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EXOSC2
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	2NN6
Identifiers
Aliases	EXOSC2, RRP4, Rrp4p, hRrp4p, p7, Exosome component 2, SHRF
External IDs	OMIM: 602238; MGI: 2385133; HomoloGene: 6095; GeneCards: EXOSC2; OMA:EXOSC2 - orthologs
Gene location (Human)
Chr.	Chromosome 9 (human)
End	130,707,288 bp
Gene location (Mouse)
Chr.	Chromosome 2 (mouse)
End	31,571,361 bp
RNA expression pattern
	Top expressed in
	ganglionic eminence; ; ventricular zone; ; gonad; ; Achilles tendon; ; cerebellar hemisphere; ; left ovary; ; granulocyte; ; right hemisphere of cerebellum; ; right ovary; ; rectum;
	Top expressed in
	embryo; ; molar; ; epiblast; ; blastocyst; ; yolk sac; ; embryo; ; morula; ; somite; ; ventricular zone; ; neural layer of retina;
	More reference expression data
	; ;
	More reference expression data
Gene ontology
Molecular function	3'-5'-exoribonuclease activity; exoribonuclease activity; 7S RNA binding; protein binding; RNA binding;
Cellular component	cytoplasm; cytosol; exosome (RNase complex); nuclear exosome (RNase complex); cytoplasmic exosome (RNase complex); nucleus; nucleoplasm; nucleolus;
Biological process	nuclear polyadenylation-dependent tRNA catabolic process; nuclear polyadenylation-dependent rRNA catabolic process; regulation of mRNA stability; 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'; CUT catabolic process; positive regulation of cell growth; exonucleolytic catabolism of deadenylated mRNA; rRNA processing; U4 snRNA 3'-end processing; polyadenylation-dependent snoRNA 3'-end processing;
	Sources:Amigo / QuickGO
Orthologs
	23404
	227715
	ENSG00000130713
	ENSMUSG00000039356
	Q13868
	Q8VBV3
	NM_001282708; NM_001282709; NM_014285
	NM_144886
	NP_001269637; NP_001269638; NP_055100
	NP_659135
	Wikidata
View/Edit Human	View/Edit Mouse

Exosome component 2, also known as EXOSC2, is a protein which in humans is encoded by the EXOSC2 gene.^[5]^[6]

Function

Mammalian mRNAs contain AU-rich elements (AREs) within their three prime untranslated regions. In yeast, 3-prime-to-5-prime mRNA degradation is mediated by the exosome, a multisubunit particle. EXOSC2 (which is homologous to the yeast Rrp4 protein) is a component of the human exosome.^[7]

Interactions

Exosome component 2 has been shown to interact with:

Exosome component 4,^[8] and
Exosome component 7.^[8]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000130713 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000039356 – 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: EXOSC2 exosome component 2".
^ Mitchell P, Petfalski E, Shevchenko A, Mann M, Tollervey D (November 1997). "The exosome: a conserved eukaryotic RNA processing complex containing multiple 3'-->5' exoribonucleases". Cell. 91 (4): 457–66. doi:10.1016/S0092-8674(00)80432-8. PMID 9390555. S2CID 16035676.
^ Chen CY, Gherzi R, Ong SE, Chan EL, Raijmakers R, Pruijn GJ, Stoecklin G, Moroni C, Mann M, Karin M (November 2001). "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.
^ ^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.

