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Dystonin (230 kDa bullous pemphigoid antigen) (230/240 kDa bullous pemphigoid antigen) (Bullous pemphigoid antigen 1) (BPA) (Bullous pemphigoid antigen) (Dystonia musculorum protein) (Hemidesmosomal plaque protein)

 DYST_HUMAN              Reviewed;        7570 AA.
Q03001; B7Z3H1; E7ERU0; O94833; Q12825; Q13266; Q13267; Q13775;
Q5TBT0; Q5TBT2; Q5TF23; Q5TF24; Q8N1T8; Q8N8J3; Q8WXK8; Q8WXK9;
Q96AK9; Q96DQ5; Q96J76; Q96QT5; Q9H555; Q9UGD7; Q9UGD8; Q9UN10;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
20-APR-2010, sequence version 4.
22-NOV-2017, entry version 199.
RecName: Full=Dystonin;
AltName: Full=230 kDa bullous pemphigoid antigen;
AltName: Full=230/240 kDa bullous pemphigoid antigen;
AltName: Full=Bullous pemphigoid antigen 1;
Short=BPA;
Short=Bullous pemphigoid antigen;
AltName: Full=Dystonia musculorum protein;
AltName: Full=Hemidesmosomal plaque protein;
Name=DST; Synonyms=BP230, BP240, BPAG1, DMH, DT, KIAA0728;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND DISEASE.
TISSUE=Keratinocyte;
PubMed=1717441;
Sawamura D., Li K., Chu M.-L., Uitto J.;
"Human bullous pemphigoid antigen (BPAG1). Amino acid sequences
deduced from cloned cDNAs predict biologically important peptide
segments and protein domains.";
J. Biol. Chem. 266:17784-17790(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
TISSUE=Keratinocyte;
PubMed=8345227; DOI=10.1111/1523-1747.ep12365083;
Elgart G.W., Stanley J.R.;
"Cloning of the 5' mRNA for the 230-kD bullous pemphigoid antigen by
rapid amplification of cDNA ends.";
J. Invest. Dermatol. 101:244-246(1993).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [MRNA] OF
1-3386 (ISOFORM 4), SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
TISSUE=Keratinocyte;
PubMed=11751855; DOI=10.1074/jbc.M109209200;
Okumura M., Yamakawa H., Ohara O., Owaribe K.;
"Novel alternative splicings of BPAG1 (bullous pemphigoid antigen 1)
including the domain structure closely related to MACF (microtubule
actin cross-linking factor).";
J. Biol. Chem. 277:6682-6687(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 8), NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 4114-6568 (ISOFORM 1), AND VARIANT
ALA-5138.
TISSUE=Brain, Hippocampus, Placenta, and Tongue;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
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.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-461 (ISOFORM 1), AND NUCLEOTIDE
SEQUENCE [MRNA] OF 1-46 (ISOFORM 6).
TISSUE=Fetal brain, and Retina;
PubMed=8575775; DOI=10.1006/geno.1995.9936;
Brown A., Dalpe G., Mathieu M., Kothary R.;
"Cloning and characterization of the neural isoforms of human
dystonin.";
Genomics 29:777-780(1995).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-188 (ISOFORM 7), ALTERNATIVE SPLICING
(ISOFORMS 6 AND 7), FUNCTION OF ISOFORMS 6 AND 7, AND SUBCELLULAR
LOCATION (ISOFORMS 6 AND 7).
TISSUE=Fetal brain;
PubMed=10428034; DOI=10.1016/S0092-8674(00)81017-X;
Yang Y., Bauer C., Strasser G., Wollman R., Julien J.P., Fuchs E.;
"Integrators of the cytoskeleton that stabilize microtubules.";
Cell 98:229-238(1999).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 208-308 (ISOFORM 1).
TISSUE=Pineal gland;
Geerts D., Sonnenberg A.;
Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 881-7570 (ISOFORM 3).
TISSUE=Keratinocyte;
PubMed=1712022;
Tanaka T., Parry D.A.D., Klaus-Kovtun V., Steinert P.M., Stanley J.R.;
"Comparison of molecularly cloned bullous pemphigoid antigen to
desmoplakin I confirms that they define a new family of cell adhesion
junction plaque proteins.";
J. Biol. Chem. 266:12555-12559(1991).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3754-7570 (ISOFORM 5).
TISSUE=Duodenum;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5947-7570 (ISOFORM 2).
TISSUE=Brain;
PubMed=9872452; DOI=10.1093/dnares/5.5.277;
Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A.,
Kotani H., Nomura N., Ohara O.;
"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.";
DNA Res. 5:277-286(1998).
[12]
SEQUENCE REVISION.
PubMed=12168954; DOI=10.1093/dnares/9.3.99;
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
"Construction of expression-ready cDNA clones for KIAA genes: manual
curation of 330 KIAA cDNA clones.";
DNA Res. 9:99-106(2002).
[13]
PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
TISSUE=Keratinocyte;
PubMed=2461961; DOI=10.1172/JCI113803;
Stanley J.R., Tanaka T., Mueller S., Klaus-Kovtun V., Roop D.;
"Isolation of complementary DNA for bullous pemphigoid antigen by use
of patients' autoantibodies.";
J. Clin. Invest. 82:1864-1870(1988).
[14]
PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
PubMed=2090522; DOI=10.1111/j.1432-0436.1990.tb00475.x;
Owaribe K., Kartenbeck J., Stumpp S., Magin T.M., Krieg T., Diaz L.A.,
Franke W.W.;
"The hemidesmosomal plaque. I. Characterization of a major constituent
protein as a differentiation marker for certain forms of epithelia.";
Differentiation 45:207-220(1990).
[15]
PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING
(ISOFORM 3).
PubMed=8010969; DOI=10.1042/bj3000851;
Hopkinson S.B., Jones J.C.;
"Identification of a second protein product of the gene encoding a
human epidermal autoantigen.";
Biochem. J. 300:851-857(1994).
[16]
ALTERNATIVE SPLICING (ISOFORMS 3 AND 6), AND TISSUE SPECIFICITY.
PubMed=8752219; DOI=10.1016/S0092-8674(00)80138-5;
Yang Y., Dowling J., Yu Q.C., Kouklis P., Cleveland D.W., Fuchs E.;
"An essential cytoskeletal linker protein connecting actin
microfilaments to intermediate filaments.";
Cell 86:655-665(1996).
[17]
ALTERNATIVE SPLICING (ISOFORM 3), AND INTERACTION WITH COL17A1 AND
ITGB4.
PubMed=10637308; DOI=10.1091/mbc.11.1.277;
Hopkinson S.B., Jones J.C.;
"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.";
Mol. Biol. Cell 11:277-286(2000).
[18]
DOMAINS.
PubMed=8621649; DOI=10.1074/jbc.271.16.9716;
Tang H.-Y., Chaffotte A.-F., Thacher S.M.;
"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.";
J. Biol. Chem. 271:9716-9722(1996).
[19]
INTERACTION WITH ITGB4 AND ERBIN.
PubMed=11375975; DOI=10.1074/jbc.M011005200;
Favre B., Fontao L., Koster J., Shafaatian R., Jaunin F.,
Saurat J.-H., Sonnenberg A., Borradori L.;
"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.";
J. Biol. Chem. 276:32427-32436(2001).
[20]
ALTERNATIVE SPLICING (ISOFORM 9).
PubMed=14581450; DOI=10.1083/jcb.200306075;
Liu J.J., Ding J., Kowal A.S., Nardine T., Allen E., Delcroix J.D.,
Wu C., Mobley W., Fuchs E., Yang Y.;
"BPAG1n4 is essential for retrograde axonal transport in sensory
neurons.";
J. Cell Biol. 163:223-229(2003).
[21]
ALTERNATIVE SPLICING (ISOFORM 3), FUNCTION OF ISOFORM 3, INTERACTION
WITH COL17A1 AND ITGB4, AND SUBCELLULAR LOCATION (ISOFORM 3).
PubMed=12482924; DOI=10.1242/jcs.00241;
Koster J., Geerts D., Favre B., Borradori L., Sonnenberg A.;
"Analysis of the interactions between BP180, BP230, plectin and the
integrin alpha6beta4 important for hemidesmosome assembly.";
J. Cell Sci. 116:387-399(2003).
[22]
ALTERNATIVE SPLICING (ISOFORM 3), ASSOCIATION WITH KERATIN FILAMENTS,
AND SUBCELLULAR LOCATION (ISOFORM 3).
