YCL057W - 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=YCL057W YCL057W]
|-
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''PRD1 ''
|-
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Aliases''' ||'' ''
|-
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Feature type''' || ORF, Verified[[Category:ORF]][[Category:ORF, Verified]]
|-
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
|nowrap| Chr III:24768..26906
|-
|colspan = '3'|{{Don'tEditThisBox}}
|}
 
'''Description of {{PAGENAME}}:''' Zinc metalloendopeptidase, found in the cytoplasm and intermembrane space of mitochondria; with Cym1p, involved in degradation of mitochondrial proteins and of presequence peptides cleaved from imported proteins<ref name='S000081142'>Kambacheld M, et al. (2005) Role of the novel metallopeptidase Mop112 and saccharolysin for the complete degradation of proteins residing in different subcompartments of mitochondria. J Biol Chem 280(20):20132-9 {{SGDpaper|S000081142}} PMID 15772085</ref><ref name='S000057643'>Hrycyna CA and Clarke S (1993) Purification and characterization of a novel metalloendopeptidase from Saccharomyces cerevisiae. Biochemistry 32(42):11293-301 {{SGDpaper|S000057643}} PMID 8218194</ref><ref name='S000055068'>Buchler M, et al. (1994) Proteinase yscD (oligopeptidase yscD). Structure, function and relationship of the yeast enzyme with mammalian thimet oligopeptidase (metalloendopeptidase, EP 24.15). Eur J Biochem 219(1-2):627-39
{{SGDpaper|S000055068}} PMID 8307027</ref>
 
 
 
 

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==Community Commentary==
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==References==

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@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YCL057W:''' Zinc metalloendopeptidase, found in the cytoplasm and intermembrane space of mitochondria; with Cym1p, involved in degradation of mitochondrial proteins and of presequence peptides cleaved from imported proteins<ref name='S000081142'>Kambacheld M, et al. (2005) Role of the novel metallopeptidase Mop112 and saccharolysin for the complete degradation of proteins residing in different subcompartments of mitochondria. J Biol Chem 280(20):20132-9 {{SGDpaper|S000081142}} PMID 15772085</ref><ref name='S000057643'>Hrycyna CA and Clarke S (1993) Purification and characterization of a novel metalloendopeptidase from Saccharomyces cerevisiae. Biochemistry 32(42):11293-301 {{SGDpaper|S000057643}} PMID 8218194</ref><ref name='S000055068'>Buchler M, et al. (1994) Proteinase yscD (oligopeptidase yscD). Structure, function and relationship of the yeast enzyme with mammalian thimet oligopeptidase (metalloendopeptidase, EP 24.15). Eur J Biochem 219(1-2):627-39
+'''Description of YCL057W:''' Zinc metalloendopeptidase, found in the cytoplasm and intermembrane space of mitochondria; with Cym1p, involved in degradation of mitochondrial proteins and of presequence peptides cleaved from imported proteins<ref name='S000055068'>Buchler M, et al. (1994) Proteinase yscD (oligopeptidase yscD). Structure, function and relationship of the yeast enzyme with mammalian thimet oligopeptidase (metalloendopeptidase, EP 24.15). Eur J Biochem 219(1-2):627-39 {{SGDpaper|S000055068}} PMID 8307027</ref><ref name='S000057643'>Hrycyna CA and Clarke S (1993) Purification and characterization of a novel metalloendopeptidase from Saccharomyces cerevisiae. Biochemistry 32(42):11293-301 {{SGDpaper|S000057643}} PMID 8218194</ref><ref name='S000081142'>Kambacheld M, et al. (2005) Role of the novel metallopeptidase Mop112 and saccharolysin for the complete degradation of proteins residing in different subcompartments of mitochondria. J Biol Chem 280(20):20132-9
-  {{SGDpaper|S000055068}} PMID 8307027</ref>
+  {{SGDpaper|S000081142}} PMID 15772085</ref>
 <br>
 <br>

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YCL057W:''' Zinc metalloendopeptidase, found in the cytoplasm and intermembrane space of mitochondria; with Cym1p, involved in degradation of mitochondrial proteins and of presequence peptides cleaved from imported proteins<ref name='S000055068'>Buchler M, et al. (1994) Proteinase yscD (oligopeptidase yscD). Structure, function and relationship of the yeast enzyme with mammalian thimet oligopeptidase (metalloendopeptidase, EP 24.15). Eur J Biochem 219(1-2):627-39 {{SGDpaper|S000055068}} PMID 8307027</ref><ref name='S000057643'>Hrycyna CA and Clarke S (1993) Purification and characterization of a novel metalloendopeptidase from Saccharomyces cerevisiae. Biochemistry 32(42):11293-301 {{SGDpaper|S000057643}} PMID 8218194</ref><ref name='S000081142'>Kambacheld M, et al. (2005) Role of the novel metallopeptidase Mop112 and saccharolysin for the complete degradation of proteins residing in different subcompartments of mitochondria. J Biol Chem 280(20):20132-9
+'''Description of YCL057W:''' Zinc metalloendopeptidase, found in the cytoplasm and intermembrane space of mitochondria; with Cym1p, involved in degradation of mitochondrial proteins and of presequence peptides cleaved from imported proteins<ref name='S000081142'>Kambacheld M, et al. (2005) Role of the novel metallopeptidase Mop112 and saccharolysin for the complete degradation of proteins residing in different subcompartments of mitochondria. J Biol Chem 280(20):20132-9 {{SGDpaper|S000081142}} PMID 15772085</ref><ref name='S000057643'>Hrycyna CA and Clarke S (1993) Purification and characterization of a novel metalloendopeptidase from Saccharomyces cerevisiae. Biochemistry 32(42):11293-301 {{SGDpaper|S000057643}} PMID 8218194</ref><ref name='S000055068'>Buchler M, et al. (1994) Proteinase yscD (oligopeptidase yscD). Structure, function and relationship of the yeast enzyme with mammalian thimet oligopeptidase (metalloendopeptidase, EP 24.15). Eur J Biochem 219(1-2):627-39
-  {{SGDpaper|S000081142}} PMID 15772085</ref>
+  {{SGDpaper|S000055068}} PMID 8307027</ref>
 <br>
 <br>

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YCL057W:''' Zinc metalloendopeptidase, found in the cytoplasm and intermembrane space of mitochondria; with Cym1p, involved in degradation of mitochondrial proteins and of presequence peptides cleaved from imported proteins<ref name='S000081142'>Kambacheld M, et al. (2005) Role of the novel metallopeptidase Mop112 and saccharolysin for the complete degradation of proteins residing in different subcompartments of mitochondria. J Biol Chem 280(20):20132-9 {{SGDpaper|S000081142}} PMID 15772085</ref><ref name='S000057643'>Hrycyna CA and Clarke S (1993) Purification and characterization of a novel metalloendopeptidase from Saccharomyces cerevisiae. Biochemistry 32(42):11293-301 {{SGDpaper|S000057643}} PMID 8218194</ref><ref name='S000055068'>Buchler M, et al. (1994) Proteinase yscD (oligopeptidase yscD). Structure, function and relationship of the yeast enzyme with mammalian thimet oligopeptidase (metalloendopeptidase, EP 24.15). Eur J Biochem 219(1-2):627-39
+'''Description of YCL057W:''' Zinc metalloendopeptidase, found in the cytoplasm and intermembrane space of mitochondria; with Cym1p, involved in degradation of mitochondrial proteins and of presequence peptides cleaved from imported proteins<ref name='S000055068'>Buchler M, et al. (1994) Proteinase yscD (oligopeptidase yscD). Structure, function and relationship of the yeast enzyme with mammalian thimet oligopeptidase (metalloendopeptidase, EP 24.15). Eur J Biochem 219(1-2):627-39 {{SGDpaper|S000055068}} PMID 8307027</ref><ref name='S000057643'>Hrycyna CA and Clarke S (1993) Purification and characterization of a novel metalloendopeptidase from Saccharomyces cerevisiae. Biochemistry 32(42):11293-301 {{SGDpaper|S000057643}} PMID 8218194</ref><ref name='S000081142'>Kambacheld M, et al. (2005) Role of the novel metallopeptidase Mop112 and saccharolysin for the complete degradation of proteins residing in different subcompartments of mitochondria. J Biol Chem 280(20):20132-9
-  {{SGDpaper|S000055068}} PMID 8307027</ref>
+  {{SGDpaper|S000081142}} PMID 15772085</ref>
 <br>
 <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 -->
		+	<!--
		+	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=S000000562 YCL057W]
+|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000000562 YCL057W]
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''         ||''PRD1 ''

@@ Line 4: / Line 4: @@
 {|{{Prettytable}} align = 'right' width = '200px'
 |-
-|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?locus=YCL057W YCL057W]
+|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000000562 YCL057W]
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''         ||''PRD1 ''
@@ Line 14: / Line 14: @@
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
 |nowrap| Chr III:24768..26906
 |}
 <br>
-'''Description of {{PAGENAME}}:''' Zinc metalloendopeptidase, found in the cytoplasm and intermembrane space of mitochondria; with Cym1p, involved in degradation of mitochondrial proteins and of presequence peptides cleaved from imported proteins<ref name='S000081142'>Kambacheld M, et al. (2005) Role of the novel metallopeptidase Mop112 and saccharolysin for the complete degradation of proteins residing in different subcompartments of mitochondria. J Biol Chem 280(20):20132-9 {{SGDpaper|S000081142}} PMID 15772085</ref><ref name='S000057643'>Hrycyna CA and Clarke S (1993) Purification and characterization of a novel metalloendopeptidase from Saccharomyces cerevisiae. Biochemistry 32(42):11293-301 {{SGDpaper|S000057643}} PMID 8218194</ref><ref name='S000055068'>Buchler M, et al. (1994) Proteinase yscD (oligopeptidase yscD). Structure, function and relationship of the yeast enzyme with mammalian thimet oligopeptidase (metalloendopeptidase, EP 24.15). Eur J Biochem 219(1-2):627-39
+'''Description of YCL057W:''' Zinc metalloendopeptidase, found in the cytoplasm and intermembrane space of mitochondria; with Cym1p, involved in degradation of mitochondrial proteins and of presequence peptides cleaved from imported proteins<ref name='S000081142'>Kambacheld M, et al. (2005) Role of the novel metallopeptidase Mop112 and saccharolysin for the complete degradation of proteins residing in different subcompartments of mitochondria. J Biol Chem 280(20):20132-9 {{SGDpaper|S000081142}} PMID 15772085</ref><ref name='S000057643'>Hrycyna CA and Clarke S (1993) Purification and characterization of a novel metalloendopeptidase from Saccharomyces cerevisiae. Biochemistry 32(42):11293-301 {{SGDpaper|S000057643}} PMID 8218194</ref><ref name='S000055068'>Buchler M, et al. (1994) Proteinase yscD (oligopeptidase yscD). Structure, function and relationship of the yeast enzyme with mammalian thimet oligopeptidase (metalloendopeptidase, EP 24.15). Eur J Biochem 219(1-2):627-39
   {{SGDpaper|S000055068}} PMID 8307027</ref>
 <br>
@@ Line 37: / Line 39: @@
 J Biol Chem 278(5):3265-74</ref>
 -->
 <protect>

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 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
 |nowrap| Chr III:24768..26906
 |}
 <br>
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 __TOC__
 ==Community Commentary==
 {{CommentaryHelp}}
 ==References==
 <!-- REFERENCES ARE AUTOMATICALLY GENERATED.  PLEASE DON'T EDIT THIS SECTION-->
 {{RefHelp}}