Exosome component 8

Protein-coding gene in the species Homo sapiens

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)^[1]

Band	13q13.3	Start	36,998,816 bp^[1]
Band	13q13.3	End	37,025,881 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 3 (mouse)^[2]

Band	3\|3 C	Start	54,636,099 bp^[2]
Band	3\|3 C	End	54,642,814 bp^[2]

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

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

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

Interactions

Exosome component 8 has been shown to interact with:

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

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000120699 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000027752 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Entrez Gene: EXOSC8 exosome component 8".
^ ^a ^b 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. hdl:2066/186665. PMID 12419256.

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.