PubMed=12802069; DOI=10.1091/mbc.E02-08-0548;
Fontao L., Favre B., Riou S., Geerts D., Jaunin F., Saurat J.H.,
Green K.J., Sonnenberg A., Borradori L.;
"Interaction of the bullous pemphigoid antigen 1 (BP230) and
desmoplakin with intermediate filaments is mediated by distinct
sequences within their COOH terminus.";
Mol. Biol. Cell 14:1978-1992(2003).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7432, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[24]
ALTERNATIVE SPLICING (ISOFORM 3), FUNCTION OF ISOFORM 3, AND
SUBCELLULAR LOCATION (ISOFORM 3).
PubMed=19403692; DOI=10.1091/mbc.E09-01-0051;
Hamill K.J., Hopkinson S.B., DeBiase P., Jones J.C.;
"BPAG1e maintains keratinocyte polarity through beta4 integrin-
mediated modulation of Rac1 and cofilin activities.";
Mol. Biol. Cell 20:2954-2962(2009).
[25]
ALTERNATIVE SPLICING (ISOFORM 1), HOMODIMERIZATION, INTERACTION WITH
ACTN2 AND PLEC, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=19932097; DOI=10.1016/j.yexcr.2009.11.010;
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.;
"BPAG1 isoform-b: complex distribution pattern in striated and heart
muscle and association with plectin and alpha-actinin.";
Exp. Cell Res. 316:297-313(2010).
[26]
INVOLVEMENT IN EBSB2.
PubMed=20164846; DOI=10.1038/jid.2010.19;
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.;
"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.";
J. Invest. Dermatol. 130:1551-1557(2010).
[27]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2919, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[29]
INVOLVEMENT IN HSAN6.
PubMed=22522446; DOI=10.1002/ana.23524;
Edvardson S., Cinnamon Y., Jalas C., Shaag A., Maayan C.,
Axelrod F.B., Elpeleg O.;
"Hereditary sensory autonomic neuropathy caused by a mutation in
dystonin.";
Ann. Neurol. 71:569-572(2012).
[30]
INVOLVEMENT IN EBSB2.
PubMed=22113475; DOI=10.1038/jid.2011.379;
Liu L., Dopping-Hepenstal P.J., Lovell P.A., Michael M., Horn H.,
Fong K., Lai-Cheong J.E., Mellerio J.E., Parsons M., McGrath J.A.;
"Autosomal recessive epidermolysis bullosa simplex due to loss of
BPAG1-e expression.";
J. Invest. Dermatol. 132:742-744(2012).
[31]
INTERACTION WITH TMIGD2.
PubMed=22419821; DOI=10.1091/mbc.E11-11-0934;
Rahimi N., Rezazadeh K., Mahoney J.E., Hartsough E., Meyer R.D.;
"Identification of IGPR-1 as a novel adhesion molecule involved in
angiogenesis.";
Mol. Biol. Cell 23:1646-1656(2012).
[32]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3968, PHOSPHORYLATION
[LARGE SCALE ANALYSIS] AT SER-135 (ISOFORM 6), AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[33]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3968, PHOSPHORYLATION
[LARGE SCALE ANALYSIS] AT SER-184 (ISOFORM 8), AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[34]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 7541-7570 IN COMPLEX WITH
MAPRE1, DOMAIN MICROTUBULE TIP LOCALIZATION SIGNAL, AND MUTAGENESIS OF
LYS-7548; SER-7550; ILE-7552; PRO-7553 AND 7557-ARG-LYS-7558.
PubMed=19632184; DOI=10.1016/j.cell.2009.04.065;
Honnappa S., Gouveia S.M., Weisbrich A., Damberger F.F., Bhavesh N.S.,
Jawhari H., Grigoriev I., van Rijssel F.J., Buey R.M., Lawera A.,
Jelesarov I., Winkler F.K., Wuthrich K., Akhmanova A., Steinmetz M.O.;
"An EB1-binding motif acts as a microtubule tip localization signal.";
Cell 138:366-376(2009).
-!- FUNCTION: Cytoskeletal linker protein. Acts as an integrator of
intermediate filaments, actin and microtubule cytoskeleton
networks. Required for anchoring either intermediate filaments to
the actin cytoskeleton in neural and muscle cells or keratin-
containing intermediate filaments to hemidesmosomes in epithelial
cells. The proteins may self-aggregate to form filaments or a two-
dimensional mesh. Regulates the organization and stability of the
microtubule network of sensory neurons to allow axonal transport.
Mediates docking of the dynein/dynactin motor complex to vesicle
cargos for retrograde axonal transport through its interaction
with TMEM108 and DCTN1 (By similarity).
{ECO:0000250|UniProtKB:Q91ZU6}.
-!- FUNCTION: 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.
-!- FUNCTION: Isoform 6: required for bundling actin filaments around
the nucleus. {ECO:0000250, ECO:0000269|PubMed:10428034,
ECO:0000269|PubMed:12482924, ECO:0000269|PubMed:19403692}.
-!- FUNCTION: Isoform 7: regulates the organization and stability of
the microtubule network of sensory neurons to allow axonal
transport.
-!- SUBUNIT: 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 ERBIN (via C-terminus). Isoform 3 associates (via
C-terminal) with KRT5-KRT14 (via rod region) intermediate
filaments of keratins. Interacts with MAPRE1; probably required
for targeting to the growing microtubule plus ends. Interacts with
TMIGD2. Isoform 9 interacts with TMEM108 (By similarity).
{ECO:0000250|UniProtKB:Q91ZU6, ECO:0000269|PubMed:10637308,
ECO:0000269|PubMed:11375975, ECO:0000269|PubMed:12482924,
ECO:0000269|PubMed:19632184, ECO:0000269|PubMed:19932097,
ECO:0000269|PubMed:22419821}.
-!- INTERACTION:
P29991:- (xeno); NbExp=4; IntAct=EBI-310758, EBI-8826488;
Q9UKG1:APPL1; NbExp=3; IntAct=EBI-310758, EBI-741243;
Q9NRI5:DISC1; NbExp=5; IntAct=EBI-310758, EBI-529989;
Q15691:MAPRE1; NbExp=3; IntAct=EBI-310758, EBI-1004115;
Q61166:Mapre1 (xeno); NbExp=4; IntAct=EBI-310758, EBI-2027055;
Q96CV9:OPTN; NbExp=2; IntAct=EBI-310758, EBI-748974;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
{ECO:0000269|PubMed:11751855, ECO:0000269|PubMed:19932097}. Cell
projection, axon {ECO:0000250|UniProtKB:Q91ZU6}. Note=Associates
with intermediate filaments, actin 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. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Isoform 1: Cytoplasm, cytoskeleton
{ECO:0000250}. Cytoplasm, myofibril, sarcomere, Z line. Cytoplasm,
myofibril, sarcomere, H zone {ECO:0000250}. Note=Localizes to
microtubules and actin microfilaments throughout the cytoplasm and
at focal contact attachments at the plasma membrane.
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm, cytoskeleton
{ECO:0000250}. Note=Colocalizes both cortical and cytoplasmic
actin filaments. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Isoform 3: Cytoplasm, cytoskeleton. Cell
junction, hemidesmosome. 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. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Isoform 6: Nucleus {ECO:0000250}. Nucleus
envelope {ECO:0000269|PubMed:10428034}. Membrane
{ECO:0000269|PubMed:10428034}; Single-pass membrane protein
{ECO:0000269|PubMed:10428034}. Endoplasmic reticulum membrane
{ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10428034}.
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. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Isoform 7: Cytoplasm, cytoskeleton
{ECO:0000269|PubMed:10428034}. Cell projection, axon
{ECO:0000269|PubMed:10428034}. Membrane
{ECO:0000269|PubMed:10428034}. Note=Associates with axonal
microtubules and intermediate filaments, but not with actin
cytoskeleton, in sensory neurons.
-!- SUBCELLULAR LOCATION: Isoform 8: Cytoplasm, cytoskeleton
{ECO:0000250}. Cytoplasm, cell cortex {ECO:0000250}. Cell membrane
{ECO:0000250}; Lipid-anchor {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative promoter usage, Alternative splicing; Named isoforms=9;
Name=1; Synonyms=BPAG1-b;
IsoId=Q03001-7; Sequence=Displayed;
Note=No experimental confirmation available. Derived from EST
data.;
Name=2; Synonyms=BPAG1eA, Dystonin-1, eA;
IsoId=Q03001-8; Sequence=VSP_041525, VSP_041535, VSP_041539,
VSP_041540;
Name=3; Synonyms=BPAG1e, eBPAG1;
IsoId=Q03001-3; Sequence=VSP_041525, VSP_041533, VSP_041534;
Note=Ref.1 (M69225) sequence is in conflict in position:
1644:R->T. Ref.1 (M69225) sequence is in conflict in position:
2364:S->T. Ref.1 (M69225) sequence is in conflict in position:
2495:G->V. Ref.1 (M69225) sequence is in conflict in position:
2543:N->K. Ref.1 (M69225) sequence is in conflict in position:
2621:A->P. Ref.13 (CAA41528) sequence is in conflict in
position: 1943:G->R. Contains a phosphoserine at position 1565.
