Exosome component 8

EXOSC8
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2NN6
Identifiers
Aliases	EXOSC8, CIP3, EAP2, OIP2, RRP43, Rrp43p, bA421P11.3, p9, PCH1C, Exosome component 8
External IDs	OMIM: 606019; MGI: 1916889; HomoloGene: 12323; GeneCards: EXOSC8; OMA:EXOSC8 - orthologs
Gene location (Human) Chr. Chromosome 13 (human) Band 13q13.3 Start 36,998,816 bp End 37,025,881 bp
Gene location (Mouse) Chr. Chromosome 3 (mouse) Band 3|3 C Start 54,636,099 bp End 54,642,814 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in ventricular zone ganglionic eminence right uterine tube gonad left ovary right ovary right testis left testis body of uterus canal of the cervix Top expressed in yolk sac tail of embryo genital tubercle blastocyst primitive streak morula medial ganglionic eminence endothelial cell of lymphatic vessel ventricular zone endocardial cushion More reference expression data BioGPS More reference expression data
Gene ontology Molecular function exoribonuclease activity protein binding RNA binding identical protein binding mRNA 3'-UTR AU-rich region binding Cellular component cytoplasm cytosol exosome (RNase complex) nucleolus nucleus nucleoplasm nuclear exosome (RNase complex) cytoplasmic exosome (RNase complex) Biological process regulation of mRNA stability RNA processing RNA catabolic process rRNA processing exonucleolytic trimming to generate mature 3'-end of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) nuclear-transcribed mRNA catabolic process, exonucleolytic, 3'-5' U1 snRNA 3'-end processing U4 snRNA 3'-end processing U5 snRNA 3'-end processing exonucleolytic catabolism of deadenylated mRNA nuclear mRNA surveillance nuclear polyadenylation-dependent rRNA catabolic process nuclear polyadenylation-dependent tRNA catabolic process nuclear polyadenylation-dependent mRNA catabolic process biological process rRNA catabolic process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 11340 69639 Ensembl ENSG00000120699 ENSMUSG00000027752 UniProt Q96B26 Q9D753 RefSeq (mRNA) NM_181503 NM_001163570 NM_027148 RefSeq (protein) NP_852480 NP_001157042 NP_081424 Location (UCSC) Chr 13: 37 – 37.03 Mb Chr 3: 54.64 – 54.64 Mb PubMed search
Wikidata
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Exosome component 8, also known as EXOSC8, is a human gene, the protein product of which is part of the exosome complex.

Interactions

Exosome component 8 has been shown to interact with:

• Exosome component 5 and
• Exosome component 6.

Further reading

• Andersen JS, Lam YW, Leung AK, et al. (2005). "Nucleolar proteome dynamics". Nature. 433 (7021): 77–83. Bibcode:2005Natur.433...77A. doi:10.1038/nature03207. PMID 15635413. S2CID 4344740.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Lehner B, Sanderson CM (2004). "A Protein Interaction Framework for Human mRNA Degradation". Genome Res. 14 (7): 1315–23. doi:10.1101/gr.2122004. PMC 442147. PMID 15231747.
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Raijmakers R, Egberts WV, van Venrooij WJ, Pruijn GJ (2002). "Protein-protein interactions between human exosome components support the assembly of RNase PH-type subunits into a six-membered PNPase-like ring". J. Mol. Biol. 323 (4): 653–63. doi:10.1016/S0022-2836(02)00947-6. hdl:2066/186665. PMID 12419256.
• Jiang T, Altman S (2002). "A protein subunit of human RNase P, Rpp14, and its interacting partner, OIP2, have 3′→5′ exoribonuclease activity". Proc. Natl. Acad. Sci. U.S.A. 99 (8): 5295–300. doi:10.1073/pnas.072083699. PMC 122763. PMID 11929972.
• Raijmakers R, Noordman YE, van Venrooij WJ, Pruijn GJ (2002). "Protein-protein interactions of hCsl4p with other human exosome subunits". J. Mol. Biol. 315 (4): 809–18. doi:10.1006/jmbi.2001.5265. hdl:2066/261980. PMID 11812149.
• Chen CY, Gherzi R, Ong SE, et al. (2002). "AU binding proteins recruit the exosome to degrade ARE-containing mRNAs". Cell. 107 (4): 451–64. doi:10.1016/S0092-8674(01)00578-5. PMID 11719186.
• Jiang T, Altman S (2001). "Protein–protein interactions with subunits of human nuclear RNase P". Proc. Natl. Acad. Sci. U.S.A. 98 (3): 920–5. doi:10.1073/pnas.021561498. PMC 14685. PMID 11158571.
• Brouwer R, Allmang C, Raijmakers R, et al. (2001). "Three novel components of the human exosome". J. Biol. Chem. 276 (9): 6177–84. doi:10.1074/jbc.M007603200. hdl:2066/186951. PMID 11110791.
• Williams JM, Chen GC, Zhu L, Rest RF (1998). "Using the yeast two-hybrid system to identify human epithelial cell proteins that bind gonococcal Opa proteins: intracellular gonococci bind pyruvate kinase via their Opa proteins and require host pyruvate for growth". Mol. Microbiol. 27 (1): 171–86. doi:10.1046/j.1365-2958.1998.00670.x. PMID 9466265.