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Q03001

- DYST_HUMAN

UniProt

Q03001 - DYST_HUMAN

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Protein
Dystonin
Gene
DST, BP230, BP240, BPAG1, DMH, DT, KIAA0728
Organism
Homo sapiens (Human)
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.3 Publications
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.3 Publications
Isoform 6: required for bundling actin filaments around the nucleus By similarity.3 Publications
Isoform 7: regulates the organization and stability of the microtubule network of sensory neurons to allow axonal transport.3 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi7210 – 7221121 Reviewed prediction
Add
BLAST
Calcium bindingi7246 – 7257122 Reviewed prediction
Add
BLAST

GO - Molecular functioni

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

GO - Biological processi

  1. axonogenesis Source: Ensembl
  2. cell adhesion Source: UniProtKB-KW
  3. cell cycle arrest Source: InterPro
  4. cell motility Source: UniProtKB
  5. cytoplasmic microtubule organization Source: Ensembl
  6. cytoskeleton organization Source: UniProtKB
  7. extracellular matrix organization Source: Reactome
  8. hemidesmosome assembly Source: UniProtKB
  9. integrin-mediated signaling pathway Source: UniProtKB
  10. intermediate filament cytoskeleton organization Source: UniProtKB
  11. maintenance of cell polarity Source: UniProtKB
  12. microtubule cytoskeleton organization Source: UniProtKB
  13. regulation of microtubule polymerization or depolymerization Source: Ensembl
  14. response to wounding Source: UniProtKB
  15. retrograde axon cargo transport Source: Ensembl
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_150180. Assembly of collagen fibrils and other multimeric structures.
REACT_20537. Type I hemidesmosome assembly.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:DST
Synonyms:BP230, BP240, BPAG1, DMH, DT, KIAA0728
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:1090. DST.

Subcellular locationi

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.6 Publications
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.6 Publications
Isoform 2 : Cytoplasmcytoskeleton By similarity
Note: Colocalizes both cortical and cytoplasmic actin filaments By similarity.6 Publications
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.6 Publications
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.6 Publications
Isoform 7 : Cytoplasmcytoskeleton. Cell projectionaxon. Membrane
Note: Associates with axonal microtubules and intermediate filaments, but not with actin cytoskeleton, in sensory neurons.6 Publications
Isoform 8 : Cytoplasmcytoskeleton By similarity. Cytoplasmcell cortex By similarity. Cell membrane; Lipid-anchor By similarity 6 Publications

GO - Cellular componenti

  1. H zone Source: UniProtKB-SubCell
  2. Z disc Source: UniProtKB
  3. actin cytoskeleton Source: UniProtKB
  4. axon Source: UniProtKB
  5. basal plasma membrane Source: UniProtKB
  6. basement membrane Source: ProtInc
  7. cell cortex Source: UniProtKB-SubCell
  8. cell leading edge Source: UniProtKB
  9. cytoplasm Source: UniProtKB
  10. cytoplasmic membrane-bounded vesicle Source: MGI
  11. cytosol Source: Reactome
  12. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  13. extracellular vesicular exosome Source: UniProt
  14. hemidesmosome Source: UniProtKB
  15. integral component of membrane Source: UniProtKB-KW
  16. intermediate filament Source: UniProtKB-KW
  17. intermediate filament cytoskeleton Source: UniProtKB
  18. microtubule cytoskeleton Source: HPA
  19. microtubule plus-end Source: UniProtKB
  20. neurofilament cytoskeleton Source: Ensembl
  21. nuclear envelope Source: UniProtKB-SubCell
  22. nucleus Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Involvement in diseasei

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.2 Publications
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.3 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi7548 – 75481K → Q: Loss of interaction with MAPRE1 and association with microtubule growing ends. 1 Publication
Mutagenesisi7550 – 75501S → A or N: Loss of association with microtubule growing ends. 1 Publication
Mutagenesisi7552 – 75521I → N: Loss of interaction with MAPRE1 and association with the growing microtubule plus ends; when associated with N-7553. 1 Publication
Mutagenesisi7553 – 75531P → N: Loss of interaction with MAPRE1 and association with the growing microtubule plus ends; when associated with N-7552. 1 Publication
Mutagenesisi7557 – 75571R → N: Loss of interaction with MAPRE1 and association with the growing microtubule plus ends.
Mutagenesisi7558 – 75581K → N: Loss of interaction with MAPRE1 and association with the growing microtubule plus ends.

Keywords - Diseasei

Epidermolysis bullosa, Neuropathy

Organism-specific databases

MIMi614653. phenotype.
615425. phenotype.
Orphaneti89838. Autosomal recessive epidermolysis bullosa simplex.
314381. Hereditary sensory and autonomic neuropathy type 6.
PharmGKBiPA25399.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 75707570Dystonin
PRO_0000078138Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2919 – 29191Phosphoserine1 Publication
Cross-linki5470 – 5470Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Modified residuei7432 – 74321Phosphoserine1 Publication

Keywords - PTMi

Isopeptide bond, Lipoprotein, Palmitate, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ03001.
PaxDbiQ03001.
PRIDEiQ03001.

PTM databases

PhosphoSiteiQ03001.

Expressioni

Tissue specificityi

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.3 Publications

Gene expression databases

ArrayExpressiQ03001.
BgeeiQ03001.
CleanExiHS_DST.
GenevestigatoriQ03001.

Organism-specific databases

HPAiHPA030200.

