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Exosome complex component RRP4 (Exosome component 2) (Ribosomal RNA-processing protein 4)

 EXOS2_HUMAN             Reviewed;         293 AA.
Q13868; A3KFL3; A3KFL4; B4DKK6; Q9NUY4;
27-APR-2001, integrated into UniProtKB/Swiss-Prot.
27-APR-2001, sequence version 2.
23-MAY-2018, entry version 177.
RecName: Full=Exosome complex component RRP4;
AltName: Full=Exosome component 2;
AltName: Full=Ribosomal RNA-processing protein 4;
Name=EXOSC2; Synonyms=RRP4;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Lung carcinoma;
Chissoe S.L.;
"Sequence of the human abl and bcr genes.";
Thesis (1994), University of Oklahoma, United States.
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND SEQUENCE REVISION.
TISSUE=Cervix adenocarcinoma;
PubMed=9390555; DOI=10.1016/S0092-8674(00)80432-8;
Mitchell P., Petfalski E., Shevchenko A., Mann M., Tollervey D.;
"The exosome: a conserved eukaryotic RNA processing complex containing
multiple 3'-->5' exoribonucleases.";
Cell 91:457-466(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Colon, Mammary gland, and Placenta;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
CHARACTERIZATION.
PubMed=8600032; DOI=10.1101/gad.10.4.502;
Mitchell P., Petfalski E., Tollervey D.;
"The 3' end of yeast 5.8S rRNA is generated by an exonuclease
processing mechanism.";
Genes Dev. 10:502-513(1996).
[8]
CHARACTERIZATION.
PubMed=10465791; DOI=10.1101/gad.13.16.2148;
Allmang C., Petfalski E., Podtelejnikov A., Mann M., Tollervey D.,
Mitchell P.;
"The yeast exosome and human PM-Scl are related complexes of 3'-->5'
exonucleases.";
Genes Dev. 13:2148-2158(1999).
[9]
IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE RNA EXOSOME
CORE COMPLEX, AND PROTEIN INTERACTION.
PubMed=11719186; DOI=10.1016/S0092-8674(01)00578-5;
Chen C.-Y., Gherzi R., Ong S.-E., Chan E.L., Raijmakers R.,
Pruijn G.J.M., Stoecklin G., Moroni C., Mann M., Karin M.;
"AU binding proteins recruit the exosome to degrade ARE-containing
mRNAs.";
Cell 107:451-464(2001).
[10]
INTERACTION WITH ZFP36L1.
PubMed=15687258; DOI=10.1101/gad.1282305;
Lykke-Andersen J., Wagner E.;
"Recruitment and activation of mRNA decay enzymes by two ARE-mediated
decay activation domains in the proteins TTP and BRF-1.";
Genes Dev. 19:351-361(2005).
[11]
FUNCTION IN MRNA DEGRADATION, AND SUBCELLULAR LOCATION.
PubMed=17545563; DOI=10.1261/rna.575107;
van Dijk E.L., Schilders G., Pruijn G.J.;
"Human cell growth requires a functional cytoplasmic exosome, which is
involved in various mRNA decay pathways.";
RNA 13:1027-1035(2007).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[15]
IDENTIFICATION IN THE RNA EXOSOME COMPLEX, IDENTIFICATION BY MASS
SPECTROMETRY, SUBCELLULAR LOCATION, AND INTERACTION WITH DIS3.
PubMed=20531389; DOI=10.1038/emboj.2010.122;
Staals R.H., Bronkhorst A.W., Schilders G., Slomovic S., Schuster G.,
Heck A.J., Raijmakers R., Pruijn G.J.;
"Dis3-like 1: a novel exoribonuclease associated with the human
exosome.";
EMBO J. 29:2358-2367(2010).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[18]
INTERACTION WITH GTPBP1.
PubMed=21515746; DOI=10.1096/fj.10-178715;
Woo K.C., Kim T.D., Lee K.H., Kim D.Y., Kim S., Lee H.R., Kang H.J.,
Chung S.J., Senju S., Nishimura Y., Kim K.T.;
"Modulation of exosome-mediated mRNA turnover by interaction of GTP-
binding protein 1 (GTPBP1) with its target mRNAs.";
FASEB J. 25:2757-2769(2011).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[20]
X-RAY CRYSTALLOGRAPHY (3.35 ANGSTROMS), AND RECONSTITUTION OF THE RNA
EXOSOME CORE COMPLEX.
