MATR3_HUMAN
ID MATR3_HUMAN Reviewed; 847 AA.
AC P43243; B7ZAV5; D3DQC3; Q9UHW0; Q9UQ27;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2001, sequence version 2.
DT 03-AUG-2022, entry version 225.
DE RecName: Full=Matrin-3;
GN Name=MATR3; Synonyms=KIAA0723;
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 [LARGE SCALE MRNA] (ISOFORM 1).
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Hypothalamus;
RX PubMed=10931946; DOI=10.1073/pnas.160270997;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W.,
RA Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J.,
RA Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z.,
RA Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis
RT and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
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 GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [5]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Skin;
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 PROTEIN SEQUENCE OF 2-12; 150-160; 187-207 AND 374-387, CLEAVAGE OF
RP INITIATOR METHIONINE, ACETYLATION AT SER-2, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Mammary carcinoma;
RA Bienvenut W.V., Matallanas D., Kolch W.;
RL Submitted (JUL-2009) to UniProtKB.
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 432-847 (ISOFORM 1).
RX PubMed=2033075; DOI=10.1016/s0021-9258(18)92902-9;
RA Belgrader P., Dey R., Berezney R.;
RT "Molecular cloning of matrin 3. A 125-kilodalton protein of the nuclear
RT matrix contains an extensive acidic domain.";
RL J. Biol. Chem. 266:9893-9899(1991).
RN [9]
RP FUNCTION IN NUCLEAR RETENTION OF A-TO-I EDITED RNAS, AND IDENTIFICATION IN
RP A COMPLEX WITH SFPQ AND NONO.
RX PubMed=11525732; DOI=10.1016/s0092-8674(01)00466-4;
RA Zhang Z., Carmichael G.G.;
RT "The fate of dsRNA in the nucleus: a p54(nrb)-containing complex mediates
RT the nuclear retention of promiscuously A-to-I edited RNAs.";
RL Cell 106:465-475(2001).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [11]
RP INTERACTION WITH AGO1 AND AGO2.
RX PubMed=17932509; DOI=10.1038/sj.embor.7401088;
RA Hoeck J., Weinmann L., Ender C., Ruedel S., Kremmer E., Raabe M.,
RA Urlaub H., Meister G.;
RT "Proteomic and functional analysis of Argonaute-containing mRNA-protein
RT complexes in human cells.";
RL EMBO Rep. 8:1052-1060(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17924679; DOI=10.1021/pr070152u;
RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells
RT and high confident phosphopeptide identification by cross-validation of
RT MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188 AND SER-206, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=T-cell;
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using sequential
RT IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188; SER-195; SER-208;
RP SER-533; SER-596; SER-598 AND SER-604, AND IDENTIFICATION BY MASS
RP 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [18]
RP IDENTIFICATION IN A COMPLEX WITH ZNF335; MKI67; EMSY; ZNF335; HSPA8;
RP TUBB2A; CCAR2; ASCL2; RBBP5 AND WDR5.
RX PubMed=19131338; DOI=10.1074/jbc.m805872200;
RA Garapaty S., Xu C.F., Trojer P., Mahajan M.A., Neubert T.A., Samuels H.H.;
RT "Identification and characterization of a novel nuclear protein complex
RT involved in nuclear hormone receptor-mediated gene regulation.";
RL J. Biol. Chem. 284:7542-7552(2009).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22 AND SER-118, AND
RP IDENTIFICATION BY 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 [20]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-3; LYS-522; LYS-571 AND LYS-836,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4; SER-14; SER-41; SER-188;
RP SER-195; SER-206; SER-208; SER-533; SER-598; SER-604; SER-606; SER-689 AND
RP SER-766, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [22]
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 [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4; SER-9; SER-188; SER-195;
RP SER-206; SER-208; TYR-219; SER-533; SER-596; SER-598; SER-604; THR-741;
RP SER-747 AND SER-766, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [24]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4; SER-9; SER-11; SER-14;
RP SER-118; SER-126; THR-150; SER-157; TYR-158; SER-164; SER-188; SER-195;
RP TYR-202; SER-206; SER-211; SER-234; SER-264; SER-275; SER-509; SER-511;
RP SER-533; SER-598; SER-604 AND SER-766, 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 [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4; THR-150; SER-188; SER-206;
RP SER-598; SER-604; SER-654; SER-671; SER-673; SER-674 AND THR-679, AND
RP IDENTIFICATION BY 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 INTERACTION WITH TARDBP, VARIANTS ALS21 CYS-85; CYS-115; SER-154 AND
RP ALA-622, AND CHARACTERIZATION OF VARIANT ALS21 CYS-85.
