Difference between revisions of "YHR028C"
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| − | '''Description of YHR028C:''' Dipeptidyl aminopeptidase, synthesized as a glycosylated precursor; localizes to the vacuolar membrane; similar to Ste13p<ref name=' | + | '''Description of YHR028C:''' Dipeptidyl aminopeptidase, synthesized as a glycosylated precursor; localizes to the vacuolar membrane; similar to Ste13p<ref name='S000056547'>Roberts CJ, et al. (1992) Membrane protein sorting in the yeast secretory pathway: evidence that the vacuole may be the default compartment. J Cell Biol 119(1):69-83 {{SGDpaper|S000056547}} PMID 1527174</ref><ref name='S000039425'>Roberts CJ, et al. (1989) Structure, biosynthesis, and localization of dipeptidyl aminopeptidase B, an integral membrane glycoprotein of the yeast vacuole. J Cell Biol 108(4):1363-73 |
| − | {{SGDpaper| | + | {{SGDpaper|S000039425}} PMID 2647766</ref> |
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Revision as of 14:05, 16 January 2009
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| Systematic name | YHR028C |
| Gene name | DAP2 |
| Aliases | DPP2 |
| Feature type | ORF, Verified |
| Coordinates | Chr VIII:167427..164971 |
| Primary SGDID | S000001070 |
Description of YHR028C: Dipeptidyl aminopeptidase, synthesized as a glycosylated precursor; localizes to the vacuolar membrane; similar to Ste13p[1][2]
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Contents
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References
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- ↑ Roberts CJ, et al. (1992) Membrane protein sorting in the yeast secretory pathway: evidence that the vacuole may be the default compartment. J Cell Biol 119(1):69-83 SGD PMID 1527174
- ↑ Roberts CJ, et al. (1989) Structure, biosynthesis, and localization of dipeptidyl aminopeptidase B, an integral membrane glycoprotein of the yeast vacuole. J Cell Biol 108(4):1363-73 SGD PMID 2647766
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