RRP44_HUMAN
ID RRP44_HUMAN Reviewed; 958 AA.
AC Q9Y2L1; A6NI21; B2RBL2; Q5W0P7; Q5W0P8; Q658Z7; Q7Z481; Q8WWI2; Q9UG36;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 213.
DE RecName: Full=Exosome complex exonuclease RRP44;
DE EC=3.1.13.-;
DE EC=3.1.26.-;
DE AltName: Full=Protein DIS3 homolog;
DE AltName: Full=Ribosomal RNA-processing protein 44;
GN Name=DIS3; Synonyms=KIAA1008, RRP44;
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], AND CHARACTERIZATION.
RX PubMed=9562621; DOI=10.1093/oxfordjournals.jbchem.a022020;
RA Shiomi T., Fukushima K., Suzuki N., Nakashima N., Noguchi E., Nishimoto T.;
RT "Human dis3p, which binds to either GTP- or GDP-Ran, complements
RT Saccharomyces cerevisiae dis3.";
RL J. Biochem. 123:883-890(1998).
RN [2]
RP ERRATUM OF PUBMED:9562621.
RA Shiomi T., Fukushima K., Suzuki N., Nakashima N., Noguchi E., Nishimoto T.;
RL J. Biochem. 124:250-250(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT SER-269.
RC TISSUE=Brain, and Peripheral blood leukocyte;
RX PubMed=11935316; DOI=10.1007/s00439-001-0646-6;
RA Rozenblum E., Vahteristo P., Sandberg T., Bergthorsson J.T., Syrjakoski K.,
RA Weaver D., Haraldsson K., Johannsdottir H.K., Vehmanen P., Nigam S.,
RA Golberger N., Robbins C., Pak E., Dutra A., Gillander E., Stephan D.A.,
RA Bailey-Wilson J., Juo S.-H.H., Kainu T., Arason A., Barkardottir R.B.,
RA Nevanlinna H., Borg A., Kallioniemi O.-P.;
RT "A genomic map of a 6-Mb region at 13q21-q22 implicated in cancer
RT development: identification and characterization of candidate genes.";
RL Hum. Genet. 110:111-121(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT ARG-326.
RC TISSUE=Brain;
RX PubMed=10231032; DOI=10.1093/dnares/6.1.63;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:63-70(1999).
RN [5]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT SER-269.
RC TISSUE=Trachea;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT SER-269.
RC TISSUE=Lymph node, and Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [9]
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 [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ARG-326.
RC TISSUE=Lymph;
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 [11]
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 [12]
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 [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-18, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [14]
RP ASSOCIATION WITH THE RNA EXOSOME COMPLEX, IDENTIFICATION BY MASS
RP SPECTROMETRY, FUNCTION, COFACTOR, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP ASP-146 AND ASP-487.
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 [15]
RP ASSOCIATION WITH THE RNA EXOSOME COMPLEX, IDENTIFICATION BY MASS
RP SPECTROMETRY, SUBCELLULAR LOCATION, AND INTERACTION WITH EXOSC3.
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 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 [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, 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., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215, 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 [19]
RP INTERACTION WITH DHX34.
RX PubMed=25220460; DOI=10.1016/j.celrep.2014.08.020;
RA Hug N., Caceres J.F.;
RT "The RNA helicase DHX34 activates NMD by promoting a transition from the
RT surveillance to the decay-inducing complex.";
RL Cell Rep. 8:1845-1856(2014).
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: 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 DIS3 has both 3'-5' exonuclease and endonuclease activities.
CC {ECO:0000269|PubMed:19056938, ECO:0000269|PubMed:20531386}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:20531386};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:20531386};
CC -!- SUBUNIT: Component of the RNA exosome complex (PubMed:29906447). The
CC catalytically inactive RNA exosome core (Exo-9) complex is believed to
CC associate with catalytic subunits EXOSC10, and DIS3 or DIS3L in
CC cytoplasmic- and nuclear-specific RNA exosome complex forms
CC (PubMed:29906447). Interacts with DHX34; the interaction is RNA-
CC independent (PubMed:25220460). {ECO:0000269|PubMed:25220460,
CC ECO:0000269|PubMed:29906447}.
CC -!- INTERACTION:
CC Q9Y2L1; Q01780: EXOSC10; NbExp=4; IntAct=EBI-373539, EBI-358236;
CC Q9Y2L1; Q9NQT5: EXOSC3; NbExp=3; IntAct=EBI-373539, EBI-371866;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20531386}. Nucleus,
CC nucleolus {ECO:0000269|PubMed:12429849}. Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:20531389}. Nucleus {ECO:0000269|PubMed:20531386}.
