YER125W
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| Systematic name | YER125W |
| Gene name | RSP5 |
| Aliases | MDP1, MUT2, NPI1, SMM1, UBY1 |
| Feature type | ORF, Verified |
| Coordinates | Chr V:410189..412618 |
| Primary SGDID | S000000927 |
Description of YER125W: E3 ubiquitin ligase of the NEDD4 family; involved in regulating many cellular processes, including MVB sorting, heat shock response, transcription, and endocytosis; human homolog is involved in Liddle syndrome; mutant tolerates aneuploidy[1][2][3][4][5][6][7]
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References
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- ↑ Dunn R and Hicke L (2001) Domains of the Rsp5 ubiquitin-protein ligase required for receptor-mediated and fluid-phase endocytosis. Mol Biol Cell 12(2):421-35 SGD PMID 11179425
- ↑ Gajewska B, et al. (2003) Functional analysis of the human orthologue of the RSP5-encoded ubiquitin protein ligase, hNedd4, in yeast. Curr Genet 43(1):1-10 SGD PMID 12684839
- ↑ Huibregtse JM, et al. (1997) The large subunit of RNA polymerase II is a substrate of the Rsp5 ubiquitin-protein ligase. Proc Natl Acad Sci U S A 94(8):3656-61 SGD PMID 9108033
- ↑ Kaida D, et al. (2003) Rsp5-Bul1/2 complex is necessary for the HSE-mediated gene expression in budding yeast. Biochem Biophys Res Commun 306(4):1037-41 SGD PMID 12821147
- ↑ Katzmann DJ, et al. (2004) Multivesicular body sorting: ubiquitin ligase Rsp5 is required for the modification and sorting of carboxypeptidase S. Mol Biol Cell 15(2):468-80 SGD PMID 14657247
- ↑ Somesh BP, et al. (2005) Multiple mechanisms confining RNA polymerase II ubiquitylation to polymerases undergoing transcriptional arrest. Cell 121(6):913-23 SGD PMID 15960978
- ↑ Torres EM, et al. (2010) Identification of aneuploidy-tolerating mutations. Cell 143(1):71-83 SGD PMID 20850176
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