YBR217W - 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=S000000421 YBR217W]
+|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000000421 YBR217W]
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''         ||''ATG12 ''

@@ Line 13: / Line 13: @@
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
-|nowrap| Chr II:657827..658387
+|nowrap| Chr II:657832..658392
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''           || S000000421

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YBR217W:''' Conserved ubiquitin-like modifier involved in autophagy and the Cvt pathway; conjugated to Atg5p to form a complex involved in Atg8p lipidation; Atg12p-Atg5p also forms a complex with Atg16p that is required for autophagosome formation<ref name='S000039962'>Mizushima N, et al. (1998) A protein conjugation system essential for autophagy. Nature 395(6700):395-8 {{SGDpaper|S000039962}} PMID 9759731</ref><ref name='S000045627'>Shintani T, et al. (1999) Apg10p, a novel protein-conjugating enzyme essential for autophagy in yeast. EMBO J 18(19):5234-41 {{SGDpaper|S000045627}} PMID 10508157</ref><ref name='S000048125'>Tanida I, et al. (1999) Apg7p/Cvt2p: A novel protein-activating enzyme essential for autophagy. Mol Biol Cell 10(5):1367-79 {{SGDpaper|S000048125}} PMID 10233150</ref><ref name='S000051835'>Tsukada M and Ohsumi Y (1993) Isolation and characterization of autophagy-defective mutants of Saccharomyces cerevisiae. FEBS Lett 333(1-2):169-74 {{SGDpaper|S000051835}} PMID 8224160</ref><ref name='S000069879'>Kuma A, et al. (2002) Formation of the approximately 350-kDa Apg12-Apg5.Apg16 multimeric complex, mediated by Apg16 oligomerization, is essential for autophagy in yeast. J Biol Chem 277(21):18619-25 {{SGDpaper|S000069879}} PMID 11897782</ref><ref name='S000124888'>Hanada T, et al. (2007) The Atg12-Atg5 Conjugate Has a Novel E3-like Activity for Protein Lipidation in Autophagy. J Biol Chem 282(52):37298-302
+'''Description of YBR217W:''' Conserved ubiquitin-like modifier involved in autophagy and the Cvt pathway; conjugated to Atg5p to form a complex involved in Atg8p lipidation; Atg12p-Atg5p also forms a complex with Atg16p that is required for autophagosome formation<ref name='S000124888'>Hanada T, et al. (2007) The Atg12-Atg5 Conjugate Has a Novel E3-like Activity for Protein Lipidation in Autophagy. J Biol Chem 282(52):37298-302 {{SGDpaper|S000124888}} PMID 17986448</ref><ref name='S000069879'>Kuma A, et al. (2002) Formation of the approximately 350-kDa Apg12-Apg5.Apg16 multimeric complex, mediated by Apg16 oligomerization, is essential for autophagy in yeast. J Biol Chem 277(21):18619-25 {{SGDpaper|S000069879}} PMID 11897782</ref><ref name='S000039962'>Mizushima N, et al. (1998) A protein conjugation system essential for autophagy. Nature 395(6700):395-8 {{SGDpaper|S000039962}} PMID 9759731</ref><ref name='S000045627'>Shintani T, et al. (1999) Apg10p, a novel protein-conjugating enzyme essential for autophagy in yeast. EMBO J 18(19):5234-41 {{SGDpaper|S000045627}} PMID 10508157</ref><ref name='S000048125'>Tanida I, et al. (1999) Apg7p/Cvt2p: A novel protein-activating enzyme essential for autophagy. Mol Biol Cell 10(5):1367-79 {{SGDpaper|S000048125}} PMID 10233150</ref><ref name='S000051835'>Tsukada M and Ohsumi Y (1993) Isolation and characterization of autophagy-defective mutants of Saccharomyces cerevisiae. FEBS Lett 333(1-2):169-74
- {{SGDpaper|S000124888}} PMID 17986448</ref>
+ {{SGDpaper|S000051835}} PMID 8224160</ref>
 <br>
 <br>

