ID EXOSX_HUMAN Reviewed; 885 AA.
AC Q01780; B1AKQ0; B1AKQ1; Q15158;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 27-MAR-2024, entry version 231.
DE RecName: Full=Exosome complex component 10 {ECO:0000305};
DE EC=3.1.13.- {ECO:0000269|PubMed:21705430};
DE AltName: Full=Autoantigen PM/Scl 2;
DE AltName: Full=P100 polymyositis-scleroderma overlap syndrome-associated autoantigen;
DE AltName: Full=Polymyositis/scleroderma autoantigen 100 kDa;
DE Short=PM/Scl-100;
DE AltName: Full=Polymyositis/scleroderma autoantigen 2;
GN Name=EXOSC10 {ECO:0000312|HGNC:HGNC:9138};
GN Synonyms=PMSCL, PMSCL2, RRP6 {ECO:0000303|PubMed:26166824};
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).
RC TISSUE=Placenta;
RX PubMed=1383382; DOI=10.1084/jem.176.4.973;
RA Bluethner M., Bautz F.A.;
RT "Cloning and characterization of the cDNA coding for a polymyositis-
RT scleroderma overlap syndrome-related nucleolar 100-kD protein.";
RL J. Exp. Med. 176:973-980(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Thymocyte;
RX PubMed=1644924; DOI=10.1172/jci115895;
RA Ge Q., Frank M.B., O'Brien C., Targoff I.N.;
RT "Cloning of a complementary DNA coding for the 100-kD antigenic protein of
RT the PM-Scl autoantigen.";
RL J. Clin. Invest. 90:559-570(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2).
RX PubMed=11426320; DOI=10.1038/sj.gene.6363745;
RA Stover C., Endo Y., Takahashi M., Lynch N., Constantinescu C.,
RA Vorup-Jensen T., Thiel S., Friedl H., Hankeln T., Hall R., Gregory S.,
RA Fujita T., Schwaeble W.;
RT "The human gene for mannan-binding lectin-associated serine protease-2
RT (MASP-2), the effector component of the lectin route of complement
RT activation, is part of a tightly linked gene cluster on chromosome 1p36.2-
RT 3.";
RL Genes Immun. 2:119-127(2001).
RN [4]
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 [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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lymph, and 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 CHARACTERIZATION.
RX PubMed=10465791; DOI=10.1101/gad.13.16.2148;
RA Allmang C., Petfalski E., Podtelejnikov A., Mann M., Tollervey D.,
RA Mitchell P.;
RT "The yeast exosome and human PM-Scl are related complexes of 3'-->5'
RT exonucleases.";
RL Genes Dev. 13:2148-2158(1999).
RN [8]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=12429849; DOI=10.1091/mbc.e02-05-0271;
RA Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C.,
RA Greco A., Hochstrasser D.F., Diaz J.-J.;
RT "Functional proteomic analysis of human nucleolus.";
RL Mol. Biol. Cell 13:4100-4109(2002).
RN [9]
RP FUNCTION IN NONSENSE-MEDIATED MRNA DECAY, AND SUBCELLULAR LOCATION.
RX PubMed=14527413; DOI=10.1016/s1097-2765(03)00349-6;
RA Lejeune F., Li X., Maquat L.E.;
RT "Nonsense-mediated mRNA decay in mammalian cells involves decapping,
RT deadenylating, and exonucleolytic activities.";
RL Mol. Cell 12:675-687(2003).
RN [10]
RP PROTEIN INTERACTION.
RX PubMed=15231747; DOI=10.1101/gr.2122004;
RA Lehner B., Sanderson C.M.;
RT "A protein interaction framework for human mRNA degradation.";
RL Genome Res. 14:1315-1323(2004).
RN [11]
RP INTERACTION WITH DHX36.
RX PubMed=14731398; DOI=10.1016/s1097-2765(03)00481-7;
RA Tran H., Schilling M., Wirbelauer C., Hess D., Nagamine Y.;
RT "Facilitation of mRNA deadenylation and decay by the exosome-bound, DExH
RT protein RHAU.";
RL Mol. Cell 13:101-111(2004).
RN [12]
RP FUNCTION IN NUCLEAR PRE-MRNA DEGRADATION.
RX PubMed=16455498; DOI=10.1016/j.molcel.2005.12.008;
RA West S., Gromak N., Norbury C.J., Proudfoot N.J.;
RT "Adenylation and exosome-mediated degradation of cotranscriptionally
RT cleaved pre-messenger RNA in human cells.";
RL Mol. Cell 21:437-443(2006).
RN [13]
RP INTERACTION WITH ALYREF.
RX PubMed=17234882; DOI=10.1101/gad.1503107;
RA Yoh S.M., Cho H., Pickle L., Evans R.M., Jones K.A.;
RT "The Spt6 SH2 domain binds Ser2-P RNAPII to direct Iws1-dependent mRNA
RT splicing and export.";
RL Genes Dev. 21:160-174(2007).
RN [14]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH C1D AND MPHOSPH6.
RX PubMed=17412707; DOI=10.1093/nar/gkm082;
RA Schilders G., van Dijk E., Pruijn G.J.M.;
RT "C1D and hMtr4p associate with the human exosome subunit PM/Scl-100 and are
RT involved in pre-rRNA processing.";
RL Nucleic Acids Res. 35:2564-2572(2007).
