EXOS1_HUMAN
ID EXOS1_HUMAN Reviewed; 195 AA.
AC Q9Y3B2; B2R9B3; Q5JTH3;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Exosome complex component CSL4;
DE AltName: Full=Exosome component 1;
GN Name=EXOSC1; Synonyms=CSL4; ORFNames=CGI-108;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE RNA EXOSOME
RP 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., 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 [7]
RP PROTEIN INTERACTION.
RX PubMed=12419256; DOI=10.1016/s0022-2836(02)00947-6;
RA Raijmakers R., Vree Egberts W., van Venrooij W.J., Pruijn G.J.M.;
RT "Protein-protein interactions between human exosome components support the
RT assembly of RNase PH-type subunits into a six-membered PNPase-like ring.";
RL J. Mol. Biol. 323:653-663(2002).
RN [8]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH EXOSC5; EXOSC7 AND EXOSC10.
RX PubMed=11812149; DOI=10.1006/jmbi.2001.5265;
RA Raijmakers R., Noordman Y.E., van Venrooij W.J., Pruijn G.J.M.;
RT "Protein-protein interactions of hCsl4p with other human exosome
RT subunits.";
RL J. Mol. Biol. 315:809-818(2002).
RN [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND IDENTIFICATION BY
RP 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 [12]
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, 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 [14]
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 [15]
RP INTERACTION WITH DDX60.
RX PubMed=21791617; DOI=10.1128/mcb.01368-10;
RA Miyashita M., Oshiumi H., Matsumoto M., Seya T.;
RT "DDX60, a DEXD/H box helicase, is a novel antiviral factor promoting RIG-I-
RT like receptor-mediated signaling.";
RL Mol. Cell. Biol. 31:3802-3819(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21 AND SER-98, AND
RP IDENTIFICATION BY 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 [17]
RP INVOLVEMENT IN PCH1F, VARIANT PCH1F LEU-35, AND CHARACTERIZATION OF VARIANT
RP PCH1F LEU-35.
RX PubMed=33463720; DOI=10.1111/cge.13928;
RA Somashekar P.H., Kaur P., Stephen J., Guleria V.S., Kadavigere R.,
RA Girisha K.M., Bielas S., Upadhyai P., Shukla A.;
RT "Bi-allelic missense variant, p.Ser35Leu in EXOSC1 is associated with
RT pontocerebellar hypoplasia.";
RL Clin. Genet. 99:594-600(2021).
RN [18]
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 [19]
RP ERRATUM OF PUBMED:17174896.
RA Liu Q., Greimann J.C., Lima C.D.;
RL Cell 131:188-189(2007).
RN [20] {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. EXOSC1 as
CC peripheral part of the Exo-9 complex stabilizes the hexameric ring of
CC RNase PH-domain subunits through contacts with EXOSC6 and EXOSC8.
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. 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. Interacts with EXOSC5, EXOSC7 and EXOSC10.
CC Interacts with DDX60. {ECO:0000269|PubMed:11719186,
CC ECO:0000269|PubMed:11812149, ECO:0000269|PubMed:20531389,
CC ECO:0000269|PubMed:21791617, ECO:0000269|PubMed:29906447}.
CC -!- INTERACTION:
CC Q9Y3B2; Q96DX5: ASB9; NbExp=3; IntAct=EBI-371892, EBI-745641;
CC Q9Y3B2; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-371892, EBI-742054;
CC Q9Y3B2; Q9NPD3: EXOSC4; NbExp=9; IntAct=EBI-371892, EBI-371823;
CC Q9Y3B2; Q9NQT4: EXOSC5; NbExp=33; IntAct=EBI-371892, EBI-371876;
CC Q9Y3B2; Q15024: EXOSC7; NbExp=9; IntAct=EBI-371892, EBI-371841;
CC Q9Y3B2; Q96B26: EXOSC8; NbExp=7; IntAct=EBI-371892, EBI-371922;
CC Q9Y3B2; Q719H9: KCTD1; NbExp=6; IntAct=EBI-371892, EBI-9027502;
CC Q9Y3B2; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-371892, EBI-739832;
CC Q9Y3B2; Q9P286: PAK5; NbExp=3; IntAct=EBI-371892, EBI-741896;
CC Q9Y3B2; Q04864: REL; NbExp=4; IntAct=EBI-371892, EBI-307352;
CC Q9Y3B2; Q04864-2: REL; NbExp=3; IntAct=EBI-371892, EBI-10829018;
CC Q9Y3B2; P15884: TCF4; NbExp=4; IntAct=EBI-371892, EBI-533224;
CC Q9Y3B2; P52747: ZNF143; NbExp=3; IntAct=EBI-371892, EBI-2849334;
CC Q9Y3B2; P36508: ZNF76; NbExp=3; IntAct=EBI-371892, EBI-7254550;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:11812149}.
