EXOS2_HUMAN
ID EXOS2_HUMAN Reviewed; 293 AA.
AC Q13868; A3KFL3; A3KFL4; B4DKK6; Q9NUY4;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 03-AUG-2022, entry version 205.
DE RecName: Full=Exosome complex component RRP4 {ECO:0000305};
DE AltName: Full=Exosome component 2;
DE AltName: Full=Ribosomal RNA-processing protein 4;
GN Name=EXOSC2 {ECO:0000312|HGNC:HGNC:17097};
GN Synonyms=RRP4 {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 [GENOMIC DNA].
RC TISSUE=Lung carcinoma;
RA Chissoe S.L.;
RT "Sequence of the human abl and bcr genes.";
RL Thesis (1994), University of Oklahoma, United States.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND SEQUENCE REVISION.
RC TISSUE=Cervix adenocarcinoma;
RX PubMed=9390555; DOI=10.1016/s0092-8674(00)80432-8;
RA Mitchell P., Petfalski E., Shevchenko A., Mann M., Tollervey D.;
RT "The exosome: a conserved eukaryotic RNA processing complex containing
RT multiple 3'-->5' exoribonucleases.";
RL Cell 91:457-466(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Colon, Mammary gland, and Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., 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., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., 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., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
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=8600032; DOI=10.1101/gad.10.4.502;
RA Mitchell P., Petfalski E., Tollervey D.;
RT "The 3' end of yeast 5.8S rRNA is generated by an exonuclease processing
RT mechanism.";
RL Genes Dev. 10:502-513(1996).
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, IDENTIFICATION IN THE RNA EXOSOME CORE
RP COMPLEX, AND PROTEIN INTERACTION.
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., Pruijn G.J.M.,
RA Stoecklin G., Moroni C., Mann M., Karin M.;
RT "AU binding proteins recruit the exosome to degrade ARE-containing mRNAs.";
RL Cell 107:451-464(2001).
RN [10]
RP INTERACTION WITH ZFP36L1.
RX PubMed=15687258; DOI=10.1101/gad.1282305;
RA Lykke-Andersen J., Wagner E.;
RT "Recruitment and activation of mRNA decay enzymes by two ARE-mediated decay
RT activation domains in the proteins TTP and BRF-1.";
RL Genes Dev. 19:351-361(2005).
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [15]
RP IDENTIFICATION IN THE RNA EXOSOME COMPLEX, IDENTIFICATION BY MASS
RP SPECTROMETRY, SUBCELLULAR LOCATION, AND INTERACTION WITH DIS3.
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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [17]
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 [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-binding
RT protein 1 (GTPBP1) with its target mRNAs.";
RL FASEB J. 25:2757-2769(2011).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [20]
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 [21]
RP INVOLVEMENT IN SHRF, AND VARIANTS SHRF VAL-30 AND ASP-198.
RX PubMed=26843489; DOI=10.1136/jmedgenet-2015-103511;
RA Di Donato N., Neuhann T., Kahlert A.K., Klink B., Hackmann K., Neuhann I.,
RA Novotna B., Schallner J., Krause C., Glass I.A., Parnell S.E.,
RA Benet-Pages A., Nissen A.M., Berger W., Altmueller J., Thiele H.,
RA Weber B.H., Schrock E., Dobyns W.B., Bier A., Rump A.;
RT "Mutations in EXOSC2 are associated with a novel syndrome characterised by
RT retinitis pigmentosa, progressive hearing loss, premature ageing, short
RT stature, mild intellectual disability and distinctive gestalt.";
RL J. Med. Genet. 53:419-425(2016).
RN [22]
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 exosome.";
RL Cell 127:1223-1237(2006).
RN [23]
RP ERRATUM OF PUBMED:17174896.
RA Liu Q., Greimann J.C., Lima C.D.;
RL Cell 131:188-189(2007).
RN [24] {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: Non-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. 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 The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9)
CC is proposed to play a pivotal role in the binding and presentation of
CC RNA for ribonucleolysis, and to serve as a scaffold for the association
CC with catalytic subunits and accessory proteins or complexes. EXOSC2 as
CC peripheral part of the Exo-9 complex stabilizes the hexameric ring of
CC RNase PH-domain subunits through contacts with EXOSC4 and EXOSC7.
CC {ECO:0000269|PubMed:17545563}.
CC -!- SUBUNIT: Component of the RNA exosome complex (PubMed:29906447).
