DYST_HUMAN
ID DYST_HUMAN Reviewed; 7570 AA.
AC Q03001; B7Z3H1; E7ERU0; O94833; Q12825; Q13266; Q13267; Q13775; Q5TBT0;
AC Q5TBT2; Q5TF23; Q5TF24; Q8N1T8; Q8N8J3; Q8WXK8; Q8WXK9; Q96AK9; Q96DQ5;
AC Q96J76; Q96QT5; Q9H555; Q9UGD7; Q9UGD8; Q9UN10;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 4.
DT 03-AUG-2022, entry version 230.
DE RecName: Full=Dystonin {ECO:0000305};
DE AltName: Full=230 kDa bullous pemphigoid antigen;
DE AltName: Full=230/240 kDa bullous pemphigoid antigen;
DE AltName: Full=Bullous pemphigoid antigen 1;
DE Short=BPA;
DE Short=Bullous pemphigoid antigen;
DE AltName: Full=Dystonia musculorum protein;
DE AltName: Full=Hemidesmosomal plaque protein;
GN Name=DST {ECO:0000312|HGNC:HGNC:1090};
GN Synonyms=BP230, BP240, BPAG1, DMH, DT, KIAA0728;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND DISEASE.
RC TISSUE=Keratinocyte;
RX PubMed=1717441; DOI=10.1016/s0021-9258(18)55195-4;
RA Sawamura D., Li K., Chu M.-L., Uitto J.;
RT "Human bullous pemphigoid antigen (BPAG1). Amino acid sequences deduced
RT from cloned cDNAs predict biologically important peptide segments and
RT protein domains.";
RL J. Biol. Chem. 266:17784-17790(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC TISSUE=Keratinocyte;
RX PubMed=8345227; DOI=10.1111/1523-1747.ep12365083;
RA Elgart G.W., Stanley J.R.;
RT "Cloning of the 5' mRNA for the 230-kD bullous pemphigoid antigen by rapid
RT amplification of cDNA ends.";
RL J. Invest. Dermatol. 101:244-246(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [MRNA] OF
RP 1-3386 (ISOFORM 4), SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Keratinocyte;
RX PubMed=11751855; DOI=10.1074/jbc.m109209200;
RA Okumura M., Yamakawa H., Ohara O., Owaribe K.;
RT "Novel alternative splicings of BPAG1 (bullous pemphigoid antigen 1)
RT including the domain structure closely related to MACF (microtubule actin
RT cross-linking factor).";
RL J. Biol. Chem. 277:6682-6687(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 8), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 4114-6568 (ISOFORM 1), AND VARIANT ALA-5138.
RC TISSUE=Brain, Hippocampus, Placenta, and Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC TISSUE=Duodenum;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-461 (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [MRNA] OF 1-46 (ISOFORM 6).
RC TISSUE=Fetal brain, and Retina;
RX PubMed=8575775; DOI=10.1006/geno.1995.9936;
RA Brown A., Dalpe G., Mathieu M., Kothary R.;
RT "Cloning and characterization of the neural isoforms of human dystonin.";
RL Genomics 29:777-780(1995).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-188 (ISOFORM 7), ALTERNATIVE SPLICING
RP (ISOFORMS 6 AND 7), FUNCTION OF ISOFORMS 6 AND 7, AND SUBCELLULAR LOCATION
RP (ISOFORMS 6 AND 7).
RC TISSUE=Fetal brain;
RX PubMed=10428034; DOI=10.1016/s0092-8674(00)81017-x;
RA Yang Y., Bauer C., Strasser G., Wollman R., Julien J.P., Fuchs E.;
RT "Integrators of the cytoskeleton that stabilize microtubules.";
RL Cell 98:229-238(1999).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 208-308 (ISOFORM 1).
RC TISSUE=Pineal gland;
RA Geerts D., Sonnenberg A.;
RL Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 881-7570 (ISOFORM 3).
RC TISSUE=Keratinocyte;
RX PubMed=1712022; DOI=10.1016/s0021-9258(18)98934-9;
RA Tanaka T., Parry D.A.D., Klaus-Kovtun V., Steinert P.M., Stanley J.R.;
RT "Comparison of molecularly cloned bullous pemphigoid antigen to desmoplakin
RT I confirms that they define a new family of cell adhesion junction plaque
RT proteins.";
RL J. Biol. Chem. 266:12555-12559(1991).
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5947-7570 (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=9872452; DOI=10.1093/dnares/5.5.277;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XI. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 5:277-286(1998).
RN [12]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [13]
RP PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC TISSUE=Keratinocyte;
RX PubMed=2461961; DOI=10.1172/jci113803;
RA Stanley J.R., Tanaka T., Mueller S., Klaus-Kovtun V., Roop D.;
RT "Isolation of complementary DNA for bullous pemphigoid antigen by use of
RT patients' autoantibodies.";
RL J. Clin. Invest. 82:1864-1870(1988).
RN [14]
RP PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RX PubMed=2090522; DOI=10.1111/j.1432-0436.1990.tb00475.x;
RA Owaribe K., Kartenbeck J., Stumpp S., Magin T.M., Krieg T., Diaz L.A.,
RA Franke W.W.;
RT "The hemidesmosomal plaque. I. Characterization of a major constituent
RT protein as a differentiation marker for certain forms of epithelia.";
RL Differentiation 45:207-220(1990).
RN [15]
RP PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING
RP (ISOFORM 3).
RX PubMed=8010969; DOI=10.1042/bj3000851;
RA Hopkinson S.B., Jones J.C.;
RT "Identification of a second protein product of the gene encoding a human
RT epidermal autoantigen.";
RL Biochem. J. 300:851-857(1994).
RN [16]
RP ALTERNATIVE SPLICING (ISOFORMS 3 AND 6), AND TISSUE SPECIFICITY.
RX PubMed=8752219; DOI=10.1016/s0092-8674(00)80138-5;
RA Yang Y., Dowling J., Yu Q.C., Kouklis P., Cleveland D.W., Fuchs E.;
RT "An essential cytoskeletal linker protein connecting actin microfilaments
RT to intermediate filaments.";
RL Cell 86:655-665(1996).
RN [17]
RP ALTERNATIVE SPLICING (ISOFORM 3), AND INTERACTION WITH COL17A1 AND ITGB4.
RX PubMed=10637308; DOI=10.1091/mbc.11.1.277;
RA Hopkinson S.B., Jones J.C.;
RT "The N terminus of the transmembrane protein BP180 interacts with the N-
RT terminal domain of BP230, thereby mediating keratin cytoskeleton anchorage
RT to the cell surface at the site of the hemidesmosome.";
RL Mol. Biol. Cell 11:277-286(2000).
RN [18]
RP DOMAINS.
