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Q91ZU6

- DYST_MOUSE

UniProt

Q91ZU6 - DYST_MOUSE

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Protein
Dystonin
Gene
Dst, Bpag1, Macf2
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Cytoskeletal linker protein. Acts as an integrator of intermediate filaments, actin and microtubule cytoskeleton networks. Required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. The proteins may self-aggregate to form filaments or a two-dimensional mesh. May regulate the organization and stability of the microtubule network of sensory neurons to allow axonal transport.4 Publications
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.4 Publications
Isoform 6: required for bundling actin filaments around the nucleus.4 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi7032 – 7043121 Reviewed prediction
Add
BLAST
Calcium bindingi7068 – 7079122 Reviewed prediction
Add
BLAST

GO - Molecular functioni

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

GO - Biological processi

  1. axonogenesis Source: MGI
  2. cell adhesion Source: UniProtKB-KW
  3. cell cycle arrest Source: InterPro
  4. cytoplasmic microtubule organization Source: MGI
  5. intermediate filament cytoskeleton organization Source: UniProtKB
  6. intracellular transport Source: UniProtKB
  7. regulation of microtubule polymerization or depolymerization Source: MGI
  8. retrograde axon cargo transport Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Muscle protein

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Actin-binding, Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Dystonin
Alternative name(s):
Bullous pemphigoid antigen 1
Short name:
BPA
Dystonia musculorum protein
Hemidesmosomal plaque protein
Microtubule actin cross-linking factor 2
Gene namesi
Name:Dst
Synonyms:Bpag1, Macf2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Unplaced

Organism-specific databases

MGIiMGI:104627. Dst.

Subcellular locationi

Cytoplasmcytoskeleton. Cell projectionaxon. Membrane
Note: Associates with axonal microtubules at the growing distal tip and intermediate filaments, but not with actin cytoskeleton, in sensory neurons By similarity. Associates with intermediate filaments, acin and microtubule cytoskeletons. Localizes to actin stress fibers and to actin-rich ruffling at the cortex of cells.8 Publications
Isoform 1 : Cytoplasmcytoskeleton
Note: Colocalizes both cortical and cytoplasmic actin filaments.8 Publications
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.8 Publications
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.8 Publications
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.8 Publications
Isoform 7 : Cytoplasmcytoskeleton. Cytoplasmcell cortex. Cell membrane; Lipid-anchor 8 Publications

GO - Cellular componenti

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

Keywords - Cellular componenti

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

Pathology & Biotechi

Disruption phenotypei

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

Mutagenesis

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 73937393Dystonin
PRO_0000078141Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Lipoprotein, Myristate, Palmitate, Phosphoprotein

Proteomic databases

MaxQBiQ91ZU6.
PaxDbiQ91ZU6.
PRIDEiQ91ZU6.

2D gel databases

REPRODUCTION-2DPAGEIPI00230689.
IPI00230690.
IPI00284272.

Expressioni

Tissue specificityi

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

Developmental stagei

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

Gene expression databases

ArrayExpressiE9PXE5.
BgeeiE9PXE5.
CleanExiMM_DST.
GenevestigatoriQ91ZU6.

Interactioni

Subunit structurei

Homodimer. Interacts with MAPRE1; probably required for targeting to the growing microtubule plus ends. Isoform 2 interacts (via N-terminus) with ACTN2. Isoform 2 interacts (via N-terminus) with PLEC (via N-terminus). Isoform 5 interacts (via N-terminus) with COL17A1 (via cytoplasmic region). Isoform 5 interacts (via N-terminus) with ITGB4 isoform beta-4a (via cytoplasmic region). Isoform 5 interacts (via N-terminus) with ERBB2IP (via C-terminus). Isoform 5 associates (via C-terminal) with KRT5-KRT14 (via rod region) intermadiate filaments of keratins By similarity. Isoform 2 and isoform 6 can homodimerize (via N-terminus). Isoform 2 interacts (via N-terminus) with PLEC (via N-terminus). Interacts with the neuronal intermediate filament protein, PRPH. Interacts with DES. Interacts with SYNE3.5 Publications

Binary interactionsi

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

Protein-protein interaction databases

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

Structurei

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ91ZU6.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini35 – 252218Actin-binding
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BLAST
Domaini35 – 138104CH 1
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BLAST
Domaini151 – 252102CH 2
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BLAST
Repeati701 – 801101Spectrin 1
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BLAST
Domaini889 – 94153SH3
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BLAST
Repeati1582 – 162443Plectin 1
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BLAST
Repeati1657 – 170145Plectin 2
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BLAST
Repeati1772 – 181544Plectin 3
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BLAST
Repeati1816 – 184429Plectin 4
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BLAST
Repeati1848 – 188942Plectin 5
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BLAST
Repeati3850 – 393081Spectrin 2
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BLAST
Repeati4002 – 408483Spectrin 3
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BLAST
Repeati4445 – 4553109Spectrin 4
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BLAST
Repeati4557 – 4662106Spectrin 5
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BLAST
Repeati4780 – 4882103Spectrin 6
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BLAST
Repeati5213 – 5320108Spectrin 7
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BLAST
Repeati5327 – 5428102Spectrin 8
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BLAST
Repeati5435 – 5537103Spectrin 9
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BLAST
Repeati5651 – 5755105Spectrin 10
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BLAST
Repeati5762 – 586099Spectrin 11
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BLAST
Repeati6006 – 608681Spectrin 12
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BLAST
Repeati6093 – 6195103Spectrin 13
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BLAST
Repeati6201 – 6304104Spectrin 14
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BLAST
Repeati6312 – 6414103Spectrin 15
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BLAST
Repeati6419 – 6523105Spectrin 16
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BLAST
Repeati6527 – 6633107Spectrin 17
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BLAST
Repeati6640 – 6740101Spectrin 18
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BLAST
Repeati6745 – 6848104Spectrin 19
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BLAST
Domaini7019 – 705436EF-hand 1
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BLAST
Domaini7055 – 709036EF-hand 2
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BLAST
Domaini7095 – 717379GAR
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BLAST

Motif

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

Compositional bias

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

Domaini

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

Sequence similaritiesi

Belongs to the plakin or cytolinker family.By similarity
Contains 2 EF-hand domains.
Contains 1 GAR domain.
Contains 5 plectin repeats.
Contains 1 SH3 domain.
Contains 19 spectrin repeats.

