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Q91ZU6

- DYST_MOUSE

UniProt

Q91ZU6 - DYST_MOUSE

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Protein

Dystonin

Gene

Dst

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.
Isoform 5: plays a structural role in the assembly of hemidesmosomes of epithelial cells; anchors keratin-containing intermediate filaments to the inner plaque of hemidesmosomes. Required for the regulation of keratinocyte polarity and motility; mediates integrin ITGB4 regulation of RAC1 activity.
Isoform 6: required for bundling actin filaments around the nucleus.

Regions

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

GO - Molecular functioni

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

Enzyme and pathway databases

ReactomeiREACT_199046. Assembly of collagen fibrils and other multimeric structures.
REACT_262098. Type I hemidesmosome assembly.

Names & Taxonomyi

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

Organism-specific databases

MGIiMGI:104627. Dst.

Subcellular locationi

Cytoplasmcytoskeleton. Cell projectionaxon. Membrane
Note: Associates with axonal microtubules at the growing distal tip and intermediate filaments, but not with actin cytoskeleton, in sensory neurons (By similarity). Associates with intermediate filaments, acin and microtubule cytoskeletons. Localizes to actin stress fibers and to actin-rich ruffling at the cortex of cells.By similarity
Isoform 1 : Cytoplasmcytoskeleton 1 Publication
Note: Colocalizes both cortical and cytoplasmic actin filaments.
Isoform 2 : Cell membranesarcolemma. CytoplasmmyofibrilsarcomereZ line. CytoplasmmyofibrilsarcomereH zone. Cytoplasmcytoskeleton
Note: Localizes to microtubules and actin microfilaments throughout the cytoplasm and at focal contact attachments at the plasma membrane.
Isoform 5 : Cytoplasmcytoskeleton. Cell junctionhemidesmosome
Note: Colocalizes with the epidermal KRT5-KRT14 intermediate filaments network of keratins. Colocalizes with ITGB4 at the leading edge of migrating keratinocytes (By similarity). Localizes to actin and intermediate filaments cytoskeletons.By similarity
Isoform 6 : Nucleus. Nucleus envelope. Membrane; Single-pass membrane protein. Endoplasmic reticulum membrane; Single-pass membrane protein. Cytoplasmcytoskeleton
Note: Associates with actin cytoskeleton in sensory neurons (By similarity). Localizes to actin and intermediate filaments cytoskeletons. Localizes to central actin stress fibers around the nucleus and is excluded form focal contact sites in myoblast cells. Translocates to the nucleus.By similarity

GO - Cellular componenti

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

Keywords - Cellular componenti

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

Pathology & Biotechi

Disruption phenotypei

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

Mutagenesis

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

PTM / Processingi

Molecule processing

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

Amino acid modifications

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

Keywords - PTMi

Lipoprotein, Myristate, Palmitate, Phosphoprotein

Proteomic databases

MaxQBiQ91ZU6.
PaxDbiQ91ZU6.
PRIDEiQ91ZU6.

2D gel databases

REPRODUCTION-2DPAGEIPI00230689.
IPI00230690.
IPI00284272.

Expressioni

Tissue specificityi

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

Developmental stagei

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

Gene expression databases

BgeeiE9PXE5.
CleanExiMM_DST.
GenevestigatoriQ91ZU6.

Interactioni

Subunit structurei

Homodimer. Interacts with MAPRE1; probably required for targeting to the growing microtubule plus ends. Isoform 2 interacts (via N-terminus) with ACTN2. Isoform 2 interacts (via N-terminus) with PLEC (via N-terminus). Isoform 5 interacts (via N-terminus) with COL17A1 (via cytoplasmic region). Isoform 5 interacts (via N-terminus) with ITGB4 isoform beta-4a (via cytoplasmic region). Isoform 5 interacts (via N-terminus) with ERBB2IP (via C-terminus). Isoform 5 associates (via C-terminal) with KRT5-KRT14 (via rod region) intermadiate filaments of keratins (By similarity). Isoform 2 and isoform 6 can homodimerize (via N-terminus). Isoform 2 interacts (via N-terminus) with PLEC (via N-terminus). Interacts with the neuronal intermediate filament protein, PRPH. Interacts with DES. Interacts with SYNE3.By similarity4 Publications

Binary interactionsi

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

Protein-protein interaction databases

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

Structurei

Secondary structure

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

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ91ZU6.

