QRLQNAFSSL SSVSSERMKL 

      3430       3440       3450       3460       3470       3480 
IKLAINSEMS KLAVRHEDFL HKLTSYSDWV SEKSRSVKAI QTVNVQDTEL VKNSVKFLKN 

      3490       3500       3510       3520       3530       3540 
VLADLSHTKM QLETTAFDVQ SFISDYAQDL SPSQSRQLLR LLNTTQKGFL DLQELVTTEA 

      3550       3560       3570       3580       3590       3600 
DRLEALLQLE QELGHQKVVA ERQQEYREKL QGLCDLLTQT ENRLISNQEA FVIGDGTVEL 

      3610       3620       3630       3640       3650       3660 
QKYQSKQEEL QRDMQGSTQA MEEIVRNTEL FLKESGDELS QADRALIEQK LNEVKMKCAQ 

      3670       3680       3690       3700       3710       3720 
LNLKAEQSRK ELDKAVTTAL KEETEKVAAV RQLEESKTKI ENLLNWLSNV EEDSEGVWTK 

      3730       3740       3750       3760       3770       3780 
HTQPMEQNGT YLHEGDSKLG AGEEDEVNGN LLETDAEGHS EATKGNLNQQ YEKVKAQHGK 

      3790       3800       3810       3820       3830       3840 
IMAQHQAVLL ATQSAQVLLE KQGHYLSPEE KEKLQKNTQE LKVHYEKVLA ECEKKVKLTH 

      3850       3860       3870       3880       3890       3900 
SLQEELEKFD TDYSEFEHWL QQSEQELANL EAGADDLSGL MDKLTRQKSF SEDVISHKGD 

      3910       3920       3930       3940       3950       3960 
LRYITISGNR VIDAAKSCSK RDSDRIGKDS VETSATHREV QTKLDQVTDR FRSLYSKCSV 

      3970       3980       3990       4000       4010       4020 
LGNNLKDLVD QYQQYEDASC GLLSGLQACE AKASKHLREP IALDPKNLQR QLEETKALQG 

      4030       4040       4050       4060       4070       4080 
QISSQQVAVE KLKKTAEVLL DAKGSLLPAK NDIQKTLDDI VGRYDDLSKC VNERNEKLQI 

      4090       4100       4110       4120       4130       4140 
TLTRSLSVQD ALDEMLDWMG SVESSLVKPG QVPLNSTALQ DLISKDTMLE QDITGRQSSI 

      4150       4160       4170       4180       4190       4200 
NAMNEKVKTF IETTDPSTAS SLQAKMKDLS ARFSEASQKH KEKLAKMVEL KAKVEQFEKL 

      4210       4220       4230       4240       4250       4260 
SDKLQTFLET QSQALTEVAM PGKDVPELSQ HMQESTAKFL EHRKDLEALH SLLKEISSHG 

      4270       4280       4290       4300       4310       4320 
LPGDKALVFE KTNNLSRKFK EMEDTIQEKK DALSSCQEQL SAFQTLAQSL KTWIKETTKQ 

      4330       4340       4350       4360       4370       4380 
VPVVKPSLGT EDLRKSLEET KKLQEKWNLK APEIHKASNS GVSLCNLLSA LISPAKAIAA 

      4390       4400       4410       4420       4430       4440 
AKSGGVILNG EGTDTNTQDF LANKGLTSIK KDMTDISHSY EDLGLLLKDK IVELNTKLSK 

      4450       4460       4470       4480       4490       4500 
LQKAQEESSA MMQWLEKMNK TASRWRQTPT PADTESVKLQ VEQNKSFEAE LKQNVNKVQE 

      4510       4520       4530       4540       4550       4560 
LKDKLSELLE ENPEAPEAQS WKQALAEMDT KWQELNQLTM DRQQKLEESS NNLTQFQTTE 

      4570       4580       4590       4600       4610       4620 
AQLKQWLMEK ELMVSVLGPL SIDPNMLNTQ KQQVQILLQE FDTRKPQYEQ LTAAGQGILS 

      4630       4640       4650       4660       4670       4680 
RPGEDPSLHG IVNEQLEAVT QKWDNLTGQL RDRCDWIDQA IVKSTQYQSL LRSLSGTLTE 

      4690       4700       4710       4720       4730       4740 
LDDKLSSGLT SGALPDAVNQ QLEAAQRLKQ EIEQQAPKIK EAQEVCEDLS ALVKEEYLKA 

