Difference between revisions of "YER125W"
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− | '''Description of YER125W:''' Ubiquitin-protein ligase involved in ubiquitin-mediated protein degradation; functions in multivesicular body sorting, heat shock response and ubiquitylation of arrested RNAPII; contains a hect (homologous to E6-AP carboxyl terminus) domain<ref name='S000086109'>Somesh BP, et al. (2005) Multiple mechanisms confining RNA polymerase II ubiquitylation to polymerases undergoing transcriptional arrest. Cell 121(6):913-23 {{SGDpaper|S000086109}} PMID 15960978</ref><ref name='S000077431'>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 {{SGDpaper|S000077431}} PMID 14657247</ref><ref name='S000073465'>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 {{SGDpaper|S000073465}} PMID 12821147 | + | '''Description of YER125W:''' Ubiquitin-protein ligase involved in ubiquitin-mediated protein degradation; functions in multivesicular body sorting, heat shock response and ubiquitylation of arrested RNAPII; contains a hect (homologous to E6-AP carboxyl terminus) domain<ref name='S000053994'>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 {{SGDpaper|S000053994}} PMID 9108033</ref><ref name='S000086109'>Somesh BP, et al. (2005) Multiple mechanisms confining RNA polymerase II ubiquitylation to polymerases undergoing transcriptional arrest. Cell 121(6):913-23 {{SGDpaper|S000086109}} PMID 15960978</ref><ref name='S000077431'>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 {{SGDpaper|S000077431}} PMID 14657247</ref><ref name='S000073465'>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 |
− | + | {{SGDpaper|S000073465}} PMID 12821147</ref> | |
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Revision as of 13:05, 31 March 2009
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Systematic name | YER125W |
Gene name | RSP5 |
Aliases | MDP1, MUT2, NPI1, SMM1, UBY1 |
Feature type | ORF, Verified |
Coordinates | Chr V:410185..412614 |
Primary SGDID | S000000927 |
Description of YER125W: Ubiquitin-protein ligase involved in ubiquitin-mediated protein degradation; functions in multivesicular body sorting, heat shock response and ubiquitylation of arrested RNAPII; contains a hect (homologous to E6-AP carboxyl terminus) domain[1][2][3][4]
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References
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- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 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
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