ID EXOS3_HUMAN Reviewed; 275 AA. AC Q9NQT5; A8K0K6; Q5QP85; Q9Y3A8; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 20-DEC-2017, entry version 166. DE RecName: Full=Exosome complex component RRP40; DE AltName: Full=Exosome component 3; DE AltName: Full=Ribosomal RNA-processing protein 40; DE AltName: Full=p10; GN Name=EXOSC3; Synonyms=RRP40; ORFNames=CGI-102; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND CHARACTERIZATION. RX PubMed=11110791; DOI=10.1074/jbc.M007603200; RA Brouwer R., Allmang C., Raijmakers R., van Aarssen Y., Egberts W.V., RA Petfalski E., van Venrooij W.J., Tollervey D., Pruijn G.J.M.; RT "Three novel components of the human exosome."; RL J. Biol. Chem. 276:6177-6184(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Cerebellum; 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164053; DOI=10.1038/nature02465; RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R., RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., RA Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., RA Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., RA Rogers J., Dunham I.; RT "DNA sequence and analysis of human chromosome 9."; RL Nature 429:369-374(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Skin, and Uterus; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP PROTEIN SEQUENCE OF 2-16 AND 202-208, CLEAVAGE OF INITIATOR RP METHIONINE, ACETYLATION AT ALA-2, SUBCELLULAR LOCATION, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Cervix carcinoma; RA Bienvenut W.V.; RL Submitted (AUG-2005) to UniProtKB. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 56-275 (ISOFORM 1). RX PubMed=10810093; DOI=10.1101/gr.10.5.703; RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.; RT "Identification of novel human genes evolutionarily conserved in RT Caenorhabditis elegans by comparative proteomics."; RL Genome Res. 10:703-713(2000). RN [8] 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 [9] RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE RNA RP EXOSOME CORE COMPLEX. RX PubMed=11719186; DOI=10.1016/S0092-8674(01)00578-5; RA Chen C.-Y., Gherzi R., Ong S.-E., Chan E.L., Raijmakers R., RA Pruijn G.J.M., Stoecklin G., Moroni C., Mann M., Karin M.; RT "AU binding proteins recruit the exosome to degrade ARE-containing RT mRNAs."; RL Cell 107:451-464(2001). RN [10] RP FUNCTION IN CYTOPLASMIC MRNA DEGRADATION. RX PubMed=11782436; DOI=10.1093/emboj/21.1.165; RA Mukherjee D., Gao M., O'Connor J.P., Raijmakers R., Pruijn G., RA Lutz C.S., Wilusz J.; RT "The mammalian exosome mediates the efficient degradation of mRNAs RT that contain AU-rich elements."; RL EMBO J. 21:165-174(2002). RN [11] 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 [12] RP INTERACTION WITH DDX17. RX PubMed=18334637; DOI=10.1073/pnas.0712276105; RA Chen G., Guo X., Lv F., Xu Y., Gao G.; RT "p72 DEAD box RNA helicase is required for optimal function of the RT zinc-finger antiviral protein."; RL Proc. Natl. Acad. Sci. U.S.A. 105:4352-4357(2008). RN [13] RP FUNCTION IN PROMPT DEGRADATION. RX PubMed=19056938; DOI=10.1126/science.1164096; RA Preker P., Nielsen J., Kammler S., Lykke-Andersen S., RA Christensen M.S., 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 [14] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., RA Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in RT a refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [15] RP IDENTIFICATION IN THE RNA EXOSOME COMPLEX, IDENTIFICATION BY MASS RP SPECTROMETRY, SUBCELLULAR LOCATION, AND INTERACTION WITH DIS3L. 