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 [28]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-3; LYS-487; LYS-491; LYS-617;
RP LYS-719 AND LYS-736, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [29]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-487 AND LYS-491, 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 [30]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-3; LYS-146; LYS-491; LYS-554 AND
RP LYS-617, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [31]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [32]
RP INTERACTION WITH FUS.
RX PubMed=27731383; DOI=10.1038/srep35195;
RA Yamaguchi A., Takanashi K.;
RT "FUS interacts with nuclear matrix-associated protein SAFB1 as well as
RT Matrin3 to regulate splicing and ligand-mediated transcription.";
RL Sci. Rep. 6:35195-35195(2016).
RN [33]
RP FUNCTION, AND MIRNA-BINDING.
RX PubMed=28431233; DOI=10.1016/j.molcel.2017.03.014;
RA Treiber T., Treiber N., Plessmann U., Harlander S., Daiss J.L., Eichner N.,
RA Lehmann G., Schall K., Urlaub H., Meister G.;
RT "A Compendium of RNA-Binding Proteins that Regulate MicroRNA Biogenesis.";
RL Mol. Cell 66:270-284(2017).
RN [34]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PRKDC; XRCC5; XRCC6;
RP SFPQ; NONO; PSPC1; RBM14 AND HEXIM1.
RX PubMed=28712728; DOI=10.1016/j.molcel.2017.06.020;
RA Morchikh M., Cribier A., Raffel R., Amraoui S., Cau J., Severac D.,
RA Dubois E., Schwartz O., Bennasser Y., Benkirane M.;
RT "HEXIM1 and NEAT1 Long non-coding RNA form a multi-subunit complex that
RT regulates DNA-mediated innate immune response.";
RL Mol. Cell 67:387-399(2017).
RN [35]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-3; LYS-132; LYS-146; LYS-245;
RP LYS-269; LYS-478; LYS-487; LYS-491; LYS-515; LYS-522; LYS-554; LYS-555;
RP LYS-617; LYS-630; LYS-719; LYS-736; LYS-770 AND LYS-836, AND IDENTIFICATION
RP 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 [36]
RP INTERACTION WITH IGF2BP1; IGF2BP2 AND IGF2BP3.
RX PubMed=29476152; DOI=10.1038/s41556-018-0045-z;
RA Huang H., Weng H., Sun W., Qin X., Shi H., Wu H., Zhao B.S., Mesquita A.,
RA Liu C., Yuan C.L., Hu Y.C., Huettelmaier S., Skibbe J.R., Su R., Deng X.,
RA Dong L., Sun M., Li C., Nachtergaele S., Wang Y., Hu C., Ferchen K.,
RA Greis K.D., Jiang X., Wei M., Qu L., Guan J.L., He C., Yang J., Chen J.;
RT "Recognition of RNA N6-methyladenosine by IGF2BP proteins enhances mRNA
RT stability and translation.";
RL Nat. Cell Biol. 20:285-295(2018).
RN [37]
RP FUNCTION, AND INTERACTION WITH IGF2BP1.