CC Note=Predominantly located in the nucleus (PubMed:20531386). According
CC to PubMed:12429849, found in the nucleolus (PubMed:12429849). According
CC to PubMed:20531386, excluded from nucleolus supporting the existence of
CC a nucleolar RNA exosome complex devoid of DIS3 (PubMed:20531386).
CC {ECO:0000269|PubMed:12429849, ECO:0000269|PubMed:20531386}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Y2L1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y2L1-2; Sequence=VSP_014971;
CC -!- TISSUE SPECIFICITY: Widely expressed.
CC -!- MISCELLANEOUS: The association of DIS3 with the RNA exosome complex
CC appears to be weak explaining its absence in some complex
CC purifications.
CC -!- SIMILARITY: Belongs to the RNR ribonuclease family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA76852.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF330044; AAL37479.1; -; mRNA.
DR EMBL; AB023225; BAA76852.2; ALT_INIT; mRNA.
DR EMBL; AL832266; CAH56266.1; -; mRNA.
DR EMBL; AK314715; BAG37259.1; -; mRNA.
DR EMBL; AL080158; CAB45749.1; -; mRNA.
DR EMBL; AL138695; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL391384; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471093; EAW80517.1; -; Genomic_DNA.
DR EMBL; BC056143; AAH56143.1; -; mRNA.
DR CCDS; CCDS45057.1; -. [Q9Y2L1-2]
DR CCDS; CCDS9447.1; -. [Q9Y2L1-1]
DR PIR; JE0110; JE0110.
DR RefSeq; NP_001121698.1; NM_001128226.2. [Q9Y2L1-2]
DR RefSeq; NP_055768.3; NM_014953.4. [Q9Y2L1-1]
DR PDB; 6D6Q; EM; 3.45 A; K=1-958.
DR PDB; 6D6R; EM; 3.45 A; K=1-958.
DR PDB; 6H25; EM; 3.80 A; J=1-958.
DR PDBsum; 6D6Q; -.
DR PDBsum; 6D6R; -.
DR PDBsum; 6H25; -.
DR AlphaFoldDB; Q9Y2L1; -.
DR SMR; Q9Y2L1; -.
DR BioGRID; 116559; 176.
DR ComplexPortal; CPX-476; Nuclear exosome complex, DIS3-EXOSC10 variant.
DR ComplexPortal; CPX-593; Exosome complex, DIS3 variant.
DR CORUM; Q9Y2L1; -.
DR IntAct; Q9Y2L1; 49.
DR MINT; Q9Y2L1; -.
DR STRING; 9606.ENSP00000366997; -.
DR GlyGen; Q9Y2L1; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9Y2L1; -.
DR MetOSite; Q9Y2L1; -.
DR PhosphoSitePlus; Q9Y2L1; -.
DR SwissPalm; Q9Y2L1; -.
DR BioMuta; DIS3; -.
DR DMDM; 73620993; -.
DR SWISS-2DPAGE; Q9Y2L1; -.
DR EPD; Q9Y2L1; -.
DR jPOST; Q9Y2L1; -.
DR MassIVE; Q9Y2L1; -.
DR MaxQB; Q9Y2L1; -.
DR PaxDb; Q9Y2L1; -.
DR PeptideAtlas; Q9Y2L1; -.
DR PRIDE; Q9Y2L1; -.
DR ProteomicsDB; 85832; -. [Q9Y2L1-1]
DR ProteomicsDB; 85833; -. [Q9Y2L1-2]
DR Antibodypedia; 24401; 229 antibodies from 30 providers.
DR DNASU; 22894; -.
DR Ensembl; ENST00000377767.9; ENSP00000366997.4; ENSG00000083520.15. [Q9Y2L1-1]
DR Ensembl; ENST00000377780.8; ENSP00000367011.4; ENSG00000083520.15. [Q9Y2L1-2]
DR GeneID; 22894; -.
DR KEGG; hsa:22894; -.
DR MANE-Select; ENST00000377767.9; ENSP00000366997.4; NM_014953.5; NP_055768.3.
DR UCSC; uc001vix.6; human. [Q9Y2L1-1]
DR CTD; 22894; -.
DR DisGeNET; 22894; -.
DR GeneCards; DIS3; -.
DR HGNC; HGNC:20604; DIS3.