RX PubMed=8621649; DOI=10.1074/jbc.271.16.9716;
RA Tang H.-Y., Chaffotte A.-F., Thacher S.M.;
RT "Structural analysis of the predicted coiled-coil rod domain of the
RT cytoplasmic bullous pemphigoid antigen (BPAG1). Empirical localization of
RT the N-terminal globular domain-rod boundary.";
RL J. Biol. Chem. 271:9716-9722(1996).
RN [19]
RP INTERACTION WITH ITGB4 AND ERBIN.
RX PubMed=11375975; DOI=10.1074/jbc.m011005200;
RA Favre B., Fontao L., Koster J., Shafaatian R., Jaunin F., Saurat J.-H.,
RA Sonnenberg A., Borradori L.;
RT "The hemidesmosomal protein bullous pemphigoid antigen 1 and the integrin
RT beta 4 subunit bind to ERBIN. Molecular cloning of multiple alternative
RT splice variants of ERBIN and analysis of their tissue expression.";
RL J. Biol. Chem. 276:32427-32436(2001).
RN [20]
RP ALTERNATIVE SPLICING (ISOFORM 9).
RX PubMed=14581450; DOI=10.1083/jcb.200306075;
RA Liu J.J., Ding J., Kowal A.S., Nardine T., Allen E., Delcroix J.D., Wu C.,
RA Mobley W., Fuchs E., Yang Y.;
RT "BPAG1n4 is essential for retrograde axonal transport in sensory neurons.";
RL J. Cell Biol. 163:223-229(2003).
RN [21]
RP ALTERNATIVE SPLICING (ISOFORM 3), FUNCTION OF ISOFORM 3, INTERACTION WITH
RP COL17A1 AND ITGB4, AND SUBCELLULAR LOCATION (ISOFORM 3).
RX PubMed=12482924; DOI=10.1242/jcs.00241;
RA Koster J., Geerts D., Favre B., Borradori L., Sonnenberg A.;
RT "Analysis of the interactions between BP180, BP230, plectin and the
RT integrin alpha6beta4 important for hemidesmosome assembly.";
RL J. Cell Sci. 116:387-399(2003).
RN [22]
RP ALTERNATIVE SPLICING (ISOFORM 3), ASSOCIATION WITH KERATIN FILAMENTS, AND
RP SUBCELLULAR LOCATION (ISOFORM 3).
RX PubMed=12802069; DOI=10.1091/mbc.e02-08-0548;
RA Fontao L., Favre B., Riou S., Geerts D., Jaunin F., Saurat J.H.,
RA Green K.J., Sonnenberg A., Borradori L.;
RT "Interaction of the bullous pemphigoid antigen 1 (BP230) and desmoplakin
RT with intermediate filaments is mediated by distinct sequences within their
RT COOH terminus.";
RL Mol. Biol. Cell 14:1978-1992(2003).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7432, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [24]
RP ALTERNATIVE SPLICING (ISOFORM 3), FUNCTION OF ISOFORM 3, AND SUBCELLULAR
RP LOCATION (ISOFORM 3).
RX PubMed=19403692; DOI=10.1091/mbc.e09-01-0051;
RA Hamill K.J., Hopkinson S.B., DeBiase P., Jones J.C.;
RT "BPAG1e maintains keratinocyte polarity through beta4 integrin-mediated
RT modulation of Rac1 and cofilin activities.";
RL Mol. Biol. Cell 20:2954-2962(2009).
RN [25]
RP ALTERNATIVE SPLICING (ISOFORM 1), HOMODIMERIZATION, INTERACTION WITH ACTN2
RP AND PLEC, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=19932097; DOI=10.1016/j.yexcr.2009.11.010;
RA Steiner-Champliaud M.F., Schneider Y., Favre B., Paulhe F.,
RA Praetzel-Wunder S., Faulkner G., Konieczny P., Raith M., Wiche G.,
RA Adebola A., Liem R.K., Langbein L., Sonnenberg A., Fontao L., Borradori L.;
RT "BPAG1 isoform-b: complex distribution pattern in striated and heart muscle
RT and association with plectin and alpha-actinin.";
RL Exp. Cell Res. 316:297-313(2010).
RN [26]
RP INVOLVEMENT IN EBSB2.
RX PubMed=20164846; DOI=10.1038/jid.2010.19;
RA Groves R.W., Liu L., Dopping-Hepenstal P.J., Markus H.S., Lovell P.A.,
RA Ozoemena L., Lai-Cheong J.E., Gawler J., Owaribe K., Hashimoto T.,
RA Mellerio J.E., Mee J.B., McGrath J.A.;
RT "A homozygous nonsense mutation within the dystonin gene coding for the
RT coiled-coil domain of the epithelial isoform of BPAG1 underlies a new
RT subtype of autosomal recessive epidermolysis bullosa simplex.";
RL J. Invest. Dermatol. 130:1551-1557(2010).
RN [27]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [28]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2919, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [29]
RP INVOLVEMENT IN HSAN6.
RX PubMed=22522446; DOI=10.1002/ana.23524;
RA Edvardson S., Cinnamon Y., Jalas C., Shaag A., Maayan C., Axelrod F.B.,
RA Elpeleg O.;
RT "Hereditary sensory autonomic neuropathy caused by a mutation in
RT dystonin.";
RL Ann. Neurol. 71:569-572(2012).
RN [30]
RP INVOLVEMENT IN EBSB2.
RX PubMed=22113475; DOI=10.1038/jid.2011.379;
RA Liu L., Dopping-Hepenstal P.J., Lovell P.A., Michael M., Horn H., Fong K.,
RA Lai-Cheong J.E., Mellerio J.E., Parsons M., McGrath J.A.;
RT "Autosomal recessive epidermolysis bullosa simplex due to loss of BPAG1-e
RT expression.";
RL J. Invest. Dermatol. 132:742-744(2012).
RN [31]
RP INTERACTION WITH TMIGD2.
RX PubMed=22419821; DOI=10.1091/mbc.e11-11-0934;
RA Rahimi N., Rezazadeh K., Mahoney J.E., Hartsough E., Meyer R.D.;
RT "Identification of IGPR-1 as a novel adhesion molecule involved in
RT angiogenesis.";
RL Mol. Biol. Cell 23:1646-1656(2012).
RN [32]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3968, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-135 (ISOFORM 6), AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [33]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3968, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-184 (ISOFORM 8), AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [34]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 7541-7570 IN COMPLEX WITH MAPRE1,
RP DOMAIN MICROTUBULE TIP LOCALIZATION SIGNAL, AND MUTAGENESIS OF LYS-7548;
RP SER-7550; ILE-7552; PRO-7553 AND 7557-ARG-LYS-7558.