{ECO:0000250, ECO:0000305};
Name=4; Synonyms=BPAG1eA, eB;
IsoId=Q03001-9; Sequence=VSP_041525, VSP_041536;
Note=Incomplete sequence.;
Name=5;
IsoId=Q03001-10; Sequence=VSP_041524, VSP_041537, VSP_041538;
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.;
Name=6; Synonyms=BPAG1n1, BPAG1n2, Dystonin-2;
IsoId=Q03001-11; Sequence=VSP_041528, VSP_041529;
Note=Incomplete sequence. Transmembrane protein (helical
transmembrane domain from amino acid 18 to 38). Ref.6 (AAC50244)
sequence differs from that shown due to a frameshift in position
51. Ref.6 (AAC50244) sequence is in conflict in position:
48:P->L. Contains a phosphoserine at position 135.
{ECO:0000244|PubMed:23186163, ECO:0000305};
Name=7; Synonyms=BPAG1n3;
IsoId=Q03001-12; Sequence=VSP_041526, VSP_041530;
Note=Incomplete sequence.;
Name=8;
IsoId=Q03001-13; Sequence=VSP_041527, VSP_041531, VSP_041532;
Note=Probably myristoylated on Gly-2. Probably S-palmitoylated
on Cys-5 and Cys-7. Contains a phosphoserine at position 184.
{ECO:0000244|PubMed:24275569, ECO:0000250};
Name=9; Synonyms=BPAG1-a {ECO:0000303|PubMed:14581450}, BAPG1n4
{ECO:0000303|PubMed:14581450};
IsoId=Q03001-14; Sequence=VSP_058835, VSP_058836;
-!- TISSUE SPECIFICITY: Isoform 1 is expressed in myoblasts (at
protein level). Isoform 3 is expressed in the skin. Isoform 6 is
expressed in the brain. Highly expressed in skeletal muscle and
cultured keratinocytes. {ECO:0000269|PubMed:11751855,
ECO:0000269|PubMed:19932097, ECO:0000269|PubMed:8752219}.
-!- DOMAIN: Its association with epidermal and simple keratins is
dependent on the tertiary structure induced by heterodimerization
of these intermedaite filaments proteins and most likely involves
recognition sites located in the rod domain of these keratins.
-!- DOMAIN: The microtubule tip localization signal (MtLS) motif;
mediates interaction with MAPRE1 and targeting to the growing
microtubule plus ends.
-!- DISEASE: Neuropathy, hereditary sensory and autonomic, 6 (HSAN6)
[MIM:614653]: A form of hereditary sensory and autonomic
neuropathy, a genetically and clinically heterogeneous group of
disorders characterized by degeneration of dorsal root and
autonomic ganglion cells, and by sensory and/or autonomic
abnormalities. HSAN6 is a severe autosomal recessive disorder
characterized by neonatal hypotonia, respiratory and feeding
difficulties, lack of psychomotor development, and autonomic
abnormalities including labile cardiovascular function, lack of
corneal reflexes leading to corneal scarring, areflexia, and
absent axonal flare response after intradermal histamine
injection. {ECO:0000269|PubMed:22522446}. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-!- DISEASE: 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.
{ECO:0000269|PubMed:20164846, ECO:0000269|PubMed:22113475}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SEQUENCE CAUTION:
Sequence=AAA35538.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the C-terminal part.; Evidence={ECO:0000305};
Sequence=AAA57185.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=BAB70870.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAC04449.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAC04848.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; M69225; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; L11690; AAA52288.1; -; mRNA.
EMBL; AF400226; AAL62061.1; -; mRNA.
EMBL; AF400227; AAL62062.1; -; mRNA.
EMBL; AK055189; BAB70870.1; ALT_INIT; mRNA.
EMBL; AK094883; BAC04449.1; ALT_INIT; mRNA.
EMBL; AK096713; BAC04848.1; ALT_INIT; mRNA.
EMBL; AK295864; BAH12207.1; -; mRNA.
EMBL; AL049215; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL096710; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL590005; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL137008; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL512422; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL512448; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL590037; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; KF458172; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; U31850; AAC50243.1; -; mRNA.
EMBL; U31851; AAC50244.1; ALT_FRAME; mRNA.
EMBL; AF165191; AAD49334.1; -; mRNA.
EMBL; AY032900; AAK63130.1; -; mRNA.
EMBL; AY032901; AAK63131.1; -; mRNA.
EMBL; M63618; AAA35606.1; -; mRNA.
EMBL; BC016991; AAH16991.1; -; mRNA.
EMBL; AB018271; BAA34448.2; -; mRNA.
EMBL; M22942; AAA35538.1; ALT_SEQ; mRNA.
EMBL; X58677; CAA41528.1; -; mRNA.
EMBL; U04850; AAA57184.1; -; Genomic_DNA.
EMBL; U04850; AAA57185.1; ALT_SEQ; Genomic_DNA.
CCDS; CCDS47443.1; -. [Q03001-8]
CCDS; CCDS4959.1; -. [Q03001-3]
PIR; I56317; A40937.
RefSeq; NP_001138241.1; NM_001144769.2.
RefSeq; NP_001138242.1; NM_001144770.1.
RefSeq; NP_001714.1; NM_001723.5. [Q03001-3]
RefSeq; NP_056363.2; NM_015548.4. [Q03001-8]
RefSeq; NP_899236.1; NM_183380.3.
RefSeq; XP_016866713.1; XM_017011224.1. [Q03001-14]
UniGene; Hs.604915; -.
UniGene; Hs.669931; -.
UniGene; Hs.728928; -.
UniGene; Hs.735651; -.
PDB; 3GJO; X-ray; 2.50 A; E/F/G/H=7541-7570.
PDBsum; 3GJO; -.
ProteinModelPortal; Q03001; -.
SMR; Q03001; -.
BioGrid; 107135; 72.
DIP; DIP-33131N; -.
ELM; Q03001; -.
IntAct; Q03001; 44.
MINT; MINT-119936; -.
STRING; 9606.ENSP00000244364; -.
iPTMnet; Q03001; -.
PhosphoSitePlus; Q03001; -.
BioMuta; DST; -.
DMDM; 294862529; -.
EPD; Q03001; -.
MaxQB; Q03001; -.
PaxDb; Q03001; -.
PeptideAtlas; Q03001; -.
PRIDE; Q03001; -.
DNASU; 667; -.
Ensembl; ENST00000244364; ENSP00000244364; ENSG00000151914. [Q03001-8]
Ensembl; ENST00000370765; ENSP00000359801; ENSG00000151914. [Q03001-3]
Ensembl; ENST00000370788; ENSP00000359824; ENSG00000151914. [Q03001-14]
Ensembl; ENST00000439203; ENSP00000404924; ENSG00000151914. [Q03001-9]
GeneID; 667; -.
KEGG; hsa:667; -.
UCSC; uc003pcy.5; human. [Q03001-7]
CTD; 667; -.
DisGeNET; 667; -.
EuPathDB; HostDB:ENSG00000151914.18; -.
GeneCards; DST; -.
H-InvDB; HIX0005976; -.
H-InvDB; HIX0164999; -.
HGNC; HGNC:1090; DST.
HPA; HPA030200; -.
MalaCards; DST; -.
MIM; 113810; gene.
MIM; 614653; phenotype.
MIM; 615425; phenotype.
neXtProt; NX_Q03001; -.
OpenTargets; ENSG00000151914; -.
Orphanet; 314381; Hereditary sensory and autonomic neuropathy type 6.
Orphanet; 89838; KRT14-related epidermolysis bullosa simplex.
PharmGKB; PA25399; -.
eggNOG; ENOG410IQBP; Eukaryota.
eggNOG; ENOG410XP41; LUCA.
GeneTree; ENSGT00760000119163; -.
HOVERGEN; HBG031127; -.
InParanoid; Q03001; -.
KO; K10382; -.
PhylomeDB; Q03001; -.
TreeFam; TF335163; -.