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 RT exosome."; RL EMBO J. 29:2358-2367(2010). RN [16] 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., RA Buerckstuemmer T., 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 [17] RP FUNCTION IN DEAMINATION OF TRANSCRIBED DNA SUBSTRATE. RX PubMed=21255825; DOI=10.1016/j.cell.2011.01.001; RA Basu U., Meng F.L., Keim C., Grinstein V., Pefanis E., Eccleston J., RA Zhang T., Myers D., Wasserman C.R., Wesemann D.R., Januszyk K., RA Gregory R.I., Deng H., Lima C.D., Alt F.W.; RT "The RNA exosome targets the AID cytidine deaminase to both strands of RT transcribed duplex DNA substrates."; RL Cell 144:353-363(2011). RN [18] RP INTERACTION WITH GTPBP1. RX PubMed=21515746; DOI=10.1096/fj.10-178715; RA Woo K.C., Kim T.D., Lee K.H., Kim D.Y., Kim S., Lee H.R., Kang H.J., RA Chung S.J., Senju S., Nishimura Y., Kim K.T.; RT "Modulation of exosome-mediated mRNA turnover by interaction of GTP- RT binding protein 1 (GTPBP1) with its target mRNAs."; RL FASEB J. 25:2757-2769(2011). RN [19] RP INTERACTION WITH ZC3HAV1. RX PubMed=21876179; DOI=10.1073/pnas.1101676108; RA Zhu Y., Chen G., Lv F., Wang X., Ji X., Xu Y., Sun J., Wu L., RA Zheng Y.T., Gao G.; RT "Zinc-finger antiviral protein inhibits HIV-1 infection by selectively RT targeting multiply spliced viral mRNAs for degradation."; RL Proc. Natl. Acad. Sci. U.S.A. 108:15834-15839(2011). RN [20] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.M111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., RA Meinnel T., Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [21] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS RP SPECTROMETRY [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., RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., RA Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N- RT terminal acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [22] RP IDENTIFICATION BY 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 [23] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-151, AND IDENTIFICATION BY RP 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- RT modification with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [24] RP X-RAY CRYSTALLOGRAPHY (3.35 ANGSTROMS), AND RECONSTITUTION OF THE RNA RP EXOSOME CORE COMPLEX. RX PubMed=17174896; DOI=10.1016/j.cell.2006.10.037; RA Liu Q., Greimann J.C., Lima C.D.; RT "Reconstitution, activities, and structure of the eukaryotic RNA RT exosome."; RL Cell 127:1223-1237(2006). RN [25] RP ERRATUM. RA Liu Q., Greimann J.C., Lima C.D.; RL Cell 131:188-189(2007). RN [26] RP VARIANTS PCH1B ALA-31; ALA-132; PRO-139 AND ARG-238. RX PubMed=22544365; DOI=10.1038/ng.2254; RA Wan J., Yourshaw M., Mamsa H., Rudnik-Schoneborn S., Menezes M.P., RA Hong J.E., Leong D.W., Senderek J., Salman M.S., Chitayat D., RA Seeman P., von Moers A., Graul-Neumann L., Kornberg A.J., RA Castro-Gago M., Sobrido M.J., Sanefuji M., Shieh P.B., Salamon N., RA Kim R.C., Vinters H.V., Chen Z., Zerres K., Ryan M.M., Nelson S.F., RA Jen J.C.; RT "Mutations in the RNA exosome component gene EXOSC3 cause RT pontocerebellar hypoplasia and spinal motor neuron degeneration."; RL Nat. Genet. 