YNR047W - Revision history

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@@ Line 4: / Line 4: @@
 {|{{Prettytable}} align = 'right' width = '200px'
 |-
-|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000005330 YNR047W]
+|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000005330 YNR047W]
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''         ||''FPK1 ''

@@ Line 13: / Line 13: @@
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
-|nowrap| Chr XIV:708526..711207
+|nowrap| Chr XIV:708523..711204
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''           || S000005330

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YNR047W:''' Ser/Thr protein kinase that regulates the putative phospholipid translocases Lem3p-Dnf1p/Dnf2p; phosphorylates and inhibits upstream inhibitory kinase, Ypk1p; localizes to the cytoplasm, early endosome/TGN compartments, and plasma membrane<ref name='S000061243'>Burchett SA, et al. (2001) Identification of novel pheromone-response regulators through systematic overexpression of 120 protein kinases in yeast. J Biol Chem 276(28):26472-8 {{SGDpaper|S000061243}} PMID 11337509</ref><ref name='S000074306'>Ubersax JA, et al. (2003) Targets of the cyclin-dependent kinase Cdk1. Nature 425(6960):859-64 {{SGDpaper|S000074306}} PMID 14574415</ref><ref name='S000128228'>Nakano K, et al. (2008) Protein kinases Fpk1p and Fpk2p are novel regulators of phospholipid asymmetry. Mol Biol Cell 19(4):1783-97 {{SGDpaper|S000128228}} PMID 18199685</ref><ref name='S000132460'>Roelants FM, et al. (2010) A protein kinase network regulates the function of aminophospholipid flippases. Proc Natl Acad Sci U S A 107(1):34-9
+'''Description of YNR047W:''' Ser/Thr protein kinase that regulates the putative phospholipid translocases Lem3p-Dnf1p/Dnf2p; phosphorylates and inhibits upstream inhibitory kinase, Ypk1p; localizes to the cytoplasm, early endosome/TGN compartments, and plasma membrane<ref name='S000061243'>Burchett SA, et al. (2001) Identification of novel pheromone-response regulators through systematic overexpression of 120 protein kinases in yeast. J Biol Chem 276(28):26472-8 {{SGDpaper|S000061243}} PMID 11337509</ref><ref name='S000128228'>Nakano K, et al. (2008) Protein kinases Fpk1p and Fpk2p are novel regulators of phospholipid asymmetry. Mol Biol Cell 19(4):1783-97 {{SGDpaper|S000128228}} PMID 18199685</ref><ref name='S000132460'>Roelants FM, et al. (2010) A protein kinase network regulates the function of aminophospholipid flippases. Proc Natl Acad Sci U S A 107(1):34-9 {{SGDpaper|S000132460}} PMID 19966303</ref><ref name='S000074306'>Ubersax JA, et al. (2003) Targets of the cyclin-dependent kinase Cdk1. Nature 425(6960):859-64
-  {{SGDpaper|S000132460}} PMID 19966303</ref>
+  {{SGDpaper|S000074306}} PMID 14574415</ref>
 <br>
 <br>

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YNR047W:''' Ser/Thr protein kinase that regulates the putative phospholipid translocases Lem3p-Dnf1p/Dnf2p; phosphorylates and inhibits upstream inhibitory kinase, Ypk1p; localizes to the cytoplasm, early endosome/TGN compartments, and plasma membrane<ref name='S000061243'>Burchett SA, et al. (2001) Identification of novel pheromone-response regulators through systematic overexpression of 120 protein kinases in yeast. J Biol Chem 276(28):26472-8 {{SGDpaper|S000061243}} PMID 11337509</ref><ref name='S000074306'>Ubersax JA, et al. (2003) Targets of the cyclin-dependent kinase Cdk1. Nature 425(6960):859-64 {{SGDpaper|S000074306}} PMID 14574415</ref><ref name='S000128228'>Nakano K, et al. (2008) Protein kinases Fpk1p and Fpk2p are novel regulators of phospholipid asymmetry. Mol Biol Cell 19(4):1783-97 {{SGDpaper|S000128228}} PMID 18199685</ref><ref name='S000132460'>Roelants FM, et al. (2009) A protein kinase network regulates the function of aminophospholipid flippases. Proc Natl Acad Sci U S A ()
+'''Description of YNR047W:''' Ser/Thr protein kinase that regulates the putative phospholipid translocases Lem3p-Dnf1p/Dnf2p; phosphorylates and inhibits upstream inhibitory kinase, Ypk1p; localizes to the cytoplasm, early endosome/TGN compartments, and plasma membrane<ref name='S000061243'>Burchett SA, et al. (2001) Identification of novel pheromone-response regulators through systematic overexpression of 120 protein kinases in yeast. J Biol Chem 276(28):26472-8 {{SGDpaper|S000061243}} PMID 11337509</ref><ref name='S000074306'>Ubersax JA, et al. (2003) Targets of the cyclin-dependent kinase Cdk1. Nature 425(6960):859-64 {{SGDpaper|S000074306}} PMID 14574415</ref><ref name='S000128228'>Nakano K, et al. (2008) Protein kinases Fpk1p and Fpk2p are novel regulators of phospholipid asymmetry. Mol Biol Cell 19(4):1783-97 {{SGDpaper|S000128228}} PMID 18199685</ref><ref name='S000132460'>Roelants FM, et al. (2010) A protein kinase network regulates the function of aminophospholipid flippases. Proc Natl Acad Sci U S A 107(1):34-9
   {{SGDpaper|S000132460}} PMID 19966303</ref>
 <br>