Reactome; R-HSA-2022090; Assembly of collagen fibrils and other multimeric structures.
Reactome; R-HSA-446107; Type I hemidesmosome assembly.
SIGNOR; Q03001; -.
ChiTaRS; DST; human.
EvolutionaryTrace; Q03001; -.
GeneWiki; Dystonin; -.
GenomeRNAi; 667; -.
PRO; PR:Q03001; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000151914; -.
CleanEx; HS_DST; -.
ExpressionAtlas; Q03001; baseline and differential.
Genevisible; Q03001; HS.
GO; GO:0015629; C:actin cytoskeleton; IDA:UniProtKB.
GO; GO:0030424; C:axon; IDA:UniProtKB.
GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
GO; GO:0009925; C:basal plasma membrane; NAS:UniProtKB.
GO; GO:0005604; C:basement membrane; TAS:ProtInc.
GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
GO; GO:0031252; C:cell leading edge; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
GO; GO:0031673; C:H zone; IEA:UniProtKB-SubCell.
GO; GO:0030056; C:hemidesmosome; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005882; C:intermediate filament; IEA:UniProtKB-KW.
GO; GO:0045111; C:intermediate filament cytoskeleton; IDA:UniProtKB.
GO; GO:0015630; C:microtubule cytoskeleton; IDA:UniProtKB.
GO; GO:0035371; C:microtubule plus-end; IDA:UniProtKB.
GO; GO:0005635; C:nuclear envelope; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0030018; C:Z disc; IDA:UniProtKB.
GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0005178; F:integrin binding; IPI:UniProtKB.
GO; GO:0051010; F:microtubule plus-end binding; IDA:UniProtKB.
GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0048870; P:cell motility; IMP:UniProtKB.
GO; GO:0007010; P:cytoskeleton organization; IMP:UniProtKB.
GO; GO:0031581; P:hemidesmosome assembly; IDA:UniProtKB.
GO; GO:0007229; P:integrin-mediated signaling pathway; NAS:UniProtKB.
GO; GO:0045104; P:intermediate filament cytoskeleton organization; IEP:UniProtKB.
GO; GO:0030011; P:maintenance of cell polarity; IMP:UniProtKB.
GO; GO:0000226; P:microtubule cytoskeleton organization; IDA:UniProtKB.
GO; GO:0009611; P:response to wounding; IDA:UniProtKB.
GO; GO:0008090; P:retrograde axonal transport; ISS:UniProtKB.
CDD; cd00014; CH; 2.
CDD; cd00051; EFh; 1.
Gene3D; 1.10.418.10; -; 2.
Gene3D; 3.30.920.20; -; 1.
Gene3D; 3.90.1290.10; -; 3.
InterPro; IPR001589; Actinin_actin-bd_CS.
InterPro; IPR036872; Calponin-like_dom_sf.
InterPro; IPR001715; CH-domain.
InterPro; IPR011992; EF-hand-dom_pair.
InterPro; IPR018247; EF_Hand_1_Ca_BS.
InterPro; IPR002048; EF_hand_dom.
InterPro; IPR003108; GAR_dom.
InterPro; IPR036534; GAR_dom_sf.
InterPro; IPR035915; Plakin_repeat_sf.
InterPro; IPR001101; Plectin_repeat.
InterPro; IPR018159; Spectrin/alpha-actinin.
InterPro; IPR002017; Spectrin_repeat.
Pfam; PF00307; CH; 2.
Pfam; PF13499; EF-hand_7; 1.
Pfam; PF02187; GAS2; 1.
Pfam; PF00681; Plectin; 2.
Pfam; PF00435; Spectrin; 20.
SMART; SM00033; CH; 2.
SMART; SM00054; EFh; 2.
SMART; SM00243; GAS2; 1.
SMART; SM00250; PLEC; 8.
SMART; SM00150; SPEC; 32.
SUPFAM; SSF143575; SSF143575; 1.
SUPFAM; SSF47473; SSF47473; 1.
SUPFAM; SSF47576; SSF47576; 1.
SUPFAM; SSF75399; SSF75399; 2.
PROSITE; PS00019; ACTININ_1; 1.
PROSITE; PS00020; ACTININ_2; 1.
PROSITE; PS50021; CH; 2.
PROSITE; PS00018; EF_HAND_1; 2.
PROSITE; PS50222; EF_HAND_2; 2.
PROSITE; PS51460; GAR; 1.
PROSITE; PS50002; SH3; 1.
1: Evidence at protein level;
3D-structure; Actin-binding; Alternative promoter usage;
Alternative splicing; Calcium; Cell adhesion; Cell junction;
Cell membrane; Cell projection; Coiled coil; Complete proteome;
Cytoplasm; Cytoskeleton; Endoplasmic reticulum; Epidermolysis bullosa;
Intermediate filament; Isopeptide bond; Lipoprotein; Membrane;
Metal-binding; Microtubule; Muscle protein; Neurodegeneration;
Neuropathy; Nucleus; Palmitate; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; SH3 domain; Transmembrane;
Ubl conjugation.
CHAIN 1 7570 Dystonin.
/FTId=PRO_0000078138.
DOMAIN 35 138 Calponin-homology (CH) 1.
{ECO:0000255|PROSITE-ProRule:PRU00044}.
DOMAIN 151 255 Calponin-homology (CH) 2.
{ECO:0000255|PROSITE-ProRule:PRU00044}.
REPEAT 701 797 Spectrin 1.
DOMAIN 887 944 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
REPEAT 1584 1626 Plectin 1.
REPEAT 1660 1703 Plectin 2.
REPEAT 1774 1817 Plectin 3.
REPEAT 1818 1855 Plectin 4.
REPEAT 1856 1891 Plectin 5.
REPEAT 3924 4000 Spectrin 2.
REPEAT 4069 4153 Spectrin 3.
REPEAT 4514 4622 Spectrin 4.
REPEAT 4626 4731 Spectrin 5.
REPEAT 4849 4952 Spectrin 6.
REPEAT 5281 5389 Spectrin 7.
REPEAT 5396 5497 Spectrin 8.
REPEAT 5504 5606 Spectrin 9.
REPEAT 5829 5933 Spectrin 10.
REPEAT 5940 6042 Spectrin 11.
REPEAT 6048 6154 Spectrin 12.
REPEAT 6184 6264 Spectrin 13.
REPEAT 6270 6373 Spectrin 14.
REPEAT 6379 6481 Spectrin 15.
REPEAT 6490 6592 Spectrin 16.
REPEAT 6597 6700 Spectrin 17.
REPEAT 6705 6811 Spectrin 18.
REPEAT 6818 6918 Spectrin 19.
REPEAT 6923 7026 Spectrin 20.
DOMAIN 7197 7232 EF-hand 1. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 7233 7268 EF-hand 2. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 7273 7351 GAR. {ECO:0000255|PROSITE-
ProRule:PRU00792}.
CA_BIND 7210 7221 1. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
CA_BIND 7246 7257 2. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
REGION 35 252 Actin-binding.
MOTIF 1383 1389 Nuclear localization signal; in isoform
6. {ECO:0000250}.
MOTIF 7550 7553 Microtubule tip localization signal.
COMPBIAS 2394 2431 Asp-rich.
COMPBIAS 2592 2599 Poly-Asp.
MOD_RES 236 236 Phosphoserine.
{ECO:0000250|UniProtKB:Q91ZU6}.
MOD_RES 237 237 Phosphoserine.
{ECO:0000250|UniProtKB:Q91ZU6}.
MOD_RES 1382 1382 Phosphoserine.
{ECO:0000250|UniProtKB:Q91ZU6}.
MOD_RES 2229 2229 Phosphoserine.
{ECO:0000250|UniProtKB:Q91ZU6}.
MOD_RES 2919 2919 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 3968 3968 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 4749 4749 Phosphoserine.
{ECO:0000250|UniProtKB:Q91ZU6}.
MOD_RES 7432 7432 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 7510 7510 Phosphoserine.
{ECO:0000250|UniProtKB:Q91ZU6}.
MOD_RES 7513 7513 Phosphoserine.
{ECO:0000250|UniProtKB:Q91ZU6}.
MOD_RES 7525 7525 Phosphoserine.
{ECO:0000250|UniProtKB:Q91ZU6}.
CROSSLNK 5470 5470 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
VAR_SEQ 1 3753 Missing (in isoform 5).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_041524.
