Difference between revisions of "YGL047W"
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− | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http:// | + | |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''' | ||
− | |nowrap| Chr VII: | + | |nowrap| Chr VII:411552..412160 |
|- | |- | ||
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID''' || S000003015 | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID''' || S000003015 | ||
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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=' | + | '''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 |
− | {{SGDpaper| | + | {{SGDpaper|S000086112}} PMID 16100110</ref> |
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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 <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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+ | ==References== | ||
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==References== | ==References== |
Latest revision as of 06:45, 23 January 2012
Share your knowledge...Edit this entry! <protect>
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
See Help:References on how to add references
- ↑ 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
- ↑ 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
- ↑ 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>