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YBR217W:''' Conserved ubiquitin-like modifier involved in autophagy and the Cvt pathway; conjugated to Atg5p to form a complex involved in Atg8p lipidation; Atg12p-Atg5p also forms a complex with Atg16p that is required for autophagosome formation<ref name='S000124888'>Hanada T, et al. (2007) The Atg12-Atg5 Conjugate Has a Novel E3-like Activity for Protein Lipidation in Autophagy. J Biol Chem 282(52):37298-302 {{SGDpaper|S000124888}} PMID 17986448</ref><ref name='S000069879'>Kuma A, et al. (2002) Formation of the approximately 350-kDa Apg12-Apg5.Apg16 multimeric complex, mediated by Apg16 oligomerization, is essential for autophagy in yeast. J Biol Chem 277(21):18619-25 {{SGDpaper|S000069879}} PMID 11897782</ref><ref name='S000051835'>Tsukada M and Ohsumi Y (1993) Isolation and characterization of autophagy-defective mutants of Saccharomyces cerevisiae. FEBS Lett 333(1-2):169-74 {{SGDpaper|S000051835}} PMID 8224160</ref><ref name='S000048125'>Tanida I, et al. (1999) Apg7p/Cvt2p: A novel protein-activating enzyme essential for autophagy. Mol Biol Cell 10(5):1367-79 {{SGDpaper|S000048125}} PMID 10233150</ref><ref name='S000045627'>Shintani T, et al. (1999) Apg10p, a novel protein-conjugating enzyme essential for autophagy in yeast. EMBO J 18(19):5234-41 {{SGDpaper|S000045627}} PMID 10508157</ref><ref name='S000039962'>Mizushima N, et al. (1998) A protein conjugation system essential for autophagy. Nature 395(6700):395-8
+'''Description of YBR217W:''' Conserved ubiquitin-like modifier involved in autophagy and the Cvt pathway; conjugated to Atg5p to form a complex involved in Atg8p lipidation; Atg12p-Atg5p also forms a complex with Atg16p that is required for autophagosome formation<ref name='S000039962'>Mizushima N, et al. (1998) A protein conjugation system essential for autophagy. Nature 395(6700):395-8 {{SGDpaper|S000039962}} PMID 9759731</ref><ref name='S000045627'>Shintani T, et al. (1999) Apg10p, a novel protein-conjugating enzyme essential for autophagy in yeast. EMBO J 18(19):5234-41 {{SGDpaper|S000045627}} PMID 10508157</ref><ref name='S000048125'>Tanida I, et al. (1999) Apg7p/Cvt2p: A novel protein-activating enzyme essential for autophagy. Mol Biol Cell 10(5):1367-79 {{SGDpaper|S000048125}} PMID 10233150</ref><ref name='S000051835'>Tsukada M and Ohsumi Y (1993) Isolation and characterization of autophagy-defective mutants of Saccharomyces cerevisiae. FEBS Lett 333(1-2):169-74 {{SGDpaper|S000051835}} PMID 8224160</ref><ref name='S000069879'>Kuma A, et al. (2002) Formation of the approximately 350-kDa Apg12-Apg5.Apg16 multimeric complex, mediated by Apg16 oligomerization, is essential for autophagy in yeast. J Biol Chem 277(21):18619-25 {{SGDpaper|S000069879}} PMID 11897782</ref><ref name='S000124888'>Hanada T, et al. (2007) The Atg12-Atg5 Conjugate Has a Novel E3-like Activity for Protein Lipidation in Autophagy. J Biol Chem 282(52):37298-302
-  {{SGDpaper|S000039962}} PMID 9759731</ref>
+  {{SGDpaper|S000124888}} PMID 17986448</ref>
 <br>
 <br>