CC Specifically part of the catalytically inactive RNA exosome core (Exo-
CC 9) complex which is believed to associate with catalytic subunits
CC EXOSC10, and DIS3 or DIS3L in cytoplasmic- and nuclear-specific RNA
CC exosome complex forms (PubMed:11719186, PubMed:20531389,
CC PubMed:26166824). Exo-9 is formed by a hexameric ring of RNase PH
CC domain-containing subunits specifically containing the heterodimers
CC EXOSC4-EXOSC9, EXOSC5-EXOSC8 and EXOSC6-EXOSC7, and peripheral S1
CC domain-containing components EXOSC1, EXOSC2 and EXOSC3 located on the
CC top of the ring structure (PubMed:11719186, PubMed:20531389). Interacts
CC with DIS3 (PubMed:20531389). Interacts with GTPBP1 (PubMed:21515746).
CC Interacts with ZFP36L1 (via N-terminus) (PubMed:15687258).
CC {ECO:0000269|PubMed:11719186, ECO:0000269|PubMed:15687258,
CC ECO:0000269|PubMed:20531389, ECO:0000269|PubMed:21515746,
CC ECO:0000269|PubMed:26166824, ECO:0000269|PubMed:29906447}.
CC -!- INTERACTION:
CC Q13868; Q8TF46-1: DIS3L; NbExp=2; IntAct=EBI-301735, EBI-3895807;
CC Q13868; Q9NQT5: EXOSC3; NbExp=8; IntAct=EBI-301735, EBI-371866;
CC Q13868; Q9NPD3: EXOSC4; NbExp=8; IntAct=EBI-301735, EBI-371823;
CC Q13868; Q15024: EXOSC7; NbExp=7; IntAct=EBI-301735, EBI-371841;
CC Q13868; Q99547: MPHOSPH6; NbExp=3; IntAct=EBI-301735, EBI-373187;
CC Q13868; P0C264: SBK3; NbExp=3; IntAct=EBI-301735, EBI-17181801;
CC Q13868; Q9H9D4: ZNF408; NbExp=3; IntAct=EBI-301735, EBI-347633;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus, nucleolus. Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q13868-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q13868-2; Sequence=VSP_054921;
CC Name=3;
CC IsoId=Q13868-3; Sequence=VSP_057568;
CC -!- DISEASE: Short stature, hearing loss, retinitis pigmentosa, and
CC distinctive facies (SHRF) [MIM:617763]: An autosomal recessive disorder
CC characterized by childhood myopia, early onset retinitis pigmentosa,
CC progressive sensorineural hearing loss, hypothyroidism, short stature,
CC brachydactyly, recognisable facial gestalt, premature ageing and mild
CC intellectual disability. {ECO:0000269|PubMed:26843489}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the RRP4 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB60392.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; U07561; AAB60392.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AK001916; BAA91977.1; -; mRNA.
DR EMBL; AK022460; BAB14043.1; -; mRNA.
DR EMBL; AK296605; BAG59218.1; -; mRNA.
DR EMBL; AL359092; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471090; EAW87942.1; -; Genomic_DNA.
DR EMBL; CH471090; EAW87944.1; -; Genomic_DNA.
DR EMBL; BC000747; AAH00747.1; -; mRNA.
DR CCDS; CCDS65160.1; -. [Q13868-2]
DR CCDS; CCDS65161.1; -. [Q13868-3]
DR CCDS; CCDS6935.1; -. [Q13868-1]
DR RefSeq; NP_001269637.1; NM_001282708.1. [Q13868-2]
DR RefSeq; NP_001269638.1; NM_001282709.1. [Q13868-3]
DR RefSeq; NP_055100.2; NM_014285.6. [Q13868-1]
DR PDB; 2NN6; X-ray; 3.35 A; H=1-293.
DR PDB; 6D6Q; EM; 3.45 A; H=1-293.
DR PDB; 6D6R; EM; 3.45 A; H=1-293.
DR PDB; 6H25; EM; 3.80 A; H=1-293.
DR PDBsum; 2NN6; -.
DR PDBsum; 6D6Q; -.
DR PDBsum; 6D6R; -.
DR PDBsum; 6H25; -.
DR AlphaFoldDB; Q13868; -.
DR SMR; Q13868; -.
DR BioGRID; 116977; 136.
DR ComplexPortal; CPX-476; Nuclear exosome complex, DIS3-EXOSC10 variant.
DR ComplexPortal; CPX-591; Nucleolar exosome complex, EXOSC10 variant.
DR ComplexPortal; CPX-592; Cytoplasmic exosome complex, DIS3L variant.