RN [15]
RP FUNCTION IN MRNA DEGRADATION, AND SUBCELLULAR LOCATION.
RX PubMed=17545563; DOI=10.1261/rna.575107;
RA van Dijk E.L., Schilders G., Pruijn G.J.;
RT "Human cell growth requires a functional cytoplasmic exosome, which is
RT involved in various mRNA decay pathways.";
RL RNA 13:1027-1035(2007).
RN [16]
RP FUNCTION IN HISTONE MRNA DEGRADATION ACTIVITY.
RX PubMed=18172165; DOI=10.1101/gad.1622708;
RA Mullen T.E., Marzluff W.F.;
RT "Degradation of histone mRNA requires oligouridylation followed by
RT decapping and simultaneous degradation of the mRNA both 5' to 3' and 3' to
RT 5'.";
RL Genes Dev. 22:50-65(2008).
RN [17]
RP FUNCTION IN PROMPT DEGRADATION.
RX PubMed=19056938; DOI=10.1126/science.1164096;
RA Preker P., Nielsen J., Kammler S., Lykke-Andersen S., Christensen M.S.,
RA Mapendano C.K., Schierup M.H., Jensen T.H.;
RT "RNA exosome depletion reveals transcription upstream of active human
RT promoters.";
RL Science 322:1851-1854(2008).
RN [18]
RP ASSOCIATION WITH THE RNA EXOSOME COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=20531386; DOI=10.1038/emboj.2010.121;
RA Tomecki R., Kristiansen M.S., Lykke-Andersen S., Chlebowski A.,
RA Larsen K.M., Szczesny R.J., Drazkowska K., Pastula A., Andersen J.S.,
RA Stepien P.P., Dziembowski A., Jensen T.H.;
RT "The human core exosome interacts with differentially localized processive
RT RNases: hDIS3 and hDIS3L.";
RL EMBO J. 29:2342-2357(2010).
RN [19]
RP IDENTIFICATION IN THE RNA EXOSOME COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=20531389; DOI=10.1038/emboj.2010.122;
RA Staals R.H., Bronkhorst A.W., Schilders G., Slomovic S., Schuster G.,
RA Heck A.J., Raijmakers R., Pruijn G.J.;
RT "Dis3-like 1: a novel exoribonuclease associated with the human exosome.";
RL EMBO J. 29:2358-2367(2010).
RN [20]
RP FUNCTION IN NUCLEAR MRNA SURVEILLANCE.
RX PubMed=20699273; DOI=10.1093/nar/gkq703;
RA de Almeida S.F., Garcia-Sacristan A., Custodio N., Carmo-Fonseca M.;
RT "A link between nuclear RNA surveillance, the human exosome and RNA
RT polymerase II transcriptional termination.";
RL Nucleic Acids Res. 38:8015-8026(2010).
RN [21]
RP FUNCTION IN RRNA MATURATION.
RX PubMed=20368444; DOI=10.1073/pnas.0910621107;
RA Slomovic S., Fremder E., Staals R.H., Pruijn G.J., Schuster G.;
RT "Addition of poly(A) and poly(A)-rich tails during RNA degradation in the
RT cytoplasm of human cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:7407-7412(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-821, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [24]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-583, 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 [25]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-583, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [26]
RP IDENTIFICATION IN THE RNA EXOSOME COMPLEX.
RX PubMed=26166824; DOI=10.1016/j.bbrc.2015.07.032;
RA Yoshikatsu Y., Ishida Y., Sudo H., Yuasa K., Tsuji A., Nagahama M.;
RT "NVL2, a nucleolar AAA-ATPase, is associated with the nuclear exosome and
RT is involved in pre-rRNA processing.";
RL Biochem. Biophys. Res. Commun. 464:780-786(2015).
RN [27]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-826, AND IDENTIFICATION BY MASS
RP 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 [28] {ECO:0000305}
RP FUNCTION.
RX PubMed=25632158; DOI=10.1242/jcs.158733;
RA Marin-Vicente C., Domingo-Prim J., Eberle A.B., Visa N.;
RT "RRP6/EXOSC10 is required for the repair of DNA double-strand breaks by
RT homologous recombination.";
RL J. Cell Sci. 128:1097-1107(2015).
RN [29] {ECO:0000305}
RP FUNCTION, INDUCTION, SUMOYLATION, AND MUTAGENESIS OF LYS-168; LYS-201 AND
RP LYS-583.
RX PubMed=26857222; DOI=10.1261/rna.054411.115;
RA Knight J.R., Bastide A., Peretti D., Roobol A., Roobol J., Mallucci G.R.,
RA Smales C.M., Willis A.E.;
RT "Cooling-induced SUMOylation of EXOSC10 down-regulates ribosome
RT biogenesis.";
RL RNA 22:623-635(2016).
RN [30]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-19; LYS-583; LYS-710; LYS-826;
RP LYS-833; LYS-859 AND LYS-873, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [31] {ECO:0000305}
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=31086179; DOI=10.1038/s41467-019-10153-9;
RA Domingo-Prim J., Endara-Coll M., Bonath F., Jimeno S., Prados-Carvajal R.,
RA Friedlaender M.R., Huertas P., Visa N.;
RT "EXOSC10 is required for RPA assembly and controlled DNA end resection at
RT DNA double-strand breaks.";
RL Nat. Commun. 10:2135-2135(2019).
