Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q03001 (DYST_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 161. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dystonin
Alternative name(s):
230 kDa bullous pemphigoid antigen
230/240 kDa bullous pemphigoid antigen
Bullous pemphigoid antigen 1
Short name=BPA
Short name=Bullous pemphigoid antigen
Dystonia musculorum protein
Hemidesmosomal plaque protein
Gene names
Name:DST
Synonyms:BP230, BP240, BPAG1, DMH, DT, KIAA0728
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length7570 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cytoskeletal linker protein. Acts as an integrator of intermediate filaments, actin and microtubule cytoskeleton networks. Required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. The proteins may self-aggregate to form filaments or a two-dimensional mesh. Ref.7 Ref.20 Ref.23

Isoform 3:plays a structural role in the assembly of hemidesmosomes of epithelial cells; anchors keratin-containing intermediate filaments to the inner plaque of hemidesmosomes. Required for the regulation of keratinocyte polarity and motility; mediates integrin ITGB4 regulation of RAC1 activity. Ref.7 Ref.20 Ref.23

Isoform 6:required for bundling actin filaments around the nucleus By similarity. Ref.7 Ref.20 Ref.23

Isoform 7:regulates the organization and stability of the microtubule network of sensory neurons to allow axonal transport. Ref.7 Ref.20 Ref.23

Subunit structure

Homodimer. Isoform 1 interacts (via N-terminus) with PLEC (via N-terminus). Interacts with the neuronal intermediate filament protein, PRPH. Interacts with DES. Interacts with SYNE3 By similarity. Isoform 1 and isoform 6 can homodimerize (via N-terminus). Isoform 1 interacts (via N-terminus) with ACTN2. Isoform 1 interacts (via N-terminus) with PLEC (via N-terminus). Isoform 3 interacts (via N-terminus) with COL17A1 (via cytoplasmic region). Isoform 3 interacts (via N-terminus) with ITGB4 isoform beta-4a(via cytoplasmic region). Isoform 3 interacts (via N-terminus) with ERBB2IP (via C-terminus). Isoform 3 associates (via C-terminal) with KRT5-KRT14 (via rod region) intermadiate filaments of keratins. Interacts with MAPRE1; probably required for targeting to the growing microtubule plus ends. Interacts with TMIGD2. Ref.17 Ref.19 Ref.20 Ref.24 Ref.30

Subcellular location

Cytoplasmcytoskeleton. Note: Associates with intermediate filaments, acin and microtubule cytoskeletons. Localizes to actin stress fibers and to actin-rich ruffling at the cortex of cells By similarity. Associated at the growing distal tip of microtubules. Ref.3 Ref.7 Ref.20 Ref.21 Ref.23 Ref.24

Isoform 1: Cytoplasmcytoskeleton By similarity. CytoplasmmyofibrilsarcomereZ line. CytoplasmmyofibrilsarcomereH zone By similarity. Note: Localizes to microtubules and actin microfilaments throughout the cytoplasm and at focal contact attachments at the plasma membrane By similarity. Ref.3 Ref.7 Ref.20 Ref.21 Ref.23 Ref.24

Isoform 2: Cytoplasmcytoskeleton By similarity. Note: Colocalizes both cortical and cytoplasmic actin filaments By similarity. Ref.3 Ref.7 Ref.20 Ref.21 Ref.23 Ref.24

Isoform 3: Cytoplasmcytoskeleton. Cell junctionhemidesmosome. Note: Localizes to actin and intermediate filaments cytoskeletons By similarity. Colocalizes with the epidermal KRT5-KRT14 intermediate filaments network of keratins. Colocalizes with ITGB4 at the leading edge of migrating keratinocytes. Ref.3 Ref.7 Ref.20 Ref.21 Ref.23 Ref.24

Isoform 6: Nucleus By similarity. Nucleus envelope. Membrane; Single-pass membrane protein By similarity. Endoplasmic reticulum membrane; Single-pass membrane protein By similarity. Cytoplasmcytoskeleton. Membrane; Single-pass membrane protein. Note: Localizes to actin and intermediate filaments cytoskeletons. Localizes to central actin stress fibers around the nucleus and is excluded form focal contact sites in myoblast cells. Translocates to the nucleus By similarity. Associates with actin cytoskeleton in sensory neurons. Ref.3 Ref.7 Ref.20 Ref.21 Ref.23 Ref.24

Isoform 7: Cytoplasmcytoskeleton. Cell projectionaxon. Membrane. Note: Associates with axonal microtubules and intermediate filaments, but not with actin cytoskeleton, in sensory neurons. Ref.3 Ref.7 Ref.20 Ref.21 Ref.23 Ref.24

Isoform 8: Cytoplasmcytoskeleton By similarity. Cytoplasmcell cortex By similarity. Cell membrane; Lipid-anchor By similarity Ref.3 Ref.7 Ref.20 Ref.21 Ref.23 Ref.24.

Tissue specificity

Isoform 1 is expressed in myoblasts (at protein level). Isoform 3 is expressed in the skin. Isoform 6 is expressed in the brain. Highly expressed in skeletal muscle and cultured keratinocytes. Ref.3 Ref.16 Ref.24

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. Ref.18 Ref.31

The microtubule tip localization signal (MtLS) motif; mediates interaction with MAPRE1 and targeting to the growing microtubule plus ends. Ref.18 Ref.31

Involvement in disease

Neuropathy, hereditary sensory and autonomic, 6 (HSAN6) [MIM:614653]: A form of hereditary sensory and autonomic neuropathy, a genetically and clinically heterogeneous group of disorders characterized by degeneration of dorsal root and autonomic ganglion cells, and by sensory and/or autonomic abnormalities. HSAN6 is a severe autosomal recessive disorder characterized by neonatal hypotonia, respiratory and feeding difficulties, lack of psychomotor development, and autonomic abnormalities including labile cardiovascular function, lack of corneal reflexes leading to corneal scarring, areflexia, and absent axonal flare response after intradermal histamine injection.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.1 Ref.28

Epidermolysis bullosa simplex, autosomal recessive 2 (EBSB2) [MIM:615425]: A form of epidermolysis bullosa, a dermatologic disorder characterized by localized blistering on the dorsal, lateral and plantar surfaces of the feet. EBSB2 is characterized by trauma-induced blistering mainly occurring on the feet and ankles. Ultrastructural analysis of skin biopsy shows abnormal hemidesmosomes with poorly formed inner plaques.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.1 Ref.25 Ref.29

Sequence similarities

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 20 spectrin repeats.

Sequence caution

The sequence AAA35538.1 differs from that shown. Reason: Contaminating sequence. Sequence of unknown origin in the C-terminal part.

The sequence AAA57185.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence BAB70870.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BAC04449.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BAC04848.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence CAI14341.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAI14989.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAI16609.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAI16610.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAI20330.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAI20332.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAI22044.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAI22045.1 differs from that shown. Reason: Erroneous gene model prediction.

Isoform 6: The sequence AAC50244.1 differs from that shown. Reason: Frameshift at position 51.

