Q91ZU6 (DYST_MOUSE) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 108.
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Names·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | 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 names |
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| Organism | Mus musculus (Mouse) [Reference proteome] | ||||
| Taxonomic identifier | 10090 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus |
Protein attributes
| Sequence length | 7389 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Cytoskeletal linker protein. Acts as an integrator of intermediate filaments, actin and microtubule cytoskeleton networks. Required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. The proteins may self-aggregate to form filaments or a two-dimensional mesh. May regulate the organization and stability of the microtubule network of sensory neurons to allow axonal transport. Ref.4 Ref.7 Ref.13 Ref.19 Isoform 5: plays a structural role in the assembly of hemidesmosomes of epithelial cells; anchors keratin-containing intermediate filaments to the inner plaque of hemidesmosomes. Required for the regulation of keratinocyte polarity and motility; mediates integrin ITGB4 regulation of RAC1 activity. Ref.4 Ref.7 Ref.13 Ref.19 Isoform 6: required for bundling actin filaments around the nucleus. Ref.4 Ref.7 Ref.13 Ref.19 |
| Subunit structure | Homodimer. Interacts with MAPRE1; probably required for targeting to the growing microtubule plus ends. Isoform 2 interacts (via N-terminus) with ACTN2. Isoform 2 interacts (via N-terminus) with PLEC (via N-terminus). Isoform 5 interacts (via N-terminus) with COL17A1 (via cytoplasmic region). Isoform 5 interacts (via N-terminus) with ITGB4 isoform beta-4a (via cytoplasmic region). Isoform 5 interacts (via N-terminus) with ERBB2IP (via C-terminus). Isoform 5 associates (via C-terminal) with KRT5-KRT14 (via rod region) intermadiate filaments of keratins By similarity. Isoform 2 and isoform 6 can homodimerize (via N-terminus). Isoform 2 interacts (via N-terminus) with PLEC (via N-terminus). Interacts with the neuronal intermediate filament protein, PRPH. Interacts with DES. Interacts with SYNE3. Ref.7 Ref.12 Ref.14 Ref.17 Ref.18 |
| Subcellular location | Cytoplasm › cytoskeleton. Cell projection › axon. Membrane. Note: Associates with axonal microtubules at the growing distal tip and intermediate filaments, but not with actin cytoskeleton, in sensory neurons By similarity. Associates with intermediate filaments, acin and microtubule cytoskeletons. Localizes to actin stress fibers and to actin-rich ruffling at the cortex of cells. Ref.3 Ref.4 Ref.9 Ref.10 Ref.14 Ref.17 Ref.18 Ref.19 Isoform 1: Cytoplasm › cytoskeleton. Note: Colocalizes both cortical and cytoplasmic actin filaments. Ref.3 Ref.4 Ref.9 Ref.10 Ref.14 Ref.17 Ref.18 Ref.19 Isoform 2: Cell membrane › sarcolemma. Cytoplasm › myofibril › sarcomere › Z line. Cytoplasm › myofibril › sarcomere › H zone. Cytoplasm › cytoskeleton. Note: Localizes to microtubules and actin microfilaments throughout the cytoplasm and at focal contact attachments at the plasma membrane. Ref.3 Ref.4 