44:704-708(2012). RN [27] RP VARIANT PHE-80. RX PubMed=25841024; DOI=10.1212/WNL.0000000000001524; RA Coutelier M., Burglen L., Mundwiller E., Abada-Bendib M., RA Rodriguez D., Chantot-Bastaraud S., Rougeot C., Cournelle M.A., RA Milh M., Toutain A., Bacq D., Meyer V., Afenjar A., Deleuze J.F., RA Brice A., Heron D., Stevanin G., Durr A.; RT "GRID2 mutations span from congenital to mild adult-onset cerebellar RT ataxia."; RL Neurology 84:1751-1759(2015). CC -!- FUNCTION: Non-catalytic component of the RNA exosome complex which CC has 3'->5' exoribonuclease activity and participates in a CC multitude of cellular RNA processing and degradation events. In CC the nucleus, the RNA exosome complex is involved in proper CC maturation of stable RNA species such as rRNA, snRNA and snoRNA, CC in the elimination of RNA processing by-products and non-coding CC 'pervasive' transcripts, such as antisense RNA species and CC promoter-upstream transcripts (PROMPTs), and of mRNAs with CC 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 CC hypermutation (SHM) by targeting AICDA deamination activity to CC transcribed dsDNA substrates. In the cytoplasm, the RNA exosome CC complex is involved in general mRNA turnover and specifically CC degrades inherently unstable mRNAs containing AU-rich elements CC (AREs) within their 3' untranslated regions, and in RNA CC surveillance pathways, preventing translation of aberrant mRNAs. CC It seems to be involved in degradation of histone mRNA. The CC catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) CC is proposed to play a pivotal role in the binding and presentation CC of RNA for ribonucleolysis, and to serve as a scaffold for the CC association with catalytic subunits and accessory proteins or CC complexes. EXOSC3 as peripheral part of the Exo-9 complex CC stabilizes the hexameric ring of RNase PH-domain subunits through CC contacts with EXOSC9 and EXOSC5. {ECO:0000269|PubMed:11782436, CC ECO:0000269|PubMed:17545563, ECO:0000269|PubMed:19056938, CC ECO:0000269|PubMed:21255825}. CC -!- SUBUNIT: Component of the RNA exosome complex. Specifically part CC of the catalytically inactive RNA exosome core (Exo-9) complex CC which is believed to associate with catalytic subunits EXOSC10, CC and DIS3 or DIS3L in cytoplasmic- and nuclear-specific RNA exosome CC complex forms. Exo-9 is formed by a hexameric ring of RNase PH CC domain-containing subunits specifically containing the CC heterodimers EXOSC4-EXOSC9, EXOSC5-EXOSC8 and EXOSC6-EXOSC7, and CC peripheral S1 domain-containing components EXOSC1, EXOSC2 and CC EXOSC3 located on the top of the ring structure. Interacts with CC GTPBP1. Interacts with ZC3HAV1. Interacts with DDX17 only in the CC presence of ZC3HAV1 in an RNA-independent manner. CC {ECO:0000269|PubMed:11719186, ECO:0000269|PubMed:18334637, CC ECO:0000269|PubMed:20531389, ECO:0000269|PubMed:21515746, CC ECO:0000269|PubMed:21876179}. CC -!