PubMed=17174896; DOI=10.1016/j.cell.2006.10.037;
Liu Q., Greimann J.C., Lima C.D.;
"Reconstitution, activities, and structure of the eukaryotic RNA
exosome.";
Cell 127:1223-1237(2006).
[21]
ERRATUM.
Liu Q., Greimann J.C., Lima C.D.;
Cell 131:188-189(2007).
-!- FUNCTION: Non-catalytic component of the RNA exosome complex which
has 3'->5' exoribonuclease activity and participates in a
multitude of cellular RNA processing and degradation events. In
the nucleus, the RNA exosome complex is involved in proper
maturation of stable RNA species such as rRNA, snRNA and snoRNA,
in the elimination of RNA processing by-products and non-coding
'pervasive' transcripts, such as antisense RNA species and
promoter-upstream transcripts (PROMPTs), and of mRNAs with
processing defects, thereby limiting or excluding their export to
the cytoplasm. The RNA exosome may be involved in Ig class switch
recombination (CSR) and/or Ig variable region somatic
hypermutation (SHM) by targeting AICDA deamination activity to
transcribed dsDNA substrates. In the cytoplasm, the RNA exosome
complex is involved in general mRNA turnover and specifically
degrades inherently unstable mRNAs containing AU-rich elements
(AREs) within their 3' untranslated regions, and in RNA
surveillance pathways, preventing translation of aberrant mRNAs.
It seems to be involved in degradation of histone mRNA. The
catalytic inactive RNA exosome core complex of 9 subunits (Exo-9)
is proposed to play a pivotal role in the binding and presentation
of RNA for ribonucleolysis, and to serve as a scaffold for the
association with catalytic subunits and accessory proteins or
complexes. EXOSC2 as peripheral part of the Exo-9 complex
stabilizes the hexameric ring of RNase PH-domain subunits through
contacts with EXOSC4 and EXOSC7. {ECO:0000269|PubMed:17545563}.
-!- SUBUNIT: Component of the RNA exosome complex. Specifically part
of the catalytically inactive RNA exosome core (Exo-9) complex
which is believed to associate with catalytic subunits EXOSC10,
and DIS3 or DIS3L in cytoplasmic- and nuclear-specific RNA exosome
complex forms (PubMed:11719186, PubMed:20531389). Exo-9 is formed
by a hexameric ring of RNase PH domain-containing subunits
specifically containing the heterodimers EXOSC4-EXOSC9, EXOSC5-
EXOSC8 and EXOSC6-EXOSC7, and peripheral S1 domain-containing
components EXOSC1, EXOSC2 and EXOSC3 located on the top of the
ring structure (PubMed:11719186, PubMed:20531389). Interacts with
DIS3 (PubMed:20531389). Interacts with GTPBP1 (PubMed:21515746).
Interacts with ZFP36L1 (via N-terminus) (PubMed:15687258).
{ECO:0000269|PubMed:11719186, ECO:0000269|PubMed:15687258,
ECO:0000269|PubMed:20531389, ECO:0000269|PubMed:21515746}.
-!- INTERACTION:
Q8TF46-1:DIS3L; NbExp=2; IntAct=EBI-301735, EBI-3895807;
Q9NQT5:EXOSC3; NbExp=6; IntAct=EBI-301735, EBI-371866;
Q9NPD3:EXOSC4; NbExp=7; IntAct=EBI-301735, EBI-371823;
Q15024:EXOSC7; NbExp=6; IntAct=EBI-301735, EBI-371841;
Q99547:MPHOSPH6; NbExp=3; IntAct=EBI-301735, EBI-373187;
Q9H9D4:ZNF408; NbExp=3; IntAct=EBI-301735, EBI-347633;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus, nucleolus. Nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q13868-1; Sequence=Displayed;
Name=2;
IsoId=Q13868-2; Sequence=VSP_054921;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q13868-3; Sequence=VSP_057568;
-!- SIMILARITY: Belongs to the RRP4 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAB60392.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; U07561; AAB60392.1; ALT_SEQ; Genomic_DNA.