Ref.9 Ref.10 Ref.14 Ref.17 Ref.18 Ref.19 Isoform 5: Cytoplasm › cytoskeleton. Cell junction › hemidesmosome. Note: Colocalizes with the epidermal KRT5-KRT14 intermediate filaments network of keratins. Colocalizes with ITGB4 at the leading edge of migrating keratinocytes By similarity. Localizes to actin and intermediate filaments cytoskeletons. Ref.3 Ref.4 Ref.9 Ref.10 Ref.14 Ref.17 Ref.18 Ref.19 Isoform 6: Nucleus. Nucleus envelope. Membrane; Single-pass membrane protein. Endoplasmic reticulum membrane; Single-pass membrane protein. Cytoplasm › cytoskeleton. Note: Associates with actin cytoskeleton in sensory neurons By similarity. Localizes to actin and intermediate filaments cytoskeletons. Localizes to central actin stress fibers around the nucleus and is excluded form focal contact sites in myoblast cells. Translocates to the nucleus. Ref.3 Ref.4 Ref.9 Ref.10 Ref.14 Ref.17 Ref.18 Ref.19 Isoform 7: Cytoplasm › cytoskeleton. Cytoplasm › cell cortex. Cell membrane; Lipid-anchor Ref.3 Ref.4 Ref.9 Ref.10 Ref.14 Ref.17 Ref.18 Ref.19. |
| Tissue specificity | Isoform 1 and 2 are expressed in striated and heart muscle cells. Isoform 5 is expressed in the skin. Isoform 6 is expressed in sensory neural cells of the dorsal root ganglion and with low level in the skin (at protein level). Isoform 1 is expressed predominantly in the brain and spinal cord with low levels in the heart. Isoform 2 is predominantly expressed in muscle and heart and with low levels in the brain. Isoform 5 is expressed in the skin and with low levels in myoblast cells. Isoform 6 is expressed in neurons. Isoform 7 is expressed in lung and with low levels in the brain. Ref.1 Ref.2 Ref.4 Ref.9 Ref.10 Ref.14 Ref.17 Ref.18 Ref.19 |
| Developmental stage | Isoform 1 is the major form expressed in the dorsal root ganglia at 14.5 dpc. Isoform 2 is predominantly expressed in the myocardium, skeletal muscles, bone cartilage and epithelia of the tongue at 14.5 dpc. Isoform 5 is expressed at high levels in the epidermis and mucosal epithelia of the digestive tracts at 14.5 dpc. Ref.1 Ref.2 |
| Domain | Its association with epidermal and simple keratins is dependent on the tertiary structure induced by heterodimerization of these intermedaite filaments proteins and most likely involves recognition sites located in the rod domain of these keratins. The microtubule tip localization signal (MtLS) motif; mediates interaction with MAPRE1 and targeting to the growing microtubule plus ends By similarity. |
| Disruption phenotype | Mice show progressive deterioration in motor function and sensory neurodegeneration. Exhibit axonal swellings packed with disorganized intermediate filaments (IFs) and microtubules. Show poorly defined Z lines and display a reduction in sarcomere length. Have increased accumulation of vesicles and severely disrupted retrograde axonal transport. In stratified epithelia, hemidesmosomes are normal but they lack the inner plate and have no cytoskeleton attached. Ref.9 Ref.11 Ref.12 Ref.13 |
| Sequence similarities | Belongs to the plakin or cytolinker family. UniProtKB Q03001 Contains 1 actin-binding domain. Contains 2 CH (calponin-homology) domains. Contains 2 EF-hand domains. Contains 1 GAR domain. Contains 5 plectin repeats. Contains 1 SH3 domain. Contains 19 spectrin repeats. |