@@ Line 13: / Line 13: @@
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
-|nowrap| Chr XIV:708525..711206
+|nowrap| Chr XIV:708526..711207
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''           || S000005330

@@ Line 6: / Line 6: @@
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000005330 YNR047W]
 |-
-|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''         ||'' ''
+|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''         ||''FPK1 ''
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Aliases'''           ||'' ''
 |-
-|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Feature type'''           || ORF, Uncharacterized[[Category:ORF]][[Category:ORF, Uncharacterized]]
+|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Feature type'''           || ORF, Verified[[Category:ORF]][[Category:ORF, Verified]]
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YNR047W:''' Putative protein kinase that, when overexpressed, interferes with pheromone-induced growth arrest; localizes to the cytoplasm; potential Cdc28p substrate<ref name='S000074306'>Ubersax JA, et al. (2003) Targets of the cyclin-dependent kinase Cdk1. Nature 425(6960):859-64 {{SGDpaper|S000074306}} PMID 14574415</ref><ref name='S000074185'>Huh WK, et al. (2003) Global analysis of protein localization in budding yeast. Nature 425(6959):686-91 {{SGDpaper|S000074185}} PMID 14562095</ref><ref name='S000061243'>Burchett SA, et al. (2001) Identification of novel pheromone-response regulators through systematic overexpression of 120 protein kinases in yeast. J Biol Chem 276(28):26472-8 {{SGDpaper|S000061243}} PMID 11337509</ref><ref name='S000058030'>Hunter T and Plowman GD (1997) The protein kinases of budding yeast: six score and more. Trends Biochem Sci 22(1):18-22
+'''Description of YNR047W:''' Protein kinase proposed to regulate the putative phospholipid translocases Lem3p-Dnf1p/Dnf2p; overexpression interferes with pheromone-induced growth arrest; localizes to the cytoplasm, early endosome/TGN compartments, and plasma membrane<ref name='S000128228'>Nakano K, et al. (2008) Protein kinases Fpk1p and Fpk2p are novel regulators of phospholipid asymmetry. Mol Biol Cell 19(4):1783-97 {{SGDpaper|S000128228}} PMID 18199685</ref><ref name='S000074306'>Ubersax JA, et al. (2003) Targets of the cyclin-dependent kinase Cdk1. Nature 425(6960):859-64 {{SGDpaper|S000074306}} PMID 14574415</ref><ref name='S000061243'>Burchett SA, et al. (2001) Identification of novel pheromone-response regulators through systematic overexpression of 120 protein kinases in yeast. J Biol Chem 276(28):26472-8
- {{SGDpaper|S000058030}} PMID 9020587</ref>
+ {{SGDpaper|S000061243}} PMID 11337509</ref>
 <br>
 <br>

← Older revision		Revision as of 20:02, 21 February 2007
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		+	<!-- PLEASE ADD Community Commentary ABOVE THIS MESSAGE. See below for an example of community annotation -->
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		+	Specifically higher expression in carbon limited chemostat cultures versus carbon excess.
		+	<ref>Boer VM, et al. (2003) The genome-wide transcriptional responses of Saccharomyces cerevisiae grown on glucose in aerobic chemostat cultures limited for carbon, nitrogen, phosphorus, or sulfur.
		+	J Biol Chem 278(5):3265-74</ref>
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