Ontologies

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

Inferred from electronic annotation. Source: Ensembl

cell adhesion

Inferred from electronic annotation. Source: UniProtKB-KW

cell cycle arrest

Inferred from electronic annotation. Source: InterPro

cell motility

Inferred from mutant phenotype Ref.23. Source: UniProtKB

cytoplasmic microtubule organization

Inferred from electronic annotation. Source: Ensembl

cytoskeleton organization

Inferred from mutant phenotype Ref.23. Source: UniProtKB

extracellular matrix organization

Traceable author statement. Source: Reactome

hemidesmosome assembly

Inferred from direct assay Ref.20. Source: UniProtKB

integrin-mediated signaling pathway

Non-traceable author statement Ref.19. Source: UniProtKB

intermediate filament cytoskeleton organization

Inferred from expression pattern Ref.3. Source: UniProtKB

maintenance of cell polarity

Inferred from mutant phenotype Ref.23. Source: UniProtKB

microtubule cytoskeleton organization

Inferred from direct assay Ref.7. Source: UniProtKB

regulation of microtubule polymerization or depolymerization

Inferred from electronic annotation. Source: Ensembl

response to wounding

Inferred from direct assay Ref.23. Source: UniProtKB

retrograde axon cargo transport

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentH zone

Inferred from electronic annotation. Source: UniProtKB-SubCell

Z disc

Inferred from direct assay Ref.24. Source: UniProtKB

actin cytoskeleton

Inferred from direct assay Ref.7. Source: UniProtKB

axon

Inferred from direct assay Ref.7. Source: UniProtKB

basal plasma membrane

Non-traceable author statement Ref.19. Source: UniProtKB

basement membrane

Traceable author statement Ref.13. Source: ProtInc

cell cortex

Inferred from electronic annotation. Source: UniProtKB-SubCell

cell leading edge

Inferred from direct assay Ref.23. Source: UniProtKB

cytoplasm

Inferred from direct assay Ref.3Ref.24. Source: UniProtKB

cytoplasmic membrane-bounded vesicle

Inferred from direct assay PubMed 14581450. Source: MGI

cytosol

Traceable author statement. Source: Reactome

endoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

hemidesmosome

Inferred from direct assay Ref.20. Source: UniProtKB

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

intermediate filament

Inferred from electronic annotation. Source: UniProtKB-KW

intermediate filament cytoskeleton

Inferred from direct assay Ref.7. Source: UniProtKB

microtubule cytoskeleton

Inferred from direct assay. Source: HPA

microtubule plus-end

Inferred from direct assay Ref.31. Source: UniProtKB

neurofilament cytoskeleton

Inferred from electronic annotation. Source: Ensembl

nuclear envelope

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

integrin binding

Inferred from physical interaction Ref.19. Source: UniProtKB

microtubule plus-end binding

Inferred from direct assay Ref.31. Source: UniProtKB

protein C-terminus binding

Inferred from physical interaction Ref.19. Source: UniProtKB

protein homodimerization activity

Inferred from direct assay Ref.24. Source: UniProtKB

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 8 isoforms produced by alternative promoter usage and alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q03001-7)

Also known as: BPAG1-b;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Note: No experimental confirmation available. Derived from EST data.
Isoform 2 (identifier: Q03001-8)

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

The sequence of this isoform differs from the canonical sequence as follows:
     1-381: MAGYLSPAAY...REKALRPEVE → MHSSSYSYRS...SFGSESFDGH
     1550-3635: Missing.
     7352-7375: Missing.
     7442-7442: K → KILHPLTRNYGKPWLTNSKMSTPCKAAECSDFPVPSAE
Isoform 3 (identifier: Q03001-3)

Also known as: BPAG1e; eBPAG1;

The sequence of this isoform differs from the canonical sequence as follows:
     1-381: MAGYLSPAAY...REKALRPEVE → MHSSSYSYRS...SFGSESFDGH
     1433-1433: K → IKRCKETSEH...TGISSLYYSS
     1434-7570: Missing.
Note: Contains a phosphothreonine at position 1129. Contains a phosphoserine at position 1565 (By similarity).
Isoform 4 (identifier: Q03001-9)

Also known as: BPAG1eA; eB;

The sequence of this isoform differs from the canonical sequence as follows:
     1-381: MAGYLSPAAY...REKALRPEVE → MHSSSYSYRS...SFGSESFDGH
     3387-7570: Missing.
Note: Incomplete sequence.
Isoform 5 (identifier: Q03001-10)

The sequence of this isoform differs from the canonical sequence as follows:
     1-3753: Missing.
     4184-4200: GQVPLNSTALQDIISKN → DVGTGYCRSSEQYKCHE
     4201-7570: Missing.
Note: Incomplete sequence. No experimental confirmation available. Note=May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Isoform 6 (identifier: Q03001-11)

Also known as: BPAG1n1; BPAG1n2; Dystonin-2;

The sequence of this isoform differs from the canonical sequence as follows:
     1-30: MAGYLSPAAYLYVEEQEYLQAYEDVLERYK → MIAAAFLVLL...PAERAVLRIA
     47-7570: Missing.
Note: Incomplete sequence. Transmembrane protein (helical transmembrane domain from amino acid 18 to 38). Contains a phosphoserine at position 170.
Isoform 7 (identifier: Q03001-12)

Also known as: BPAG1n3;

The sequence of this isoform differs from the canonical sequence as follows:
     1-138: MAGYLSPAAY...LIWTIILHFQ → MQHSIFSLKKKRCHSLYTSMSSVSKDTDGNE
     189-7570: Missing.
Note: Incomplete sequence.
Isoform 8 (identifier: Q03001-13)

The sequence of this isoform differs from the canonical sequence as follows:
     1-138: MAGYLSPAAY...LIWTIILHFQ → MGNVCGCVRA...SVSKDTDGNE
     778-789: AYRAAMQTQWSW → VKLESVMVLVEY
     790-7570: Missing.
Note: Probably myristoylated on Gly-2 (By similarity). Probably S-palmitoylated on Cys-5 and Cys-7 (By similarity).

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 75707570Dystonin
PRO_0000078138

Regions

Domain35 – 252218Actin-binding
Domain35 – 138104CH 1
Domain151 – 252102CH 2
Repeat701 – 79797Spectrin 1
Domain890 – 94253SH3
Repeat1584 – 162643Plectin 1
Repeat1660 – 170344Plectin 2
Repeat1774 – 181744Plectin 3
Repeat1818 – 185538Plectin 4
Repeat1856 – 189136Plectin 5
Repeat3924 – 400077Spectrin 2
Repeat4069 – 415385Spectrin 3
Repeat4514 – 4622109Spectrin 4
Repeat4626 – 4731106Spectrin 5
Repeat4849 – 4952104Spectrin 6
Repeat5281 – 5389109Spectrin 7
Repeat5396 – 5497102Spectrin 8
Repeat5504 – 5606103Spectrin 9
Repeat5829 – 5933105Spectrin 10
Repeat5940 – 6042103Spectrin 11
Repeat6048 – 6154107Spectrin 12
Repeat6184 – 626481Spectrin 13
Repeat6270 – 6373104Spectrin 14
Repeat6379 – 6481103Spectrin 15
Repeat6490 – 6592103Spectrin 16
Repeat6597 – 6700104Spectrin 17
Repeat6705 – 6811107Spectrin 18
Repeat6818 – 6918101Spectrin 19
Repeat6923 – 7026104Spectrin 20
Domain7197 – 723236EF-hand 1
Domain7233 – 726836EF-hand 2
Domain7273 – 735179GAR
Calcium binding7210 – 7221121 Potential
Calcium binding7246 – 7257122 Potential
Motif1383 – 13897Nuclear localization signal; in isoform 6 By similarity
Motif7550 – 75534Microtubule tip localization signal
Compositional bias2394 – 243138Asp-rich
Compositional bias2592 – 25998Poly-Asp

Amino acid modifications

Modified residue29191Phosphoserine Ref.27
Modified residue74321Phosphoserine Ref.22
Cross-link5470Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)