- INTERACTION: CC Q92841:DDX17; NbExp=2; IntAct=EBI-371866, EBI-746012; CC Q9Y2L1:DIS3; NbExp=3; IntAct=EBI-371866, EBI-373539; CC Q8TF46:DIS3L; NbExp=4; IntAct=EBI-371866, EBI-3672244; CC Q13868:EXOSC2; NbExp=6; IntAct=EBI-371866, EBI-301735; CC Q9NPD3:EXOSC4; NbExp=5; IntAct=EBI-371866, EBI-371823; CC Q9NQT4:EXOSC5; NbExp=8; IntAct=EBI-371866, EBI-371876; CC Q96B26:EXOSC8; NbExp=3; IntAct=EBI-371866, EBI-371922; CC Q8K3Y6:Zc3hav1 (xeno); NbExp=3; IntAct=EBI-371866, EBI-8860250; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17545563}. CC Nucleus, nucleolus {ECO:0000269|PubMed:20531389}. Nucleus CC {ECO:0000269|PubMed:17545563}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9NQT5-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9NQT5-2; Sequence=VSP_043457; CC Note=No experimental confirmation available.; CC -!- DISEASE: Pontocerebellar hypoplasia 1B (PCH1B) [MIM:614678]: A CC severe autosomal recessive neurologic disorder characterized by a CC combination of cerebellar and spinal motor neuron degeneration CC beginning at birth. There is diffuse muscle weakness, progressive CC microcephaly, global developmental delay, and brainstem CC involvement. {ECO:0000269|PubMed:22544365}. Note=The disease is CC caused by mutations affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the RRP40 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF281132; AAF82133.1; -; mRNA. DR EMBL; AK289571; BAF82260.1; -; mRNA. DR EMBL; AK290864; BAF83553.1; -; mRNA. DR EMBL; AL138752; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471071; EAW58264.1; -; Genomic_DNA. DR EMBL; BC002437; AAH02437.1; -; mRNA. DR EMBL; BC008880; AAH08880.1; -; mRNA. DR EMBL; AF151860; AAD34097.1; -; mRNA. DR CCDS; CCDS35016.1; -. [Q9NQT5-1] DR CCDS; CCDS43805.1; -. [Q9NQT5-2] DR RefSeq; NP_001002269.1; NM_001002269.2. [Q9NQT5-2] DR RefSeq; NP_057126.2; NM_016042.3. [Q9NQT5-1] DR UniGene; Hs.602571; -. DR UniGene; Hs.713483; -. DR PDB; 2NN6; X-ray; 3.35 A; G=1-275. DR PDBsum; 2NN6; -. DR ProteinModelPortal; Q9NQT5; -. DR SMR; Q9NQT5; -. DR BioGrid; 119217; 31. DR CORUM; Q9NQT5; -. DR DIP; DIP-29847N; -. DR IntAct; Q9NQT5; 26. DR MINT; MINT-3072286; -. DR STRING; 9606.ENSP00000323046; -. DR iPTMnet; Q9NQT5; -. DR PhosphoSitePlus; Q9NQT5; -. DR BioMuta; EXOSC3; -. DR DMDM; 14285758; -. DR EPD; Q9NQT5; -. DR MaxQB; Q9NQT5; -. DR PaxDb; Q9NQT5; -. DR PeptideAtlas; Q9NQT5; -. DR PRIDE; Q9NQT5; -. DR DNASU; 51010; -. DR Ensembl; ENST00000327304; ENSP00000323046; ENSG00000107371. [Q9NQT5-1] DR Ensembl; ENST00000396521; ENSP00000379775; ENSG00000107371. [Q9NQT5-2] DR Ensembl; ENST00000465229; ENSP00000418422; ENSG00000107371. [Q9NQT5-2] DR GeneID; 51010; -. DR KEGG; hsa:51010; -. DR UCSC; uc004aal.4; human. [Q9NQT5-1] DR CTD; 51010; -. DR DisGeNET; 51010; -. DR EuPathDB; HostDB:ENSG00000107371.12; -. DR GeneCards; EXOSC3; -. DR HGNC; HGNC:17944; EXOSC3. DR HPA; HPA020485; -. DR MalaCards; EXOSC3; -. DR MIM; 