YBR070C - Revision history

SGDwikiBot: Automated import of articles

2012-01-23T14:45:17Z

Automated import of articles

SGDwikiBot: Automated import of articles

2011-02-03T21:05:14Z

Automated import of articles

SGDwikiBot: Automated import of articles

2010-02-25T21:05:12Z

Automated import of articles

SGDwikiBot: Automated import of articles

2009-03-31T21:05:09Z

Automated import of articles

SGDwikiBot: Automated import of articles

2009-01-16T21:05:11Z

Automated import of articles

SGDwikiBot: Automated import of articles

2008-12-18T11:40:06Z

Automated import of articles

SGDwikiBot: Automated import of articles

2007-05-21T23:20:05Z

Automated import of articles

SGDwikiBot: Automated import of articles

2007-05-21T11:31:52Z

Automated import of articles

SGDwikiBot: Automated import of articles

2007-03-21T15:40:44Z

Automated import of articles

SGDwikiBot: Automated import of articles

2007-02-27T15:45:55Z

Automated import of articles

@@ 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=S000000274 YBR070C]
+|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000000274 YBR070C]
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''         ||''ALG14 ''

@@ Line 13: / Line 13: @@
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
-|nowrap| Chr II:379931..379218
+|nowrap| Chr II:379934..379221
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''           || S000000274

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YBR070C:''' Component of UDP-GlcNAc transferase required for the second step of dolichyl-linked oligosaccharide synthesis; anchors the catalytic subunit Alg13p to the ER membrane; similar to bacterial and human glycosyltransferases<ref name='S000080148'>Chantret I, et al. (2005) Two proteins homologous to the N- and C-terminal domains of the bacterial glycosyltransferase Murg are required for the second step of dolichyl-linked oligosaccharide synthesis in Saccharomyces cerevisiae. J Biol Chem 280(10):9236-42 {{SGDpaper|S000080148}} PMID 15615718</ref><ref name='S000086112'>Gao XD, et al. (2005) Alg14 Recruits Alg13 to the Cytoplasmic Face of the Endoplasmic Reticulum to Form a Novel Bipartite UDP-N-acetylglucosamine Transferase Required for the Second Step of N-Linked Glycosylation. J Biol Chem 280(43):36254-62 {{SGDpaper|S000086112}} PMID 16100110</ref><ref name='S000086130'>Bickel T, et al. (2005) Biosynthesis of lipid-linked oligosaccharides in Saccharomyces cerevisiae: Alg13p and Alg14p form a complex required for the formation of GlcNAc(2)-PP-dolichol. J Biol Chem 280(41):34500-6
+'''Description of YBR070C:''' Component of UDP-GlcNAc transferase required for the second step of dolichyl-linked oligosaccharide synthesis; anchors the catalytic subunit Alg13p to the ER membrane; similar to bacterial and human glycosyltransferases<ref name='S000086130'>Bickel T, et al. (2005) Biosynthesis of lipid-linked oligosaccharides in Saccharomyces cerevisiae: Alg13p and Alg14p form a complex required for the formation of GlcNAc(2)-PP-dolichol. J Biol Chem 280(41):34500-6 {{SGDpaper|S000086130}} PMID 16100113</ref><ref name='S000080148'>Chantret I, et al. (2005) Two proteins homologous to the N- and C-terminal domains of the bacterial glycosyltransferase Murg are required for the second step of dolichyl-linked oligosaccharide synthesis in Saccharomyces cerevisiae. J Biol Chem 280(10):9236-42 {{SGDpaper|S000080148}} PMID 15615718</ref><ref name='S000086112'>Gao XD, et al. (2005) Alg14 Recruits Alg13 to the Cytoplasmic Face of the Endoplasmic Reticulum to Form a Novel Bipartite UDP-N-acetylglucosamine Transferase Required for the Second Step of N-Linked Glycosylation. J Biol Chem 280(43):36254-62
- {{SGDpaper|S000086130}} PMID 16100113</ref>
+ {{SGDpaper|S000086112}} PMID 16100110</ref>
 <br>
 <br>