Natural variations

Alternative sequence1 – 37533753Missing in isoform 5.
VSP_041524
Alternative sequence1 – 381381MAGYL…RPEVE → MHSSSYSYRSSDSVFSNTTS TRTSLDSNENLLLVHCGPTL INSCISFGSESFDGH in isoform 2, isoform 3 and isoform 4.
VSP_041525
Alternative sequence1 – 138138MAGYL…ILHFQ → MQHSIFSLKKKRCHSLYTSM SSVSKDTDGNE in isoform 7.
VSP_041526
Alternative sequence1 – 138138MAGYL…ILHFQ → MGNVCGCVRAEKEEQYVDPA KTPLNPEKYSPGRKYFRRKP IKKTGGDKESVGANNENEGK KKSSSQPSKEQPAPLSRGLV QQESVTLNSALGDGIQQKKT EVVADSVKQKLLPSAVSSWS DCVNTSPAKDSETEVKVSEL DERISEKDSTPYCAKRKKHL DDVNTSEITFQEKTDVFSFR KAASLSSIPSGIERSLEKGG FPEDPPKSYSSIQEKQNTER FCPHATQHFQFKKKRCHSLY TSMSSVSKDTDGNE in isoform 8.
VSP_041527
Alternative sequence1 – 3030MAGYL…LERYK → MIAAAFLVLLRPYSIQCALF LLLLLLGTIATIVFFCCWHR KLQKGRHPMKSVFSGRSRSR DAVLRSHHFRSEGFRASPRH LRRRVAAAAAARLEEVKPVV EVHHQSEQETSVRKRRIKKS SRVQPEFYHSVQGASIRRPS SGNASYRCSMSSSADFSDED DFSQKSGSASPAPGDTLPWN LPKHERSKRKIQGGSVLDPA ERAVLRIA in isoform 6.
VSP_041528
Alternative sequence47 – 75707524Missing in isoform 6.
VSP_041529
Alternative sequence189 – 75707382Missing in isoform 7.
VSP_041530
Alternative sequence778 – 78912AYRAA…TQWSW → VKLESVMVLVEY in isoform 8.
VSP_041531
Alternative sequence790 – 75706781Missing in isoform 8.
VSP_041532
Alternative sequence14331K → IKRCKETSEHGAYSDLLQRQ KATVLENSKLTGKISELERM VAELKKQKSRVEEELPKVRE AAENELRKQQRNVEDISLQK IRAESEAKQYRRELETIVRE KEAAERELERVRQLTIEAEA KRAAVEENLLNFRNQLEENT FTRRTLEDHLKRKDLSLNDL EQQKNKLMEELRRKRDNEEE LLKLIKQMEKDLAFQKQVAE KQLKEKQKIELEARRKITEI QYTCRENALPVCPITQATSC RAVTGLQQEHDKQKAEELKQ QVDELTAANRKAEQDMRELT YELNALQLEKTSSEEKARLL KDKLDETNNTLRCLKLELER KDQAEKGYSQQLRELGRQLN QTTGKAEEAMQEASDLKKIK RNYQLELESLNHEKGKLQRE VDRITRAHAVAEKNIQHLNS QIHSFRDEKELERLQICQRK SDHLKEQFEKSHEQLLQNIK AEKENNDKIQRLNEELEKSN ECAEMLKQKVEELTRQNNET KLMMQRIQAESENIVLEKQT IQQRCEALKIQADGFKDQLR STNEHLHKQTKTEQDFQRKI KCLEEDLAKSQNLVSEFKQK CDQQNIIIQNTKKEVRNLNA ELNASKEEKRRGEQKVQLQQ AQVQELNNRLKKVQDELHLK TIEEQMTHRKMVLFQEESGK FKQSAEEFRKKMEKLMESKV ITENDISGIRLDFVSLQQEN SRAQENAKLCETNIKELERQ LQQYREQMQQGQHMEANHYQ KCQKLEDELIAQKREVENLK QKMDQQIKEHEHQLVLLQCE IQKKSTAKDCTFKPDFEMTV KECQHSGELSSRNTGHLHPT PRSPLLRWTQEPQPLEEKWQ HRVVEQIPKEVQFQPPGAPL EKEKSQQCYSEYFSQTSTEL QITFDETNPITRLSEIEKIR DQALNNSRPPVRYQDNACEM ELVKVLTPLEIAKNKQYDMH TEVTTLKQEKNPVPSAEEWM LEGCRASGGLKKGDFLKKGL EPETFQNFDGDHACSVRDDE FKFQGLRHTVTARQLVEAKL LDMRTIEQLRLGLKTVEEVQ KTLNKFLTKATSIAGLYLES TKEKISFASAAERIIIDKMV ALAFLEAQAATGFIIDPISG QTYSVEDAVLKGVVDPEFRI RLLEAEKAAVGYSYSSKTLS VFQAMENRMLDRQKGKHILE AQIASGGVIDPVRGIRVPPE IALQQGLLNNAILQFLHEPS SNTRVFPNPNNKQALYYSEL LRMCVFDVESQCFLFPFGER NISNLNVKKTHRISVVDTKT GSELTVYEAFQRNLIEKSIY LELSGQQYQWKEAMFFESYG HSSHMLTDTKTGLHFNINEA IEQGTIDKALVKKYQEGLIT LTELADSLLSRLVPKKDLHS PVAGYWLTASGERISVLKAS RRNLVDRITALRCLEAQVST GGIIDPLTGKKYRVAEALHR GLVDEGFAQQLRQCELVITG IGHPITNKMMSVVEAVNANI INKEMGIRCLEFQYLTGGLI EPQVHSRLSIEEALQVGIID VLIATKLKDQKSYVRNIICP QTKRKLTYKEALEKADFDFH TGLKLLEVSEPLMTGISSLY YSS in isoform 3.
VSP_041533
Alternative sequence1434 – 75706137Missing in isoform 3.
VSP_041534
Alternative sequence1550 – 36352086Missing in isoform 2.
VSP_041535
Alternative sequence3387 – 75704184Missing in isoform 4.
VSP_041536
Alternative sequence4184 – 420017GQVPL…IISKN → DVGTGYCRSSEQYKCHE in isoform 5.
VSP_041537
Alternative sequence4201 – 75703370Missing in isoform 5.
VSP_041538
Alternative sequence7352 – 737524Missing in isoform 2.
VSP_041539
Alternative sequence74421K → KILHPLTRNYGKPWLTNSKM STPCKAAECSDFPVPSAE in isoform 2.
VSP_041540
Natural variant13191N → K.
Corresponds to variant rs35014998 [ dbSNP | Ensembl ].
VAR_063045
Natural variant23321Q → R.
Corresponds to variant rs16888053 [ dbSNP | Ensembl ].
VAR_063046
Natural variant37201Q → R.
Corresponds to variant rs4712138 [ dbSNP | Ensembl ].
VAR_063047
Natural variant51381T → A. Ref.4
Corresponds to variant rs4715631 [ dbSNP | Ensembl ].
VAR_063048

Experimental info

Mutagenesis75481K → Q: Loss of interaction with MAPRE1 and association with microtubule growing ends. Ref.31
Mutagenesis75501S → A or N: Loss of association with microtubule growing ends. Ref.31
Mutagenesis75521I → N: Loss of interaction with MAPRE1 and association with the growing microtubule plus ends; when associated with N-7553. Ref.31
Mutagenesis75531P → N: Loss of interaction with MAPRE1 and association with the growing microtubule plus ends; when associated with N-7552. Ref.31
Mutagenesis75571R → N: Loss of interaction with MAPRE1 and association with the growing microtubule plus ends.
Mutagenesis75581K → N: Loss of interaction with MAPRE1 and association with the growing microtubule plus ends.
Sequence conflict5731P → A in BAH12207. Ref.4
Sequence conflict11771V → G in M69225. Ref.1
Sequence conflict11771V → G in AAL62061. Ref.3
Sequence conflict11771V → G in AAL62062. Ref.3
Sequence conflict13631K → E in AAL62061. Ref.3
Sequence conflict47031R → H in BAC04449. Ref.4
Sequence conflict49351N → S in BAC04449. Ref.4
Sequence conflict50301E → G in AAL62061. Ref.3
Sequence conflict51771Q → R in AAL62061. Ref.3
Sequence conflict52251M → I in BAB70870. Ref.4
Sequence conflict52991K → R in AAL62061. Ref.3
Sequence conflict58231I → V in AAL62061. Ref.3
Sequence conflict58821K → R in AAL62061. Ref.3
Sequence conflict59861L → S in AAL62061. Ref.3
Sequence conflict60801K → E in BAC04848. Ref.4
Sequence conflict61861D → G in AAL62061. Ref.3
Sequence conflict64401A → G in AAL62061. Ref.3
Isoform 3:
Sequence conflict16441R → T in M69225. Ref.1
Sequence conflict23641S → T in M69225. Ref.1
Sequence conflict24951G → V in M69225. Ref.1
Sequence conflict25431N → K in M69225. Ref.1
Sequence conflict26211A → P in M69225. Ref.1
Sequence conflict19431G → R in CAA41528. Ref.13
Isoform 6:
Sequence conflict481P → L in AAC50244. Ref.6