Interactioni

Subunit structurei

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 TMIGD2.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
P299914EBI-310758,EBI-8826488From a different organism.
APPL1Q9UKG13EBI-310758,EBI-741243
DISC1Q9NRI55EBI-310758,EBI-529989
MAPRE1Q156912EBI-310758,EBI-1004115
Mapre1Q611663EBI-310758,EBI-2027055From a different organism.
OPTNQ96CV92EBI-310758,EBI-748974

Protein-protein interaction databases

BioGridi107135. 36 interactions.
DIPiDIP-33131N.
IntActiQ03001. 31 interactions.
MINTiMINT-119936.

Structurei

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3GJOX-ray2.50E/F/G/H7541-7570[»]
ProteinModelPortaliQ03001.
SMRiQ03001. Positions 31-255, 583-795.

Miscellaneous databases

EvolutionaryTraceiQ03001.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini35 – 252218Actin-binding
Add
BLAST
Domaini35 – 138104CH 1
Add
BLAST
Domaini151 – 252102CH 2
Add
BLAST
Repeati701 – 79797Spectrin 1
Add
BLAST
Domaini890 – 94253SH3
Add
BLAST
Repeati1584 – 162643Plectin 1
Add
BLAST
Repeati1660 – 170344Plectin 2
Add
BLAST
Repeati1774 – 181744Plectin 3
Add
BLAST
Repeati1818 – 185538Plectin 4
Add
BLAST
Repeati1856 – 189136Plectin 5
Add
BLAST
Repeati3924 – 400077Spectrin 2
Add
BLAST
Repeati4069 – 415385Spectrin 3
Add
BLAST
Repeati4514 – 4622109Spectrin 4
Add
BLAST
Repeati4626 – 4731106Spectrin 5
Add
BLAST
Repeati4849 – 4952104Spectrin 6
Add
BLAST
Repeati5281 – 5389109Spectrin 7
Add
BLAST
Repeati5396 – 5497102Spectrin 8
Add
BLAST
Repeati5504 – 5606103Spectrin 9
Add
BLAST
Repeati5829 – 5933105Spectrin 10
Add
BLAST
Repeati5940 – 6042103Spectrin 11
Add
BLAST
Repeati6048 – 6154107Spectrin 12
Add
BLAST
Repeati6184 – 626481Spectrin 13
Add
BLAST
Repeati6270 – 6373104Spectrin 14
Add
BLAST
Repeati6379 – 6481103Spectrin 15
Add
BLAST
Repeati6490 – 6592103Spectrin 16
Add
BLAST
Repeati6597 – 6700104Spectrin 17
Add
BLAST
Repeati6705 – 6811107Spectrin 18
Add
BLAST
Repeati6818 – 6918101Spectrin 19
Add
BLAST
Repeati6923 – 7026104Spectrin 20
Add
BLAST
Domaini7197 – 723236EF-hand 1
Add
BLAST
Domaini7233 – 726836EF-hand 2
Add
BLAST
Domaini7273 – 735179GAR
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1383 – 13897Nuclear localization signal; in isoform 6 By similarity
Motifi7550 – 75534Microtubule tip localization signal

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi2394 – 243138Asp-rich
Add
BLAST
Compositional biasi2592 – 25998Poly-Asp

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.2 Publications
The microtubule tip localization signal (MtLS) motif; mediates interaction with MAPRE1 and targeting to the growing microtubule plus ends.2 Publications

Sequence similaritiesi

Contains 2 EF-hand domains.
Contains 1 GAR domain.
Contains 5 plectin repeats.
Contains 1 SH3 domain.
Contains 20 spectrin repeats.

Keywords - Domaini

Coiled coil, Repeat, SH3 domain, Transmembrane

Phylogenomic databases

eggNOGiCOG5069.
HOVERGENiHBG031127.
InParanoidiQ8WXK8.
KOiK10382.
OMAiRKITEIQ.
PhylomeDBiQ03001.
TreeFamiTF335163.

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. 2 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. 19 hits.
[Graphical view]
SMARTiSM00033. CH. 2 hits.
SM00054. EFh. 2 hits.
SM00243. GAS2. 1 hit.
SM00250. PLEC. 8 hits.
SM00150. SPEC. 32 hits.
[Graphical view]
SUPFAMiSSF143575. SSF143575. 1 hit.
SSF47576. SSF47576. 1 hit.
SSF75399. SSF75399. 2 hits.
PROSITEiPS00019. ACTININ_1. 1 hit.
PS00020. ACTININ_2. 1 hit.
PS50021. CH. 2 hits.
PS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 2 hits.
PS51460. GAR. 1 hit.
[Graphical view]

Sequences (8)i

Sequence statusi: Complete.

This entry describes 8 isoformsi produced by alternative promoter usage and alternative splicing. Align

Isoform 1 (identifier: Q03001-7) [UniParc]FASTAAdd to Basket

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.