DR HPA; ENSG00000083520; Low tissue specificity.
DR MIM; 607533; gene.
DR neXtProt; NX_Q9Y2L1; -.
DR OpenTargets; ENSG00000083520; -.
DR PharmGKB; PA162383628; -.
DR VEuPathDB; HostDB:ENSG00000083520; -.
DR eggNOG; KOG2102; Eukaryota.
DR GeneTree; ENSGT00530000063106; -.
DR InParanoid; Q9Y2L1; -.
DR OMA; VVKRNWR; -.
DR OrthoDB; 1104619at2759; -.
DR PhylomeDB; Q9Y2L1; -.
DR TreeFam; TF105755; -.
DR PathwayCommons; Q9Y2L1; -.
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; Q9Y2L1; -.
DR BioGRID-ORCS; 22894; 567 hits in 1089 CRISPR screens.
DR ChiTaRS; DIS3; human.
DR GeneWiki; DIS3; -.
DR GenomeRNAi; 22894; -.
DR Pharos; Q9Y2L1; Tbio.
DR PRO; PR:Q9Y2L1; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; Q9Y2L1; protein.
DR Bgee; ENSG00000083520; Expressed in sperm and 189 other tissues.
DR ExpressionAtlas; Q9Y2L1; baseline and differential.
DR Genevisible; Q9Y2L1; HS.
DR GO; GO:0000177; C:cytoplasmic exosome (RNase complex); IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0000178; C:exosome (RNase complex); IBA:GO_Central.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0000176; C:nuclear exosome (RNase complex); IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:ComplexPortal.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; IMP:UniProtKB.
DR GO; GO:0004519; F:endonuclease activity; IMP:UniProtKB.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0071034; P:CUT catabolic process; IMP:UniProtKB.
DR GO; GO:0043928; P:exonucleolytic catabolism of deadenylated mRNA; TAS:Reactome.
DR GO; GO:0006401; P:RNA catabolic process; IDA:ComplexPortal.
DR GO; GO:0006396; P:RNA processing; IDA:ComplexPortal.
DR GO; GO:0016075; P:rRNA catabolic process; IMP:UniProtKB.
DR GO; GO:0006364; P:rRNA processing; TAS:UniProtKB.
DR Gene3D; 2.40.50.140; -; 1.
DR InterPro; IPR041505; Dis3_CSD2.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR029060; PIN-like_dom_sf.
DR InterPro; IPR002716; PIN_dom.
DR InterPro; IPR001900; RNase_II/R.
DR InterPro; IPR022966; RNase_II/R_CS.
DR InterPro; IPR033771; Rrp44_CSD1.
DR InterPro; IPR033770; RRP44_S1.
DR Pfam; PF17849; OB_Dis3; 1.
DR Pfam; PF13638; PIN_4; 1.
DR Pfam; PF00773; RNB; 1.
DR Pfam; PF17216; Rrp44_CSD1; 1.
DR Pfam; PF17215; Rrp44_S1; 1.
DR SMART; SM00670; PINc; 1.
DR SMART; SM00955; RNB; 1.
DR SUPFAM; SSF50249; SSF50249; 3.
DR SUPFAM; SSF88723; SSF88723; 1.
DR PROSITE; PS01175; RIBONUCLEASE_II; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm; Endonuclease;
KW Exonuclease; Exosome; Hydrolase; Magnesium; Manganese; Nuclease; Nucleus;
KW Phosphoprotein; Reference proteome; RNA-binding; rRNA processing.
FT CHAIN 1..958
FT /note="Exosome complex exonuclease RRP44"
FT /id="PRO_0000166419"
FT DOMAIN 64..182
FT /note="PINc"
FT REGION 938..958
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 18
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 215
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 78..129
FT /note="DVLEDPAIRNVIVLQTVLQEVRNRSAPVYKRIRDVTNNQEKHFYTFTNEHHR
FT -> VSAWRPGTWASVASSLRLPGSL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10231032"
FT /id="VSP_014971"
FT VARIANT 269
FT /note="N -> S (in dbSNP:rs4883918)"
FT /evidence="ECO:0000269|PubMed:11935316,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:17974005"
FT /id="VAR_023099"
FT VARIANT 326
FT /note="T -> R (in dbSNP:rs7332388)"
FT /evidence="ECO:0000269|PubMed:10231032,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_023100"
FT MUTAGEN 146
FT /note="D->N: Loss of endonuclease activity; when associated
FT with N-487."
