Exosome component 7

Exosome component 7, also known as EXOSC7, is a human gene, the protein product of which is part of the exosome complex.

EXOSC7
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2NN6
Identifiers
Aliases	EXOSC7, EAP1, RRP42, Rrp42p, hRrp42p, p8, Exosome component 7
External IDs	OMIM: 606488; MGI: 1913696; HomoloGene: 8994; GeneCards: EXOSC7; OMA:EXOSC7 - orthologs
Gene location (Human) Chr. Chromosome 3 (human) Band 3p21.31 Start 44,975,241 bp End 45,036,066 bp
Gene location (Mouse) Chr. Chromosome 9 (mouse) Band 9|9 F4 Start 122,942,280 bp End 122,965,194 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in oocyte secondary oocyte thoracic diaphragm skin of leg right adrenal gland left adrenal gland skin of abdomen left adrenal cortex right adrenal cortex body of tongue Top expressed in otic placode morula saccule otic vesicle primitive streak embryo epiblast yolk sac somite blastocyst 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 cytoplasm cytosol exosome (RNase complex) nucleolus nucleoplasm nucleus nuclear exosome (RNase complex) cytoplasmic exosome (RNase complex) Biological process regulation of mRNA stability 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 rRNA catabolic process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 23016 66446 Ensembl ENSG00000075914 ENSMUSG00000025785 UniProt Q15024 Q9D0M0 RefSeq (mRNA) NM_015004 NM_001081188 NM_025568 RefSeq (protein) NP_055819 NP_001074657 Location (UCSC) Chr 3: 44.98 – 45.04 Mb Chr 9: 122.94 – 122.97 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Interactions

Exosome component 7 has been shown to interact with:

• Exosome component 1,
• Exosome component 2, and
• Exosome component 6.

Further reading

• Butler JS (2002). "The yin and yang of the exosome". Trends Cell Biol. 12 (2): 90–6. doi:10.1016/S0962-8924(01)02225-5. PMID 11849973.
• Nagase T, Miyajima N, Tanaka A, et al. (1995). "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". DNA Res. 2 (1): 37–43. doi:10.1093/dnares/2.1.37. PMID 7788527.
• 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.
• 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.
• 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.
• 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.
• 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.