RN [32]
RP INTERACTION WITH NRDE2.
RX PubMed=30538148; DOI=10.1261/rna.069773.118;
RA Jiao A.L., Perales R., Umbreit N.T., Haswell J.R., Piper M.E., Adams B.D.,
RA Pellman D., Kennedy S., Slack F.J.;
RT "Human nuclear RNAi-defective 2 (NRDE2) is an essential RNA splicing
RT factor.";
RL RNA 25:352-363(2019).
RN [33] {ECO:0000305}
RP FUNCTION, ACTIVITY REGULATION, AND SUBCELLULAR LOCATION.
RX PubMed=32830871; DOI=10.15252/embj.2019102700;
RA Kawabe Y., Mori K., Yamashita T., Gotoh S., Ikeda M.;
RT "The RNA exosome complex degrades expanded hexanucleotide repeat RNA in
RT C9orf72 FTLD/ALS.";
RL EMBO J. 39:e102700-e102700(2020).
RN [34] {ECO:0000305}
RP FUNCTION, INTERACTION WITH USP36, SUBCELLULAR LOCATION, SUMOYLATION, AND
RP MUTAGENESIS OF LYS-19; LYS-168; LYS-583; LYS-710; LYS-826; LYS-833; LYS-859
RP AND LYS-873.
RX PubMed=36912080; DOI=10.1093/nar/gkad140;
RA Chen Y., Li Y., Dai R.S., Savage J.C., Shinde U., Klimek J., David L.L.,
RA Young E.A., Hafner M., Sears R.C., Sun X.X., Dai M.S.;
RT "The ubiquitin-specific protease USP36 SUMOylates EXOSC10 and promotes the
RT nucleolar RNA exosome function in rRNA processing.";
RL Nucleic Acids Res. 51:3934-3949(2023).
RN [35]
RP STRUCTURE BY NMR OF 483-593.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the HRDC domain of human exosome component 10.";
RL Submitted (NOV-2005) to the PDB data bank.
RN [36] {ECO:0007744|PDB:3SAF, ECO:0007744|PDB:3SAG, ECO:0007744|PDB:3SAH}
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 180-606 OF MUTANTS ASN-313 AND
RP ALA-436 IN COMPLEX WITH MAGNESIUM, CATALYTIC ACTIVITY, COFACTOR, AND
RP MUTAGENESIS OF ASP-313; GLU-315; HIS-316; ASP-371; ASP-404 AND TYR-436.
RX PubMed=21705430; DOI=10.1261/rna.2763111;
RA Januszyk K., Liu Q., Lima C.D.;
RT "Activities of human RRP6 and structure of the human RRP6 catalytic
RT domain.";
RL RNA 17:1566-1577(2011).
RN [37] {ECO:0007744|PDB:6D6Q, ECO:0007744|PDB:6D6R}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.45 ANGSTROMS), AND SUBUNIT.
RX PubMed=29906447; DOI=10.1016/j.cell.2018.05.041;
RA Weick E.M., Puno M.R., Januszyk K., Zinder J.C., DiMattia M.A., Lima C.D.;
RT "Helicase-Dependent RNA Decay Illuminated by a Cryo-EM Structure of a Human
RT Nuclear RNA Exosome-MTR4 Complex.";
RL Cell 173:1663-1677.e21(2018).
RN [38] {ECO:0007744|PDB:7MQA}
RP STRUCTURE BY ELECTRON MICROSCOPY (2.70 ANGSTROMS), FUNCTION, SUBCELLULAR
RP LOCATION, AND SUBUNIT.
RX PubMed=34516797; DOI=10.1126/science.abj5338;
RA Singh S., Vanden Broeck A., Miller L., Chaker-Margot M., Klinge S.;
RT "Nucleolar maturation of the human small subunit processome.";
RL Science 373:eabj5338-eabj5338(2021).
CC -!- FUNCTION: Catalytic component of the RNA exosome complex which has
CC 3'->5' exoribonuclease activity and participates in a multitude of
CC cellular RNA processing and degradation events. In the nucleus, the RNA
CC exosome complex is involved in proper maturation of stable RNA species
CC such as rRNA, snRNA and snoRNA, in the elimination of RNA processing
CC by-products and non-coding 'pervasive' transcripts, such as antisense
CC RNA species and promoter-upstream transcripts (PROMPTs), and of mRNAs
CC with processing defects, thereby limiting or excluding their export to
CC the cytoplasm. Part of the small subunit (SSU) processome, first
CC precursor of the small eukaryotic ribosomal subunit. During the
CC assembly of the SSU processome in the nucleolus, many ribosome
CC biogenesis factors, an RNA chaperone and ribosomal proteins associate
CC with the nascent pre-rRNA and work in concert to generate RNA folding,
CC modifications, rearrangements and cleavage as well as targeted
CC degradation of pre-ribosomal RNA by the RNA exosome (PubMed:34516797).