606489; gene. DR MIM; 614678; phenotype. DR neXtProt; NX_Q9NQT5; -. DR OpenTargets; ENSG00000107371; -. DR Orphanet; 2254; Pontocerebellar hypoplasia type 1. DR PharmGKB; PA134926550; -. DR eggNOG; KOG1004; Eukaryota. DR eggNOG; COG1097; LUCA. DR GeneTree; ENSGT00390000012042; -. DR HOGENOM; HOG000012998; -. DR HOVERGEN; HBG051518; -. DR InParanoid; Q9NQT5; -. DR KO; K03681; -. DR OMA; ISYLAFE; -. DR OrthoDB; EOG091G0Q58; -. DR PhylomeDB; Q9NQT5; -. DR TreeFam; TF314927; -. DR Reactome; R-HSA-380994; ATF4 activates genes. DR Reactome; R-HSA-429958; mRNA decay by 3' to 5' exoribonuclease. DR Reactome; R-HSA-450385; Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA. DR Reactome; R-HSA-450513; Tristetraprolin (TTP, ZFP36) binds and destabilizes mRNA. DR Reactome; R-HSA-450604; KSRP (KHSRP) binds and destabilizes mRNA. DR Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol. DR EvolutionaryTrace; Q9NQT5; -. DR GeneWiki; Exosome_component_3; -. DR GenomeRNAi; 51010; -. DR PRO; PR:Q9NQT5; -. DR Proteomes; UP000005640; Chromosome 9. DR Bgee; ENSG00000107371; -. DR CleanEx; HS_EXOSC3; -. DR Genevisible; Q9NQT5; HS. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0000177; C:cytoplasmic exosome (RNase complex); IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0000178; C:exosome (RNase complex); IDA:UniProtKB. DR GO; GO:0000176; C:nuclear exosome (RNase complex); IDA:UniProtKB. 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:0035327; C:transcriptionally active chromatin; IMP:UniProtKB. DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; NAS:UniProtKB. DR GO; GO:0003723; F:RNA binding; IBA:GO_Central. DR GO; GO:0071034; P:CUT catabolic process; IMP:UniProtKB. DR GO; GO:0045006; P:DNA deamination; IDA:UniProtKB. DR GO; GO:0043928; P:exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay; IMP:UniProtKB. 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:0045190; P:isotype switching; ISS:UniProtKB. DR GO; GO:0071035; P:nuclear polyadenylation-dependent rRNA catabolic process; IBA:GO_Central. DR GO; GO:0071038; P:nuclear polyadenylation-dependent tRNA catabolic process; IBA:GO_Central. DR GO; GO:0071049; P:nuclear retention of pre-mRNA with aberrant 3'-ends at the site of transcription; IBA:GO_Central. DR GO; GO:0034427; P:nuclear-transcribed mRNA catabolic process, exonucleolytic, 3'-5'; IBA:GO_Central. DR GO; GO:0071051; P:polyadenylation-dependent snoRNA 3'-end processing; IBA:GO_Central. DR GO; GO:0045830; P:positive regulation of isotype switching; IEA:Ensembl. DR GO; GO:0043488; P:regulation of mRNA stability; TAS:Reactome. DR GO; GO:0006364; P:rRNA processing; IDA:UniProtKB. DR GO; GO:0034475; P:U4 snRNA 3'-end processing; IBA:GO_Central. DR CDD; cd05790; S1_Rrp40; 1. DR InterPro; IPR026699; Exosome_RNA_bind1/RRP40/RRP4. DR InterPro; IPR004088; KH_dom_type_1. DR InterPro; IPR036612; KH_dom_type_1_sf. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR037319; Rrp40_S1. DR PANTHER; PTHR21321; PTHR21321; 1. DR Pfam; PF15985; KH_6; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR SUPFAM; SSF54791; SSF54791; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Complete proteome; KW Cytoplasm; Direct protein sequencing; Disease mutation; Exosome; KW Isopeptide bond; Neurodegeneration; Nucleus; Polymorphism; KW Reference proteome; RNA-binding; rRNA processing; Ubl conjugation. FT INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330, FT ECO:0000244|PubMed:22223895, FT ECO:0000244|PubMed:22814378, FT ECO:0000269|Ref.6}. FT CHAIN 2 275 Exosome complex component RRP40. FT /FTId=PRO_0000087131. FT MOD_RES 2 2 N-acetylalanine. FT {ECO:0000244|PubMed:19413330, FT ECO:0000244|PubMed:22223895, FT ECO:0000244|PubMed:22814378, FT ECO:0000269|Ref.6}. FT CROSSLNK 151 151 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000244|PubMed:28112733}. FT VAR_SEQ 159 275 VGDLIYGQFVVANKDMEPEMVCIDSCGRANGMGVIGQDGLL FT FKVTLGLIRKLLAPDCEIIQEVGKLYPLEIVFGMNGRIWVK FT AKTIQQTLILANILEACEHMTSDQRKQIFSRLAES -> AI FT SSRL (in isoform 2). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_043457. FT VARIANT 31 31 G -> A (in PCH1B; dbSNP:rs387907196). FT {ECO:0000269|PubMed:22544365}. FT /FTId=VAR_068505. FT VARIANT 80 80 V -> F (in dbSNP:rs374550999). FT {ECO:0000269|PubMed:25841024}. FT /FTId=VAR_074169. FT VARIANT 132 132 D -> A (in PCH1B; dbSNP:rs141138948). FT {ECO:0000269|PubMed:22544365}. FT /FTId=VAR_068506. FT VARIANT 139 139 A -> P (in PCH1B; dbSNP:rs387907195). FT {ECO:0000269|PubMed:22544365}. FT /FTId=VAR_068507. FT VARIANT 225 225 Y -> H (in dbSNP:rs3208406). FT /FTId=VAR_054098. FT VARIANT 238 238 W -> R (in PCH1B; dbSNP:rs672601332). FT {ECO:0000269|PubMed:22544365}. FT /FTId=VAR_068508. FT CONFLICT 56 65 NARACSRVRV -> MLERARGCAF (in Ref. 7; FT AAD34097). {ECO:0000305}. FT CONFLICT 95 95 S -> G (in Ref. 7; AAD34097). FT {ECO:0000305}. FT HELIX 22 24 {ECO:0000244|PDB:2NN6}. FT STRAND 25 27 {ECO:0000244|PDB:2NN6}. FT STRAND 30 34 {ECO:0000244|PDB:2NN6}. FT STRAND 45 49 {ECO:0000244|PDB:2NN6}. FT STRAND 78 80 {ECO:0000244|PDB:2NN6}. FT STRAND 85 89 {ECO:0000244|PDB:2NN6}. FT TURN 92 94 {ECO:0000244|PDB:2NN6}. FT STRAND 99 103 {ECO:0000244|PDB:2NN6}. FT STRAND 113 125 {ECO:0000244|PDB:2NN6}. FT STRAND 128 132 {ECO:0000244|PDB:2NN6}. FT STRAND 134 137 {ECO:0000244|PDB:2NN6}. FT STRAND 141 143 {ECO:0000244|PDB:2NN6}. FT STRAND 145 147 {ECO:0000244|PDB:2NN6}. FT STRAND 153 157 {ECO:0000244|PDB:2NN6}. FT STRAND 162 169 {ECO:0000244|PDB:2NN6}. FT STRAND 177 179 {ECO:0000244|PDB:2NN6}. FT TURN 183 185 {ECO:0000244|PDB:2NN6}. FT STRAND 198 200 {ECO:0000244|PDB:2NN6}. FT HELIX 204 211 {ECO:0000244|PDB:2NN6}. FT HELIX 217 220 {ECO:0000244|PDB:2NN6}. FT STRAND 224 226 {ECO:0000244|PDB:2NN6}. FT STRAND 230 232 {ECO:0000244|PDB:2NN6}. FT TURN 233 235 {ECO:0000244|PDB:2NN6}. FT STRAND 236 239 {ECO:0000244|PDB:2NN6}. FT HELIX 244 256 {ECO:0000244|PDB:2NN6}. FT TURN 262 264 {ECO:0000244|PDB:2NN6}. FT HELIX 265 274 {ECO:0000244|PDB:2NN6}. SQ SEQUENCE 275 AA; 29572 MW; 264322144A199166 CRC64; MAEPASVAAE SLAGSRARAA RTVLGQVVLP GEELLLPEQE DAEGPGGAVE RPLSLNARAC SRVRVVCGPG LRRCGDRLLV TKCGRLRHKE PGSGSGGGVY WVDSQQKRYV PVKGDHVIGI VTAKSGDIFK VDVGGSEPAS LSYLSFEGAT KRNRPNVQVG DLIYGQFVVA NKDMEPEMVC IDSCGRANGM GVIGQDGLLF KVTLGLIRKL LAPDCEIIQE VGKLYPLEIV FGMNGRIWVK AKTIQQTLIL ANILEACEHM TSDQRKQIFS RLAES //