Sequences

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

Last modified April 20, 2010. Version 4.
Checksum: 1EA992E53D1C243E

FASTA7,570860,662
        10         20         30         40         50         60 
MAGYLSPAAY LYVEEQEYLQ AYEDVLERYK DERDKVQKKT FTKWINQHLM KVRKHVNDLY 

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

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

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

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

       310        320        330        340        350        360 
NNPVELKALY NQYLQFKETE IPPKETEKSK IKRLYKLLEI WIEFGRIKLL QGYHPNDIEK 

       370        380        390        400        410        420 
EWGKLIIAML EREKALRPEV ERLEMLQQIA NRVQRDSVIC EDKLILAGNA LQSDSKRLES 

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

       490        500        510        520        530        540 
SSVYSKGRIL TTEQTKLMIS GITQSLNSGF AQTLHPSLTS GLTQSLTPSL TSSSMTSGLS 

       550        560        570        580        590        600 
SGMTSRLTPS VTPAYTPGFP SGLVPNFSSG VEPNSLQTLK LMQIRKPLLK SSLLDQNLTE 

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

       670        680        690        700        710        720 
SEIQMTAPLK LTYAEKLHRL ESQYAKLLNT SRNQERHLDT LHNFVSRATN ELIWLNEKEE 

       730        740        750        760        770        780 
EEVAYDWSER NTNIARKKDY HAELMRELDQ KEENIKSVQE IAEQLLLENH PARLTIEAYR 

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

       850        860        870        880        890        900 
HKLEDLVQES MEEKEELLQY KSTIANLMGK AKTIIQLKPR NSDCPLKTSI PIKAICDYRQ 

       910        920        930        940        950        960 
IEITIYKDDE CVLANNSHRA KWKVISPTGN EAMVPSVCFT VPPPNKEAVD LANRIEQQYQ 

       970        980        990       1000       1010       1020 
NVLTLWHESH INMKSVVSWH YLINEIDRIR ASNVASIKTM LPGEHQQVLS NLQSRFEDFL 

      1030       1040       1050       1060       1070       1080 
EDSQESQVFS GSDITQLEKE VNVCKQYYQE LLKSAEREEQ EESVYNLYIS EVRNIRLRLE 

      1090       1100       1110       1120       1130       1140 
NCEDRLIRQI RTPLERDDLH ESVFRITEQE KLKKELERLK DDLGTITNKC EEFFSQAAAS 

      1150       1160       1170       1180       1190       1200 
SSVPTLRSEL NVVLQNMNQV YSMSSTYIDK LKTVNLVLKN TQAAEALVKL YETKLCEEEA 

      1210       1220       1230       1240       1250       1260 
VIADKNNIEN LISTLKQWRS EVDEKRQVFH ALEDELQKAK AISDEMFKTY KERDLDFDWH 

      1270       1280       1290       1300       1310       1320 
KEKADQLVER WQNVHVQIDN RLRDLEGIGK SLKYYRDTYH PLDDWIQQVE TTQRKIQENQ 

      1330       1340       1350       1360       1370       1380 
PENSKTLATQ LNQQKMLVSE IEMKQSKMDE CQKYAEQYSA TVKDYELQTM TYRAMVDSQQ 

      1390       1400       1410       1420       1430       1440 
KSPVKRRRMQ SSADLIIQEF MDLRTRYTAL VTLMTQYIKF AGDSLKRLEE EEKSLEEEKK 

      1450       1460       1470       1480       1490       1500 
EHVEKAKELQ KWVSNISKTL KDAEKAGKPP FSKQKISSEE ISTKKEQLSE ALQTIQLFLA 

      1510       1520       1530       1540       1550       1560 
KHGDKMTDEE RNELEKQVKT LQESYNLLFS ESLKQLQESQ TSGDVKVEEK LDKVIAGTID 

      1570       1580       1590       1600       1610       1620 
QTTGEVLSVF QAVLRGLIDY DTGIRLLETQ LMISGLISPE LRKCFDLKDA KSHGLIDEQI 

      1630       1640       1650       1660       1670       1680 
LCQLKELSKA KEIISAASPT TIPVLDALAQ SMITESMAIK VLEILLSTGS LVIPATGEQL 

      1690       1700       1710       1720       1730       1740 
TLQKAFQQNL VSSALFSKVL ERQNMCKDLI DPCTSEKVSL IDMVQRSTLQ ENTGMWLLPV 

      1750       1760       1770       1780       1790       1800 
RPQEGGRITL KCGRNISILR AAHEGLIDRE TMFRLLSAQL LSGGLINSNS GQRMTVEEAV 

      1810       1820       1830       1840       1850       1860 
REGVIDRDTA SSILTYQVQT GGIIQSNPAK RLTVDEAVQC DLITSSSALL VLEAQRGYVG 

      1870       1880       1890       1900       1910       1920 
LIWPHSGEIF PTSSSLQQEL ITNELAYKIL NGRQKIAALY IPESSQVIGL DAAKQLGIID 

      1930       1940       1950       1960       1970       1980 
NNTASILKNI TLPDKMPDLG DLEACKNARR WLSFCKFQPS TVHDYRQEED VFDGEEPVTT 

      1990       2000       2010       2020       2030       2040 
QTSEETKKLF LSYLMINSYM DANTGQRLLL YDGDLDEAVG MLLEGCHAEF DGNTAIKECL 

      2050       2060       2070       2080       2090       2100 
DVLSSSGVFL NNASGREKDE CTATPSSFNK CHCGEPEHEE TPENRKCAID EEFNEMRNTV 

      2110       2120       2130       2140       2150       2160 
INSEFSQSGK LASTISIDPK VNSSPSVCVP SLISYLTQTE LADISMLRSD SENILTNYEN 

      2170       2180       2190       2200       2210       2220 
QSRVETNERA NECSHSKNIQ NFPSDLIENP IMKSKMSKFC GVNETENEDN TNRDSPIFDY 

      2230       2240       2250       2260       2270       2280 
SPRLSALLSH DKLMHSQGSF NDTHTPESNG NKCEAPALSF SDKTMLSGQR IGEKFQDQFL 

      2290       2300       2310       2320       2330       2340 
GIAAINISLP GEQYGQKSLN MISSNPQVQY HNDKYISNTS GEDEKTHPGF QQMPEDKEDE 

      2350       2360       2370       2380       2390       2400 
SEIEEYSCAV TPGGDTDNAI VSLTCATPLL DETISASDYE TSLLNDQQNN TGTDTDSDDD 

      2410       2420       2430       2440       2450       2460 
FYDTPLFEDD DHDSLLLDGD DRDCLHPEDY DTLQEENDET ASPADVFYDV SKENENSMVP 

      2470       2480       2490       2500       2510       2520 
QGAPVGSLSV KNKAHCLQDF LMDVEKDELD SGEKIHLNPV GSDKVNGQSL ETGSERECTN 

      2530       2540       2550       2560       2570       2580 
ILEGDESDSL TDYDIVGGKE SFTASLKFDD SGSWRGRKEE YVTGQEFHSD TDHLDSMQSE 

      2590       2600       2610       2620       2630       2640 
ESYGDYIYDS NDQDDDDDDG IDEEGGGIRD ENGKPRCQNV AEDMDIQLCA SILNENSDEN 

      2650       2660       2670       2680       2690       2700 
ENINTMILLD KMHSCSSLEK QQRVNVVQLA SPSENNLVTE KSNLPEYTTE IAGKSKENLL 

      2710       2720       2730       2740       2750       2760 
NHEMVLKDVL PPIIKDTESE KTFGPASISH DNNNISSTSE LGTDLANTKV KLIQGSELPE 

      2770       2780       2790       2800       2810       2820 
LTDSVKGKDE YFKNMTPKVD SSLDHIICTE PDLIGKPAEE SHLSLIASVT DKDPQGNGSD 

      2830       2840       2850       2860       2870       2880 
LIKGRDGKSD ILIEDETSIQ KMYLGEGEVL VEGLVEEENR HLKLLPGKNT RDSFKLINSQ 