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MAGYLSPAAY LYVEEQEYLQ AYEDVLERYK DERDKVQKKT FTKWINQHLM     50
KVRKHVNDLY EDLRDGHNLI SLLEVLSGDT LPREKGRMRF HRLQNVQIAL 100
DYLKRRQVKL VNIRNDDITD GNPKLTLGLI WTIILHFQIS DIHVTGESED 150
MSAKERLLLW TQQATEGYAG IRCENFTTCW RDGKLFNAII HKYRPDLIDM 200
NTVAVQSNLA NLEHAFYVAE KIGVIRLLDP EDVDVSSPDE KSVITYVSSL 250
YDAFPKVPEG GEGIGANDVE VKWIEYQNMV NYLIQWIRHH VTTMSERTFP 300
NNPVELKALY NQYLQFKETE IPPKETEKSK IKRLYKLLEI WIEFGRIKLL 350
QGYHPNDIEK EWGKLIIAML EREKALRPEV ERLEMLQQIA NRVQRDSVIC 400
EDKLILAGNA LQSDSKRLES GVQFQNEAEI AGYILECENL LRQHVIDVQI 450
LIDGKYYQAD QLVQRVAKLR DEIMALRNEC SSVYSKGRIL TTEQTKLMIS 500
GITQSLNSGF AQTLHPSLTS GLTQSLTPSL TSSSMTSGLS SGMTSRLTPS 550
VTPAYTPGFP SGLVPNFSSG VEPNSLQTLK LMQIRKPLLK SSLLDQNLTE 600
EEINMKFVQD LLNWVDEMQV QLDRTEWGSD LPSVESHLEN HKNVHRAIEE 650
FESSLKEAKI SEIQMTAPLK LTYAEKLHRL ESQYAKLLNT SRNQERHLDT 700
LHNFVSRATN ELIWLNEKEE EEVAYDWSER NTNIARKKDY HAELMRELDQ 750
KEENIKSVQE IAEQLLLENH PARLTIEAYR AAMQTQWSWI LQLCQCVEQH 800
IKENTAYFEF FNDAKEATDY LRNLKDAIQR KYSCDRSSSI HKLEDLVQES 850
MEEKEELLQY KSTIANLMGK AKTIIQLKPR NSDCPLKTSI PIKAICDYRQ 900
IEITIYKDDE CVLANNSHRA KWKVISPTGN EAMVPSVCFT VPPPNKEAVD 950
LANRIEQQYQ NVLTLWHESH INMKSVVSWH YLINEIDRIR ASNVASIKTM 1000
LPGEHQQVLS NLQSRFEDFL EDSQESQVFS GSDITQLEKE VNVCKQYYQE 1050
LLKSAEREEQ EESVYNLYIS EVRNIRLRLE NCEDRLIRQI RTPLERDDLH 1100
ESVFRITEQE KLKKELERLK DDLGTITNKC EEFFSQAAAS SSVPTLRSEL 1150
NVVLQNMNQV YSMSSTYIDK LKTVNLVLKN TQAAEALVKL YETKLCEEEA 1200
VIADKNNIEN LISTLKQWRS EVDEKRQVFH ALEDELQKAK AISDEMFKTY 1250
KERDLDFDWH KEKADQLVER WQNVHVQIDN RLRDLEGIGK SLKYYRDTYH 1300
PLDDWIQQVE TTQRKIQENQ PENSKTLATQ LNQQKMLVSE IEMKQSKMDE 1350
CQKYAEQYSA TVKDYELQTM TYRAMVDSQQ KSPVKRRRMQ SSADLIIQEF 1400
MDLRTRYTAL VTLMTQYIKF AGDSLKRLEE EEKSLEEEKK EHVEKAKELQ 1450
KWVSNISKTL KDAEKAGKPP FSKQKISSEE ISTKKEQLSE ALQTIQLFLA 1500
KHGDKMTDEE RNELEKQVKT LQESYNLLFS ESLKQLQESQ TSGDVKVEEK 1550
LDKVIAGTID QTTGEVLSVF QAVLRGLIDY DTGIRLLETQ LMISGLISPE 1600
LRKCFDLKDA KSHGLIDEQI LCQLKELSKA KEIISAASPT TIPVLDALAQ 1650
SMITESMAIK VLEILLSTGS LVIPATGEQL TLQKAFQQNL VSSALFSKVL 1700
ERQNMCKDLI DPCTSEKVSL IDMVQRSTLQ ENTGMWLLPV RPQEGGRITL 1750
KCGRNISILR AAHEGLIDRE TMFRLLSAQL LSGGLINSNS GQRMTVEEAV 1800
REGVIDRDTA SSILTYQVQT GGIIQSNPAK RLTVDEAVQC DLITSSSALL 1850
VLEAQRGYVG LIWPHSGEIF PTSSSLQQEL ITNELAYKIL NGRQKIAALY 1900
IPESSQVIGL DAAKQLGIID NNTASILKNI TLPDKMPDLG DLEACKNARR 1950
WLSFCKFQPS TVHDYRQEED VFDGEEPVTT QTSEETKKLF LSYLMINSYM 2000
DANTGQRLLL YDGDLDEAVG MLLEGCHAEF DGNTAIKECL DVLSSSGVFL 2050
NNASGREKDE CTATPSSFNK CHCGEPEHEE TPENRKCAID EEFNEMRNTV 2100
INSEFSQSGK LASTISIDPK VNSSPSVCVP SLISYLTQTE LADISMLRSD 2150
SENILTNYEN QSRVETNERA NECSHSKNIQ NFPSDLIENP IMKSKMSKFC 2200
GVNETENEDN TNRDSPIFDY SPRLSALLSH DKLMHSQGSF NDTHTPESNG 2250
NKCEAPALSF SDKTMLSGQR IGEKFQDQFL GIAAINISLP GEQYGQKSLN 2300
MISSNPQVQY HNDKYISNTS GEDEKTHPGF QQMPEDKEDE SEIEEYSCAV 2350
TPGGDTDNAI VSLTCATPLL DETISASDYE TSLLNDQQNN TGTDTDSDDD 2400
FYDTPLFEDD DHDSLLLDGD DRDCLHPEDY DTLQEENDET ASPADVFYDV 2450
SKENENSMVP QGAPVGSLSV KNKAHCLQDF LMDVEKDELD SGEKIHLNPV 2500