Keywords - Domaini

Coiled coil, Repeat, SH3 domain, Transmembrane

Phylogenomic databases

eggNOGiCOG5069.
HOVERGENiHBG031127.
OrthoDBiEOG76738T.
PhylomeDBiQ91ZU6.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
1.10.418.10. 2 hits.
3.30.920.20. 1 hit.
3.90.1290.10. 3 hits.
InterProiIPR001589. Actinin_actin-bd_CS.
IPR001715. CH-domain.
IPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR003108. GAS2_dom.
IPR001101. Plectin_repeat.
IPR018159. Spectrin/alpha-actinin.
IPR002017. Spectrin_repeat.
[Graphical view]
PfamiPF00307. CH. 2 hits.
PF13499. EF-hand_7. 1 hit.
PF02187. GAS2. 1 hit.
PF00681. Plectin. 5 hits.
PF00435. Spectrin. 18 hits.
[Graphical view]
SMARTiSM00033. CH. 2 hits.
SM00054. EFh. 2 hits.
SM00243. GAS2. 1 hit.
SM00250. PLEC. 9 hits.
SM00150. SPEC. 32 hits.
[Graphical view]
SUPFAMiSSF143575. SSF143575. 1 hit.
SSF47576. SSF47576. 1 hit.
SSF75399. SSF75399. 2 hits.
PROSITEiPS00019. ACTININ_1. 1 hit.
PS00020. ACTININ_2. 1 hit.
PS50021. CH. 2 hits.
PS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 2 hits.
PS51460. GAR. 1 hit.
[Graphical view]

Sequences (7)i

Sequence statusi: Complete.

This entry describes 7 isoformsi produced by alternative promoter usage and alternative splicing. Align

