Difference between revisions of "YER125W"

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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000000927 YER125W]  
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000000927 YER125W]  
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''RSP5 ''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''RSP5 ''
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
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|nowrap| Chr V:410185..412614
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|nowrap| Chr V:410189..412618
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''          || S000000927
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''          || S000000927
 
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'''Description of YER125W:''' Ubiquitin-protein ligase involved in ubiquitin-mediated protein degradation; plays a role in heat shock element (HSE)-mediated gene expression and multivesicular body sorting; contains a hect (homologous to E6-AP carboxyl terminus) domain<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><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
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'''Description of YER125W:''' E3 ubiquitin ligase of the NEDD4 family; involved in regulating many cellular processes including MVB sorting, heat shock response, transcription, endocytosis, and ribosome stability; human homolog is involved in Liddle syndrome; mutant tolerates aneuploidy; ubiquitylates Sec23p<ref name='S000060760'>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 {{SGDpaper|S000060760}} PMID 11179425</ref><ref name='S000074703'>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 {{SGDpaper|S000074703}} PMID 12684839</ref><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='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><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='S000143769'>Ossareh-Nazari B, et al. (2010) The Rsp5 ubiquitin ligase and the AAA-ATPase Cdc48 control the ubiquitin-mediated degradation of the COPII component Sec23. Exp Cell Res 316(20):3351-7 {{SGDpaper|S000143769}} PMID 20846524</ref><ref name='S000145720'>Shcherbik N and Pestov DG (2011) The ubiquitin ligase Rsp5 is required for ribosome stability in Saccharomyces cerevisiae. RNA () {{SGDpaper|S000145720}} PMID 21665996</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='S000136872'>Torres EM, et al. (2010) Identification of aneuploidy-tolerating mutations. Cell 143(1):71-83
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Specifically higher expression in carbon limited chemostat cultures versus carbon excess.
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<ref>Boer VM, et al. (2003) The genome-wide transcriptional responses of Saccharomyces cerevisiae grown on glucose in aerobic chemostat cultures limited for carbon, nitrogen, phosphorus, or sulfur.
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J Biol Chem 278(5):3265-74</ref>
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Latest revision as of 07:45, 23 January 2012

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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, endocytosis, and ribosome stability; human homolog is involved in Liddle syndrome; mutant tolerates aneuploidy; ubiquitylates Sec23p[1][2][3][4][5][6][7][8][9]




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References

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  1. ↑ 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
  2. ↑ 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
  3. ↑ 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
  4. ↑ 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
  5. ↑ 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
  6. ↑ Ossareh-Nazari B, et al. (2010) The Rsp5 ubiquitin ligase and the AAA-ATPase Cdc48 control the ubiquitin-mediated degradation of the COPII component Sec23. Exp Cell Res 316(20):3351-7 SGD PMID 20846524
  7. ↑ Shcherbik N and Pestov DG (2011) The ubiquitin ligase Rsp5 is required for ribosome stability in Saccharomyces cerevisiae. RNA () SGD PMID 21665996
  8. ↑ 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
  9. ↑ Torres EM, et al. (2010) Identification of aneuploidy-tolerating mutations. Cell 143(1):71-83 SGD PMID 20850176

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