View source for S000000054

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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?locus=YAL058W YAL058W] 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''         ||''CNE1 ''
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Aliases'''           ||''FUN48''
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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'''
|nowrap| Chr I:37465..38973
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'''Description of {{PAGENAME}}:''' Calnexin; integral membrane ER chaperone involved in folding and quality control of glycoproteins; chaperone activity is inhibited by Mpd1p, with which Cne1p interacts; 24% identical to mammalian calnexin; Ca+ binding not yet shown in yeast<ref name='S000082272'>Kimura T, et al. (2005) Interactions among Yeast Protein-Disulfide Isomerase Proteins and Endoplasmic Reticulum Chaperone Proteins Influence Their Activities. J Biol Chem 280(36):31438-41 {{SGDpaper|S000082272}} PMID 16002399</ref><ref name='S000076690'>Xu X, et al. (2004) P-domain and lectin site are involved in the chaperone function of Saccharomyces cerevisiae calnexin homologue. FEBS Lett 570(1-3):155-60 {{SGDpaper|S000076690}} PMID 15251457</ref><ref name='S000076464'>Xu X, et al. (2004) Expression and characterization of Saccharomyces cerevisiae Cne1p, a calnexin homologue. J Biochem (Tokyo) 135(5):615-8 {{SGDpaper|S000076464}} PMID 15173200</ref><ref name='S000039200'>Parlati F, et al. (1995) Saccharomyces cerevisiae CNE1 encodes an endoplasmic reticulum (ER) membrane protein with sequence similarity to calnexin and calreticulin and functions as a constituent of the ER quality control apparatus. J Biol Chem 270(1):244-53
 {{SGDpaper|S000039200}} PMID 7814381</ref>
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==References==
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