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Exosome complex component RRP42

 
Known also as: Exosome component 7, p8, Ribosomal RNA-processing protein 42

Known abbreviations: hRrp42, EXOS7, KIAA0116

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.

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 EXOSC1.

CELLULAR LOCALIZATION:

Nucleus › nucleolus. Cytoplasm (Probable). Nucleus (Probable)



This protein can be a part of a given complexes:
NCBI GI number(s): 189083688
Species: Homo sapiens

Links to other databases:

Database ID Link
Uniprot Q15024 Q15024
BRENDA - -
KEGG - -
PFAM: - Q15024 (Link - using uniprot id)
InterPro: - Q15024 (Link - using uniprot id)
CATH: - -
SCOP: - -
Solved crystal structures: 2NN6
[PDB] [details]


Protein sequence:
MASVTLSEAEKVYIVHGVQEDLRVDGRGCEDYRCVEVETDVVSNTSGSAR
VKLGHTDILVGVKAEMGTPKLEKPNEGYLEFFVDCSASATPEFEGRGGDD
LGTEIANTLYRIFNNKSSVDLKTLCISPREHCWVLYVDVLLLECGGNLFD
AISIAVKAALFNTRIPRVRVLEDEEGSKDIELSDDPYDCIRLSVENVPCI
VTLCKIGYRHVVDATLQEEACSLASLLVSVTSKGVVTCMRKVGKGSLDPE
SIFEMMETGKRVGKVLHASLQSVVHKEESLGPKRQKVGFLG

Exosome complex component RRP42 (Homo sapiens) is product of expression of EXOSC7 exosome component 7 gene.

Exosome complex component RRP42 (Homo sapiens) belongs to following protein families:
References:

Title Authors Journal Publication date (Issue) PubMed ID
Protein-protein interactions between human exosome components support the assembly of RNase PH-type subunits into a six-membered PNPase-like ring. Raijmakers R, Egberts WV, van Venrooij WJ, Pruijn GJ J Mol Biol 2002-11-01 (323) 12419256
Protein-protein interactions of hCsl4p with other human exosome subunits. Raijmakers R, Noordman YE, van Venrooij WJ, Pruijn GJ J Mol Biol 2002-02-25 (315) 11812149
A protein interaction framework for human mRNA degradation. Lehner B, Sanderson CM Genome Res 2004-07-01 (14) 15231747
Reconstitution, activities, and structure of the eukaryotic RNA exosome. Liu Q, Greimann JC, Lima CD Cell 2006-12-15 (127) 17174896
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
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
The DNA sequence, annotation and analysis of human chromosome 3. Muzny DM, Scherer SE, Kaul R, Wang J, Yu J, Sudbrak R, Buhay CJ, Chen R, Cree A, Ding Y Nature 2006-04-27 (440) 16641997
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
Prediction of the coding sequences of unidentified human genes. III. The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of cDNA clones from human cell line KG-1. Nagase T, Miyajima N, Tanaka A, Sazuka T, Seki N, Sato S, Tabata S, Ishikawa K, Kawarabayasi Y, Kotani H, et al. DNA Res 1995-01-01 (2) 7788527
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



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

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