      2890       2900       2910       2920       2930       2940 
FPFPQITNNE ELNQKGSLKK ATVTLKDEPN NLQIIVSKSP VQFENLEEIF DTSVSKEISD 

      2950       2960       2970       2980       2990       3000 
DITSDITSWE GNTHFEESFT DGPEKELDLF TYLKHCAKNI KAKDVAKPNE DVPSHVLITA 

      3010       3020       3030       3040       3050       3060 
PPMKEHLQLG VNNTKEKSTS TQKDSPLNDM IQSNDLCSKE SISGGGTEIS QFTPESIEAT 

      3070       3080       3090       3100       3110       3120 
LSILSRKHVE DVGKNDFLQS ERCANGLGND NSSNTLNTDY SFLEINNKKE RIEQQLPKEQ 

      3130       3140       3150       3160       3170       3180 
ALSPRSQEKE VQIPELSQVF VEDVKDILKS RLKEGHMNPQ EVEEPSACAD TKILIQNLIK 

      3190       3200       3210       3220       3230       3240 
RITTSQLVNE ASTVPSDSQM SDSSGVSPMT NSSELKPESR DDPFCIGNLK SELLLNILKQ 

      3250       3260       3270       3280       3290       3300 
DQHSQKITGV FELMRELTHM EYDLEKRGIT SKVLPLQLEN IFYKLLADGY SEKIEHVGDF 

      3310       3320       3330       3340       3350       3360 
NQKACSTSEM MEEKPHILGD IKSKEGNYYS PNLETVKEIG LESSTVWAST LPRDEKLKDL 

      3370       3380       3390       3400       3410       3420 
CNDFPSHLEC TSGSKEMASG DSSTEQFSSE LQQCLQHTEK MHEYLTLLQD MKPPLDNQES 

      3430       3440       3450       3460       3470       3480 
LDNNLEALKN QLRQLETFEL GLAPIAVILR KDMKLAEEFL KSLPSDFPRG HVEELSISHQ 

      3490       3500       3510       3520       3530       3540 
SLKTAFSSLS NVSSERTKQI MLAIDSEMSK LAVSHEEFLH KLKSFSDWVS EKSKSVKDIE 

      3550       3560       3570       3580       3590       3600 
IVNVQDSEYV KKRLEFLKNV LKDLGHTKMQ LETTAFDVQF FISEYAQDLS PNQSKQLLRL 

      3610       3620       3630       3640       3650       3660 
LNTTQKCFLD VQESVTTQVE RLETQLHLEQ DLDDQKIVAE RQQEYKEKLQ GICDLLTQTE 

      3670       3680       3690       3700       3710       3720 
NRLIGHQEAF MIGDGTVELK KYQSKQEELQ KDMQGSAQAL AEVVKNTENF LKENGEKLSQ 

      3730       3740       3750       3760       3770       3780 
EDKALIEQKL NEAKIKCEQL NLKAEQSKKE LDKVVTTAIK EETEKVAAVK QLEESKTKIE 

      3790       3800       3810       3820       3830       3840 
NLLDWLSNVD KDSERAGTKH KQVIEQNGTH FQEGDGKSAI GEEDEVNGNL LETDVDGQVG 

      3850       3860       3870       3880       3890       3900 
TTQENLNQQY QKVKAQHEKI ISQHQAVIIA TQSAQVLLEK QGQYLSPEEK EKLQKNMKEL 

      3910       3920       3930       3940       3950       3960 
KVHYETALAE SEKKMKLTHS LQEELEKFDA DYTEFEHWLQ QSEQELENLE AGADDINGLM 

      3970       3980       3990       4000       4010       4020 
TKLKRQKSFS EDVISHKGDL RYITISGNRV LEAAKSCSKR DGGKVDTSAT HREVQRKLDH 

      4030       4040       4050       4060       4070       4080 
ATDRFRSLYS KCNVLGNNLK DLVDKYQHYE DASCGLLAGL QACEATASKH LSEPIAVDPK 

      4090       4100       4110       4120       4130       4140 
NLQRQLEETK ALQGQISSQQ VAVEKLKKTA EVLLDARGSL LPAKNDIQKT LDDIVGRYED 

      4150       4160       4170       4180       4190       4200 
LSKSVNERNE KLQITLTRSL SVQDGLDEML DWMGNVESSL KEQGQVPLNS TALQDIISKN 

      4210       4220       4230       4240       4250       4260 
IMLEQDIAGR QSSINAMNEK VKKFMETTDP STASSLQAKM KDLSARFSEA SHKHKETLAK 

      4270       4280       4290       4300       4310       4320 
MEELKTKVEL FENLSEKLQT FLETKTQALT EVDVPGKDVT ELSQYMQEST SEFLEHKKHL 

      4330       4340       4350       4360       4370       4380 
EVLHSLLKEI SSHGLPSDKA LVLEKTNNLS KKFKEMEDTI KEKKEAVTSC QEQLDAFQVL 

      4390       4400       4410       4420       4430       4440 
VKSLKSWIKE TTKKVPIVQP SFGAEDLGKS LEDTKKLQEK WSLKTPEIQK VNNSGISLCN 

      4450       4460       4470       4480       4490       4500 
LISAVTTPAK AIAAVKSGGA VLNGEGTATN TEEFWANKGL TSIKKDMTDI SHGYEDLGLL 

      4510       4520       4530       4540       4550       4560 
LKDKIAELNT KLSKLQKAQE ESSAMMQWLQ KMNKTATKWQ QTPAPTDTEA VKTQVEQNKS 

      4570       4580       4590       4600       4610       4620 
FEAELKQNVN KVQELKDKLT ELLEENPDTP EAPRWKQMLT EIDSKWQELN QLTIDRQQKL 

      4630       4640       4650       4660       4670       4680 
EESSNNLTQF QTVEAQLKQW LVEKELMVSV LGPLSIDPNM LNTQRQQVQI LLQEFATRKP 

      4690       4700       4710       4720       4730       4740 
QYEQLTAAGQ GILSRPGEDP SLRGIVKEQL AAVTQKWDSL TGQLSDRCDW IDQAIVKSTQ 

      4750       4760       4770       4780       4790       4800 
YQSLLRSLSD KLSDLDNKLS SSLAVSTHPD AMNQQLETAQ KMKQEIQQEK KQIKVAQALC 

      4810       4820       4830       4840       4850       4860 
EDLSALVKEE YLKAELSRQL EGILKSFKDV EQKAENHVQH LQSACASSHQ FQQMSRDFQA 

      4870       4880       4890       4900       4910       4920 
WLDTKKEEQN KSHPISAKLD VLESLIKDHK DFSKTLTAQS HMYEKTIAEG ENLLLKTQGS 

      4930       4940       4950       4960       4970       4980 
EKAALQLQLN TIKTNWDTFN KQVKERENKL KESLEKALKY KEQVETLWPW IDKCQNNLEE 

      4990       5000       5010       5020       5030       5040 
IKFCLDPAEG ENSIAKLKSL QKEMDQHFGM VELLNNTANS LLSVCEIDKE VVTDENKSLI 

      5050       5060       5070       5080       5090       5100 
QKVDMVTEQL HSKKFCLENM TQKFKEFQEV SKESKRQLQC AKEQLDIHDS LGSQAYSNKY 

      5110       5120       5130       5140       5150       5160 
LTMLQTQQKS LQALKHQVDL AKRLAQDLVV EASDSKGTSD VLLQVETIAQ EHSTLSQQVD 

      5170       5180       5190       5200       5210       5220 
EKCSFLETKL QGIGHFQNTI REMFSQFAEF DDELDSMAPV GRDAETLQKQ KETIKAFLKK 

      5230       5240       5250       5260       5270       5280 
LEALMASNDN ANKTCKMMLA TEETSPDLVG IKRDLEALSK QCNKLLDRAQ AREEQVEGTI 

      5290       5300       5310       5320       5330       5340 
KRLEEFYSKL KEFSILLQKA EEHEESQGPV GMETETINQQ LNMFKVFQKE EIEPLQGKQQ 