| Sequence caution | Isoform 6: The sequence AAC52231.1 differs from that shown. Reason: Frameshift at position 51. |
Ontologies
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| Prph | P21807 | 3 | EBI-446159,EBI-446227 | From a different organism. |
Alternative products
| This entry describes 7 isoforms produced by alternative promoter usage and alternative splicing. [Align] [Select] | ||||||
| Isoform 2 Ref.1 (identifier: Q91ZU6-1) Also known as: BPAG1-b; BPAG1a1; dystonin-1; This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. | ||||||
| Isoform 1 Ref.1 (identifier: Q91ZU6-2) Also known as: BPAG1-a; BPAG1a2; The sequence of this isoform differs from the canonical sequence as follows: 1549-3557: Missing. | ||||||
| Isoform 3 (identifier: Q91ZU6-3) The sequence of this isoform differs from the canonical sequence as follows: 7125-7130: Missing. 7170-7193: Missing. 7261-7261: K → KILHPLTRNYGKPWLANSKMSTPCKAAECPDFPVSSAE | ||||||
| Note: No experimental confirmation available. | ||||||
| Isoform 4 (identifier: Q91ZU6-4) The sequence of this isoform differs from the canonical sequence as follows: 7170-7193: Missing. 7261-7261: K → KILHPLTRNYGKPWLANSKMSTPCKAAECPDFPVSSAE | ||||||
| Note: No experimental confirmation available. | ||||||
| Isoform 5 Ref.1 (identifier: Q91ZU6-5) Also known as: BPAG1-e; The sequence of this isoform differs from the canonical sequence as follows: 1-381: MAGYLSPAAY...REKALRPEVE → MRISCPFIVVPLINSCISFSNESLDGH 1432-1432: K → MKRSKENSEH...GISNLYYSSQ 1433-7389: Missing. | ||||||
| Note: Contains a phosphothreonine at position 1100. Contains a phosphoserine at position 1527. Contains a phosphothreonine at position 1533. | ||||||
| Isoform 6 (identifier: Q91ZU6-6) Also known as: BPAG1n; BPAG1-n1; BPAG1-n2; BPAG1a2; dystonin-2; The sequence of this isoform differs from the canonical sequence as follows: 1-30: MAGYLSPAAYMYVEEQEYLQAYEDVLERYK → MIAAAFLVLL...PAERAVLRIA 305-7389: Missing. | ||||||
| Note: Incomplete sequence. Transmembrane protein (helical transmembrane domain from amino acid 18 to 38). Contains a phosphoserine at position 163. Contains a phosphoserine at position 165. Contains a phosphoserine at position 167 (By similarity). | ||||||
| Isoform 7 (identifier: Q91ZU6-8) Also known as: BPAG1a3; The sequence of this isoform differs from the canonical sequence as follows: 1-137: MAGYLSPAAY...GLIWTIILHF → MGNVCGCVRA...SKDAPRDDGC 271-272: VK → KG 273-7389: Missing. | ||||||
| Note: Incomplete sequence. Probably myristoylated on Gly-2. Probably S-palmitoylated on Cys-5 and Cys-7. Mutagenesis of Gly-2 to Ala inhibits cortical localization. Mutagenesis of Cys-5 to Ser inhibits cortical localization. Mutagenesis of Cys-7 to Ser inhibits cortical localization. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 7389 | 7389 | Dystonin | PRO_0000078141 | |||||
Regions | |||||||||
| Domain | 35 – 252 | 218 | Actin-binding | ||||||
| Domain | 35 – 138 | 104 | CH 1 | ||||||
| Domain | 151 – 252 | 102 | CH 2 | ||||||
| Repeat | 701 – 801 | 101 | Spectrin 1 | ||||||