DR ComplexPortal; CPX-593; Exosome complex, DIS3 variant.
DR ComplexPortal; CPX-600; Cytoplasmic exosome complex, DIS3L-EXOSC10 variant.
DR CORUM; Q13868; -.
DR DIP; DIP-31264N; -.
DR IntAct; Q13868; 72.
DR MINT; Q13868; -.
DR STRING; 9606.ENSP00000361433; -.
DR iPTMnet; Q13868; -.
DR MetOSite; Q13868; -.
DR PhosphoSitePlus; Q13868; -.
DR SwissPalm; Q13868; -.
DR BioMuta; EXOSC2; -.
DR DMDM; 13878748; -.
DR EPD; Q13868; -.
DR jPOST; Q13868; -.
DR MassIVE; Q13868; -.
DR MaxQB; Q13868; -.
DR PaxDb; Q13868; -.
DR PeptideAtlas; Q13868; -.
DR PRIDE; Q13868; -.
DR ProteomicsDB; 4467; -.
DR ProteomicsDB; 563; -.
DR ProteomicsDB; 59704; -. [Q13868-1]
DR Antibodypedia; 17999; 186 antibodies from 28 providers.
DR DNASU; 23404; -.
DR Ensembl; ENST00000372351.7; ENSP00000361426.3; ENSG00000130713.17. [Q13868-3]
DR Ensembl; ENST00000372358.10; ENSP00000361433.5; ENSG00000130713.17. [Q13868-1]
DR Ensembl; ENST00000546165.6; ENSP00000444917.1; ENSG00000130713.17. [Q13868-2]
DR Ensembl; ENST00000691284.1; ENSP00000508620.1; ENSG00000130713.17. [Q13868-1]
DR GeneID; 23404; -.
DR KEGG; hsa:23404; -.
DR MANE-Select; ENST00000372358.10; ENSP00000361433.5; NM_014285.7; NP_055100.2.
DR UCSC; uc004bzu.4; human. [Q13868-1]
DR UCSC; uc033djg.2; human.
DR CTD; 23404; -.
DR DisGeNET; 23404; -.
DR GeneCards; EXOSC2; -.
DR HGNC; HGNC:17097; EXOSC2.
DR HPA; ENSG00000130713; Low tissue specificity.
DR MalaCards; EXOSC2; -.
DR MIM; 602238; gene.
DR MIM; 617763; phenotype.
DR neXtProt; NX_Q13868; -.
DR OpenTargets; ENSG00000130713; -.
DR Orphanet; 494439; Retinitis pigmentosa-hearing loss-premature aging-short stature-facial dysmorphism syndrome.
DR PharmGKB; PA134876020; -.
DR VEuPathDB; HostDB:ENSG00000130713; -.
DR eggNOG; KOG3013; Eukaryota.
DR GeneTree; ENSGT00940000153596; -.
DR InParanoid; Q13868; -.
DR OMA; GVNGFIW; -.
DR OrthoDB; 1121868at2759; -.
DR PhylomeDB; Q13868; -.
DR TreeFam; TF105623; -.
DR PathwayCommons; Q13868; -.
DR Reactome; R-HSA-380994; ATF4 activates genes in response to endoplasmic reticulum stress.
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 SignaLink; Q13868; -.
DR SIGNOR; Q13868; -.
DR BioGRID-ORCS; 23404; 770 hits in 1093 CRISPR screens.
DR ChiTaRS; EXOSC2; human.
DR EvolutionaryTrace; Q13868; -.
DR GeneWiki; Exosome_component_2; -.
DR GenomeRNAi; 23404; -.
DR Pharos; Q13868; Tbio.
DR PRO; PR:Q13868; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q13868; protein.
DR Bgee; ENSG00000130713; Expressed in ganglionic eminence and 170 other tissues.
DR ExpressionAtlas; Q13868; baseline and differential.
DR Genevisible; Q13868; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0000177; C:cytoplasmic exosome (RNase complex); IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:ComplexPortal.
DR GO; GO:0000178; C:exosome (RNase complex); IDA: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:HPA.
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; TAS:ProtInc.
DR GO; GO:0008312; F:7S RNA binding; TAS:ProtInc.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0071034; P:CUT catabolic process; IBA:GO_Central.
DR GO; GO:0043928; P:exonucleolytic catabolism of deadenylated mRNA; IBA:GO_Central.
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: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: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:0030307; P:positive regulation of cell growth; IMP: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:ProtInc.
