Difference between revisions of "YBR082C"

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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
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''          || S000000286

Revision as of 14:05, 3 February 2011

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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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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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