Isoform 21 Publication (identifier: Q91ZU6-1) [UniParc]FASTAAdd to Basket

Also known as: BPAG1-b, BPAG1a1, dystonin-1

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

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MAGYLSPAAY MYVEEQEYLQ AYEDVLERYK DERDKVQKKT FTKWINQHLM     50
KVRKHVNDLY EDLRDGHNLI SLLEVLSGDT LPREKGRMRF HRLQNVQIAL 100
DYLKRRQVKL VNIRNDDITD GNPKLTLGLI WTIILHFQIS DIHVTGESED 150
MSAKERLLLW TQQATEGYAG VRCENFTTCW RDGKLFNAII HKYRPDLIDM 200
NTVAVQSNLA NLEHAFYVAE KIGVIRLLDP EDVDVSSPDE KSVITYVSSL 250
YDAFPKVPEG GEGIGANDVE VKWIEYQNMV NYLIQWIRHH VVTMSERTFP 300
NNPLELKALY NQYLQFKEKE IPPKEMEKSK IKRLYKLLEI WIEFGRIKLL 350
QGYHPNDIEK EWGKLIIAML EREKALRPEV ERLDMLQQIA TRVQRDSVSC 400
EDKLILARNA LQSDSKRLES GVQFQNEAEI AGYILECENL LRQHVIDVQI 450
LIDGKYYQAD QLVQRVAKLR DEIMALRNEC SSVYSKGRML TTEQTKLMIS 500
GITQSLNSGF AQTLHPSLNS GLTQSLTPSL TSSSVTSGLS SGMTSRLTPS 550
VTPVYAPGFP SVVAPNFSLG VEPNSLQTLK LMQIRKPLLK SSLLDQNLTE 600
EEVNMKFVQD LLNWVDEMQV QLDRTEWGSD LPSVESHLEN HKNVHRAIEE 650
FESSLKEAKI SEIQMTAPLK LSYTDKLHRL ESQYAKLLNT SRNQERHLDT 700
LHNFVTRATN ELIWLNEKEE SEVAYDWSER NSSVARKKSY HAELMRELEQ 750
KEESIKAVQE IAEQLLLENH PARLTIEAYR AAMQTQWSWI LQLCQCVEQH 800
IQENSAYFEF FNDAKEATDY LRNLKDAIQR KYSCDRSSSI HKLEDLVQES 850
MEKEELLQYR SVVAGLMGRA KTVVQLKPRN PDNPLKTSIP IKAICDYRQI 900
EITIYKDDEC VLANNSHRAK WKVISPTGNE AMVPSVCFTV PPPNKEAVDF 950
ANRIEQQYQS VLTLWHESHI NMKSVVSWHY LVNEIDRIRA SNVASIKTML 1000
PGEHQQVLSN LQSRLEDFLE DSQESQIFSG SDISQLEKEV SVCRKYYQEL 1050
LKSAEREEQE ESVYNLYISE VRNIRLRLES CEDRLIRQIR TPLERDDLHE 1100
SMLRITEQEK LKKELDRLKD DLGTITNKCE EFFSQAADSP SVPALRSELS 1150
VVIQSLSQIY SMSSTYIEKL KTVNLVLKNT QAAEALVKLY ETKLCEEEAV 1200
IADKNNIENL MSTLKQWRSE VDEKREVFHA LEDELQKAKA ISDEMFKTHK 1250
ERDLDFDWHK EKADQLVERW QSVHVQIDNR LRDLEGIGKS LKHYRDSYHP 1300
LDDWIQHIET TQRKIQENQP ENSKALALQL NQQKMLVSEI EVKQSKMDEC 1350
QKYSEQYSAA VKDYELQTMT YRAMVESQQK SPVKRRRIQS SADLVIQEFM 1400
DLRTRYTALV TLMTQYIKFA GDSLKRLEEE EKSLDEEKKQ HIEKAKELQK 1450
WVSNISKTLG DGEKAGKPLF SKQQMSSKEI STKKEQFSEA LQTTQIFLAK 1500
HGDKLTEEER SDLEKQVKTL QEGYNLLFSE SLKQQELQPS GESKVPEKPD 1550
KVIAGTINQT TGEVLSVFQA VLRGLIDYET GIRLLEAQLV ITGLISPELR 1600
KCFDLRDAES HGLIDEQVLR QLKELNRAKQ LISTASPTSI PVLDSLAQGM 1650
VSESMAIRVL EILLSAGPLL VPATGEHLTL QQAFQQNLIS SALFSKVLER 1700
QDTCKDLIDP CTSEKVSLTD MVQRSILQEN TRMWLLPVRP QEAGRITLKC 1750
GRSVSILRAA HEGLIDRETM FRLLGAQLLS GGLIDCNSGQ KMTVEEAVAE 1800
GVIDRDTASS ILTYQVQTGG IVHSNPAKRL TVDEAVQCEL ITSSSALLVL 1850
EAQRGYVGLI WPHSGEIFPT SSSLQQELIT NELASKILNG RQKIAALYIP 1900
ESSQVIGLDA AKQLGIIDNN TASVLKSVTL PDKMPDLGDL EDCKNAKRWL 1950
SFCKLQPSTV HDYRQEEGGS DGEEPVTAQS SEQTKKLFLS YLMVNSYMDA 2000
HTGQRLLLYD GDLDEAVGML LESCGTELGA DTSTRESLSV LTIPDAFPDC 2050
ALSEEKHECS AAAAGPDKCH YSHPGHKESL ENAKWDMNEA FCKMGNNDSN 2100
GELPRPENLA DTTVVQKGSE SPSRVRVPKP TSSSTQPEGS VLRPESGSIL 2150
KGCKSQSEPV TKKYPDGANH SHFLTSETSR PCDSNEREDE ENIQKGPSVF 2200
DYSPRLSALL SHDELRQSQG RFSDTSTPQN TGYLCEASTL SPSDQRVLAD 2250
QSTREKFQDQ FLGIAAISVS LQGAPCGQKP VDTECSSSQV HYHSEESMSD 2300
ASAESGATRQ TDESEKTGSK VEDNSCTMVP GGGSRNDNTS DCGPLSHKGA 2350
IDAGDYETSL LAGQQSDTAT DSDSDDYFYD TPLFEDEDHD SLILQGDDRD 2400
CLQPEDYDTS LQEENDRTPP PDDIFYDVMK EKENPEFPHG GMDESLGVEN 2450
KVCCPQGFPV GIEKPELYLA GEKEFNSGGS EQLVESVSES ENPPGLWDSE 2500
SDSLTEGEII GRKERLGASL TPDGHWRGDR EECDTSRESQ SDTDGVGSIQ 2550
SSESYRPYMS DGSDLDEEDN GGRSSEDSGD GRGGQGVADE GGEPQYQADP 2600
TQLYTAIRKE HGGETQNVSD MIPLDKTHSY SPLETQHGAG VFQPESAGRG 2650
GWDTERSSHP ELTTEADEED EASLSTHMAT KGVSLSNAEG TASEEIRLVQ 2700
GPDSTGILKA EDLENVSPEI SPSSDNIVRS EAELGGGASE DGHLSFTGSD 2750
RDQQGPGRGL VKGRDGQSDK LVDETSIREM GFQKEGVLMS SPEEGGEEER 2800
DLEPFPNGSA TESLNMGKSQ VPPLLTHTEE LSHRGAPHTT TMTTTMTLEG 2850
EAKNVQTGLT ESPVLLETLA EIFDTPASKV TRADLTSAVT ASEMKSQVKE 2900
DSLTGGPEKE TGPCTSLGHC DKCIHVDMLE PNEHTPSCAL VAPPTVKDNL 2950
CSVNNAGEKS VRPQEDWPPA AEVRLSDACV EESISEGKAG ILQFTPENSD 3000
STLSRLPHQS VAGWGKSADS VQARLPVSGV RHTSADTLDV GCPQLESSRE 3050
KASAEEEPHR ERALSLKPQE REHHMLGFVE DGRSILKSSL DKVHMNLQEV 3100
GDPSAGTGTK ISIQNLIRRA ILSELPNEVS NVPSHGISPI SNSSEVRAES 3150
GGDPFCITSF LHLLKQNQPP QETPGISELA KVLTQMDCDP EQRGLGSELL 3200
PPQLKNAFYK LLFDGYATEK DQAEALGQTS CAVPKMAEEK PHVCSDLRNK 3250
EGHHCPLNPQ AVGEAEVEPF SVHIAALPGG EKLGELCSEP PEHSESTSGS 3300
KERSSDSSSK EKCSNGLQQC LQHTEKMHEY LVLLQDMKPP LDNQASVESS 3350
LEALKSQLKQ LEAFELGLAP IAVFLRKDLK LAEEFLKSFP SDLPRRHHEE 3400
LSKSHQRLQN AFSSLSSVSS ERMKLIKLAI NSEMSKLAVR HEDFLHKLTS 3450
YSDWVSEKSR SVKAIQTVNV QDTELVKNSV KFLKNVLADL SHTKMQLETT 3500
AFDVQSFISD YAQDLSPSQS RQLLRLLNTT QKGFLDLQEL VTTEADRLEA 3550
LLQLEQELGH QKVVAERQQE YREKLQGLCD LLTQTENRLI SNQEAFVIGD 3600
GTVELQKYQS KQEELQRDMQ GSTQAMEEIV RNTELFLKES GDELSQADRA 3650
LIEQKLNEVK MKCAQLNLKA EQSRKELDKA VTTALKEETE KVAAVRQLEE 3700