DR GO; GO:0034475; P:U4 snRNA 3'-end processing; IBA:GO_Central.
DR Gene3D; 2.40.50.140; -; 1.
DR InterPro; IPR025721; Exosome_cplx_N_dom.
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 PANTHER; PTHR21321; PTHR21321; 1.
DR Pfam; PF14382; ECR1_N; 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; Alternative splicing; Cytoplasm; Deafness; Disease variant;
KW Dwarfism; Exosome; Nucleus; Phosphoprotein; Reference proteome;
KW Retinitis pigmentosa; RNA-binding; rRNA processing.
FT CHAIN 1..293
FT /note="Exosome complex component RRP4"
FT /id="PRO_0000087129"
FT DOMAIN 79..159
FT /note="S1 motif"
FT MOD_RES 124
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT VAR_SEQ 91..120
FT /note="Missing (in isoform 3)"
FT /id="VSP_057568"
FT VAR_SEQ 143..168
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054921"
FT VARIANT 30
FT /note="G -> V (in SHRF; dbSNP:rs537467155)"
FT /evidence="ECO:0000269|PubMed:26843489"
FT /id="VAR_080552"
FT VARIANT 198
FT /note="G -> D (in SHRF; dbSNP:rs756204866)"
FT /evidence="ECO:0000269|PubMed:26843489"
FT /id="VAR_080553"
FT HELIX 13..15
FT /evidence="ECO:0007829|PDB:6D6Q"
FT TURN 16..18
FT /evidence="ECO:0007829|PDB:6D6Q"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:2NN6"
FT STRAND 49..54
FT /evidence="ECO:0007829|PDB:2NN6"
FT STRAND 56..63
FT /evidence="ECO:0007829|PDB:2NN6"
FT STRAND 66..73
FT /evidence="ECO:0007829|PDB:2NN6"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:2NN6"
FT STRAND 86..92
FT /evidence="ECO:0007829|PDB:2NN6"
FT STRAND 95..99
FT /evidence="ECO:0007829|PDB:2NN6"
FT STRAND 101..104
FT /evidence="ECO:0007829|PDB:2NN6"
FT STRAND 106..111
FT /evidence="ECO:0007829|PDB:2NN6"
FT HELIX 129..134
FT /evidence="ECO:0007829|PDB:2NN6"
FT STRAND 144..149
FT /evidence="ECO:0007829|PDB:2NN6"
FT TURN 150..152
FT /evidence="ECO:0007829|PDB:2NN6"
FT STRAND 153..157
FT /evidence="ECO:0007829|PDB:2NN6"
FT STRAND 163..165
FT /evidence="ECO:0007829|PDB:6D6Q"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:2NN6"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:6D6Q"
FT STRAND 186..189
FT /evidence="ECO:0007829|PDB:6D6Q"
FT TURN 190..192
FT /evidence="ECO:0007829|PDB:6D6Q"
FT STRAND 193..198
FT /evidence="ECO:0007829|PDB:2NN6"
FT TURN 199..201
FT /evidence="ECO:0007829|PDB:2NN6"
FT STRAND 202..206
FT /evidence="ECO:0007829|PDB:2NN6"
FT HELIX 220..222
FT /evidence="ECO:0007829|PDB:2NN6"
FT HELIX 228..246
FT /evidence="ECO:0007829|PDB:2NN6"
FT HELIX 253..261
FT /evidence="ECO:0007829|PDB:2NN6"
FT TURN 262..266
FT /evidence="ECO:0007829|PDB:2NN6"
FT HELIX 275..289
FT /evidence="ECO:0007829|PDB:2NN6"
FT TURN 290..292
FT /evidence="ECO:0007829|PDB:2NN6"
SQ SEQUENCE 293 AA; 32789 MW; 882033F50791643F CRC64;
MAMEMRLPVA RKPLSERLGR DTKKHLVVPG DTITTDTGFM RGHGTYMGEE KLIASVAGSV
ERVNKLICVK ALKTRYIGEV GDIVVGRITE VQQKRWKVET NSRLDSVLLL SSMNLPGGEL
RRRSAEDELA MRGFLQEGDL ISAEVQAVFS DGAVSLHTRS LKYGKLGQGV LVQVSPSLVK
RQKTHFHDLP CGASVILGNN GFIWIYPTPE HKEEEAGGFI ANLEPVSLAD REVISRLRNC
IISLVTQRMM LYDTSILYCY EASLPHQIKD ILKPEIMEEI VMETRQRLLE QEG