RX PubMed=32245947; DOI=10.1038/s41467-020-15403-9;
RA Zhu S., Wang J.Z., Chen D., He Y.T., Meng N., Chen M., Lu R.X., Chen X.H.,
RA Zhang X.L., Yan G.R.;
RT "An oncopeptide regulates m6A recognition by the m6A reader IGF2BP1 and
RT tumorigenesis.";
RL Nat. Commun. 11:1685-1685(2020).
RN [38]
RP VARIANT ALS21 CYS-85.
RX PubMed=19344878; DOI=10.1016/j.ajhg.2009.03.006;
RA Senderek J., Garvey S.M., Krieger M., Guergueltcheva V., Urtizberea A.,
RA Roos A., Elbracht M., Stendel C., Tournev I., Mihailova V., Feit H.,
RA Tramonte J., Hedera P., Crooks K., Bergmann C., Rudnik-Schoeneborn S.,
RA Zerres K., Lochmueller H., Seboun E., Weis J., Beckmann J.S., Hauser M.A.,
RA Jackson C.E.;
RT "Autosomal-dominant distal myopathy associated with a recurrent missense
RT mutation in the gene encoding the nuclear matrix protein, matrin 3.";
RL Am. J. Hum. Genet. 84:511-518(2009).
RN [39]
RP VARIANT ALS21 TRP-147.
RX PubMed=26199109; DOI=10.3109/21678421.2015.1058397;
RA Origone P., Verdiani S., Bandettini Di Poggio M., Zuccarino R., Vignolo M.,
RA Caponnetto C., Mandich P.;
RT "A novel Arg147Trp MATR3 missense mutation in a slowly progressive ALS
RT Italian patient.";
RL Amyotroph. Lateral Scler. Frontotemporal Degener. 16:530-531(2015).
RN [40]
RP VARIANTS VAL-89; ALA-664 AND SER-787, AND VARIANT ALS21 THR-72.
RX PubMed=25771394; DOI=10.1016/j.neurobiolaging.2015.02.008;
RA Lin K.P., Tsai P.C., Liao Y.C., Chen W.T., Tsai C.P., Soong B.W., Lee Y.C.;
RT "Mutational analysis of MATR3 in Taiwanese patients with amyotrophic
RT lateral sclerosis.";
RL Neurobiol. Aging 36:2005.E1-2005.E4(2015).
CC -!- FUNCTION: May play a role in transcription or may interact with other
CC nuclear matrix proteins to form the internal fibrogranular network. In
CC association with the SFPQ-NONO heteromer may play a role in nuclear
CC retention of defective RNAs. Plays a role in the regulation of DNA
CC virus-mediated innate immune response by assembling into the HDP-RNP
CC complex, a complex that serves as a platform for IRF3 phosphorylation
CC and subsequent innate immune response activation through the cGAS-STING
CC pathway (PubMed:28712728). Binds to N6-methyladenosine (m6A)-containing
CC mRNAs and contributes to MYC stability by binding to m6A-containing MYC
CC mRNAs (PubMed:32245947). May bind to specific miRNA hairpins
CC (PubMed:28431233). {ECO:0000269|PubMed:11525732,
CC ECO:0000269|PubMed:28431233, ECO:0000269|PubMed:28712728,
CC ECO:0000269|PubMed:32245947}.
CC -!- SUBUNIT: Part of a complex consisting of SFPQ, NONO and MATR3.
CC Interacts with AGO1 and AGO2. Part of a complex composed at least of
CC ASCL2, EMSY, HCFC1, HSPA8, CCAR2, MATR3, MKI67, RBBP5, TUBB2A, WDR5 and
CC ZNF335; this complex may have a histone H3-specific methyltransferase
CC activity. Interacts with TARDBP. Part of the HDP-RNP complex composed
CC of at least HEXIM1, PRKDC, XRCC5, XRCC6, paraspeckle proteins (SFPQ,
CC NONO, PSPC1, RBM14, and MATR3) and NEAT1 RNA (PubMed:28712728).
CC Interacts with FUS. Interacts with IGF2BP1; the interaction is enhanced
CC by SEPIN14P20 peptide RBPR (PubMed:32245947, PubMed:29476152).
