YCR034W - Revision history

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{{PageTop}}
{|{{Prettytable}} align = 'right' width = '200px'
|-
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?locus=YCR034W YCR034W]
|-
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''FEN1 ''
|-
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Aliases''' ||''ELO2, GNS1, VBM2''
|-
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Feature type''' || ORF, Verified[[Category:ORF]][[Category:ORF, Verified]]
|-
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
|nowrap| Chr III:190588..191631
|-
|colspan = '3'|{{Don'tEditThisBox}}
|}
 
'''Description of {{PAGENAME}}:''' Fatty acid elongase, involved in sphingolipid biosynthesis; acts on fatty acids of up to 24 carbons in length; mutations have regulatory effects on 1,3-beta-glucan synthase, vacuolar ATPase, and the secretory pathway<ref name='S000073969'>Chung JH, et al. (2003) Sphingolipid requirement for generation of a functional v1 component of the vacuolar ATPase. J Biol Chem 278(31):28872-81 {{SGDpaper|S000073969}} PMID 12746460</ref><ref name='S000060998'>Abe M, et al. (2001) Yeast 1,3-beta-glucan synthase activity is inhibited by phytosphingosine localized to the endoplasmic reticulum. J Biol Chem 276(29):26923-30 {{SGDpaper|S000060998}} PMID 11337502</ref><ref name='S000055688'>Oh CS, et al. (1997) ELO2 and ELO3, homologues of the Saccharomyces cerevisiae ELO1 gene, function in fatty acid elongation and are required for sphingolipid formation. J Biol Chem 272(28):17376-84 {{SGDpaper|S000055688}} PMID 9211877</ref><ref name='S000043234'>David D, et al. (1998) Involvement of long chain fatty acid elongation in the trafficking of secretory vesicles in yeast. J Cell Biol 143(5):1167-82
{{SGDpaper|S000043234}} PMID 9832547</ref>
 
 
 
 

__TOC__
==Community Commentary==
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==References==

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@@ Line 13: / Line 13: @@
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
-|nowrap| Chr III:190588..191631
+|nowrap| Chr III:190592..191635
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''           || S000000630

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YCR034W:''' Fatty acid elongase, involved in sphingolipid biosynthesis; acts on fatty acids of up to 24 carbons in length; mutations have regulatory effects on 1,3-beta-glucan synthase, vacuolar ATPase, and the secretory pathway<ref name='S000043234'>David D, et al. (1998) Involvement of long chain fatty acid elongation in the trafficking of secretory vesicles in yeast. J Cell Biol 143(5):1167-82 {{SGDpaper|S000043234}} PMID 9832547</ref><ref name='S000055688'>Oh CS, et al. (1997) ELO2 and ELO3, homologues of the Saccharomyces cerevisiae ELO1 gene, function in fatty acid elongation and are required for sphingolipid formation. J Biol Chem 272(28):17376-84 {{SGDpaper|S000055688}} PMID 9211877</ref><ref name='S000060998'>Abe M, et al. (2001) Yeast 1,3-beta-glucan synthase activity is inhibited by phytosphingosine localized to the endoplasmic reticulum. J Biol Chem 276(29):26923-30 {{SGDpaper|S000060998}} PMID 11337502</ref><ref name='S000073969'>Chung JH, et al. (2003) Sphingolipid requirement for generation of a functional v1 component of the vacuolar ATPase. J Biol Chem 278(31):28872-81
+'''Description of YCR034W:''' Fatty acid elongase, involved in sphingolipid biosynthesis; acts on fatty acids of up to 24 carbons in length; mutations have regulatory effects on 1,3-beta-glucan synthase, vacuolar ATPase, and the secretory pathway<ref name='S000060998'>Abe M, et al. (2001) Yeast 1,3-beta-glucan synthase activity is inhibited by phytosphingosine localized to the endoplasmic reticulum. J Biol Chem 276(29):26923-30 {{SGDpaper|S000060998}} PMID 11337502</ref><ref name='S000073969'>Chung JH, et al. (2003) Sphingolipid requirement for generation of a functional v1 component of the vacuolar ATPase. J Biol Chem 278(31):28872-81 {{SGDpaper|S000073969}} PMID 12746460</ref><ref name='S000043234'>David D, et al. (1998) Involvement of long chain fatty acid elongation in the trafficking of secretory vesicles in yeast. J Cell Biol 143(5):1167-82 {{SGDpaper|S000043234}} PMID 9832547</ref><ref name='S000055688'>Oh CS, et al. (1997) ELO2 and ELO3, homologues of the Saccharomyces cerevisiae ELO1 gene, function in fatty acid elongation and are required for sphingolipid formation. J Biol Chem 272(28):17376-84
-  {{SGDpaper|S000073969}} PMID 12746460</ref>
+  {{SGDpaper|S000055688}} PMID 9211877</ref>
 <br>
 <br>