GSDKVNGQSL ETGSERECTN ILEGDESDSL TDYDIVGGKE SFTASLKFDD 2550
SGSWRGRKEE YVTGQEFHSD TDHLDSMQSE ESYGDYIYDS NDQDDDDDDG 2600
IDEEGGGIRD ENGKPRCQNV AEDMDIQLCA SILNENSDEN ENINTMILLD 2650
KMHSCSSLEK QQRVNVVQLA SPSENNLVTE KSNLPEYTTE IAGKSKENLL 2700
NHEMVLKDVL PPIIKDTESE KTFGPASISH DNNNISSTSE LGTDLANTKV 2750
KLIQGSELPE LTDSVKGKDE YFKNMTPKVD SSLDHIICTE PDLIGKPAEE 2800
SHLSLIASVT DKDPQGNGSD LIKGRDGKSD ILIEDETSIQ KMYLGEGEVL 2850
VEGLVEEENR HLKLLPGKNT RDSFKLINSQ FPFPQITNNE ELNQKGSLKK 2900
ATVTLKDEPN NLQIIVSKSP VQFENLEEIF DTSVSKEISD DITSDITSWE 2950
GNTHFEESFT DGPEKELDLF TYLKHCAKNI KAKDVAKPNE DVPSHVLITA 3000
PPMKEHLQLG VNNTKEKSTS TQKDSPLNDM IQSNDLCSKE SISGGGTEIS 3050
QFTPESIEAT LSILSRKHVE DVGKNDFLQS ERCANGLGND NSSNTLNTDY 3100
SFLEINNKKE RIEQQLPKEQ ALSPRSQEKE VQIPELSQVF VEDVKDILKS 3150
RLKEGHMNPQ EVEEPSACAD TKILIQNLIK RITTSQLVNE ASTVPSDSQM 3200
SDSSGVSPMT NSSELKPESR DDPFCIGNLK SELLLNILKQ DQHSQKITGV 3250
FELMRELTHM EYDLEKRGIT SKVLPLQLEN IFYKLLADGY SEKIEHVGDF 3300
NQKACSTSEM MEEKPHILGD IKSKEGNYYS PNLETVKEIG LESSTVWAST 3350
LPRDEKLKDL CNDFPSHLEC TSGSKEMASG DSSTEQFSSE LQQCLQHTEK 3400
MHEYLTLLQD MKPPLDNQES LDNNLEALKN QLRQLETFEL GLAPIAVILR 3450
KDMKLAEEFL KSLPSDFPRG HVEELSISHQ SLKTAFSSLS NVSSERTKQI 3500
MLAIDSEMSK LAVSHEEFLH KLKSFSDWVS EKSKSVKDIE IVNVQDSEYV 3550
KKRLEFLKNV LKDLGHTKMQ LETTAFDVQF FISEYAQDLS PNQSKQLLRL 3600
LNTTQKCFLD VQESVTTQVE RLETQLHLEQ DLDDQKIVAE RQQEYKEKLQ 3650
GICDLLTQTE NRLIGHQEAF MIGDGTVELK KYQSKQEELQ KDMQGSAQAL 3700
AEVVKNTENF LKENGEKLSQ EDKALIEQKL NEAKIKCEQL NLKAEQSKKE 3750
LDKVVTTAIK EETEKVAAVK QLEESKTKIE NLLDWLSNVD KDSERAGTKH 3800
KQVIEQNGTH FQEGDGKSAI GEEDEVNGNL LETDVDGQVG TTQENLNQQY 3850
QKVKAQHEKI ISQHQAVIIA TQSAQVLLEK QGQYLSPEEK EKLQKNMKEL 3900
KVHYETALAE SEKKMKLTHS LQEELEKFDA DYTEFEHWLQ QSEQELENLE 3950
AGADDINGLM TKLKRQKSFS EDVISHKGDL RYITISGNRV LEAAKSCSKR 4000
DGGKVDTSAT HREVQRKLDH ATDRFRSLYS KCNVLGNNLK DLVDKYQHYE 4050
DASCGLLAGL QACEATASKH LSEPIAVDPK NLQRQLEETK ALQGQISSQQ 4100
VAVEKLKKTA EVLLDARGSL LPAKNDIQKT LDDIVGRYED LSKSVNERNE 4150
KLQITLTRSL SVQDGLDEML DWMGNVESSL KEQGQVPLNS TALQDIISKN 4200
IMLEQDIAGR QSSINAMNEK VKKFMETTDP STASSLQAKM KDLSARFSEA 4250
SHKHKETLAK MEELKTKVEL FENLSEKLQT FLETKTQALT EVDVPGKDVT 4300
ELSQYMQEST SEFLEHKKHL EVLHSLLKEI SSHGLPSDKA LVLEKTNNLS 4350
KKFKEMEDTI KEKKEAVTSC QEQLDAFQVL VKSLKSWIKE TTKKVPIVQP 4400
SFGAEDLGKS LEDTKKLQEK WSLKTPEIQK VNNSGISLCN LISAVTTPAK 4450
AIAAVKSGGA VLNGEGTATN TEEFWANKGL TSIKKDMTDI SHGYEDLGLL 4500
LKDKIAELNT KLSKLQKAQE ESSAMMQWLQ KMNKTATKWQ QTPAPTDTEA 4550
VKTQVEQNKS FEAELKQNVN KVQELKDKLT ELLEENPDTP EAPRWKQMLT 4600
EIDSKWQELN QLTIDRQQKL EESSNNLTQF QTVEAQLKQW LVEKELMVSV 4650
LGPLSIDPNM LNTQRQQVQI LLQEFATRKP QYEQLTAAGQ GILSRPGEDP 4700
SLRGIVKEQL AAVTQKWDSL TGQLSDRCDW IDQAIVKSTQ YQSLLRSLSD 4750
KLSDLDNKLS SSLAVSTHPD AMNQQLETAQ KMKQEIQQEK KQIKVAQALC 4800
EDLSALVKEE YLKAELSRQL EGILKSFKDV EQKAENHVQH LQSACASSHQ 4850
FQQMSRDFQA WLDTKKEEQN KSHPISAKLD VLESLIKDHK DFSKTLTAQS 4900
HMYEKTIAEG ENLLLKTQGS EKAALQLQLN TIKTNWDTFN KQVKERENKL 4950
KESLEKALKY KEQVETLWPW IDKCQNNLEE IKFCLDPAEG ENSIAKLKSL 5000
QKEMDQHFGM VELLNNTANS LLSVCEIDKE VVTDENKSLI QKVDMVTEQL 5050
HSKKFCLENM TQKFKEFQEV SKESKRQLQC AKEQLDIHDS LGSQAYSNKY 5100
LTMLQTQQKS LQALKHQVDL AKRLAQDLVV EASDSKGTSD VLLQVETIAQ 5150
EHSTLSQQVD EKCSFLETKL QGIGHFQNTI REMFSQFAEF DDELDSMAPV 5200
GRDAETLQKQ KETIKAFLKK LEALMASNDN ANKTCKMMLA TEETSPDLVG 5250
IKRDLEALSK QCNKLLDRAQ AREEQVEGTI KRLEEFYSKL KEFSILLQKA 5300
EEHEESQGPV GMETETINQQ LNMFKVFQKE EIEPLQGKQQ DVNWLGQGLI 5350
QSAAKSTSTQ GLEHDLDDVN ARWKTLNKKV AQRAAQLQEA LLHCGRFQDA 5400
LESLLSWMVD TEELVANQKP PSAEFKVVKA QIQEQKLLQR LLDDRKSTVE 5450
VIKREGEKIA TTAEPADKVK ILKQLSLLDS RWEALLNKAE TRNRQLEGIS 5500
VVAQQFHETL EPLNEWLTTI EKRLVNCEPI GTQASKLEEQ IAQHKALEDD 5550
IINHNKHLHQ AVSIGQSLKV LSSREDKDMV QSKLDFSQVW YIEIQEKSHS 5600
RSELLQQALC NAKIFGEDEV ELMNWLNEVH DKLSKLSVQD YSTEGLWKQQ 5650
SELRVLQEDI LLRKQNVDQA LLNGLELLKQ TTGDEVLIIQ DKLEAIKARY 5700
KDITKLSTDV AKTLEQALQL ARRLHSTHEE LCTWLDKVEV ELLSYETQVL 5750
KGEEASQAQM RPKELKKEAK NNKALLDSLN EVSSALLELV PWRAREGLEK 5800
MVAEDNERYR LVSDTITQKV EEIDAAILRS QQFDQAADAE LSWITETEKK 5850
LMSLGDIRLE QDQTSAQLQV QKTFTMEILR HKDIIDDLVK SGHKIMTACS 5900
EEEKQSMKKK LDKVLKNYDT ICQINSERYL QLERAQSLVN QFWETYEELW 5950
PWLTETQSII SQLPAPALEY ETLRQQQEEH RQLRELIAEH KPHIDKMNKT 6000
GPQLLELSPG EGFSIQEKYV AADTLYSQIK EDVKKRAVAL DEAISQSTQF 6050
HDKIDQILES LERIVERLRQ PPSISAEVEK IKEQISENKN VSVDMEKLQP 6100
LYETLKQRGE EMIARSGGTD KDISAKAVQD KLDQMVFIWE NIHTLVEERE 6150
AKLLDVMELA EKFWCDHMSL IVTIKDTQDF IRDLEDPGID PSVVKQQQEA 6200
AETIREEIDG LQEELDIVIN LGSELIAACG EPDKPIVKKS IDELNSAWDS 6250
LNKAWKDRID KLEEAMQAAV QYQDGLQAVF DWVDIAGGKL ASMSPIGTDL 6300
ETVKQQIEEL KQFKSEAYQQ QIEMERLNHQ AELLLKKVTE ESDKHTVQDP 6350
LMELKLIWDS LEERIINRQH KLEGALLALG QFQHALDELL AWLTHTEGLL 6400
SEQKPVGGDP KAIEIELAKH HVLQNDVLAH QSTVEAVNKA GNDLIESSAG 6450
EEASNLQNKL EVLNQRWQNV LEKTEQRKQQ LDGALRQAKG FHGEIEDLQQ 6500
WLTDTERHLL ASKPLGGLPE TAKEQLNVHM EVCAAFEAKE ETYKSLMQKG 6550
QQMLARCPKS AETNIDQDIN NLKEKWESVE TKLNERKTKL EEALNLAMEF 6600
HNSLQDFINW LTQAEQTLNV ASRPSLILDT VLFQIDEHKV FANEVNSHRE 6650
QIIELDKTGT HLKYFSQKQD VVLIKNLLIS VQSRWEKVVQ RLVERGRSLD 6700
DARKRAKQFH EAWSKLMEWL EESEKSLDSE LEIANDPDKI KTQLAQHKEF 6750
QKSLGAKHSV YDTTNRTGRS LKEKTSLADD NLKLDDMLSE LRDKWDTICG 6800
KSVERQNKLE EALLFSGQFT DALQALIDWL YRVEPQLAED QPVHGDIDLV 6850
MNLIDNHKAF QKELGKRTSS VQALKRSARE LIEGSRDDSS WVKVQMQELS 6900
TRWETVCALS ISKQTRLEAA LRQAEEFHSV VHALLEWLAE AEQTLRFHGV 6950
LPDDEDALRT LIDQHKEFMK KLEEKRAELN KATTMGDTVL AICHPDSITT 7000
IKHWITIIRA RFEEVLAWAK QHQQRLASAL AGLIAKQELL EALLAWLQWA 7050
ETTLTDKDKE VIPQEIEEVK ALIAEHQTFM EEMTRKQPDV DKVTKTYKRR 7100
AADPSSLQSH IPVLDKGRAG RKRFPASSLY PSGSQTQIET KNPRVNLLVS 7150
KWQQVWLLAL ERRRKLNDAL DRLEELREFA NFDFDIWRKK YMRWMNHKKS 7200
RVMDFFRRID KDQDGKITRQ EFIDGILSSK FPTSRLEMSA VADIFDRDGD 7250
GYIDYYEFVA ALHPNKDAYK PITDADKIED EVTRQVAKCK CAKRFQVEQI 7300
GDNKYRFFLG NQFGDSQQLR LVRILRSTVM VRVGGGWMAL DEFLVKNDPC 7350
RVHHHGSKML RSESNSSITT TQPTIAKGRT NMELREKFIL ADGASQGMAA 7400
FRPRGRRSRP SSRGASPNRS TSVSSQAAQA ASPQVPATTT PKGTPIQGSK 7450
LRLPGYLSGK GFHSGEDSGL ITTAAARVRT QFADSKKTPS RPGSRAGSKA 7500
GSRASSRRGS DASDFDISEI QSVCSDVETV PQTHRPTPRA GSRPSTAKPS 7550
KIPTPQRKSP ASKLDKSSKR 7570