CC Interacts with IGF2BP2 and IGF2BP3 (PubMed:29476152).
CC {ECO:0000269|PubMed:11525732, ECO:0000269|PubMed:17932509,
CC ECO:0000269|PubMed:19131338, ECO:0000269|PubMed:24686783,
CC ECO:0000269|PubMed:27731383, ECO:0000269|PubMed:28712728,
CC ECO:0000269|PubMed:29476152, ECO:0000269|PubMed:32245947}.
CC -!- INTERACTION:
CC P43243; Q9NRI5: DISC1; NbExp=3; IntAct=EBI-352602, EBI-529989;
CC P43243; P61978: HNRNPK; NbExp=4; IntAct=EBI-352602, EBI-304185;
CC P43243; P61978-2: HNRNPK; NbExp=4; IntAct=EBI-352602, EBI-7060731;
CC P43243; P34969: HTR7; NbExp=2; IntAct=EBI-352602, EBI-2625020;
CC P43243; P42858: HTT; NbExp=4; IntAct=EBI-352602, EBI-466029;
CC P43243; Q7Z3Y8: KRT27; NbExp=3; IntAct=EBI-352602, EBI-3044087;
CC P43243; O76011: KRT34; NbExp=3; IntAct=EBI-352602, EBI-1047093;
CC P43243; P43243: MATR3; NbExp=4; IntAct=EBI-352602, EBI-352602;
CC P43243; P22736: NR4A1; NbExp=2; IntAct=EBI-352602, EBI-721550;
CC P43243; P57721-2: PCBP3; NbExp=3; IntAct=EBI-352602, EBI-11983983;
CC P43243; Q58EX7: PLEKHG4; NbExp=3; IntAct=EBI-352602, EBI-949255;
CC P43243; Q9UKA9-2: PTBP2; NbExp=3; IntAct=EBI-352602, EBI-12255608;
CC P43243; Q9Y272: RASD1; NbExp=6; IntAct=EBI-352602, EBI-740818;
CC P43243; Q13148: TARDBP; NbExp=6; IntAct=EBI-352602, EBI-372899;
CC P43243; Q13077: TRAF1; NbExp=3; IntAct=EBI-352602, EBI-359224;
CC P43243; Q9BZW7: TSGA10; NbExp=3; IntAct=EBI-352602, EBI-744794;
CC -!- SUBCELLULAR LOCATION: Nucleus matrix.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P43243-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P43243-2; Sequence=VSP_042624;
CC -!- DISEASE: Amyotrophic lateral sclerosis 21 (ALS21) [MIM:606070]: A
CC neurodegenerative disorder affecting upper and lower motor neurons,
CC resulting in muscle weakness and respiratory failure. Some patients may
CC develop myopathic features or dementia. {ECO:0000269|PubMed:19344878,
CC ECO:0000269|PubMed:24686783, ECO:0000269|PubMed:25771394,
CC ECO:0000269|PubMed:26199109}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF17217.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAA34443.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB018266; BAA34443.2; ALT_INIT; mRNA.
DR EMBL; AF117236; AAF17217.1; ALT_FRAME; mRNA.
DR EMBL; AK316420; BAH14791.1; -; mRNA.
DR EMBL; AC011404; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471062; EAW62114.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW62115.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW62116.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW62117.1; -; Genomic_DNA.
DR EMBL; BC015031; AAH15031.1; -; mRNA.
DR EMBL; M63483; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS4210.1; -. [P43243-1]
DR CCDS; CCDS54908.1; -. [P43243-2]
DR RefSeq; NP_001181883.1; NM_001194954.1. [P43243-1]
DR RefSeq; NP_001181884.1; NM_001194955.1. [P43243-1]
DR RefSeq; NP_001181885.1; NM_001194956.1. [P43243-2]
DR RefSeq; NP_001269207.1; NM_001282278.1.