VAR_SEQ 1 381 MAGYLSPAAYLYVEEQEYLQAYEDVLERYKDERDKVQKKTF
TKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLP
REKGRMRFHRLQNVQIALDYLKRRQVKLVNIRNDDITDGNP
KLTLGLIWTIILHFQISDIHVTGESEDMSAKERLLLWTQQA
TEGYAGIRCENFTTCWRDGKLFNAIIHKYRPDLIDMNTVAV
QSNLANLEHAFYVAEKIGVIRLLDPEDVDVSSPDEKSVITY
VSSLYDAFPKVPEGGEGIGANDVEVKWIEYQNMVNYLIQWI
RHHVTTMSERTFPNNPVELKALYNQYLQFKETEIPPKETEK
SKIKRLYKLLEIWIEFGRIKLLQGYHPNDIEKEWGKLIIAM
LEREKALRPEVE -> MHSSSYSYRSSDSVFSNTTSTRTSL
DSNENLLLVHCGPTLINSCISFGSESFDGH (in
isoform 2, isoform 3 and isoform 4).
{ECO:0000303|PubMed:11751855,
ECO:0000303|PubMed:1712022,
ECO:0000303|PubMed:1717441,
ECO:0000303|PubMed:8345227,
ECO:0000303|PubMed:9872452}.
/FTId=VSP_041525.
VAR_SEQ 1 138 MAGYLSPAAYLYVEEQEYLQAYEDVLERYKDERDKVQKKTF
TKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLP
REKGRMRFHRLQNVQIALDYLKRRQVKLVNIRNDDITDGNP
KLTLGLIWTIILHFQ -> MQHSIFSLKKKRCHSLYTSMSS
VSKDTDGNE (in isoform 7).
{ECO:0000303|PubMed:10428034}.
/FTId=VSP_041526.
VAR_SEQ 1 138 MAGYLSPAAYLYVEEQEYLQAYEDVLERYKDERDKVQKKTF
TKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLP
REKGRMRFHRLQNVQIALDYLKRRQVKLVNIRNDDITDGNP
KLTLGLIWTIILHFQ -> MGNVCGCVRAEKEEQYVDPAKT
PLNPEKYSPGRKYFRRKPIKKTGGDKESVGANNENEGKKKS
SSQPSKEQPAPLSRGLVQQESVTLNSALGDGIQQKKTEVVA
DSVKQKLLPSAVSSWSDCVNTSPAKDSETEVKVSELDERIS
EKDSTPYCAKRKKHLDDVNTSEITFQEKTDVFSFRKAASLS
SIPSGIERSLEKGGFPEDPPKSYSSIQEKQNTERFCPHATQ
HFQFKKKRCHSLYTSMSSVSKDTDGNE (in isoform
8). {ECO:0000303|PubMed:14702039}.
/FTId=VSP_041527.
VAR_SEQ 1 30 MAGYLSPAAYLYVEEQEYLQAYEDVLERYK -> MIAAAFL
VLLRPYSIQCALFLLLLLLGTIATIVFFCCWHRKLQKGRHP
MKSVFSGRSRSRDAVLRSHHFRSEGFRASPRHLRRRVAAAA
AARLEEVKPVVEVHHQSEQETSVRKRRIKKSSRVQPEFYHS
VQGASIRRPSSGNASYRCSMSSSADFSDEDDFSQKSGSASP
APGDTLPWNLPKHERSKRKIQGGSVLDPAERAVLRIA (in
isoform 6). {ECO:0000303|PubMed:8575775}.
/FTId=VSP_041528.
VAR_SEQ 47 7570 Missing (in isoform 6).
{ECO:0000303|PubMed:8575775}.
/FTId=VSP_041529.
VAR_SEQ 189 7570 Missing (in isoform 7).
{ECO:0000303|PubMed:10428034}.
/FTId=VSP_041530.
VAR_SEQ 778 789 AYRAAMQTQWSW -> VKLESVMVLVEY (in isoform
8). {ECO:0000303|PubMed:14702039}.
/FTId=VSP_041531.
VAR_SEQ 790 7570 Missing (in isoform 8).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_041532.
VAR_SEQ 1433 1433 K -> IKRCKETSEHGAYSDLLQRQKATVLENSKLTGKISE
LERMVAELKKQKSRVEEELPKVREAAENELRKQQRNVEDIS
LQKIRAESEAKQYRRELETIVREKEAAERELERVRQLTIEA
EAKRAAVEENLLNFRNQLEENTFTRRTLEDHLKRKDLSLND
LEQQKNKLMEELRRKRDNEEELLKLIKQMEKDLAFQKQVAE
KQLKEKQKIELEARRKITEIQYTCRENALPVCPITQATSCR
AVTGLQQEHDKQKAEELKQQVDELTAANRKAEQDMRELTYE
LNALQLEKTSSEEKARLLKDKLDETNNTLRCLKLELERKDQ
AEKGYSQQLRELGRQLNQTTGKAEEAMQEASDLKKIKRNYQ
LELESLNHEKGKLQREVDRITRAHAVAEKNIQHLNSQIHSF
RDEKELERLQICQRKSDHLKEQFEKSHEQLLQNIKAEKENN
DKIQRLNEELEKSNECAEMLKQKVEELTRQNNETKLMMQRI
QAESENIVLEKQTIQQRCEALKIQADGFKDQLRSTNEHLHK
QTKTEQDFQRKIKCLEEDLAKSQNLVSEFKQKCDQQNIIIQ
NTKKEVRNLNAELNASKEEKRRGEQKVQLQQAQVQELNNRL
KKVQDELHLKTIEEQMTHRKMVLFQEESGKFKQSAEEFRKK
MEKLMESKVITENDISGIRLDFVSLQQENSRAQENAKLCET
NIKELERQLQQYREQMQQGQHMEANHYQKCQKLEDELIAQK
REVENLKQKMDQQIKEHEHQLVLLQCEIQKKSTAKDCTFKP
DFEMTVKECQHSGELSSRNTGHLHPTPRSPLLRWTQEPQPL
EEKWQHRVVEQIPKEVQFQPPGAPLEKEKSQQCYSEYFSQT
STELQITFDETNPITRLSEIEKIRDQALNNSRPPVRYQDNA
CEMELVKVLTPLEIAKNKQYDMHTEVTTLKQEKNPVPSAEE
WMLEGCRASGGLKKGDFLKKGLEPETFQNFDGDHACSVRDD
EFKFQGLRHTVTARQLVEAKLLDMRTIEQLRLGLKTVEEVQ
KTLNKFLTKATSIAGLYLESTKEKISFASAAERIIIDKMVA
LAFLEAQAATGFIIDPISGQTYSVEDAVLKGVVDPEFRIRL
LEAEKAAVGYSYSSKTLSVFQAMENRMLDRQKGKHILEAQI
ASGGVIDPVRGIRVPPEIALQQGLLNNAILQFLHEPSSNTR
VFPNPNNKQALYYSELLRMCVFDVESQCFLFPFGERNISNL
NVKKTHRISVVDTKTGSELTVYEAFQRNLIEKSIYLELSGQ
QYQWKEAMFFESYGHSSHMLTDTKTGLHFNINEAIEQGTID
KALVKKYQEGLITLTELADSLLSRLVPKKDLHSPVAGYWLT
ASGERISVLKASRRNLVDRITALRCLEAQVSTGGIIDPLTG
KKYRVAEALHRGLVDEGFAQQLRQCELVITGIGHPITNKMM
SVVEAVNANIINKEMGIRCLEFQYLTGGLIEPQVHSRLSIE
EALQVGIIDVLIATKLKDQKSYVRNIICPQTKRKLTYKEAL
EKADFDFHTGLKLLEVSEPLMTGISSLYYSS (in
isoform 3). {ECO:0000303|PubMed:1712022,
ECO:0000303|PubMed:1717441,
ECO:0000303|PubMed:8345227}.
/FTId=VSP_041533.
VAR_SEQ 1434 7570 Missing (in isoform 3).
{ECO:0000303|PubMed:1712022,
ECO:0000303|PubMed:1717441,
ECO:0000303|PubMed:8345227}.
/FTId=VSP_041534.
VAR_SEQ 1550 3635 Missing (in isoform 2).
{ECO:0000303|PubMed:11751855,
ECO:0000303|PubMed:9872452}.
/FTId=VSP_041535.
VAR_SEQ 1551 3636 Missing (in isoform 9).
/FTId=VSP_058835.
VAR_SEQ 3387 7570 Missing (in isoform 4).
{ECO:0000303|PubMed:11751855}.
/FTId=VSP_041536.
VAR_SEQ 4184 4200 GQVPLNSTALQDIISKN -> DVGTGYCRSSEQYKCHE
(in isoform 5).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_041537.
