Exosome component 8

Exosome component 8, also known as EXOSC8, is a human gene, the protein product of which is part of the exosome complex.[5]

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
Gene location (Human) Chr. Chromosome 13 (human)[1] Band 13q13.3 Start 36,998,816 bp[1] End 37,009,614 bp[1]
Gene location (Mouse) Chr. Chromosome 3 (mouse)[2] Band 3|3 C Start 54,728,678 bp[2] End 54,735,393 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • exoribonuclease activity • AU-rich element binding • GO:0001948 protein binding • RNA binding • identical protein binding • mRNA 3'-UTR AU-rich region binding Cellular component • cytoplasm • cytosol • exosome (RNase complex) • nucleolus • cell 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 nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay • 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 – 37.01 Mb	Chr 3: 54.73 – 54.74 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Interactions

Exosome component 8 has been shown to interact with:

• Exosome component 5[6] and
• Exosome component 6.[6]

References

1. GRCh38: Ensembl release 89: ENSG00000120699 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000027752 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. "Entrez Gene: EXOSC8 exosome component 8".
6. Raijmakers R, Egberts WV, van Venrooij WJ, Pruijn GJ (Nov 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. PMID 12419256.

Further reading

• Andersen JS, Lam YW, Leung AK, et al. (2005). "Nucleolar proteome dynamics". Nature. 433 (7021): 77–83. doi:10.1038/nature03207. PMID 15635413.
• 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. 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. 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. 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. 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.