CC Nucleus {ECO:0000305|PubMed:11812149}. Cytoplasm
CC {ECO:0000305|PubMed:11812149}.
CC -!- DISEASE: Pontocerebellar hypoplasia 1F (PCH1F) [MIM:619304]: A form of
CC pontocerebellar hypoplasia, a disorder characterized by structural
CC defects of the pons and cerebellum, evident upon brain imaging. PCH1F
CC is an autosomal recessive form characterized by hypotonia, global
CC developmental delay, poor overall growth, and dysmorphic facial
CC features. Brain imaging shows pontocerebellar hypoplasia, thin corpus
CC callosum, cerebral atrophy, and delayed myelination.
CC {ECO:0000269|PubMed:33463720}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the CSL4 family. {ECO:0000305}.
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DR EMBL; AF151866; AAD34103.1; -; mRNA.
DR EMBL; AK313717; BAG36460.1; -; mRNA.
DR EMBL; AL355490; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471066; EAW49936.1; -; Genomic_DNA.
DR EMBL; BC022067; AAH22067.1; -; mRNA.
DR CCDS; CCDS7459.1; -.
DR RefSeq; NP_001305291.1; NM_001318362.1.
DR RefSeq; NP_001305292.1; NM_001318363.1.
DR RefSeq; NP_001305293.1; NM_001318364.1.
DR RefSeq; NP_001305294.1; NM_001318365.1.
DR RefSeq; NP_001305295.1; NM_001318366.1.
DR RefSeq; NP_057130.1; NM_016046.4.
DR PDB; 2NN6; X-ray; 3.35 A; I=1-195.
DR PDB; 6D6Q; EM; 3.45 A; I=1-195.
DR PDB; 6D6R; EM; 3.45 A; I=1-195.
DR PDB; 6H25; EM; 3.80 A; I=1-195.
DR PDBsum; 2NN6; -.
DR PDBsum; 6D6Q; -.
DR PDBsum; 6D6R; -.
DR PDBsum; 6H25; -.
DR AlphaFoldDB; Q9Y3B2; -.
DR SMR; Q9Y3B2; -.
DR BioGRID; 119220; 101.
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; Q9Y3B2; -.
DR DIP; DIP-31261N; -.
DR IntAct; Q9Y3B2; 74.
DR MINT; Q9Y3B2; -.
DR STRING; 9606.ENSP00000359939; -.
DR GlyGen; Q9Y3B2; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9Y3B2; -.
DR PhosphoSitePlus; Q9Y3B2; -.
DR SwissPalm; Q9Y3B2; -.
DR BioMuta; EXOSC1; -.
DR DMDM; 14285410; -.
DR EPD; Q9Y3B2; -.
DR jPOST; Q9Y3B2; -.
DR MassIVE; Q9Y3B2; -.
DR MaxQB; Q9Y3B2; -.
DR PaxDb; Q9Y3B2; -.
DR PeptideAtlas; Q9Y3B2; -.
DR PRIDE; Q9Y3B2; -.
DR ProteomicsDB; 86000; -.
DR Antibodypedia; 30884; 242 antibodies from 25 providers.
DR DNASU; 51013; -.
DR Ensembl; ENST00000370902.8; ENSP00000359939.3; ENSG00000171311.13.
DR GeneID; 51013; -.
DR KEGG; hsa:51013; -.
DR MANE-Select; ENST00000370902.8; ENSP00000359939.3; NM_016046.5; NP_057130.1.
DR UCSC; uc001kni.4; human.
DR CTD; 51013; -.
DR DisGeNET; 51013; -.
DR GeneCards; EXOSC1; -.
DR HGNC; HGNC:17286; EXOSC1.
DR HPA; ENSG00000171311; Low tissue specificity.
DR MIM; 606493; gene.
DR MIM; 619304; phenotype.
DR neXtProt; NX_Q9Y3B2; -.
DR OpenTargets; ENSG00000171311; -.