CC The RNA exosome may be involved in Ig class switch recombination (CSR)
CC and/or Ig variable region somatic hypermutation (SHM) by targeting
CC AICDA deamination activity to transcribed dsDNA substrates. In the
CC cytoplasm, the RNA exosome complex is involved in general mRNA turnover
CC and specifically degrades inherently unstable mRNAs containing AU-rich
CC elements (AREs) within their 3' untranslated regions, and in RNA
CC surveillance pathways, preventing translation of aberrant mRNAs. It
CC seems to be involved in degradation of histone mRNA. EXOSC10 is
CC required for nucleolar localization of C1D and probably mediates the
CC association of MTREX, C1D and MPHOSPH6 with the RNA exosome involved in
CC the maturation of 5.8S rRNA. Plays a role in the recruitment of
CC replication protein A complex (RPA) and RAD51 to DNA double-strand
CC breaks caused by irradiation, contributing to DNA repair by homologous
CC recombination (PubMed:31086179, PubMed:25632158). Regulates levels of
CC damage-induced RNAs in order to prevent DNA-RNA hybrid formation at DNA
CC double-strand breaks and limit DNA end resection after damage
CC (PubMed:31086179). Plays a role in oocyte development, maturation and
CC survival (By similarity). Required for normal testis development and
CC mitotic division of spermatogonia (By similarity). Plays a role in
CC proper embryo development (By similarity). Required for global protein
CC translation (PubMed:36912080, PubMed:26857222). Required for cell
CC proliferation (PubMed:36912080). Regulates metabolism of C9orf72-
CC derived repeat RNA that can be translated into toxic dipeptide repeat
CC proteins (PubMed:32830871). {ECO:0000250|UniProtKB:P56960,
CC ECO:0000269|PubMed:14527413, ECO:0000269|PubMed:16455498,
CC ECO:0000269|PubMed:17412707, ECO:0000269|PubMed:17545563,
CC ECO:0000269|PubMed:18172165, ECO:0000269|PubMed:19056938,
CC ECO:0000269|PubMed:20368444, ECO:0000269|PubMed:20699273,
CC ECO:0000269|PubMed:25632158, ECO:0000269|PubMed:26857222,
CC ECO:0000269|PubMed:31086179, ECO:0000269|PubMed:32830871,
CC ECO:0000269|PubMed:34516797, ECO:0000269|PubMed:36912080}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:21705430};
CC -!- ACTIVITY REGULATION: Arginine-rich dipeptide repeat proteins expressed
CC from C9orf72-derived repeat RNA interact with EXOSC10 and inhibit its
CC ability to promote degradation of this RNA.
CC {ECO:0000269|PubMed:32830871}.
CC -!- SUBUNIT: Component of the RNA exosome complex (PubMed:20531389,
CC PubMed:26166824, PubMed:29906447). The catalytically inactive RNA
CC exosome core (Exo-9) complex is believed to associate with catalytic
CC subunits EXOSC10, and DIS3 or DIS3L in cytoplasmic- and nuclear-
CC specific RNA exosome complex forms (PubMed:20531389). Part of the small
CC subunit (SSU) processome, composed of more than 70 proteins and the RNA
CC chaperone small nucleolar RNA (snoRNA) U3 (PubMed:34516797). Interacts
CC with C1D and MPHOSPH6 (PubMed:17412707). Interacts with ALYREF/THOC4
CC (PubMed:17234882). Interacts with MTREX; the interaction mediates the
CC association of MTREX with nuclear RNA exosomes (PubMed:26166824).
CC Interacts with DHX36; this interaction occurs in a RNase-insensitive
CC manner (PubMed:14731398). Interacts with NRDE2 (PubMed:30538148).
CC Interacts (via C-terminus) with USP36 (via C-terminus); the interaction
CC is facilitated by the association with RNA and promotes sumoylation of
CC EXOSC10 (PubMed:36912080). {ECO:0000269|PubMed:14731398,
CC ECO:0000269|PubMed:17234882, ECO:0000269|PubMed:17412707,
CC ECO:0000269|PubMed:20531389, ECO:0000269|PubMed:26166824,
CC ECO:0000269|PubMed:29906447, ECO:0000269|PubMed:30538148,
CC ECO:0000269|PubMed:34516797, ECO:0000269|PubMed:36912080}.
CC -!- INTERACTION:
CC Q01780; Q13901: C1D; NbExp=5; IntAct=EBI-358236, EBI-3844053;
CC Q01780; P17844: DDX5; NbExp=3; IntAct=EBI-358236, EBI-351962;
CC Q01780; Q9Y2L1: DIS3; NbExp=4; IntAct=EBI-358236, EBI-373539;
CC Q01780; Q9NPD3: EXOSC4; NbExp=5; IntAct=EBI-358236, EBI-371823;
CC Q01780; Q9NQT4: EXOSC5; NbExp=4; IntAct=EBI-358236, EBI-371876;
CC Q01780; Q99547: MPHOSPH6; NbExp=4; IntAct=EBI-358236, EBI-373187;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20531386}. Nucleus
CC {ECO:0000269|PubMed:36912080}. Nucleus, nucleolus
CC {ECO:0000269|PubMed:20531386, ECO:0000269|PubMed:31086179,
CC ECO:0000269|PubMed:32830871, ECO:0000269|PubMed:34516797,
CC ECO:0000269|PubMed:36912080}. Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:32830871, ECO:0000269|PubMed:36912080}.
CC Note=Strongly enriched in the nucleolus and a small amount has been
CC found in cytoplasm supporting the existence of a nucleolar RNA exosome
CC complex form (PubMed:20531386, PubMed:34516797). Arginine-rich
CC dipeptide repeat proteins expressed from C9orf72-derived repeat RNA
CC cause diffuse nuclear misdistribution of EXOSC10 (PubMed:32830871).
