Difference between revisions of "YBR082C"

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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?locus=YBR082C YBR082C]  
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000000286 YBR082C]  
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''UBC4 ''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''UBC4 ''
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
|nowrap| Chr II:407163..406622
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|nowrap| Chr II:407169..406628
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''          || S000000286
 
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'''Description of {{PAGENAME}}:''' Ubiquitin-conjugating enzyme that mediates degradation of short-lived and abnormal proteins; interacts with E3-CaM in ubiquitinating calmodulin; interacts with many SCF ubiquitin protein ligases; component of the cellular stress response<ref name='S000075480'>Kus BM, et al. (2004) Functional interaction of 13 yeast SCF complexes with a set of yeast E2 enzymes in vitro. Proteins 54(3):455-67 {{SGDpaper|S000075480}} PMID 14747994</ref><ref name='S000052341'>Seufert W and Jentsch S (1991) Yeast ubiquitin-conjugating enzymes involved in selective protein degradation are essential for cell viability. Acta Biol Hung 42(1-3):27-37 {{SGDpaper|S000052341}} PMID 1844315</ref><ref name='S000042741'>Seufert W and Jentsch S (1990) Ubiquitin-conjugating enzymes UBC4 and UBC5 mediate selective degradation of short-lived and abnormal proteins. EMBO J 9(2):543-50 {{SGDpaper|S000042741}} PMID 2154373</ref><ref name='S000042559'>Parag HA, et al. (1993) Selective ubiquitination of calmodulin by UBC4 and a putative ubiquitin protein ligase (E3) from Saccharomyces cerevisiae. FEBS Lett 325(3):242-6
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'''Description of YBR082C:''' Ubiquitin-conjugating enzyme (E2), mediates degradation of abnormal or excess proteins, including calmodulin and histone H3; interacts with many SCF ubiquitin protein ligases; component of the cellular stress response<ref name='S000075480'>Kus BM, et al. (2004) Functional interaction of 13 yeast SCF complexes with a set of yeast E2 enzymes in vitro. Proteins 54(3):455-67 {{SGDpaper|S000075480}} PMID 14747994</ref><ref name='S000042559'>Parag HA, et al. (1993) Selective ubiquitination of calmodulin by UBC4 and a putative ubiquitin protein ligase (E3) from Saccharomyces cerevisiae. FEBS Lett 325(3):242-6 {{SGDpaper|S000042559}} PMID 8391479</ref><ref name='S000042741'>Seufert W and Jentsch S (1990) Ubiquitin-conjugating enzymes UBC4 and UBC5 mediate selective degradation of short-lived and abnormal proteins. EMBO J 9(2):543-50 {{SGDpaper|S000042741}} PMID 2154373</ref><ref name='S000052341'>Seufert W and Jentsch S (1991) Yeast ubiquitin-conjugating enzymes involved in selective protein degradation are essential for cell viability. Acta Biol Hung 42(1-3):27-37 {{SGDpaper|S000052341}} PMID 1844315</ref><ref name='S000130860'>Singh RK, et al. (2009) Histone levels are regulated by phosphorylation and ubiquitylation-dependent proteolysis. Nat Cell Biol 11(8):925-33
  {{SGDpaper|S000042559}} PMID 8391479</ref>
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  {{SGDpaper|S000130860}} PMID 19578373</ref>
 
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==Community Commentary==
 
==Community Commentary==
 
{{CommentaryHelp}}
 
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<!-- PLEASE ADD Community Commentary ABOVE THIS MESSAGE. See below for an example of community annotation -->
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<!--
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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 YBR082C
Gene name UBC4
Aliases
Feature type ORF, Verified
Coordinates Chr II:407169..406628
Primary SGDID S000000286


Description of YBR082C: Ubiquitin-conjugating enzyme (E2), mediates degradation of abnormal or excess proteins, including calmodulin and histone H3; interacts with many SCF ubiquitin protein ligases; component of the cellular stress response[1][2][3][4][5]




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Community Commentary

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References

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  1. Kus BM, et al. (2004) Functional interaction of 13 yeast SCF complexes with a set of yeast E2 enzymes in vitro. Proteins 54(3):455-67 SGD PMID 14747994
  2. Parag HA, et al. (1993) Selective ubiquitination of calmodulin by UBC4 and a putative ubiquitin protein ligase (E3) from Saccharomyces cerevisiae. FEBS Lett 325(3):242-6 SGD PMID 8391479
  3. Seufert W and Jentsch S (1990) Ubiquitin-conjugating enzymes UBC4 and UBC5 mediate selective degradation of short-lived and abnormal proteins. EMBO J 9(2):543-50 SGD PMID 2154373
  4. Seufert W and Jentsch S (1991) Yeast ubiquitin-conjugating enzymes involved in selective protein degradation are essential for cell viability. Acta Biol Hung 42(1-3):27-37 SGD PMID 1844315
  5. Singh RK, et al. (2009) Histone levels are regulated by phosphorylation and ubiquitylation-dependent proteolysis. Nat Cell Biol 11(8):925-33 SGD PMID 19578373

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