EMBL; AK001916; BAA91977.1; -; mRNA.
EMBL; AK022460; BAB14043.1; -; mRNA.
EMBL; AK296605; BAG59218.1; -; mRNA.
EMBL; AL359092; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471090; EAW87942.1; -; Genomic_DNA.
EMBL; CH471090; EAW87944.1; -; Genomic_DNA.
EMBL; BC000747; AAH00747.1; -; mRNA.
CCDS; CCDS65160.1; -. [Q13868-2]
CCDS; CCDS65161.1; -. [Q13868-3]
CCDS; CCDS6935.1; -. [Q13868-1]
RefSeq; NP_001269637.1; NM_001282708.1. [Q13868-2]
RefSeq; NP_001269638.1; NM_001282709.1. [Q13868-3]
RefSeq; NP_055100.2; NM_014285.6. [Q13868-1]
UniGene; Hs.654643; -.
PDB; 2NN6; X-ray; 3.35 A; H=1-293.
PDBsum; 2NN6; -.
ProteinModelPortal; Q13868; -.
BioGrid; 116977; 59.
CORUM; Q13868; -.
DIP; DIP-31264N; -.
IntAct; Q13868; 51.
MINT; Q13868; -.
STRING; 9606.ENSP00000361433; -.
iPTMnet; Q13868; -.
PhosphoSitePlus; Q13868; -.
SwissPalm; Q13868; -.
DMDM; 13878748; -.
EPD; Q13868; -.
MaxQB; Q13868; -.
PaxDb; Q13868; -.
PeptideAtlas; Q13868; -.
PRIDE; Q13868; -.
DNASU; 23404; -.
Ensembl; ENST00000372351; ENSP00000361426; ENSG00000130713. [Q13868-3]
Ensembl; ENST00000372358; ENSP00000361433; ENSG00000130713. [Q13868-1]
Ensembl; ENST00000546165; ENSP00000444917; ENSG00000130713. [Q13868-2]
GeneID; 23404; -.
KEGG; hsa:23404; -.
UCSC; uc004bzu.4; human. [Q13868-1]
UCSC; uc033djg.2; human.
CTD; 23404; -.
DisGeNET; 23404; -.
EuPathDB; HostDB:ENSG00000130713.15; -.
GeneCards; EXOSC2; -.
H-InvDB; HIX0008473; -.
HGNC; HGNC:17097; EXOSC2.
HPA; HPA021756; -.
HPA; HPA021790; -.
MalaCards; EXOSC2; -.
MIM; 602238; gene.
neXtProt; NX_Q13868; -.
OpenTargets; ENSG00000130713; -.
PharmGKB; PA134876020; -.
eggNOG; KOG3013; Eukaryota.
eggNOG; COG1097; LUCA.
GeneTree; ENSGT00440000033656; -.
HOGENOM; HOG000193685; -.
HOVERGEN; HBG051517; -.
InParanoid; Q13868; -.
KO; K03679; -.
OMA; QYAYEES; -.
OrthoDB; EOG091G0E3V; -.
PhylomeDB; Q13868; -.
TreeFam; TF105623; -.
Reactome; R-HSA-380994; ATF4 activates genes.
Reactome; R-HSA-429958; mRNA decay by 3' to 5' exoribonuclease.
Reactome; R-HSA-450385; Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA.
Reactome; R-HSA-450513; Tristetraprolin (TTP, ZFP36) binds and destabilizes mRNA.
Reactome; R-HSA-450604; KSRP (KHSRP) binds and destabilizes mRNA.
Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
ChiTaRS; EXOSC2; human.
EvolutionaryTrace; Q13868; -.
GeneWiki; Exosome_component_2; -.
GenomeRNAi; 23404; -.
PRO; PR:Q13868; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000130713; -.
CleanEx; HS_EXOSC2; -.
ExpressionAtlas; Q13868; baseline and differential.
Genevisible; Q13868; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0000177; C:cytoplasmic exosome (RNase complex); IBA:GO_Central.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0000178; C:exosome (RNase complex); IDA:UniProtKB.
