EXOSX_HUMAN
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 03-AUG-2022, entry version 222.
DE RecName: Full=Exosome component 10 {ECO:0000305};
DE EC=3.1.13.-;
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]
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 [29]
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 [30]
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 [31] {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).
CC -!- FUNCTION: Putative catalytic component of the RNA exosome complex which
CC has 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. The RNA exosome may be involved in Ig class switch
CC recombination (CSR) and/or Ig variable region somatic hypermutation
CC (SHM) by targeting AICDA deamination activity to transcribed dsDNA
CC substrates. In the cytoplasm, the RNA exosome complex is involved in
CC general mRNA turnover and specifically degrades inherently unstable
CC mRNAs containing AU-rich elements (AREs) within their 3' untranslated
CC regions, and in RNA surveillance pathways, preventing translation of
CC aberrant mRNAs. It seems to be involved in degradation of histone mRNA.
CC EXOSC10 has 3'-5' exonuclease activity (By similarity). 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. {ECO:0000250, ECO:0000269|PubMed:14527413,
CC ECO:0000269|PubMed:16455498, ECO:0000269|PubMed:17412707,
CC ECO:0000269|PubMed:17545563, ECO:0000269|PubMed:18172165,
CC ECO:0000269|PubMed:19056938, ECO:0000269|PubMed:20368444,
CC ECO:0000269|PubMed:20699273}.
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). Interacts with
CC 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 {ECO:0000269|PubMed:14731398, ECO:0000269|PubMed:17234882,
CC ECO:0000269|PubMed:17412707, ECO:0000269|PubMed:20531389,
CC ECO:0000269|PubMed:26166824, ECO:0000269|PubMed:29906447,
CC ECO:0000269|PubMed:30538148}.
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. Nucleus, nucleolus. Nucleus.
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.
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;
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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 SMR; Q01780; -.
DR BioGRID; 111403; 169.
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; 83.
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; Q01780; -.
DR PeptideAtlas; Q01780; -.
DR PRIDE; Q01780; -.
DR ProteomicsDB; 57986; -. [Q01780-1]
DR ProteomicsDB; 57987; -. [Q01780-2]
DR Antibodypedia; 13683; 200 antibodies from 29 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 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; 677201at2759; -.
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; 472 hits in 1090 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 201 other 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); IC: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); IC:ComplexPortal.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; IMP:BHF-UCL.
DR GO; GO:0004532; F:exoribonuclease activity; IDA:UniProtKB.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; HDA: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:0009048; P:dosage compensation by inactivation of X chromosome; IEA:Ensembl.
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:1904872; P:regulation of telomerase RNA localization to Cajal body; IMP:BHF-UCL.
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 Gene3D; 1.10.150.80; -; 1.
DR Gene3D; 3.30.420.10; -; 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 PANTHER; PTHR12124; PTHR12124; 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; SSF47819; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR PROSITE; PS50967; HRDC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Exonuclease; Exosome;
KW Hydrolase; Isopeptide bond; Nonsense-mediated mRNA decay; Nuclease;
KW Nucleus; Phosphoprotein; Reference proteome; RNA-binding; rRNA processing;
KW Ubl conjugation.
FT CHAIN 1..885
FT /note="Exosome component 10"
FT /id="PRO_0000087133"
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 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:0007744|PubMed:25114211"
FT CROSSLNK 583
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: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 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
