YNL239W - 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=YNL239W YNL239W]
|-
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''LAP3 ''
|-
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Aliases''' ||''BLH1, GAL6, YCP1''
|-
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Feature type''' || ORF, Verified[[Category:ORF]][[Category:ORF, Verified]]
|-
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
|nowrap| Chr XIV:200570..201934
|-
|colspan = '3'|{{Don'tEditThisBox}}
|}
 
'''Description of {{PAGENAME}}:''' Aminopeptidase of cysteine protease family, has a DNA binding activity and acts as bleomycin hydrolase in vitro; transcription is regulated by galactose via Gal4p<ref name='S000063844'>Zheng W, et al. (1997) The cysteine-peptidase bleomycin hydrolase is a member of the galactose regulon in yeast. J Biol Chem 272(48):30350-5 {{SGDpaper|S000063844}} PMID 9374524</ref><ref name='S000063843'>Xu HE and Johnston SA (1994) Yeast bleomycin hydrolase is a DNA-binding cysteine protease. Identification, purification, biochemical characterization. J Biol Chem 269(33):21177-83 {{SGDpaper|S000063843}} PMID 8063738</ref><ref name='S000045477'>Kambouris NG, et al. (1992) Cloning and characterization of a cysteine proteinase from Saccharomyces cerevisiae. J Biol Chem 267(30):21570-6
{{SGDpaper|S000045477}} PMID 1400467</ref>
 
 
 
 

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

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 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
-|nowrap| Chr XIV:200570..201934
+|nowrap| Chr XIV:200569..201933
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''           || S000005183

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YNL239W:''' Cysteine aminopeptidase with homocysteine-thiolactonase activity; protects cells against homocysteine toxicity; has bleomycin hydrolase activity in vitro; transcription is regulated by galactose via Gal4p; orthologous to human BLMH<ref name='S000045477'>Kambouris NG, et al. (1992) Cloning and characterization of a cysteine proteinase from Saccharomyces cerevisiae. J Biol Chem 267(30):21570-6 {{SGDpaper|S000045477}} PMID 1400467</ref><ref name='S000063843'>Xu HE and Johnston SA (1994) Yeast bleomycin hydrolase is a DNA-binding cysteine protease. Identification, purification, biochemical characterization. J Biol Chem 269(33):21177-83 {{SGDpaper|S000063843}} PMID 8063738</ref><ref name='S000063844'>Zheng W, et al. (1997) The cysteine-peptidase bleomycin hydrolase is a member of the galactose regulon in yeast. J Biol Chem 272(48):30350-5 {{SGDpaper|S000063844}} PMID 9374524</ref><ref name='S000117710'>Zimny J, et al. (2006) Protective mechanisms against homocysteine toxicity: the role of bleomycin hydrolase. J Biol Chem 281(32):22485-92 {{SGDpaper|S000117710}} PMID 16769724</ref><ref name='S000122739'>Ferrando AA, et al. (1996) Cloning and expression analysis of human bleomycin hydrolase, a cysteine proteinase involved in chemotherapy resistance. Cancer Res 56(8):1746-50
+'''Description of YNL239W:''' Cysteine aminopeptidase with homocysteine-thiolactonase activity; protects cells against homocysteine toxicity; has bleomycin hydrolase activity in vitro; transcription is regulated by galactose via Gal4p; orthologous to human BLMH<ref name='S000122739'>Ferrando AA, et al. (1996) Cloning and expression analysis of human bleomycin hydrolase, a cysteine proteinase involved in chemotherapy resistance. Cancer Res 56(8):1746-50 {{SGDpaper|S000122739}} PMID 8620487</ref><ref name='S000045477'>Kambouris NG, et al. (1992) Cloning and characterization of a cysteine proteinase from Saccharomyces cerevisiae. J Biol Chem 267(30):21570-6 {{SGDpaper|S000045477}} PMID 1400467</ref><ref name='S000063843'>Xu HE and Johnston SA (1994) Yeast bleomycin hydrolase is a DNA-binding cysteine protease. Identification, purification, biochemical characterization. J Biol Chem 269(33):21177-83 {{SGDpaper|S000063843}} PMID 8063738</ref><ref name='S000063844'>Zheng W, et al. (1997) The cysteine-peptidase bleomycin hydrolase is a member of the galactose regulon in yeast. J Biol Chem 272(48):30350-5 {{SGDpaper|S000063844}} PMID 9374524</ref><ref name='S000117710'>Zimny J, et al. (2006) Protective mechanisms against homocysteine toxicity: the role of bleomycin hydrolase. J Biol Chem 281(32):22485-92
- {{SGDpaper|S000122739}} PMID 8620487</ref>
+ {{SGDpaper|S000117710}} PMID 16769724</ref>
 <br>
 <br>