| Domain | 889 – 941 | 53 | SH3 | ||||||
| Repeat | 1582 – 1624 | 43 | Plectin 1 | ||||||
| Repeat | 1657 – 1701 | 45 | Plectin 2 | ||||||
| Repeat | 1772 – 1815 | 44 | Plectin 3 | ||||||
| Repeat | 1816 – 1844 | 29 | Plectin 4 | ||||||
| Repeat | 1848 – 1889 | 42 | Plectin 5 | ||||||
| Repeat | 3845 – 3925 | 81 | Spectrin 2 | ||||||
| Repeat | 3997 – 4079 | 83 | Spectrin 3 | ||||||
| Repeat | 4440 – 4548 | 109 | Spectrin 4 | ||||||
| Repeat | 4552 – 4657 | 106 | Spectrin 5 | ||||||
| Repeat | 4775 – 4877 | 103 | Spectrin 6 | ||||||
| Repeat | 5208 – 5315 | 108 | Spectrin 7 | ||||||
| Repeat | 5322 – 5423 | 102 | Spectrin 8 | ||||||
| Repeat | 5430 – 5532 | 103 | Spectrin 9 | ||||||
| Repeat | 5647 – 5751 | 105 | Spectrin 10 | ||||||
| Repeat | 5758 – 5856 | 99 | Spectrin 11 | ||||||
| Repeat | 6002 – 6082 | 81 | Spectrin 12 | ||||||
| Repeat | 6089 – 6191 | 103 | Spectrin 13 | ||||||
| Repeat | 6197 – 6300 | 104 | Spectrin 14 | ||||||
| Repeat | 6308 – 6410 | 103 | Spectrin 15 | ||||||
| Repeat | 6415 – 6519 | 105 | Spectrin 16 | ||||||
| Repeat | 6523 – 6629 | 107 | Spectrin 17 | ||||||
| Repeat | 6636 – 6736 | 101 | Spectrin 18 | ||||||
| Repeat | 6741 – 6844 | 104 | Spectrin 19 | ||||||
| Domain | 7015 – 7050 | 36 | EF-hand 1 | ||||||
| Domain | 7051 – 7086 | 36 | EF-hand 2 | ||||||
| Domain | 7091 – 7169 | 79 | GAR | ||||||
| Calcium binding | 7028 – 7039 | 12 | 1 Potential | ||||||
| Calcium binding | 7064 – 7075 | 12 | 2 Potential | ||||||
| Motif | 1382 – 1388 | 7 | Nuclear localization signal; in isoform 6 | ||||||
| Motif | 7369 – 7372 | 4 | Microtubule tip localization signal | ||||||
| Compositional bias | 2362 – 2422 | 61 | Asp-rich | ||||||
Amino acid modifications | |||||||||
| Modified residue | 2857 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 7182 | 1 | Phosphoserine Ref.16 | ||||||
| Modified residue | 7250 | 1 | Phosphoserine By similarity | ||||||
Natural variations | |||||||||
| Alternative sequence | 1 – 381 | 381 | MAGYL…RPEVE → MRISCPFIVVPLINSCISFS NESLDGH in isoform 5. | VSP_041541 | |||||
| Alternative sequence | 1 – 137 | 137 | MAGYL…IILHF → MGNVCGCVRAEKEEPYFDPA KSPLSPEKYSPGRKYFRRKP CQKVVDDTEPVRQSSEREGK KGVSQPAGGQPAVSSGELPW EDPAASPTKEDAVQLGKRAA TEHGDQKPLPSSVDGYPHRV TVSSAQGRYSEVQVSIPDKI ISEEDSPPYCPETERHLDDV NSKHRTFLRKDNVSLSQTAA SSSPILCVTEKSLKNSALMG NLSRSCHSVLEQDSDERGHP FGVHRLQLTKRRCHSLSSGV SCVSKDAPRDDGC in isoform 7. | VSP_041542 | |||||
| Alternative sequence | 1 – 30 | 30 | MAGYL…LERYK → MIAAAFLVLLRPYSIQCALF LLLLLLGTVATIVFFCCWHR KLQKGRHPMKSVFSGRSRSR DAALRSHHFRSEGFRASPRH IRRRVAAAAAARLEEVKPVV EVHHQSEQESSGRKRRIKKN SRVQPEFYHSVQGASTRRPS SGNASYRCSMSSSADFSDED DFSQKSGSASPAPGDTLPWN LPKHERSKRKIQGGSVLDPA ERAVLRIA in isoform 6. | VSP_041543 | |||||
| Alternative sequence | 271 – 272 | 2 | VK → KG in isoform 7. | VSP_041544 | |||||
| Alternative sequence | 273 – 7389 | 7117 | Missing in isoform 7. | VSP_041545 | |||||
| Alternative sequence | 305 – 7389 | 7085 | Missing in isoform 6. | VSP_041546 | |||||