VAR_SEQ 4201 7570 Missing (in isoform 5).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_041538.
VAR_SEQ 5546 5654 Missing (in isoform 9).
/FTId=VSP_058836.
VAR_SEQ 7352 7375 Missing (in isoform 2).
{ECO:0000303|PubMed:11751855,
ECO:0000303|PubMed:9872452}.
/FTId=VSP_041539.
VAR_SEQ 7442 7442 K -> KILHPLTRNYGKPWLTNSKMSTPCKAAECSDFPVPS
AE (in isoform 2).
{ECO:0000303|PubMed:11751855,
ECO:0000303|PubMed:9872452}.
/FTId=VSP_041540.
VARIANT 1319 1319 N -> K (in dbSNP:rs35014998).
/FTId=VAR_063045.
VARIANT 2332 2332 Q -> R (in dbSNP:rs16888053).
/FTId=VAR_063046.
VARIANT 3720 3720 Q -> R (in dbSNP:rs4712138).
/FTId=VAR_063047.
VARIANT 5138 5138 T -> A (in dbSNP:rs4715631).
{ECO:0000269|PubMed:14702039}.
/FTId=VAR_063048.
MUTAGEN 7548 7548 K->Q: Loss of interaction with MAPRE1 and
association with microtubule growing
ends. {ECO:0000269|PubMed:19632184}.
MUTAGEN 7550 7550 S->A,N: Loss of association with
microtubule growing ends.
{ECO:0000269|PubMed:19632184}.
MUTAGEN 7552 7552 I->N: Loss of interaction with MAPRE1 and
association with the growing microtubule
plus ends; when associated with N-7553.
{ECO:0000269|PubMed:19632184}.
MUTAGEN 7553 7553 P->N: Loss of interaction with MAPRE1 and
association with the growing microtubule
plus ends; when associated with N-7552.
{ECO:0000269|PubMed:19632184}.
MUTAGEN 7557 7557 R->N: Loss of interaction with MAPRE1 and
association with the growing microtubule
plus ends.
MUTAGEN 7558 7558 K->N: Loss of interaction with MAPRE1 and
association with the growing microtubule
plus ends.
CONFLICT 573 573 P -> A (in Ref. 4; BAH12207).
{ECO:0000305}.
CONFLICT 1177 1177 V -> G (in Ref. 1; M69225 and 3;
AAL62061/AAL62062). {ECO:0000305}.
CONFLICT 1363 1363 K -> E (in Ref. 3; AAL62061).
{ECO:0000305}.
CONFLICT 4703 4703 R -> H (in Ref. 4; BAC04449).
{ECO:0000305}.
CONFLICT 4935 4935 N -> S (in Ref. 4; BAC04449).
{ECO:0000305}.
CONFLICT 5030 5030 E -> G (in Ref. 3; AAL62061).
{ECO:0000305}.
CONFLICT 5177 5177 Q -> R (in Ref. 3; AAL62061).
{ECO:0000305}.
CONFLICT 5225 5225 M -> I (in Ref. 4; BAB70870).
{ECO:0000305}.
CONFLICT 5299 5299 K -> R (in Ref. 3; AAL62061).
{ECO:0000305}.
CONFLICT 5823 5823 I -> V (in Ref. 3; AAL62061).
{ECO:0000305}.
CONFLICT 5882 5882 K -> R (in Ref. 3; AAL62061).
{ECO:0000305}.
CONFLICT 5986 5986 L -> S (in Ref. 3; AAL62061).
{ECO:0000305}.
CONFLICT 6080 6080 K -> E (in Ref. 4; BAC04848).
{ECO:0000305}.
CONFLICT 6186 6186 D -> G (in Ref. 3; AAL62061).
{ECO:0000305}.
CONFLICT 6440 6440 A -> G (in Ref. 3; AAL62061).
{ECO:0000305}.
SEQUENCE 7570 AA; 860662 MW; 1EA992E53D1C243E CRC64;
MAGYLSPAAY LYVEEQEYLQ AYEDVLERYK DERDKVQKKT FTKWINQHLM KVRKHVNDLY
EDLRDGHNLI SLLEVLSGDT LPREKGRMRF HRLQNVQIAL DYLKRRQVKL VNIRNDDITD
GNPKLTLGLI WTIILHFQIS DIHVTGESED MSAKERLLLW TQQATEGYAG IRCENFTTCW
RDGKLFNAII HKYRPDLIDM NTVAVQSNLA NLEHAFYVAE KIGVIRLLDP EDVDVSSPDE
KSVITYVSSL YDAFPKVPEG GEGIGANDVE VKWIEYQNMV NYLIQWIRHH VTTMSERTFP
NNPVELKALY NQYLQFKETE IPPKETEKSK IKRLYKLLEI WIEFGRIKLL QGYHPNDIEK
EWGKLIIAML EREKALRPEV ERLEMLQQIA NRVQRDSVIC EDKLILAGNA LQSDSKRLES
GVQFQNEAEI AGYILECENL LRQHVIDVQI LIDGKYYQAD QLVQRVAKLR DEIMALRNEC
SSVYSKGRIL TTEQTKLMIS GITQSLNSGF AQTLHPSLTS GLTQSLTPSL TSSSMTSGLS
SGMTSRLTPS VTPAYTPGFP SGLVPNFSSG VEPNSLQTLK LMQIRKPLLK SSLLDQNLTE
EEINMKFVQD LLNWVDEMQV QLDRTEWGSD LPSVESHLEN HKNVHRAIEE FESSLKEAKI
SEIQMTAPLK LTYAEKLHRL ESQYAKLLNT SRNQERHLDT LHNFVSRATN ELIWLNEKEE
EEVAYDWSER NTNIARKKDY HAELMRELDQ KEENIKSVQE IAEQLLLENH PARLTIEAYR
AAMQTQWSWI LQLCQCVEQH IKENTAYFEF FNDAKEATDY LRNLKDAIQR KYSCDRSSSI
HKLEDLVQES MEEKEELLQY KSTIANLMGK AKTIIQLKPR NSDCPLKTSI PIKAICDYRQ
IEITIYKDDE CVLANNSHRA KWKVISPTGN EAMVPSVCFT VPPPNKEAVD LANRIEQQYQ
NVLTLWHESH INMKSVVSWH YLINEIDRIR ASNVASIKTM LPGEHQQVLS NLQSRFEDFL
EDSQESQVFS GSDITQLEKE VNVCKQYYQE LLKSAEREEQ EESVYNLYIS EVRNIRLRLE
NCEDRLIRQI RTPLERDDLH ESVFRITEQE KLKKELERLK DDLGTITNKC EEFFSQAAAS
SSVPTLRSEL NVVLQNMNQV YSMSSTYIDK LKTVNLVLKN TQAAEALVKL YETKLCEEEA
VIADKNNIEN LISTLKQWRS EVDEKRQVFH ALEDELQKAK AISDEMFKTY KERDLDFDWH
KEKADQLVER WQNVHVQIDN RLRDLEGIGK SLKYYRDTYH PLDDWIQQVE TTQRKIQENQ
PENSKTLATQ LNQQKMLVSE IEMKQSKMDE CQKYAEQYSA TVKDYELQTM TYRAMVDSQQ
KSPVKRRRMQ SSADLIIQEF MDLRTRYTAL VTLMTQYIKF AGDSLKRLEE EEKSLEEEKK
EHVEKAKELQ KWVSNISKTL KDAEKAGKPP FSKQKISSEE ISTKKEQLSE ALQTIQLFLA
KHGDKMTDEE RNELEKQVKT LQESYNLLFS ESLKQLQESQ TSGDVKVEEK LDKVIAGTID
QTTGEVLSVF QAVLRGLIDY DTGIRLLETQ LMISGLISPE LRKCFDLKDA KSHGLIDEQI
LCQLKELSKA KEIISAASPT TIPVLDALAQ SMITESMAIK VLEILLSTGS LVIPATGEQL