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YCR034W:''' Fatty acid elongase, involved in sphingolipid biosynthesis; acts on fatty acids of up to 24 carbons in length; mutations have regulatory effects on 1,3-beta-glucan synthase, vacuolar ATPase, and the secretory pathway<ref name='S000073969'>Chung JH, et al. (2003) Sphingolipid requirement for generation of a functional v1 component of the vacuolar ATPase. J Biol Chem 278(31):28872-81 {{SGDpaper|S000073969}} PMID 12746460</ref><ref name='S000060998'>Abe M, et al. (2001) Yeast 1,3-beta-glucan synthase activity is inhibited by phytosphingosine localized to the endoplasmic reticulum. J Biol Chem 276(29):26923-30 {{SGDpaper|S000060998}} PMID 11337502</ref><ref name='S000055688'>Oh CS, et al. (1997) ELO2 and ELO3, homologues of the Saccharomyces cerevisiae ELO1 gene, function in fatty acid elongation and are required for sphingolipid formation. J Biol Chem 272(28):17376-84 {{SGDpaper|S000055688}} PMID 9211877</ref><ref name='S000043234'>David D, et al. (1998) Involvement of long chain fatty acid elongation in the trafficking of secretory vesicles in yeast. J Cell Biol 143(5):1167-82
+'''Description of YCR034W:''' Fatty acid elongase, involved in sphingolipid biosynthesis; acts on fatty acids of up to 24 carbons in length; mutations have regulatory effects on 1,3-beta-glucan synthase, vacuolar ATPase, and the secretory pathway<ref name='S000043234'>David D, et al. (1998) Involvement of long chain fatty acid elongation in the trafficking of secretory vesicles in yeast. J Cell Biol 143(5):1167-82 {{SGDpaper|S000043234}} PMID 9832547</ref><ref name='S000055688'>Oh CS, et al. (1997) ELO2 and ELO3, homologues of the Saccharomyces cerevisiae ELO1 gene, function in fatty acid elongation and are required for sphingolipid formation. J Biol Chem 272(28):17376-84 {{SGDpaper|S000055688}} PMID 9211877</ref><ref name='S000060998'>Abe M, et al. (2001) Yeast 1,3-beta-glucan synthase activity is inhibited by phytosphingosine localized to the endoplasmic reticulum. J Biol Chem 276(29):26923-30 {{SGDpaper|S000060998}} PMID 11337502</ref><ref name='S000073969'>Chung JH, et al. (2003) Sphingolipid requirement for generation of a functional v1 component of the vacuolar ATPase. J Biol Chem 278(31):28872-81
-  {{SGDpaper|S000043234}} PMID 9832547</ref>
+  {{SGDpaper|S000073969}} PMID 12746460</ref>
 <br>
 <br>

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YCR034W:''' Fatty acid elongase, involved in sphingolipid biosynthesis; acts on fatty acids of up to 24 carbons in length; mutations have regulatory effects on 1,3-beta-glucan synthase, vacuolar ATPase, and the secretory pathway<ref name='S000043234'>David D, et al. (1998) Involvement of long chain fatty acid elongation in the trafficking of secretory vesicles in yeast. J Cell Biol 143(5):1167-82 {{SGDpaper|S000043234}} PMID 9832547</ref><ref name='S000055688'>Oh CS, et al. (1997) ELO2 and ELO3, homologues of the Saccharomyces cerevisiae ELO1 gene, function in fatty acid elongation and are required for sphingolipid formation. J Biol Chem 272(28):17376-84 {{SGDpaper|S000055688}} PMID 9211877</ref><ref name='S000060998'>Abe M, et al. (2001) Yeast 1,3-beta-glucan synthase activity is inhibited by phytosphingosine localized to the endoplasmic reticulum. J Biol Chem 276(29):26923-30 {{SGDpaper|S000060998}} PMID 11337502</ref><ref name='S000073969'>Chung JH, et al. (2003) Sphingolipid requirement for generation of a functional v1 component of the vacuolar ATPase. J Biol Chem 278(31):28872-81
+'''Description of YCR034W:''' Fatty acid elongase, involved in sphingolipid biosynthesis; acts on fatty acids of up to 24 carbons in length; mutations have regulatory effects on 1,3-beta-glucan synthase, vacuolar ATPase, and the secretory pathway<ref name='S000073969'>Chung JH, et al. (2003) Sphingolipid requirement for generation of a functional v1 component of the vacuolar ATPase. J Biol Chem 278(31):28872-81 {{SGDpaper|S000073969}} PMID 12746460</ref><ref name='S000060998'>Abe M, et al. (2001) Yeast 1,3-beta-glucan synthase activity is inhibited by phytosphingosine localized to the endoplasmic reticulum. J Biol Chem 276(29):26923-30 {{SGDpaper|S000060998}} PMID 11337502</ref><ref name='S000055688'>Oh CS, et al. (1997) ELO2 and ELO3, homologues of the Saccharomyces cerevisiae ELO1 gene, function in fatty acid elongation and are required for sphingolipid formation. J Biol Chem 272(28):17376-84 {{SGDpaper|S000055688}} PMID 9211877</ref><ref name='S000043234'>David D, et al. (1998) Involvement of long chain fatty acid elongation in the trafficking of secretory vesicles in yeast. J Cell Biol 143(5):1167-82
-  {{SGDpaper|S000073969}} PMID 12746460</ref>
+  {{SGDpaper|S000043234}} PMID 9832547</ref>
 <br>
 <br>