| Alternative sequence | 1432 | 1 | K → MKRSKENSEHGAYSDLLQRQ RATMVENSKLTGKISELETM VAELKKQKSRVEEELPKVKE AAENELRKQQRNVEDIALQK LRAESEAKQYRRELETIVRE KEAAERELERVRQLTAEAEA RRAAVEENLRNFRSQLQENT FTRQTLEDHLRRKDSSLSDL EQQKRALVEELQRKRDHEEE LLRLVKQMERDLAFQKQVAE KQLKEKQKVELEARRKITEI QFSCRESAAVAQARPQREQG RQKEEELKQQVDELTLANRK AEKEMRELKYELSAVQLEKA SSEEKARLLKDKLDETNNTL KCLKEDLERKDQAQERYSQQ LRDLGGQLNQTTDKAEEVRQ EANDLKKIKHTYQLELESLH QEKGKLQREVDRVTRAHALA ERNIQCLNSQVHASRDEKDL SEERRRLCQRKSDHLKEEFE RSHAQLLQNIQAEKENNDKI QKLNKELEKSNECAETLKQK VDELTRQNNETKLMMQRIQA ESKNIVREKQAIQQRCEVLR IQADGFKDQLRNTNEHLHKQ TKTEQDFHRKIKSLEDDLAQ SQNLVSEFKQKCDQQSMIIQ KTEKEVRSLSAELSASKEEK RREEQKAQLQRAQVQELNDR LKRVQDELHLKTIEEQMTHR KMILLQEESDKFKRSADEFR KKMEKLMESKVVTETDLSGI KHDFVSLQRENFRAQENAKL WETNIRELERQLQCYREKMQ QGPPVEANHYQKCRRLEEEL LAQRREVENLKQKMDQQIKE HEHQLLRLQCEIQKKSTTQD HTFASAFDTAGRECHHPAEI SPGNSGHLNLKTRLPLSRWT QEPHQTEGKWPHRAAEQLPK EVQFRQPGAPLDRESSQPCY SEYFSQTSTELQITFDDKNP ITRLSELETMREQALHPSRP PVTYQDDKLERELVKLLTPL EIAKNKQCGMHTEVTTLKQE KRLGSSAGGWMLEGCRTSGG LKGDFLKKSVEPEASPSLDL NQACSVRDEEFQFQGLRHTV TGRQLVEAKLLDMRTVEQLR LGLKTVEEVQRSLSKFLTKA TSIAGLYLESSKEKMSFTSA AQKIIIDKMIALAFLEAQAA TGFIIDPVSGQTYCVEDAVL HGIVDPEFRSRLLEAEKAVL GYSHASKTLSVFQAMENRML DRKKGKHILEAQIASGGVID PVRGVRVPPEMAVQQGLLNN AVLQFLHEPSSNTRVFPNPN NKQALYYSELLQICVFDVDC QCFLLPFGEREISNLNIEKT HKIAVVDTKTGAELTAFEAF QRNLIDKGIYLELSGQQYQW KEATFFDSYGHPSHMLTDTK TGLQFNISEAVEQGTLDKAL VQKYQEGLTTLTELADFLLS KVVPKKDLHSPIAGYWLTAS GERISLLKASRRNLVDRVTA LRCLEAQICTGGIIDPLTGK KYRVAEALHRGLVDEGFAQQ LRQCELVITGISHPVSNKMM SVVEAVNANIISKEMGMRCL EFQYLTGGLIEPKVFSRLTI EEALHVGIIDVLIATRLKDQ KSYVRDIMCPQTKRKLTYKE ALEKADFDFHTGLKLLEVSE PLGTGISNLYYSSQ in isoform 5. | VSP_041547 | |||||
| Alternative sequence | 1433 – 7389 | 5957 | Missing in isoform 5. | VSP_041548 | |||||
| Alternative sequence | 1549 – 3557 | 2009 | Missing in isoform 1. Ref.1 | VSP_041549 | |||||
| Alternative sequence | 7125 – 7130 | 6 | Missing in isoform 3. | VSP_041550 | |||||
| Alternative sequence | 7170 – 7193 | 24 | Missing in isoform 3 and isoform 4. | VSP_041551 | |||||
| Alternative sequence | 7261 | 1 | K → KILHPLTRNYGKPWLANSKM STPCKAAECPDFPVSSAE in isoform 3 and isoform 4. | VSP_041552 | |||||
Experimental info | |||||||||
| Mutagenesis | 1385 | 1 | R → A: Prevents isoform 6 from localizing to the nucleus; when associated with A-1386. Ref.14 | ||||||
| Mutagenesis | 1386 | 1 | R → A: Prevents isoform 6 from localizing to the nucleus; when associated with A-1385. Ref.14 | ||||||
| Sequence conflict | 6193 | 1 | T → A in AAK83383. Ref.1 | ||||||
| Sequence conflict | 7097 | 1 | G → E in BAC29753. Ref.6 | ||||||
| Sequence conflict | 7097 | 1 | G → E in BAC34695. Ref.6 | ||||||
| Sequence conflict | 7241 | 1 | G → A in BAC29753. Ref.6 | ||||||
| Sequence conflict | 7241 | 1 | G → A in BAC34695. Ref.6 | ||||||
| Isoform 5: | |||||||||
| Sequence conflict | 2325 | 1 | G → D in BAB93448. Ref.7 | ||||||
| Sequence conflict | 2416 | 1 | A → T in BAB93448. Ref.7 | ||||||
| Sequence conflict | 2530 | 1 | K → Q in BAB93448. Ref.7 | ||||||
| Isoform 6: | |||||||||