Adams MD, Dubnick M, Kerlavage AR, et al. (1992). "Sequence identification of 2,375 human brain genes". Nature. 355 (6361): 632–4. Bibcode:1992Natur.355..632A. doi:10.1038/355632a0. PMID 1538749. S2CID 4234345.
Morris CM, Heisterkamp N, Groffen J, Fitzgerald PH (1991). "Entire ABL gene is joined with 5'-BCR in some patients with Philadelphia-positive leukemia". Blood. 78 (4): 1078–84. doi:10.1182/blood.V78.4.1078.1078. PMID 1868241.
Zhu QS, Heisterkamp N, Groffen J (1990). "Characterization of the human ABL promoter regions". Oncogene. 5 (6): 885–91. PMID 2163052.
Soekarman D, van Denderen J, Hoefsloot L, et al. (1990). "A novel variant of the bcr-abl fusion product in Philadelphia chromosome-positive acute lymphoblastic leukemia". Leukemia. 4 (6): 397–403. PMID 2193202.
Chen SJ, Chen Z, Font MP, et al. (1989). "Structural alterations of the BCR and ABL genes in Ph1 positive acute leukemias with rearrangements in the BCR gene first intron: further evidence implicating Alu sequences in the chromosome translocation". Nucleic Acids Res. 17 (19): 7631–42. doi:10.1093/nar/17.19.7631. PMC 334872. PMID 2678002.
Heisterkamp N, Stam K, Groffen J, et al. (1985). "Structural organization of the bcr gene and its role in the Ph' translocation". Nature. 315 (6022): 758–61. Bibcode:1985Natur.315..758H. doi:10.1038/315758a0. PMID 2989703. S2CID 4343076.
Shtivelman E, Lifshitz B, Gale RP, et al. (1986). "Alternative splicing of RNAs transcribed from the human abl gene and from the bcr-abl fused gene". Cell. 47 (2): 277–84. doi:10.1016/0092-8674(86)90450-2. PMID 3021337. S2CID 36324337.
Grosveld G, Verwoerd T, van Agthoven T, et al. (1987). "The chronic myelocytic cell line K562 contains a breakpoint in bcr and produces a chimeric bcr/c-abl transcript". Mol. Cell. Biol. 6 (2): 607–16. doi:10.1128/mcb.6.2.607. PMC 367552. PMID 3023859.
Bernards A, Rubin CM, Westbrook CA, et al. (1987). "The first intron in the human c-abl gene is at least 200 kilobases long and is a target for translocations in chronic myelogenous leukemia". Mol. Cell. Biol. 7 (9): 3231–6. doi:10.1128/mcb.7.9.3231. PMC 367959. PMID 3313010.
Groffen J, Heisterkamp N, Grosveld F, et al. (1982). "Isolation of human oncogene sequences (v-fes homolog) from a cosmid library". Science. 216 (4550): 1136–8. Bibcode:1982Sci...216.1136G. doi:10.1126/science.6281890. PMID 6281890.
Heisterkamp N, Groffen J, Stephenson JR (1983). "The human v-abl cellular homologue". J. Mol. Appl. Genet. 2 (1): 57–68. PMID 6302194.
Heisterkamp N, Stephenson JR, Groffen J, et al. (1984). "Localization of the c-ab1 oncogene adjacent to a translocation break point in chronic myelocytic leukaemia". Nature. 306 (5940): 239–42. doi:10.1038/306239a0. PMID 6316147. S2CID 4258884.
Groffen J, Stephenson JR, Heisterkamp N, et al. (1984). "Philadelphia chromosomal breakpoints are clustered within a limited region, bcr, on chromosome 22". Cell. 36 (1): 93–9. doi:10.1016/0092-8674(84)90077-1. PMID 6319012. S2CID 9876892.
Chissoe SL, Bodenteich A, Wang YF, et al. (1995). "Sequence and analysis of the human ABL gene, the BCR gene, and regions involved in the Philadelphia chromosomal translocation". Genomics. 27 (1): 67–82. doi:10.1006/geno.1995.1008. PMID 7665185.
Litz CE, McClure JS, Copenhaver CM, Brunning RD (1993). "Duplication of small segments within the major breakpoint cluster region in chronic myelogenous leukemia". Blood. 81 (6): 1567–72. doi:10.1182/blood.V81.6.1567.1567. PMID 8453102.
Mitchell P, Petfalski E, Tollervey D (1996). "The 3' end of yeast 5.8S rRNA is generated by an exonuclease processing mechanism". Genes Dev. 10 (4): 502–13. doi:10.1101/gad.10.4.502. PMID 8600032.
Mitchell P, Petfalski E, Shevchenko A, et al. (1997). "The exosome: a conserved eukaryotic RNA processing complex containing multiple 3'-->5' exoribonucleases". Cell. 91 (4): 457–66. doi:10.1016/S0092-8674(00)80432-8. PMID 9390555. S2CID 16035676.
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.
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.

This article on a gene on human chromosome 9 is a stub. You can help Wikipedia by expanding it.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000130713 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000039356 – 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: EXOSC2 exosome component 2".

[pmid9390555-6] Mitchell P, Petfalski E, Shevchenko A, Mann M, Tollervey D (November 1997). "The exosome: a conserved eukaryotic RNA processing complex containing multiple 3'-->5' exoribonucleases". Cell. 91 (4): 457–66. doi:10.1016/S0092-8674(00)80432-8. PMID 9390555. S2CID 16035676.

[pmid11719186-7] Chen CY, Gherzi R, Ong SE, Chan EL, Raijmakers R, Pruijn GJ, Stoecklin G, Moroni C, Mann M, Karin M (November 2001). "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.

[pmid12419256-8] 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.

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Exosome component 2

Function

Interactions

References

Further reading