Exosome component 2

EXOSC2

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
2NN6

Identifiers

Aliases

EXOSC2, RRP4, Rrp4p, hRrp4p, p7, Exosome component 2

External IDs

MGI: 2385133 HomoloGene: 6095 GeneCards: EXOSC2

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) • nucleolus • nucleus • nucleoplasm
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 • nuclear retention of pre-mRNA with aberrant 3'-ends at the site of transcription • positive regulation of cell growth • exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay • rRNA processing • U4 snRNA 3'-end processing • polyadenylation-dependent snoRNA 3'-end processing
Sources:Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

Entrez


23404


227715

Ensembl


ENSG00000130713


ENSMUSG00000039356

UniProt


Q13868


Q8VBV3

RefSeq (mRNA)


NM_001282708 NM_001282709 NM_014285


NM_144886

RefSeq (protein)


NP_001269637.1 NP_001269638.1 NP_055100.2


NP_659135.1

Location (UCSC)

Chr 9: 130.69 – 130.7 Mb

Chr 2: 31.67 – 31.68 Mb

PubMed search

^[1]

^[2]

Wikidata

View/Edit Human

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Exosome component 2, also known as EXOSC2, is a protein which in humans is encoded by the EXOSC2 gene.^[3]^[4]

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.^[5]

Interactions

Exosome component 2 has been shown to interact with:

Exosome component 4,^[6] and
Exosome component 7.^[6]

References

↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ "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.
↑ 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.
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.

Adams MD, Dubnick M, Kerlavage AR, et al. (1992). "Sequence identification of 2,375 human brain genes.". Nature. 355 (6361): 632–4. doi:10.1038/355632a0. PMID 1538749.
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. 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. doi:10.1038/315758a0. PMID 2989703.
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.
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. 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. 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. 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.
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.
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. 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.
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. 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.

PDB gallery

2nn6: Structure of the human RNA exosome composed of Rrp41, Rrp45, Rrp46, Rrp43, Mtr3, Rrp42, Csl4, Rrp4, and Rrp40

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Exosome component 2

Function

Interactions

References

Further reading