      5350       5360       5370       5380       5390       5400 
DVNWLGQGLI QSAAKSTSTQ GLEHDLDDVN ARWKTLNKKV AQRAAQLQEA LLHCGRFQDA 

      5410       5420       5430       5440       5450       5460 
LESLLSWMVD TEELVANQKP PSAEFKVVKA QIQEQKLLQR LLDDRKSTVE VIKREGEKIA 

      5470       5480       5490       5500       5510       5520 
TTAEPADKVK ILKQLSLLDS RWEALLNKAE TRNRQLEGIS VVAQQFHETL EPLNEWLTTI 

      5530       5540       5550       5560       5570       5580 
EKRLVNCEPI GTQASKLEEQ IAQHKALEDD IINHNKHLHQ AVSIGQSLKV LSSREDKDMV 

      5590       5600       5610       5620       5630       5640 
QSKLDFSQVW YIEIQEKSHS RSELLQQALC NAKIFGEDEV ELMNWLNEVH DKLSKLSVQD 

      5650       5660       5670       5680       5690       5700 
YSTEGLWKQQ SELRVLQEDI LLRKQNVDQA LLNGLELLKQ TTGDEVLIIQ DKLEAIKARY 

      5710       5720       5730       5740       5750       5760 
KDITKLSTDV AKTLEQALQL ARRLHSTHEE LCTWLDKVEV ELLSYETQVL KGEEASQAQM 

      5770       5780       5790       5800       5810       5820 
RPKELKKEAK NNKALLDSLN EVSSALLELV PWRAREGLEK MVAEDNERYR LVSDTITQKV 

      5830       5840       5850       5860       5870       5880 
EEIDAAILRS QQFDQAADAE LSWITETEKK LMSLGDIRLE QDQTSAQLQV QKTFTMEILR 

      5890       5900       5910       5920       5930       5940 
HKDIIDDLVK SGHKIMTACS EEEKQSMKKK LDKVLKNYDT ICQINSERYL QLERAQSLVN 

      5950       5960       5970       5980       5990       6000 
QFWETYEELW PWLTETQSII SQLPAPALEY ETLRQQQEEH RQLRELIAEH KPHIDKMNKT 

      6010       6020       6030       6040       6050       6060 
GPQLLELSPG EGFSIQEKYV AADTLYSQIK EDVKKRAVAL DEAISQSTQF HDKIDQILES 

      6070       6080       6090       6100       6110       6120 
LERIVERLRQ PPSISAEVEK IKEQISENKN VSVDMEKLQP LYETLKQRGE EMIARSGGTD 

      6130       6140       6150       6160       6170       6180 
KDISAKAVQD KLDQMVFIWE NIHTLVEERE AKLLDVMELA EKFWCDHMSL IVTIKDTQDF 

      6190       6200       6210       6220       6230       6240 
IRDLEDPGID PSVVKQQQEA AETIREEIDG LQEELDIVIN LGSELIAACG EPDKPIVKKS 

      6250       6260       6270       6280       6290       6300 
IDELNSAWDS LNKAWKDRID KLEEAMQAAV QYQDGLQAVF DWVDIAGGKL ASMSPIGTDL 

      6310       6320       6330       6340       6350       6360 
ETVKQQIEEL KQFKSEAYQQ QIEMERLNHQ AELLLKKVTE ESDKHTVQDP LMELKLIWDS 

      6370       6380       6390       6400       6410       6420 
LEERIINRQH KLEGALLALG QFQHALDELL AWLTHTEGLL SEQKPVGGDP KAIEIELAKH 

      6430       6440       6450       6460       6470       6480 
HVLQNDVLAH QSTVEAVNKA GNDLIESSAG EEASNLQNKL EVLNQRWQNV LEKTEQRKQQ 

      6490       6500       6510       6520       6530       6540 
LDGALRQAKG FHGEIEDLQQ WLTDTERHLL ASKPLGGLPE TAKEQLNVHM EVCAAFEAKE 

      6550       6560       6570       6580       6590       6600 
ETYKSLMQKG QQMLARCPKS AETNIDQDIN NLKEKWESVE TKLNERKTKL EEALNLAMEF 

      6610       6620       6630       6640       6650       6660 
HNSLQDFINW LTQAEQTLNV ASRPSLILDT VLFQIDEHKV FANEVNSHRE QIIELDKTGT 

      6670       6680       6690       6700       6710       6720 
HLKYFSQKQD VVLIKNLLIS VQSRWEKVVQ RLVERGRSLD DARKRAKQFH EAWSKLMEWL 

      6730       6740       6750       6760       6770       6780 
EESEKSLDSE LEIANDPDKI KTQLAQHKEF QKSLGAKHSV YDTTNRTGRS LKEKTSLADD 

      6790       6800       6810       6820       6830       6840 
NLKLDDMLSE LRDKWDTICG KSVERQNKLE EALLFSGQFT DALQALIDWL YRVEPQLAED 

      6850       6860       6870       6880       6890       6900 
QPVHGDIDLV MNLIDNHKAF QKELGKRTSS VQALKRSARE LIEGSRDDSS WVKVQMQELS 

      6910       6920       6930       6940       6950       6960 
TRWETVCALS ISKQTRLEAA LRQAEEFHSV VHALLEWLAE AEQTLRFHGV LPDDEDALRT 

      6970       6980       6990       7000       7010       7020 
LIDQHKEFMK KLEEKRAELN KATTMGDTVL AICHPDSITT IKHWITIIRA RFEEVLAWAK 

      7030       7040       7050       7060       7070       7080 
QHQQRLASAL AGLIAKQELL EALLAWLQWA ETTLTDKDKE VIPQEIEEVK ALIAEHQTFM 

      7090       7100       7110       7120       7130       7140 
EEMTRKQPDV DKVTKTYKRR AADPSSLQSH IPVLDKGRAG RKRFPASSLY PSGSQTQIET 

      7150       7160       7170       7180       7190       7200 
KNPRVNLLVS KWQQVWLLAL ERRRKLNDAL DRLEELREFA NFDFDIWRKK YMRWMNHKKS 

      7210       7220       7230       7240       7250       7260 
RVMDFFRRID KDQDGKITRQ EFIDGILSSK FPTSRLEMSA VADIFDRDGD GYIDYYEFVA 

      7270       7280       7290       7300       7310       7320 
ALHPNKDAYK PITDADKIED EVTRQVAKCK CAKRFQVEQI GDNKYRFFLG NQFGDSQQLR 

      7330       7340       7350       7360       7370       7380 
LVRILRSTVM VRVGGGWMAL DEFLVKNDPC RVHHHGSKML RSESNSSITT TQPTIAKGRT 

      7390       7400       7410       7420       7430       7440 
NMELREKFIL ADGASQGMAA FRPRGRRSRP SSRGASPNRS TSVSSQAAQA ASPQVPATTT 

      7450       7460       7470       7480       7490       7500 
PKGTPIQGSK LRLPGYLSGK GFHSGEDSGL ITTAAARVRT QFADSKKTPS RPGSRAGSKA 

      7510       7520       7530       7540       7550       7560 
GSRASSRRGS DASDFDISEI QSVCSDVETV PQTHRPTPRA GSRPSTAKPS KIPTPQRKSP 

      7570 
ASKLDKSSKR 

« Hide

Isoform 2 (BPAG1-a) (BPAG1eA) (Dystonin-1) (eA) [UniParc].

Checksum: EF1B5C94E21ED130
Show »

FASTA5,171591,036
Isoform 3 (BPAG1e) (eBPAG1) [UniParc].

Checksum: 5D0C62D26120E069
Show »

FASTA2,649306,755
Isoform 4 (BPAG1eA) (eB) [UniParc].

Checksum: 71C7175B93F7E1EC
Show »

FASTA3,060345,032
Isoform 5 [UniParc].

Checksum: D462C85D9FA1C903
Show »

FASTA44750,373
Isoform 6 (BPAG1n1) (BPAG1n2) (Dystonin-2) [UniParc].

Checksum: 9AD0D616AC22B94E
Show »

FASTA22425,379
Isoform 7 (BPAG1n3) [UniParc].