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YNL239W:''' Cysteine aminopeptidase with homocysteine-thiolactonase activity; protects cells against homocysteine toxicity; has bleomycin hydrolase activity in vitro; transcription is regulated by galactose via Gal4p; orthologous to human BLMH<ref name='S000122739'>Ferrando AA, et al. (1996) Cloning and expression analysis of human bleomycin hydrolase, a cysteine proteinase involved in chemotherapy resistance. Cancer Res 56(8):1746-50 {{SGDpaper|S000122739}} PMID 8620487</ref><ref name='S000117710'>Zimny J, et al. (2006) Protective mechanisms against homocysteine toxicity: the role of bleomycin hydrolase. J Biol Chem 281(32):22485-92 {{SGDpaper|S000117710}} PMID 16769724</ref><ref name='S000063844'>Zheng W, et al. (1997) The cysteine-peptidase bleomycin hydrolase is a member of the galactose regulon in yeast. J Biol Chem 272(48):30350-5 {{SGDpaper|S000063844}} PMID 9374524</ref><ref name='S000063843'>Xu HE and Johnston SA (1994) Yeast bleomycin hydrolase is a DNA-binding cysteine protease. Identification, purification, biochemical characterization. J Biol Chem 269(33):21177-83 {{SGDpaper|S000063843}} PMID 8063738</ref><ref name='S000045477'>Kambouris NG, et al. (1992) Cloning and characterization of a cysteine proteinase from Saccharomyces cerevisiae. J Biol Chem 267(30):21570-6
+'''Description of YNL239W:''' Cysteine aminopeptidase with homocysteine-thiolactonase activity; protects cells against homocysteine toxicity; has bleomycin hydrolase activity in vitro; transcription is regulated by galactose via Gal4p; orthologous to human BLMH<ref name='S000045477'>Kambouris NG, et al. (1992) Cloning and characterization of a cysteine proteinase from Saccharomyces cerevisiae. J Biol Chem 267(30):21570-6 {{SGDpaper|S000045477}} PMID 1400467</ref><ref name='S000063843'>Xu HE and Johnston SA (1994) Yeast bleomycin hydrolase is a DNA-binding cysteine protease. Identification, purification, biochemical characterization. J Biol Chem 269(33):21177-83 {{SGDpaper|S000063843}} PMID 8063738</ref><ref name='S000063844'>Zheng W, et al. (1997) The cysteine-peptidase bleomycin hydrolase is a member of the galactose regulon in yeast. J Biol Chem 272(48):30350-5 {{SGDpaper|S000063844}} PMID 9374524</ref><ref name='S000117710'>Zimny J, et al. (2006) Protective mechanisms against homocysteine toxicity: the role of bleomycin hydrolase. J Biol Chem 281(32):22485-92 {{SGDpaper|S000117710}} PMID 16769724</ref><ref name='S000122739'>Ferrando AA, et al. (1996) Cloning and expression analysis of human bleomycin hydrolase, a cysteine proteinase involved in chemotherapy resistance. Cancer Res 56(8):1746-50
-  {{SGDpaper|S000045477}} PMID 1400467</ref>
+  {{SGDpaper|S000122739}} PMID 8620487</ref>
 <br>
 <br>

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YNL239W:''' Aminopeptidase of cysteine protease family, has a DNA binding activity and acts as bleomycin hydrolase in vitro; transcription is regulated by galactose via Gal4p<ref name='S000063844'>Zheng W, et al. (1997) The cysteine-peptidase bleomycin hydrolase is a member of the galactose regulon in yeast. J Biol Chem 272(48):30350-5 {{SGDpaper|S000063844}} PMID 9374524</ref><ref name='S000063843'>Xu HE and Johnston SA (1994) Yeast bleomycin hydrolase is a DNA-binding cysteine protease. Identification, purification, biochemical characterization. J Biol Chem 269(33):21177-83 {{SGDpaper|S000063843}} PMID 8063738</ref><ref name='S000045477'>Kambouris NG, et al. (1992) Cloning and characterization of a cysteine proteinase from Saccharomyces cerevisiae. J Biol Chem 267(30):21570-6
+'''Description of YNL239W:''' Cysteine aminopeptidase with homocysteine-thiolactonase activity; protects cells against homocysteine toxicity; has bleomycin hydrolase activity in vitro; transcription is regulated by galactose via Gal4p; orthologous to human BLMH<ref name='S000122739'>Ferrando AA, et al. (1996) Cloning and expression analysis of human bleomycin hydrolase, a cysteine proteinase involved in chemotherapy resistance. Cancer Res 56(8):1746-50 {{SGDpaper|S000122739}} PMID 8620487</ref><ref name='S000117710'>Zimny J, et al. (2006) Protective mechanisms against homocysteine toxicity: the role of bleomycin hydrolase. J Biol Chem 281(32):22485-92 {{SGDpaper|S000117710}} PMID 16769724</ref><ref name='S000063844'>Zheng W, et al. (1997) The cysteine-peptidase bleomycin hydrolase is a member of the galactose regulon in yeast. J Biol Chem 272(48):30350-5 {{SGDpaper|S000063844}} PMID 9374524</ref><ref name='S000063843'>Xu HE and Johnston SA (1994) Yeast bleomycin hydrolase is a DNA-binding cysteine protease. Identification, purification, biochemical characterization. J Biol Chem 269(33):21177-83 {{SGDpaper|S000063843}} PMID 8063738</ref><ref name='S000045477'>Kambouris NG, et al. (1992) Cloning and characterization of a cysteine proteinase from Saccharomyces cerevisiae. J Biol Chem 267(30):21570-6
   {{SGDpaper|S000045477}} PMID 1400467</ref>
 <br>

← 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 -->
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		+	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>
		+	-->

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 {|{{Prettytable}} align = 'right' width = '200px'
 |-
-|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000005183 YNL239W]
+|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000005183 YNL239W]
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''         ||''LAP3 ''

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 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
 |nowrap| Chr XIV:200570..201934
 |}
 <br>
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 <br>
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+<br>
 __TOC__
 ==Community Commentary==
 {{CommentaryHelp}}
 ==References==
 <!-- REFERENCES ARE AUTOMATICALLY GENERATED.  PLEASE DON'T EDIT THIS SECTION-->
 {{RefHelp}}