RX PubMed=19632184; DOI=10.1016/j.cell.2009.04.065;
RA Honnappa S., Gouveia S.M., Weisbrich A., Damberger F.F., Bhavesh N.S.,
RA Jawhari H., Grigoriev I., van Rijssel F.J., Buey R.M., Lawera A.,
RA Jelesarov I., Winkler F.K., Wuthrich K., Akhmanova A., Steinmetz M.O.;
RT "An EB1-binding motif acts as a microtubule tip localization signal.";
RL Cell 138:366-376(2009).
CC -!- FUNCTION: Cytoskeletal linker protein. Acts as an integrator of
CC intermediate filaments, actin and microtubule cytoskeleton networks.
CC Required for anchoring either intermediate filaments to the actin
CC cytoskeleton in neural and muscle cells or keratin-containing
CC intermediate filaments to hemidesmosomes in epithelial cells. The
CC proteins may self-aggregate to form filaments or a two-dimensional
CC mesh. Regulates the organization and stability of the microtubule
CC network of sensory neurons to allow axonal transport. Mediates docking
CC of the dynein/dynactin motor complex to vesicle cargos for retrograde
CC axonal transport through its interaction with TMEM108 and DCTN1 (By
CC similarity). {ECO:0000250|UniProtKB:Q91ZU6}.
CC -!- FUNCTION: [Isoform 3]: Plays a structural role in the assembly of
CC hemidesmosomes of epithelial cells; anchors keratin-containing
CC intermediate filaments to the inner plaque of hemidesmosomes. Required
CC for the regulation of keratinocyte polarity and motility; mediates
CC integrin ITGB4 regulation of RAC1 activity.
CC -!- FUNCTION: [Isoform 6]: Required for bundling actin filaments around the
CC nucleus. {ECO:0000250, ECO:0000269|PubMed:10428034,
CC ECO:0000269|PubMed:12482924, ECO:0000269|PubMed:19403692}.
CC -!- FUNCTION: [Isoform 7]: Regulates the organization and stability of the
CC microtubule network of sensory neurons to allow axonal transport.
CC -!- SUBUNIT: Homodimer. Isoform 1 interacts (via N-terminus) with PLEC (via
CC N-terminus). Interacts with the neuronal intermediate filament protein,
CC PRPH. Interacts with DES. Interacts with SYNE3 (By similarity). Isoform
CC 1 and isoform 6 can homodimerize (via N-terminus). Isoform 1 interacts
CC (via N-terminus) with ACTN2. Isoform 1 interacts (via N-terminus) with
CC PLEC (via N-terminus). Isoform 3 interacts (via N-terminus) with
CC COL17A1 (via cytoplasmic region). Isoform 3 interacts (via N-terminus)
CC with ITGB4 isoform beta-4a (via cytoplasmic region). Isoform 3
CC interacts (via N-terminus) with ERBIN (via C-terminus). Isoform 3
CC associates (via C-terminal) with KRT5-KRT14 (via rod region)
CC intermediate filaments of keratins. Interacts with MAPRE1; probably
CC required for targeting to the growing microtubule plus ends. Interacts
CC with TMIGD2. Isoform 9 interacts with TMEM108 (By similarity).
CC {ECO:0000250|UniProtKB:Q91ZU6, ECO:0000269|PubMed:10637308,
CC ECO:0000269|PubMed:11375975, ECO:0000269|PubMed:12482924,
CC ECO:0000269|PubMed:19632184, ECO:0000269|PubMed:19932097,
CC ECO:0000269|PubMed:22419821}.
CC -!- INTERACTION:
CC Q03001; Q9UKG1: APPL1; NbExp=3; IntAct=EBI-310758, EBI-741243;
CC Q03001; Q9NRI5: DISC1; NbExp=4; IntAct=EBI-310758, EBI-529989;
CC Q03001; Q15691: MAPRE1; NbExp=4; IntAct=EBI-310758, EBI-1004115;
CC Q03001; Q61166: Mapre1; Xeno; NbExp=4; IntAct=EBI-310758, EBI-2027055;
CC Q03001; PRO_0000037946 [P29991]; Xeno; NbExp=4; IntAct=EBI-310758, EBI-8826488;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:11751855, ECO:0000269|PubMed:19932097}. Cytoplasm,
CC cytoskeleton, stress fiber {ECO:0000250|UniProtKB:Q91ZU6}. Cell
CC projection, axon {ECO:0000250|UniProtKB:Q91ZU6}. Note=Associates with
CC intermediate filaments, actin and microtubule cytoskeletons. Localizes
CC to actin stress fibers and to actin-rich ruffling at the cortex of
CC cells (By similarity). Associated at the growing distal tip of
CC microtubules. {ECO:0000250|UniProtKB:Q91ZU6}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm, cytoskeleton
CC {ECO:0000250}. Cytoplasm, myofibril, sarcomere, Z line. Cytoplasm,
CC myofibril, sarcomere, H zone {ECO:0000250}. Note=Localizes to
CC microtubules and actin microfilaments throughout the cytoplasm and at
CC focal contact attachments at the plasma membrane. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm, cytoskeleton
CC {ECO:0000250}. Note=Colocalizes both cortical and cytoplasmic actin
CC filaments. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm, cytoskeleton. Cell
CC junction, hemidesmosome. Note=Localizes to actin and intermediate
CC filaments cytoskeletons (By similarity). Colocalizes with the epidermal
CC KRT5-KRT14 intermediate filaments network of keratins. Colocalizes with
CC ITGB4 at the leading edge of migrating keratinocytes. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform 6]: Nucleus
CC {ECO:0000250|UniProtKB:Q91ZU6}. Nucleus envelope
CC {ECO:0000269|PubMed:10428034}. Membrane {ECO:0000269|PubMed:10428034};
CC Single-pass membrane protein {ECO:0000269|PubMed:10428034}. Endoplasmic
CC reticulum membrane {ECO:0000250|UniProtKB:Q91ZU6}; Single-pass membrane
CC protein {ECO:0000250|UniProtKB:Q91ZU6}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:10428034}. Cytoplasm, cytoskeleton, stress fiber
CC {ECO:0000250|UniProtKB:Q91ZU6}. Note=Localizes to actin and
CC intermediate filaments cytoskeletons. Localizes to central actin stress
CC fibers around the nucleus and is excluded form focal contact sites in
CC myoblast cells. Translocates to the nucleus (By similarity). Associates
CC with actin cytoskeleton in sensory neurons.
CC {ECO:0000250|UniProtKB:Q91ZU6}.
CC -!- SUBCELLULAR LOCATION: [Isoform 7]: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:10428034}. Cell projection, axon
CC {ECO:0000269|PubMed:10428034}. Membrane {ECO:0000269|PubMed:10428034}.