TLQKAFQQNL VSSALFSKVL ERQNMCKDLI DPCTSEKVSL IDMVQRSTLQ ENTGMWLLPV
RPQEGGRITL KCGRNISILR AAHEGLIDRE TMFRLLSAQL LSGGLINSNS GQRMTVEEAV
REGVIDRDTA SSILTYQVQT GGIIQSNPAK RLTVDEAVQC DLITSSSALL VLEAQRGYVG
LIWPHSGEIF PTSSSLQQEL ITNELAYKIL NGRQKIAALY IPESSQVIGL DAAKQLGIID
NNTASILKNI TLPDKMPDLG DLEACKNARR WLSFCKFQPS TVHDYRQEED VFDGEEPVTT
QTSEETKKLF LSYLMINSYM DANTGQRLLL YDGDLDEAVG MLLEGCHAEF DGNTAIKECL
DVLSSSGVFL NNASGREKDE CTATPSSFNK CHCGEPEHEE TPENRKCAID EEFNEMRNTV
INSEFSQSGK LASTISIDPK VNSSPSVCVP SLISYLTQTE LADISMLRSD SENILTNYEN
QSRVETNERA NECSHSKNIQ NFPSDLIENP IMKSKMSKFC GVNETENEDN TNRDSPIFDY
SPRLSALLSH DKLMHSQGSF NDTHTPESNG NKCEAPALSF SDKTMLSGQR IGEKFQDQFL
GIAAINISLP GEQYGQKSLN MISSNPQVQY HNDKYISNTS GEDEKTHPGF QQMPEDKEDE
SEIEEYSCAV TPGGDTDNAI VSLTCATPLL DETISASDYE TSLLNDQQNN TGTDTDSDDD
FYDTPLFEDD DHDSLLLDGD DRDCLHPEDY DTLQEENDET ASPADVFYDV SKENENSMVP
QGAPVGSLSV KNKAHCLQDF LMDVEKDELD SGEKIHLNPV GSDKVNGQSL ETGSERECTN
ILEGDESDSL TDYDIVGGKE SFTASLKFDD SGSWRGRKEE YVTGQEFHSD TDHLDSMQSE
ESYGDYIYDS NDQDDDDDDG IDEEGGGIRD ENGKPRCQNV AEDMDIQLCA SILNENSDEN
ENINTMILLD KMHSCSSLEK QQRVNVVQLA SPSENNLVTE KSNLPEYTTE IAGKSKENLL
NHEMVLKDVL PPIIKDTESE KTFGPASISH DNNNISSTSE LGTDLANTKV KLIQGSELPE
LTDSVKGKDE YFKNMTPKVD SSLDHIICTE PDLIGKPAEE SHLSLIASVT DKDPQGNGSD
LIKGRDGKSD ILIEDETSIQ KMYLGEGEVL VEGLVEEENR HLKLLPGKNT RDSFKLINSQ
FPFPQITNNE ELNQKGSLKK ATVTLKDEPN NLQIIVSKSP VQFENLEEIF DTSVSKEISD
DITSDITSWE GNTHFEESFT DGPEKELDLF TYLKHCAKNI KAKDVAKPNE DVPSHVLITA
PPMKEHLQLG VNNTKEKSTS TQKDSPLNDM IQSNDLCSKE SISGGGTEIS QFTPESIEAT
LSILSRKHVE DVGKNDFLQS ERCANGLGND NSSNTLNTDY SFLEINNKKE RIEQQLPKEQ
ALSPRSQEKE VQIPELSQVF VEDVKDILKS RLKEGHMNPQ EVEEPSACAD TKILIQNLIK
RITTSQLVNE ASTVPSDSQM SDSSGVSPMT NSSELKPESR DDPFCIGNLK SELLLNILKQ
DQHSQKITGV FELMRELTHM EYDLEKRGIT SKVLPLQLEN IFYKLLADGY SEKIEHVGDF
NQKACSTSEM MEEKPHILGD IKSKEGNYYS PNLETVKEIG LESSTVWAST LPRDEKLKDL
CNDFPSHLEC TSGSKEMASG DSSTEQFSSE LQQCLQHTEK MHEYLTLLQD MKPPLDNQES
LDNNLEALKN QLRQLETFEL GLAPIAVILR KDMKLAEEFL KSLPSDFPRG HVEELSISHQ
SLKTAFSSLS NVSSERTKQI MLAIDSEMSK LAVSHEEFLH KLKSFSDWVS EKSKSVKDIE
IVNVQDSEYV KKRLEFLKNV LKDLGHTKMQ LETTAFDVQF FISEYAQDLS PNQSKQLLRL
LNTTQKCFLD VQESVTTQVE RLETQLHLEQ DLDDQKIVAE RQQEYKEKLQ GICDLLTQTE
NRLIGHQEAF MIGDGTVELK KYQSKQEELQ KDMQGSAQAL AEVVKNTENF LKENGEKLSQ
EDKALIEQKL NEAKIKCEQL NLKAEQSKKE LDKVVTTAIK EETEKVAAVK QLEESKTKIE
NLLDWLSNVD KDSERAGTKH KQVIEQNGTH FQEGDGKSAI GEEDEVNGNL LETDVDGQVG
TTQENLNQQY QKVKAQHEKI ISQHQAVIIA TQSAQVLLEK QGQYLSPEEK EKLQKNMKEL
KVHYETALAE SEKKMKLTHS LQEELEKFDA DYTEFEHWLQ QSEQELENLE AGADDINGLM
TKLKRQKSFS EDVISHKGDL RYITISGNRV LEAAKSCSKR DGGKVDTSAT HREVQRKLDH
ATDRFRSLYS KCNVLGNNLK DLVDKYQHYE DASCGLLAGL QACEATASKH LSEPIAVDPK
NLQRQLEETK ALQGQISSQQ VAVEKLKKTA EVLLDARGSL LPAKNDIQKT LDDIVGRYED
LSKSVNERNE KLQITLTRSL SVQDGLDEML DWMGNVESSL KEQGQVPLNS TALQDIISKN
IMLEQDIAGR QSSINAMNEK VKKFMETTDP STASSLQAKM KDLSARFSEA SHKHKETLAK
MEELKTKVEL FENLSEKLQT FLETKTQALT EVDVPGKDVT ELSQYMQEST SEFLEHKKHL
EVLHSLLKEI SSHGLPSDKA LVLEKTNNLS KKFKEMEDTI KEKKEAVTSC QEQLDAFQVL
VKSLKSWIKE TTKKVPIVQP SFGAEDLGKS LEDTKKLQEK WSLKTPEIQK VNNSGISLCN
LISAVTTPAK AIAAVKSGGA VLNGEGTATN TEEFWANKGL TSIKKDMTDI SHGYEDLGLL
LKDKIAELNT KLSKLQKAQE ESSAMMQWLQ KMNKTATKWQ QTPAPTDTEA VKTQVEQNKS
FEAELKQNVN KVQELKDKLT ELLEENPDTP EAPRWKQMLT EIDSKWQELN QLTIDRQQKL
EESSNNLTQF QTVEAQLKQW LVEKELMVSV LGPLSIDPNM LNTQRQQVQI LLQEFATRKP
QYEQLTAAGQ GILSRPGEDP SLRGIVKEQL AAVTQKWDSL TGQLSDRCDW IDQAIVKSTQ
YQSLLRSLSD KLSDLDNKLS SSLAVSTHPD AMNQQLETAQ KMKQEIQQEK KQIKVAQALC
EDLSALVKEE YLKAELSRQL EGILKSFKDV EQKAENHVQH LQSACASSHQ FQQMSRDFQA
WLDTKKEEQN KSHPISAKLD VLESLIKDHK DFSKTLTAQS HMYEKTIAEG ENLLLKTQGS
EKAALQLQLN TIKTNWDTFN KQVKERENKL KESLEKALKY KEQVETLWPW IDKCQNNLEE
IKFCLDPAEG ENSIAKLKSL QKEMDQHFGM VELLNNTANS LLSVCEIDKE VVTDENKSLI
QKVDMVTEQL HSKKFCLENM TQKFKEFQEV SKESKRQLQC AKEQLDIHDS LGSQAYSNKY
LTMLQTQQKS LQALKHQVDL AKRLAQDLVV EASDSKGTSD VLLQVETIAQ EHSTLSQQVD
EKCSFLETKL QGIGHFQNTI REMFSQFAEF DDELDSMAPV GRDAETLQKQ KETIKAFLKK
LEALMASNDN ANKTCKMMLA TEETSPDLVG IKRDLEALSK QCNKLLDRAQ AREEQVEGTI
KRLEEFYSKL KEFSILLQKA EEHEESQGPV GMETETINQQ LNMFKVFQKE EIEPLQGKQQ
DVNWLGQGLI QSAAKSTSTQ GLEHDLDDVN ARWKTLNKKV AQRAAQLQEA LLHCGRFQDA
LESLLSWMVD TEELVANQKP PSAEFKVVKA QIQEQKLLQR LLDDRKSTVE VIKREGEKIA
TTAEPADKVK ILKQLSLLDS RWEALLNKAE TRNRQLEGIS VVAQQFHETL EPLNEWLTTI
EKRLVNCEPI GTQASKLEEQ IAQHKALEDD IINHNKHLHQ AVSIGQSLKV LSSREDKDMV
QSKLDFSQVW YIEIQEKSHS RSELLQQALC NAKIFGEDEV ELMNWLNEVH DKLSKLSVQD
YSTEGLWKQQ SELRVLQEDI LLRKQNVDQA LLNGLELLKQ TTGDEVLIIQ DKLEAIKARY
KDITKLSTDV AKTLEQALQL ARRLHSTHEE LCTWLDKVEV ELLSYETQVL KGEEASQAQM