GO; GO:0000176; C:nuclear exosome (RNase complex); IBA:GO_Central.
GO; GO:0005730; C:nucleolus; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0000175; F:3'-5'-exoribonuclease activity; TAS:ProtInc.
GO; GO:0008312; F:7S RNA binding; TAS:ProtInc.
GO; GO:0071034; P:CUT catabolic process; IBA:GO_Central.
GO; GO:0043928; P:exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay; IBA:GO_Central.
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.
GO; GO:0071035; P:nuclear polyadenylation-dependent rRNA catabolic process; IBA:GO_Central.
GO; GO:0071038; P:nuclear polyadenylation-dependent tRNA catabolic process; IBA:GO_Central.
GO; GO:0071049; P:nuclear retention of pre-mRNA with aberrant 3'-ends at the site of transcription; IBA:GO_Central.
GO; GO:0034427; P:nuclear-transcribed mRNA catabolic process, exonucleolytic, 3'-5'; IBA:GO_Central.
GO; GO:0071051; P:polyadenylation-dependent snoRNA 3'-end processing; IBA:GO_Central.
GO; GO:0030307; P:positive regulation of cell growth; IMP:UniProtKB.
GO; GO:0043488; P:regulation of mRNA stability; TAS:Reactome.
GO; GO:0006364; P:rRNA processing; TAS:Reactome.
GO; GO:0034475; P:U4 snRNA 3'-end processing; IBA:GO_Central.
InterPro; IPR025721; Exosome_cplx_N_dom.
InterPro; IPR026699; Exosome_RNA_bind1/RRP40/RRP4.
InterPro; IPR004088; KH_dom_type_1.
InterPro; IPR036612; KH_dom_type_1_sf.
InterPro; IPR012340; NA-bd_OB-fold.
PANTHER; PTHR21321; PTHR21321; 1.
Pfam; PF14382; ECR1_N; 1.
Pfam; PF15985; KH_6; 1.
SUPFAM; SSF50249; SSF50249; 1.
SUPFAM; SSF54791; SSF54791; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
Exosome; Nucleus; Phosphoprotein; Reference proteome; RNA-binding;
rRNA processing.
CHAIN 1 293 Exosome complex component RRP4.
/FTId=PRO_0000087129.
DOMAIN 79 159 S1 motif.
MOD_RES 124 124 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
VAR_SEQ 91 120 Missing (in isoform 3).
/FTId=VSP_057568.
VAR_SEQ 143 168 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_054921.
STRAND 45 47 {ECO:0000244|PDB:2NN6}.
STRAND 49 54 {ECO:0000244|PDB:2NN6}.
STRAND 56 63 {ECO:0000244|PDB:2NN6}.
STRAND 66 73 {ECO:0000244|PDB:2NN6}.
STRAND 80 82 {ECO:0000244|PDB:2NN6}.
STRAND 86 92 {ECO:0000244|PDB:2NN6}.
STRAND 95 99 {ECO:0000244|PDB:2NN6}.
STRAND 101 104 {ECO:0000244|PDB:2NN6}.
STRAND 106 111 {ECO:0000244|PDB:2NN6}.
HELIX 129 134 {ECO:0000244|PDB:2NN6}.
STRAND 144 149 {ECO:0000244|PDB:2NN6}.
TURN 150 152 {ECO:0000244|PDB:2NN6}.
STRAND 153 157 {ECO:0000244|PDB:2NN6}.
STRAND 171 173 {ECO:0000244|PDB:2NN6}.
STRAND 193 198 {ECO:0000244|PDB:2NN6}.
TURN 199 201 {ECO:0000244|PDB:2NN6}.
STRAND 202 206 {ECO:0000244|PDB:2NN6}.
HELIX 220 222 {ECO:0000244|PDB:2NN6}.
HELIX 228 246 {ECO:0000244|PDB:2NN6}.
HELIX 253 261 {ECO:0000244|PDB:2NN6}.
TURN 262 266 {ECO:0000244|PDB:2NN6}.
HELIX 275 289 {ECO:0000244|PDB:2NN6}.
TURN 290 292 {ECO:0000244|PDB:2NN6}.
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


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