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Exosome complex exonuclease RRP41

Known also as: Exosome component 4

Known abbreviations: hRrp41


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. EXOSC4 binds to ARE-containing RNAs.


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.


Cytoplasm. Nucleus › nucleolus. Nucleus

This protein can be a part of a given complexes:
NCBI GI number(s): 9506689
Species: Homo sapiens

Links to other databases:

Database ID Link
Uniprot Q9NPD3 Q9NPD3
KEGG 54512 54512
PFAM: - Q9NPD3 (Link - using uniprot id)
InterPro: - Q9NPD3 (Link - using uniprot id)
CATH: - -
SCOP: - -
Solved crystal structures: 2NN6
[PDB] [details]

Protein sequence:

Exosome complex exonuclease RRP41 (Homo sapiens) is product of expression of EXOSC4 gene.

Exosome complex exonuclease RRP41 (Homo sapiens) belongs to following protein families:

Title Authors Journal Publication date (Issue) PubMed ID
Three novel components of the human exosome. Brouwer R, Allmang C, Raijmakers R, van Aarssen Y, Egberts WV, Petfalski E, van Venrooij WJ, Tollervey D, Pruijn GJ J Biol Chem 2001-03-02 (276) 11110791
Sequence-specific RNA binding mediated by the RNase PH domain of components of the exosome. Anderson JR, Mukherjee D, Muthukumaraswamy K, Moraes KC, Wilusz CJ, Wilusz J RNA 2006-10-01 (12) 16912217
Reconstitution, activities, and structure of the eukaryotic RNA exosome. Liu Q, Greimann JC, Lima CD Cell 2006-12-15 (127) 17174896
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 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
Degradation of histone mRNA requires oligouridylation followed by decapping and simultaneous degradation of the mRNA both 5' to 3' and 3' to 5'. Mullen TE, Marzluff WF Genes Dev 2008-02-01 (22) 18172165
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
DNA sequence and analysis of human chromosome 8. Nusbaum C, Mikkelsen TS, Zody MC, Asakawa S, Taudien S, Garber M, Kodira CD, Schueler MG, Shimizu A, Whittaker CA Nature 2006-02-19 (439) 16421571
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
The RNA exosome targets the AID cytidine deaminase to both strands of transcribed duplex DNA substrates. Basu U, Meng FL, Keim C, Grinstein V, Pefanis E, Eccleston J, Zhang T, Myers D, Wasserman CR, Wesemann DR, Januszyk K, Gregory RI, Deng H, Lima CD, Alt FW Cell 2011-01-04 (144) 21255825
DDX60, a DEXD/H box helicase, is a novel antiviral factor promoting RIG-I-like receptor-mediated signaling. Miyashita M, Oshiumi H, Matsumoto M, Seya T Mol Cell Biol 2011-09-01 (31) 21791617
Addition of poly(A) and poly(A)-rich tails during RNA degradation in the cytoplasm of human cells. Slomovic S, Fremder E, Staals RH, Pruijn GJ, Schuster G Proc Natl Acad Sci U S A 2010-04-20 (107) 20368444

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

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