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YBR217W:''' Conserved ubiquitin-like modifier involved in autophagy and the Cvt pathway; conjugated to Atg5p to form a complex involved in Atg8p lipidation; Atg12p-Atg5p also forms a complex with Atg16p that is required for autophagosome formation<ref name='S000039962'>Mizushima N, et al. (1998) A protein conjugation system essential for autophagy. Nature 395(6700):395-8 {{SGDpaper|S000039962}} PMID 9759731</ref><ref name='S000045627'>Shintani T, et al. (1999) Apg10p, a novel protein-conjugating enzyme essential for autophagy in yeast. EMBO J 18(19):5234-41 {{SGDpaper|S000045627}} PMID 10508157</ref><ref name='S000048125'>Tanida I, et al. (1999) Apg7p/Cvt2p: A novel protein-activating enzyme essential for autophagy. Mol Biol Cell 10(5):1367-79 {{SGDpaper|S000048125}} PMID 10233150</ref><ref name='S000051835'>Tsukada M and Ohsumi Y (1993) Isolation and characterization of autophagy-defective mutants of Saccharomyces cerevisiae. FEBS Lett 333(1-2):169-74 {{SGDpaper|S000051835}} PMID 8224160</ref><ref name='S000069879'>Kuma A, et al. (2002) Formation of the approximately 350-kDa Apg12-Apg5.Apg16 multimeric complex, mediated by Apg16 oligomerization, is essential for autophagy in yeast. J Biol Chem 277(21):18619-25 {{SGDpaper|S000069879}} PMID 11897782</ref><ref name='S000124888'>Hanada T, et al. (2007) The Atg12-Atg5 Conjugate Has a Novel E3-like Activity for Protein Lipidation in Autophagy. J Biol Chem 282(52):37298-302
+'''Description of YBR217W:''' Conserved ubiquitin-like modifier involved in autophagy and the Cvt pathway; conjugated to Atg5p to form a complex involved in Atg8p lipidation; Atg12p-Atg5p also forms a complex with Atg16p that is required for autophagosome formation<ref name='S000124888'>Hanada T, et al. (2007) The Atg12-Atg5 Conjugate Has a Novel E3-like Activity for Protein Lipidation in Autophagy. J Biol Chem 282(52):37298-302 {{SGDpaper|S000124888}} PMID 17986448</ref><ref name='S000069879'>Kuma A, et al. (2002) Formation of the approximately 350-kDa Apg12-Apg5.Apg16 multimeric complex, mediated by Apg16 oligomerization, is essential for autophagy in yeast. J Biol Chem 277(21):18619-25 {{SGDpaper|S000069879}} PMID 11897782</ref><ref name='S000051835'>Tsukada M and Ohsumi Y (1993) Isolation and characterization of autophagy-defective mutants of Saccharomyces cerevisiae. FEBS Lett 333(1-2):169-74 {{SGDpaper|S000051835}} PMID 8224160</ref><ref name='S000048125'>Tanida I, et al. (1999) Apg7p/Cvt2p: A novel protein-activating enzyme essential for autophagy. Mol Biol Cell 10(5):1367-79 {{SGDpaper|S000048125}} PMID 10233150</ref><ref name='S000045627'>Shintani T, et al. (1999) Apg10p, a novel protein-conjugating enzyme essential for autophagy in yeast. EMBO J 18(19):5234-41 {{SGDpaper|S000045627}} PMID 10508157</ref><ref name='S000039962'>Mizushima N, et al. (1998) A protein conjugation system essential for autophagy. Nature 395(6700):395-8
-  {{SGDpaper|S000124888}} PMID 17986448</ref>
+  {{SGDpaper|S000039962}} PMID 9759731</ref>
 <br>
 <br>

← Older revision		Revision as of 20:02, 21 February 2007
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		+	<!-- PLEASE ADD Community Commentary ABOVE THIS MESSAGE. See below for an example of community annotation -->
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		+	Specifically higher expression in carbon limited chemostat cultures versus carbon excess.
		+	<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.
		+	J Biol Chem 278(5):3265-74</ref>
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 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
 |nowrap| Chr II:657827..658387
 |}
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 ==Community Commentary==
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 ==References==
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