Difference between revisions of "YKR031C"
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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=S000001739 YKR031C] |
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''SPO14 '' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''SPO14 '' | ||
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | ||
| − | |nowrap| Chr XI: | + | |nowrap| Chr XI:506395..501344 |
|- | |- | ||
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID''' || S000001739 | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID''' || S000001739 | ||
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| − | '''Description of YKR031C:''' Phospholipase D | + | '''Description of YKR031C:''' Phospholipase D; catalyzes the hydrolysis of phosphatidylcholine, producing choline and phosphatidic acid; involved in Sec14p-independent secretion; required for meiosis and spore formation; differently regulated in secretion and meiosis; participates in transcription initiation and/or early elongation of specific genes; interacts with "foot domain" of RNA polymerase II; deletion results in abnormal CTD-Ser5 phosphorylation of RNA polymerase II at specific promoter regions<ref name='S000146910'>Garcia-Lopez MC, et al. (2011) The Conserved Foot Domain of RNA Pol II Associates with Proteins Involved in Transcriptional Initiation and/or Early Elongation. Genetics () {{SGDpaper|S000146910}} PMID 21954159</ref><ref name='S000055339'>Rudge SA, et al. (1998) Relocalization of phospholipase D activity mediates membrane formation during meiosis. J Cell Biol 140(1):81-90 {{SGDpaper|S000055339}} PMID 9425156</ref><ref name='S000069708'>Rudge SA, et al. (2002) Differential regulation of Saccharomyces cerevisiae phospholipase D in sporulation and Sec14-independent secretion. Genetics 160(4):1353-61 {{SGDpaper|S000069708}} PMID 11973292</ref><ref name='S000051159'>Sreenivas A, et al. (1998) A role for phospholipase D (Pld1p) in growth, secretion, and regulation of membrane lipid synthesis in yeast. J Biol Chem 273(27):16635-8 {{SGDpaper|S000051159}} PMID 9642212</ref><ref name='S000047187'>Xie Z, et al. (1998) Phospholipase D activity is required for suppression of yeast phosphatidylinositol transfer protein defects. Proc Natl Acad Sci U S A 95(21):12346-51 |
{{SGDpaper|S000047187}} PMID 9770489</ref> | {{SGDpaper|S000047187}} PMID 9770489</ref> | ||
<br> | <br> | ||
Latest revision as of 06:45, 23 January 2012
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| Systematic name | YKR031C |
| Gene name | SPO14 |
| Aliases | PLD1 |
| Feature type | ORF, Verified |
| Coordinates | Chr XI:506395..501344 |
| Primary SGDID | S000001739 |
Description of YKR031C: Phospholipase D; catalyzes the hydrolysis of phosphatidylcholine, producing choline and phosphatidic acid; involved in Sec14p-independent secretion; required for meiosis and spore formation; differently regulated in secretion and meiosis; participates in transcription initiation and/or early elongation of specific genes; interacts with "foot domain" of RNA polymerase II; deletion results in abnormal CTD-Ser5 phosphorylation of RNA polymerase II at specific promoter regions[1][2][3][4][5]
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References
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- ↑ Garcia-Lopez MC, et al. (2011) The Conserved Foot Domain of RNA Pol II Associates with Proteins Involved in Transcriptional Initiation and/or Early Elongation. Genetics () SGD PMID 21954159
- ↑ Rudge SA, et al. (1998) Relocalization of phospholipase D activity mediates membrane formation during meiosis. J Cell Biol 140(1):81-90 SGD PMID 9425156
- ↑ Rudge SA, et al. (2002) Differential regulation of Saccharomyces cerevisiae phospholipase D in sporulation and Sec14-independent secretion. Genetics 160(4):1353-61 SGD PMID 11973292
- ↑ Sreenivas A, et al. (1998) A role for phospholipase D (Pld1p) in growth, secretion, and regulation of membrane lipid synthesis in yeast. J Biol Chem 273(27):16635-8 SGD PMID 9642212
- ↑ Xie Z, et al. (1998) Phospholipase D activity is required for suppression of yeast phosphatidylinositol transfer protein defects. Proc Natl Acad Sci U S A 95(21):12346-51 SGD PMID 9770489
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