Difference between revisions of "YBL091C"

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'''Description of YBL091C:''' Methionine aminopeptidase, catalyzes the cotranslational removal of N-terminal methionine from nascent polypeptides; function is partially redundant with that of Map1p<ref name='S000080260'>Vetro JA, et al. (2005) Evidence of a dominant negative mutant of yeast methionine aminopeptidase type 2 in Saccharomyces cerevisiae. J Cell Biochem 94(4):656-68 {{SGDpaper|S000080260}} PMID 15547949</ref><ref name='S000047004'>Li X and Chang YH (1995) Amino-terminal protein processing in Saccharomyces cerevisiae is an essential function that requires two distinct methionine aminopeptidases. Proc Natl Acad Sci U S A 92(26):12357-61
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'''Description of YBL091C:''' Methionine aminopeptidase, catalyzes the cotranslational removal of N-terminal methionine from nascent polypeptides; function is partially redundant with that of Map1p<ref name='S000047004'>Li X and Chang YH (1995) Amino-terminal protein processing in Saccharomyces cerevisiae is an essential function that requires two distinct methionine aminopeptidases. Proc Natl Acad Sci U S A 92(26):12357-61 {{SGDpaper|S000047004}} PMID 8618900</ref><ref name='S000080260'>Vetro JA, et al. (2005) Evidence of a dominant negative mutant of yeast methionine aminopeptidase type 2 in Saccharomyces cerevisiae. J Cell Biochem 94(4):656-68
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  {{SGDpaper|S000080260}} PMID 15547949</ref>
 
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Revision as of 13:05, 31 March 2009

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Systematic name YBL091C
Gene name MAP2
Aliases
Feature type ORF, Verified
Coordinates Chr II:48625..47360
Primary SGDID S000000187


Description of YBL091C: Methionine aminopeptidase, catalyzes the cotranslational removal of N-terminal methionine from nascent polypeptides; function is partially redundant with that of Map1p[1][2]




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References

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  1. Li X and Chang YH (1995) Amino-terminal protein processing in Saccharomyces cerevisiae is an essential function that requires two distinct methionine aminopeptidases. Proc Natl Acad Sci U S A 92(26):12357-61 SGD PMID 8618900
  2. Vetro JA, et al. (2005) Evidence of a dominant negative mutant of yeast methionine aminopeptidase type 2 in Saccharomyces cerevisiae. J Cell Biochem 94(4):656-68 SGD PMID 15547949

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