CC Note=Associates with axonal microtubules and intermediate filaments,
CC but not with actin cytoskeleton, in sensory neurons.
CC -!- SUBCELLULAR LOCATION: [Isoform 8]: Cytoplasm, cytoskeleton
CC {ECO:0000250}. Cytoplasm, cell cortex {ECO:0000250}. Cell membrane
CC {ECO:0000250}; Lipid-anchor {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=9;
CC Name=1; Synonyms=BPAG1-b;
CC IsoId=Q03001-7; Sequence=Displayed;
CC Name=2; Synonyms=BPAG1eA, Dystonin-1, eA;
CC IsoId=Q03001-8; Sequence=VSP_041525, VSP_041535, VSP_041539,
CC VSP_041540;
CC Name=3; Synonyms=BPAG1e, eBPAG1;
CC IsoId=Q03001-3; Sequence=VSP_041525, VSP_041533, VSP_041534;
CC Name=4; Synonyms=BPAG1eA, eB;
CC IsoId=Q03001-9; Sequence=VSP_041525, VSP_041536;
CC Name=5;
CC IsoId=Q03001-10; Sequence=VSP_041524, VSP_041537, VSP_041538;
CC Name=6; Synonyms=BPAG1n1, BPAG1n2, Dystonin-2;
CC IsoId=Q03001-11; Sequence=VSP_041528, VSP_041529;
CC Name=7; Synonyms=BPAG1n3;
CC IsoId=Q03001-12; Sequence=VSP_041526, VSP_041530;
CC Name=8;
CC IsoId=Q03001-13; Sequence=VSP_041527, VSP_041531, VSP_041532;
CC Name=9; Synonyms=BPAG1-a {ECO:0000303|PubMed:14581450}, BAPG1n4
CC {ECO:0000303|PubMed:14581450};
CC IsoId=Q03001-14; Sequence=VSP_058835, VSP_058836;
CC -!- TISSUE SPECIFICITY: Isoform 1 is expressed in myoblasts (at protein
CC level). Isoform 3 is expressed in the skin. Isoform 6 is expressed in
CC the brain. Highly expressed in skeletal muscle and cultured
CC keratinocytes. {ECO:0000269|PubMed:11751855,
CC ECO:0000269|PubMed:19932097, ECO:0000269|PubMed:8752219}.
CC -!- DOMAIN: Its association with epidermal and simple keratins is dependent
CC on the tertiary structure induced by heterodimerization of these
CC intermediate filaments proteins and most likely involves recognition
CC sites located in the rod domain of these keratins.
CC -!- DOMAIN: The microtubule tip localization signal (MtLS) motif; mediates
CC interaction with MAPRE1 and targeting to the growing microtubule plus
CC ends.
CC -!- DISEASE: Neuropathy, hereditary sensory and autonomic, 6 (HSAN6)
CC [MIM:614653]: A form of hereditary sensory and autonomic neuropathy, a
CC genetically and clinically heterogeneous group of disorders
CC characterized by degeneration of dorsal root and autonomic ganglion
CC cells, and by sensory and/or autonomic abnormalities. HSAN6 is a severe
CC autosomal recessive disorder characterized by neonatal hypotonia,
CC respiratory and feeding difficulties, lack of psychomotor development,
CC and autonomic abnormalities including labile cardiovascular function,
CC lack of corneal reflexes leading to corneal scarring, areflexia, and
CC absent axonal flare response after intradermal histamine injection.
CC {ECO:0000269|PubMed:22522446}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Epidermolysis bullosa simplex, autosomal recessive 2 (EBSB2)
CC [MIM:615425]: A form of epidermolysis bullosa, a dermatologic disorder
CC characterized by localized blistering on the dorsal, lateral and
CC plantar surfaces of the feet. EBSB2 is characterized by trauma-induced
CC blistering mainly occurring on the feet and ankles. Ultrastructural
CC analysis of skin biopsy shows abnormal hemidesmosomes with poorly
CC formed inner plaques. {ECO:0000269|PubMed:20164846,
CC ECO:0000269|PubMed:22113475}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: [Isoform 4]: Incomplete sequence. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 5]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 6]: Incomplete sequence. Transmembrane protein
CC (helical transmembrane domain from amino acid 18 to 38). {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 7]: Incomplete sequence. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 8]: Probably myristoylated on Gly-2. Probably
CC S-palmitoylated on Cys-5 and Cys-7. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA35538.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the C-terminal part.; Evidence={ECO:0000305};
CC Sequence=AAA57185.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAH16991.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB70870.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC04449.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC04848.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC -!- SEQUENCE CAUTION: [Isoform 6]:
CC Sequence=AAC50244.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M69225; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; L11690; AAA52288.1; -; mRNA.
DR EMBL; AF400226; AAL62061.1; -; mRNA.
DR EMBL; AF400227; AAL62062.1; -; mRNA.
DR EMBL; AK055189; BAB70870.1; ALT_INIT; mRNA.
DR EMBL; AK094883; BAC04449.1; ALT_INIT; mRNA.
DR EMBL; AK096713; BAC04848.1; ALT_INIT; mRNA.
DR EMBL; AK295864; BAH12207.1; -; mRNA.
DR EMBL; AL049215; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL096710; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL590005; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL137008; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL512422; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL512448; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL590037; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KF458172; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC016991; AAH16991.1; ALT_INIT; mRNA.
DR EMBL; U31850; AAC50243.1; -; mRNA.
DR EMBL; U31851; AAC50244.1; ALT_FRAME; mRNA.
DR EMBL; AF165191; AAD49334.1; -; mRNA.
DR EMBL; AY032900; AAK63130.1; -; mRNA.
DR EMBL; AY032901; AAK63131.1; -; mRNA.
DR EMBL; M63618; AAA35606.1; -; mRNA.
DR EMBL; AB018271; BAA34448.2; -; mRNA.
DR EMBL; M22942; AAA35538.1; ALT_SEQ; mRNA.
DR EMBL; X58677; CAA41528.1; -; mRNA.
DR EMBL; U04850; AAA57184.1; -; Genomic_DNA.
DR EMBL; U04850; AAA57185.1; ALT_SEQ; Genomic_DNA.
DR CCDS; CCDS47443.1; -. [Q03001-8]
DR CCDS; CCDS4959.1; -. [Q03001-3]
DR PIR; I56317; A40937.
DR RefSeq; NP_001138241.1; NM_001144769.2.
DR RefSeq; NP_001138242.1; NM_001144770.1.
DR RefSeq; NP_001714.1; NM_001723.5. [Q03001-3]
DR RefSeq; NP_056363.2; NM_015548.4. [Q03001-8]
DR RefSeq; NP_899236.1; NM_183380.3.