FT /evidence="ECO:0000269|PubMed:20531386"
FT MUTAGEN 487
FT /note="D->N: Loss of exonuclease activity. Loss of
FT endonuclease activity; when associated with N-146."
FT /evidence="ECO:0000269|PubMed:20531386"
FT CONFLICT 635
FT /note="P -> S (in Ref. 7; CAH56266)"
FT /evidence="ECO:0000305"
FT STRAND 2..10
FT /evidence="ECO:0007829|PDB:6D6Q"
FT STRAND 12..14
FT /evidence="ECO:0007829|PDB:6D6Q"
FT STRAND 16..24
FT /evidence="ECO:0007829|PDB:6D6Q"
FT HELIX 70..75
FT /evidence="ECO:0007829|PDB:6D6Q"
FT HELIX 77..81
FT /evidence="ECO:0007829|PDB:6D6Q"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:6D6Q"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:6D6Q"
FT HELIX 93..101
FT /evidence="ECO:0007829|PDB:6D6Q"
FT HELIX 103..113
FT /evidence="ECO:0007829|PDB:6D6Q"
FT STRAND 116..122
FT /evidence="ECO:0007829|PDB:6D6Q"
FT TURN 129..131
FT /evidence="ECO:0007829|PDB:6D6Q"
FT HELIX 141..163
FT /evidence="ECO:0007829|PDB:6D6Q"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:6D6Q"
FT STRAND 173..177
FT /evidence="ECO:0007829|PDB:6D6Q"
FT HELIX 178..186
FT /evidence="ECO:0007829|PDB:6D6Q"
FT HELIX 194..200
FT /evidence="ECO:0007829|PDB:6D6Q"
FT HELIX 206..209
FT /evidence="ECO:0007829|PDB:6D6Q"
FT HELIX 234..243
FT /evidence="ECO:0007829|PDB:6D6Q"
FT STRAND 247..252
FT /evidence="ECO:0007829|PDB:6D6Q"
FT STRAND 261..265
FT /evidence="ECO:0007829|PDB:6D6Q"
FT STRAND 274..277
FT /evidence="ECO:0007829|PDB:6D6Q"
FT TURN 280..282
FT /evidence="ECO:0007829|PDB:6D6Q"
FT STRAND 291..296
FT /evidence="ECO:0007829|PDB:6D6Q"
FT STRAND 342..350
FT /evidence="ECO:0007829|PDB:6D6Q"
FT STRAND 356..361
FT /evidence="ECO:0007829|PDB:6D6Q"
FT STRAND 371..377
FT /evidence="ECO:0007829|PDB:6D6Q"
FT STRAND 383..385
FT /evidence="ECO:0007829|PDB:6D6Q"
FT STRAND 391..393
FT /evidence="ECO:0007829|PDB:6D6Q"
FT STRAND 396..404
FT /evidence="ECO:0007829|PDB:6D6Q"
FT STRAND 413..422
FT /evidence="ECO:0007829|PDB:6D6Q"
FT HELIX 426..436
FT /evidence="ECO:0007829|PDB:6D6Q"
FT HELIX 446..451
FT /evidence="ECO:0007829|PDB:6D6Q"
FT HELIX 463..465
FT /evidence="ECO:0007829|PDB:6D6Q"
FT STRAND 466..469
FT /evidence="ECO:0007829|PDB:6D6Q"
FT STRAND 489..494
FT /evidence="ECO:0007829|PDB:6D6Q"
FT STRAND 500..506
FT /evidence="ECO:0007829|PDB:6D6Q"
FT HELIX 509..511
FT /evidence="ECO:0007829|PDB:6D6Q"
FT HELIX 518..525
FT /evidence="ECO:0007829|PDB:6D6Q"
FT HELIX 542..546
FT /evidence="ECO:0007829|PDB:6D6Q"
FT STRAND 555..566
FT /evidence="ECO:0007829|PDB:6D6Q"
FT STRAND 574..585
FT /evidence="ECO:0007829|PDB:6D6Q"
FT HELIX 590..598
