Difference between revisions of "YOR001W"
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| − | '''Description of YOR001W:''' | + | '''Description of YOR001W:''' Nuclear exosome exonuclease component; has 3'-5' exonuclease activity; involved in RNA processing, maturation, surveillance, degradation, tethering, and export; has similarity to E. coli RNase D and to human PM-Sc1 100 (EXOSC10)<ref name='S000126973'>Vodala S, et al. (2008) The nuclear exosome and adenylation regulate posttranscriptional tethering of yeast GAL genes to the nuclear periphery. Mol Cell 31(1):104-13 {{SGDpaper|S000126973}} PMID 18614049</ref><ref name='S000077467'>Hieronymus H, et al. (2004) Genome-wide mRNA surveillance is coupled to mRNA export. Genes Dev 18(21):2652-62 {{SGDpaper|S000077467}} PMID 15489286</ref><ref name='S000074753'>Bousquet-Antonelli C, et al. (2000) Identification of a regulated pathway for nuclear pre-mRNA turnover. Cell 102(6):765-75 {{SGDpaper|S000074753}} PMID 11030620</ref><ref name='S000065959'>Hilleren P, et al. (2001) Quality control of mRNA 3'-end processing is linked to the nuclear exosome. Nature 413(6855):538-42 {{SGDpaper|S000065959}} PMID 11586364</ref><ref name='S000043381'>Burkard KT and Butler JS (2000) A nuclear 3'-5' exonuclease involved in mRNA degradation interacts with Poly(A) polymerase and the hnRNA protein Npl3p. Mol Cell Biol 20(2):604-16 {{SGDpaper|S000043381}} PMID 10611239</ref><ref name='S000042261'>Briggs MW, et al. (1998) Rrp6p, the yeast homologue of the human PM-Scl 100-kDa autoantigen, is essential for efficient 5.8 S rRNA 3' end formation. J Biol Chem 273(21):13255-63 |
{{SGDpaper|S000042261}} PMID 9582370</ref> | {{SGDpaper|S000042261}} PMID 9582370</ref> | ||
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Revision as of 06:21, 26 February 2009
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| Systematic name | YOR001W |
| Gene name | RRP6 |
| Aliases | |
| Feature type | ORF, Verified |
| Coordinates | Chr XV:326833..329034 |
| Primary SGDID | S000005527 |
Description of YOR001W: Nuclear exosome exonuclease component; has 3'-5' exonuclease activity; involved in RNA processing, maturation, surveillance, degradation, tethering, and export; has similarity to E. coli RNase D and to human PM-Sc1 100 (EXOSC10)[1][2][3][4][5][6]
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Protein Details
Protein Modification
Modification(s): Phosphorylation
Identified as an efficient substrate of Clb2-Cdk1-as1 in a screen of a proteomic GST-fusion library. [7] [8]
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References
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- ↑ Vodala S, et al. (2008) The nuclear exosome and adenylation regulate posttranscriptional tethering of yeast GAL genes to the nuclear periphery. Mol Cell 31(1):104-13 SGD PMID 18614049
- ↑ Hieronymus H, et al. (2004) Genome-wide mRNA surveillance is coupled to mRNA export. Genes Dev 18(21):2652-62 SGD PMID 15489286
- ↑ Bousquet-Antonelli C, et al. (2000) Identification of a regulated pathway for nuclear pre-mRNA turnover. Cell 102(6):765-75 SGD PMID 11030620
- ↑ Hilleren P, et al. (2001) Quality control of mRNA 3'-end processing is linked to the nuclear exosome. Nature 413(6855):538-42 SGD PMID 11586364
- ↑ Burkard KT and Butler JS (2000) A nuclear 3'-5' exonuclease involved in mRNA degradation interacts with Poly(A) polymerase and the hnRNA protein Npl3p. Mol Cell Biol 20(2):604-16 SGD PMID 10611239
- ↑ Briggs MW, et al. (1998) Rrp6p, the yeast homologue of the human PM-Scl 100-kDa autoantigen, is essential for efficient 5.8 S rRNA 3' end formation. J Biol Chem 273(21):13255-63 SGD PMID 9582370
- ↑ Ubersax JA, et al. (2003) Targets of the cyclin-dependent kinase Cdk1. Nature 425(6960):859-64 SGD PMID 14574415
- ↑ submitted by Jeff Ubersax on 2004-01-29
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