      4750       4760       4770       4780       4790       4800 
ELSRQLEGIL KSFKDIEQKT ENHVQHLQSA CASSHQFQQM SKDFQAWLDA KKEEQRDSPP 

      4810       4820       4830       4840       4850       4860 
ISAKLDVLES LLNSQKDFGK TFTEQSNIYE KTISEGENLL LKTQGAEKAA LQLQLNTMKT 

      4870       4880       4890       4900       4910       4920 
DWDRFRKQVK EREEKLKDSL EKALKYREQV ETLRPWIDRC QHSLDGVTFS LDPTESESSI 

      4930       4940       4950       4960       4970       4980 
AELKSLQKEM DHHFGMLELL NNTANSLLSV CEVDKEAVTE ENQSLMEKVN RVTEQLQSKT 

      4990       5000       5010       5020       5030       5040 
VSLENMAQKF KEFQEVSRDT QRQLQDTKEQ LEVHHSLGPQ AYSNKHLSVL QAQQKSLQTL 

      5050       5060       5070       5080       5090       5100 
KQQVDEAKRL AQDLVVEAAD SKGTSDVLLQ AETLAEEHSE LSQQVDEKCS FLETKLQGLG 

      5110       5120       5130       5140       5150       5160 
HFQNTIREMF SQFTECDDEL DGMAPVGRDA ETLRKQKACM QTFLKKLEAL MASNDSANRT 

      5170       5180       5190       5200       5210       5220 
CKMMLATEET SPDLIGVKRD LEALSKQCNK LLDRAKTREE QVDGATEKLE EFHRKLEEFS 

      5230       5240       5250       5260       5270       5280 
TLLQKAEEHE ESQGPVGTET ETINQQLDVF KVFQKEEIEP LQVKQQDVNW LGQGLIQSAA 

      5290       5300       5310       5320       5330       5340 
ANTCTQGLEH DLDSVNSRWK TLNKKVAQRT SQLQEALLHC GRFQDALESL LSWMADTEEL 

      5350       5360       5370       5380       5390       5400 
VANQKPPSAE FKVVKAQIQE QKLLQRLLED RKSTVEVIKR EGEKIAASAE PADRVKLTRQ 

      5410       5420       5430       5440       5450       5460 
LSLLDSRWEA LLSRAEARNR QLEGISVVAQ EFHGTLEPLN EWLTAVEKKL ANSEPIGTQA 

      5470       5480       5490       5500       5510       5520 
PKLEEQISQH KALQEDILLR KQSVDQALLN GLELLKQTTG DEVLIIQDKL EAIKARYKDI 

      5530       5540       5550       5560       5570       5580 
TKLSADVAKT LEHALQLAGQ LQSMHKELCN WLDKVEVELL SYETQGLKGE AASQVQERQK 

      5590       5600       5610       5620       5630       5640 
ELKNEVRSNK ALVDSLNEVS SALLELVPCR AKEGLEKTIA DDNEPLPDCE PTQSRHKVEE 

      5650       5660       5670       5680       5690       5700 
IDAAILRSQQ FEQAADAELS WITETQKKLM SLGDIRLEQD QTSAQLQVQK AFTMDILRHK 

      5710       5720       5730       5740       5750       5760 
DIIDELVTSG HKIMTTSGEE EKQSMKKKLD KVLKKYDAVC QINSERHLQL ERAQSLVSQF 

      5770       5780       5790       5800       5810       5820 
WETYEELWPW LTETQRIISQ LPAPALEYET FERQQEEHRQ LRELIAEHKP HIDKMNKTGP 

      5830       5840       5850       5860       5870       5880 
QLLELSPKEG IYIQEKYVAA DTLYSQIKED VKKRAVVLDE AISQSTQFHD KIDQILESLE 

      5890       5900       5910       5920       5930       5940 
RIAERLRQPP SISAEVEKIK EQIGENKSVS VDMEKLQPLY ETLRQRGEEM IARSEGTEKD 

      5950       5960       5970       5980       5990       6000 
VSARAVQDKL DQMVFIWGSI HTLVEEREAK LLDVMELAEK FWCDHMSLVV TIKDTQDFIR 

      6010       6020       6030       6040       6050       6060 
DLEDPGIDPS VVKQQQEAAE AIREEIDGLQ EELDMVITLG SELIAACGEP DKPIVKKSID 