DR RefSeq; NP_061322.2; NM_018834.5. [P43243-1]
DR RefSeq; NP_954659.1; NM_199189.2. [P43243-1]
DR AlphaFoldDB; P43243; -.
DR SMR; P43243; -.
DR BioGRID; 115126; 524.
DR CORUM; P43243; -.
DR IntAct; P43243; 203.
DR MINT; P43243; -.
DR STRING; 9606.ENSP00000354346; -.
DR GlyGen; P43243; 8 sites, 2 O-linked glycans (8 sites).
DR iPTMnet; P43243; -.
DR MetOSite; P43243; -.
DR PhosphoSitePlus; P43243; -.
DR SwissPalm; P43243; -.
DR BioMuta; MATR3; -.
DR DMDM; 12643409; -.
DR EPD; P43243; -.
DR jPOST; P43243; -.
DR MassIVE; P43243; -.
DR MaxQB; P43243; -.
DR PaxDb; P43243; -.
DR PeptideAtlas; P43243; -.
DR PRIDE; P43243; -.
DR ProteomicsDB; 55599; -. [P43243-1]
DR ProteomicsDB; 55600; -. [P43243-2]
DR TopDownProteomics; P43243-1; -. [P43243-1]
DR ABCD; P43243; 1 sequenced antibody.
DR Antibodypedia; 15070; 239 antibodies from 30 providers.
DR DNASU; 9782; -.
DR Ensembl; ENST00000394805.8; ENSP00000378284.3; ENSG00000015479.20. [P43243-1]
DR Ensembl; ENST00000503811.5; ENSP00000423587.1; ENSG00000015479.20. [P43243-2]
DR Ensembl; ENST00000618441.5; ENSP00000482895.1; ENSG00000015479.20. [P43243-1]
DR GeneID; 9782; -.
DR KEGG; hsa:9782; -.
DR MANE-Select; ENST00000394805.8; ENSP00000378284.3; NM_018834.6; NP_061322.2.
DR UCSC; uc003ldx.4; human. [P43243-1]
DR CTD; 9782; -.
DR DisGeNET; 9782; -.
DR GeneCards; MATR3; -.
DR HGNC; HGNC:6912; MATR3.
DR HPA; ENSG00000015479; Low tissue specificity.
DR MalaCards; MATR3; -.
DR MIM; 164015; gene.
DR MIM; 606070; phenotype.
DR neXtProt; NX_P43243; -.
DR OpenTargets; ENSG00000015479; -.
DR OpenTargets; ENSG00000280987; -.
DR Orphanet; 803; Amyotrophic lateral sclerosis.
DR Orphanet; 600; Vocal cord and pharyngeal distal myopathy.
DR PharmGKB; PA30655; -.
DR VEuPathDB; HostDB:ENSG00000015479; -.
DR eggNOG; ENOG502QRVG; Eukaryota.
DR GeneTree; ENSGT00940000153322; -.
DR HOGENOM; CLU_015917_0_0_1; -.
DR InParanoid; P43243; -.
DR OMA; PSMFPHV; -.
DR OrthoDB; 200901at2759; -.
DR PhylomeDB; P43243; -.
DR TreeFam; TF333921; -.
DR PathwayCommons; P43243; -.
DR SignaLink; P43243; -.
DR SIGNOR; P43243; -.
DR BioGRID-ORCS; 9782; 143 hits in 1083 CRISPR screens.
DR ChiTaRS; MATR3; human.
DR GeneWiki; MATR3; -.
DR GenomeRNAi; 9782; -.
DR Pharos; P43243; Tbio.
DR PRO; PR:P43243; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; P43243; protein.
DR Bgee; ENSG00000015479; Expressed in cortical plate and 104 other tissues.
DR ExpressionAtlas; P43243; baseline and differential.
DR Genevisible; P43243; HS.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005637; C:nuclear inner membrane; TAS:ProtInc.