Checksum: 8C50813157B4E7D3
Show »

FASTA819,221
Isoform 8 [UniParc].

Checksum: AB344F0B597C1961
Show »

FASTA905102,868

References

« Hide 'large scale' references
[1]"Human bullous pemphigoid antigen (BPAG1). Amino acid sequences deduced from cloned cDNAs predict biologically important peptide segments and protein domains."
Sawamura D., Li K., Chu M.-L., Uitto J.
J. Biol. Chem. 266:17784-17790(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), DISEASE.
Tissue: Keratinocyte.
[2]"Cloning of the 5' mRNA for the 230-kD bullous pemphigoid antigen by rapid amplification of cDNA ends."
Elgart G.W., Stanley J.R.
J. Invest. Dermatol. 101:244-246(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
Tissue: Keratinocyte.
[3]"Novel alternative splicings of BPAG1 (bullous pemphigoid antigen 1) including the domain structure closely related to MACF (microtubule actin cross-linking factor)."
Okumura M., Yamakawa H., Ohara O., Owaribe K.
J. Biol. Chem. 277:6682-6687(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [MRNA] OF 1-3386 (ISOFORM 4), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Tissue: Keratinocyte.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 8), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4114-6568 (ISOFORM 1), VARIANT ALA-5138.
Tissue: Brain, Hippocampus, Placenta and Tongue.
[5]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"Cloning and characterization of the neural isoforms of human dystonin."
Brown A., Dalpe G., Mathieu M., Kothary R.
Genomics 29:777-780(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-461 (ISOFORM 1), NUCLEOTIDE SEQUENCE [MRNA] OF 1-46 (ISOFORM 6).
Tissue: Fetal brain and Retina.
[7]"Integrators of the cytoskeleton that stabilize microtubules."
Yang Y., Bauer C., Strasser G., Wollman R., Julien J.P., Fuchs E.
Cell 98:229-238(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-188 (ISOFORM 7), ALTERNATIVE SPLICING (ISOFORMS 6 AND 7), FUNCTION OF ISOFORMS 6 AND 7, SUBCELLULAR LOCATION (ISOFORMS 6 AND 7).
Tissue: Fetal brain.
[8]Geerts D., Sonnenberg A.
Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 208-308 (ISOFORM 1).
Tissue: Pineal gland.
[9]"Comparison of molecularly cloned bullous pemphigoid antigen to desmoplakin I confirms that they define a new family of cell adhesion junction plaque proteins."
Tanaka T., Parry D.A.D., Klaus-Kovtun V., Steinert P.M., Stanley J.R.
J. Biol. Chem. 266:12555-12559(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 881-7570 (ISOFORM 3).
Tissue: Keratinocyte.
[10]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3754-7570 (ISOFORM 5).
Tissue: Duodenum.
[11]"Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 5:277-286(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5947-7570 (ISOFORM 2).
Tissue: Brain.
[12]"Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION.
[13]"Isolation of complementary DNA for bullous pemphigoid antigen by use of patients' autoantibodies."
Stanley J.R., Tanaka T., Mueller S., Klaus-Kovtun V., Roop D.
J. Clin. Invest. 82:1864-1870(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
Tissue: Keratinocyte.
[14]"The hemidesmosomal plaque. I. Characterization of a major constituent protein as a differentiation marker for certain forms of epithelia."
Owaribe K., Kartenbeck J., Stumpp S., Magin T.M., Krieg T., Diaz L.A., Franke W.W.
Differentiation 45:207-220(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
[15]"Identification of a second protein product of the gene encoding a human epidermal autoantigen."
Hopkinson S.B., Jones J.C.
Biochem. J. 300:851-857(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM 3).
[16]"An essential cytoskeletal linker protein connecting actin microfilaments to intermediate filaments."
Yang Y., Dowling J., Yu Q.C., Kouklis P., Cleveland D.W., Fuchs E.
Cell 86:655-665(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING (ISOFORMS 3 AND 6), TISSUE SPECIFICITY.
[17]"The N terminus of the transmembrane protein BP180 interacts with the N-terminal domain of BP230, thereby mediating keratin cytoskeleton anchorage to the cell surface at the site of the hemidesmosome."
Hopkinson S.B., Jones J.C.
Mol. Biol. Cell 11:277-286(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING (ISOFORM 3), INTERACTION WITH COL17A1 AND ITGB4.
[18]"Structural analysis of the predicted coiled-coil rod domain of the cytoplasmic bullous pemphigoid antigen (BPAG1). Empirical localization of the N-terminal globular domain-rod boundary."
Tang H.-Y., Chaffotte A.-F., Thacher S.M.
J. Biol. Chem. 271:9716-9722(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: DOMAINS.
[19]"The hemidesmosomal protein bullous pemphigoid antigen 1 and the integrin beta 4 subunit bind to ERBIN. Molecular cloning of multiple alternative splice variants of ERBIN and analysis of their tissue expression."
Favre B., Fontao L., Koster J., Shafaatian R., Jaunin F., Saurat J.-H., Sonnenberg A., Borradori L.
J. Biol. Chem. 276:32427-32436(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ITGB4 AND ERBB2IP.
[20]"Analysis of the interactions between BP180, BP230, plectin and the integrin alpha6beta4 important for hemidesmosome assembly."
Koster J., Geerts D., Favre B., Borradori L., Sonnenberg A.
J. Cell Sci. 116:387-399(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING (ISOFORM 3), FUNCTION OF ISOFORM 3, INTERACTION WITH COL17A1 AND ITGB4, SUBCELLULAR LOCATION (ISOFORM 3).
[21]"Interaction of the bullous pemphigoid antigen 1 (BP230) and desmoplakin with intermediate filaments is mediated by distinct sequences within their COOH terminus."
Fontao L., Favre B., Riou S., Geerts D., Jaunin F., Saurat J.H., Green K.J., Sonnenberg A., Borradori L.
Mol. Biol. Cell 14:1978-1992(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING (ISOFORM 3), ASSOCIATION WITH KERATIN FILAMENTS, SUBCELLULAR LOCATION (ISOFORM 3).
[22]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7432, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[23]"BPAG1e maintains keratinocyte polarity through beta4 integrin-mediated modulation of Rac1 and cofilin activities."
Hamill K.J., Hopkinson S.B., DeBiase P., Jones J.C.
Mol. Biol. Cell 20:2954-2962(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING (ISOFORM 3), FUNCTION OF ISOFORM 3, SUBCELLULAR LOCATION (ISOFORM 3).
[24]"BPAG1 isoform-b: complex distribution pattern in striated and heart muscle and association with plectin and alpha-actinin."
Steiner-Champliaud M.F., Schneider Y., Favre B., Paulhe F., Praetzel-Wunder S., Faulkner G., Konieczny P., Raith M., Wiche G., Adebola A., Liem R.K., Langbein L., Sonnenberg A., Fontao L., Borradori L.
Exp. Cell Res. 316:297-313(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING (ISOFORM 1), HOMODIMERIZATION, INTERACTION WITH ACTN2 AND PLEC, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[25]"A homozygous nonsense mutation within the dystonin gene coding for the coiled-coil domain of the epithelial isoform of BPAG1 underlies a new subtype of autosomal recessive epidermolysis bullosa simplex."
Groves R.W., Liu L., Dopping-Hepenstal P.J., Markus H.S., Lovell P.A., Ozoemena L., Lai-Cheong J.E., Gawler J., Owaribe K., Hashimoto T., Mellerio J.E., Mee J.B., McGrath J.A.
J. Invest. Dermatol. 130:1551-1557(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN EBSB2.
[26]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[27]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2919, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[28]"Hereditary sensory autonomic neuropathy caused by a mutation in dystonin."
Edvardson S., Cinnamon Y., Jalas C., Shaag A., Maayan C., Axelrod F.B., Elpeleg O.
Ann. Neurol. 71:569-572(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN HSAN6.
[29]"Autosomal recessive epidermolysis bullosa simplex due to loss of BPAG1-e expression."
Liu L., Dopping-Hepenstal P.J., Lovell P.A., Michael M., Horn H., Fong K., Lai-Cheong J.E., Mellerio J.E., Parsons M., McGrath J.A.
J. Invest. Dermatol. 132:742-744(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN EBSB2.
[30]"Identification of IGPR-1 as a novel adhesion molecule involved in angiogenesis."
Rahimi N., Rezazadeh K., Mahoney J.E., Hartsough E., Meyer R.D.
Mol. Biol. Cell 23:1646-1656(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TMIGD2.
[31]"An EB1-binding motif acts as a microtubule tip localization signal."
Honnappa S., Gouveia S.M., Weisbrich A., Damberger F.F., Bhavesh N.S., Jawhari H., Grigoriev I., van Rijssel F.J., Buey R.M., Lawera A., Jelesarov I., Winkler F.K., Wuthrich K., Akhmanova A., Steinmetz M.O.
Cell 138:366-376(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 7541-7570 IN COMPLEX WITH MAPRE1, DOMAIN MICROTUBULE TIP LOCALIZATION SIGNAL, MUTAGENESIS OF LYS-7548; SER-7550; ILE-7552; PRO-7553 AND 7557-ARG-LYS-7558.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M69225 mRNA. No translation available.
L11690 mRNA. Translation: AAA52288.1.
AF400226 mRNA. Translation: AAL62061.1.
AF400227 mRNA. Translation: AAL62062.1.
AK055189 mRNA. Translation: BAB70870.1. Different initiation.
AK094883 mRNA. Translation: BAC04449.1. Different initiation.
AK096713 mRNA. Translation: BAC04848.1. Different initiation.
AK295864 mRNA. Translation: BAH12207.1.
AL049215 Genomic DNA. No translation available.
AL512422 expand/collapse EMBL AC list , AL096710, AL137008, AL512448, AL590005 Genomic DNA. Translation: CAI14341.1. Sequence problems.
AL590005 expand/collapse EMBL AC list , AL096710, AL137008, AL512422, AL512448 Genomic DNA. Translation: CAI14989.1. Sequence problems.
AL512448 expand/collapse EMBL AC list , AL096710, AL137008, AL512422, AL590005 Genomic DNA. Translation: CAI16609.1. Sequence problems.
AL512448, AL096710, AL137008 Genomic DNA. Translation: CAI16610.1. Sequence problems.
AL137008 expand/collapse EMBL AC list , AL096710, AL512422, AL512448, AL590005 Genomic DNA. Translation: CAI20330.1. Sequence problems.
AL137008, AL096710, AL512448 Genomic DNA. Translation: CAI20332.1. Sequence problems.
AL096710 expand/collapse EMBL AC list , AL137008, AL512422, AL512448, AL590005 Genomic DNA. Translation: CAI22044.1. Sequence problems.
AL096710, AL137008, AL512448 Genomic DNA. Translation: CAI22045.1. Sequence problems.
AL096710 Genomic DNA. Translation: CAI22046.1.
AL096710 Genomic DNA. Translation: CAI22047.1.
U31850 mRNA. Translation: AAC50243.1.
U31851 mRNA. Translation: AAC50244.1. Frameshift.
AF165191 mRNA. Translation: AAD49334.1.
AY032900 mRNA. Translation: AAK63130.1.
AY032901 mRNA. Translation: AAK63131.1.
M63618 mRNA. Translation: AAA35606.1.
BC016991 mRNA. Translation: AAH16991.1.
AB018271 mRNA. Translation: BAA34448.2.
M22942 mRNA. Translation: AAA35538.1. Sequence problems.
X58677 mRNA. Translation: CAA41528.1.
U04850 Genomic DNA. Translation: AAA57184.1.
U04850 Genomic DNA. Translation: AAA57185.1. Sequence problems.
PIRA40937. I56317.
RefSeqNP_001138241.1. NM_001144769.2.
NP_001138242.1. NM_001144770.1.
NP_001714.1. NM_001723.5.
NP_056363.2. NM_015548.4.
NP_899236.1. NM_183380.3.
UniGeneHs.604915.
Hs.669931.
Hs.728928.
Hs.735651.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3GJOX-ray2.50E/F/G/H7541-7570[»]
ProteinModelPortalQ03001.
SMRQ03001. Positions 31-255, 583-795.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107135. 36 interactions.
DIPDIP-33131N.
IntActQ03001. 31 interactions.
MINTMINT-119936.

