Exosome component 3

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) Band 9p13.2 Start 37,759,234 bp End 37,832,117 bp
Gene location (Mouse) Chr. Chromosome 4 (mouse) Band 4|4 B1 Start 45,316,613 bp End 45,342,732 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in oocyte secondary oocyte Achilles tendon stromal cell of endometrium sperm ganglionic eminence right adrenal gland appendix left adrenal gland monocyte Top expressed in yolk sac spermatid interventricular septum spermatocyte morula hand superior cervical ganglion thymus secondary oocyte neural tube More reference expression data BioGPS More reference expression data
Gene ontology Molecular function 3'-5'-exoribonuclease activity exoribonuclease activity protein binding RNA binding Cellular component cytosol nuclear exosome (RNase complex) cytoplasmic exosome (RNase complex) 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 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 catabolism of deadenylated mRNA 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: 37.76 – 37.83 Mb Chr 4: 45.32 – 45.34 Mb PubMed search
Wikidata
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Exosome component 3, also known as EXOSC3, is a human gene, which is part of the exosome complex.

Clinical significance

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

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. hdl:2066/186951. 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. S2CID 14817671.
• Andersen JS, Lyon CE, Fox AH, et al. (2002). "Directed proteomic analysis of the human nucleolus". Curr. Biol. 12 (1): 1–11. Bibcode:2002CBio...12....1A. doi:10.1016/S0960-9822(01)00650-9. PMID 11790298. S2CID 14132033.
• 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.
• 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. hdl:2066/186665. 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. Bibcode:2002PNAS...9916899M. 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. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.

External links

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