DR GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0035198; F:miRNA binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0005198; F:structural molecule activity; TAS:ProtInc.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0002218; P:activation of innate immune response; IDA:UniProtKB.
DR GO; GO:0001825; P:blastocyst formation; IEA:Ensembl.
DR GO; GO:0003170; P:heart valve development; ISS:BHF-UCL.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0010608; P:post-transcriptional regulation of gene expression; IDA:CACAO.
DR GO; GO:0003281; P:ventricular septum development; ISS:BHF-UCL.
DR CDD; cd12714; RRM1_MATR3; 1.
DR CDD; cd12715; RRM2_MATR3; 1.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR034928; MATR3_RRM1.
DR InterPro; IPR034930; MATR3_RRM2.
DR InterPro; IPR000690; Matrin/U1-C_Znf_C2H2.
DR InterPro; IPR003604; Matrin/U1-like-C_Znf_C2H2.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR SMART; SM00360; RRM; 2.
DR SMART; SM00451; ZnF_U1; 2.
DR SUPFAM; SSF54928; SSF54928; 2.
DR PROSITE; PS50102; RRM; 2.
DR PROSITE; PS50171; ZF_MATRIN; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Amyotrophic lateral sclerosis;
KW Direct protein sequencing; Disease variant; Immunity; Innate immunity;
KW Isopeptide bond; Metal-binding; Neurodegeneration; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; RNA-binding; Ubl conjugation; Zinc;
KW Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.7, ECO:0007744|PubMed:22814378"
FT CHAIN 2..847
FT /note="Matrin-3"
FT /id="PRO_0000081622"
FT DOMAIN 398..473
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 496..571
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT ZN_FING 801..832
FT /note="Matrin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00130"
FT REGION 146..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 187..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 342..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 588..786
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 710..718
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 588..647
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 648..664
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 690..735
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 749..777
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|Ref.7, ECO:0007744|PubMed:22814378"
FT MOD_RES 3
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 126
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 150
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 157
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 158
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 164
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 188
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:17924679, ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 195
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 202
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 206
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 208
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 211
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 219
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 234
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 264
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 275
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 509
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 511
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 522
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 533
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 571
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 596
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 598
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 604
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 606
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 654
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 671
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 673
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 674
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 679
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 689
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 741
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 747
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 759
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43244"
FT MOD_RES 766
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 836
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT CROSSLNK 3
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733"
FT CROSSLNK 132
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 146
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 245
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 269
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 478
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 487
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 491
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 515
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 522
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 554
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 555
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 617
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733"
FT CROSSLNK 630
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 719
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 736
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 770
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 836
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..304
FT /note="MSKSFQQSSLSRDSQGHGRDLSAAGIGLLAAATQSLSMPASLGRMNQGTARL
FT ASLMNLGMSSSLNQQGAHSALSSASTSSHNLQSIFNIGSRGPLPLSSQHRGDADQASNI
FT LASFGLSARDLDELSRYPEDKITPENLPQILLQLKRRRTEEGPTLSYGRDGRSATREPP
FT YRVPRDDWEEKRHFRRDSFDDRGPSLNPVLDYDHGSRSQESGYYDRMDYEDDRLRDGER
FT CRDDSFFGETSHNYHKFDSEYERMGRGPGPLQERSLFEKKRGAPPSSNIEDFHGLLPKG
FT YPHLCSICDLPVHSNK -> MLGAQWRRNQPSRAAE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042624"
FT VARIANT 72
FT /note="A -> T (in ALS21; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:25771394"
FT /id="VAR_074067"
FT VARIANT 85
FT /note="S -> C (in ALS21; results in increased interaction
FT with TARDBP; dbSNP:rs121434591)"
FT /evidence="ECO:0000269|PubMed:19344878,
FT ECO:0000269|PubMed:24686783"
FT /id="VAR_063421"
FT VARIANT 89
FT /note="I -> V (in dbSNP:rs528548235)"
FT /evidence="ECO:0000269|PubMed:25771394"
FT /id="VAR_074068"
FT VARIANT 115
FT /note="F -> C (in ALS21; dbSNP:rs587777300)"
FT /evidence="ECO:0000269|PubMed:24686783"
FT /id="VAR_071078"
FT VARIANT 147
FT /note="R -> W (in ALS21; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:26199109"
FT /id="VAR_078513"
FT VARIANT 154
FT /note="P -> S (in ALS21; unknown pathological significance;
FT dbSNP:rs587777302)"
FT /evidence="ECO:0000269|PubMed:24686783"
FT /id="VAR_071079"
FT VARIANT 622
FT /note="T -> A (in ALS21; dbSNP:rs587777301)"
FT /evidence="ECO:0000269|PubMed:24686783"
FT /id="VAR_071080"
FT VARIANT 664
FT /note="E -> A (in dbSNP:rs139589527)"
FT /evidence="ECO:0000269|PubMed:25771394"
FT /id="VAR_074069"
FT VARIANT 787
FT /note="N -> S (in dbSNP:rs148402819)"
FT /evidence="ECO:0000269|PubMed:25771394"
FT /id="VAR_074070"
FT CONFLICT 257
FT /note="P -> S (in Ref. 2; AAF17217)"
FT /evidence="ECO:0000305"
FT CONFLICT 274
FT /note="P -> S (in Ref. 2; AAF17217)"
FT /evidence="ECO:0000305"
FT CONFLICT 572
FT /note="Y -> C (in Ref. 2; AAF17217 and 8; M63483)"
FT /evidence="ECO:0000305"
FT CONFLICT 691
FT /note="G -> P (in Ref. 8; M63483)"
FT /evidence="ECO:0000305"
FT CONFLICT 703
FT /note="D -> H (in Ref. 8; M63483)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 847 AA; 94623 MW; 530AA49214BC1611 CRC64;
MSKSFQQSSL SRDSQGHGRD LSAAGIGLLA AATQSLSMPA SLGRMNQGTA RLASLMNLGM
SSSLNQQGAH SALSSASTSS HNLQSIFNIG SRGPLPLSSQ HRGDADQASN ILASFGLSAR
DLDELSRYPE DKITPENLPQ ILLQLKRRRT EEGPTLSYGR DGRSATREPP YRVPRDDWEE
KRHFRRDSFD DRGPSLNPVL DYDHGSRSQE SGYYDRMDYE DDRLRDGERC RDDSFFGETS
HNYHKFDSEY ERMGRGPGPL QERSLFEKKR GAPPSSNIED FHGLLPKGYP HLCSICDLPV
HSNKEWSQHI NGASHSRRCQ LLLEIYPEWN PDNDTGHTMG DPFMLQQSTN PAPGILGPPP
PSFHLGGPAV GPRGNLGAGN GNLQGPRHMQ KGRVETSRVV HIMDFQRGKN LRYQLLQLVE
PFGVISNHLI LNKINEAFIE MATTEDAQAA VDYYTTTPAL VFGKPVRVHL SQKYKRIKKP
EGKPDQKFDQ KQELGRVIHL SNLPHSGYSD SAVLKLAEPY GKIKNYILMR MKSQAFIEME
TREDAMAMVD HCLKKALWFQ GRCVKVDLSE KYKKLVLRIP NRGIDLLKKD KSRKRSYSPD
GKESPSDKKS KTDGSQKTES STEGKEQEEK SGEDGEKDTK DDQTEQEPNM LLESEDELLV
DEEEAAALLE SGSSVGDETD LANLGDVASD GKKEPSDKAV KKDGSASAAA KKKLKKVDKI
EELDQENEAA LENGIKNEEN TEPGAESSEN ADDPNKDTSE NADGQSDENK DDYTIPDEYR
IGPYQPNVPV GIDYVIPKTG FYCKLCSLFY TNEEVAKNTH CSSLPHYQKL KKFLNKLAEE
RRQKKET
