Difference between revisions of "YGL167C"
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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=S000003135 YGL167C] |
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''PMR1 '' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''PMR1 '' | ||
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | ||
| − | |nowrap| Chr VII: | + | |nowrap| Chr VII:190468..187616 |
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID''' || S000003135 | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID''' || S000003135 | ||
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| − | '''Description of YGL167C:''' High affinity Ca2+/Mn2+ P-type ATPase required for Ca2+ and Mn2+ transport into Golgi; involved in Ca2+ dependent protein sorting and processing; mutations in human homolog ATP2C1 cause acantholytic skin condition Hailey-Hailey disease | + | '''Description of YGL167C:''' High affinity Ca2+/Mn2+ P-type ATPase required for Ca2+ and Mn2+ transport into Golgi; involved in Ca2+ dependent protein sorting and processing; mutations in human homolog ATP2C1 cause acantholytic skin condition Hailey-Hailey disease<ref name='S000074937'>Kellermayer R, et al. (2003) Extracellular Ca(2+) sensing contributes to excess Ca(2+) accumulation and vacuolar fragmentation in a pmr1Delta mutant of S. cerevisiae. J Cell Sci 116(Pt 8):1637-46 {{SGDpaper|S000074937}} PMID 12640047</ref><ref name='S000074316'>Mandal D, et al. (2003) Packing interactions between transmembrane helices alter ion selectivity of the yeast Golgi Ca2+/Mn2+-ATPase PMR1. J Biol Chem 278(37):35292-8 {{SGDpaper|S000074316}} PMID 12824173</ref><ref name='S000080071'>Marie Mauro T (2004) Yeast researchers consider Hailey-Hailey disease. J Invest Dermatol 123(6):xxii-xxiii {{SGDpaper|S000080071}} PMID 15610504</ref><ref name='S000073696'>Vashist S, et al. (2002) Two distinctly localized p-type ATPases collaborate to maintain organelle homeostasis required for glycoprotein processing and quality control. Mol Biol Cell 13(11):3955-66 |
{{SGDpaper|S000073696}} PMID 12429838</ref> | {{SGDpaper|S000073696}} PMID 12429838</ref> | ||
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Latest revision as of 07:45, 23 January 2012
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| Systematic name | YGL167C |
| Gene name | PMR1 |
| Aliases | BSD1, LDB1, SSC1 |
| Feature type | ORF, Verified |
| Coordinates | Chr VII:190468..187616 |
| Primary SGDID | S000003135 |
Description of YGL167C: High affinity Ca2+/Mn2+ P-type ATPase required for Ca2+ and Mn2+ transport into Golgi; involved in Ca2+ dependent protein sorting and processing; mutations in human homolog ATP2C1 cause acantholytic skin condition Hailey-Hailey disease[1][2][3][4]
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References
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- ↑ Kellermayer R, et al. (2003) Extracellular Ca(2+) sensing contributes to excess Ca(2+) accumulation and vacuolar fragmentation in a pmr1Delta mutant of S. cerevisiae. J Cell Sci 116(Pt 8):1637-46 SGD PMID 12640047
- ↑ Mandal D, et al. (2003) Packing interactions between transmembrane helices alter ion selectivity of the yeast Golgi Ca2+/Mn2+-ATPase PMR1. J Biol Chem 278(37):35292-8 SGD PMID 12824173
- ↑ Marie Mauro T (2004) Yeast researchers consider Hailey-Hailey disease. J Invest Dermatol 123(6):xxii-xxiii SGD PMID 15610504
- ↑ Vashist S, et al. (2002) Two distinctly localized p-type ATPases collaborate to maintain organelle homeostasis required for glycoprotein processing and quality control. Mol Biol Cell 13(11):3955-66 SGD PMID 12429838
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