RPKELKKEAK NNKALLDSLN EVSSALLELV PWRAREGLEK MVAEDNERYR LVSDTITQKV
EEIDAAILRS QQFDQAADAE LSWITETEKK LMSLGDIRLE QDQTSAQLQV QKTFTMEILR
HKDIIDDLVK SGHKIMTACS EEEKQSMKKK LDKVLKNYDT ICQINSERYL QLERAQSLVN
QFWETYEELW PWLTETQSII SQLPAPALEY ETLRQQQEEH RQLRELIAEH KPHIDKMNKT
GPQLLELSPG EGFSIQEKYV AADTLYSQIK EDVKKRAVAL DEAISQSTQF HDKIDQILES
LERIVERLRQ PPSISAEVEK IKEQISENKN VSVDMEKLQP LYETLKQRGE EMIARSGGTD
KDISAKAVQD KLDQMVFIWE NIHTLVEERE AKLLDVMELA EKFWCDHMSL IVTIKDTQDF
IRDLEDPGID PSVVKQQQEA AETIREEIDG LQEELDIVIN LGSELIAACG EPDKPIVKKS
IDELNSAWDS LNKAWKDRID KLEEAMQAAV QYQDGLQAVF DWVDIAGGKL ASMSPIGTDL
ETVKQQIEEL KQFKSEAYQQ QIEMERLNHQ AELLLKKVTE ESDKHTVQDP LMELKLIWDS
LEERIINRQH KLEGALLALG QFQHALDELL AWLTHTEGLL SEQKPVGGDP KAIEIELAKH
HVLQNDVLAH QSTVEAVNKA GNDLIESSAG EEASNLQNKL EVLNQRWQNV LEKTEQRKQQ
LDGALRQAKG FHGEIEDLQQ WLTDTERHLL ASKPLGGLPE TAKEQLNVHM EVCAAFEAKE
ETYKSLMQKG QQMLARCPKS AETNIDQDIN NLKEKWESVE TKLNERKTKL EEALNLAMEF
HNSLQDFINW LTQAEQTLNV ASRPSLILDT VLFQIDEHKV FANEVNSHRE QIIELDKTGT
HLKYFSQKQD VVLIKNLLIS VQSRWEKVVQ RLVERGRSLD DARKRAKQFH EAWSKLMEWL
EESEKSLDSE LEIANDPDKI KTQLAQHKEF QKSLGAKHSV YDTTNRTGRS LKEKTSLADD
NLKLDDMLSE LRDKWDTICG KSVERQNKLE EALLFSGQFT DALQALIDWL YRVEPQLAED
QPVHGDIDLV MNLIDNHKAF QKELGKRTSS VQALKRSARE LIEGSRDDSS WVKVQMQELS
TRWETVCALS ISKQTRLEAA LRQAEEFHSV VHALLEWLAE AEQTLRFHGV LPDDEDALRT
LIDQHKEFMK KLEEKRAELN KATTMGDTVL AICHPDSITT IKHWITIIRA RFEEVLAWAK
QHQQRLASAL AGLIAKQELL EALLAWLQWA ETTLTDKDKE VIPQEIEEVK ALIAEHQTFM
EEMTRKQPDV DKVTKTYKRR AADPSSLQSH IPVLDKGRAG RKRFPASSLY PSGSQTQIET
KNPRVNLLVS KWQQVWLLAL ERRRKLNDAL DRLEELREFA NFDFDIWRKK YMRWMNHKKS
RVMDFFRRID KDQDGKITRQ EFIDGILSSK FPTSRLEMSA VADIFDRDGD GYIDYYEFVA
ALHPNKDAYK PITDADKIED EVTRQVAKCK CAKRFQVEQI GDNKYRFFLG NQFGDSQQLR
LVRILRSTVM VRVGGGWMAL DEFLVKNDPC RVHHHGSKML RSESNSSITT TQPTIAKGRT
NMELREKFIL ADGASQGMAA FRPRGRRSRP SSRGASPNRS TSVSSQAAQA ASPQVPATTT
PKGTPIQGSK LRLPGYLSGK GFHSGEDSGL ITTAAARVRT QFADSKKTPS RPGSRAGSKA
GSRASSRRGS DASDFDISEI QSVCSDVETV PQTHRPTPRA GSRPSTAKPS KIPTPQRKSP
ASKLDKSSKR


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U0309b CLIA 180 kDa bullous pemphigoid antigen 2,Bos taurus,Bovine,BP180,BPAG2,Bullous pemphigoid antigen 2,COL17A1,Collagen alpha-1(XVII) chain 96T
U0309m CLIA 180 kDa bullous pemphigoid antigen 2,Bp180,Bpag2,Bullous pemphigoid antigen 2,Col17a1,Collagen alpha-1(XVII) chain,Mouse,Mus musculus 96T
U0309h CLIA 180 kDa bullous pemphigoid antigen 2,BP180,BPAG2,Bullous pemphigoid antigen 2,COL17A1,Collagen alpha-1(XVII) chain,Homo sapiens,Human 96T
E0309h ELISA 180 kDa bullous pemphigoid antigen 2,BP180,BPAG2,Bullous pemphigoid antigen 2,COL17A1,Collagen alpha-1(XVII) chain,Homo sapiens,Human 96T
E0309h ELISA kit 180 kDa bullous pemphigoid antigen 2,BP180,BPAG2,Bullous pemphigoid antigen 2,COL17A1,Collagen alpha-1(XVII) chain,Homo sapiens,Human 96T
U0309c CLIA 180 kDa bullous pemphigoid antigen 2,BP180,BPAG2,Bullous pemphigoid antigen 2,Chicken,COL17A1,Collagen alpha-1(XVII) chain,Gallus gallus 96T
E0309c ELISA 180 kDa bullous pemphigoid antigen 2,BP180,BPAG2,Bullous pemphigoid antigen 2,Chicken,COL17A1,Collagen alpha-1(XVII) chain,Gallus gallus 96T
E0309c ELISA kit 180 kDa bullous pemphigoid antigen 2,BP180,BPAG2,Bullous pemphigoid antigen 2,Chicken,COL17A1,Collagen alpha-1(XVII) chain,Gallus gallus 96T
E0309c ELISA 180 kDa bullous pemphigoid antigen 2,BP180,BPAG2,Bullous pemphigoid antigen 2,Canis familiaris,Canis lupus familiaris,COL17A1,Collagen alpha-1(XVII) chain,Dog 96T
U0309c CLIA 180 kDa bullous pemphigoid antigen 2,BP180,BPAG2,Bullous pemphigoid antigen 2,Canis familiaris,Canis lupus familiaris,COL17A1,Collagen alpha-1(XVII) chain,Dog 96T
E0309c ELISA kit 180 kDa bullous pemphigoid antigen 2,BP180,BPAG2,Bullous pemphigoid antigen 2,Canis familiaris,Canis lupus familiaris,COL17A1,Collagen alpha-1(XVII) chain,Dog 96T
gen5769 COHA1_MOUSE 180 kDa bullous pemphigoid antigen 2 ELISA tesk kit 1
gen5772 COHA1_MOUSE Bullous pemphigoid antigen 2 ELISA tesk kit 1
gen5757 COHA1_CHICK 180 kDa bullous pemphigoid antigen 2 ELISA tesk kit 1
gen5754 COHA1_CANFA Bullous pemphigoid antigen 2 ELISA tesk kit 1
gen5751 COHA1_CANFA 180 kDa bullous pemphigoid antigen 2 ELISA tesk kit 1
gen5766 COHA1_HUMAN Bullous pemphigoid antigen 2 ELISA tesk kit 1
gen5745 COHA1_BOVIN 180 kDa bullous pemphigoid antigen 2 ELISA tesk kit 1
gen5763 COHA1_HUMAN 180 kDa bullous pemphigoid antigen 2 ELISA tesk kit 1


 

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