DR PharmGKB; PA134900737; -.
DR VEuPathDB; HostDB:ENSG00000171311; -.
DR eggNOG; KOG3409; Eukaryota.
DR GeneTree; ENSGT00390000015287; -.
DR InParanoid; Q9Y3B2; -.
DR OMA; MDEMFRV; -.
DR OrthoDB; 1200489at2759; -.
DR PhylomeDB; Q9Y3B2; -.
DR TreeFam; TF316607; -.
DR PathwayCommons; Q9Y3B2; -.
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; Q9Y3B2; -.
DR SIGNOR; Q9Y3B2; -.
DR BioGRID-ORCS; 51013; 424 hits in 1083 CRISPR screens.
DR ChiTaRS; EXOSC1; human.
DR EvolutionaryTrace; Q9Y3B2; -.
DR GeneWiki; Exosome_component_1; -.
DR GenomeRNAi; 51013; -.
DR Pharos; Q9Y3B2; Tbio.
DR PRO; PR:Q9Y3B2; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q9Y3B2; protein.
DR Bgee; ENSG00000171311; Expressed in granulocyte and 179 other tissues.
DR ExpressionAtlas; Q9Y3B2; baseline and differential.
DR Genevisible; Q9Y3B2; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0000177; C:cytoplasmic exosome (RNase complex); IC:ComplexPortal.
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); IBA:GO_Central.
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; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:ComplexPortal.
DR GO; GO:0003723; F:RNA binding; NAS: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; IEA:UniProtKB-KW.
DR Gene3D; 2.40.50.140; -; 1.
DR InterPro; IPR039771; Csl4.
DR InterPro; IPR019495; EXOSC1_C.
DR InterPro; IPR025721; Exosome_cplx_N_dom.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR022967; S1_dom.
DR PANTHER; PTHR12686; PTHR12686; 1.
DR Pfam; PF14382; ECR1_N; 1.
DR Pfam; PF10447; EXOSC1; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Disease variant; Exosome; Neurodegeneration;
KW Nucleus; Phosphoprotein; Reference proteome; RNA-binding; rRNA processing.
FT CHAIN 1..195
FT /note="Exosome complex component CSL4"
FT /id="PRO_0000087127"
FT DOMAIN 66..147
FT /note="S1 motif"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 98
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 35
FT /note="S -> L (in PCH1F; decreased protein abundance)"
FT /evidence="ECO:0000269|PubMed:33463720"
FT /id="VAR_085726"
FT STRAND 13..16
FT /evidence="ECO:0007829|PDB:2NN6"
FT TURN 17..19
FT /evidence="ECO:0007829|PDB:2NN6"
FT STRAND 23..25
FT /evidence="ECO:0007829|PDB:2NN6"
FT STRAND 27..29
FT /evidence="ECO:0007829|PDB:2NN6"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:2NN6"
FT STRAND 41..45
FT /evidence="ECO:0007829|PDB:2NN6"
FT STRAND 49..52
FT /evidence="ECO:0007829|PDB:2NN6"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:6D6Q"
FT STRAND 70..78
FT /evidence="ECO:0007829|PDB:2NN6"
FT STRAND 80..93
FT /evidence="ECO:0007829|PDB:2NN6"
FT STRAND 103..106
FT /evidence="ECO:0007829|PDB:2NN6"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:2NN6"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:2NN6"
FT STRAND 124..135
FT /evidence="ECO:0007829|PDB:2NN6"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:6D6Q"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:2NN6"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:2NN6"
FT STRAND 152..155
FT /evidence="ECO:0007829|PDB:6D6Q"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:2NN6"
FT STRAND 165..168
FT /evidence="ECO:0007829|PDB:2NN6"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:2NN6"
FT TURN 175..178
FT /evidence="ECO:0007829|PDB:2NN6"
SQ SEQUENCE 195 AA; 21452 MW; E9C3B0A66F911195 CRC64;
MAPPVRYCIP GERLCNLEEG SPGSGTYTRH GYIFSSLAGC LMKSSENGAL PVVSVVRETE
SQLLPDVGAI VTCKVSSINS RFAKVHILYV GSMPLKNSFR GTIRKEDVRA TEKDKVEIYK
SFRPGDIVLA KVISLGDAQS NYLLTTAENE LGVVVAHSES GIQMVPISWC EMQCPKTHTK
EFRKVARVQP EFLQT