| Sequence conflict | 101 | 1 | E → K in AAC52231. Ref.2 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "The BPAG1 locus: alternative splicing produces multiple isoforms with distinct cytoskeletal linker domains, including predominant isoforms in neurons and muscles." Leung C.L., Zheng M., Prater S.M., Liem R.K.H. J. Cell Biol. 154:691-697(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 5), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, ALTERNATIVE SPLICING. Strain: BALB/c. Tissue: Epithelium, Muscle and Neuron. |
| [2] | "The mouse dystonia musculorum gene is a neural isoform of bullous pemphigoid antigen 1." Brown A., Bernier G., Mathieu M., Rossant J., Kothary R. Nat. Genet. 10:301-306(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-511 (ISOFORM 2), PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE. Tissue: Brain. |
| [3] | "A Bpag1 isoform involved in cytoskeletal organization surrounding the nucleus." Young K.G., Pinheiro B., Kothary R. Exp. Cell Res. 312:121-134(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-304 (ISOFORM 6), ALTERNATIVE SPLICING (ISOFORMS 2 AND 6), SUBCELLULAR LOCATION (ISOFORMS 2 AND 6). Strain: C3H. |
| [4] | "Dissecting the sequence specific functions of alternative N-terminal isoforms of mouse bullous pemphigoid antigen 1." Jefferson J.J., Leung C.L., Liem R.K. Exp. Cell Res. 312:2712-2725(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-270 (ISOFORM 7), ALTERNATIVE SPLICING (ISOFORMS 1; 6 AND 7), FUNCTION OF ISOFORMS 1; 6 AND 7, PALMITOYLATION, MYRISTOYLATION, MUTAGENESIS, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. Strain: C57BL/6 X CBA. |
| [5] | "Structural analysis of the plakin domain of bullous pemphigoid antigen1 (BPAG1) suggests that plakins are members of the spectrin superfamily." Jefferson J.J., Ciatto C., Shapiro L., Liem R.K. J. Mol. Biol. 366:244-257(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 580-584; 1043-1047 AND 1053-1057, X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 580-803. |
| [6] | "The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.  Hayashizaki Y.Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 6693-7389 (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 6870-7389 (ISOFORM 4). Strain: C57BL/6J. Tissue: Fetal skin and Fetal spinal cord. |
| [7] | "The intermediate filament protein peripherin is the specific interaction partner of mouse BPAG1-n (dystonin) in neurons." Leung C.L., Sun D., Liem R.K. J. Cell Biol. 144:435-446(1999) [PubMed] [Europe PMC] [Abstract] Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), FUNCTION, INTERACTION WITH PRPH. Strain: BALB/c. |
| [8] | "Molecular network in NGF-mediated neural differentiation." Kubo Y., Ohba M., Iwashita S. Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5). Strain: Swiss Webster / NIH. |
| [9] | "Gene targeting of BPAG1: abnormalities in mechanical strength and cell migration in stratified epithelia and neurologic degeneration." Guo L., Degenstein L., Dowling J., Yu Q.C., Wollmann R., Perman B., Fuchs E. Cell 81:233-243(1995) [PubMed] [Europe PMC] [Abstract] Cited for: ALTERNATIVE SPLICING (ISOFORM 5), DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION (ISOFORM 5), TISSUE SPECIFICITY. |
| [10] | "An essential cytoskeletal linker protein connecting actin microfilaments to intermediate filaments." Yang Y., Dowling J., Yu Q.C., Kouklis P., Cleveland D.W., Fuchs E. Cell 86:655-665(1996) [PubMed] [Europe PMC] [Abstract] Cited for: ALTERNATIVE SPLICING (ISOFORMS 5 AND 6), SUBCELLULAR LOCATION (ISOFORMS 5 AND 6), TISSUE SPECIFICITY. |
