Difference between revisions of "YNL231C"

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{|{{Prettytable}} align = 'right' width = '200px'
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?locus=YNL231C YNL231C]  
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000005175 YNL231C]  
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''PDR16 ''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''PDR16 ''
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
|nowrap| Chr XIV:217043..215988
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|nowrap| Chr XIV:217042..215987
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''          || S000005175
 
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'''Description of {{PAGENAME}}:''' Phosphatidylinositol transfer protein (PITP) controlled by the multiple drug resistance regulator Pdr1p, localizes to lipid particles and microsomes, controls levels of various lipids, may regulate lipid synthesis, homologous to Pdr17p<ref name='S000073885'>Schnabl M, et al. (2003) Subcellular localization of yeast Sec14 homologues and their involvement in regulation of phospholipid turnover. Eur J Biochem 270(15):3133-45 {{SGDpaper|S000073885}} PMID 12869188</ref><ref name='S000044730'>van den Hazel HB, et al. (1999) PDR16 and PDR17, two homologous genes of Saccharomyces cerevisiae, affect lipid biosynthesis and resistance to multiple drugs. J Biol Chem 274(4):1934-41 {{SGDpaper|S000044730}} PMID 9890948</ref><ref name='S000043659'>Li X, et al. (2000) Identification of a novel family of nonclassic yeast phosphatidylinositol transfer proteins whose function modulates phospholipase D activity and Sec14p-independent cell growth. Mol Biol Cell 11(6):1989-2005
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'''Description of YNL231C:''' Phosphatidylinositol transfer protein (PITP) controlled by the multiple drug resistance regulator Pdr1p, localizes to lipid particles and microsomes, controls levels of various lipids, may regulate lipid synthesis, homologous to Pdr17p<ref name='S000043659'>Li X, et al. (2000) Identification of a novel family of nonclassic yeast phosphatidylinositol transfer proteins whose function modulates phospholipase D activity and Sec14p-independent cell growth. Mol Biol Cell 11(6):1989-2005 {{SGDpaper|S000043659}} PMID 10848624</ref><ref name='S000073885'>Schnabl M, et al. (2003) Subcellular localization of yeast Sec14 homologues and their involvement in regulation of phospholipid turnover. Eur J Biochem 270(15):3133-45 {{SGDpaper|S000073885}} PMID 12869188</ref><ref name='S000044730'>van den Hazel HB, et al. (1999) PDR16 and PDR17, two homologous genes of Saccharomyces cerevisiae, affect lipid biosynthesis and resistance to multiple drugs. J Biol Chem 274(4):1934-41
{{SGDpaper|S000043659}} PMID 10848624</ref>
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{{SGDpaper|S000044730}} PMID 9890948</ref>
 
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J Biol Chem 278(5):3265-74</ref>
 
J Biol Chem 278(5):3265-74</ref>
 
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Latest revision as of 07:45, 23 January 2012

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Systematic name YNL231C
Gene name PDR16
Aliases SFH3
Feature type ORF, Verified
Coordinates Chr XIV:217042..215987
Primary SGDID S000005175


Description of YNL231C: Phosphatidylinositol transfer protein (PITP) controlled by the multiple drug resistance regulator Pdr1p, localizes to lipid particles and microsomes, controls levels of various lipids, may regulate lipid synthesis, homologous to Pdr17p[1][2][3]




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References

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  1. Li X, et al. (2000) Identification of a novel family of nonclassic yeast phosphatidylinositol transfer proteins whose function modulates phospholipase D activity and Sec14p-independent cell growth. Mol Biol Cell 11(6):1989-2005 SGD PMID 10848624
  2. Schnabl M, et al. (2003) Subcellular localization of yeast Sec14 homologues and their involvement in regulation of phospholipid turnover. Eur J Biochem 270(15):3133-45 SGD PMID 12869188
  3. van den Hazel HB, et al. (1999) PDR16 and PDR17, two homologous genes of Saccharomyces cerevisiae, affect lipid biosynthesis and resistance to multiple drugs. J Biol Chem 274(4):1934-41 SGD PMID 9890948

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