CC Relocates to the DNA double-strand breaks in response to irradiation
CC (PubMed:31086179). {ECO:0000269|PubMed:20531386,
CC ECO:0000269|PubMed:31086179, ECO:0000269|PubMed:32830871,
CC ECO:0000269|PubMed:34516797}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q01780-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q01780-2; Sequence=VSP_004362;
CC -!- INDUCTION: Down-regulated by mild hypothermia (at protein level).
CC {ECO:0000269|PubMed:26857222}.
CC -!- PTM: Sumoylated by USP36; sumoylation does not significantly affect
CC EXOSC10 nucleolar localization and association with core exosome and
CC USP36, but regulates the nucleolar RNA exosome activity in rRNA
CC processing by promoting binding of EXOSC10 to pre-rRNAs
CC (PubMed:36912080). Effects of sumoylation on EXOSC10 levels vary
CC between different studies (PubMed:26857222, PubMed:36912080).
CC Sumoylation of EXOSC10 is required for the modulation of EXOSC10
CC effects on cellular protein translation and cell proliferation
CC (PubMed:36912080). Sumoylation is promoted by mild hypothermia
CC (PubMed:26857222). {ECO:0000269|PubMed:26857222,
CC ECO:0000269|PubMed:36912080}.
CC -!- SIMILARITY: Belongs to the exosome component 10/RRP6 family.
CC {ECO:0000305}.
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DR EMBL; X66113; CAA46904.1; -; mRNA.
DR EMBL; L01457; AAB59352.1; -; mRNA.
DR EMBL; AJ300188; CAC15569.1; -; Genomic_DNA.
DR EMBL; AL109811; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471130; EAW71679.1; -; Genomic_DNA.
DR EMBL; BC039901; AAH39901.1; -; mRNA.
DR EMBL; BC073788; AAH73788.1; -; mRNA.
DR CCDS; CCDS126.1; -. [Q01780-2]
DR CCDS; CCDS30584.1; -. [Q01780-1]
DR PIR; A43920; A43920.
DR PIR; JH0796; JH0796.
DR RefSeq; NP_001001998.1; NM_001001998.2. [Q01780-1]
DR RefSeq; NP_002676.1; NM_002685.3. [Q01780-2]
DR PDB; 2CPR; NMR; -; A=483-593.
DR PDB; 3SAF; X-ray; 2.50 A; A/B=180-606.
DR PDB; 3SAG; X-ray; 2.70 A; A/B=180-606.
DR PDB; 3SAH; X-ray; 2.65 A; A/B=180-606.
DR PDB; 6D6Q; EM; 3.45 A; J=1-648, J=705-804.
DR PDB; 6D6R; EM; 3.45 A; J=1-648, J=705-804.
DR PDB; 7MQA; EM; 2.70 A; NV=1-885.
DR PDBsum; 2CPR; -.
DR PDBsum; 3SAF; -.
DR PDBsum; 3SAG; -.
DR PDBsum; 3SAH; -.
DR PDBsum; 6D6Q; -.
DR PDBsum; 6D6R; -.
DR PDBsum; 7MQA; -.
DR AlphaFoldDB; Q01780; -.
DR EMDB; EMD-0127; -.
DR EMDB; EMD-14515; -.
DR EMDB; EMD-23938; -.
DR EMDB; EMD-7808; -.
DR EMDB; EMD-7809; -.
DR EMDB; EMD-7818; -.
DR EMDB; EMD-7819; -.
DR SMR; Q01780; -.
DR BioGRID; 111403; 212.
DR ComplexPortal; CPX-476; Nuclear exosome complex, DIS3-EXOSC10 variant.
DR ComplexPortal; CPX-591; Nucleolar exosome complex, EXOSC10 variant.
DR ComplexPortal; CPX-600; Cytoplasmic exosome complex, DIS3L-EXOSC10 variant.
DR CORUM; Q01780; -.
DR DIP; DIP-31249N; -.
DR IntAct; Q01780; 88.
DR MINT; Q01780; -.
DR STRING; 9606.ENSP00000366135; -.
DR GlyGen; Q01780; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q01780; -.
DR MetOSite; Q01780; -.
DR PhosphoSitePlus; Q01780; -.
DR SwissPalm; Q01780; -.
DR BioMuta; EXOSC10; -.
DR DMDM; 8928564; -.
DR SWISS-2DPAGE; Q01780; -.
DR EPD; Q01780; -.
DR jPOST; Q01780; -.
DR MassIVE; Q01780; -.
DR MaxQB; Q01780; -.
DR PaxDb; 9606-ENSP00000366135; -.
DR PeptideAtlas; Q01780; -.
DR ProteomicsDB; 57986; -. [Q01780-1]
DR ProteomicsDB; 57987; -. [Q01780-2]
DR Pumba; Q01780; -.
DR Antibodypedia; 13683; 228 antibodies from 30 providers.
DR DNASU; 5394; -.
DR Ensembl; ENST00000304457.11; ENSP00000307307.7; ENSG00000171824.14. [Q01780-2]
DR Ensembl; ENST00000376936.9; ENSP00000366135.4; ENSG00000171824.14. [Q01780-1]
DR GeneID; 5394; -.
DR KEGG; hsa:5394; -.
DR MANE-Select; ENST00000376936.9; ENSP00000366135.4; NM_001001998.3; NP_001001998.1.