      6070       6080       6090       6100       6110       6120 
ELNSAWDSLN KAWKDRVDRL EEAMQAAVQY QDGLQGIFDW VDIAGDKLAT MSPIGTDLET 

      6130       6140       6150       6160       6170       6180 
VKQQIEELKQ FKSEAYQQQM EMERLNHQAE LLLKKVTEEA DKHTVQDPLM ELKLIWDSLD 

      6190       6200       6210       6220       6230       6240 
ERIVSRQHKL EGTLLALGQF QHALDELLAW LTHTKGLLSE QKPVGGDPKA IEIELAKHHV 

      6250       6260       6270       6280       6290       6300 
LQNDVLAHQS TVEAVNKAGN DLIESSEGEE ASNLQYKLRI LNQRWQDILE KTDQRKQQLD 

      6310       6320       6330       6340       6350       6360 
SALRQAKGFH GEIEDLQQWL TDTERHLLAS KPLGGLPETA KEQLNAHMEV CTAFAIKEET 

      6370       6380       6390       6400       6410       6420 
YKSLMLRGQQ MLARCPRSAE TNIDQDITNL KEKWESVKSK LNEKKTKLEE ALHLAMNFHN 

      6430       6440       6450       6460       6470       6480 
SLQDFINWLT QAEQTLNVAS RPSLILDTIL FQIDEHKVFA NEVNSHREQI IELDKTGTHL 

      6490       6500       6510       6520       6530       6540 
KYFSQKQDVV LIKNLLISVQ SRWEKVVQRL VERGRSLDEA RKRAKQFHEA WSKLMEWLEE 

      6550       6560       6570       6580       6590       6600 
SEKSLDSELE IANDPDKIKA QLVQHKEFQK SLGGKHSVYD TTNRTGRSLK EKTSLADDNL 

      6610       6620       6630       6640       6650       6660 
KLDNMLSELR DKWDTICGKS VERQNKLEEA LLFSGQFTDA LQALIDWLYR VEPQLAEDQP 

      6670       6680       6690       6700       6710       6720 
VHGDIDLVMS LIDNHKVFQK ELGKRTSSVQ ALKRSARELI EGSRDDSSWV RVQMQELSTR 

      6730       6740       6750       6760       6770       6780 
WETVCALSIS KQTRLESALQ QAEEFHSVVH TLLEWLAEAE QTLRFHGALP DDEDALRTLI 

      6790       6800       6810       6820       6830       6840 
EQHKEFMKRL EEKRAELSKA TGMGDALLAV CHPDSITTIK HWITIIQARF EEVLAWAKQH 

      6850       6860       6870       6880       6890       6900 
QQRLAGALAG LIAKQELLET LLAWLQWAET TLTEKDKEVI PQEIEEVKTL IAEHQTFMEE 

      6910       6920       6930       6940       6950       6960 
MTRKQPDVDK VTKTYKRRAT DPPSLQSHIP VLDKGRAGRK RFPASGFYPS GSQTQIETKN 

      6970       6980       6990       7000       7010       7020 
PRVNLLVSKW QQVWLLALER RRKLNDALDR LEELREFANF DFDIWRKKYM RWMNHKKSRV 

      7030       7040       7050       7060       7070       7080 
MDFFRRIDKD QDGKITRQEF IDGILSSKFP TSRLEMSAVA DIFDRDGDGY IDYYEFVAAL 

      7090       7100       7110       7120       7130       7140 
HPNKDAYKPI TDADKIGDEV TRQVAKCKCA KRFQVEQIGD NKYRFFLGNQ FGDSQQLRLV 

      7150       7160       7170       7180       7190       7200 
RILRSTVMVR VGGGWMALDE FLVKNDPCRV HHHGSKMLRS ESNSSITATQ PTLAKGRTNM 

      7210       7220       7230       7240       7250       7260 
ELREKFILAD GASQGMAAFR PRGRRSRPSS RGASPNRSTS GSSHACQAAS PPVPAAASTP 

      7270       7280       7290       7300       7310       7320 
KGTPIQGSKL RLPGYLSGKG FHSGEDSALI TTAAARVRTQ FAESRKTPSR PGSRAGSKAG 

      7330       7340       7350       7360       7370       7380 
SRASSRRGSD ASDFDISEIQ SVCSDVETVP QTHRPVPRAG SRPSTAKPSK IPTPQRRSPA 


SKLDKSSKR 

« Hide

Isoform 1 (BPAG1-a) (BPAG1a2) [UniParc].

