Difference between revisions of "YHR081W"
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| − | '''Description of YHR081W:''' | + | '''Description of YHR081W:''' Nuclear exosome-associated nucleic acid binding protein; involved in RNA processing, surveillance, degradation, and export; homolog of mammalian nuclear matrix protein C1D involved in regulation of DNA repair and recombination<ref name='S000074272'>Mitchell P, et al. (2003) Rrp47p is an exosome-associated protein required for the 3' processing of stable RNAs. Mol Cell Biol 23(19):6982-92 {{SGDpaper|S000074272}} PMID 12972615</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='S000125047'>Stead JA, et al. (2007) The PMC2NT domain of the catalytic exosome subunit Rrp6p provides the interface for binding with its cofactor Rrp47p, a nucleic acid-binding protein. Nucleic Acids Res 35(16):5556-67 |
| − | {{SGDpaper| | + | {{SGDpaper|S000125047}} PMID 17704127</ref> |
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Revision as of 14:05, 15 January 2009
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| Systematic name | YHR081W |
| Gene name | LRP1 |
| Aliases | RRP47, YC1D |
| Feature type | ORF, Verified |
| Coordinates | Chr VIII:267540..268094 |
| Primary SGDID | S000001123 |
Description of YHR081W: Nuclear exosome-associated nucleic acid binding protein; involved in RNA processing, surveillance, degradation, and export; homolog of mammalian nuclear matrix protein C1D involved in regulation of DNA repair and recombination[1][2][3]
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Contents
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References
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- ↑ Mitchell P, et al. (2003) Rrp47p is an exosome-associated protein required for the 3' processing of stable RNAs. Mol Cell Biol 23(19):6982-92 SGD PMID 12972615
- ↑ Hieronymus H, et al. (2004) Genome-wide mRNA surveillance is coupled to mRNA export. Genes Dev 18(21):2652-62 SGD PMID 15489286
- ↑ Stead JA, et al. (2007) The PMC2NT domain of the catalytic exosome subunit Rrp6p provides the interface for binding with its cofactor Rrp47p, a nucleic acid-binding protein. Nucleic Acids Res 35(16):5556-67 SGD PMID 17704127
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