DR UCSC; uc001asa.4; human. [Q01780-1]
DR AGR; HGNC:9138; -.
DR CTD; 5394; -.
DR DisGeNET; 5394; -.
DR GeneCards; EXOSC10; -.
DR HGNC; HGNC:9138; EXOSC10.
DR HPA; ENSG00000171824; Low tissue specificity.
DR MIM; 605960; gene.
DR neXtProt; NX_Q01780; -.
DR OpenTargets; ENSG00000171824; -.
DR PharmGKB; PA33464; -.
DR VEuPathDB; HostDB:ENSG00000171824; -.
DR eggNOG; KOG2206; Eukaryota.
DR GeneTree; ENSGT00390000015408; -.
DR HOGENOM; CLU_010129_1_1_1; -.
DR InParanoid; Q01780; -.
DR OMA; NIMRPQM; -.
DR OrthoDB; 2880475at2759; -.
DR PhylomeDB; Q01780; -.
DR TreeFam; TF105991; -.
DR PathwayCommons; Q01780; -.
DR Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR SignaLink; Q01780; -.
DR SIGNOR; Q01780; -.
DR BioGRID-ORCS; 5394; 505 hits in 1167 CRISPR screens.
DR ChiTaRS; EXOSC10; human.
DR EvolutionaryTrace; Q01780; -.
DR GeneWiki; Exosome_component_10; -.
DR GenomeRNAi; 5394; -.
DR Pharos; Q01780; Tbio.
DR PRO; PR:Q01780; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q01780; Protein.
DR Bgee; ENSG00000171824; Expressed in cerebellar hemisphere and 203 other cell types or tissues.
DR ExpressionAtlas; Q01780; baseline and differential.
DR Genevisible; Q01780; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0000177; C:cytoplasmic exosome (RNase complex); NAS:ComplexPortal.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0000791; C:euchromatin; IMP:UniProtKB.
DR GO; GO:0000178; C:exosome (RNase complex); IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0000176; C:nuclear exosome (RNase complex); IDA:UniProtKB.
DR GO; GO:0101019; C:nucleolar exosome (RNase complex); NAS:ComplexPortal.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032040; C:small-subunit processome; IDA:UniProtKB.
DR GO; GO:0000175; F:3'-5'-RNA exonuclease activity; IMP:BHF-UCL.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0004532; F:RNA exonuclease activity; IDA:UniProtKB.
DR GO; GO:0003727; F:single-stranded RNA binding; IBA:GO_Central.
DR GO; GO:0070034; F:telomerase RNA binding; IC:BHF-UCL.
DR GO; GO:0071034; P:CUT catabolic process; IMP:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0000467; P:exonucleolytic trimming to generate mature 3'-end of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR GO; GO:0071044; P:histone mRNA catabolic process; IMP:UniProtKB.
DR GO; GO:0000460; P:maturation of 5.8S rRNA; IMP:UniProtKB.
DR GO; GO:0032211; P:negative regulation of telomere maintenance via telomerase; IMP:BHF-UCL.
DR GO; GO:0071028; P:nuclear mRNA surveillance; IMP:UniProtKB.
DR GO; GO:0071040; P:nuclear polyadenylation-dependent antisense transcript catabolic process; IBA:GO_Central.
DR GO; GO:0071039; P:nuclear polyadenylation-dependent CUT catabolic process; IBA:GO_Central.
DR GO; GO:0071035; P:nuclear polyadenylation-dependent rRNA catabolic process; IMP:UniProtKB.
DR GO; GO:0071036; P:nuclear polyadenylation-dependent snoRNA catabolic process; IBA:GO_Central.
DR GO; GO:0071037; P:nuclear polyadenylation-dependent snRNA catabolic process; IBA:GO_Central.
DR GO; GO:0071038; P:nuclear polyadenylation-dependent tRNA catabolic process; IBA:GO_Central.
DR GO; GO:0000956; P:nuclear-transcribed mRNA catabolic process; IMP:UniProtKB.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:UniProtKB-KW.
DR GO; GO:0071051; P:polyadenylation-dependent snoRNA 3'-end processing; IBA:GO_Central.
DR GO; GO:1905746; P:positive regulation of mRNA cis splicing, via spliceosome; IEA:Ensembl.
DR GO; GO:1904872; P:regulation of telomerase RNA localization to Cajal body; IMP:BHF-UCL.
DR GO; GO:0042274; P:ribosomal small subunit biogenesis; IDA:UniProtKB.
DR GO; GO:0006401; P:RNA catabolic process; IDA:ComplexPortal.
DR GO; GO:0006396; P:RNA processing; IDA:ComplexPortal.
DR GO; GO:0006364; P:rRNA processing; TAS:Reactome.
DR CDD; cd06147; Rrp6p_like_exo; 1.
DR Gene3D; 1.10.150.80; HRDC domain; 1.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR InterPro; IPR002562; 3'-5'_exonuclease_dom.
DR InterPro; IPR012588; Exosome-assoc_fac_Rrp6_N.
DR InterPro; IPR010997; HRDC-like_sf.
DR InterPro; IPR002121; HRDC_dom.
DR InterPro; IPR044876; HRDC_dom_sf.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR045092; Rrp6-like.
DR InterPro; IPR049559; Rrp6p-like_exo.
DR PANTHER; PTHR12124:SF47; EXOSOME COMPONENT 10; 1.