Checksum: E13CE8D1208B2BD5
Show »

FASTA5,380614,927
Isoform 3 [UniParc].

Checksum: B35C8666379E4313
Show »

FASTA7,396834,373
Isoform 4 [UniParc].

Checksum: 23266E5A1EF3BFED
Show »

FASTA7,402835,080
Isoform 5 (BPAG1-e) [UniParc].

Checksum: 56CA2AC3D1215E91
Show »

FASTA2,611301,692
Isoform 6 (BPAG1n) (BPAG1-n1) (BPAG1-n2) (BPAG1a2) (dystonin-2) [UniParc].

Checksum: A40496BA1F6125BD
Show »

FASTA48255,058
Isoform 7 (BPAG1a3) [UniParc].

Checksum: 7258EC5F1E2DA4E7
Show »

FASTA38842,618

References

« Hide 'large scale' references
[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]"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.
[3]"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.
[4]"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.
[5]"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.
[6]"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. expand/collapse author list , 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 6693-7389 (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 6870-7389 (ISOFORM 4).
Strain: C57BL/6J.
Tissue: Fetal skin and Fetal spinal cord.
[7]"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.
[8]"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.
[9]"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.
[10]"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.
[11]"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.
[12]"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.
[13]"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.
[14]"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.
[15]"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.
[16]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[17]"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.
[18]"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.
[19]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF396877 mRNA. Translation: AAK83382.1.
AF396878 mRNA. Translation: AAK83383.1.
AF396879 mRNA. Translation: AAK83384.1.
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.
PIRA60776.
I49290.
I49298.
UniGeneMm.336625.
Mm.478284.
Mm.487428.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2IAKX-ray3.00A580-803[»]
ProteinModelPortalQ91ZU6.
SMRQ91ZU6. Positions 31-255, 268-479, 583-1051, 1553-1927, 4476-4570, 5208-5532, 6115-6480, 7098-7170.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ91ZU6. 5 interactions.
MINTMINT-1861530.
STRING10090.ENSMUSP00000095392.

Chemistry

ChEMBLCHEMBL2176789.

2D gel databases

REPRODUCTION-2DPAGEIPI00230689.
IPI00230690.
IPI00284272.

Proteomic databases

MaxQBQ91ZU6.
PaxDbQ91ZU6.
PRIDEQ91ZU6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

UCSCuc007aof.1. mouse. [Q91ZU6-6]

Organism-specific databases

MGIMGI:104627. Dst.

Phylogenomic databases

eggNOGCOG5069.
HOVERGENHBG031127.
PhylomeDBQ91ZU6.

Gene expression databases

CleanExMM_DST.
GenevestigatorQ91ZU6.

Family and domain databases

Gene3D1.10.238.10. 1 hit.
1.10.418.10. 2 hits.
3.30.920.20. 1 hit.
3.90.1290.10. 3 hits.
InterProIPR001589. 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]
PfamPF00307. CH. 2 hits.
PF13499. EF-hand_7. 1 hit.
PF02187. GAS2. 1 hit.
PF00681. Plectin. 5 hits.
PF00435. Spectrin. 18 hits.
[Graphical view]
SMARTSM00033. CH. 2 hits.
SM00054. EFh. 2 hits.
SM00243. GAS2. 1 hit.
SM00250. PLEC. 9 hits.
SM00150. SPEC. 32 hits.
[Graphical view]
SUPFAMSSF143575. SSF143575. 1 hit.
SSF47576. SSF47576. 1 hit.
SSF75399. SSF75399. 2 hits.
PROSITEPS00019. 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]
ProtoNetSearch...

Other

ChiTaRSDST. mouse.
EvolutionaryTraceQ91ZU6.
NextBio284082.
PROQ91ZU6.
SOURCESearch...

Entry information

Entry nameDYST_MOUSE
AccessionPrimary (citable) accession number: Q91ZU6
Secondary accession number(s): Q1KP04 expand/collapse secondary AC list , Q3I6J6, Q60824, Q60845, Q8K5D4, Q91ZU7, Q91ZU8, Q9WU50
Entry history
Integrated into UniProtKB/Swiss-Prot: April 30, 2003
Last sequence update: December 1, 2001
Last modified: July 9, 2014
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot