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Q03001

- DYST_HUMAN

UniProt

Q03001 - DYST_HUMAN

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Protein

Dystonin

Gene

DST

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.
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.
Isoform 6: required for bundling actin filaments around the nucleus.By similarity
Isoform 7: regulates the organization and stability of the microtubule network of sensory neurons to allow axonal transport.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi7210 – 7221121PROSITE-ProRule annotationAdd
BLAST
Calcium bindingi7246 – 7257122PROSITE-ProRule annotationAdd
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 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 2 Publications
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.By similarity
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
Isoform 2 : Cytoplasmcytoskeleton By similarity
Note: Colocalizes both cortical and cytoplasmic actin filaments.By similarity
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.By similarity
Isoform 6 : Nucleus By similarity. Nucleus envelope 1 Publication. Membrane 1 Publication; Single-pass membrane protein 1 Publication. Endoplasmic reticulum membrane By similarity; Single-pass membrane protein By similarity. Cytoplasmcytoskeleton 1 Publication
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.By similarity
Isoform 7 : Cytoplasmcytoskeleton 1 Publication. Cell projectionaxon 1 Publication. Membrane 1 Publication
Note: Associates with axonal microtubules and intermediate filaments, but not with actin cytoskeleton, in sensory neurons.
Isoform 8 : Cytoplasmcytoskeleton By similarity. Cytoplasmcell cortex By similarity. Cell membrane By similarity; Lipid-anchor By similarity

GO - Cellular componenti

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

Keywords - Cellular componenti

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

Pathology & Biotechi

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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
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.2 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.

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 – 75707570DystoninPRO_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

BgeeiQ03001.
CleanExiHS_DST.
ExpressionAtlasiQ03001. baseline and differential.
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.By similarity6 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. 38 interactions.
DIPiDIP-33131N.
IntActiQ03001. 34 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ03001.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini35 – 252218Actin-bindingAdd
BLAST
Domaini35 – 138104CH 1PROSITE-ProRule annotationAdd
BLAST
Domaini151 – 252102CH 2PROSITE-ProRule annotationAdd
BLAST
Repeati701 – 79797Spectrin 1Add
BLAST
Domaini890 – 94253SH3Add
BLAST
Repeati1584 – 162643Plectin 1Add
BLAST
Repeati1660 – 170344Plectin 2Add
BLAST
Repeati1774 – 181744Plectin 3Add
BLAST
Repeati1818 – 185538Plectin 4Add
BLAST
Repeati1856 – 189136Plectin 5Add
BLAST
Repeati3924 – 400077Spectrin 2Add
BLAST
Repeati4069 – 415385Spectrin 3Add
BLAST
Repeati4514 – 4622109Spectrin 4Add
BLAST
Repeati4626 – 4731106Spectrin 5Add
BLAST
Repeati4849 – 4952104Spectrin 6Add
BLAST
Repeati5281 – 5389109Spectrin 7Add
BLAST
Repeati5396 – 5497102Spectrin 8Add
BLAST
Repeati5504 – 5606103Spectrin 9Add
BLAST
Repeati5829 – 5933105Spectrin 10Add
BLAST
Repeati5940 – 6042103Spectrin 11Add
BLAST
Repeati6048 – 6154107Spectrin 12Add
BLAST
Repeati6184 – 626481Spectrin 13Add
BLAST
Repeati6270 – 6373104Spectrin 14Add
BLAST
Repeati6379 – 6481103Spectrin 15Add
BLAST
Repeati6490 – 6592103Spectrin 16Add
BLAST
Repeati6597 – 6700104Spectrin 17Add
BLAST
Repeati6705 – 6811107Spectrin 18Add
BLAST
Repeati6818 – 6918101Spectrin 19Add
BLAST
Repeati6923 – 7026104Spectrin 20Add
BLAST
Domaini7197 – 723236EF-hand 1PROSITE-ProRule annotationAdd
BLAST
Domaini7233 – 726836EF-hand 2PROSITE-ProRule annotationAdd
BLAST
Domaini7273 – 735179GARPROSITE-ProRule annotationAdd
BLAST

Motif

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

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi2394 – 243138Asp-richAdd
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.
The microtubule tip localization signal (MtLS) motif; mediates interaction with MAPRE1 and targeting to the growing microtubule plus ends.

Sequence similaritiesi

Contains 1 actin-binding domain.Curated
Contains 2 CH (calponin-homology) domains.PROSITE-ProRule annotation
Contains 2 EF-hand domains.PROSITE-ProRule annotation
Contains 1 GAR domain.PROSITE-ProRule annotation
Contains 5 plectin repeats.Curated
Contains 1 SH3 domain.Curated
Contains 20 spectrin repeats.Curated

Keywords - Domaini

Coiled coil, Repeat, SH3 domain, Transmembrane

Phylogenomic databases

eggNOGiCOG5069.
GeneTreeiENSGT00760000119163.
HOVERGENiHBG031127.
InParanoidiQ03001.
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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        10         20         30         40         50
MAGYLSPAAY LYVEEQEYLQ AYEDVLERYK DERDKVQKKT FTKWINQHLM
60 70 80 90 100
KVRKHVNDLY EDLRDGHNLI SLLEVLSGDT LPREKGRMRF HRLQNVQIAL
110 120 130 140 150
DYLKRRQVKL VNIRNDDITD GNPKLTLGLI WTIILHFQIS DIHVTGESED
160 170 180 190 200
MSAKERLLLW TQQATEGYAG IRCENFTTCW RDGKLFNAII HKYRPDLIDM
210 220 230 240 250
NTVAVQSNLA NLEHAFYVAE KIGVIRLLDP EDVDVSSPDE KSVITYVSSL
260 270 280 290 300
YDAFPKVPEG GEGIGANDVE VKWIEYQNMV NYLIQWIRHH VTTMSERTFP
310 320 330 340 350
NNPVELKALY NQYLQFKETE IPPKETEKSK IKRLYKLLEI WIEFGRIKLL
360 370 380 390 400
QGYHPNDIEK EWGKLIIAML EREKALRPEV ERLEMLQQIA NRVQRDSVIC
410 420 430 440 450
EDKLILAGNA LQSDSKRLES GVQFQNEAEI AGYILECENL LRQHVIDVQI
460 470 480 490 500
LIDGKYYQAD QLVQRVAKLR DEIMALRNEC SSVYSKGRIL TTEQTKLMIS
510 520 530 540 550
GITQSLNSGF AQTLHPSLTS GLTQSLTPSL TSSSMTSGLS SGMTSRLTPS
560 570 580 590 600
VTPAYTPGFP SGLVPNFSSG VEPNSLQTLK LMQIRKPLLK SSLLDQNLTE
610 620 630 640 650
EEINMKFVQD LLNWVDEMQV QLDRTEWGSD LPSVESHLEN HKNVHRAIEE
660 670 680 690 700
FESSLKEAKI SEIQMTAPLK LTYAEKLHRL ESQYAKLLNT SRNQERHLDT
710 720 730 740 750
LHNFVSRATN ELIWLNEKEE EEVAYDWSER NTNIARKKDY HAELMRELDQ
760 770 780 790 800
KEENIKSVQE IAEQLLLENH PARLTIEAYR AAMQTQWSWI LQLCQCVEQH
810 820 830 840 850
IKENTAYFEF FNDAKEATDY LRNLKDAIQR KYSCDRSSSI HKLEDLVQES
860 870 880 890 900
MEEKEELLQY KSTIANLMGK AKTIIQLKPR NSDCPLKTSI PIKAICDYRQ
910 920 930 940 950
IEITIYKDDE CVLANNSHRA KWKVISPTGN EAMVPSVCFT VPPPNKEAVD
960 970 980 990 1000
LANRIEQQYQ NVLTLWHESH INMKSVVSWH YLINEIDRIR ASNVASIKTM
1010 1020 1030 1040 1050
LPGEHQQVLS NLQSRFEDFL EDSQESQVFS GSDITQLEKE VNVCKQYYQE
1060 1070 1080 1090 1100
LLKSAEREEQ EESVYNLYIS EVRNIRLRLE NCEDRLIRQI RTPLERDDLH
1110 1120 1130 1140 1150
ESVFRITEQE KLKKELERLK DDLGTITNKC EEFFSQAAAS SSVPTLRSEL
1160 1170 1180 1190 1200
NVVLQNMNQV YSMSSTYIDK LKTVNLVLKN TQAAEALVKL YETKLCEEEA
1210 1220 1230 1240 1250
VIADKNNIEN LISTLKQWRS EVDEKRQVFH ALEDELQKAK AISDEMFKTY
1260 1270 1280 1290 1300
KERDLDFDWH KEKADQLVER WQNVHVQIDN RLRDLEGIGK SLKYYRDTYH
1310 1320 1330 1340 1350
PLDDWIQQVE TTQRKIQENQ PENSKTLATQ LNQQKMLVSE IEMKQSKMDE
1360 1370 1380 1390 1400
CQKYAEQYSA TVKDYELQTM TYRAMVDSQQ KSPVKRRRMQ SSADLIIQEF
1410 1420 1430 1440 1450
MDLRTRYTAL VTLMTQYIKF AGDSLKRLEE EEKSLEEEKK EHVEKAKELQ
1460 1470 1480 1490 1500
KWVSNISKTL KDAEKAGKPP FSKQKISSEE ISTKKEQLSE ALQTIQLFLA
1510 1520 1530 1540 1550
KHGDKMTDEE RNELEKQVKT LQESYNLLFS ESLKQLQESQ TSGDVKVEEK
1560 1570 1580 1590 1600
LDKVIAGTID QTTGEVLSVF QAVLRGLIDY DTGIRLLETQ LMISGLISPE
1610 1620 1630 1640 1650
LRKCFDLKDA KSHGLIDEQI LCQLKELSKA KEIISAASPT TIPVLDALAQ
1660 1670 1680 1690 1700
SMITESMAIK VLEILLSTGS LVIPATGEQL TLQKAFQQNL VSSALFSKVL
1710 1720 1730 1740 1750
ERQNMCKDLI DPCTSEKVSL IDMVQRSTLQ ENTGMWLLPV RPQEGGRITL
1760 1770 1780 1790 1800
KCGRNISILR AAHEGLIDRE TMFRLLSAQL LSGGLINSNS GQRMTVEEAV
1810 1820 1830 1840 1850
REGVIDRDTA SSILTYQVQT GGIIQSNPAK RLTVDEAVQC DLITSSSALL
1860 1870 1880 1890 1900
VLEAQRGYVG LIWPHSGEIF PTSSSLQQEL ITNELAYKIL NGRQKIAALY
1910 1920 1930 1940 1950
IPESSQVIGL DAAKQLGIID NNTASILKNI TLPDKMPDLG DLEACKNARR
1960 1970 1980 1990 2000
WLSFCKFQPS TVHDYRQEED VFDGEEPVTT QTSEETKKLF LSYLMINSYM
2010 2020 2030 2040 2050
DANTGQRLLL YDGDLDEAVG MLLEGCHAEF DGNTAIKECL DVLSSSGVFL
2060 2070 2080 2090 2100
NNASGREKDE CTATPSSFNK CHCGEPEHEE TPENRKCAID EEFNEMRNTV
2110 2120 2130 2140 2150
INSEFSQSGK LASTISIDPK VNSSPSVCVP SLISYLTQTE LADISMLRSD
2160 2170 2180 2190 2200
SENILTNYEN QSRVETNERA NECSHSKNIQ NFPSDLIENP IMKSKMSKFC
2210 2220 2230 2240 2250
GVNETENEDN TNRDSPIFDY SPRLSALLSH DKLMHSQGSF NDTHTPESNG
2260 2270 2280 2290 2300
NKCEAPALSF SDKTMLSGQR IGEKFQDQFL GIAAINISLP GEQYGQKSLN
2310 2320 2330 2340 2350
MISSNPQVQY HNDKYISNTS GEDEKTHPGF QQMPEDKEDE SEIEEYSCAV
2360 2370 2380 2390 2400
TPGGDTDNAI VSLTCATPLL DETISASDYE TSLLNDQQNN TGTDTDSDDD
2410 2420 2430 2440 2450
FYDTPLFEDD DHDSLLLDGD DRDCLHPEDY DTLQEENDET ASPADVFYDV
2460 2470 2480 2490 2500
SKENENSMVP QGAPVGSLSV KNKAHCLQDF LMDVEKDELD SGEKIHLNPV
2510 2520 2530 2540 2550
GSDKVNGQSL ETGSERECTN ILEGDESDSL TDYDIVGGKE SFTASLKFDD
2560 2570 2580 2590 2600
SGSWRGRKEE YVTGQEFHSD TDHLDSMQSE ESYGDYIYDS NDQDDDDDDG
2610 2620 2630 2640 2650
IDEEGGGIRD ENGKPRCQNV AEDMDIQLCA SILNENSDEN ENINTMILLD
2660 2670 2680 2690 2700
KMHSCSSLEK QQRVNVVQLA SPSENNLVTE KSNLPEYTTE IAGKSKENLL
2710 2720 2730 2740 2750
NHEMVLKDVL PPIIKDTESE KTFGPASISH DNNNISSTSE LGTDLANTKV
2760 2770 2780 2790 2800
KLIQGSELPE LTDSVKGKDE YFKNMTPKVD SSLDHIICTE PDLIGKPAEE
2810 2820 2830 2840 2850
SHLSLIASVT DKDPQGNGSD LIKGRDGKSD ILIEDETSIQ KMYLGEGEVL
2860 2870 2880 2890 2900
VEGLVEEENR HLKLLPGKNT RDSFKLINSQ FPFPQITNNE ELNQKGSLKK
2910 2920 2930 2940 2950
ATVTLKDEPN NLQIIVSKSP VQFENLEEIF DTSVSKEISD DITSDITSWE
2960 2970 2980 2990 3000
GNTHFEESFT DGPEKELDLF TYLKHCAKNI KAKDVAKPNE DVPSHVLITA
3010 3020 3030 3040 3050
PPMKEHLQLG VNNTKEKSTS TQKDSPLNDM IQSNDLCSKE SISGGGTEIS
3060 3070 3080 3090 3100
QFTPESIEAT LSILSRKHVE DVGKNDFLQS ERCANGLGND NSSNTLNTDY
3110 3120 3130 3140 3150
SFLEINNKKE RIEQQLPKEQ ALSPRSQEKE VQIPELSQVF VEDVKDILKS
3160 3170 3180 3190 3200
RLKEGHMNPQ EVEEPSACAD TKILIQNLIK RITTSQLVNE ASTVPSDSQM
3210 3220 3230 3240 3250
SDSSGVSPMT NSSELKPESR DDPFCIGNLK SELLLNILKQ DQHSQKITGV
3260 3270 3280 3290 3300
FELMRELTHM EYDLEKRGIT SKVLPLQLEN IFYKLLADGY SEKIEHVGDF
3310 3320 3330 3340 3350
NQKACSTSEM MEEKPHILGD IKSKEGNYYS PNLETVKEIG LESSTVWAST
3360 3370 3380 3390 3400
LPRDEKLKDL CNDFPSHLEC TSGSKEMASG DSSTEQFSSE LQQCLQHTEK
3410 3420 3430 3440 3450
MHEYLTLLQD MKPPLDNQES LDNNLEALKN QLRQLETFEL GLAPIAVILR
3460 3470 3480 3490 3500
KDMKLAEEFL KSLPSDFPRG HVEELSISHQ SLKTAFSSLS NVSSERTKQI
3510 3520 3530 3540 3550
MLAIDSEMSK LAVSHEEFLH KLKSFSDWVS EKSKSVKDIE IVNVQDSEYV
3560 3570 3580 3590 3600
KKRLEFLKNV LKDLGHTKMQ LETTAFDVQF FISEYAQDLS PNQSKQLLRL
3610 3620 3630 3640 3650
LNTTQKCFLD VQESVTTQVE RLETQLHLEQ DLDDQKIVAE RQQEYKEKLQ
3660 3670 3680 3690 3700
GICDLLTQTE NRLIGHQEAF MIGDGTVELK KYQSKQEELQ KDMQGSAQAL
3710 3720 3730 3740 3750
AEVVKNTENF LKENGEKLSQ EDKALIEQKL NEAKIKCEQL NLKAEQSKKE
3760 3770 3780 3790 3800
LDKVVTTAIK EETEKVAAVK QLEESKTKIE NLLDWLSNVD KDSERAGTKH
3810 3820 3830 3840 3850
KQVIEQNGTH FQEGDGKSAI GEEDEVNGNL LETDVDGQVG TTQENLNQQY
3860 3870 3880 3890 3900
QKVKAQHEKI ISQHQAVIIA TQSAQVLLEK QGQYLSPEEK EKLQKNMKEL
3910 3920 3930 3940 3950
KVHYETALAE SEKKMKLTHS LQEELEKFDA DYTEFEHWLQ QSEQELENLE
3960 3970 3980 3990 4000
AGADDINGLM TKLKRQKSFS EDVISHKGDL RYITISGNRV LEAAKSCSKR
4010 4020 4030 4040 4050
DGGKVDTSAT HREVQRKLDH ATDRFRSLYS KCNVLGNNLK DLVDKYQHYE
4060 4070 4080 4090 4100
DASCGLLAGL QACEATASKH LSEPIAVDPK NLQRQLEETK ALQGQISSQQ
4110 4120 4130 4140 4150
VAVEKLKKTA EVLLDARGSL LPAKNDIQKT LDDIVGRYED LSKSVNERNE
4160 4170 4180 4190 4200
KLQITLTRSL SVQDGLDEML DWMGNVESSL KEQGQVPLNS TALQDIISKN
4210 4220 4230 4240 4250
IMLEQDIAGR QSSINAMNEK VKKFMETTDP STASSLQAKM KDLSARFSEA
4260 4270 4280 4290 4300
SHKHKETLAK MEELKTKVEL FENLSEKLQT FLETKTQALT EVDVPGKDVT
4310 4320 4330 4340 4350
ELSQYMQEST SEFLEHKKHL EVLHSLLKEI SSHGLPSDKA LVLEKTNNLS
4360 4370 4380 4390 4400
KKFKEMEDTI KEKKEAVTSC QEQLDAFQVL VKSLKSWIKE TTKKVPIVQP
4410 4420 4430 4440 4450
SFGAEDLGKS LEDTKKLQEK WSLKTPEIQK VNNSGISLCN LISAVTTPAK
4460 4470 4480 4490 4500
AIAAVKSGGA VLNGEGTATN TEEFWANKGL TSIKKDMTDI SHGYEDLGLL
4510 4520 4530 4540 4550
LKDKIAELNT KLSKLQKAQE ESSAMMQWLQ KMNKTATKWQ QTPAPTDTEA
4560 4570 4580 4590 4600
VKTQVEQNKS FEAELKQNVN KVQELKDKLT ELLEENPDTP EAPRWKQMLT
4610 4620 4630 4640 4650
EIDSKWQELN QLTIDRQQKL EESSNNLTQF QTVEAQLKQW LVEKELMVSV
4660 4670 4680 4690 4700
LGPLSIDPNM LNTQRQQVQI LLQEFATRKP QYEQLTAAGQ GILSRPGEDP
4710 4720 4730 4740 4750
SLRGIVKEQL AAVTQKWDSL TGQLSDRCDW IDQAIVKSTQ YQSLLRSLSD
4760 4770 4780 4790 4800
KLSDLDNKLS SSLAVSTHPD AMNQQLETAQ KMKQEIQQEK KQIKVAQALC
4810 4820 4830 4840 4850
EDLSALVKEE YLKAELSRQL EGILKSFKDV EQKAENHVQH LQSACASSHQ
4860 4870 4880 4890 4900
FQQMSRDFQA WLDTKKEEQN KSHPISAKLD VLESLIKDHK DFSKTLTAQS
4910 4920 4930 4940 4950
HMYEKTIAEG ENLLLKTQGS EKAALQLQLN TIKTNWDTFN KQVKERENKL
4960 4970 4980 4990 5000
KESLEKALKY KEQVETLWPW IDKCQNNLEE IKFCLDPAEG ENSIAKLKSL
5010 5020 5030 5040 5050
QKEMDQHFGM VELLNNTANS LLSVCEIDKE VVTDENKSLI QKVDMVTEQL
5060 5070 5080 5090 5100
HSKKFCLENM TQKFKEFQEV SKESKRQLQC AKEQLDIHDS LGSQAYSNKY
5110 5120 5130 5140 5150
LTMLQTQQKS LQALKHQVDL AKRLAQDLVV EASDSKGTSD VLLQVETIAQ
5160 5170 5180 5190 5200
EHSTLSQQVD EKCSFLETKL QGIGHFQNTI REMFSQFAEF DDELDSMAPV
5210 5220 5230 5240 5250
GRDAETLQKQ KETIKAFLKK LEALMASNDN ANKTCKMMLA TEETSPDLVG
5260 5270 5280 5290 5300
IKRDLEALSK QCNKLLDRAQ AREEQVEGTI KRLEEFYSKL KEFSILLQKA
5310 5320 5330 5340 5350
EEHEESQGPV GMETETINQQ LNMFKVFQKE EIEPLQGKQQ DVNWLGQGLI
5360 5370 5380 5390 5400
QSAAKSTSTQ GLEHDLDDVN ARWKTLNKKV AQRAAQLQEA LLHCGRFQDA
5410 5420 5430 5440 5450
LESLLSWMVD TEELVANQKP PSAEFKVVKA QIQEQKLLQR LLDDRKSTVE
5460 5470 5480 5490 5500
VIKREGEKIA TTAEPADKVK ILKQLSLLDS RWEALLNKAE TRNRQLEGIS
5510 5520 5530 5540 5550
VVAQQFHETL EPLNEWLTTI EKRLVNCEPI GTQASKLEEQ IAQHKALEDD
5560 5570 5580 5590 5600
IINHNKHLHQ AVSIGQSLKV LSSREDKDMV QSKLDFSQVW YIEIQEKSHS
5610 5620 5630 5640 5650
RSELLQQALC NAKIFGEDEV ELMNWLNEVH DKLSKLSVQD YSTEGLWKQQ
5660 5670 5680 5690 5700
SELRVLQEDI LLRKQNVDQA LLNGLELLKQ TTGDEVLIIQ DKLEAIKARY
5710 5720 5730 5740 5750
KDITKLSTDV AKTLEQALQL ARRLHSTHEE LCTWLDKVEV ELLSYETQVL
5760 5770 5780 5790 5800
KGEEASQAQM RPKELKKEAK NNKALLDSLN EVSSALLELV PWRAREGLEK
5810 5820 5830 5840 5850
MVAEDNERYR LVSDTITQKV EEIDAAILRS QQFDQAADAE LSWITETEKK
5860 5870 5880 5890 5900
LMSLGDIRLE QDQTSAQLQV QKTFTMEILR HKDIIDDLVK SGHKIMTACS
5910 5920 5930 5940 5950
EEEKQSMKKK LDKVLKNYDT ICQINSERYL QLERAQSLVN QFWETYEELW
5960 5970 5980 5990 6000
PWLTETQSII SQLPAPALEY ETLRQQQEEH RQLRELIAEH KPHIDKMNKT
6010 6020 6030 6040 6050
GPQLLELSPG EGFSIQEKYV AADTLYSQIK EDVKKRAVAL DEAISQSTQF
6060 6070 6080 6090 6100
HDKIDQILES LERIVERLRQ PPSISAEVEK IKEQISENKN VSVDMEKLQP
6110 6120 6130 6140 6150
LYETLKQRGE EMIARSGGTD KDISAKAVQD KLDQMVFIWE NIHTLVEERE
6160 6170 6180 6190 6200
AKLLDVMELA EKFWCDHMSL IVTIKDTQDF IRDLEDPGID PSVVKQQQEA
6210 6220 6230 6240 6250
AETIREEIDG LQEELDIVIN LGSELIAACG EPDKPIVKKS IDELNSAWDS
6260 6270 6280 6290 6300
LNKAWKDRID KLEEAMQAAV QYQDGLQAVF DWVDIAGGKL ASMSPIGTDL
6310 6320 6330 6340 6350
ETVKQQIEEL KQFKSEAYQQ QIEMERLNHQ AELLLKKVTE ESDKHTVQDP
6360 6370 6380 6390 6400
LMELKLIWDS LEERIINRQH KLEGALLALG QFQHALDELL AWLTHTEGLL
6410 6420 6430 6440 6450
SEQKPVGGDP KAIEIELAKH HVLQNDVLAH QSTVEAVNKA GNDLIESSAG
6460 6470 6480 6490 6500
EEASNLQNKL EVLNQRWQNV LEKTEQRKQQ LDGALRQAKG FHGEIEDLQQ
6510 6520 6530 6540 6550
WLTDTERHLL ASKPLGGLPE TAKEQLNVHM EVCAAFEAKE ETYKSLMQKG
6560 6570 6580 6590 6600
QQMLARCPKS AETNIDQDIN NLKEKWESVE TKLNERKTKL EEALNLAMEF
6610 6620 6630 6640 6650
HNSLQDFINW LTQAEQTLNV ASRPSLILDT VLFQIDEHKV FANEVNSHRE
6660 6670 6680 6690 6700
QIIELDKTGT HLKYFSQKQD VVLIKNLLIS VQSRWEKVVQ RLVERGRSLD
6710 6720 6730 6740 6750
DARKRAKQFH EAWSKLMEWL EESEKSLDSE LEIANDPDKI KTQLAQHKEF
6760 6770 6780 6790 6800
QKSLGAKHSV YDTTNRTGRS LKEKTSLADD NLKLDDMLSE LRDKWDTICG
6810 6820 6830 6840 6850
KSVERQNKLE EALLFSGQFT DALQALIDWL YRVEPQLAED QPVHGDIDLV
6860 6870 6880 6890 6900
MNLIDNHKAF QKELGKRTSS VQALKRSARE LIEGSRDDSS WVKVQMQELS
6910 6920 6930 6940 6950
TRWETVCALS ISKQTRLEAA LRQAEEFHSV VHALLEWLAE AEQTLRFHGV
6960 6970 6980 6990 7000
LPDDEDALRT LIDQHKEFMK KLEEKRAELN KATTMGDTVL AICHPDSITT
7010 7020 7030 7040 7050
IKHWITIIRA RFEEVLAWAK QHQQRLASAL AGLIAKQELL EALLAWLQWA
7060 7070 7080 7090 7100
ETTLTDKDKE VIPQEIEEVK ALIAEHQTFM EEMTRKQPDV DKVTKTYKRR
7110 7120 7130 7140 7150
AADPSSLQSH IPVLDKGRAG RKRFPASSLY PSGSQTQIET KNPRVNLLVS
7160 7170 7180 7190 7200
KWQQVWLLAL ERRRKLNDAL DRLEELREFA NFDFDIWRKK YMRWMNHKKS
7210 7220 7230 7240 7250
RVMDFFRRID KDQDGKITRQ EFIDGILSSK FPTSRLEMSA VADIFDRDGD
7260 7270 7280 7290 7300
GYIDYYEFVA ALHPNKDAYK PITDADKIED EVTRQVAKCK CAKRFQVEQI
7310 7320 7330 7340 7350
GDNKYRFFLG NQFGDSQQLR LVRILRSTVM VRVGGGWMAL DEFLVKNDPC
7360 7370 7380 7390 7400
RVHHHGSKML RSESNSSITT TQPTIAKGRT NMELREKFIL ADGASQGMAA
7410 7420 7430 7440 7450
FRPRGRRSRP SSRGASPNRS TSVSSQAAQA ASPQVPATTT PKGTPIQGSK
7460 7470 7480 7490 7500
LRLPGYLSGK GFHSGEDSGL ITTAAARVRT QFADSKKTPS RPGSRAGSKA
7510 7520 7530 7540 7550
GSRASSRRGS DASDFDISEI QSVCSDVETV PQTHRPTPRA GSRPSTAKPS
7560 7570
KIPTPQRKSP ASKLDKSSKR

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 similarityCurated

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).Curated

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. 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.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti573 – 5731P → A in BAH12207. (PubMed:14702039)Curated
Sequence conflicti1177 – 11771V → G in M69225. (PubMed:1717441)Curated
Sequence conflicti1177 – 11771V → G in AAL62061. (PubMed:11751855)Curated
Sequence conflicti1177 – 11771V → G in AAL62062. (PubMed:11751855)Curated
Sequence conflicti1363 – 13631K → E in AAL62061. (PubMed:11751855)Curated
Sequence conflicti4703 – 47031R → H in BAC04449. (PubMed:14702039)Curated
Sequence conflicti4935 – 49351N → S in BAC04449. (PubMed:14702039)Curated
Sequence conflicti5030 – 50301E → G in AAL62061. (PubMed:11751855)Curated
Sequence conflicti5177 – 51771Q → R in AAL62061. (PubMed:11751855)Curated
Sequence conflicti5225 – 52251M → I in BAB70870. (PubMed:14702039)Curated
Sequence conflicti5299 – 52991K → R in AAL62061. (PubMed:11751855)Curated
Sequence conflicti5823 – 58231I → V in AAL62061. (PubMed:11751855)Curated
Sequence conflicti5882 – 58821K → R in AAL62061. (PubMed:11751855)Curated
Sequence conflicti5986 – 59861L → S in AAL62061. (PubMed:11751855)Curated
Sequence conflicti6080 – 60801K → E in BAC04848. (PubMed:14702039)Curated
Sequence conflicti6186 – 61861D → G in AAL62061. (PubMed:11751855)Curated
Sequence conflicti6440 – 64401A → G in AAL62061. (PubMed:11751855)Curated
Isoform 6 (identifier: Q03001-11)
Sequence conflicti48 – 481P → L in AAC50244. (PubMed:8575775)Curated
Isoform 3 (identifier: Q03001-3)
Sequence conflicti1644 – 16441R → T in M69225. (PubMed:1717441)By similarityCurated
Sequence conflicti1943 – 19431G → R in CAA41528. (PubMed:2461961)By similarityCurated
Sequence conflicti2364 – 23641S → T in M69225. (PubMed:1717441)By similarityCurated
Sequence conflicti2495 – 24951G → V in M69225. (PubMed:1717441)By similarityCurated
Sequence conflicti2543 – 25431N → K in M69225. (PubMed:1717441)By similarityCurated
Sequence conflicti2621 – 26211A → P in M69225. (PubMed:1717441)By similarityCurated

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. 1 PublicationVSP_041524Add
BLAST
Alternative sequencei1 – 381381MAGYL…RPEVE → MHSSSYSYRSSDSVFSNTTS TRTSLDSNENLLLVHCGPTL INSCISFGSESFDGH in isoform 2, isoform 3 and isoform 4. 5 PublicationsVSP_041525Add
BLAST
Alternative sequencei1 – 138138MAGYL…ILHFQ → MQHSIFSLKKKRCHSLYTSM SSVSKDTDGNE in isoform 7. 1 PublicationVSP_041526Add
BLAST
Alternative sequencei1 – 138138MAGYL…ILHFQ → MGNVCGCVRAEKEEQYVDPA KTPLNPEKYSPGRKYFRRKP IKKTGGDKESVGANNENEGK KKSSSQPSKEQPAPLSRGLV QQESVTLNSALGDGIQQKKT EVVADSVKQKLLPSAVSSWS DCVNTSPAKDSETEVKVSEL DERISEKDSTPYCAKRKKHL DDVNTSEITFQEKTDVFSFR KAASLSSIPSGIERSLEKGG FPEDPPKSYSSIQEKQNTER FCPHATQHFQFKKKRCHSLY TSMSSVSKDTDGNE in isoform 8. 1 PublicationVSP_041527Add
BLAST
Alternative sequencei1 – 3030MAGYL…LERYK → MIAAAFLVLLRPYSIQCALF LLLLLLGTIATIVFFCCWHR KLQKGRHPMKSVFSGRSRSR DAVLRSHHFRSEGFRASPRH LRRRVAAAAAARLEEVKPVV EVHHQSEQETSVRKRRIKKS SRVQPEFYHSVQGASIRRPS SGNASYRCSMSSSADFSDED DFSQKSGSASPAPGDTLPWN LPKHERSKRKIQGGSVLDPA ERAVLRIA in isoform 6. 1 PublicationVSP_041528Add
BLAST
Alternative sequencei47 – 75707524Missing in isoform 6. 1 PublicationVSP_041529Add
BLAST
Alternative sequencei189 – 75707382Missing in isoform 7. 1 PublicationVSP_041530Add
BLAST
Alternative sequencei778 – 78912AYRAA…TQWSW → VKLESVMVLVEY in isoform 8. 1 PublicationVSP_041531Add
BLAST
Alternative sequencei790 – 75706781Missing in isoform 8. 1 PublicationVSP_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. 3 PublicationsVSP_041533
Alternative sequencei1434 – 75706137Missing in isoform 3. 3 PublicationsVSP_041534Add
BLAST
Alternative sequencei1550 – 36352086Missing in isoform 2. 2 PublicationsVSP_041535Add
BLAST
Alternative sequencei3387 – 75704184Missing in isoform 4. 1 PublicationVSP_041536Add
BLAST
Alternative sequencei4184 – 420017GQVPL…IISKN → DVGTGYCRSSEQYKCHE in isoform 5. 1 PublicationVSP_041537Add
BLAST
Alternative sequencei4201 – 75703370Missing in isoform 5. 1 PublicationVSP_041538Add
BLAST
Alternative sequencei7352 – 737524Missing in isoform 2. 2 PublicationsVSP_041539Add
BLAST
Alternative sequencei7442 – 74421K → KILHPLTRNYGKPWLTNSKM STPCKAAECSDFPVPSAE in isoform 2. 2 PublicationsVSP_041540

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. 38 interactions.
DIPi DIP-33131N.
IntActi Q03001. 34 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 GC06M056322.
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.
GeneTreei ENSGT00760000119163.
HOVERGENi HBG031127.
InParanoidi Q03001.
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

Bgeei Q03001.
CleanExi HS_DST.
ExpressionAtlasi Q03001. baseline and differential.
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: October 29, 2014
This is version 167 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