Note: No experimental confirmation available. Derived from EST data.

Length:7,570
Mass (Da):860,662
Last modified:April 20, 2010 - v4
Checksum:i1EA992E53D1C243E
GO
Isoform 2 (identifier: Q03001-8) [UniParc]FASTAAdd to Basket

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

Show »
Length:5,171
Mass (Da):591,036
Checksum:iEF1B5C94E21ED130
GO
Isoform 3 (identifier: Q03001-3) [UniParc]FASTAAdd to Basket

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 phosphoserine at position 1565 (By similarity).

Show »
Length:2,649
Mass (Da):306,755
Checksum:i5D0C62D26120E069
GO
Isoform 4 (identifier: Q03001-9) [UniParc]FASTAAdd to Basket

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.

Show »
Length:3,060
Mass (Da):345,032
Checksum:i71C7175B93F7E1EC
GO
Isoform 5 (identifier: Q03001-10) [UniParc]FASTAAdd to Basket

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.

Show »
Length:447
Mass (Da):50,373
Checksum:iD462C85D9FA1C903
GO
Isoform 6 (identifier: Q03001-11) [UniParc]FASTAAdd to Basket

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).

Show »
Length:224
Mass (Da):25,379
Checksum:i9AD0D616AC22B94E
GO
Isoform 7 (identifier: Q03001-12) [UniParc]FASTAAdd to Basket

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.

Show »
Length:81
Mass (Da):9,221
Checksum:i8C50813157B4E7D3
GO
Isoform 8 (identifier: Q03001-13) [UniParc]FASTAAdd to Basket

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).

Show »
Length:905
Mass (Da):102,868
Checksum:iAB344F0B597C1961
GO

Sequence cautioni

The sequence AAA35538.1 differs from that shown. Reason: Contaminating sequence. Sequence of unknown origin in the C-terminal part.
Isoform 6 : The sequence AAC50244.1 differs from that shown. Reason: Frameshift at position 51.
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 AAA57185.1 differs from that shown. Reason: Erroneous gene model prediction.
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.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1319 – 13191N → K.
Corresponds to variant rs35014998 [ dbSNP | Ensembl ].
VAR_063045
Natural varianti2332 – 23321Q → R.
Corresponds to variant rs16888053 [ dbSNP | Ensembl ].
VAR_063046
Natural varianti3720 – 37201Q → R.
Corresponds to variant rs4712138 [ dbSNP | Ensembl ].
VAR_063047
Natural varianti5138 – 51381T → A.1 Publication
Corresponds to variant rs4715631 [ dbSNP | Ensembl ].
VAR_063048

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 37533753Missing in isoform 5.
VSP_041524Add
BLAST
Alternative sequencei1 – 381381MAGYL…RPEVE → MHSSSYSYRSSDSVFSNTTS TRTSLDSNENLLLVHCGPTL INSCISFGSESFDGH in isoform 2, isoform 3 and isoform 4.
VSP_041525Add
BLAST
Alternative sequencei1 – 138138MAGYL…ILHFQ → MQHSIFSLKKKRCHSLYTSM SSVSKDTDGNE in isoform 7.
VSP_041526Add
BLAST
Alternative sequencei1 – 138138MAGYL…ILHFQ → MGNVCGCVRAEKEEQYVDPA KTPLNPEKYSPGRKYFRRKP IKKTGGDKESVGANNENEGK KKSSSQPSKEQPAPLSRGLV QQESVTLNSALGDGIQQKKT EVVADSVKQKLLPSAVSSWS DCVNTSPAKDSETEVKVSEL DERISEKDSTPYCAKRKKHL DDVNTSEITFQEKTDVFSFR KAASLSSIPSGIERSLEKGG FPEDPPKSYSSIQEKQNTER FCPHATQHFQFKKKRCHSLY TSMSSVSKDTDGNE in isoform 8.
VSP_041527Add
BLAST
Alternative sequencei1 – 3030MAGYL…LERYK → MIAAAFLVLLRPYSIQCALF LLLLLLGTIATIVFFCCWHR KLQKGRHPMKSVFSGRSRSR DAVLRSHHFRSEGFRASPRH LRRRVAAAAAARLEEVKPVV EVHHQSEQETSVRKRRIKKS SRVQPEFYHSVQGASIRRPS SGNASYRCSMSSSADFSDED DFSQKSGSASPAPGDTLPWN LPKHERSKRKIQGGSVLDPA ERAVLRIA in isoform 6.
VSP_041528Add
BLAST
Alternative sequencei47 – 75707524Missing in isoform 6.
VSP_041529Add
BLAST
Alternative sequencei189 – 75707382Missing in isoform 7.
VSP_041530Add
BLAST
Alternative sequencei778 – 78912AYRAA…TQWSW → VKLESVMVLVEY in isoform 8.
VSP_041531Add
BLAST
Alternative sequencei790 – 75706781Missing in isoform 8.
VSP_041532Add
BLAST
Alternative sequencei1433 – 14331K → 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 sequencei1434 – 75706137Missing in isoform 3.
VSP_041534Add
BLAST
Alternative sequencei1550 – 36352086Missing in isoform 2.
VSP_041535Add
BLAST
Alternative sequencei3387 – 75704184Missing in isoform 4.
VSP_041536Add
BLAST
Alternative sequencei4184 – 420017GQVPL…IISKN → DVGTGYCRSSEQYKCHE in isoform 5.
VSP_041537Add
BLAST
Alternative sequencei4201 – 75703370Missing in isoform 5.
VSP_041538Add
BLAST
Alternative sequencei7352 – 737524Missing in isoform 2.
VSP_041539Add
BLAST
Alternative sequencei7442 – 74421K → KILHPLTRNYGKPWLTNSKM STPCKAAECSDFPVPSAE in isoform 2.
VSP_041540

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti573 – 5731P → A in BAH12207. 1 Publication
Sequence conflicti1177 – 11771V → G in M69225. 1 Publication
Sequence conflicti1177 – 11771V → G in AAL62061. 1 Publication
Sequence conflicti1177 – 11771V → G in AAL62062. 1 Publication
Sequence conflicti1363 – 13631K → E in AAL62061. 1 Publication
Sequence conflicti4703 – 47031R → H in BAC04449. 1 Publication
Sequence conflicti4935 – 49351N → S in BAC04449. 1 Publication
Sequence conflicti5030 – 50301E → G in AAL62061. 1 Publication
Sequence conflicti5177 – 51771Q → R in AAL62061. 1 Publication
Sequence conflicti5225 – 52251M → I in BAB70870. 1 Publication
Sequence conflicti5299 – 52991K → R in AAL62061. 1 Publication
Sequence conflicti5823 – 58231I → V in AAL62061. 1 Publication
Sequence conflicti5882 – 58821K → R in AAL62061. 1 Publication
Sequence conflicti5986 – 59861L → S in AAL62061. 1 Publication
Sequence conflicti6080 – 60801K → E in BAC04848. 1 Publication
Sequence conflicti6186 – 61861D → G in AAL62061. 1 Publication
Sequence conflicti6440 – 64401A → G in AAL62061. 1 Publication
Isoform 6 (identifier: Q03001-11)
Sequence conflicti48 – 481P → L in AAC50244. 1 Publication
Isoform 3 (identifier: Q03001-3)
Sequence conflicti1644 – 16441R → T in M69225. 1 Publication
Sequence conflicti1943 – 19431G → R in CAA41528. 1 Publication
Sequence conflicti2364 – 23641S → T in M69225. 1 Publication
Sequence conflicti2495 – 24951G → V in M69225. 1 Publication
Sequence conflicti2543 – 25431N → K in M69225. 1 Publication
Sequence conflicti2621 – 26211A → P in M69225. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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
, AL096710, AL137008, AL512448, AL590005 Genomic DNA. Translation: CAI14341.1. Sequence problems.
AL590005
, AL096710, AL137008, AL512422, AL512448 Genomic DNA. Translation: CAI14989.1. Sequence problems.
AL512448
, AL096710, AL137008, AL512422, AL590005 Genomic DNA. Translation: CAI16609.1. Sequence problems.
AL512448, AL096710, AL137008 Genomic DNA. Translation: CAI16610.1. Sequence problems.
AL137008
, AL096710, AL512422, AL512448, AL590005 Genomic DNA. Translation: CAI20330.1. Sequence problems.
AL137008, AL096710, AL512448 Genomic DNA. Translation: CAI20332.1. Sequence problems.
AL096710
, 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.
CCDSiCCDS47443.1. [Q03001-8]
CCDS4959.1. [Q03001-3]
PIRiI56317. A40937.
RefSeqiNP_001138241.1. NM_001144769.2.
NP_001138242.1. NM_001144770.1.
NP_001714.1. NM_001723.5. [Q03001-3]
NP_056363.2. NM_015548.4. [Q03001-8]
NP_899236.1. NM_183380.3.
UniGeneiHs.604915.
Hs.669931.
Hs.728928.
Hs.735651.

