Difference between revisions of "YOR124C"
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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=S000005650 YOR124C] |
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''UBP2 '' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''UBP2 '' | ||
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | ||
|nowrap| Chr XV:558643..554825 | |nowrap| Chr XV:558643..554825 | ||
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| + | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID''' || S000005650 | ||
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<br> | <br> | ||
| − | '''Description of | + | '''Description of YOR124C:''' Ubiquitin-specific protease that removes ubiquitin from ubiquitinated proteins, cleaves at the C terminus of ubiquitin fusions; capable of cleaving polyubiquitin and possesses isopeptidase activity<ref name='S000052610'>Layfield R, et al. (1999) Chemically synthesized ubiquitin extension proteins detect distinct catalytic capacities of deubiquitinating enzymes. Anal Biochem 274(1):40-9 {{SGDpaper|S000052610}} PMID 10527495</ref><ref name='S000051210'>Baker RT, et al. (1992) Ubiquitin-specific proteases of Saccharomyces cerevisiae. Cloning of UBP2 and UBP3, and functional analysis of the UBP gene family. J Biol Chem 267(32):23364-75 |
{{SGDpaper|S000051210}} PMID 1429680</ref> | {{SGDpaper|S000051210}} PMID 1429680</ref> | ||
<br> | <br> | ||
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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
Share your knowledge...Edit this entry! <protect>
| Systematic name | YOR124C |
| Gene name | UBP2 |
| Aliases | |
| Feature type | ORF, Verified |
| Coordinates | Chr XV:558643..554825 |
| Primary SGDID | S000005650 |
Description of YOR124C: Ubiquitin-specific protease that removes ubiquitin from ubiquitinated proteins, cleaves at the C terminus of ubiquitin fusions; capable of cleaving polyubiquitin and possesses isopeptidase activity[1][2]
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Contents
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References
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- ↑ Layfield R, et al. (1999) Chemically synthesized ubiquitin extension proteins detect distinct catalytic capacities of deubiquitinating enzymes. Anal Biochem 274(1):40-9 SGD PMID 10527495
- ↑ Baker RT, et al. (1992) Ubiquitin-specific proteases of Saccharomyces cerevisiae. Cloning of UBP2 and UBP3, and functional analysis of the UBP gene family. J Biol Chem 267(32):23364-75 SGD PMID 1429680
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