SKTKIENLLN WLSNVEEDSE GVWTKHTQPM EQNGTYLHEG DSKLGAGEED 3750
EVNGNLLETD AEGHSEATKG NLNQQYEKVK AQHGKIMAQH QAVLLATQSA 3800
QVLLEKQGHY LSPEEKEKLQ KNTQELKVHY EKVLAECEKK VKLTHSLQEE 3850
LEKFDTDYSE FEHWLQQSEQ ELANLEAGAD DLSGLMDKLT RQKSFSEDVI 3900
SHKGDLRYIT ISGNRVIDAA KSCSKRDSDR IGKDSVETSA THREVQTKLD 3950
QVTDRFRSLY SKCSVLGNNL KDLVDQYQQY EDASCGLLSG LQACEAKASK 4000
HLREPIALDP KNLQRQLEET KALQGQISSQ QVAVEKLKKT AEVLLDAKGS 4050
LLPAKNDIQK TLDDIVGRYD DLSKCVNERN EKLQITLTRS LSVQDALDEM 4100
LDWMGSVESS LVKPGQVPLN STALQDLISK DTMLEQDITG RQSSINAMNE 4150
KVKTFIETTD PSTASSLQAK MKDLSARFSE ASQKHKEKLA KMVELKAKVE 4200
QFEKLSDKLQ TFLETQSQAL TEVAMPGKDV PELSQHMQES TAKFLEHRKD 4250
LEALHSLLKE ISSHGLPGDK ALVFEKTNNL SRKFKEMEDT IQEKKDALSS 4300
CQEQLSAFQT LAQSLKTWIK ETTKQVPVVK PSLGTEDLRK SLEETKKLQE 4350
KWNLKAPEIH KANNSGVSLC NLLSALISPA KAIAAAKSGG VILNGEGTDT 4400
NTQDFLANKG LTSIKKDMTD ISHSYEDLGL LLKDKIVELN TKLSKLQKAQ 4450
EESSAMMQWL EKMNKTASRW RQTPTPADTE SVKLQVEQNK SFEAELKQNV 4500
NKVQELKDKL SELLEENPEA PEAQSWKQAL AEMDTKWQEL NQLTMDRQQK 4550
LEESSNNLTQ FQTTEAQLKQ WLMEKELMVS VLGPLSIDPN MLNTQKQQVQ 4600
ILLQEFDTRK PQYEQLTAAG QGILSRPGED PSLHGIVNEQ LEAVTQKWDN 4650
LTGQLRDRCD WIDQAIVKST QYQSLLRSLS GTLTELDDKL SSGLTSGALP 4700
DAVNQQLEAA QRLKQEIEQQ APKIKEAQEV CEDLSALVKE EYLKAELSRQ 4750
LEGILKSFKD IEQKTENHVQ HLQSACASSH QFQQMSKDFQ AWLDAKKEEQ 4800
RDSPPISAKL DVLESLLNSQ KDFGKTFTEQ SNIYEKTISE GENLLLKTQG 4850
AEKAALQLQL NTMKTDWDRF RKQVKEREEK LKDSLEKALK YREQVETLRP 4900
WIDRCQHSLD GVTFSLDPTE SESSIAELKS LQKEMDHHFG MLELLNNTAN 4950
SLLSVCEVDK EAVTEENQSL MEKVNRVTEQ LQSKTVSLEN MAQKFKEFQE 5000
VSRDTQRQLQ DTKEQLEVHH SLGPQAYSNK HLSVLQAQQK SLQTLKQQVD 5050
EAKRLAQDLV VEAADSKGTS DVLLQAETLA EEHSELSQQV DEKCSFLETK 5100
LQGLGHFQNT IREMFSQFTE CDDELDGMAP VGRDAETLRK QKACMQTFLK 5150
KLEALMASND SANRTCKMML ATEETSPDLI GVKRDLEALS KQCNKLLDRA 5200
KTREEQVDGA TEKLEEFHRK LEEFSTLLQK AEEHEESQGP VGTETETINQ 5250
QLDVFKVFQK EEIEPLQVKQ QDVNWLGQGL IQSAAANTCT QGLEHDLDSV 5300
NSRWKTLNKK VAQRTSQLQE ALLHCGRFQD ALESLLSWMA DTEELVANQK 5350
PPSAEFKVVK AQIQEQKLLQ RLLEDRKSTV EVIKREGEKI AASAEPADRV 5400
KLTRQLSLLD SRWEALLSRA EARNRQLEGI SVVAQEFHET LEPLNEWLTA 5450
VEKKLANSEP IGTQAPKLEE QISQHKALQE DILLRKQSVD QALLNGLELL 5500
KQTTGDEVLI IQDKLEAIKA RYKDITKLSA DVAKTLEHAL QLAGQLQSMH 5550
KELCNWLDKV EVELLSYETQ GLKGEAASQV QERQKELKNE VRSNKALVDS 5600
LNEVSSALLE LVPWRAREGL EKTIAEDNER YRLVSDTITQ KVEEIDAAIL 5650
RSQQFEQAAD AELSWITETQ KKLMSLGDIR LEQDQTSAQL QVQKAFTMDI 5700
LRHKDIIDEL VTSGHKIMTT SSEEEKQSMK KKLDKVLKKY DAVCQINSER 5750
HLQLERAQSL VSQFWETYEE LWPWLTETQR IISQLPAPAL EYETLRRQQE 5800
EHRQLRELIA EHKPHIDKMN KTGPQLLELS PKEGIYIQEK YVAADTLYSQ 5850
IKEDVKKRAV VLDEAISQST QFHDKIDQIL ESLERIAERL RQPPSISAEV 5900
EKIKEQIGEN KSVSVDMEKL QPLYETLRQR GEEMIARSEG TEKDVSARAV 5950
QDKLDQMVFI WGSIHTLVEE REAKLLDVME LAEKFWCDHM SLVVTIKDTQ 6000
DFIRDLEDPG IDPSVVKQQQ EAAEAIREEI DGLQEELDMV ITLGSELIAA 6050
CGEPDKPIVK KSIDELNSAW DSLNKAWKDR VDRLEEAMQA AVQYQDGLQG 6100
IFDWVDIAGN KLATMSPIGT DLETVKQQIE ELKQFKSEAY QQQIEMERLN 6150
HQAELLLKKV TEEADKHTVQ DPLMELKLIW DSLDERIVSR QHKLEGALLA 6200
LGQFQHALDE LLAWLTHTKG LLSEQKPVGG DPKAIEIELA KHHVLQNDVL 6250
AHQSTVEAVN KAGNDLIESS EGEEASNLQY KLRILNQRWQ DILEKTDQRK 6300
QQLDSALRQA KGFHGEIEDL QQWLTDTERH LLASKPLGGL PETAKEQLNA 6350
HMEVCTAFAI KEETYKSLML RGQQMLARCP RSAETNIDQD ITNLKEKWES 6400
VKSKLNEKKT KLEEALHLAM NFHNSLQDFI NWLTQAEQTL NVASRPSLIL 6450
DTILFQIDEH KVFANEVNSH REQIIELDKT GTHLKYFSQK QDVVLIKNLL 6500
ISVQSRWEKV VQRLVERGRS LDEARKRAKQ FHEAWSKLME WLEESEKSLD 6550
SELEIANDPD KIKAQLVQHK EFQKSLGGKH SVYDTTNRTG RSLKEKTSLA 6600
DDNLKLDNML SELRDKWDTI CGKSVERQNK LEEALLFSGQ FTDALQALID 6650
WLYRVEPQLA EDQPVHGDID LVMNLIDNHK VFQKELGKRT SSVQALKRSA 6700
RELIEGSRDD SSWVRVQMQE LSTRWETVCA LSISKQTRLE SALQQAEEFH 6750
SVVHTLLEWL AEAEQTLRFH GALPDDEDAL RTLIEQHKEF MKRLEEKRAE 6800
LSKATGMGDA LLAVCHPDSI TTIKHWITII QARFEEVLAW AKQHQQRLAG 6850
ALAGLIAKQE LLETLLAWLQ WAETTLTEKD KEVIPQEIEE VKTLIAEHQT 6900
FMEEMTRKQP DVDKVTKTYK RRATDPPSLQ SHIPVLDKGR AGRKRFPASG 6950
FYPSGSQTQI ETKNPRVNLL VSKWQQVWLL ALERRRKLND ALDRLEELRE 7000
FANFDFDIWR KKYMRWMNHK KSRVMDFFRR IDKDQDGKIT RQEFIDGILS 7050
SKFPTSRLEM SAVADIFDRD GDGYIDYYEF VAALHPNKDA YKPITDADKI 7100
EDEVTRQVAK CKCAKRFQVE QIGDNKYRFF LGNQFGDSQQ LRLVRILRST 7150
VMVRVGGGWM ALDEFLVKND PCRVHHHGSK MLRSESNSSI TATQPTLAKG 7200
RTNMELREKF ILADGASQGM AAFRPRGRRS RPSSRGASPN RSTSASSHAC 7250
QAASPPVPAA ASTPKGTPIQ GSKLRLPGYL SGKGFHSGED SALITTAAAR 7300
VRTQFAESRK TPSRPGSRAG SKAGSRASSR RGSDASDFDI SEIQSVCSDV 7350
ETVPQTHRPV PRAGSRPSTA KPSKIPTPQR RSPASKLDKS SKR 7393
Length:7,393
Mass (Da):834,218
Last modified:September 3, 2014 - v2
Checksum:iC3CDF88978C33EF1
GO
Isoform 11 Publication (identifier: Q91ZU6-2) [UniParc]FASTAAdd to Basket

