Difference between revisions of "YLR449W"
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| − | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl? | + | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000004441 YLR449W] |
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''FPR4 '' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''FPR4 '' | ||
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | ||
|nowrap| Chr XII:1030830..1032008 | |nowrap| Chr XII:1030830..1032008 | ||
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| + | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID''' || S000004441 | ||
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| − | '''Description of | + | '''Description of YLR449W:''' Peptidyl-prolyl cis-trans isomerase (PPIase) (proline isomerase) localized to the nucleus; catalyzes isomerization of proline residues in histones H3 and H4, which affects lysine methylation of those histones<ref name='S000118781'>Nelson CJ, et al. (2006) Proline isomerization of histone h3 regulates lysine methylation and gene expression. Cell 126(5):905-16 {{SGDpaper|S000118781}} PMID 16959570</ref><ref name='S000061678'>Davey M, et al. (2000) The yeast peptidyl proline isomerases FPR3 and FPR4, in high copy numbers, suppress defects resulting from the absence of the E3 ubiquitin ligase TOM1. Mol Gen Genet 263(3):520-6 {{SGDpaper|S000061678}} PMID 10821187</ref><ref name='S000046250'>Dolinski K, et al. (1997) All cyclophilins and FK506 binding proteins are, individually and collectively, dispensable for viability in Saccharomyces cerevisiae. Proc Natl Acad Sci U S A 94(24):13093-8 |
{{SGDpaper|S000046250}} PMID 9371805</ref> | {{SGDpaper|S000046250}} PMID 9371805</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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Revision as of 07:46, 27 February 2007
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| Systematic name | YLR449W |
| Gene name | FPR4 |
| Aliases | |
| Feature type | ORF, Verified |
| Coordinates | Chr XII:1030830..1032008 |
| Primary SGDID | S000004441 |
Description of YLR449W: Peptidyl-prolyl cis-trans isomerase (PPIase) (proline isomerase) localized to the nucleus; catalyzes isomerization of proline residues in histones H3 and H4, which affects lysine methylation of those histones[1][2][3]
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References
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- ↑ Nelson CJ, et al. (2006) Proline isomerization of histone h3 regulates lysine methylation and gene expression. Cell 126(5):905-16 SGD PMID 16959570
- ↑ Davey M, et al. (2000) The yeast peptidyl proline isomerases FPR3 and FPR4, in high copy numbers, suppress defects resulting from the absence of the E3 ubiquitin ligase TOM1. Mol Gen Genet 263(3):520-6 SGD PMID 10821187
- ↑ Dolinski K, et al. (1997) All cyclophilins and FK506 binding proteins are, individually and collectively, dispensable for viability in Saccharomyces cerevisiae. Proc Natl Acad Sci U S A 94(24):13093-8 SGD PMID 9371805
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