Difference between revisions of "YCL057W"

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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?locus=YCL057W YCL057W]  
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000000562 YCL057W]  
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''PRD1 ''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''PRD1 ''
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
 
|nowrap| Chr III:24768..26906
 
|nowrap| Chr III:24768..26906
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''          || S000000562
 
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'''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
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'''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>
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  {{SGDpaper|S000081142}} PMID 15772085</ref>
 
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J Biol Chem 278(5):3265-74</ref>
 
J Biol Chem 278(5):3265-74</ref>
 
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Latest revision as of 06:45, 23 January 2012

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Systematic name YCL057W
Gene name PRD1
Aliases
Feature type ORF, Verified
Coordinates Chr III:24768..26906
Primary SGDID S000000562


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[1][2][3]




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References

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  1. 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 SGD PMID 8307027
  2. Hrycyna CA and Clarke S (1993) Purification and characterization of a novel metalloendopeptidase from Saccharomyces cerevisiae. Biochemistry 32(42):11293-301 SGD PMID 8218194
  3. 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 SGD PMID 15772085

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