| [11] | "Integrators of the cytoskeleton that stabilize microtubules." Yang Y., Bauer C., Strasser G., Wollman R., Julien J.P., Fuchs E. Cell 98:229-238(1999) [PubMed] [Europe PMC] [Abstract] Cited for: DISRUPTION PHENOTYPE. |
| [12] | "Dystonin-deficient mice exhibit an intrinsic muscle weakness and an instability of skeletal muscle cytoarchitecture." Dalpe G., Mathieu M., Comtois A., Zhu E., Wasiak S., De Repentigny Y., Leclerc N., Kothary R. Dev. Biol. 210:367-380(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH DES, DISRUPTION PHENOTYPE. |
| [13] | "BPAG1n4 is essential for retrograde axonal transport in sensory neurons." Liu J.J., Ding J., Kowal A.S., Nardine T., Allen E., Delcroix J.D., Wu C., Mobley W., Fuchs E., Yang Y. J. Cell Biol. 163:223-229(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE. |
| [14] | "Bpag1 localization to actin filaments and to the nucleus is regulated by its N-terminus." Young K.G., Pool M., Kothary R. J. Cell Sci. 116:4543-4555(2003) [PubMed] [Europe PMC] [Abstract] Cited for: ALTERNATIVE SPLICING (ISOFORMS 2; 5 AND 6), HOMODIMERIZATION, MUTAGENESIS OF ARG-1385 AND ARG-1386, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. |
| [15] | "A differential phosphoproteomic analysis of retinoic acid-treated P19 cells." Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D. J. Proteome Res. 6:3174-3186(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1100; SER-1527 AND THR-1533 (ISOFORM 5), MASS SPECTROMETRY. Tissue: Teratocarcinoma. |
| [16] | "Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations." Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M. Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7182, MASS SPECTROMETRY. Tissue: Brain cortex. |
| [17] | "Dystonin/Bpag1 is a necessary endoplasmic reticulum/nuclear envelope protein in sensory neurons." Young K.G., Kothary R. Exp. Cell Res. 314:2750-2761(2008) [PubMed] [Europe PMC] [Abstract] Cited for: ALTERNATIVE SPLICING (ISOFORM 6), INTERACTION WITH SYNE3, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. |
| [18] | "BPAG1 isoform-b: complex distribution pattern in striated and heart muscle and association with plectin and alpha-actinin." Steiner-Champliaud M.F., Schneider Y., Favre B., Paulhe F., Praetzel-Wunder S., Faulkner G., Konieczny P., Raith M., Wiche G., Adebola A., Liem R.K., Langbein L., Sonnenberg A., Fontao L., Borradori L. Exp. Cell Res. 316:297-313(2010) [PubMed] [Europe PMC] [Abstract] Cited for: ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), INTERACTION WITH PLEC, SUBCELLULAR LOCATION (ISOFORMS 1 AND 2), TISSUE SPECIFICITY. |
