Exosome component 3

Exosome component 3, also known as EXOSC3, is a human gene, which is part of the exosome complex.[5]

EXOSC3
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2NN6
Identifiers
Aliases	EXOSC3, PCH1B, RRP40, Rrp40p, bA3J10.7, hRrp-40, p10, CGI-102, Exosome component 3
External IDs	OMIM: 606489 MGI: 1913612 HomoloGene: 6867 GeneCards: EXOSC3
Gene location (Human) Chr. Chromosome 9 (human)[1] Band 9p13.2 Start 37,766,978 bp[1] End 37,801,437 bp[1]
Gene location (Mouse) Chr. Chromosome 4 (mouse)[2] Band 4|4 B1 Start 45,316,613 bp[2] End 45,342,732 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • 3'-5'-exoribonuclease activity • exoribonuclease activity • GO:0001948 protein binding • RNA binding Cellular component • transcriptionally active chromatin • cytosol • nuclear exosome (RNase complex) • cytoplasmic exosome (RNase complex) • cell nucleus • cytoplasm • exosome (RNase complex) • nucleolus • nucleoplasm Biological process • nuclear polyadenylation-dependent tRNA catabolic process • exonucleolytic trimming to generate mature 3'-end of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) • regulation of mRNA stability • polyadenylation-dependent snoRNA 3'-end processing • DNA deamination • nuclear retention of pre-mRNA with aberrant 3'-ends at the site of transcription • CUT catabolic process • nuclear polyadenylation-dependent rRNA catabolic process • positive regulation of isotype switching • isotype switching • nuclear-transcribed mRNA catabolic process, exonucleolytic, 3'-5' • U4 snRNA 3'-end processing • rRNA processing • exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	51010	66362
Ensembl	ENSG00000107371	ENSMUSG00000028322
UniProt	Q9NQT5	Q7TQK4
RefSeq (mRNA)	NM_016042 NM_001002269	NM_025513 NM_001362788
RefSeq (protein)	NP_001002269 NP_057126	NP_079789 NP_001349717
Location (UCSC)	Chr 9: 37.77 – 37.8 Mb	Chr 4: 45.32 – 45.34 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Clinical significance

Mutations in EXOSC3 cause pontocerebellar hypoplasia and spinal motor neuron degeneration.[6]

References

1. GRCh38: Ensembl release 89: ENSG00000107371 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000028322 - 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: EXOSC3 exosome component 3".
6. Wan J, Yourshaw M, Mamsa H, Rudnik-Schöneborn S, Menezes MP, Hong JE, Leong DW, Senderek J, Salman MS, Chitayat D, Seeman P, von Moers A, Graul-Neumann L, Kornberg AJ, Castro-Gago M, Sobrido MJ, Sanefuji M, Shieh PB, Salamon N, Kim RC, Vinters HV, Chen Z, Zerres K, Ryan MM, Nelson SF, Jen JC (2012). "Mutations in the RNA exosome component gene EXOSC3 cause pontocerebellar hypoplasia and spinal motor neuron degeneration". Nat. Genet. 44 (6): 704–8. doi:10.1038/ng.2254. PMC 3366034. PMID 22544365.

Further reading

• Allmang C, Petfalski E, Podtelejnikov A, et al. (1999). "The yeast exosome and human PM-Scl are related complexes of 3' --> 5' exonucleases". Genes Dev. 13 (16): 2148–58. doi:10.1101/gad.13.16.2148. PMC 316947. PMID 10465791.
• Lai CH, Chou CY, Ch'ang LY, et al. (2000). "Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics". Genome Res. 10 (5): 703–13. doi:10.1101/gr.10.5.703. PMC 310876. PMID 10810093.
• 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.
• 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.
• Andersen JS, Lyon CE, Fox AH, et al. (2002). "Directed proteomic analysis of the human nucleolus". Curr. Biol. 12 (1): 1–11. doi:10.1016/S0960-9822(01)00650-9. PMID 11790298.
• 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.
• Brouwer R, Vree Egberts WT, Hengstman GJ, et al. (2002). "Autoantibodies directed to novel components of the PM/Scl complex, the human exosome". Arthritis Res. 4 (2): 134–8. doi:10.1186/ar389. PMC 83843. PMID 11879549.
• 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.
• 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.
• Gherzi R, Lee KY, Briata P, et al. (2004). "A KH domain RNA binding protein, KSRP, promotes ARE-directed mRNA turnover by recruiting the degradation machinery". Mol. Cell. 14 (5): 571–83. doi:10.1016/j.molcel.2004.05.002. PMID 15175153.
• 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.
• 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.
• Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.

External links

• Overview of all the structural information available in the PDB for UniProt: Q9NQT5 (Human Exosome complex component RRP40) at the PDBe-KB.