Difference between revisions of "YBR082C"

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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='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='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='S000130860'>Singh RK, et al. (2009) Histone levels are regulated by phosphorylation and ubiquitylation-dependent proteolysis. Nat Cell Biol
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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='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='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='S000130860'>Singh RK, et al. (2009) Histone levels are regulated by phosphorylation and ubiquitylation-dependent proteolysis. Nat Cell Biol 11(8):925-33
 
  {{SGDpaper|S000130860}} PMID 19578373</ref>
 
  {{SGDpaper|S000130860}} PMID 19578373</ref>
 
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Revision as of 14:05, 8 August 2009

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Systematic name YBR082C
Gene name UBC4
Aliases
Feature type ORF, Verified
Coordinates Chr II:407163..406622
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. 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
  2. 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
  3. 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
  4. 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
  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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