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YCR034W:''' Fatty acid elongase, involved in sphingolipid biosynthesis; acts on fatty acids of up to 24 carbons in length; mutations have regulatory effects on 1,3-beta-glucan synthase, vacuolar ATPase, and the secretory pathway<ref name='S000073969'>Chung JH, et al. (2003) Sphingolipid requirement for generation of a functional v1 component of the vacuolar ATPase. J Biol Chem 278(31):28872-81 {{SGDpaper|S000073969}} PMID 12746460</ref><ref name='S000060998'>Abe M, et al. (2001) Yeast 1,3-beta-glucan synthase activity is inhibited by phytosphingosine localized to the endoplasmic reticulum. J Biol Chem 276(29):26923-30 {{SGDpaper|S000060998}} PMID 11337502</ref><ref name='S000055688'>Oh CS, et al. (1997) ELO2 and ELO3, homologues of the Saccharomyces cerevisiae ELO1 gene, function in fatty acid elongation and are required for sphingolipid formation. J Biol Chem 272(28):17376-84 {{SGDpaper|S000055688}} PMID 9211877</ref><ref name='S000043234'>David D, et al. (1998) Involvement of long chain fatty acid elongation in the trafficking of secretory vesicles in yeast. J Cell Biol 143(5):1167-82
+'''Description of YCR034W:''' Fatty acid elongase, involved in sphingolipid biosynthesis; acts on fatty acids of up to 24 carbons in length; mutations have regulatory effects on 1,3-beta-glucan synthase, vacuolar ATPase, and the secretory pathway<ref name='S000043234'>David D, et al. (1998) Involvement of long chain fatty acid elongation in the trafficking of secretory vesicles in yeast. J Cell Biol 143(5):1167-82 {{SGDpaper|S000043234}} PMID 9832547</ref><ref name='S000055688'>Oh CS, et al. (1997) ELO2 and ELO3, homologues of the Saccharomyces cerevisiae ELO1 gene, function in fatty acid elongation and are required for sphingolipid formation. J Biol Chem 272(28):17376-84 {{SGDpaper|S000055688}} PMID 9211877</ref><ref name='S000060998'>Abe M, et al. (2001) Yeast 1,3-beta-glucan synthase activity is inhibited by phytosphingosine localized to the endoplasmic reticulum. J Biol Chem 276(29):26923-30 {{SGDpaper|S000060998}} PMID 11337502</ref><ref name='S000073969'>Chung JH, et al. (2003) Sphingolipid requirement for generation of a functional v1 component of the vacuolar ATPase. J Biol Chem 278(31):28872-81
-  {{SGDpaper|S000043234}} PMID 9832547</ref>
+  {{SGDpaper|S000073969}} PMID 12746460</ref>
 <br>
 <br>

@@ 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=S000000630 YCR034W]
+|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000000630 YCR034W]
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''         ||''FEN1 ''

← Older revision		Revision as of 20:02, 21 February 2007
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		+	<!-- 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>

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 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
 |nowrap| Chr III:190588..191631
 |}
 <br>
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+<br>
 __TOC__
 ==Community Commentary==
 {{CommentaryHelp}}
 ==References==
 <!-- REFERENCES ARE AUTOMATICALLY GENERATED.  PLEASE DON'T EDIT THIS SECTION-->
 {{RefHelp}}