PTM databases

PhosphoSiteQ03001.

Polymorphism databases

DMDM294862529.

Proteomic databases

PaxDbQ03001.
PRIDEQ03001.

Protocols and materials databases

DNASU667.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000244364; ENSP00000244364; ENSG00000151914. [Q03001-8]
ENST00000370765; ENSP00000359801; ENSG00000151914. [Q03001-3]
ENST00000439203; ENSP00000404924; ENSG00000151914. [Q03001-9]
GeneID667.
KEGGhsa:667.
UCSCuc003pcy.4. human. [Q03001-8]
uc003pdc.4. human. [Q03001-3]
uc003pde.2. human. [Q03001-13]
uc021zax.1. human. [Q03001-9]
uc021zay.2. human. [Q03001-7]

Organism-specific databases

CTD667.
GeneCardsGC06M056370.
H-InvDBHIX0005976.
HIX0164999.
HGNCHGNC:1090. DST.
HPAHPA030200.
MIM113810. gene.
614653. phenotype.
615425. phenotype.
neXtProtNX_Q03001.
Orphanet89838. Autosomal recessive epidermolysis bullosa simplex.
314381. Hereditary sensory and autonomic neuropathy type 6.
PharmGKBPA25399.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5069.
HOVERGENHBG031127.
InParanoidQ8WXK8.
KOK10382.
OMARKITEIQ.
PhylomeDBQ03001.
TreeFamTF335163.

Enzyme and pathway databases

ReactomeREACT_111155. Cell-Cell communication.
REACT_118779. Extracellular matrix organization.

Gene expression databases

ArrayExpressQ03001.
BgeeQ03001.
CleanExHS_DST.
GenevestigatorQ03001.

Family and domain databases

Gene3D1.10.238.10. 1 hit.
1.10.418.10. 2 hits.
3.30.920.20. 1 hit.
3.90.1290.10. 2 hits.
InterProIPR001589. Actinin_actin-bd_CS.
IPR001715. CH-domain.
IPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR003108. GAS2_dom.
IPR001101. Plectin_repeat.
IPR018159. Spectrin/alpha-actinin.
IPR002017. Spectrin_repeat.
[Graphical view]
PfamPF00307. CH. 2 hits.
PF13499. EF-hand_7. 1 hit.
PF02187. GAS2. 1 hit.
PF00681. Plectin. 5 hits.
PF00435. Spectrin. 19 hits.
[Graphical view]
SMARTSM00033. CH. 2 hits.
SM00054. EFh. 2 hits.
SM00243. GAS2. 1 hit.
SM00250. PLEC. 8 hits.
SM00150. SPEC. 32 hits.
[Graphical view]
SUPFAMSSF143575. SSF143575. 1 hit.
SSF47576. SSF47576. 1 hit.
SSF75399. SSF75399. 2 hits.
PROSITEPS00019. ACTININ_1. 1 hit.
PS00020. ACTININ_2. 1 hit.
PS50021. CH. 2 hits.
PS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 2 hits.
PS51460. GAR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSDST. human.
EvolutionaryTraceQ03001.
GeneWikiDystonin.
GenomeRNAi667.
NextBio2720.
PROQ03001.
SOURCESearch...

Entry information

Entry nameDYST_HUMAN
AccessionPrimary (citable) accession number: Q03001
Secondary accession number(s): B7Z3H1 expand/collapse secondary AC list , O94833, Q12825, Q13266, Q13267, Q13775, Q5TBT0, Q5TBT2, Q5TF23, Q5TF24, Q8N1T8, Q8N8J3, Q8WXK8, Q8WXK9, Q96AK9, Q96DQ5, Q96J76, Q96QT5, Q9H555, Q9UGD7, Q9UGD8, Q9UN10
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: April 20, 2010
Last modified: April 16, 2014
This is version 161 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM