TADBP_HUMAN
ID TADBP_HUMAN Reviewed; 414 AA.
AC Q13148; A4GUK4; A4GUK5; A4GUK6; B2R629; B4DJ45; E2PU12; Q53H27; Q6FI92;
AC Q96DJ0;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 225.
DE RecName: Full=TAR DNA-binding protein 43 {ECO:0000303|PubMed:7745706};
DE Short=TDP-43 {ECO:0000303|PubMed:7745706};
GN Name=TARDBP {ECO:0000303|PubMed:18396105, ECO:0000312|HGNC:HGNC:11571};
GN Synonyms=TDP43 {ECO:0000303|PubMed:7745706};
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 1), AND CHARACTERIZATION.
RC TISSUE=Cervix carcinoma;
RX PubMed=7745706; DOI=10.1128/jvi.69.6.3584-3596.1995;
RA Ou S.-H.I., Wu F., Harrich D., Garcia-Martinez L.F., Gaynor R.B.;
RT "Cloning and characterization of a novel cellular protein, TDP-43, that
RT binds to human immunodeficiency virus type 1 TAR DNA sequence motifs.";
RL J. Virol. 69:3584-3596(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, AND
RP UBIQUITINATION.
RX PubMed=17481916; DOI=10.1016/j.mcn.2007.03.007;
RA Strong M.J., Volkening K., Hammond R., Yang W., Strong W.,
RA Leystra-Lantz C., Shoesmith C.;
RT "TDP43 is a human low molecular weight neurofilament (hNFL) mRNA-binding
RT protein.";
RL Mol. Cell. Neurosci. 35:320-327(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Substantia nigra;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lymph, and Testis;
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 [10]
RP PROTEIN SEQUENCE OF 122-136 AND 276-293, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Brain, and Cajal-Retzius cell;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (MAR-2007) to UniProtKB.
RN [11]
RP PROTEIN SEQUENCE OF 252-263; 276-293 AND 409-414, SUBCELLULAR LOCATION,
RP PHOSPHORYLATION, AND UBIQUITINATION.
RX PubMed=17023659; DOI=10.1126/science.1134108;
RA Neumann M., Sampathu D.M., Kwong L.K., Truax A.C., Micsenyi M.C.,
RA Chou T.T., Bruce J., Schuck T., Grossman M., Clark C.M., McCluskey L.F.,
RA Miller B.L., Masliah E., Mackenzie I.R., Feldman H., Feiden W.,
RA Kretzschmar H.A., Trojanowski J.Q., Lee V.M.-Y.;
RT "Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic
RT lateral sclerosis.";
RL Science 314:130-133(2006).
RN [12]
RP FUNCTION.
RX PubMed=11285240; DOI=10.1093/emboj/20.7.1774;
RA Buratti E., Doerk T., Zuccato E., Pagani F., Romano M., Baralle F.E.;
RT "Nuclear factor TDP-43 and SR proteins promote in vitro and in vivo CFTR
RT exon 9 skipping.";
RL EMBO J. 20:1774-1784(2001).
RN [13]
RP RNA-BINDING, AND MUTAGENESIS.
RX PubMed=11470789; DOI=10.1074/jbc.m104236200;
RA Buratti E., Baralle F.E.;
RT "Characterization and functional implications of the RNA binding properties
RT of nuclear factor TDP-43, a novel splicing regulator of CFTR exon 9.";
RL J. Biol. Chem. 276:36337-36343(2001).
RN [14]
RP SUBCELLULAR LOCATION, AND MOTIF.
RX PubMed=18957508; DOI=10.1242/jcs.038950;
RA Ayala Y.M., Zago P., D'Ambrogio A., Xu Y.F., Petrucelli L., Buratti E.,
RA Baralle F.E.;
RT "Structural determinants of the cellular localization and shuttling of TDP-
RT 43.";
RL J. Cell Sci. 121:3778-3785(2008).
RN [15]
RP INTERACTION WITH HNRNPA2B1.
RX PubMed=19429692; DOI=10.1093/nar/gkp342;
RA D'Ambrogio A., Buratti E., Stuani C., Guarnaccia C., Romano M., Ayala Y.M.,
RA Baralle F.E.;
RT "Functional mapping of the interaction between TDP-43 and hnRNP A2 in
RT vivo.";
RL Nucleic Acids Res. 37:4116-4126(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-292, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [17]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=19765185; DOI=10.1111/j.1471-4159.2009.06383.x;
RA Colombrita C., Zennaro E., Fallini C., Weber M., Sommacal A., Buratti E.,
RA Silani V., Ratti A.;
RT "TDP-43 is recruited to stress granules in conditions of oxidative
RT insult.";
RL J. Neurochem. 111:1051-1061(2009).
RN [18]
RP SUBUNIT.
RX PubMed=20043239; DOI=10.1007/s10571-009-9489-9;
RA Shiina Y., Arima K., Tabunoki H., Satoh J.;
RT "TDP-43 dimerizes in human cells in culture.";
RL Cell. Mol. Neurobiol. 30:641-652(2010).
RN [19]
RP INTERACTION WITH ATXN2, AND CHARACTERIZATION OF VARIANT ALS10 LYS-331.
RX PubMed=20740007; DOI=10.1038/nature09320;
RA Elden A.C., Kim H.J., Hart M.P., Chen-Plotkin A.S., Johnson B.S., Fang X.,
RA Armakola M., Geser F., Greene R., Lu M.M., Padmanabhan A., Clay-Falcone D.,
RA McCluskey L., Elman L., Juhr D., Gruber P.J., Rub U., Auburger G.,
RA Trojanowski J.Q., Lee V.M., Van Deerlin V.M., Bonini N.M., Gitler A.D.;
RT "Ataxin-2 intermediate-length polyglutamine expansions are associated with
RT increased risk for ALS.";
RL Nature 466:1069-1075(2010).
RN [20]
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 [21]
RP FUNCTION.
RX PubMed=21358640; DOI=10.1038/nn.2778;
RA Tollervey J.R., Curk T., Rogelj B., Briese M., Cereda M., Kayikci M.,
RA Koenig J., Hortobagyi T., Nishimura A.L., Zupunski V., Patani R.,
RA Chandran S., Rot G., Zupan B., Shaw C.E., Ule J.;
RT "Characterizing the RNA targets and position-dependent splicing regulation
RT by TDP-43.";
RL Nat. Neurosci. 14:452-458(2011).
RN [22]
RP FUNCTION, AND RNA-BINDING.
RX PubMed=23519609; DOI=10.1093/nar/gkt189;
RA Bhardwaj A., Myers M.P., Buratti E., Baralle F.E.;
RT "Characterizing TDP-43 interaction with its RNA targets.";
RL Nucleic Acids Res. 41:5062-5074(2013).
RN [23]
RP FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX PubMed=23398327; DOI=10.1111/jnc.12194;
RA Higashi S., Kabuta T., Nagai Y., Tsuchiya Y., Akiyama H., Wada K.;
RT "TDP-43 associates with stalled ribosomes and contributes to cell survival
RT during cellular stress.";
RL J. Neurochem. 126:288-300(2013).
RN [24]
RP INTERACTION WITH UBQLN2.
RX PubMed=23541532; DOI=10.1016/j.bbapap.2013.03.020;
RA Cassel J.A., Reitz A.B.;
RT "Ubiquilin-2 (UBQLN2) binds with high affinity to the C-terminal region of
RT TDP-43 and modulates TDP-43 levels in H4 cells: characterization of
RT inhibition by nucleic acids and 4-aminoquinolines.";
RL Biochim. Biophys. Acta 1834:964-971(2013).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183 AND SER-292, AND
RP IDENTIFICATION BY MASS 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 [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-292, AND IDENTIFICATION BY
RP MASS 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 [27]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-293, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [28]
RP INTERACTION WITH MATR3.
RX PubMed=24686783; DOI=10.1038/nn.3688;
RA Johnson J.O., Pioro E.P., Boehringer A., Chia R., Feit H., Renton A.E.,
RA Pliner H.A., Abramzon Y., Marangi G., Winborn B.J., Gibbs J.R., Nalls M.A.,
RA Morgan S., Shoai M., Hardy J., Pittman A., Orrell R.W., Malaspina A.,
RA Sidle K.C., Fratta P., Harms M.B., Baloh R.H., Pestronk A., Weihl C.C.,
RA Rogaeva E., Zinman L., Drory V.E., Borghero G., Mora G., Calvo A.,
RA Rothstein J.D., Drepper C., Sendtner M., Singleton A.B., Taylor J.P.,
RA Cookson M.R., Restagno G., Sabatelli M., Bowser R., Chio A., Traynor B.J.;
RT "Mutations in the matrin 3 gene cause familial amyotrophic lateral
RT sclerosis.";
RL Nat. Neurosci. 17:664-666(2014).
RN [29]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-181, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [30]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-102 AND LYS-181, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [31]
RP FUNCTION, AND INTERACTION WITH CRY2.
RX PubMed=27123980; DOI=10.1371/journal.pone.0154263;
RA Hirano A., Nakagawa T., Yoshitane H., Oyama M., Kozuka-Hata H.,
RA Lanjakornsiripan D., Fukada Y.;
RT "USP7 and TDP-43: pleiotropic regulation of cryptochrome protein stability
RT paces the oscillation of the mammalian circadian clock.";
RL PLoS ONE 11:E0154263-E0154263(2016).
RN [32]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-79; LYS-84; LYS-95; LYS-181 AND
RP LYS-263, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [33]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=28794432; DOI=10.1038/s41598-017-06953-y;
RA Izumikawa K., Nobe Y., Yoshikawa H., Ishikawa H., Miura Y., Nakayama H.,
RA Nonaka T., Hasegawa M., Egawa N., Inoue H., Nishikawa K., Yamano K.,
RA Simpson R.J., Taoka M., Yamauchi Y., Isobe T., Takahashi N.;
RT "TDP-43 stabilises the processing intermediates of mitochondrial
RT transcripts.";
RL Sci. Rep. 7:7709-7709(2017).
RN [34]
RP FUNCTION, AND INTERACTION WITH CNOT7.
RX PubMed=30520513; DOI=10.1002/1873-3468.13310;
RA Fukushima M., Hosoda N., Chifu K., Hoshino S.I.;
RT "TDP-43 accelerates deadenylation of target mRNAs by recruiting Caf1
RT deadenylase.";
RL FEBS Lett. 593:277-287(2019).
RN [35]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=30464263; DOI=10.1038/s41586-018-0665-2;
RA Vogler T.O., Wheeler J.R., Nguyen E.D., Hughes M.P., Britson K.A.,
RA Lester E., Rao B., Betta N.D., Whitney O.N., Ewachiw T.E., Gomes E.,
RA Shorter J., Lloyd T.E., Eisenberg D.S., Taylor J.P., Johnson A.M.,
RA Olwin B.B., Parker R.;
RT "TDP-43 and RNA form amyloid-like myo-granules in regenerating muscle.";
RL Nature 563:508-513(2018).
RN [36]
RP STRUCTURE BY NMR OF 96-267.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the RNA binding domains of TAR DNA-binding protein-
RT 43.";
RL Submitted (NOV-2005) to the PDB data bank.
RN [37]
RP STRUCTURE BY NMR OF 193-267.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of RRM domain in tar DNA-binding protein-43.";
RL Submitted (FEB-2009) to the PDB data bank.
RN [38]
RP STRUCTURE BY NMR OF 102-269, RNA-BINDING, AND FUNCTION.
RX PubMed=24240615; DOI=10.1038/nsmb.2698;
RA Lukavsky P.J., Daujotyte D., Tollervey J.R., Ule J., Stuani C., Buratti E.,
RA Baralle F.E., Damberger F.F., Allain F.H.;
RT "Molecular basis of UG-rich RNA recognition by the human splicing factor
RT TDP-43.";
RL Nat. Struct. Mol. Biol. 20:1443-1449(2013).
RN [39]
RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 103-179, FUNCTION, AND SUBUNIT.
RX PubMed=24464995; DOI=10.1093/nar/gkt1407;
RA Kuo P.H., Chiang C.H., Wang Y.T., Doudeva L.G., Yuan H.S.;
RT "The crystal structure of TDP-43 RRM1-DNA complex reveals the specific
RT recognition for UG- and TG-rich nucleic acids.";
RL Nucleic Acids Res. 42:4712-4722(2014).
RN [40]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 2-80, SUBUNIT, AND SUBCELLULAR
RP LOCATION.
RX PubMed=28663553; DOI=10.1038/s41467-017-00062-0;
RA Afroz T., Hock E.M., Ernst P., Foglieni C., Jambeau M., Gilhespy L.A.B.,
RA Laferriere F., Maniecka Z., Plueckthun A., Mittl P., Paganetti P.,
RA Allain F.H.T., Polymenidou M.;
RT "Functional and dynamic polymerization of the ALS-linked protein TDP-43
RT antagonizes its pathologic aggregation.";
RL Nat. Commun. 8:45-45(2017).
RN [41]
RP STRUCTURE BY NMR OF 1-80, MUTAGENESIS OF SER-48, SUBUNIT, FUNCTION, AND
RP SUBCELLULAR LOCATION.
RX PubMed=29438978; DOI=10.15252/embj.201797452;
RA Wang A., Conicella A.E., Schmidt H.B., Martin E.W., Rhoads S.N., Reeb A.N.,
RA Nourse A., Ramirez Montero D., Ryan V.H., Rohatgi R., Shewmaker F.,
RA Naik M.T., Mittag T., Ayala Y.M., Fawzi N.L.;
RT "A single N-terminal phosphomimic disrupts TDP-43 polymerization, phase
RT separation, and RNA splicing.";
RL EMBO J. 37:0-0(2018).
RN [42]
RP STRUCTURE BY ELECTRON MICROSCOPY (1.40 ANGSTROMS) OF 247-257.
RX PubMed=29531287; DOI=10.1038/s41594-018-0045-5;
RA Guenther E.L., Ge P., Trinh H., Sawaya M.R., Cascio D., Boyer D.R.,
RA Gonen T., Zhou Z.H., Eisenberg D.S.;
RT "Atomic-level evidence for packing and positional amyloid polymorphism by
RT segment from TDP-43 RRM2.";
RL Nat. Struct. Mol. Biol. 25:311-319(2018).
RN [43]
RP VARIANT ALS10 THR-315.
RX PubMed=18288693; DOI=10.1002/ana.21344;
RA Gitcho M.A., Baloh R.H., Chakraverty S., Mayo K., Norton J.B., Levitch D.,
RA Hatanpaa K.J., White C.L. III, Bigio E.H., Caselli R., Baker M.,
RA Al-Lozi M.T., Morris J.C., Pestronk A., Rademakers R., Goate A.M.,
RA Cairns N.J.;
RT "TDP-43 A315T mutation in familial motor neuron disease.";
RL Ann. Neurol. 63:535-538(2008).
RN [44]
RP VARIANT ALS10 ARG-343.
RX PubMed=18438952; DOI=10.1002/ana.21392;
RA Yokoseki A., Shiga A., Tan C.F., Tagawa A., Kaneko H., Koyama A.,
RA Eguchi H., Tsujino A., Ikeuchi T., Kakita A., Okamoto K., Nishizawa M.,
RA Takahashi H., Onodera O.;
RT "TDP-43 mutation in familial amyotrophic lateral sclerosis.";
RL Ann. Neurol. 63:538-542(2008).
RN [45]
RP VARIANTS ALS10 ALA-290 AND SER-298.
RX PubMed=18396105; DOI=10.1016/s1474-4422(08)70071-1;
RA Van Deerlin V.M., Leverenz J.B., Bekris L.M., Bird T.D., Yuan W.,
RA Elman L.B., Clay D., Wood E.M., Chen-Plotkin A.S., Martinez-Lage M.,
RA Steinbart E., McCluskey L., Grossman M., Neumann M., Wu I.-L., Yang W.-S.,
RA Kalb R., Galasko D.R., Montine T.J., Trojanowski J.Q., Lee V.M.-Y.,
RA Schellenberg G.D., Yu C.-E.;
RT "TARDBP mutations in amyotrophic lateral sclerosis with TDP-43
RT neuropathology: a genetic and histopathological analysis.";
RL Lancet Neurol. 7:409-416(2008).
RN [46]
RP VARIANTS ALS10 GLY-169; SER-287; THR-315; CYS-348; SER-361; THR-382;
RP ASP-390 AND SER-390, AND VARIANT VAL-90.
RX PubMed=18372902; DOI=10.1038/ng.132;
RA Kabashi E., Valdmanis P.N., Dion P., Spiegelman D., McConkey B.J.,
RA Vande Velde C., Bouchard J.-P., Lacomblez L., Pochigaeva K., Salachas F.,
RA Pradat P.-F., Camu W., Meininger V., Dupre N., Rouleau G.A.;
RT "TARDBP mutations in individuals with sporadic and familial amyotrophic
RT lateral sclerosis.";
RL Nat. Genet. 40:572-574(2008).
RN [47]
RP VARIANTS ALS10 ALA-294; LYS-331 AND VAL-337, VARIANT VAL-90, AND
RP CHARACTERIZATION OF VARIANTS ALS10 LYS-331 AND VAL-337.
RX PubMed=18309045; DOI=10.1126/science.1154584;
RA Sreedharan J., Blair I.P., Tripathi V.B., Hu X., Vance C., Rogelj B.,
RA Ackerley S., Durnall J.C., Williams K.L., Buratti E., Baralle F.,
RA de Belleroche J., Mitchell J.D., Leigh P.N., Al-Chalabi A., Miller C.C.,
RA Nicholson G., Shaw C.E.;
RT "TDP-43 mutations in familial and sporadic amyotrophic lateral sclerosis.";
RL Science 319:1668-1672(2008).
RN [48]
RP INVOLVEMENT OF VARIANT ALS10 SER-295 IN FRONTOTEMPORAL LOBAR DEGENERATION
RP WITH MOTOR NEURON DISEASE.
RX PubMed=19350673; DOI=10.1002/ana.21612;
RG French clinical and genetic research network on frontotemporal lobar degeneration/frontotemporal lobar degeneration with motoneuron disease;
RA Benajiba L., Le Ber I., Camuzat A., Lacoste M., Thomas-Anterion C.,
RA Couratier P., Legallic S., Salachas F., Hannequin D., Decousus M.,
RA Lacomblez L., Guedj E., Golfier V., Camu W., Dubois B., Campion D.,
RA Meininger V., Brice A.;
RT "TARDBP mutations in motoneuron disease with frontotemporal lobar
RT degeneration.";
RL Ann. Neurol. 65:470-473(2009).
RN [49]
RP VARIANTS ALS10 SER-267; SER-287; VAL-294; SER-295; ARG-295; ASN-332;
RP ASP-335; VAL-337; PRO-379; CYS-379; THR-382 AND LEU-393.
RX PubMed=19224587; DOI=10.1002/humu.20950;
RA Corrado L., Ratti A., Gellera C., Buratti E., Castellotti B.,
RA Carlomagno Y., Ticozzi N., Mazzini L., Testa L., Taroni F., Baralle F.E.,
RA Silani V., D'Alfonso S.;
RT "High frequency of TARDBP gene mutations in Italian patients with
RT amyotrophic lateral sclerosis.";
RL Hum. Mutat. 30:688-694(2009).
RN [50]
RP INVOLVEMENT OF VARIANT ALS10 SER-267 IN FRONTOTEMPORAL DEMENTIA.
RX PubMed=19655382; DOI=10.1002/humu.21100;
RA Borroni B., Bonvicini C., Alberici A., Buratti E., Agosti C., Archetti S.,
RA Papetti A., Stuani C., Di Luca M., Gennarelli M., Padovani A.;
RT "Mutation within TARDBP leads to frontotemporal dementia without motor
RT neuron disease.";
RL Hum. Mutat. 30:E974-E983(2009).
RN [51]
RP VARIANT ALS10 ALA-294.
RX PubMed=19695877; DOI=10.1016/j.nmd.2009.07.005;
RA Luquin N., Yu B., Saunderson R.B., Trent R.J., Pamphlett R.;
RT "Genetic variants in the promoter of TARDBP in sporadic amyotrophic lateral
RT sclerosis.";
RL Neuromuscul. Disord. 19:696-700(2009).
RN [52]
RP VARIANTS ALS10 SER-287; VAL-321; VAL-337 AND VAL-348, VARIANT VAL-90,
RP CHARACTERIZATION OF VARIANTS ALS10 SER-287; VAL-321 AND VAL-337, AND
RP FUNCTION.
RX PubMed=19760257; DOI=10.1007/s10048-009-0218-9;
RA Kirby J., Goodall E.F., Smith W., Highley J.R., Masanzu R., Hartley J.A.,
RA Hibberd R., Hollinger H.C., Wharton S.B., Morrison K.E., Ince P.G.,
RA McDermott C.J., Shaw P.J.;
RT "Broad clinical phenotypes associated with TAR-DNA binding protein (TARDBP)
RT mutations in amyotrophic lateral sclerosis.";
RL Neurogenetics 11:217-225(2010).
RN [53]
RP VARIANT ALS10 THR-382.
RX PubMed=21220647; DOI=10.1001/archneurol.2010.352;
RA Chio A., Borghero G., Pugliatti M., Ticca A., Calvo A., Moglia C.,
RA Mutani R., Brunetti M., Ossola I., Marrosu M.G., Murru M.R., Floris G.,
RA Cannas A., Parish L.D., Cossu P., Abramzon Y., Johnson J.O., Nalls M.A.,
RA Arepalli S., Chong S., Hernandez D.G., Traynor B.J., Restagno G.;
RT "Large proportion of amyotrophic lateral sclerosis cases in Sardinia due to
RT a single founder mutation of the TARDBP gene.";
RL Arch. Neurol. 68:594-598(2011).
RN [54]
RP VARIANT ALS10 THR-382.
RX PubMed=21418058; DOI=10.1111/j.1399-0004.2011.01668.x;
RA Orru S., Manolakos E., Orru N., Kokotas H., Mascia V., Carcassi C.,
RA Petersen M.B.;
RT "High frequency of the TARDBP p.Ala382Thr mutation in Sardinian patients
RT with amyotrophic lateral sclerosis.";
RL Clin. Genet. 81:172-178(2012).
RN [55]
RP VARIANT VAL-90, AND VARIANTS ALS10 ARG-357; THR-361 AND PRO-379.
RX PubMed=22456481; DOI=10.1038/jhg.2012.24;
RA Chiang H.H., Andersen P.M., Tysnes O.B., Gredal O., Christensen P.B.,
RA Graff C.;
RT "Novel TARDBP mutations in Nordic ALS patients.";
RL J. Hum. Genet. 57:316-319(2012).
RN [56]
RP CHARACTERIZATION OF VARIANTS ALS10 VAL-348; THR-315 AND SER-361, FUNCTION,
RP SUBCELLULAR LOCATION, INTERACTION WITH PPIA, AND MUTAGENESIS OF
RP 103-THR--SER-183.
RX PubMed=25678563; DOI=10.1093/brain/awv005;
RA Lauranzano E., Pozzi S., Pasetto L., Stucchi R., Massignan T., Paolella K.,
RA Mombrini M., Nardo G., Lunetta C., Corbo M., Mora G., Bendotti C.,
RA Bonetto V.;
RT "Peptidylprolyl isomerase A governs TARDBP function and assembly in
RT heterogeneous nuclear ribonucleoprotein complexes.";
RL Brain 138:974-991(2015).
RN [57]
RP CHARACTERIZATION OF VARIANTS ALS10 THR-315 AND LYS-331, AND SUBCELLULAR
RP LOCATION.
RX PubMed=33031745; DOI=10.1016/j.cell.2020.09.020;
RA Yu C.H., Davidson S., Harapas C.R., Hilton J.B., Mlodzianoski M.J.,
RA Laohamonthonkul P., Louis C., Low R.R.J., Moecking J., De Nardo D.,
RA Balka K.R., Calleja D.J., Moghaddas F., Ni E., McLean C.A., Samson A.L.,
RA Tyebji S., Tonkin C.J., Bye C.R., Turner B.J., Pepin G., Gantier M.P.,
RA Rogers K.L., McArthur K., Crouch P.J., Masters S.L.;
RT "TDP-43 triggers mitochondrial DNA release via mPTP to activate cGAS/STING
RT in ALS.";
RL Cell 183:636-649(2020).
CC -!- FUNCTION: RNA-binding protein that is involved in various steps of RNA
CC biogenesis and processing (PubMed:23519609). Preferentially binds, via
CC its two RNA recognition motifs RRM1 and RRM2, to GU-repeats on RNA
CC molecules predominantly localized within long introns and in the 3'UTR
CC of mRNAs (PubMed:23519609, PubMed:24240615, PubMed:24464995). In turn,
CC regulates the splicing of many non-coding and protein-coding RNAs
CC including proteins involved in neuronal survival, as well as mRNAs that
CC encode proteins relevant for neurodegenerative diseases
CC (PubMed:21358640, PubMed:29438978). Plays a role in maintaining
CC mitochondrial homeostasis by regulating the processing of mitochondrial
CC transcripts (PubMed:28794432). Regulates also mRNA stability by
CC recruiting CNOT7/CAF1 deadenylase on mRNA 3'UTR leading to poly(A) tail
CC deadenylation and thus shortening (PubMed:30520513). In response to
CC oxidative insult, associates with stalled ribosomes localized to stress
CC granules (SGs) and contributes to cell survival (PubMed:23398327,
CC PubMed:19765185). Participates also in the normal skeletal muscle
CC formation and regeneration, forming cytoplasmic myo-granules and
CC binding mRNAs that encode sarcomeric proteins (PubMed:30464263). Plays
CC a role in the maintenance of the circadian clock periodicity via
CC stabilization of the CRY1 and CRY2 proteins in a FBXL3-dependent manner
CC (PubMed:27123980). Negatively regulates the expression of CDK6
CC (PubMed:19760257). Regulates the expression of HDAC6, ATG7 and VCP in a
CC PPIA/CYPA-dependent manner (PubMed:25678563).
CC {ECO:0000269|PubMed:11285240, ECO:0000269|PubMed:17481916,
CC ECO:0000269|PubMed:19760257, ECO:0000269|PubMed:19765185,
CC ECO:0000269|PubMed:21358640, ECO:0000269|PubMed:23398327,
CC ECO:0000269|PubMed:23519609, ECO:0000269|PubMed:24240615,
CC ECO:0000269|PubMed:24464995, ECO:0000269|PubMed:25678563,
CC ECO:0000269|PubMed:27123980, ECO:0000269|PubMed:28794432,
CC ECO:0000269|PubMed:29438978, ECO:0000269|PubMed:30464263,
CC ECO:0000269|PubMed:30520513}.
CC -!- SUBUNIT: Homodimer (PubMed:20043239, PubMed:24464995). Homooligomer
CC (via its N-terminal domain) (PubMed:28663553, PubMed:29438978).
CC Interacts with BRDT (By similarity). Binds specifically to pyrimidine-
CC rich motifs of TAR DNA and to single stranded TG repeated sequences.
CC Binds to RNA, specifically to UG repeated sequences with a minimum of
CC six contiguous repeats. Interacts with ATXN2; the interaction is RNA-
CC dependent (PubMed:20740007). Interacts with MATR3 (PubMed:24686783).
CC Interacts with UBQLN2 (PubMed:23541532). Interacts with HNRNPA2B1
CC (PubMed:19429692). Interacts with ZNF106 (By similarity). Interacts
CC with CNOT7/CAF1 (PubMed:30520513). Interacts with CRY2
CC (PubMed:27123980). Interacts with PPIA/CYPA; the interaction is
CC dependent on RNA-binding activity of TARDBP and PPIase activity of
CC PPIA/CYPA and acetylation of PPIA/CYPA at 'Lys-125' favors the
CC interaction (PubMed:25678563). {ECO:0000250|UniProtKB:Q921F2,
CC ECO:0000269|PubMed:11470789, ECO:0000269|PubMed:19429692,
CC ECO:0000269|PubMed:20043239, ECO:0000269|PubMed:20740007,
CC ECO:0000269|PubMed:23541532, ECO:0000269|PubMed:24464995,
CC ECO:0000269|PubMed:24686783, ECO:0000269|PubMed:25678563,
CC ECO:0000269|PubMed:27123980, ECO:0000269|PubMed:28663553,
CC ECO:0000269|PubMed:29438978, ECO:0000269|PubMed:30520513}.
CC -!- INTERACTION:
CC Q13148; Q969K4: ABTB1; NbExp=3; IntAct=EBI-372899, EBI-7223971;
CC Q13148; P55265: ADAR; NbExp=3; IntAct=EBI-372899, EBI-2462104;
CC Q13148; Q6ZTN6-2: ANKRD13D; NbExp=3; IntAct=EBI-372899, EBI-25840993;
CC Q13148; P13928: ANXA8; NbExp=6; IntAct=EBI-372899, EBI-2556915;
CC Q13148; P63010-2: AP2B1; NbExp=6; IntAct=EBI-372899, EBI-11529439;
CC Q13148; P05067: APP; NbExp=6; IntAct=EBI-372899, EBI-77613;
CC Q13148; P05067-2: APP; NbExp=3; IntAct=EBI-372899, EBI-17264467;
CC Q13148; Q0P5N6: ARL16; NbExp=6; IntAct=EBI-372899, EBI-10186132;
CC Q13148; Q8WXK3: ASB13; NbExp=3; IntAct=EBI-372899, EBI-707573;
CC Q13148; Q9Y575-3: ASB3; NbExp=3; IntAct=EBI-372899, EBI-14199987;
CC Q13148; Q96DX5: ASB9; NbExp=3; IntAct=EBI-372899, EBI-745641;
CC Q13148; Q96DX5-3: ASB9; NbExp=3; IntAct=EBI-372899, EBI-25843552;
CC Q13148; Q96FT7-4: ASIC4; NbExp=6; IntAct=EBI-372899, EBI-9089489;
CC Q13148; P18847: ATF3; NbExp=6; IntAct=EBI-372899, EBI-712767;
CC Q13148; O95352-2: ATG7; NbExp=3; IntAct=EBI-372899, EBI-15980880;
CC Q13148; P15313: ATP6V1B1; NbExp=6; IntAct=EBI-372899, EBI-2891281;
CC Q13148; Q99700: ATXN2; NbExp=3; IntAct=EBI-372899, EBI-697691;
CC Q13148; P46379-2: BAG6; NbExp=6; IntAct=EBI-372899, EBI-10988864;
CC Q13148; Q8TBE0: BAHD1; NbExp=6; IntAct=EBI-372899, EBI-742750;
CC Q13148; Q5H9J7: BEX5; NbExp=6; IntAct=EBI-372899, EBI-10243741;
CC Q13148; O15392: BIRC5; NbExp=6; IntAct=EBI-372899, EBI-518823;
CC Q13148; Q9H0C5: BTBD1; NbExp=3; IntAct=EBI-372899, EBI-935503;
CC Q13148; Q5SZD1: C6orf141; NbExp=6; IntAct=EBI-372899, EBI-10697767;
CC Q13148; Q96LL4: C8orf48; NbExp=6; IntAct=EBI-372899, EBI-751596;
CC Q13148; Q13191: CBLB; NbExp=6; IntAct=EBI-372899, EBI-744027;
CC Q13148; Q9ULV8: CBLC; NbExp=3; IntAct=EBI-372899, EBI-2341018;
CC Q13148; Q14781-2: CBX2; NbExp=6; IntAct=EBI-372899, EBI-11974585;
CC Q13148; Q13939: CCIN; NbExp=3; IntAct=EBI-372899, EBI-25879469;
CC Q13148; Q13042: CDC16; NbExp=3; IntAct=EBI-372899, EBI-994830;
CC Q13148; Q13042-2: CDC16; NbExp=3; IntAct=EBI-372899, EBI-10974085;
CC Q13148; Q9UJX2: CDC23; NbExp=3; IntAct=EBI-372899, EBI-396137;
CC Q13148; Q92879-3: CELF1; NbExp=3; IntAct=EBI-372899, EBI-21370617;
CC Q13148; Q8NHQ1-3: CEP70; NbExp=6; IntAct=EBI-372899, EBI-11526150;
CC Q13148; Q494V2-2: CFAP100; NbExp=6; IntAct=EBI-372899, EBI-11953200;
CC Q13148; Q16740: CLPP; NbExp=3; IntAct=EBI-372899, EBI-1056029;
CC Q13148; Q8IUI8: CRLF3; NbExp=6; IntAct=EBI-372899, EBI-2872414;
CC Q13148; P48730-2: CSNK1D; NbExp=6; IntAct=EBI-372899, EBI-9087876;
CC Q13148; P61962: DCAF7; NbExp=3; IntAct=EBI-372899, EBI-359808;
CC Q13148; Q5TAQ9-2: DCAF8; NbExp=6; IntAct=EBI-372899, EBI-25842815;
CC Q13148; Q5TDH0-2: DDI2; NbExp=3; IntAct=EBI-372899, EBI-25858598;
CC Q13148; Q92841: DDX17; NbExp=6; IntAct=EBI-372899, EBI-746012;
CC Q13148; O00571: DDX3X; NbExp=6; IntAct=EBI-372899, EBI-353779;
CC Q13148; P17844: DDX5; NbExp=3; IntAct=EBI-372899, EBI-351962;
CC Q13148; O75398: DEAF1; NbExp=3; IntAct=EBI-372899, EBI-718185;
CC Q13148; Q96EY1-3: DNAJA3; NbExp=6; IntAct=EBI-372899, EBI-11526226;
CC Q13148; Q92782-2: DPF1; NbExp=6; IntAct=EBI-372899, EBI-23669343;
CC Q13148; Q86TI2-2: DPP9; NbExp=6; IntAct=EBI-372899, EBI-21529239;
CC Q13148; O75530-2: EED; NbExp=3; IntAct=EBI-372899, EBI-11132357;
CC Q13148; O00303: EIF3F; NbExp=6; IntAct=EBI-372899, EBI-711990;
CC Q13148; Q15717: ELAVL1; NbExp=7; IntAct=EBI-372899, EBI-374260;
CC Q13148; Q8TC29: ENKUR; NbExp=6; IntAct=EBI-372899, EBI-9246952;
CC Q13148; P29323-3: EPHB2; NbExp=6; IntAct=EBI-372899, EBI-25838727;
CC Q13148; Q6NXG1: ESRP1; NbExp=6; IntAct=EBI-372899, EBI-10213520;
CC Q13148; O00471: EXOC5; NbExp=6; IntAct=EBI-372899, EBI-949824;
CC Q13148; Q6P1L5: FAM117B; NbExp=6; IntAct=EBI-372899, EBI-3893327;
CC Q13148; Q17RN3: FAM98C; NbExp=6; IntAct=EBI-372899, EBI-5461838;
CC Q13148; Q8IZU1: FAM9A; NbExp=6; IntAct=EBI-372899, EBI-8468186;
CC Q13148; Q9UKA1: FBXL5; NbExp=3; IntAct=EBI-372899, EBI-2692340;
CC Q13148; Q9UKT5: FBXO4; NbExp=3; IntAct=EBI-372899, EBI-960409;
CC Q13148; P35637: FUS; NbExp=8; IntAct=EBI-372899, EBI-400434;
CC Q13148; Q06547-2: GABPB1; NbExp=6; IntAct=EBI-372899, EBI-618189;
CC Q13148; Q96IJ6: GMPPA; NbExp=6; IntAct=EBI-372899, EBI-750953;
CC Q13148; P62879: GNB2; NbExp=7; IntAct=EBI-372899, EBI-356942;
CC Q13148; Q9Y4H4: GPSM3; NbExp=6; IntAct=EBI-372899, EBI-347538;
CC Q13148; Q969Y2: GTPBP3; NbExp=6; IntAct=EBI-372899, EBI-740290;
CC Q13148; Q9UBN7: HDAC6; NbExp=3; IntAct=EBI-372899, EBI-301697;
CC Q13148; Q9HCC6: HES4; NbExp=6; IntAct=EBI-372899, EBI-2680288;
CC Q13148; P07910: HNRNPC; NbExp=3; IntAct=EBI-372899, EBI-357966;
CC Q13148; P07910-2: HNRNPC; NbExp=6; IntAct=EBI-372899, EBI-5280084;
CC Q13148; O14979: HNRNPDL; NbExp=3; IntAct=EBI-372899, EBI-299727;
CC Q13148; P31943: HNRNPH1; NbExp=7; IntAct=EBI-372899, EBI-351590;
CC Q13148; P61978: HNRNPK; NbExp=3; IntAct=EBI-372899, EBI-304185;
CC Q13148; P61978-2: HNRNPK; NbExp=6; IntAct=EBI-372899, EBI-7060731;
CC Q13148; O43390-2: HNRNPR; NbExp=3; IntAct=EBI-372899, EBI-12236340;
CC Q13148; Q00839-2: HNRNPU; NbExp=6; IntAct=EBI-372899, EBI-351143;
CC Q13148; Q9BUJ2: HNRNPUL1; NbExp=3; IntAct=EBI-372899, EBI-1018153;
CC Q13148; Q9BUJ2-2: HNRNPUL1; NbExp=3; IntAct=EBI-372899, EBI-11018029;
CC Q13148; Q9BTB7: HNRPUL1; NbExp=3; IntAct=EBI-372899, EBI-10298318;
CC Q13148; Q02363: ID2; NbExp=6; IntAct=EBI-372899, EBI-713450;
CC Q13148; P80217-2: IFI35; NbExp=6; IntAct=EBI-372899, EBI-12823003;
CC Q13148; Q9Y6M1: IGF2BP2; NbExp=3; IntAct=EBI-372899, EBI-1024419;
CC Q13148; O00425: IGF2BP3; NbExp=6; IntAct=EBI-372899, EBI-1058566;
CC Q13148; Q12906-6: ILF3; NbExp=6; IntAct=EBI-372899, EBI-12904528;
CC Q13148; Q9NXX0: ILF3; NbExp=3; IntAct=EBI-372899, EBI-743980;
CC Q13148; Q6DN90-2: IQSEC1; NbExp=6; IntAct=EBI-372899, EBI-21911304;
CC Q13148; O43187: IRAK2; NbExp=2; IntAct=EBI-372899, EBI-447733;
CC Q13148; Q92613: JADE3; NbExp=6; IntAct=EBI-372899, EBI-10278909;
CC Q13148; Q9NVX7-2: KBTBD4; NbExp=6; IntAct=EBI-372899, EBI-25871195;
CC Q13148; Q96SI1-2: KCTD15; NbExp=6; IntAct=EBI-372899, EBI-12382297;
CC Q13148; Q8N5Z5: KCTD17; NbExp=6; IntAct=EBI-372899, EBI-743960;
CC Q13148; Q9UIH9: KLF15; NbExp=6; IntAct=EBI-372899, EBI-2796400;
CC Q13148; Q6TDP4: KLHL17; NbExp=3; IntAct=EBI-372899, EBI-21328926;
CC Q13148; Q9Y2M5: KLHL20; NbExp=3; IntAct=EBI-372899, EBI-714379;
CC Q13148; Q53GT1: KLHL22; NbExp=3; IntAct=EBI-372899, EBI-1996072;
CC Q13148; Q53HC5: KLHL26; NbExp=3; IntAct=EBI-372899, EBI-724915;
CC Q13148; Q96NJ5: KLHL32; NbExp=3; IntAct=EBI-372899, EBI-6426390;
CC Q13148; Q8N4N3-2: KLHL36; NbExp=6; IntAct=EBI-372899, EBI-10973851;
CC Q13148; O00629: KPNA4; NbExp=3; IntAct=EBI-372899, EBI-396343;
CC Q13148; Q9BYQ4: KRTAP9-2; NbExp=6; IntAct=EBI-372899, EBI-1044640;
CC Q13148; Q96JM7-2: L3MBTL3; NbExp=6; IntAct=EBI-372899, EBI-11985629;
CC Q13148; Q9BYZ2: LDHAL6B; NbExp=6; IntAct=EBI-372899, EBI-1108377;
CC Q13148; Q6DKI2: LGALS9C; NbExp=6; IntAct=EBI-372899, EBI-9088829;
CC Q13148; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-372899, EBI-739832;
CC Q13148; Q8N448: LNX2; NbExp=6; IntAct=EBI-372899, EBI-2340947;
CC Q13148; Q1L5Z9: LONRF2; NbExp=3; IntAct=EBI-372899, EBI-2510853;
CC Q13148; O95777: LSM8; NbExp=6; IntAct=EBI-372899, EBI-347779;
CC Q13148; Q8TD91-2: MAGEC3; NbExp=6; IntAct=EBI-372899, EBI-10694180;
CC Q13148; Q15759: MAPK11; NbExp=6; IntAct=EBI-372899, EBI-298304;
CC Q13148; P43243: MATR3; NbExp=6; IntAct=EBI-372899, EBI-352602;
CC Q13148; A0JLT2-2: MED19; NbExp=3; IntAct=EBI-372899, EBI-13288755;
CC Q13148; Q8N6F8: METTL27; NbExp=6; IntAct=EBI-372899, EBI-8487781;
CC Q13148; Q8TDB4: MGARP; NbExp=6; IntAct=EBI-372899, EBI-4397720;
CC Q13148; Q8N108-16: MIER1; NbExp=6; IntAct=EBI-372899, EBI-25830642;
CC Q13148; A4FUJ8: MKL1; NbExp=6; IntAct=EBI-372899, EBI-21250407;
CC Q13148; Q9H000: MKRN2; NbExp=6; IntAct=EBI-372899, EBI-2341005;
CC Q13148; Q13064: MKRN3; NbExp=3; IntAct=EBI-372899, EBI-2340269;
CC Q13148; Q15049: MLC1; NbExp=6; IntAct=EBI-372899, EBI-8475277;
CC Q13148; P51948: MNAT1; NbExp=3; IntAct=EBI-372899, EBI-716139;
CC Q13148; O95396: MOCS3; NbExp=3; IntAct=EBI-372899, EBI-373206;
CC Q13148; Q8N594: MPND; NbExp=6; IntAct=EBI-372899, EBI-2512452;
CC Q13148; Q9Y483-4: MTF2; NbExp=3; IntAct=EBI-372899, EBI-10698053;
CC Q13148; P01106: MYC; NbExp=6; IntAct=EBI-372899, EBI-447544;
CC Q13148; O00746: NME4; NbExp=6; IntAct=EBI-372899, EBI-744871;
CC Q13148; Q9UNZ2: NSFL1C; NbExp=4; IntAct=EBI-372899, EBI-721577;
CC Q13148; Q8NFH3: NUP43; NbExp=3; IntAct=EBI-372899, EBI-1059321;
CC Q13148; O15381-5: NVL; NbExp=6; IntAct=EBI-372899, EBI-18577082;
CC Q13148; Q96FW1: OTUB1; NbExp=8; IntAct=EBI-372899, EBI-1058491;
CC Q13148; Q6GQQ9-2: OTUD7B; NbExp=6; IntAct=EBI-372899, EBI-25830200;
CC Q13148; P32242: OTX1; NbExp=6; IntAct=EBI-372899, EBI-740446;
CC Q13148; Q6VY07: PACS1; NbExp=6; IntAct=EBI-372899, EBI-2555014;
CC Q13148; Q9NR21-5: PARP11; NbExp=3; IntAct=EBI-372899, EBI-17159452;
CC Q13148; Q9HBE1-4: PATZ1; NbExp=3; IntAct=EBI-372899, EBI-11022007;
CC Q13148; Q9BYU1: PBX4; NbExp=6; IntAct=EBI-372899, EBI-10302990;
CC Q13148; Q9NV79: PCMTD2; NbExp=3; IntAct=EBI-372899, EBI-6309018;
CC Q13148; Q6ZMN7-2: PDZRN4; NbExp=3; IntAct=EBI-372899, EBI-25984441;
CC Q13148; P09565: PP9974; NbExp=6; IntAct=EBI-372899, EBI-10196507;
CC Q13148; O75807: PPP1R15A; NbExp=10; IntAct=EBI-372899, EBI-714746;
CC Q13148; Q6ZMI0-5: PPP1R21; NbExp=6; IntAct=EBI-372899, EBI-25835994;
CC Q13148; O60260-5: PRKN; NbExp=3; IntAct=EBI-372899, EBI-21251460;
CC Q13148; Q6P2Q9: PRPF8; NbExp=3; IntAct=EBI-372899, EBI-538479;
CC Q13148; P60891: PRPS1; NbExp=6; IntAct=EBI-372899, EBI-749195;
CC Q13148; P28070: PSMB4; NbExp=3; IntAct=EBI-372899, EBI-603350;
CC Q13148; P28062-2: PSMB8; NbExp=6; IntAct=EBI-372899, EBI-372312;
CC Q13148; Q13200: PSMD2; NbExp=3; IntAct=EBI-372899, EBI-357648;
CC Q13148; P26599-3: PTBP1; NbExp=3; IntAct=EBI-372899, EBI-16437588;
CC Q13148; Q9NS91: RAD18; NbExp=3; IntAct=EBI-372899, EBI-2339393;
CC Q13148; Q09028: RBBP4; NbExp=6; IntAct=EBI-372899, EBI-620823;
CC Q13148; Q9BYM8: RBCK1; NbExp=3; IntAct=EBI-372899, EBI-2340624;
CC Q13148; P98175: RBM10; NbExp=3; IntAct=EBI-372899, EBI-721525;
CC Q13148; Q8TBY0: RBM46; NbExp=3; IntAct=EBI-372899, EBI-12068216;
CC Q13148; P38159: RBMX; NbExp=3; IntAct=EBI-372899, EBI-743526;
CC Q13148; Q04206: RELA; NbExp=3; IntAct=EBI-372899, EBI-73886;
CC Q13148; Q9H871: RMND5A; NbExp=3; IntAct=EBI-372899, EBI-2797992;
CC Q13148; Q96G75: RMND5B; NbExp=3; IntAct=EBI-372899, EBI-745055;
CC Q13148; Q8N5U6: RNF10; NbExp=3; IntAct=EBI-372899, EBI-714023;
CC Q13148; Q9ULX5: RNF112; NbExp=6; IntAct=EBI-372899, EBI-25829984;
CC Q13148; Q8WVD3: RNF138; NbExp=3; IntAct=EBI-372899, EBI-749039;
CC Q13148; Q9UBS8: RNF14; NbExp=3; IntAct=EBI-372899, EBI-2130308;
CC Q13148; Q96A37: RNF166; NbExp=3; IntAct=EBI-372899, EBI-2130320;
CC Q13148; Q96D59: RNF183; NbExp=3; IntAct=EBI-372899, EBI-743938;
CC Q13148; Q8N488: RYBP; NbExp=6; IntAct=EBI-372899, EBI-752324;
CC Q13148; Q15393: SF3B3; NbExp=6; IntAct=EBI-372899, EBI-346977;
CC Q13148; Q8IUQ4-2: SIAH1; NbExp=3; IntAct=EBI-372899, EBI-11522811;
CC Q13148; Q8NCS7: SLC44A5; NbExp=6; IntAct=EBI-372899, EBI-21504521;
CC Q13148; Q96GM5: SMARCD1; NbExp=6; IntAct=EBI-372899, EBI-358489;
CC Q13148; Q9HCE7-2: SMURF1; NbExp=3; IntAct=EBI-372899, EBI-9845742;
CC Q13148; O14544: SOCS6; NbExp=3; IntAct=EBI-372899, EBI-3929549;
CC Q13148; Q99932-2: SPAG8; NbExp=6; IntAct=EBI-372899, EBI-11959123;
CC Q13148; Q8NHS9: SPATA22; NbExp=6; IntAct=EBI-372899, EBI-7067260;
CC Q13148; Q96BD6: SPSB1; NbExp=3; IntAct=EBI-372899, EBI-2659201;
CC Q13148; O95630: STAMBP; NbExp=3; IntAct=EBI-372899, EBI-396676;
CC Q13148; Q92797-2: SYMPK; NbExp=6; IntAct=EBI-372899, EBI-21560407;
CC Q13148; O60506-4: SYNCRIP; NbExp=6; IntAct=EBI-372899, EBI-11123832;
CC Q13148; Q13148: TARDBP; NbExp=31; IntAct=EBI-372899, EBI-372899;
CC Q13148; Q5VWN6: TASOR2; NbExp=6; IntAct=EBI-372899, EBI-745958;
CC Q13148; Q9Y458: TBX22; NbExp=6; IntAct=EBI-372899, EBI-6427217;
CC Q13148; Q15554-4: TERF2; NbExp=6; IntAct=EBI-372899, EBI-25840535;
CC Q13148; Q8WTV1: THAP3; NbExp=6; IntAct=EBI-372899, EBI-17438286;
CC Q13148; Q92956-2: TNFRSF14; NbExp=6; IntAct=EBI-372899, EBI-25985089;
CC Q13148; P50616: TOB1; NbExp=4; IntAct=EBI-372899, EBI-723281;
CC Q13148; P36406: TRIM23; NbExp=3; IntAct=EBI-372899, EBI-740098;
CC Q13148; Q9H8W5-2: TRIM45; NbExp=3; IntAct=EBI-372899, EBI-11993364;
CC Q13148; L8E9Q5: TRIM65; NbExp=3; IntAct=EBI-372899, EBI-25843781;
CC Q13148; Q86WT6-2: TRIM69; NbExp=3; IntAct=EBI-372899, EBI-11525489;
CC Q13148; Q86UV6-2: TRIM74; NbExp=3; IntAct=EBI-372899, EBI-10259086;
CC Q13148; Q9BZR9: TRIM8; NbExp=3; IntAct=EBI-372899, EBI-2340370;
CC Q13148; Q9C026: TRIM9; NbExp=6; IntAct=EBI-372899, EBI-720828;
CC Q13148; P41226: UBA7; NbExp=3; IntAct=EBI-372899, EBI-751921;
CC Q13148; Q13404: UBE2V1; NbExp=3; IntAct=EBI-372899, EBI-1050671;
CC Q13148; O94941: UBOX5; NbExp=3; IntAct=EBI-372899, EBI-751901;
CC Q13148; Q8IYU4: UBQLNL; NbExp=3; IntAct=EBI-372899, EBI-12295223;
CC Q13148; Q92995: USP13; NbExp=3; IntAct=EBI-372899, EBI-714351;
CC Q13148; O75604-3: USP2; NbExp=6; IntAct=EBI-372899, EBI-10696113;
CC Q13148; Q86UV5: USP48; NbExp=3; IntAct=EBI-372899, EBI-2512161;
CC Q13148; P40337-2: VHL; NbExp=3; IntAct=EBI-372899, EBI-12157263;
CC Q13148; Q8NEZ2: VPS37A; NbExp=3; IntAct=EBI-372899, EBI-2850578;
CC Q13148; Q8NEZ2-2: VPS37A; NbExp=3; IntAct=EBI-372899, EBI-10270911;
CC Q13148; P58304: VSX2; NbExp=6; IntAct=EBI-372899, EBI-6427899;
CC Q13148; Q9GZL7: WDR12; NbExp=3; IntAct=EBI-372899, EBI-2490660;
CC Q13148; Q9GZS3: WDR61; NbExp=6; IntAct=EBI-372899, EBI-358545;
CC Q13148; Q9BRX9: WDR83; NbExp=6; IntAct=EBI-372899, EBI-7705033;
CC Q13148; O00308: WWP2; NbExp=3; IntAct=EBI-372899, EBI-743923;
CC Q13148; Q9H0D6: XRN2; NbExp=7; IntAct=EBI-372899, EBI-372110;
CC Q13148; P67809: YBX1; NbExp=6; IntAct=EBI-372899, EBI-354065;
CC Q13148; O43167-2: ZBTB24; NbExp=3; IntAct=EBI-372899, EBI-25842419;
CC Q13148; P24278: ZBTB25; NbExp=3; IntAct=EBI-372899, EBI-739899;
CC Q13148; Q8N895: ZNF366; NbExp=4; IntAct=EBI-372899, EBI-2813661;
CC Q13148; Q9P0T4: ZNF581; NbExp=6; IntAct=EBI-372899, EBI-745520;
CC Q13148; Q8NBB4-2: ZSCAN1; NbExp=6; IntAct=EBI-372899, EBI-12021938;
CC Q13148; A0A384ME25; NbExp=6; IntAct=EBI-372899, EBI-10211777;
CC Q13148; Q9H669; NbExp=6; IntAct=EBI-372899, EBI-10307430;
CC Q13148; Q9WMX2; Xeno; NbExp=2; IntAct=EBI-372899, EBI-710918;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17023659,
CC ECO:0000269|PubMed:17481916, ECO:0000269|PubMed:18957508,
CC ECO:0000269|PubMed:19765185, ECO:0000269|PubMed:25678563,
CC ECO:0000269|PubMed:28663553, ECO:0000269|PubMed:29438978}. Cytoplasm
CC {ECO:0000269|PubMed:18957508, ECO:0000269|PubMed:23398327,
CC ECO:0000269|PubMed:30464263}. Cytoplasm, Stress granule
CC {ECO:0000269|PubMed:19765185, ECO:0000269|PubMed:23398327}.
CC Mitochondrion {ECO:0000269|PubMed:28794432,
CC ECO:0000269|PubMed:33031745}. Note=Continuously travels in and out of
CC the nucleus (PubMed:18957508). Localizes to stress granules in response
CC to oxidative stress (PubMed:19765185). A small subset localizes in
CC mitochondria (PubMed:28794432). {ECO:0000269|PubMed:18957508,
CC ECO:0000269|PubMed:19765185, ECO:0000269|PubMed:28794432}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q13148-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q13148-4; Sequence=VSP_056406, VSP_056407;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. In particular, expression
CC is high in pancreas, placenta, lung, genital tract and spleen.
CC -!- DOMAIN: Consists of an N-terminal domain (NTD) and two tandem RNA
CC recognition motifs, RRM1 and RRM2, followed by a C-terminal glycine-
CC rich region.
CC -!- DOMAIN: Contains a nuclear localization sequence and is mostly nuclear;
CC however, its nuclear export sequence permits it to transport mRNAs to
CC the cytoplasm and even to synapses as part of neuronal granules.
CC {ECO:0000269|PubMed:18957508}.
CC -!- PTM: Hyperphosphorylated in hippocampus, neocortex, and spinal cord
CC from individuals affected with ALS and FTLDU. Phosphorylated upon
CC cellular stress. {ECO:0000269|PubMed:23398327}.
CC -!- PTM: Ubiquitinated in hippocampus, neocortex, and spinal cord from
CC individuals affected with ALS and FTLDU. {ECO:0000269|PubMed:17023659,
CC ECO:0000269|PubMed:17481916}.
CC -!- PTM: Cleaved to generate C-terminal fragments in hippocampus,
CC neocortex, and spinal cord from individuals affected with ALS and
CC FTLDU.
CC -!- DISEASE: Amyotrophic lateral sclerosis 10 (ALS10) [MIM:612069]: A
CC neurodegenerative disorder affecting upper motor neurons in the brain
CC and lower motor neurons in the brain stem and spinal cord, resulting in
CC fatal paralysis. Sensory abnormalities are absent. The pathologic
CC hallmarks of the disease include pallor of the corticospinal tract due
CC to loss of motor neurons, presence of ubiquitin-positive inclusions
CC within surviving motor neurons, and deposition of pathologic
CC aggregates. The etiology of amyotrophic lateral sclerosis is likely to
CC be multifactorial, involving both genetic and environmental factors.
CC The disease is inherited in 5-10% of the cases.
CC {ECO:0000269|PubMed:18288693, ECO:0000269|PubMed:18309045,
CC ECO:0000269|PubMed:18372902, ECO:0000269|PubMed:18396105,
CC ECO:0000269|PubMed:18438952, ECO:0000269|PubMed:19224587,
CC ECO:0000269|PubMed:19350673, ECO:0000269|PubMed:19655382,
CC ECO:0000269|PubMed:19695877, ECO:0000269|PubMed:19760257,
CC ECO:0000269|PubMed:20740007, ECO:0000269|PubMed:21220647,
CC ECO:0000269|PubMed:21418058, ECO:0000269|PubMed:22456481,
CC ECO:0000269|PubMed:25678563, ECO:0000269|PubMed:33031745}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry. Neurodegeneration is caused by activation of the cGAS-STING
CC pathway: defects in TARDBP trigger mitochondrial DNA release into the
CC cytosol via the permeability transition pore (PubMed:33031745).
CC Released mitochondrial DNA is then detected by CGAS, leading to
CC activation of the cGAS-STING pathway, triggering type-I interferon
CC production and autoinflammation (PubMed:33031745).
CC {ECO:0000269|PubMed:33031745}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABO32290.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
CC Sequence=ABO32292.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; 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; U23731; AAA70033.1; -; mRNA.
DR EMBL; EF434181; ABO32290.1; ALT_SEQ; mRNA.
DR EMBL; EF434182; ABO32291.1; -; mRNA.
DR EMBL; EF434183; ABO32292.1; ALT_SEQ; mRNA.
DR EMBL; AK295920; BAG58707.1; -; mRNA.
DR EMBL; AK312416; BAG35326.1; -; mRNA.
DR EMBL; CR533534; CAG38565.1; -; mRNA.
DR EMBL; AK222754; BAD96474.1; -; mRNA.
DR EMBL; AL050265; CAB43367.1; -; mRNA.
DR EMBL; AL109811; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471130; EAW71670.1; -; Genomic_DNA.
DR EMBL; BC071657; AAH71657.1; -; mRNA.
DR EMBL; BC095435; AAH95435.1; -; mRNA.
DR CCDS; CCDS122.1; -. [Q13148-1]
DR PIR; I38977; I38977.
DR RefSeq; NP_031401.1; NM_007375.3. [Q13148-1]
DR RefSeq; XP_016856352.1; XM_017000863.1. [Q13148-1]
DR RefSeq; XP_016856353.1; XM_017000864.1. [Q13148-1]
DR RefSeq; XP_016856354.1; XM_017000865.1. [Q13148-1]
DR RefSeq; XP_016856355.1; XM_017000866.1. [Q13148-1]
DR RefSeq; XP_016856356.1; XM_017000867.1. [Q13148-1]
DR RefSeq; XP_016856357.1; XM_017000868.1. [Q13148-1]
DR PDB; 1WF0; NMR; -; A=193-267.
DR PDB; 2CQG; NMR; -; A=96-185.
DR PDB; 2N2C; NMR; -; A=307-349.
DR PDB; 2N3X; NMR; -; A=311-360.
DR PDB; 2N4G; NMR; -; A=311-360.
DR PDB; 2N4H; NMR; -; A=311-360.
DR PDB; 2N4P; NMR; -; A=1-77.
DR PDB; 4BS2; NMR; -; A=102-269.
DR PDB; 4IUF; X-ray; 2.75 A; A=103-179.
DR PDB; 4Y00; X-ray; 3.00 A; A/B/C/D=101-191.
DR PDB; 4Y0F; X-ray; 2.65 A; A/B=101-191.
DR PDB; 5MDI; X-ray; 2.10 A; A/B=2-80.
DR PDB; 5MRG; NMR; -; A=1-102.
DR PDB; 5W50; X-ray; 1.40 A; A/B=248-253.
DR PDB; 5W52; EM; 1.40 A; A=247-257.
DR PDB; 5W7V; EM; 3.80 A; 0/1/2/3/4/5/6/7/8=247-257.
DR PDB; 5WHN; X-ray; 1.10 A; A=312-317.
DR PDB; 5WHP; X-ray; 1.00 A; A=312-317.
DR PDB; 5WIA; X-ray; 1.00 A; A=370-375.
DR PDB; 5WIQ; X-ray; 1.25 A; A/B=396-402.
DR PDB; 5WKB; EM; 1.00 A; A=312-317.
DR PDB; 5WKD; X-ray; 1.80 A; A=300-306.
DR PDB; 5X4F; NMR; -; A=1-77.
DR PDB; 6B1G; NMR; -; A/B=1-80.
DR PDB; 6CF4; EM; 0.75 A; A=312-317.
DR PDB; 6CFH; EM; 1.50 A; A/B=333-343.
DR PDB; 6N37; EM; 3.80 A; A/B/C/D/E/F/G/H/I/J=311-360.
DR PDB; 6N3A; EM; 3.30 A; A/B/C/D/E/F/G/H/I/J=311-360.
DR PDB; 6N3B; EM; 3.80 A; A/B/C/D/E/F/G/H/I/J=311-360.
DR PDB; 6N3C; EM; 3.30 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T=286-331.
DR PDB; 6T4B; X-ray; 2.55 A; A/C/E/G/I=1-80.
DR PDB; 7KWZ; EM; 3.20 A; A/B/C/D/E=267-414.
DR PDB; 7PY2; EM; 2.60 A; A/B/C/D=1-414.
DR PDBsum; 1WF0; -.
DR PDBsum; 2CQG; -.
DR PDBsum; 2N2C; -.
DR PDBsum; 2N3X; -.
DR PDBsum; 2N4G; -.
DR PDBsum; 2N4H; -.
DR PDBsum; 2N4P; -.
DR PDBsum; 4BS2; -.
DR PDBsum; 4IUF; -.
DR PDBsum; 4Y00; -.
DR PDBsum; 4Y0F; -.
DR PDBsum; 5MDI; -.
DR PDBsum; 5MRG; -.
DR PDBsum; 5W50; -.
DR PDBsum; 5W52; -.
DR PDBsum; 5W7V; -.
DR PDBsum; 5WHN; -.
DR PDBsum; 5WHP; -.
DR PDBsum; 5WIA; -.
DR PDBsum; 5WIQ; -.
DR PDBsum; 5WKB; -.
DR PDBsum; 5WKD; -.
DR PDBsum; 5X4F; -.
DR PDBsum; 6B1G; -.
DR PDBsum; 6CF4; -.
DR PDBsum; 6CFH; -.
DR PDBsum; 6N37; -.
DR PDBsum; 6N3A; -.
DR PDBsum; 6N3B; -.
DR PDBsum; 6N3C; -.
DR PDBsum; 6T4B; -.
DR PDBsum; 7KWZ; -.
DR PDBsum; 7PY2; -.
DR AlphaFoldDB; Q13148; -.
DR BMRB; Q13148; -.
DR SMR; Q13148; -.
DR BioGRID; 117003; 466.
DR CORUM; Q13148; -.
DR DIP; DIP-31167N; -.
DR IntAct; Q13148; 263.
DR MINT; Q13148; -.
DR STRING; 9606.ENSP00000240185; -.
DR BindingDB; Q13148; -.
DR ChEMBL; CHEMBL2362981; -.
DR GlyGen; Q13148; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q13148; -.
DR MetOSite; Q13148; -.
DR PhosphoSitePlus; Q13148; -.
DR SwissPalm; Q13148; -.
DR BioMuta; TARDBP; -.
DR DMDM; 20140568; -.
DR EPD; Q13148; -.
DR jPOST; Q13148; -.
DR MassIVE; Q13148; -.
DR MaxQB; Q13148; -.
DR PaxDb; Q13148; -.
DR PeptideAtlas; Q13148; -.
DR PRIDE; Q13148; -.
DR ProteomicsDB; 4344; -.
DR ProteomicsDB; 59189; -. [Q13148-1]
DR ABCD; Q13148; 22 sequenced antibodies.
DR Antibodypedia; 1854; 958 antibodies from 47 providers.
DR DNASU; 23435; -.
DR Ensembl; ENST00000240185.8; ENSP00000240185.4; ENSG00000120948.19. [Q13148-1]
DR Ensembl; ENST00000639083.1; ENSP00000491203.1; ENSG00000120948.19. [Q13148-1]
DR GeneID; 23435; -.
DR KEGG; hsa:23435; -.
DR MANE-Select; ENST00000240185.8; ENSP00000240185.4; NM_007375.4; NP_031401.1.
DR UCSC; uc001art.4; human. [Q13148-1]
DR CTD; 23435; -.
DR DisGeNET; 23435; -.
DR GeneCards; TARDBP; -.
DR HGNC; HGNC:11571; TARDBP.
DR HPA; ENSG00000120948; Low tissue specificity.
DR MalaCards; TARDBP; -.
DR MIM; 605078; gene.
DR MIM; 612069; phenotype.
DR neXtProt; NX_Q13148; -.
DR OpenTargets; ENSG00000120948; -.
DR Orphanet; 803; Amyotrophic lateral sclerosis.
DR Orphanet; 275872; Frontotemporal dementia with motor neuron disease.
DR PharmGKB; PA36336; -.
DR VEuPathDB; HostDB:ENSG00000120948; -.
DR eggNOG; ENOG502QPQ8; Eukaryota.
DR GeneTree; ENSGT00940000154343; -.
DR HOGENOM; CLU_012062_6_1_1; -.
DR InParanoid; Q13148; -.
DR OMA; WGSASNP; -.
DR PhylomeDB; Q13148; -.
DR TreeFam; TF315657; -.
DR PathwayCommons; Q13148; -.
DR SignaLink; Q13148; -.
DR SIGNOR; Q13148; -.
DR BioGRID-ORCS; 23435; 693 hits in 1053 CRISPR screens.
DR ChiTaRS; TARDBP; human.
DR EvolutionaryTrace; Q13148; -.
DR GeneWiki; TARDBP; -.
DR GenomeRNAi; 23435; -.
DR Pharos; Q13148; Tchem.
DR PRO; PR:Q13148; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q13148; protein.
DR Bgee; ENSG00000120948; Expressed in secondary oocyte and 205 other tissues.
DR ExpressionAtlas; Q13148; baseline and differential.
DR Genevisible; Q13148; HS.
DR GO; GO:0010494; C:cytoplasmic stress granule; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:BHF-UCL.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:BHF-UCL.
DR GO; GO:0097157; F:pre-mRNA intronic binding; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; IDA:BHF-UCL.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IEA:Ensembl.
DR GO; GO:0061158; P:3'-UTR-mediated mRNA destabilization; IDA:CACAO.
DR GO; GO:0070935; P:3'-UTR-mediated mRNA stabilization; IDA:BHF-UCL.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0043922; P:negative regulation by host of viral transcription; IDA:BHF-UCL.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:CACAO.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IMP:CACAO.
DR GO; GO:0071765; P:nuclear inner membrane organization; IMP:CACAO.
DR GO; GO:0042307; P:positive regulation of protein import into nucleus; IEA:Ensembl.
DR GO; GO:0042981; P:regulation of apoptotic process; IMP:CACAO.
DR GO; GO:0051726; P:regulation of cell cycle; IMP:CACAO.
DR GO; GO:0042752; P:regulation of circadian rhythm; IEA:Ensembl.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:0031647; P:regulation of protein stability; IMP:UniProtKB.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR GO; GO:0008380; P:RNA splicing; IDA:BHF-UCL.
DR DisProt; DP01108; -.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR041105; TDP43_N.
DR Pfam; PF00076; RRM_1; 2.
DR Pfam; PF18694; TDP43_N; 1.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF54928; SSF54928; 2.
DR PROSITE; PS50102; RRM; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Amyotrophic lateral sclerosis;
KW Biological rhythms; Cytoplasm; Direct protein sequencing; Disease variant;
KW DNA-binding; Isopeptide bond; Methylation; Mitochondrion; mRNA processing;
KW mRNA splicing; Neurodegeneration; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; RNA-binding; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..414
FT /note="TAR DNA-binding protein 43"
FT /id="PRO_0000081972"
FT DOMAIN 104..200
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 191..262
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 216..414
FT /note="Interaction with UBQLN2"
FT /evidence="ECO:0000269|PubMed:23541532"
FT REGION 261..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 341..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 82..98
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:18957508"
FT MOTIF 239..250
FT /note="Nuclear export signal"
FT /evidence="ECO:0000269|PubMed:18957508"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 292
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 293
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT CROSSLNK 79
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 84
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 95
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 102
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25772364"
FT CROSSLNK 181
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT CROSSLNK 263
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..18
FT /note="MSEYIRVTEDENDEPIEI -> MPQMLAGEIWCMLSTIQK (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056406"
FT VAR_SEQ 19..134
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056407"
FT VARIANT 90
FT /note="A -> V (in dbSNP:rs80356715)"
FT /evidence="ECO:0000269|PubMed:18309045,
FT ECO:0000269|PubMed:18372902, ECO:0000269|PubMed:19760257,
FT ECO:0000269|PubMed:22456481"
FT /id="VAR_045656"
FT VARIANT 169
FT /note="D -> G (in ALS10; dbSNP:rs80356717)"
FT /evidence="ECO:0000269|PubMed:18372902"
FT /id="VAR_045657"
FT VARIANT 267
FT /note="N -> S (in ALS10; also in a patient with
FT frontotemporal dementia; dbSNP:rs80356718)"
FT /evidence="ECO:0000269|PubMed:19224587"
FT /id="VAR_058611"
FT VARIANT 287
FT /note="G -> S (in ALS10; loss of ability to negatively
FT regulate the expression of CDK6; dbSNP:rs80356719)"
FT /evidence="ECO:0000269|PubMed:18372902,
FT ECO:0000269|PubMed:19224587, ECO:0000269|PubMed:19760257"
FT /id="VAR_045658"
FT VARIANT 290
FT /note="G -> A (in ALS10; dbSNP:rs121908395)"
FT /evidence="ECO:0000269|PubMed:18396105"
FT /id="VAR_045659"
FT VARIANT 294
FT /note="G -> A (in ALS10; dbSNP:rs80356721)"
FT /evidence="ECO:0000269|PubMed:18309045,
FT ECO:0000269|PubMed:19695877"
FT /id="VAR_045660"
FT VARIANT 294
FT /note="G -> V (in ALS10; a patient with bulbar signs and
FT dementia; dbSNP:rs80356721)"
FT /evidence="ECO:0000269|PubMed:19224587"
FT /id="VAR_058612"
FT VARIANT 295
FT /note="G -> R (in ALS10; dbSNP:rs80356723)"
FT /evidence="ECO:0000269|PubMed:19224587"
FT /id="VAR_058613"
FT VARIANT 295
FT /note="G -> S (in ALS10; also in patients with
FT frontotemporal lobar degeneration with motor neuron
FT disease; dbSNP:rs80356723)"
FT /evidence="ECO:0000269|PubMed:19224587"
FT /id="VAR_058614"
FT VARIANT 298
FT /note="G -> S (in ALS10; dbSNP:rs4884357)"
FT /evidence="ECO:0000269|PubMed:18396105"
FT /id="VAR_045661"
FT VARIANT 315
FT /note="A -> T (in ALS10; triggers mitochondrial DNA release
