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Exosome complex component RRP4

 
Known also as: Exosome component 2, Ribosomal RNA-processing protein 4

Known abbreviations: EXOSC2, RRP4

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.

SUBUNIT STRUCTURE:

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. 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. Interacts with GTPBP1.

CELLULAR LOCALIZATION:

Cytoplasm. Nucleus › nucleolus. Nucleus.



This protein can be a part of a given complexes:
NCBI GI number(s): 19923403
189027053
Species: Homo sapiens

Links to other databases:

Database ID Link
Uniprot Q13868 Q13868
BRENDA - -
KEGG hsa:23404 hsa:23404
PFAM: - Q13868 (Link - using uniprot id)
InterPro: - Q13868 (Link - using uniprot id)
CATH: - -
SCOP: - -
Solved crystal structures: 2NN6
[PDB] [details]


Protein sequence:
MAMEMRLPVARKPLSERLGRDTKKHLVVPGDTITTDTGFMRGHGTYMGEE
KLIASVAGSVERVNKLICVKALKTRYIGEVGDIVVGRITEVQQKRWKVET
NSRLDSVLLLSSMNLPGGELRRRSAEDELAMRGFLQEGDLISAEVQAVFS
DGAVSLHTRSLKYGKLGQGVLVQVSPSLVKRQKTHFHDLPCGASVILGNN
GFIWIYPTPEHKEEEAGGFIANLEPVSLADREVISRLRNCIISLVTQRMM
LYDTSILYCYEASLPHQIKDILKPEIMEEIVMETRQRLLEQEG

Exosome complex component RRP4 (Homo sapiens) is product of expression of EXOSC2 exosome component 2 gene.

References:

Title Authors Journal Publication date (Issue) PubMed ID
Reconstitution, activities, and structure of the eukaryotic RNA exosome. Liu Q, Greimann JC, Lima CD Cell 2006-12-15 (127) 17174896
RNA channelling by the archaeal exosome. Lorentzen E, Dziembowski A, Lindner D, Seraphin B, Conti E EMBO Rep 2007-05-01 (8) 17380186
The exosome: a conserved eukaryotic RNA processing complex containing multiple 3'-->5' exoribonucleases. Mitchell P, Petfalski E, Shevchenko A, Mann M, Tollervey D Cell 1997-11-14 (91) 9390555
The yeast exosome and human PM-Scl are related complexes of 3' --> 5' exonucleases. Allmang C, Petfalski E, Podtelejnikov A, Mann M, Tollervey D, Mitchell P Genes Dev 1999-08-15 (13) 10465791
The 3' end of yeast 5.8S rRNA is generated by an exonuclease processing mechanism. Mitchell P, Petfalski E, Tollervey D Genes Dev 1996-01-15 (10) 8600032
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, K Genome Res 2004-10-01 (14) 15489334
Complete sequencing and characterization of 21,243 full-length human cDNAs. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K Nat Genet 2004-02-01 (36) 14702039
Human cell growth requires a functional cytoplasmic exosome, which is involved in various mRNA decay pathways. van Dijk EL, Schilders G, Pruijn GJ RNA 2007-07-01 (13) 17545563
AU binding proteins recruit the exosome to degrade ARE-containing mRNAs. Chen CY, Gherzi R, Ong SE, Chan EL, Raijmakers R, Pruijn GJ, Stoecklin G, Moroni C, Mann M, Karin M Cell 2001-11-16 (107) 11719186
Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S Anal Chem 2009-06-01 (81) 19413330
Initial characterization of the human central proteome. Burkard TR, Planyavsky M, Kaupe I, Breitwieser FP, Burckstummer T, Bennett KL, Superti-Furga G, Colinge J BMC Syst Biol 2011-01-01 (5) 21269460
Lysine acetylation targets protein complexes and co-regulates major cellular functions. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M Science 2009-08-14 (325) 19608861
A quantitative atlas of mitotic phosphorylation. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP Proc Natl Acad Sci U S A 2008-08-05 (105) 18669648
Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK Sci Signal 2009-01-01 (2) 19690332
DNA sequence and analysis of human chromosome 9. Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE Nature 2004-05-27 (429) 15164053
Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis. Wang B, Malik R, Nigg EA, Korner R Anal Chem 2008-12-15 (80) 19007248
Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y Anal Sci 2008-02-01 (24) 18187866
Dis3-like 1: a novel exoribonuclease associated with the human exosome. Staals RH, Bronkhorst AW, Schilders G, Slomovic S, Schuster G, Heck AJ, Raijmakers R, Pruijn GJ EMBO J 2010-07-21 (29) 20531389
Modulation of exosome-mediated mRNA turnover by interaction of GTP-binding protein 1 (GTPBP1) with its target mRNAs. Woo KC, Kim TD, Lee KH, Kim DY, Kim S, Lee HR, Kang HJ, Chung SJ, Senju S, Nishimura Y, Kim KT FASEB J 2011-08-01 (25) 21515746



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Last modification of this entry: Sept. 25, 2012.

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