DR RefSeq; XP_016866713.1; XM_017011224.1.
DR PDB; 3GJO; X-ray; 2.50 A; E/F/G/H=7541-7570.
DR PDBsum; 3GJO; -.
DR SMR; Q03001; -.
DR BioGRID; 107135; 196.
DR DIP; DIP-33131N; -.
DR ELM; Q03001; -.
DR IntAct; Q03001; 87.
DR MINT; Q03001; -.
DR STRING; 9606.ENSP00000307959; -.
DR GlyGen; Q03001; 6 sites, 1 O-linked glycan (6 sites).
DR iPTMnet; Q03001; -.
DR MetOSite; Q03001; -.
DR PhosphoSitePlus; Q03001; -.
DR SwissPalm; Q03001; -.
DR BioMuta; DST; -.
DR DMDM; 294862529; -.
DR EPD; Q03001; -.
DR jPOST; Q03001; -.
DR MassIVE; Q03001; -.
DR MaxQB; Q03001; -.
DR PaxDb; Q03001; -.
DR PeptideAtlas; Q03001; -.
DR PRIDE; Q03001; -.
DR ProteomicsDB; 17852; -.
DR ProteomicsDB; 58151; -. [Q03001-7]
DR ProteomicsDB; 58152; -. [Q03001-10]
DR ProteomicsDB; 58153; -. [Q03001-11]
DR ProteomicsDB; 58154; -. [Q03001-12]
DR ProteomicsDB; 58155; -. [Q03001-13]
DR ProteomicsDB; 58156; -. [Q03001-3]
DR ProteomicsDB; 58157; -. [Q03001-8]
DR ProteomicsDB; 58158; -. [Q03001-9]
DR Antibodypedia; 31066; 184 antibodies from 22 providers.
DR DNASU; 667; -.
DR Ensembl; ENST00000244364.10; ENSP00000244364.6; ENSG00000151914.22. [Q03001-8]
DR Ensembl; ENST00000370765.11; ENSP00000359801.6; ENSG00000151914.22. [Q03001-3]
DR Ensembl; ENST00000370788.6; ENSP00000359824.2; ENSG00000151914.22. [Q03001-14]
DR Ensembl; ENST00000439203.5; ENSP00000404924.1; ENSG00000151914.22. [Q03001-9]
DR GeneID; 667; -.
DR KEGG; hsa:667; -.
DR UCSC; uc003pcy.5; human. [Q03001-7]
DR CTD; 667; -.
DR DisGeNET; 667; -.
DR GeneCards; DST; -.
DR HGNC; HGNC:1090; DST.
DR HPA; ENSG00000151914; Low tissue specificity.
DR MalaCards; DST; -.
DR MIM; 113810; gene.
DR MIM; 614653; phenotype.
DR MIM; 615425; phenotype.
DR neXtProt; NX_Q03001; -.
DR OpenTargets; ENSG00000151914; -.
DR Orphanet; 412181; Epidermolysis bullosa simplex due to BP230 deficiency.
DR Orphanet; 314381; Hereditary sensory and autonomic neuropathy type 6.
DR PharmGKB; PA25399; -.
DR VEuPathDB; HostDB:ENSG00000151914; -.
DR eggNOG; KOG0516; Eukaryota.
DR eggNOG; KOG0517; Eukaryota.
DR GeneTree; ENSGT00940000155008; -.
DR HOGENOM; CLU_000015_3_0_1; -.
DR InParanoid; Q03001; -.
DR OrthoDB; 24858at2759; -.
DR PhylomeDB; Q03001; -.
DR TreeFam; TF335163; -.
DR PathwayCommons; Q03001; -.
DR Reactome; R-HSA-2022090; Assembly of collagen fibrils and other multimeric structures. [Q03001-3]
DR Reactome; R-HSA-446107; Type I hemidesmosome assembly.
DR Reactome; R-HSA-9013420; RHOU GTPase cycle.
DR Reactome; R-HSA-9013424; RHOV GTPase cycle.
DR Reactome; R-HSA-9696264; RND3 GTPase cycle.
DR Reactome; R-HSA-9696270; RND2 GTPase cycle.
DR Reactome; R-HSA-9696273; RND1 GTPase cycle.
DR SignaLink; Q03001; -.
DR SIGNOR; Q03001; -.
DR BioGRID-ORCS; 667; 16 hits in 1086 CRISPR screens.
DR ChiTaRS; DST; human.
DR EvolutionaryTrace; Q03001; -.
DR GeneWiki; Dystonin; -.
DR GenomeRNAi; 667; -.
DR Pharos; Q03001; Tbio.
DR PRO; PR:Q03001; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q03001; protein.
DR Bgee; ENSG00000151914; Expressed in corpus callosum and 205 other tissues.
DR ExpressionAtlas; Q03001; baseline and differential.
DR Genevisible; Q03001; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:UniProtKB.
DR GO; GO:0030424; C:axon; IDA:UniProtKB.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0009925; C:basal plasma membrane; NAS:UniProtKB.
DR GO; GO:0005604; C:basement membrane; TAS:ProtInc.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0031252; C:cell leading edge; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0031673; C:H zone; IEA:UniProtKB-SubCell.
DR GO; GO:0030056; C:hemidesmosome; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005882; C:intermediate filament; IEA:UniProtKB-KW.
DR GO; GO:0045111; C:intermediate filament cytoskeleton; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:UniProtKB.
DR GO; GO:0035371; C:microtubule plus-end; IDA:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0030018; C:Z disc; IDA:UniProtKB.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005178; F:integrin binding; IPI:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0051010; F:microtubule plus-end binding; IDA:UniProtKB.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0005198; F:structural molecule activity; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0048870; P:cell motility; IMP:UniProtKB.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IBA:GO_Central.
DR GO; GO:0007010; P:cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:0031581; P:hemidesmosome assembly; IDA:UniProtKB.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; NAS:UniProtKB.
DR GO; GO:0045104; P:intermediate filament cytoskeleton organization; IEP:UniProtKB.
DR GO; GO:0030011; P:maintenance of cell polarity; IMP:UniProtKB.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IDA:UniProtKB.
DR GO; GO:0009611; P:response to wounding; IDA:UniProtKB.
DR GO; GO:0008090; P:retrograde axonal transport; ISS:UniProtKB.
DR GO; GO:0042060; P:wound healing; IBA:GO_Central.
DR CDD; cd00014; CH; 2.
DR CDD; cd00051; EFh; 1.
DR CDD; cd00176; SPEC; 17.
DR Gene3D; 1.10.418.10; -; 2.
DR Gene3D; 3.30.920.20; -; 1.
DR Gene3D; 3.90.1290.10; -; 3.
DR InterPro; IPR001589; Actinin_actin-bd_CS.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR041615; Desmoplakin_SH3.
