Difference between revisions of "YGL047W"
SGDwikiBot (talk | contribs) (Automated import of articles) |
SGDwikiBot (talk | contribs) (Automated import of articles) |
||
| Line 18: | Line 18: | ||
|} | |} | ||
<br> | <br> | ||
| − | '''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=' | + | '''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='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| | + | {{SGDpaper|S000080148}} PMID 15615718</ref> |
<br> | <br> | ||
<br> | <br> | ||
Revision as of 13:05, 16 January 2009
Share your knowledge...Edit this entry! <protect>
| Systematic name | YGL047W |
| Gene name | ALG13 |
| Aliases | |
| Feature type | ORF, Verified |
| Coordinates | Chr VII:411555..412163 |
| 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
About Community Commentary. Please share your knowledge!
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
-->
<protect>
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
- ↑ 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
- ↑ 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
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>