DR PANTHER; PTHR12124; POLYMYOSITIS/SCLERODERMA AUTOANTIGEN-RELATED; 1.
DR Pfam; PF01612; DNA_pol_A_exo1; 1.
DR Pfam; PF00570; HRDC; 1.
DR Pfam; PF08066; PMC2NT; 1.
DR SMART; SM00474; 35EXOc; 1.
DR SMART; SM00341; HRDC; 1.
DR SUPFAM; SSF47819; HRDC-like; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR PROSITE; PS50967; HRDC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; DNA damage; DNA repair;
KW Exonuclease; Exosome; Hydrolase; Isopeptide bond; Magnesium; Metal-binding;
KW Nonsense-mediated mRNA decay; Nuclease; Nucleus; Phosphoprotein;
KW Reference proteome; RNA-binding; rRNA processing; Ubl conjugation.
FT CHAIN 1..885
FT /note="Exosome complex component 10"
FT /id="PRO_0000087133"
FT DOMAIN 289..455
FT /note="3'-5' exonuclease"
FT /evidence="ECO:0000255"
FT DOMAIN 503..583
FT /note="HRDC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00328"
FT REGION 776..885
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 776..814
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 825..846
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 313
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:21705430,
FT ECO:0007744|PDB:3SAF, ECO:0007744|PDB:3SAG,
FT ECO:0007744|PDB:3SAH"
FT BINDING 313
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:21705430,
FT ECO:0007744|PDB:3SAH"
FT BINDING 315
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:21705430,
FT ECO:0007744|PDB:3SAH"
FT BINDING 371
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:21705430,
FT ECO:0007744|PDB:3SAF, ECO:0007744|PDB:3SAG,
FT ECO:0007744|PDB:3SAH"
FT BINDING 440
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:21705430,
FT ECO:0007744|PDB:3SAH"
FT SITE 583
FT /note="Not ubiquitinated"
FT /evidence="ECO:0000269|PubMed:36912080"
FT MOD_RES 821
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 19
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 583
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000269|PubMed:36912080,
FT ECO:0007744|PubMed:25114211"
FT CROSSLNK 583
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000269|PubMed:36912080,
FT ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:28112733"
FT CROSSLNK 710
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 826
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 833
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 859
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 873
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 695..719
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:1644924"
FT /id="VSP_004362"
FT MUTAGEN 19
FT /note="K->R: No effect on sumoylation by USP36."
FT /evidence="ECO:0000269|PubMed:36912080"
FT MUTAGEN 168
FT /note="K->R: No effect on sumoylation by USP36. Reduces
FT sumoylation levels and increases steady-state expression;
FT when associated with R-201 and R-583."
FT /evidence="ECO:0000269|PubMed:26857222,
FT ECO:0000269|PubMed:36912080"
FT MUTAGEN 201
FT /note="K->R: Reduces sumoylation levels and increases
FT steady-state expression; when associated with R-168 and R-
FT 583."
FT /evidence="ECO:0000269|PubMed:26857222"
FT MUTAGEN 313
FT /note="D->N: Abolishes exoribonuclease activity."
FT /evidence="ECO:0000269|PubMed:21705430"
FT MUTAGEN 315
FT /note="E->Q: Abolishes exoribonuclease activity."
FT /evidence="ECO:0000269|PubMed:21705430"
FT MUTAGEN 316
FT /note="H->A: Slightly reduces exoribonuclease activity."
FT /evidence="ECO:0000269|PubMed:21705430"
FT MUTAGEN 371
FT /note="D->N: Abolishes exoribonuclease activity."
FT /evidence="ECO:0000269|PubMed:21705430"
FT MUTAGEN 404
FT /note="D->A: Increases exoribonuclease activity."
FT /evidence="ECO:0000269|PubMed:21705430"
FT MUTAGEN 436
FT /note="Y->A: Significantly reduces exoribonuclease
FT activity."
FT /evidence="ECO:0000269|PubMed:21705430"
FT MUTAGEN 583
FT /note="K->R: Reduces sumoylation by USP36. Significantly
FT attenuates binding to pre-rRNA across the 5.8S-ITS2 and
FT 18S-ITS1 junctions. Reduces sumoylation levels and
FT increases steady-state expression; when associated with R-
FT 168 and R-201."
FT /evidence="ECO:0000269|PubMed:26857222,
FT ECO:0000269|PubMed:36912080"
FT MUTAGEN 710
FT /note="K->R: No effect on sumoylation by USP36."
FT /evidence="ECO:0000269|PubMed:36912080"
FT MUTAGEN 826
FT /note="K->R: No effect on sumoylation by USP36."
FT /evidence="ECO:0000269|PubMed:36912080"
FT MUTAGEN 833
FT /note="K->R: No effect on sumoylation by USP36."
FT /evidence="ECO:0000269|PubMed:36912080"
FT MUTAGEN 859
FT /note="K->R: No effect on sumoylation by USP36."
FT /evidence="ECO:0000269|PubMed:36912080"
FT MUTAGEN 873
FT /note="K->R: No effect on sumoylation by USP36."