DR InterPro; IPR041573; Desmoplakin_Spectrin-like.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR003108; GAR_dom.
DR InterPro; IPR036534; GAR_dom_sf.
DR InterPro; IPR043197; Plakin.
DR InterPro; IPR035915; Plakin_repeat_sf.
DR InterPro; IPR001101; Plectin_repeat.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR018159; Spectrin/alpha-actinin.
DR InterPro; IPR002017; Spectrin_repeat.
DR PANTHER; PTHR23169; PTHR23169; 9.
DR Pfam; PF00307; CH; 2.
DR Pfam; PF13499; EF-hand_7; 1.
DR Pfam; PF02187; GAS2; 1.
DR Pfam; PF00681; Plectin; 1.
DR Pfam; PF17902; SH3_10; 1.
DR Pfam; PF00435; Spectrin; 20.
DR Pfam; PF18373; Spectrin_like; 1.
DR SMART; SM00033; CH; 2.
DR SMART; SM00054; EFh; 2.
DR SMART; SM00243; GAS2; 1.
DR SMART; SM00250; PLEC; 8.
DR SMART; SM00150; SPEC; 32.
DR SUPFAM; SSF143575; SSF143575; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF47576; SSF47576; 1.
DR SUPFAM; SSF75399; SSF75399; 2.
DR PROSITE; PS00019; ACTININ_1; 1.
DR PROSITE; PS00020; ACTININ_2; 1.
DR PROSITE; PS50021; CH; 2.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS51460; GAR; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Alternative promoter usage;
KW Alternative splicing; Calcium; Cell adhesion; Cell junction; Cell membrane;
KW Cell projection; Coiled coil; Cytoplasm; Cytoskeleton;
KW Endoplasmic reticulum; Epidermolysis bullosa; Intermediate filament;
KW Isopeptide bond; Lipoprotein; Membrane; Metal-binding; Microtubule;
KW Muscle protein; Neurodegeneration; Neuropathy; Nucleus; Palmitate;
KW Phosphoprotein; Reference proteome; Repeat; SH3 domain; Transmembrane;
KW Ubl conjugation.
FT CHAIN 1..7570
FT /note="Dystonin"
FT /id="PRO_0000078138"
FT DOMAIN 35..138
FT /note="Calponin-homology (CH) 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 151..255
FT /note="Calponin-homology (CH) 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REPEAT 602..699
FT /note="Spectrin 1"
FT REPEAT 701..802
FT /note="Spectrin 2"
FT DOMAIN 887..944
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REPEAT 1293..1422
FT /note="Spectrin 3"
FT REPEAT 1440..1540
FT /note="Spectrin 4"
FT REPEAT 1584..1626
FT /note="Plectin 1"
FT REPEAT 1660..1703
FT /note="Plectin 2"
FT REPEAT 1774..1817
FT /note="Plectin 3"
FT REPEAT 1818..1855
FT /note="Plectin 4"
FT REPEAT 1856..1891
FT /note="Plectin 5"
FT REPEAT 3395..3501
FT /note="Spectrin 5"
FT REPEAT 3643..3752
FT /note="Spectrin 6"
FT REPEAT 3926..4040
FT /note="Spectrin 7"
FT REPEAT 4047..4153
FT /note="Spectrin 8"
FT REPEAT 4160..4259
FT /note="Spectrin 9"
FT REPEAT 4269..4368
FT /note="Spectrin 10"
FT REPEAT 4516..4621
FT /note="Spectrin 11"
FT REPEAT 4628..4732
FT /note="Spectrin 12"
FT REPEAT 4742..4842
FT /note="Spectrin 13"
FT REPEAT 4849..4951
FT /note="Spectrin 14"
FT REPEAT 4958..5058
FT /note="Spectrin 15"
FT REPEAT 5068..5167
FT /note="Spectrin 16"
FT REPEAT 5174..5277
FT /note="Spectrin 17"
FT REPEAT 5284..5388
FT /note="Spectrin 18"
FT REPEAT 5395..5497
FT /note="Spectrin 19"
FT REPEAT 5504..5715
FT /note="Spectrin 20"
FT REPEAT 5831..5933
FT /note="Spectrin 21"
FT REPEAT 5941..6041
FT /note="Spectrin 22"
FT REPEAT 6048..6154
FT /note="Spectrin 23"
FT REPEAT 6161..6263
FT /note="Spectrin 24"
FT REPEAT 6270..6373
FT /note="Spectrin 25"
FT REPEAT 6380..6482
FT /note="Spectrin 26"
FT REPEAT 6489..6591
FT /note="Spectrin 27"
FT REPEAT 6598..6700
FT /note="Spectrin 28"
FT REPEAT 6707..6810
FT /note="Spectrin 29"
FT REPEAT 6817..6918
FT /note="Spectrin 30"
FT REPEAT 6925..7027
FT /note="Spectrin 31"
FT REPEAT 7037..7167
FT /note="Spectrin 32"
FT DOMAIN 7197..7232
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 7233..7268
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 7273..7351
FT /note="GAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00792"
FT REGION 35..252
FT /note="Actin-binding"
FT REGION 2317..2346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2383..2441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2585..2616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3190..3221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 7358..7379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 7395..7452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 7481..7570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1383..1389
FT /note="Nuclear localization signal; in isoform 6"
FT /evidence="ECO:0000250"
FT MOTIF 7550..7553
FT /note="Microtubule tip localization signal"
FT COMPBIAS 2408..2431
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2587..2605
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3190..3214
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7361..7378
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7411..7446
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7515..7561
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 7210
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 7212
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 7214
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 7216
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 7221
