Difference between revisions of "YGL047W"

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{|{{Prettytable}} align = 'right' width = '200px'
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?locus=YGL047W YGL047W]  
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000003015 YGL047W]  
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''ALG13 ''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''ALG13 ''
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
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|nowrap| Chr VII:411555..412163
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|nowrap| Chr VII:411552..412160
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''          || S000003015
 
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'''Description of {{PAGENAME}}:''' Catalytic component of UDP-GlcNAc transferase, required for the second step of dolichyl-linked oligosaccharide synthesis; anchored to the ER membrane via interaction with Alg14p; similar to bacterial and human glycosyltransferases<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
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'''Description of YGL047W:''' Catalytic component of UDP-GlcNAc transferase, required for the second step of dolichyl-linked oligosaccharide synthesis; anchored to the ER membrane via interaction with Alg14p; 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
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  {{SGDpaper|S000080148}} PMID 15615718</ref>
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  {{SGDpaper|S000086112}} PMID 16100110</ref>
 
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{{CommentaryHelp}}
 
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Cytosolic Alg13 not bound to Alg14 at the ER membrane is very short-lived.
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Ubiquitin-independent proteasomal degradation is mediated by an autonomous C-terminal domain.  Addition of C-terminal epitope tags interfere with Alg13 degradation <ref> Averbeck et al., (2008) Alg13p, the catalytic subunit of the endoplasmic reticulum UDP-GlcNAc glycosyltransferase, is a target for proteasomal degradation. Mol. Biol. Cell 19:2169-2178.
  
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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.
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<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.
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J Biol Chem 278(5):3265-74</ref>
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-->
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<!-- PLEASE ADD Community Commentary ABOVE THIS MESSAGE. See below for an example of community annotation -->
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<!--
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Specifically higher expression in carbon limited chemostat cultures versus carbon excess.
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<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.
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J Biol Chem 278(5):3265-74</ref>
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-->
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<protect>
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==References==
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{{RefHelp}}
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</protect>
 
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==References==
 
==References==

Latest revision as of 06:45, 23 January 2012

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Systematic name YGL047W
Gene name ALG13
Aliases
Feature type ORF, Verified
Coordinates Chr VII:411552..412160
Primary SGDID S000003015


Description of YGL047W: Catalytic component of UDP-GlcNAc transferase, required for the second step of dolichyl-linked oligosaccharide synthesis; anchored to the ER membrane via interaction with Alg14p; similar to bacterial and human glycosyltransferases[1][2][3]




</protect>

Community Commentary

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Cytosolic Alg13 not bound to Alg14 at the ER membrane is very short-lived. Ubiquitin-independent proteasomal degradation is mediated by an autonomous C-terminal domain. Addition of C-terminal epitope tags interfere with Alg13 degradation Cite error: Closing </ref> missing for <ref> tag -->




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References

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  1. ↑ 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 SGD PMID 16100113
  2. ↑ 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 SGD PMID 15615718
  3. ↑ 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 SGD PMID 16100110

See Help:Categories on how to add the wiki page for this gene to a Category </protect> <protect>

References

See Help:References on how to add references

See Help:Categories on how to add the wiki page for this gene to a Category </protect>

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