Exosome component 8

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)
End	37,025,881 bp
Gene location (Mouse)
Chr.	Chromosome 3 (mouse)
End	54,642,814 bp
RNA expression pattern
	Top expressed in
	ganglionic eminence; ; right uterine tube; ; canal of the cervix; ; rectum; ; body of pancreas; ; lymph node; ; endometrium; ; spleen; ; tibial nerve; ; left uterine tube;
	Top expressed in
	yolk sac; ; primitive streak; ; blastocyst; ; medial ganglionic eminence; ; morula; ; endocardial cushion; ; thymus; ; abdominal wall; ; maxillary prominence; ; dermis;
	More reference expression data
	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
	11340
	69639
	ENSG00000120699
	ENSMUSG00000027752
	Q96B26
	Q9D753
	NM_181503
	NM_001163570 ; NM_027148
	NP_852480
	NP_001157042 ; NP_081424
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated October 05, 2022

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]

Related Research Articles

The exosome complex is a multi-protein intracellular complex capable of degrading various types of RNA molecules. Exosome complexes are found in both eukaryotic cells and archaea, while in bacteria a simpler complex called the degradosome carries out similar functions.

Exosome component 2, also known as EXOSC2, is a protein which in humans is encoded by the EXOSC2 gene.

Exosome component 10, also known as EXOSC10, is a human gene, the protein product of which is part of the exosome complex and is an autoantigen is patients with certain auto immune diseases, most notably scleromyositis.

Exosome complex exonuclease RRP44 or Dis3 is an enzyme that in humans is encoded by the DIS3 gene. Its protein product is an RNase enzyme homologous to the yeast protein Rrp44, and can be part of the exosome complex in the nucleus of eukaryotic cells.

Ribonuclease P protein subunit p20 is an enzyme that in humans is encoded by the POP7 gene.

Ribonucleases P/MRP protein subunit POP1 is a protein that in humans is encoded by the POP1 gene.

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

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

Ribonuclease P/MRP protein subunit POP5 is an enzyme that in humans is encoded by the POP5 gene.

Exosome component 9, also known as EXOSC9, is a human gene, the protein product of which is part of the exosome complex and is an autoantigen is patients with certain auto immune diseases, most notably scleromyositis.

Exosome component 4, also known as EXOSC4, is a human gene, which is part of the exosome complex.

Superkiller viralicidic activity 2-like 2 is a protein that in humans is encoded by the SKIV2L2 gene.

3'-5' exoribonuclease CSL4 homolog is an enzyme that in humans is encoded by the EXOSC1 gene.

Exosome component 5, also known as EXOSC5, is a human gene, which is part of the exosome complex.

Ribonuclease P protein subunit p30 is an enzyme that in humans is encoded by the RPP30 gene.

Ribonuclease P protein subunit p38 is an enzyme that in humans is encoded by the RPP38 gene.

Ribonuclease P protein subunit p14 is an enzyme that in humans is encoded by the RPP14 gene.

U3 small nucleolar RNA-interacting protein 2 is a protein that in humans is encoded by the RRP9 gene.

Ribonuclease P protein subunit p29 is an enzyme that in humans is encoded by the POP4 gene.

Exosome complex exonuclease MTR3 is an enzyme that in humans is encoded by the EXOSC6 gene.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000120699 - Ensembl, May 2017
1 2 3 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".
1 2 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.

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. 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.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000120699 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 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.

[entrez-5] "Entrez Gene: EXOSC8 exosome component 8".

[pmid12419256-6] 1 2 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.

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Exosome component 8

Contents

Interactions

Related Research Articles

References

Further reading