Also known as: BPAG1-a, BPAG1a2

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

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

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

Note: No experimental confirmation available.

Show »
Length:7,400
Mass (Da):834,953
Checksum:i80B5A7C7FDA19949
GO
Isoform 4 (identifier: Q91ZU6-4) [UniParc]FASTAAdd to Basket

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

Note: No experimental confirmation available.

Show »
Length:7,406
Mass (Da):835,660
Checksum:iFA78FB01B169CFA7
GO
Isoform 51 Publication (identifier: Q91ZU6-5) [UniParc]FASTAAdd to Basket

Also known as: BPAG1-e

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

Show »
Length:2,639
Mass (Da):304,781
Checksum:i1FB46C15C1834D29
GO
Isoform 6 (identifier: Q91ZU6-6) [UniParc]FASTAAdd to Basket

Also known as: BPAG1n, BPAG1-n1, BPAG1-n2, BPAG1a2, dystonin-2

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

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

Show »
Length:482
Mass (Da):55,058
Checksum:iA40496BA1F6125BD
GO
Isoform 7 (identifier: Q91ZU6-8) [UniParc]FASTAAdd to Basket

Also known as: BPAG1a3

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

Note: Incomplete sequence. Probably myristoylated on Gly-2. Probably S-palmitoylated on Cys-5 and Cys-7. Mutagenesis of Gly-2 to Ala inhibits cortical localization. Mutagenesis of Cys-5 to Ser inhibits cortical localization. Mutagenesis of Cys-7 to Ser inhibits cortical localization.

