YBR082C - Revision history

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@@ Line 4: / Line 4: @@
 {|{{Prettytable}} align = 'right' width = '200px'
 |-
-|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000000286 YBR082C]
+|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000000286 YBR082C]
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''         ||''UBC4 ''

@@ Line 13: / Line 13: @@
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 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
-|nowrap| Chr II:407163..406622
+|nowrap| Chr II:407169..406628
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''           || S000000286

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''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
+'''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|S000130860}} PMID 19578373</ref>
 <br>

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''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
+'''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>
 <br>

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YBR082C:''' Ubiquitin-conjugating enzyme (E2), 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='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
+'''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
-  {{SGDpaper|S000075480}} PMID 14747994</ref>
+  {{SGDpaper|S000130860}} PMID 19578373</ref>
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