FT /evidence="ECO:0000269|PubMed:36912080"
FT HELIX 183..186
FT /evidence="ECO:0007829|PDB:3SAF"
FT STRAND 194..196
FT /evidence="ECO:0007829|PDB:3SAF"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:3SAF"
FT HELIX 218..220
FT /evidence="ECO:0007829|PDB:3SAF"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:3SAF"
FT HELIX 259..263
FT /evidence="ECO:0007829|PDB:3SAF"
FT HELIX 269..272
FT /evidence="ECO:0007829|PDB:3SAF"
FT HELIX 283..285
FT /evidence="ECO:0007829|PDB:3SAF"
FT STRAND 288..291
FT /evidence="ECO:0007829|PDB:3SAF"
FT HELIX 294..304
FT /evidence="ECO:0007829|PDB:3SAF"
FT STRAND 308..317
FT /evidence="ECO:0007829|PDB:3SAF"
FT STRAND 325..332
FT /evidence="ECO:0007829|PDB:3SAF"
FT STRAND 337..341
FT /evidence="ECO:0007829|PDB:3SAF"
FT TURN 342..345
FT /evidence="ECO:0007829|PDB:3SAF"
FT HELIX 346..352
FT /evidence="ECO:0007829|PDB:3SAF"
FT HELIX 353..356
FT /evidence="ECO:0007829|PDB:3SAF"
FT STRAND 361..367
FT /evidence="ECO:0007829|PDB:3SAF"
FT HELIX 369..379
FT /evidence="ECO:0007829|PDB:3SAF"
FT STRAND 384..388
FT /evidence="ECO:0007829|PDB:3SAF"
FT HELIX 389..395
FT /evidence="ECO:0007829|PDB:3SAF"
FT HELIX 403..411
FT /evidence="ECO:0007829|PDB:3SAF"
FT TURN 418..421
FT /evidence="ECO:0007829|PDB:3SAF"
FT HELIX 431..442
FT /evidence="ECO:0007829|PDB:3SAF"
FT HELIX 444..458
FT /evidence="ECO:0007829|PDB:3SAF"
FT STRAND 461..463
FT /evidence="ECO:0007829|PDB:3SAH"
FT HELIX 464..476
FT /evidence="ECO:0007829|PDB:3SAF"
FT HELIX 490..492
FT /evidence="ECO:0007829|PDB:3SAF"
FT HELIX 493..496
FT /evidence="ECO:0007829|PDB:3SAF"
FT STRAND 497..500
FT /evidence="ECO:0007829|PDB:2CPR"
FT HELIX 504..524
FT /evidence="ECO:0007829|PDB:3SAF"
FT HELIX 528..531
FT /evidence="ECO:0007829|PDB:3SAF"
FT HELIX 534..543
FT /evidence="ECO:0007829|PDB:3SAF"
FT HELIX 548..552
FT /evidence="ECO:0007829|PDB:3SAF"
FT STRAND 555..557
FT /evidence="ECO:0007829|PDB:3SAH"
FT HELIX 560..564
FT /evidence="ECO:0007829|PDB:3SAF"
FT HELIX 566..577
FT /evidence="ECO:0007829|PDB:3SAF"
FT HELIX 583..586
FT /evidence="ECO:0007829|PDB:3SAF"
FT STRAND 636..638
FT /evidence="ECO:0007829|PDB:6D6Q"
SQ SEQUENCE 885 AA; 100831 MW; A37BDC8F49BF2E57 CRC64;
MAPPSTREPR VLSATSATKS DGEMVLPGFP DADSFVKFAL GSVVAVTKAS GGLPQFGDEY
DFYRSFPGFQ AFCETQGDRL LQCMSRVMQY HGCRSNIKDR SKVTELEDKF DLLVDANDVI
LERVGILLDE ASGVNKNQQP VLPAGLQVPK TVVSSWNRKA AEYGKKAKSE TFRLLHAKNI
IRPQLKFREK IDNSNTPFLP KIFIKPNAQK PLPQALSKER RERPQDRPED LDVPPALADF
IHQQRTQQVE QDMFAHPYQY ELNHFTPADA VLQKPQPQLY RPIEETPCHF ISSLDELVEL
NEKLLNCQEF AVDLEHHSYR SFLGLTCLMQ ISTRTEDFII DTLELRSDMY ILNESLTDPA
IVKVFHGADS DIEWLQKDFG LYVVNMFDTH QAARLLNLGR HSLDHLLKLY CNVDSNKQYQ
LADWRIRPLP EEMLSYARDD THYLLYIYDK MRLEMWERGN GQPVQLQVVW QRSRDICLKK
FIKPIFTDES YLELYRKQKK HLNTQQLTAF QLLFAWRDKT ARREDESYGY VLPNHMMLKI
AEELPKEPQG IIACCNPVPP LVRQQINEMH LLIQQAREMP LLKSEVAAGV KKSGPLPSAE
RLENVLFGPH DCSHAPPDGY PIIPTSGSVP VQKQASLFPD EKEDNLLGTT CLIATAVITL
FNEPSAEDSK KGPLTVAQKK AQNIMESFEN PFRMFLPSLG HRAPVSQAAK FDPSTKIYEI
SNRWKLAQVQ VQKDSKEAVK KKAAEQTAAR EQAKEACKAA AEQAISVRQQ VVLENAAKKR
ERATSDPRTT EQKQEKKRLK ISKKPKDPEP PEKEFTPYDY SQSDFKAFAG NSKSKVSSQF
DPNKQTPSGK KCIAAKKIKQ SVGNKSMSFP TGKSDRGFRY NWPQR
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