YAL058W - Revision history

SGDwikiBot: Automated import of articles

2012-01-23T14:45:16Z

Automated import of articles

SGDwikiBot: Automated import of articles

2011-02-03T21:05:13Z

Automated import of articles

SGDwikiBot: Automated import of articles

2010-02-25T21:05:11Z

Automated import of articles

SGDwikiBot: Automated import of articles

2009-03-31T21:05:08Z

Automated import of articles

SGDwikiBot: Automated import of articles

2009-01-16T21:05:09Z

Automated import of articles

SGDwikiBot: Automated import of articles

2008-12-18T11:40:04Z

Automated import of articles

SGDwikiBot: Automated import of articles

2007-12-22T21:05:06Z

Automated import of articles

SGDwikiBot: Automated import of articles

2007-02-27T15:45:54Z

Automated import of articles

SGDwikiBot: Automated import of articles

2007-02-21T20:02:01Z

Automated import of articles

SGDwikiBot: Automated import of articles

2007-01-30T15:17:46Z

Automated import of articles

@@ Line 4: / Line 4: @@
 {|{{Prettytable}} align = 'right' width = '200px'
 |-
-|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000000054 YAL058W]
+|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000000054 YAL058W]
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''         ||''CNE1 ''

@@ Line 13: / Line 13: @@
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
-|nowrap| Chr I:37465..38973
+|nowrap| Chr I:37464..38972
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''           || S000000054

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YAL058W:''' 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='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><ref name='S000076464'>Xu X, et al. (2004) Expression and characterization of Saccharomyces cerevisiae Cne1p, a calnexin homologue. J Biochem 135(5):615-8 {{SGDpaper|S000076464}} PMID 15173200</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='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
+'''Description of YAL058W:''' 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='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><ref name='S000076464'>Xu X, et al. (2004) Expression and characterization of Saccharomyces cerevisiae Cne1p, a calnexin homologue. J Biochem 135(5):615-8 {{SGDpaper|S000076464}} PMID 15173200</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|S000082272}} PMID 16002399</ref>
+ {{SGDpaper|S000076690}} PMID 15251457</ref>
 <br>
 <br>

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YAL058W:''' 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 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
+'''Description of YAL058W:''' 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='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><ref name='S000076464'>Xu X, et al. (2004) Expression and characterization of Saccharomyces cerevisiae Cne1p, a calnexin homologue. J Biochem 135(5):615-8 {{SGDpaper|S000076464}} PMID 15173200</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='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|S000039200}} PMID 7814381</ref>
+  {{SGDpaper|S000082272}} PMID 16002399</ref>
 <br>
 <br>

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YAL058W:''' 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='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><ref name='S000076464'>Xu X, et al. (2004) Expression and characterization of Saccharomyces cerevisiae Cne1p, a calnexin homologue. J Biochem 135(5):615-8 {{SGDpaper|S000076464}} PMID 15173200</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='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
+'''Description of YAL058W:''' 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 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|S000082272}} PMID 16002399</ref>
+  {{SGDpaper|S000039200}} PMID 7814381</ref>
 <br>
 <br>

← Older revision		Revision as of 20:02, 21 February 2007
Line 28:		Line 28:
	{{CommentaryHelp}}		{{CommentaryHelp}}

		+
		+
		+
		+	<!-- PLEASE ADD Community Commentary ABOVE THIS MESSAGE. See below for an example of community annotation -->
		+	<!--
		+	Specifically higher expression in carbon limited chemostat cultures versus carbon excess.
		+	<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.
		+	J Biol Chem 278(5):3265-74</ref>
		+	-->

	<protect>		<protect>

@@ Line 1: / Line 1: @@
 <!-- PLEASE DO NOT EDIT HERE. USE THE SECTION EDIT LINKS ON THE RIGHT MARGIN-->
 {{PageTop}}
 {|{{Prettytable}} align = 'right' width = '200px'
 |-
@@ Line 13: / Line 14: @@
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
 |nowrap| Chr I:37465..38973
 |}
 <br>
@@ Line 23: / Line 22: @@
 <br>
 <br>
+<br>
 __TOC__
 ==Community Commentary==
 {{CommentaryHelp}}
 ==References==
 <!-- REFERENCES ARE AUTOMATICALLY GENERATED.  PLEASE DON'T EDIT THIS SECTION-->
 {{RefHelp}}