Difference between revisions of "YGL167C"

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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<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><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='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
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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<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
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  {{SGDpaper|S000073696}} PMID 12429838</ref>
 
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Revision as of 13:05, 25 February 2010

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Systematic name YGL167C
Gene name PMR1
Aliases BSD1, LDB1, SSC1
Feature type ORF, Verified
Coordinates Chr VII:190474..187622
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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  1. 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
  2. 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
  3. Marie Mauro T (2004) Yeast researchers consider Hailey-Hailey disease. J Invest Dermatol 123(6):xxii-xxiii SGD PMID 15610504
  4. 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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