FT into the cytosol, which is then detected by CGAS, leading
FT to activation of the cGAS-STING pathway and
FT autoinflammation; slight reduction in interaction with
FT PPIA/CYPA; dbSNP:rs80356726)"
FT /evidence="ECO:0000269|PubMed:18288693,
FT ECO:0000269|PubMed:18372902, ECO:0000269|PubMed:25678563,
FT ECO:0000269|PubMed:33031745"
FT /id="VAR_045662"
FT VARIANT 321
FT /note="A -> V (in ALS10; loss of ability to negatively
FT regulate the expression of CDK6)"
FT /evidence="ECO:0000269|PubMed:19760257"
FT /id="VAR_083737"
FT VARIANT 331
FT /note="Q -> K (in ALS10; triggers mitochondrial DNA release
FT into the cytosol, which is then detected by CGAS, leading
FT to activation of the cGAS-STING pathway and
FT autoinflammation; impedes the development of normal limb
FT and tail buds and increases the number of apoptotic nuclei
FT when expressed in chick embryos; does not affect the
FT interaction with ATXN2; dbSNP:rs80356727)"
FT /evidence="ECO:0000269|PubMed:18309045,
FT ECO:0000269|PubMed:20740007, ECO:0000269|PubMed:33031745"
FT /id="VAR_045663"
FT VARIANT 332
FT /note="S -> N (in ALS10; dbSNP:rs80356728)"
FT /evidence="ECO:0000269|PubMed:19224587"
FT /id="VAR_058615"
FT VARIANT 335
FT /note="G -> D (in ALS10; dbSNP:rs80356729)"
FT /evidence="ECO:0000269|PubMed:19224587"
FT /id="VAR_058616"
FT VARIANT 337
FT /note="M -> V (in ALS10; impedes the development of normal
FT limb and tail buds and increases the number of apoptotic
FT nuclei when expressed in chick embryos; loss of ability to
FT negatively regulate the expression of CDK6;
FT dbSNP:rs80356730)"
FT /evidence="ECO:0000269|PubMed:18309045,
FT ECO:0000269|PubMed:19224587, ECO:0000269|PubMed:19760257"
FT /id="VAR_045664"
FT VARIANT 343
FT /note="Q -> R (in ALS10; dbSNP:rs80356731)"
FT /evidence="ECO:0000269|PubMed:18438952"
FT /id="VAR_062767"
FT VARIANT 348
FT /note="G -> C (in ALS10; dbSNP:rs80356733)"
FT /evidence="ECO:0000269|PubMed:18372902"
FT /id="VAR_045665"
FT VARIANT 348
FT /note="G -> V (in ALS10; loss of interaction with PPIA/
FT CYPA)"
FT /evidence="ECO:0000269|PubMed:19760257,
FT ECO:0000269|PubMed:25678563"
FT /id="VAR_083738"
FT VARIANT 357
FT /note="G -> R (in ALS10)"
FT /evidence="ECO:0000269|PubMed:22456481"
FT /id="VAR_067499"
FT VARIANT 361
FT /note="R -> S (in ALS10; significant reduction in
FT interaction with PPIA/CYPA; dbSNP:rs80356735)"
FT /evidence="ECO:0000269|PubMed:18372902,
FT ECO:0000269|PubMed:25678563"
FT /id="VAR_045666"
FT VARIANT 361
FT /note="R -> T (in ALS10)"
FT /evidence="ECO:0000269|PubMed:22456481"
FT /id="VAR_067500"
FT VARIANT 379
FT /note="S -> C (in ALS10; dbSNP:rs80356739)"
FT /evidence="ECO:0000269|PubMed:19224587"
FT /id="VAR_058617"
FT VARIANT 379
FT /note="S -> P (in ALS10; dbSNP:rs80356738)"
FT /evidence="ECO:0000269|PubMed:19224587,
FT ECO:0000269|PubMed:22456481"
FT /id="VAR_058618"
FT VARIANT 382
FT /note="A -> T (in ALS10; dbSNP:rs367543041)"
FT /evidence="ECO:0000269|PubMed:18372902,
FT ECO:0000269|PubMed:19224587, ECO:0000269|PubMed:21220647,
FT ECO:0000269|PubMed:21418058"
FT /id="VAR_045667"
FT VARIANT 390
FT /note="N -> D (in ALS10; dbSNP:rs80356741)"
FT /evidence="ECO:0000269|PubMed:18372902"
FT /id="VAR_045668"
FT VARIANT 390
FT /note="N -> S (in ALS10; dbSNP:rs80356742)"
FT /evidence="ECO:0000269|PubMed:18372902"
FT /id="VAR_045669"
FT VARIANT 393
FT /note="S -> L (in ALS10; dbSNP:rs80356743)"
FT /evidence="ECO:0000269|PubMed:19224587"
FT /id="VAR_058619"
FT MUTAGEN 48
FT /note="S->E: Complete loss of self-oligomerization."
FT /evidence="ECO:0000269|PubMed:29438978"
FT MUTAGEN 103..183
FT /note="Missing: Loss of RNA-binding and reduced interaction
FT with PPIA/CYPA."
FT /evidence="ECO:0000269|PubMed:25678563"
FT MUTAGEN 106..175
FT /note="Missing: Completely abolishes RNA binding."
FT /evidence="ECO:0000269|PubMed:11470789"
FT MUTAGEN 106..111
FT /note="LIVLGL->DIDLGD: Completely abolishes RNA binding."
FT /evidence="ECO:0000269|PubMed:11470789"
FT MUTAGEN 106..111
FT /note="Missing: Completely abolishes RNA binding."
FT /evidence="ECO:0000269|PubMed:11470789"
FT MUTAGEN 147..149
FT /note="FGF->LGL: Highly reduces binding to RNA and DNA."
FT /evidence="ECO:0000269|PubMed:11470789"
FT MUTAGEN 193..257
FT /note="Missing: Alters but does not abolish RNA binding."
FT /evidence="ECO:0000269|PubMed:11470789"
FT CONFLICT 200
FT /note="E -> G (in Ref. 5; BAD96474)"
FT /evidence="ECO:0000305"
FT CONFLICT 278
FT /note="G -> V (in Ref. 3; BAG35326)"
FT /evidence="ECO:0000305"
FT STRAND 4..10
FT /evidence="ECO:0007829|PDB:5MDI"
FT STRAND 16..19
FT /evidence="ECO:0007829|PDB:5MDI"
FT STRAND 22..24
FT /evidence="ECO:0007829|PDB:2N4P"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:5X4F"
FT HELIX 28..32
FT /evidence="ECO:0007829|PDB:5MDI"
FT STRAND 33..37
FT /evidence="ECO:0007829|PDB:5X4F"
FT STRAND 40..44
FT /evidence="ECO:0007829|PDB:5MDI"
FT TURN 46..48
FT /evidence="ECO:0007829|PDB:5MDI"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:5MDI"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:5MDI"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:5MDI"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:5X4F"
FT TURN 69..71
FT /evidence="ECO:0007829|PDB:6B1G"
FT STRAND 72..76
FT /evidence="ECO:0007829|PDB:5MDI"
FT STRAND 106..110
FT /evidence="ECO:0007829|PDB:4Y0F"
FT HELIX 117..124
FT /evidence="ECO:0007829|PDB:4Y0F"
FT TURN 125..127
FT /evidence="ECO:0007829|PDB:4Y0F"
FT STRAND 130..137
FT /evidence="ECO:0007829|PDB:4Y0F"
FT TURN 139..141
FT /evidence="ECO:0007829|PDB:4Y0F"
FT STRAND 144..154
FT /evidence="ECO:0007829|PDB:4Y0F"
FT HELIX 155..162
FT /evidence="ECO:0007829|PDB:4Y0F"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:4Y0F"
FT STRAND 171..176
FT /evidence="ECO:0007829|PDB:4Y0F"
FT STRAND 193..197
FT /evidence="ECO:0007829|PDB:1WF0"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:1WF0"
FT HELIX 204..210
FT /evidence="ECO:0007829|PDB:1WF0"
FT TURN 212..214
FT /evidence="ECO:0007829|PDB:1WF0"
FT STRAND 219..221
FT /evidence="ECO:0007829|PDB:1WF0"
FT STRAND 231..233
FT /evidence="ECO:0007829|PDB:1WF0"
FT HELIX 237..242
FT /evidence="ECO:0007829|PDB:1WF0"
FT TURN 243..245
FT /evidence="ECO:0007829|PDB:1WF0"
FT STRAND 247..250
FT /evidence="ECO:0007829|PDB:1WF0"
FT STRAND 253..258
FT /evidence="ECO:0007829|PDB:1WF0"
FT STRAND 263..265
FT /evidence="ECO:0007829|PDB:4BS2"
FT STRAND 283..285
FT /evidence="ECO:0007829|PDB:7PY2"
FT STRAND 298..300
FT /evidence="ECO:0007829|PDB:7PY2"
FT STRAND 302..305
FT /evidence="ECO:0007829|PDB:7KWZ"
FT STRAND 311..313
FT /evidence="ECO:0007829|PDB:7PY2"
FT STRAND 316..318
FT /evidence="ECO:0007829|PDB:7KWZ"
FT STRAND 319..321
FT /evidence="ECO:0007829|PDB:2N2C"
FT TURN 322..325
FT /evidence="ECO:0007829|PDB:7PY2"
FT STRAND 327..331
FT /evidence="ECO:0007829|PDB:7PY2"
FT STRAND 334..342
FT /evidence="ECO:0007829|PDB:6CFH"
FT TURN 343..346
FT /evidence="ECO:0007829|PDB:2N3X"
FT STRAND 348..350
FT /evidence="ECO:0007829|PDB:2N3X"
FT STRAND 354..357
FT /evidence="ECO:0007829|PDB:7PY2"
FT STRAND 367..370
FT /evidence="ECO:0007829|PDB:7KWZ"
FT STRAND 373..378
FT /evidence="ECO:0007829|PDB:7KWZ"
FT STRAND 382..384
FT /evidence="ECO:0007829|PDB:7KWZ"
FT STRAND 389..395
FT /evidence="ECO:0007829|PDB:7KWZ"
FT STRAND 405..412
FT /evidence="ECO:0007829|PDB:7KWZ"
SQ SEQUENCE 414 AA; 44740 MW; 8E09A1206FB4EF4A CRC64;
MSEYIRVTED ENDEPIEIPS EDDGTVLLST VTAQFPGACG LRYRNPVSQC MRGVRLVEGI
LHAPDAGWGN LVYVVNYPKD NKRKMDETDA SSAVKVKRAV QKTSDLIVLG LPWKTTEQDL
KEYFSTFGEV LMVQVKKDLK TGHSKGFGFV RFTEYETQVK VMSQRHMIDG RWCDCKLPNS
KQSQDEPLRS RKVFVGRCTE DMTEDELREF FSQYGDVMDV FIPKPFRAFA FVTFADDQIA
QSLCGEDLII KGISVHISNA EPKHNSNRQL ERSGRFGGNP GGFGNQGGFG NSRGGGAGLG
NNQGSNMGGG MNFGAFSINP AMMAAAQAAL QSSWGMMGML ASQQNQSGPS GNNQNQGNMQ
REPNQAFGSG NNSYSGSNSG AAIGWGSASN AGSGSGFNGG FGSSMDSKSS GWGM
