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| − | <!-- PLEASE DO NOT EDIT HERE. USE THE SECTION EDIT LINKS ON THE RIGHT MARGIN-->
| + | #REDIRECT [[YBR070C]] |
| − | {{PageTop}}
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| − | <protect>
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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=YBR070C YBR070C]
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| − | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''ALG14 ''
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| − | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Aliases''' ||'' ''
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| − | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Feature type''' || ORF, Verified[[Category:ORF]][[Category:ORF, Verified]]
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| − | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
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| − | |nowrap| Chr II:379931..379218
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| − | |}
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| − | '''Description of {{PAGENAME}}:''' 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='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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| − | {{SGDpaper|S000080148}} PMID 15615718</ref>
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| − | </protect>
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| − | __TOC__
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| − | ==Community Commentary==
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| − | {{CommentaryHelp}}
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| − | ==References==
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| − | <!-- REFERENCES ARE AUTOMATICALLY GENERATED. PLEASE DON'T EDIT THIS SECTION-->
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| − | {{RefHelp}}
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| − | </protect>
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