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

Sequence cautioni

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 381381MAGYL…RPEVE → MQSSSYSYRSSDSVFSNTTS TRTSLDSNENLLSVHCGPTL INSCISFSNESLDGH in isoform 5.
VSP_055459Add
BLAST
Alternative sequencei1 – 137137MAGYL…IILHF → MGNVCGCVRAEKEEPYFDPA KSPLSPEKYSPGRKYFRRKP CQKVVDDTEPVRQSSEREGK KGVSQPAGGQPAVSSGELPW EDPAASPTKEDAVQLGKRAA TEHGDQKPLPSSVDGYPHRV TVSSAQGRYSEVQVSIPDKI ISEEDSPPYCPETERHLDDV NSKHRTFLRKDNVSLSQTAA SSSPILCVTEKSLKNSALMG NLSRSCHSVLEQDSDERGHP FGVHRLQLTKRRCHSLSSGV SCVSKDAPRDDGC in isoform 7.
VSP_041542Add
BLAST
Alternative sequencei1 – 3030MAGYL…LERYK → MIAAAFLVLLRPYSIQCALF LLLLLLGTVATIVFFCCWHR KLQKGRHPMKSVFSGRSRSR DAALRSHHFRSEGFRASPRH IRRRVAAAAAARLEEVKPVV EVHHQSEQESSGRKRRIKKN SRVQPEFYHSVQGASTRRPS SGNASYRCSMSSSADFSDED DFSQKSGSASPAPGDTLPWN LPKHERSKRKIQGGSVLDPA ERAVLRIA in isoform 6.
VSP_041543Add
BLAST
Alternative sequencei271 – 2722VK → KG in isoform 7.
VSP_041544
Alternative sequencei273 – 73937121Missing in isoform 7.
VSP_041545Add
BLAST
Alternative sequencei305 – 73937089Missing in isoform 6.
VSP_041546Add
BLAST
Alternative sequencei1432 – 14321K → MKRSKENSEHGAYSDLLQRQ RATMVENSKLTGKISELETM VAELKKQKSRVEEELPKVKE AAENELRKQQRNVEDIALQK LRAESEAKQYRRELETIVRE KEAAERELERVRQLTAEAEA RRAAVEENLRNFRSQLQENT FTRQTLEDHLRRKDSSLSDL EQQKRALVEELQRKRDHEEE LLRLVKQMERDLAFQKQVAE KQLKEKQKVELEARRKITEI QFSCRESAAVAQARPQREQG RQKEEELKQQVDELTLANRK AEKEMRELKYELSAVQLEKA SSEEKARLLKDKLDETNNTL KCLKEDLERKDQAQERYSQQ LRDLGRQLNQTTDKAEEVRQ EANDLKKIKHTYQLELESLH QEKGKLQREVDRVTRAHALA ERNIQCLNSQVHASRDEKDL SEERRRLCQRKSDHLKEEFE RSHAQLLQNIQAEKENNDKI QKLNKELEKSNECAETLKQK VDELTRQNNETKLMMQRIQA ESKNIVREKQAIQQRCEVLR IQADGFKDQLRNTNEHLHKQ TKTEQDFHRKIKSLEDDLAQ SQNLVSEFKQKCDQQSMIIQ KTEKEVRSLSAELSASKEEK RREEQKAQLQRAQVQELNDR LKRVQDELHLKTIEEQMTHR KMILLQEESDKFKRSADEFR KKMEKLMESKVVTETDLSGI KHDFVSLQRENFRAQENAKL WETNIRELERQLQCYREKMQ QGPPVEANHYQKCRRLEEEL LAQRREVENLKQKMDQQIKE HEHQLLRLQCEIQKKSTTQD HTFASAFDTAGRECHHPAEI SPGNSGHLNLKTRLPLSRWT QEPHQTEGKWPHRAAEQLPK EVQFRQPGAPLDRESSQPCY SEYFSQTSTELQITFDDKNP ITRLSELETMREQALHPSRP PVTYQDDKLERELVKLLTPL EIAKNKQCGMHTEVTTLKQE KRLGSSAGGWMLEGCRTSGG LKGDFLKKSVEPEASPSLDL NQACSVRDEEFQFQGLRHTV TGRQLVEAKLLDMRTVEQLR LGLKTVEEVQRSLSKFLTKA TSIAGLYLESSKEKMSFTSA AQKIIIDKMIALAFLEAQAA TGFIIDPVSGQTYCVEDAVL HGIVDPEFRSRLLEAEKAVL GYSHASKTLSVFQAMENRML DRKKGKHILEAQIASGGVID PVRGVRVPPEMAVQQGLLNN AVLQFLHEPSSNTRVFPNPN NKQALYYSELLQICVFDVDC QCFLLPFGEREISNLNIEKT HKIAVVDTKTGAELTAFEAF QRNLIDKGIYLELSGQQYQW KEATFFDSYGHPSHMLTDTK TGLQFNISEAVEQGTLDKAL VQKYQEGLTTLTELADFLLS KVVPKKDLHSPIAGYWLTAS GERISLLKASRRNLVDRVTA LRCLEAQICTGGIIDPLTGK KYRVAEALHRGLVDEGFAQQ LRQCELVITGISHPVSNKMM SVVEAVNANIISKEMGMRCL EFQYLTGGLIEPKVFSRLTI EEALHVGIIDVLIATRLKDQ KSYVRDIMCPQTKRKLTYKE ALEKADFDFHTGLKLLEVSE PLGTGISNLYYSSQ in isoform 5.
VSP_055460
Alternative sequencei1433 – 73935961Missing in isoform 5.
VSP_055461Add
BLAST
Alternative sequencei1549 – 35622014Missing in isoform 1.
VSP_041549Add
BLAST
Alternative sequencei7129 – 71346Missing in isoform 3.
VSP_041550
Alternative sequencei7174 – 719724Missing in isoform 3 and isoform 4.
VSP_041551Add
BLAST
Alternative sequencei7265 – 72651K → KILHPLTRNYGKPWLANSKM STPCKAAECPDFPVSSAE in isoform 3 and isoform 4.
VSP_041552

