Difference between revisions of "YKL157W"
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− | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http:// | + | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000001640 YKL157W] |
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''APE2 '' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''APE2 '' | ||
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− | '''Description of YKL157W:''' Aminopeptidase yscII; may have a role in obtaining leucine from dipeptide substrates; | + | '''Description of YKL157W:''' Aminopeptidase yscII; may have a role in obtaining leucine from dipeptide substrates; APE2 has a paralog, AAP1, that arose from the whole genome duplication<ref name='S000113653'>Byrne KP and Wolfe KH (2005) The Yeast Gene Order Browser: combining curated homology and syntenic context reveals gene fate in polyploid species. Genome Res 15(10):1456-61 {{SGDpaper|S000113653}} PMID 16169922</ref><ref name='S000042737'>Davis CA, et al. (2000) Test of intron predictions reveals novel splice sites, alternatively spliced mRNAs and new introns in meiotically regulated genes of yeast. Nucleic Acids Res 28(8):1700-6 {{SGDpaper|S000042737}} PMID 10734188</ref><ref name='S000053939'>Garcia-Alvarez N, et al. (1991) Molecular cloning of soluble aminopeptidases from Saccharomyces cerevisiae. Sequence analysis of aminopeptidase yscII, a putative zinc-metallopeptidase. Eur J Biochem 202(3):993-1002 {{SGDpaper|S000053939}} PMID 1765107</ref><ref name='S000051861'>Hirsch HH, et al. (1988) Aminopeptidase yscII of yeast. Isolation of mutants and their biochemical and genetic analysis. Eur J Biochem 173(3):589-98 |
{{SGDpaper|S000051861}} PMID 3286257</ref> | {{SGDpaper|S000051861}} PMID 3286257</ref> | ||
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Latest revision as of 13:05, 12 October 2012
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Systematic name | YKL157W |
Gene name | APE2 |
Aliases | LAP1, YKL158W |
Feature type | ORF, Verified |
Coordinates | Chr XI:154991..158232 |
Primary SGDID | S000001640 |
Description of YKL157W: Aminopeptidase yscII; may have a role in obtaining leucine from dipeptide substrates; APE2 has a paralog, AAP1, that arose from the whole genome duplication[1][2][3][4]
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Protein Details
Protein Localization
Protein identified in a purified mitochondrial extract. [5] [6]
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References
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- ↑ Byrne KP and Wolfe KH (2005) The Yeast Gene Order Browser: combining curated homology and syntenic context reveals gene fate in polyploid species. Genome Res 15(10):1456-61 SGD PMID 16169922
- ↑ Davis CA, et al. (2000) Test of intron predictions reveals novel splice sites, alternatively spliced mRNAs and new introns in meiotically regulated genes of yeast. Nucleic Acids Res 28(8):1700-6 SGD PMID 10734188
- ↑ Garcia-Alvarez N, et al. (1991) Molecular cloning of soluble aminopeptidases from Saccharomyces cerevisiae. Sequence analysis of aminopeptidase yscII, a putative zinc-metallopeptidase. Eur J Biochem 202(3):993-1002 SGD PMID 1765107
- ↑ Hirsch HH, et al. (1988) Aminopeptidase yscII of yeast. Isolation of mutants and their biochemical and genetic analysis. Eur J Biochem 173(3):589-98 SGD PMID 3286257
- ↑ Ohlmeier S, et al. (2004) The yeast mitochondrial proteome, a study of fermentative and respiratory growth. J Biol Chem 279(6):3956-79 SGD PMID 14597615
- ↑ submitted by Steffen Ohlmeier on 2004-04-08
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