Family & Domainsi

Domains and Repeats

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

Motif

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

Compositional bias

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

Domaini

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

Sequence similaritiesi

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

Keywords - Domaini

Coiled coil, Repeat, SH3 domain, Transmembrane

Phylogenomic databases

eggNOGiCOG5069.
GeneTreeiENSGT00760000119163.
HOVERGENiHBG031127.
InParanoidiQ91ZU6.
OrthoDBiEOG76738T.

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. 33 hits.
[Graphical view]
SUPFAMiSSF143575. SSF143575. 1 hit.
SSF47576. SSF47576. 1 hit.
SSF75399. SSF75399. 2 hits.
PROSITEiPS00019. ACTININ_1. 1 hit.
PS00020. ACTININ_2. 1 hit.
PS50021. CH. 2 hits.
PS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 2 hits.
PS51460. GAR. 1 hit.
[Graphical view]

Sequences (7)i

Sequence statusi: Complete.

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

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

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

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

« Hide

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

Also known as: BPAG1-a, BPAG1a2

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

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

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

Note: No experimental confirmation available.Curated

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

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

Note: No experimental confirmation available.Curated

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

Also known as: BPAG1-e

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

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

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

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

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

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

Also known as: BPAG1a3

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

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

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

Sequence cautioni

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

Experimental Info

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

Alternative sequence

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

Sequence databases

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

Genome annotation databases

EnsembliENSMUST00000097785; ENSMUSP00000095392; ENSMUSG00000026131. [Q91ZU6-1]
ENSMUST00000097786; ENSMUSP00000095393; ENSMUSG00000026131. [Q91ZU6-2]
ENSMUST00000183302; ENSMUSP00000138376; ENSMUSG00000026131. [Q91ZU6-5]
GeneIDi13518.
UCSCiuc007aof.1. mouse. [Q91ZU6-6]

Keywords - Coding sequence diversityi

Alternative promoter usage, Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF396877 mRNA. Translation: AAK83382.1 . Sequence problems.
AF396878 mRNA. Translation: AAK83383.1 . Sequence problems.
AF396879 mRNA. Translation: AAK83384.1 . Sequence problems.
AC123072 Genomic DNA. No translation available.
AC124386 Genomic DNA. No translation available.
AC127433 Genomic DNA. No translation available.
U22452 mRNA. Translation: AAC52230.1 .
U25158 mRNA. Translation: AAC52231.1 . Frameshift.
DQ023311 mRNA. Translation: AAY46942.1 .
DQ463750 mRNA. Translation: ABF00406.1 .
AK051626 mRNA. Translation: BAC34695.1 .
AK037206 mRNA. Translation: BAC29753.1 .
AF115383 mRNA. Translation: AAD22959.1 .
AB085694 mRNA. Translation: BAB93448.1 .
CCDSi CCDS35534.1. [Q91ZU6-1 ]
CCDS35535.1. [Q91ZU6-2 ]
CCDS69875.1. [Q91ZU6-5 ]
PIRi A60776.
I49290.
I49298.
RefSeqi NP_034211.2. NM_010081.2. [Q91ZU6-5 ]
NP_598594.2. NM_133833.3. [Q91ZU6-2 ]
NP_604443.2. NM_134448.3. [Q91ZU6-1 ]
UniGenei Mm.336625.
Mm.478284.
Mm.487428.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2IAK X-ray 3.00 A 580-803 [» ]
ProteinModelPortali Q91ZU6.
SMRi Q91ZU6. Positions 31-255, 583-795.
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

Ensembli ENSMUST00000097785 ; ENSMUSP00000095392 ; ENSMUSG00000026131 . [Q91ZU6-1 ]
ENSMUST00000097786 ; ENSMUSP00000095393 ; ENSMUSG00000026131 . [Q91ZU6-2 ]
ENSMUST00000183302 ; ENSMUSP00000138376 ; ENSMUSG00000026131 . [Q91ZU6-5 ]
GeneIDi 13518.
UCSCi uc007aof.1. mouse. [Q91ZU6-6 ]

Organism-specific databases

CTDi 667.
MGIi MGI:104627. Dst.

Phylogenomic databases

eggNOGi COG5069.
GeneTreei ENSGT00760000119163.
HOVERGENi HBG031127.
InParanoidi Q91ZU6.
OrthoDBi EOG76738T.

Enzyme and pathway databases

Reactomei REACT_199046. Assembly of collagen fibrils and other multimeric structures.
REACT_262098. Type I hemidesmosome assembly.

Miscellaneous databases

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

Gene expression databases

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. 33 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: November 26, 2014
This is version 126 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