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 7246
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 7248
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 7250
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 7252
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 7257
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 236
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91ZU6"
FT MOD_RES 237
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91ZU6"
FT MOD_RES 1382
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91ZU6"
FT MOD_RES 2229
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91ZU6"
FT MOD_RES 2919
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 3968
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 4749
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91ZU6"
FT MOD_RES 7432
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 7510
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91ZU6"
FT MOD_RES 7513
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91ZU6"
FT MOD_RES 7525
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91ZU6"
FT CROSSLNK 5470
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT VAR_SEQ 1..3896
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_041524"
FT VAR_SEQ 1..381
FT /note="MAGYLSPAAYLYVEEQEYLQAYEDVLERYKDERDKVQKKTFTKWINQHLMKV
FT RKHVNDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHRLQNVQIALDYLKRRQVKLV
FT NIRNDDITDGNPKLTLGLIWTIILHFQISDIHVTGESEDMSAKERLLLWTQQATEGYAG
FT IRCENFTTCWRDGKLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEKIGVIRLLD
FT PEDVDVSSPDEKSVITYVSSLYDAFPKVPEGGEGIGANDVEVKWIEYQNMVNYLIQWIR
FT HHVTTMSERTFPNNPVELKALYNQYLQFKETEIPPKETEKSKIKRLYKLLEIWIEFGRI
FT KLLQGYHPNDIEKEWGKLIIAMLEREKALRPEVE -> MHSSSYSYRSSDSVFSNTTST
FT RTSLDSNENLLLVHCGPTLINSCISFGSESFDGH (in isoform 2, isoform 3
FT and isoform 4)"
FT /evidence="ECO:0000303|PubMed:11751855,
FT ECO:0000303|PubMed:1712022, ECO:0000303|PubMed:1717441,
FT ECO:0000303|PubMed:8345227, ECO:0000303|PubMed:9872452"
FT /id="VSP_041525"
FT VAR_SEQ 1..138
FT /note="MAGYLSPAAYLYVEEQEYLQAYEDVLERYKDERDKVQKKTFTKWINQHLMKV
FT RKHVNDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHRLQNVQIALDYLKRRQVKLV
FT NIRNDDITDGNPKLTLGLIWTIILHFQ -> MQHSIFSLKKKRCHSLYTSMSSVSKDTD
FT GNE (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:10428034"
FT /id="VSP_041526"
FT VAR_SEQ 1..138
FT /note="MAGYLSPAAYLYVEEQEYLQAYEDVLERYKDERDKVQKKTFTKWINQHLMKV
FT RKHVNDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHRLQNVQIALDYLKRRQVKLV
FT NIRNDDITDGNPKLTLGLIWTIILHFQ -> MGNVCGCVRAEKEEQYVDPAKTPLNPEK
FT YSPGRKYFRRKPIKKTGGDKESVGANNENEGKKKSSSQPSKEQPAPLSRGLVQQESVTL
FT NSALGDGIQQKKTEVVADSVKQKLLPSAVSSWSDCVNTSPAKDSETEVKVSELDERISE
FT KDSTPYCAKRKKHLDDVNTSEITFQEKTDVFSFRKAASLSSIPSGIERSLEKGGFPEDP
FT PKSYSSIQEKQNTERFCPHATQHFQFKKKRCHSLYTSMSSVSKDTDGNE (in
FT isoform 8)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_041527"
FT VAR_SEQ 1..30
FT /note="MAGYLSPAAYLYVEEQEYLQAYEDVLERYK -> MIAAAFLVLLRPYSIQCA
FT LFLLLLLLGTIATIVFFCCWHRKLQKGRHPMKSVFSGRSRSRDAVLRSHHFRSEGFRAS
FT PRHLRRRVAAAAAARLEEVKPVVEVHHQSEQETSVRKRRIKKSSRVQPEFYHSVQGASI
FT RRPSSGNASYRCSMSSSADFSDEDDFSQKSGSASPAPGDTLPWNLPKHERSKRKIQGGS
FT VLDPAERAVLRIA (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:8575775"
FT /id="VSP_041528"
FT VAR_SEQ 47..7570
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:8575775"
FT /id="VSP_041529"
FT VAR_SEQ 189..7570
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:10428034"
FT /id="VSP_041530"
FT VAR_SEQ 778..789
FT /note="AYRAAMQTQWSW -> VKLESVMVLVEY (in isoform 8)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_041531"
FT VAR_SEQ 790..7570
FT /note="Missing (in isoform 8)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_041532"
FT VAR_SEQ 1433
FT /note="K -> IKRCKETSEHGAYSDLLQRQKATVLENSKLTGKISELERMVAELKKQ
FT KSRVEEELPKVREAAENELRKQQRNVEDISLQKIRAESEAKQYRRELETIVREKEAAER
FT ELERVRQLTIEAEAKRAAVEENLLNFRNQLEENTFTRRTLEDHLKRKDLSLNDLEQQKN
FT KLMEELRRKRDNEEELLKLIKQMEKDLAFQKQVAEKQLKEKQKIELEARRKITEIQYTC
FT RENALPVCPITQATSCRAVTGLQQEHDKQKAEELKQQVDELTAANRKAEQDMRELTYEL
FT NALQLEKTSSEEKARLLKDKLDETNNTLRCLKLELERKDQAEKGYSQQLRELGRQLNQT
FT TGKAEEAMQEASDLKKIKRNYQLELESLNHEKGKLQREVDRITRAHAVAEKNIQHLNSQ
FT IHSFRDEKELERLQICQRKSDHLKEQFEKSHEQLLQNIKAEKENNDKIQRLNEELEKSN
FT ECAEMLKQKVEELTRQNNETKLMMQRIQAESENIVLEKQTIQQRCEALKIQADGFKDQL
FT RSTNEHLHKQTKTEQDFQRKIKCLEEDLAKSQNLVSEFKQKCDQQNIIIQNTKKEVRNL
FT NAELNASKEEKRRGEQKVQLQQAQVQELNNRLKKVQDELHLKTIEEQMTHRKMVLFQEE
FT SGKFKQSAEEFRKKMEKLMESKVITENDISGIRLDFVSLQQENSRAQENAKLCETNIKE
FT LERQLQQYREQMQQGQHMEANHYQKCQKLEDELIAQKREVENLKQKMDQQIKEHEHQLV
FT LLQCEIQKKSTAKDCTFKPDFEMTVKECQHSGELSSRNTGHLHPTPRSPLLRWTQEPQP
FT LEEKWQHRVVEQIPKEVQFQPPGAPLEKEKSQQCYSEYFSQTSTELQITFDETNPITRL
FT SEIEKIRDQALNNSRPPVRYQDNACEMELVKVLTPLEIAKNKQYDMHTEVTTLKQEKNP
FT VPSAEEWMLEGCRASGGLKKGDFLKKGLEPETFQNFDGDHACSVRDDEFKFQGLRHTVT
FT ARQLVEAKLLDMRTIEQLRLGLKTVEEVQKTLNKFLTKATSIAGLYLESTKEKISFASA
FT AERIIIDKMVALAFLEAQAATGFIIDPISGQTYSVEDAVLKGVVDPEFRIRLLEAEKAA
FT VGYSYSSKTLSVFQAMENRMLDRQKGKHILEAQIASGGVIDPVRGIRVPPEIALQQGLL
FT NNAILQFLHEPSSNTRVFPNPNNKQALYYSELLRMCVFDVESQCFLFPFGERNISNLNV
