Difference between revisions of "YMR304W"

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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?locus=YMR304W YMR304W]  
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000004920 YMR304W]  
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''UBP15 ''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''UBP15 ''
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
|nowrap| Chr XIII:874986..878678
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|nowrap| Chr XIII:874987..878679
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''          || S000004920
 
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'''Description of {{PAGENAME}}:''' Ubiquitin-specific protease that may play a role in ubiquitin precursor processing<ref name='S000058010'>Hochstrasser M (1996) Ubiquitin-dependent protein degradation. Annu Rev Genet 30():405-39 {{SGDpaper|S000058010}} PMID 8982460</ref><ref name='S000052610'>Layfield R, et al. (1999) Chemically synthesized ubiquitin extension proteins detect distinct catalytic capacities of deubiquitinating enzymes. Anal Biochem 274(1):40-9
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'''Description of YMR304W:''' Ubiquitin-specific protease involved in protein deubiquitination; catalytic activity regulated by an N-terminal TRAF-like domain and and C-terminal sequences; physically interacts with anaphase-promoting complex/cyclosome (APC/C) activator, Cdh1p; forms a complex with AAA peroxins Pex1p and Pex6p<ref name='S000145875'>Bozza WP and Zhuang Z (2011) Biochemical Characterization of a Multidomain Deubiquitinating Enzyme Ubp15 and the Regulatory Role of Its Terminal Domains. Biochemistry () {{SGDpaper|S000145875}} PMID 21710968</ref><ref name='S000150882'>Debelyy MO, et al. (2011) Ubp15p, a ubiquitin hydrolase associated with the peroxisomal export machinery. J Biol Chem 286(32):28223-34 {{SGDpaper|S000150882}} PMID 21665945</ref><ref name='S000052610'>Layfield R, et al. (1999) Chemically synthesized ubiquitin extension proteins detect distinct catalytic capacities of deubiquitinating enzymes. Anal Biochem 274(1):40-9
 
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==Community Commentary==
 
==Community Commentary==
 
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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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==References==
 
==References==
 
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Latest revision as of 13:05, 13 September 2012

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Systematic name YMR304W
Gene name UBP15
Aliases
Feature type ORF, Verified
Coordinates Chr XIII:874987..878679
Primary SGDID S000004920


Description of YMR304W: Ubiquitin-specific protease involved in protein deubiquitination; catalytic activity regulated by an N-terminal TRAF-like domain and and C-terminal sequences; physically interacts with anaphase-promoting complex/cyclosome (APC/C) activator, Cdh1p; forms a complex with AAA peroxins Pex1p and Pex6p[1][2][3]




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Community Commentary

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References

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  1. Bozza WP and Zhuang Z (2011) Biochemical Characterization of a Multidomain Deubiquitinating Enzyme Ubp15 and the Regulatory Role of Its Terminal Domains. Biochemistry () SGD PMID 21710968
  2. Debelyy MO, et al. (2011) Ubp15p, a ubiquitin hydrolase associated with the peroxisomal export machinery. J Biol Chem 286(32):28223-34 SGD PMID 21665945
  3. Layfield R, et al. (1999) Chemically synthesized ubiquitin extension proteins detect distinct catalytic capacities of deubiquitinating enzymes. Anal Biochem 274(1):40-9 SGD PMID 10527495

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