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Isoform 6 (identifier: Q91ZU6-6)
Sequence conflicti101 – 1011E → K in AAC52231. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF396877 mRNA. Translation: AAK83382.1. Sequence problems.
AF396878 mRNA. Translation: AAK83383.1. Sequence problems.
AF396879 mRNA. Translation: AAK83384.1. Sequence problems.
AC123072 Genomic DNA. No translation available.
AC124386 Genomic DNA. No translation available.
AC127433 Genomic DNA. No translation available.
U22452 mRNA. Translation: AAC52230.1.
U25158 mRNA. Translation: AAC52231.1. Frameshift.
DQ023311 mRNA. Translation: AAY46942.1.
DQ463750 mRNA. Translation: ABF00406.1.
AK051626 mRNA. Translation: BAC34695.1.
AK037206 mRNA. Translation: BAC29753.1.
AF115383 mRNA. Translation: AAD22959.1.
AB085694 mRNA. Translation: BAB93448.1.
PIRiA60776.
I49290.
I49298.
UniGeneiMm.336625.
Mm.478284.
Mm.487428.

Genome annotation databases

UCSCiuc007aof.1. mouse. [Q91ZU6-6]

Keywords - Coding sequence diversityi

Alternative promoter usage, Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF396877 mRNA. Translation: AAK83382.1 . Sequence problems.
AF396878 mRNA. Translation: AAK83383.1 . Sequence problems.
AF396879 mRNA. Translation: AAK83384.1 . Sequence problems.
AC123072 Genomic DNA. No translation available.
AC124386 Genomic DNA. No translation available.
AC127433 Genomic DNA. No translation available.
U22452 mRNA. Translation: AAC52230.1 .
U25158 mRNA. Translation: AAC52231.1 . Frameshift.
DQ023311 mRNA. Translation: AAY46942.1 .
DQ463750 mRNA. Translation: ABF00406.1 .
AK051626 mRNA. Translation: BAC34695.1 .
AK037206 mRNA. Translation: BAC29753.1 .
AF115383 mRNA. Translation: AAD22959.1 .
AB085694 mRNA. Translation: BAB93448.1 .
PIRi A60776.
I49290.
I49298.
UniGenei Mm.336625.
Mm.478284.
Mm.487428.

3D structure databases

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

Protein-protein interaction databases

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

Chemistry

ChEMBLi CHEMBL2176789.

2D gel databases

REPRODUCTION-2DPAGE IPI00230689.
IPI00230690.
IPI00284272.

Proteomic databases

MaxQBi Q91ZU6.
PaxDbi Q91ZU6.
PRIDEi Q91ZU6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

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

Organism-specific databases

MGIi MGI:104627. Dst.