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YBR070C:''' Component of UDP-GlcNAc transferase required for the second step of dolichyl-linked oligosaccharide synthesis; anchors the catalytic subunit Alg13p to the ER membrane; similar to bacterial and human glycosyltransferases<ref name='S000086130'>Bickel T, et al. (2005) Biosynthesis of lipid-linked oligosaccharides in Saccharomyces cerevisiae: Alg13p and Alg14p form a complex required for the formation of GlcNAc(2)-PP-dolichol. J Biol Chem 280(41):34500-6 {{SGDpaper|S000086130}} PMID 16100113</ref><ref name='S000086112'>Gao XD, et al. (2005) Alg14 Recruits Alg13 to the Cytoplasmic Face of the Endoplasmic Reticulum to Form a Novel Bipartite UDP-N-acetylglucosamine Transferase Required for the Second Step of N-Linked Glycosylation. J Biol Chem 280(43):36254-62 {{SGDpaper|S000086112}} PMID 16100110</ref><ref name='S000080148'>Chantret I, et al. (2005) Two proteins homologous to the N- and C-terminal domains of the bacterial glycosyltransferase Murg are required for the second step of dolichyl-linked oligosaccharide synthesis in Saccharomyces cerevisiae. J Biol Chem 280(10):9236-42
+'''Description of YBR070C:''' Component of UDP-GlcNAc transferase required for the second step of dolichyl-linked oligosaccharide synthesis; anchors the catalytic subunit Alg13p to the ER membrane; similar to bacterial and human glycosyltransferases<ref name='S000080148'>Chantret I, et al. (2005) Two proteins homologous to the N- and C-terminal domains of the bacterial glycosyltransferase Murg are required for the second step of dolichyl-linked oligosaccharide synthesis in Saccharomyces cerevisiae. J Biol Chem 280(10):9236-42 {{SGDpaper|S000080148}} PMID 15615718</ref><ref name='S000086112'>Gao XD, et al. (2005) Alg14 Recruits Alg13 to the Cytoplasmic Face of the Endoplasmic Reticulum to Form a Novel Bipartite UDP-N-acetylglucosamine Transferase Required for the Second Step of N-Linked Glycosylation. J Biol Chem 280(43):36254-62 {{SGDpaper|S000086112}} PMID 16100110</ref><ref name='S000086130'>Bickel T, et al. (2005) Biosynthesis of lipid-linked oligosaccharides in Saccharomyces cerevisiae: Alg13p and Alg14p form a complex required for the formation of GlcNAc(2)-PP-dolichol. J Biol Chem 280(41):34500-6
-  {{SGDpaper|S000080148}} PMID 15615718</ref>
+  {{SGDpaper|S000086130}} PMID 16100113</ref>
 <br>
 <br>

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YBR070C:''' Component of UDP-GlcNAc transferase required for the second step of dolichyl-linked oligosaccharide synthesis; anchors the catalytic subunit Alg13p to the ER membrane; similar to bacterial and human glycosyltransferases<ref name='S000080148'>Chantret I, et al. (2005) Two proteins homologous to the N- and C-terminal domains of the bacterial glycosyltransferase Murg are required for the second step of dolichyl-linked oligosaccharide synthesis in Saccharomyces cerevisiae. J Biol Chem 280(10):9236-42 {{SGDpaper|S000080148}} PMID 15615718</ref><ref name='S000086112'>Gao XD, et al. (2005) Alg14 Recruits Alg13 to the Cytoplasmic Face of the Endoplasmic Reticulum to Form a Novel Bipartite UDP-N-acetylglucosamine Transferase Required for the Second Step of N-Linked Glycosylation. J Biol Chem 280(43):36254-62 {{SGDpaper|S000086112}} PMID 16100110</ref><ref name='S000086130'>Bickel T, et al. (2005) Biosynthesis of lipid-linked oligosaccharides in Saccharomyces cerevisiae: Alg13p and Alg14p form a complex required for the formation of GlcNAc(2)-PP-dolichol. J Biol Chem 280(41):34500-6
+'''Description of YBR070C:''' Component of UDP-GlcNAc transferase required for the second step of dolichyl-linked oligosaccharide synthesis; anchors the catalytic subunit Alg13p to the ER membrane; similar to bacterial and human glycosyltransferases<ref name='S000086130'>Bickel T, et al. (2005) Biosynthesis of lipid-linked oligosaccharides in Saccharomyces cerevisiae: Alg13p and Alg14p form a complex required for the formation of GlcNAc(2)-PP-dolichol. J Biol Chem 280(41):34500-6 {{SGDpaper|S000086130}} PMID 16100113</ref><ref name='S000086112'>Gao XD, et al. (2005) Alg14 Recruits Alg13 to the Cytoplasmic Face of the Endoplasmic Reticulum to Form a Novel Bipartite UDP-N-acetylglucosamine Transferase Required for the Second Step of N-Linked Glycosylation. J Biol Chem 280(43):36254-62 {{SGDpaper|S000086112}} PMID 16100110</ref><ref name='S000080148'>Chantret I, et al. (2005) Two proteins homologous to the N- and C-terminal domains of the bacterial glycosyltransferase Murg are required for the second step of dolichyl-linked oligosaccharide synthesis in Saccharomyces cerevisiae. J Biol Chem 280(10):9236-42
-  {{SGDpaper|S000086130}} PMID 16100113</ref>
+  {{SGDpaper|S000080148}} PMID 15615718</ref>
 <br>
 <br>

← Older revision	Revision as of 23:20, 21 May 2007
(No difference)

@@ Line 30: / Line 30: @@
 {{CommentaryHelp}}
@@ Line 39: / Line 47: @@
 J Biol Chem 278(5):3265-74</ref>
 -->