Genome annotation databases

EnsembliENST00000244364; ENSP00000244364; ENSG00000151914. [Q03001-8]
ENST00000370765; ENSP00000359801; ENSG00000151914. [Q03001-3]
ENST00000439203; ENSP00000404924; ENSG00000151914. [Q03001-9]
GeneIDi667.
KEGGihsa:667.
UCSCiuc003pcy.4. human. [Q03001-8]
uc003pdc.4. human. [Q03001-3]
uc003pde.2. human. [Q03001-13]
uc021zax.1. human. [Q03001-9]
uc021zay.2. human. [Q03001-7]

Polymorphism databases

DMDMi294862529.

Keywords - Coding sequence diversityi

Alternative promoter usage, Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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
, AL096710 , AL137008 , AL512448 , AL590005 Genomic DNA. Translation: CAI14341.1 . Sequence problems.
AL590005
, AL096710 , AL137008 , AL512422 , AL512448 Genomic DNA. Translation: CAI14989.1 . Sequence problems.
AL512448
, AL096710 , AL137008 , AL512422 , AL590005 Genomic DNA. Translation: CAI16609.1 . Sequence problems.
AL512448 , AL096710 , AL137008 Genomic DNA. Translation: CAI16610.1 . Sequence problems.
AL137008
, AL096710 , AL512422 , AL512448 , AL590005 Genomic DNA. Translation: CAI20330.1 . Sequence problems.
AL137008 , AL096710 , AL512448 Genomic DNA. Translation: CAI20332.1 . Sequence problems.
AL096710
, 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.
CCDSi CCDS47443.1. [Q03001-8 ]
CCDS4959.1. [Q03001-3 ]
PIRi I56317. A40937.
RefSeqi NP_001138241.1. NM_001144769.2.
NP_001138242.1. NM_001144770.1.
NP_001714.1. NM_001723.5. [Q03001-3 ]
NP_056363.2. NM_015548.4. [Q03001-8 ]
NP_899236.1. NM_183380.3.
UniGenei Hs.604915.
Hs.669931.
Hs.728928.
Hs.735651.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3GJO X-ray 2.50 E/F/G/H 7541-7570 [» ]
ProteinModelPortali Q03001.
SMRi Q03001. Positions 31-255, 583-795.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107135. 36 interactions.
DIPi DIP-33131N.
IntActi Q03001. 31 interactions.
MINTi MINT-119936.

PTM databases

PhosphoSitei Q03001.

Polymorphism databases

DMDMi 294862529.

Proteomic databases

MaxQBi Q03001.
PaxDbi Q03001.
PRIDEi Q03001.

Protocols and materials databases

DNASUi 667.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000244364 ; ENSP00000244364 ; ENSG00000151914 . [Q03001-8 ]
ENST00000370765 ; ENSP00000359801 ; ENSG00000151914 . [Q03001-3 ]
ENST00000439203 ; ENSP00000404924 ; ENSG00000151914 . [Q03001-9 ]
GeneIDi 667.
KEGGi hsa:667.
UCSCi uc003pcy.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

CTDi 667.
GeneCardsi GC06M056370.
H-InvDB HIX0005976.
HIX0164999.
HGNCi HGNC:1090. DST.
HPAi HPA030200.
MIMi 113810. gene.
614653. phenotype.
615425. phenotype.
neXtProti NX_Q03001.
Orphaneti 89838. Autosomal recessive epidermolysis bullosa simplex.
314381. Hereditary sensory and autonomic neuropathy type 6.
PharmGKBi PA25399.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5069.
HOVERGENi HBG031127.
InParanoidi Q8WXK8.
KOi K10382.
OMAi RKITEIQ.
PhylomeDBi Q03001.
TreeFami TF335163.

Enzyme and pathway databases

Reactomei REACT_150180. Assembly of collagen fibrils and other multimeric structures.
REACT_20537. Type I hemidesmosome assembly.

Miscellaneous databases

ChiTaRSi DST. human.
EvolutionaryTracei Q03001.
GeneWikii Dystonin.
GenomeRNAii 667.
NextBioi 2720.
PROi Q03001.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q03001.
Bgeei Q03001.
CleanExi HS_DST.
Genevestigatori Q03001.

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. 2 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. 19 hits.
[Graphical view ]
SMARTi SM00033. CH. 2 hits.
SM00054. EFh. 2 hits.
SM00243. GAS2. 1 hit.
SM00250. PLEC. 8 hits.
SM00150. SPEC. 32 hits.
[Graphical view ]
SUPFAMi SSF143575. SSF143575. 1 hit.
SSF47576. SSF47576. 1 hit.
SSF75399. SSF75399. 2 hits.
PROSITEi PS00019. ACTININ_1. 1 hit.
PS00020. ACTININ_2. 1 hit.
PS50021. CH. 2 hits.
PS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 2 hits.
PS51460. GAR. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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.
    , 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.
    , 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. 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. 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. 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. 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.

Entry informationi

Entry nameiDYST_HUMAN
AccessioniPrimary (citable) accession number: Q03001
Secondary accession number(s): B7Z3H1
, O94833, Q12825, Q13266, Q13267, Q13775, Q5TBT0, Q5TBT2, Q5TF23, Q5TF24, Q8N1T8, Q8N8J3, Q8WXK8, Q8WXK9, Q96AK9, Q96DQ5, Q96J76, Q96QT5, Q9H555, Q9UGD7, Q9UGD8, Q9UN10
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: April 20, 2010
Last modified: September 3, 2014
This is version 165 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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