FT KKTHRISVVDTKTGSELTVYEAFQRNLIEKSIYLELSGQQYQWKEAMFFESYGHSSHML
FT TDTKTGLHFNINEAIEQGTIDKALVKKYQEGLITLTELADSLLSRLVPKKDLHSPVAGY
FT WLTASGERISVLKASRRNLVDRITALRCLEAQVSTGGIIDPLTGKKYRVAEALHRGLVD
FT EGFAQQLRQCELVITGIGHPITNKMMSVVEAVNANIINKEMGIRCLEFQYLTGGLIEPQ
FT VHSRLSIEEALQVGIIDVLIATKLKDQKSYVRNIICPQTKRKLTYKEALEKADFDFHTG
FT LKLLEVSEPLMTGISSLYYSS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:1712022,
FT ECO:0000303|PubMed:1717441, ECO:0000303|PubMed:8345227"
FT /id="VSP_041533"
FT VAR_SEQ 1434..7570
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:1712022,
FT ECO:0000303|PubMed:1717441, ECO:0000303|PubMed:8345227"
FT /id="VSP_041534"
FT VAR_SEQ 1550..3635
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11751855,
FT ECO:0000303|PubMed:9872452"
FT /id="VSP_041535"
FT VAR_SEQ 1551..3636
FT /note="Missing (in isoform 9)"
FT /id="VSP_058835"
FT VAR_SEQ 3387..7570
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11751855"
FT /id="VSP_041536"
FT VAR_SEQ 4184..4200
FT /note="GQVPLNSTALQDIISKN -> DVGTGYCRSSEQYKCHE (in isoform
FT 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_041537"
FT VAR_SEQ 4201..7570
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_041538"
FT VAR_SEQ 5546..5654
FT /note="Missing (in isoform 9)"
FT /id="VSP_058836"
FT VAR_SEQ 7352..7375
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11751855,
FT ECO:0000303|PubMed:9872452"
FT /id="VSP_041539"
FT VAR_SEQ 7442
FT /note="K -> KILHPLTRNYGKPWLTNSKMSTPCKAAECSDFPVPSAE (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:11751855,
FT ECO:0000303|PubMed:9872452"
FT /id="VSP_041540"
FT VARIANT 1319
FT /note="N -> K (in dbSNP:rs35014998)"
FT /id="VAR_063045"
FT VARIANT 2332
FT /note="Q -> R (in dbSNP:rs16888053)"
FT /id="VAR_063046"
FT VARIANT 3720
FT /note="Q -> R (in dbSNP:rs4712138)"
FT /id="VAR_063047"
FT VARIANT 5138
FT /note="T -> A (in dbSNP:rs4715631)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_063048"
FT MUTAGEN 7548
FT /note="K->Q: Loss of interaction with MAPRE1 and
FT association with microtubule growing ends."
FT /evidence="ECO:0000269|PubMed:19632184"
FT MUTAGEN 7550
FT /note="S->A,N: Loss of association with microtubule growing
FT ends."
FT /evidence="ECO:0000269|PubMed:19632184"
FT MUTAGEN 7552
FT /note="I->N: Loss of interaction with MAPRE1 and
FT association with the growing microtubule plus ends; when
FT associated with N-7553."
FT /evidence="ECO:0000269|PubMed:19632184"
FT MUTAGEN 7553
FT /note="P->N: Loss of interaction with MAPRE1 and
FT association with the growing microtubule plus ends; when
FT associated with N-7552."
FT /evidence="ECO:0000269|PubMed:19632184"
FT MUTAGEN 7557
FT /note="R->N: Loss of interaction with MAPRE1 and
FT association with the growing microtubule plus ends."
FT MUTAGEN 7558
FT /note="K->N: Loss of interaction with MAPRE1 and
FT association with the growing microtubule plus ends."
FT CONFLICT 573
FT /note="P -> A (in Ref. 4; BAH12207)"
FT /evidence="ECO:0000305"
FT CONFLICT 1177
FT /note="V -> G (in Ref. 1; M69225 and 3; AAL62061/AAL62062)"
FT /evidence="ECO:0000305"
FT CONFLICT 1363
FT /note="K -> E (in Ref. 3; AAL62061)"
FT /evidence="ECO:0000305"
FT CONFLICT 4703
FT /note="R -> H (in Ref. 4; BAC04449)"
FT /evidence="ECO:0000305"
FT CONFLICT 4935
FT /note="N -> S (in Ref. 4; BAC04449)"
FT /evidence="ECO:0000305"
FT CONFLICT 5030
FT /note="E -> G (in Ref. 3; AAL62061)"
FT /evidence="ECO:0000305"
FT CONFLICT 5177
FT /note="Q -> R (in Ref. 3; AAL62061)"
FT /evidence="ECO:0000305"
FT CONFLICT 5225
FT /note="M -> I (in Ref. 4; BAB70870)"
FT /evidence="ECO:0000305"
FT CONFLICT 5299
FT /note="K -> R (in Ref. 3; AAL62061)"
FT /evidence="ECO:0000305"
FT CONFLICT 5823
FT /note="I -> V (in Ref. 3; AAL62061)"
FT /evidence="ECO:0000305"
FT CONFLICT 5882
FT /note="K -> R (in Ref. 3; AAL62061)"
FT /evidence="ECO:0000305"
FT CONFLICT 5986
FT /note="L -> S (in Ref. 3; AAL62061)"
FT /evidence="ECO:0000305"
FT CONFLICT 6080
FT /note="K -> E (in Ref. 4; BAC04848)"
FT /evidence="ECO:0000305"
FT CONFLICT 6186
FT /note="D -> G (in Ref. 3; AAL62061)"
FT /evidence="ECO:0000305"
FT CONFLICT 6440
FT /note="A -> G (in Ref. 3; AAL62061)"
FT /evidence="ECO:0000305"
FT MOD_RES Q03001-3:1565
FT /note="Phosphoserine"
FT /evidence="ECO:0000305"
FT CONFLICT Q03001-3:1644
FT /note="R -> T (in Ref. 1; M69225)"
FT /evidence="ECO:0000305"
FT CONFLICT Q03001-3:1943
FT /note="G -> R (in Ref. 13; CAA41528)"
FT /evidence="ECO:0000305"
FT CONFLICT Q03001-3:2364
FT /note="S -> T (in Ref. 1; M69225)"
FT /evidence="ECO:0000305"
FT CONFLICT Q03001-3:2495
FT /note="G -> V (in Ref. 1; M69225)"
FT /evidence="ECO:0000305"
FT CONFLICT Q03001-3:2543
FT /note="N -> K (in Ref. 1; M69225)"
FT /evidence="ECO:0000305"
FT CONFLICT Q03001-3:2621
FT /note="A -> P (in Ref. 1; M69225)"
FT /evidence="ECO:0000305"
FT MOD_RES Q03001-11:135
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CONFLICT Q03001-11:48
FT /note="P -> L (in Ref. 7; AAC50244)"
FT /evidence="ECO:0000305"
FT MOD_RES Q03001-13:184
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
SQ 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