Phylogenomic databases

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

Miscellaneous databases

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

Gene expression databases

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

Family and domain databases

Gene3Di 1.10.238.10. 1 hit.
1.10.418.10. 2 hits.
3.30.920.20. 1 hit.
3.90.1290.10. 3 hits.
InterProi IPR001589. Actinin_actin-bd_CS.
IPR001715. CH-domain.
IPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR003108. GAS2_dom.
IPR001101. Plectin_repeat.
IPR018159. Spectrin/alpha-actinin.
IPR002017. Spectrin_repeat.
[Graphical view ]
Pfami PF00307. CH. 2 hits.
PF13499. EF-hand_7. 1 hit.
PF02187. GAS2. 1 hit.
PF00681. Plectin. 5 hits.
PF00435. Spectrin. 18 hits.
[Graphical view ]
SMARTi SM00033. CH. 2 hits.
SM00054. EFh. 2 hits.
SM00243. GAS2. 1 hit.
SM00250. PLEC. 9 hits.
SM00150. SPEC. 32 hits.
[Graphical view ]
SUPFAMi SSF143575. SSF143575. 1 hit.
SSF47576. SSF47576. 1 hit.
SSF75399. SSF75399. 2 hits.
PROSITEi PS00019. ACTININ_1. 1 hit.
PS00020. ACTININ_2. 1 hit.
PS50021. CH. 2 hits.
PS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 2 hits.
PS51460. GAR. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The BPAG1 locus: alternative splicing produces multiple isoforms with distinct cytoskeletal linker domains, including predominant isoforms in neurons and muscles."
    Leung C.L., Zheng M., Prater S.M., Liem R.K.H.
    J. Cell Biol. 154:691-697(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 5), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, ALTERNATIVE SPLICING.
    Strain: BALB/c.
    Tissue: Epithelium, Muscle and Neuron.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "The mouse dystonia musculorum gene is a neural isoform of bullous pemphigoid antigen 1."
    Brown A., Bernier G., Mathieu M., Rossant J., Kothary R.
    Nat. Genet. 10:301-306(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-511 (ISOFORM 2), PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    Tissue: Brain.
  4. "A Bpag1 isoform involved in cytoskeletal organization surrounding the nucleus."
    Young K.G., Pinheiro B., Kothary R.
    Exp. Cell Res. 312:121-134(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-304 (ISOFORM 6), ALTERNATIVE SPLICING (ISOFORMS 2 AND 6), SUBCELLULAR LOCATION (ISOFORMS 2 AND 6).
    Strain: C3H.
  5. "Dissecting the sequence specific functions of alternative N-terminal isoforms of mouse bullous pemphigoid antigen 1."
    Jefferson J.J., Leung C.L., Liem R.K.
    Exp. Cell Res. 312:2712-2725(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-270 (ISOFORM 7), ALTERNATIVE SPLICING (ISOFORMS 1; 6 AND 7), FUNCTION OF ISOFORMS 1; 6 AND 7, PALMITOYLATION, MYRISTOYLATION, MUTAGENESIS, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Strain: C57BL/6 X CBA.
  6. "Structural analysis of the plakin domain of bullous pemphigoid antigen1 (BPAG1) suggests that plakins are members of the spectrin superfamily."
    Jefferson J.J., Ciatto C., Shapiro L., Liem R.K.
    J. Mol. Biol. 366:244-257(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 580-584; 1043-1047 AND 1053-1057, X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 580-803.
  7. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 6697-7393 (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 6874-7393 (ISOFORM 4).
    Strain: C57BL/6J.
    Tissue: Fetal skin and Fetal spinal cord.
  8. "The intermediate filament protein peripherin is the specific interaction partner of mouse BPAG1-n (dystonin) in neurons."
    Leung C.L., Sun D., Liem R.K.
    J. Cell Biol. 144:435-446(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), FUNCTION, INTERACTION WITH PRPH.
    Strain: BALB/c.
  9. "Molecular network in NGF-mediated neural differentiation."
    Kubo Y., Ohba M., Iwashita S.
    Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
    Strain: Swiss Webster / NIH.
  10. "Gene targeting of BPAG1: abnormalities in mechanical strength and cell migration in stratified epithelia and neurologic degeneration."
    Guo L., Degenstein L., Dowling J., Yu Q.C., Wollmann R., Perman B., Fuchs E.
    Cell 81:233-243(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING (ISOFORM 5), DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION (ISOFORM 5), TISSUE SPECIFICITY.
  11. "An essential cytoskeletal linker protein connecting actin microfilaments to intermediate filaments."
    Yang Y., Dowling J., Yu Q.C., Kouklis P., Cleveland D.W., Fuchs E.
    Cell 86:655-665(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING (ISOFORMS 5 AND 6), SUBCELLULAR LOCATION (ISOFORMS 5 AND 6), TISSUE SPECIFICITY.
  12. "Integrators of the cytoskeleton that stabilize microtubules."
    Yang Y., Bauer C., Strasser G., Wollman R., Julien J.P., Fuchs E.
    Cell 98:229-238(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  13. "Dystonin-deficient mice exhibit an intrinsic muscle weakness and an instability of skeletal muscle cytoarchitecture."
    Dalpe G., Mathieu M., Comtois A., Zhu E., Wasiak S., De Repentigny Y., Leclerc N., Kothary R.
    Dev. Biol. 210:367-380(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DES, DISRUPTION PHENOTYPE.
  14. "BPAG1n4 is essential for retrograde axonal transport in sensory neurons."
    Liu J.J., Ding J., Kowal A.S., Nardine T., Allen E., Delcroix J.D., Wu C., Mobley W., Fuchs E., Yang Y.
    J. Cell Biol. 163:223-229(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  15. "Bpag1 localization to actin filaments and to the nucleus is regulated by its N-terminus."
    Young K.G., Pool M., Kothary R.
    J. Cell Sci. 116:4543-4555(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING (ISOFORMS 2; 5 AND 6), HOMODIMERIZATION, MUTAGENESIS OF ARG-1385 AND ARG-1386, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  16. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
    Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
    Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  18. "Dystonin/Bpag1 is a necessary endoplasmic reticulum/nuclear envelope protein in sensory neurons."
    Young K.G., Kothary R.
    Exp. Cell Res. 314:2750-2761(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING (ISOFORM 6), INTERACTION WITH SYNE3, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  19. "BPAG1 isoform-b: complex distribution pattern in striated and heart muscle and association with plectin and alpha-actinin."
    Steiner-Champliaud M.F., Schneider Y., Favre B., Paulhe F., Praetzel-Wunder S., Faulkner G., Konieczny P., Raith M., Wiche G., Adebola A., Liem R.K., Langbein L., Sonnenberg A., Fontao L., Borradori L.
    Exp. Cell Res. 316:297-313(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), INTERACTION WITH PLEC, SUBCELLULAR LOCATION (ISOFORMS 1 AND 2), TISSUE SPECIFICITY.
  20. "Hearts of dystonia musculorum mice display normal morphological and histological features but show signs of cardiac stress."
    Boyer J.G., Bhanot K., Kothary R., Boudreau-Lariviere C.
    PLoS ONE 5:E9465-E9465(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING (ISOFORM 2), FUNCTION OF ISOFORM 2, SUBCELLULAR LOCATION (ISOFORM 2), TISSUE SPECIFICITY.

Entry informationi

Entry nameiDYST_MOUSE
AccessioniPrimary (citable) accession number: Q91ZU6
Secondary accession number(s): E9PXE5
, E9QL23, Q1KP04, Q3I6J6, Q60824, Q60845, Q8K5D4, Q91ZU7, Q91ZU8, Q9WU50, S4R1U5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 30, 2003
Last sequence update: September 3, 2014
Last modified: September 3, 2014
This is version 123 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

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

Documents

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

External Data

Dasty 3

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