FT /evidence="ECO:0007829|PDB:6D6Q"
FT TURN 604..606
FT /evidence="ECO:0007829|PDB:6D6Q"
FT HELIX 607..626
FT /evidence="ECO:0007829|PDB:6D6Q"
FT HELIX 658..681
FT /evidence="ECO:0007829|PDB:6D6Q"
FT STRAND 683..685
FT /evidence="ECO:0007829|PDB:6D6Q"
FT STRAND 688..691
FT /evidence="ECO:0007829|PDB:6D6Q"
FT TURN 696..699
FT /evidence="ECO:0007829|PDB:6D6Q"
FT HELIX 700..708
FT /evidence="ECO:0007829|PDB:6D6Q"
FT HELIX 718..725
FT /evidence="ECO:0007829|PDB:6D6Q"
FT HELIX 737..745
FT /evidence="ECO:0007829|PDB:6D6Q"
FT STRAND 752..754
FT /evidence="ECO:0007829|PDB:6D6Q"
FT TURN 756..758
FT /evidence="ECO:0007829|PDB:6D6Q"
FT TURN 765..767
FT /evidence="ECO:0007829|PDB:6D6Q"
FT HELIX 783..795
FT /evidence="ECO:0007829|PDB:6D6Q"
FT HELIX 802..804
FT /evidence="ECO:0007829|PDB:6D6Q"
FT HELIX 807..842
FT /evidence="ECO:0007829|PDB:6D6Q"
FT STRAND 846..848
FT /evidence="ECO:0007829|PDB:6D6Q"
FT STRAND 857..859
FT /evidence="ECO:0007829|PDB:6D6Q"
FT STRAND 862..864
FT /evidence="ECO:0007829|PDB:6D6Q"
FT TURN 865..868
FT /evidence="ECO:0007829|PDB:6D6Q"
FT STRAND 869..871
FT /evidence="ECO:0007829|PDB:6D6Q"
FT STRAND 886..888
FT /evidence="ECO:0007829|PDB:6D6R"
FT TURN 889..892
FT /evidence="ECO:0007829|PDB:6D6Q"
FT STRAND 893..895
FT /evidence="ECO:0007829|PDB:6D6Q"
FT STRAND 908..911
FT /evidence="ECO:0007829|PDB:6D6Q"
FT STRAND 916..918
FT /evidence="ECO:0007829|PDB:6D6Q"
FT STRAND 925..928
FT /evidence="ECO:0007829|PDB:6D6Q"
SQ SEQUENCE 958 AA; 109003 MW; 92336BA0D06247FE CRC64;
MLKSKTFLKK TRAGGVMKIV REHYLRDDIG CGAPGCAACG GAHEGPALEP QPQDPASSVC
PQPHYLLPDT NVLLHQIDVL EDPAIRNVIV LQTVLQEVRN RSAPVYKRIR DVTNNQEKHF
YTFTNEHHRE TYVEQEQGEN ANDRNDRAIR VAAKWYNEHL KKMSADNQLQ VIFITNDRRN
KEKAIEEGIP AFTCEEYVKS LTANPELIDR LACLSEEGNE IESGKIIFSE HLPLSKLQQG
IKSGTYLQGT FRASRENYLE ATVWIHGDNE ENKEIILQGL KHLNRAVHED IVAVELLPKS
QWVAPSSVVL HDEGQNEEDV EKEEETERML KTAVSEKMLK PTGRVVGIIK RNWRPYCGML
SKSDIKESRR HLFTPADKRI PRIRIETRQA STLEGRRIIV AIDGWPRNSR YPNGHFVRNL
GDVGEKETET EVLLLEHDVP HQPFSQAVLS FLPKMPWSIT EKDMKNREDL RHLCICSVDP
PGCTDIDDAL HCRELENGNL EVGVHIADVS HFIRPGNALD QESARRGTTV YLCEKRIDMV
PELLSSNLCS LKCDVDRLAF SCIWEMNHNA EILKTKFTKS VINSKASLTY AEAQLRIDSA
NMNDDITTSL RGLNKLAKIL KKRRIEKGAL TLSSPEVRFH MDSETHDPID LQTKELRETN
SMVEEFMLLA NISVAKKIHE EFSEHALLRK HPAPPPSNYE ILVKAARSRN LEIKTDTAKS
LAESLDQAES PTFPYLNTLL RILATRCMMQ AVYFCSGMDN DFHHYGLASP IYTHFTSPIR
RYADVIVHRL LAVAIGADCT YPELTDKHKL ADICKNLNFR HKMAQYAQRA SVAFHTQLFF
KSKGIVSEEA YILFVRKNAI VVLIPKYGLE GTVFFEEKDK PNPQLIYDDE IPSLKIEDTV
FHVFDKVKVK IMLDSSNLQH QKIRMSLVEP QIPGISIPTD TSNMDLNGPK KKKMKLGK