| [19] | "Hearts of dystonia musculorum mice display normal morphological and histological features but show signs of cardiac stress." Boyer J.G., Bhanot K., Kothary R., Boudreau-Lariviere C. PLoS ONE 5:E9465-E9465(2010) [PubMed] [Europe PMC] [Abstract] Cited for: ALTERNATIVE SPLICING (ISOFORM 2), FUNCTION OF ISOFORM 2, SUBCELLULAR LOCATION (ISOFORM 2), TISSUE SPECIFICITY. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | AF396877 mRNA. Translation: AAK83382.1. AF396878 mRNA. Translation: AAK83383.1. AF396879 mRNA. Translation: AAK83384.1. U22452 mRNA. Translation: AAC52230.1. U25158 mRNA. Translation: AAC52231.1. Frameshift. DQ023311 mRNA. Translation: AAY46942.1. DQ463750 mRNA. Translation: ABF00406.1. AK051626 mRNA. Translation: BAC34695.1. AK037206 mRNA. Translation: BAC29753.1. AF115383 mRNA. Translation: AAD22959.1. AB085694 mRNA. Translation: BAB93448.1. | ||||||||||||
| IPI | IPI00131432. IPI00230689. IPI00230690. IPI00230692. IPI00284272. IPI00623531. IPI01019259. | ||||||||||||
| PIR | A60776. I49290. I49298. | ||||||||||||
| UniGene | Mm.336625. Mm.478284. Mm.487428. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||
| ProteinModelPortal | Q91ZU6. | ||||||||||||
| SMR | Q91ZU6. Positions 31-255, 268-479, 583-1051, 1553-1927, 5208-5532, 6115-6480, 7098-7170. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protein-protein interaction databases | |||||||||||||
| IntAct | Q91ZU6. 4 interactions. | ||||||||||||
| STRING | 10090.ENSMUSP00000095392. | ||||||||||||
2D gel databases | |||||||||||||
| REPRODUCTION-2DPAGE | IPI00230689. IPI00230690. IPI00284272. | ||||||||||||
Proteomic databases | |||||||||||||
| PaxDb | Q91ZU6. | ||||||||||||
| PRIDE | Q91ZU6. | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| KEGG | mmu:13518. | ||||||||||||
| UCSC | uc007aoi.1. mouse. uc007aoj.1. mouse. uc007aol.1. mouse. | ||||||||||||
Organism-specific databases | |||||||||||||
| CTD | 667. | ||||||||||||
| MGI | MGI:104627. Dst. | ||||||||||||
Phylogenomic databases | |||||||||||||
| eggNOG | COG5069. | ||||||||||||
| HOVERGEN | HBG031127. | ||||||||||||
| KO | K10382. | ||||||||||||
Gene expression databases | |||||||||||||
| CleanEx | MM_DST. | ||||||||||||
| Genevestigator | Q91ZU6. | ||||||||||||
| GermOnline | ENSMUSG00000026131. Mus musculus. | ||||||||||||
Family and domain databases | |||||||||||||
| Gene3D | 1.10.238.10. 1 hit. 1.10.418.10. 2 hits. 3.30.920.20. 1 hit. | ||||||||||||
| InterPro | IPR001589. Actinin_actin-bd_CS. IPR001715. CH-domain. IPR011992. EF-hand-like_dom. 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] | ||||||||||||
| Pfam | PF00307. CH. 2 hits. PF13499. EF_hand_5. 1 hit. PF02187. GAS2. 1 hit. PF00681. Plectin. 5 hits. PF00435. Spectrin. 18 hits. [Graphical view] | ||||||||||||
| SMART | SM00033. CH. 2 hits. SM00054. EFh. 2 hits. SM00243. GAS2. 1 hit. SM00250. PLEC. 9 hits. SM00150. SPEC. 32 hits. [Graphical view] | ||||||||||||
| SUPFAM | SSF47576. Calponin-homology. 1 hit. SSF143575. SSF143575. 1 hit. | ||||||||||||
| PROSITE | 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. PS50002. SH3. False negative. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Other | |||||||||||||
| ChiTaRS | DST. mouse. | ||||||||||||
| EvolutionaryTrace | Q91ZU6. | ||||||||||||
| NextBio | 284082. | ||||||||||||
| SOURCE | Search... | ||||||||||||
Entry information
| Entry name | DYST_MOUSE | ||||||||
| Accession | Primary (citable) accession number: Q91ZU6 Secondary accession number(s): Q1KP04 Q9WU50 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |