YMR322C - Revision history

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 {|{{Prettytable}} align = 'right' width = '200px'
 |-
-|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000004941 YMR322C]
+|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000004941 YMR322C]
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''         ||''SNO4 ''

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 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
-|nowrap| Chr XIII:919077..918364
+|nowrap| Chr XIII:919079..918366
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''           || S000004941

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YMR322C:''' Possible chaperone and cysteine protease, similar to bacterial Hsp31 and yeast Hsp31p, Hsp32p, and Hsp33p; DJ-1/ThiJ/PfpI superfamily member; predicted involvement in pyridoxine metabolism; induced by mild heat stress and copper deprivation<ref name='S000114240'>Sakaki K, et al. (2003) Response of genes associated with mitochondrial function to mild heat stress in yeast Saccharomyces cerevisiae. J Biochem 134(3):373-84 {{SGDpaper|S000114240}} PMID 14561723</ref><ref name='S000081637'>van Bakel H, et al. (2005) Gene expression profiling and phenotype analyses of S. cerevisiae in response to changing copper reveals six genes with new roles in copper and iron metabolism. Physiol Genomics 22(3):356-67 {{SGDpaper|S000081637}} PMID 15886332</ref><ref name='S000074191'>Samanta MP and Liang S (2003) Predicting protein functions from redundancies in large-scale protein interaction networks. Proc Natl Acad Sci U S A 100(22):12579-83 {{SGDpaper|S000074191}} PMID 14566057</ref><ref name='S000074850'>Wilson MA, et al. (2004) The 1.8-A resolution crystal structure of YDR533Cp from Saccharomyces cerevisiae: A member of the DJ-1/ThiJ/PfpI superfamily. Proc Natl Acad Sci U S A 101(6):1531-6
+'''Description of YMR322C:''' Possible chaperone and cysteine protease, similar to bacterial Hsp31 and yeast Hsp31p, Hsp32p, and Hsp33p; DJ-1/ThiJ/PfpI superfamily member; predicted involvement in pyridoxine metabolism; induced by mild heat stress and copper deprivation<ref name='S000114240'>Sakaki K, et al. (2003) Response of genes associated with mitochondrial function to mild heat stress in yeast Saccharomyces cerevisiae. J Biochem 134(3):373-84 {{SGDpaper|S000114240}} PMID 14561723</ref><ref name='S000074191'>Samanta MP and Liang S (2003) Predicting protein functions from redundancies in large-scale protein interaction networks. Proc Natl Acad Sci U S A 100(22):12579-83 {{SGDpaper|S000074191}} PMID 14566057</ref><ref name='S000074850'>Wilson MA, et al. (2004) The 1.8-A resolution crystal structure of YDR533Cp from Saccharomyces cerevisiae: A member of the DJ-1/ThiJ/PfpI superfamily. Proc Natl Acad Sci U S A 101(6):1531-6 {{SGDpaper|S000074850}} PMID 14745011</ref><ref name='S000081637'>van Bakel H, et al. (2005) Gene expression profiling and phenotype analyses of S. cerevisiae in response to changing copper reveals six genes with new roles in copper and iron metabolism. Physiol Genomics 22(3):356-67
-  {{SGDpaper|S000074850}} PMID 14745011</ref>
+  {{SGDpaper|S000081637}} PMID 15886332</ref>
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 <br>

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YMR322C:''' Possible chaperone and cysteine protease, similar to bacterial Hsp31 and yeast Hsp31p, Hsp32p, and Hsp33p; DJ-1/ThiJ/PfpI superfamily member; predicted involvement in pyridoxine metabolism; induced by mild heat stress and copper deprivation<ref name='S000114240'>Sakaki K, et al. (2003) Response of genes associated with mitochondrial function to mild heat stress in yeast Saccharomyces cerevisiae. J Biochem 134(3):373-84 {{SGDpaper|S000114240}} PMID 14561723</ref><ref name='S000081637'>van Bakel H, et al. (2005) Gene expression profiling and phenotype analyses of S. cerevisiae in response to changing copper reveals six genes with new roles in copper and iron metabolism. Physiol Genomics 22(3):356-67 {{SGDpaper|S000081637}} PMID 15886332</ref><ref name='S000074850'>Wilson MA, et al. (2004) The 1.8-A resolution crystal structure of YDR533Cp from Saccharomyces cerevisiae: A member of the DJ-1/ThiJ/PfpI superfamily. Proc Natl Acad Sci U S A 101(6):1531-6 {{SGDpaper|S000074850}} PMID 14745011</ref><ref name='S000074191'>Samanta MP and Liang S (2003) Predicting protein functions from redundancies in large-scale protein interaction networks. Proc Natl Acad Sci U S A 100(22):12579-83
+'''Description of YMR322C:''' Possible chaperone and cysteine protease, similar to bacterial Hsp31 and yeast Hsp31p, Hsp32p, and Hsp33p; DJ-1/ThiJ/PfpI superfamily member; predicted involvement in pyridoxine metabolism; induced by mild heat stress and copper deprivation<ref name='S000114240'>Sakaki K, et al. (2003) Response of genes associated with mitochondrial function to mild heat stress in yeast Saccharomyces cerevisiae. J Biochem 134(3):373-84 {{SGDpaper|S000114240}} PMID 14561723</ref><ref name='S000081637'>van Bakel H, et al. (2005) Gene expression profiling and phenotype analyses of S. cerevisiae in response to changing copper reveals six genes with new roles in copper and iron metabolism. Physiol Genomics 22(3):356-67 {{SGDpaper|S000081637}} PMID 15886332</ref><ref name='S000074191'>Samanta MP and Liang S (2003) Predicting protein functions from redundancies in large-scale protein interaction networks. Proc Natl Acad Sci U S A 100(22):12579-83 {{SGDpaper|S000074191}} PMID 14566057</ref><ref name='S000074850'>Wilson MA, et al. (2004) The 1.8-A resolution crystal structure of YDR533Cp from Saccharomyces cerevisiae: A member of the DJ-1/ThiJ/PfpI superfamily. Proc Natl Acad Sci U S A 101(6):1531-6
- {{SGDpaper|S000074191}} PMID 14566057</ref>
+ {{SGDpaper|S000074850}} PMID 14745011</ref>
 <br>
 <br>

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YMR322C:''' Possible chaperone and cysteine protease with similarity to E. coli Hsp31 and S. cerevisiae Hsp31p, Hsp32p, and Hsp33p; member of the DJ-1/ThiJ/PfpI superfamily; may have a role in pyridoxine metabolism<ref name='S000074850'>Wilson MA, et al. (2004) The 1.8-A resolution crystal structure of YDR533Cp from Saccharomyces cerevisiae: A member of the DJ-1/ThiJ/PfpI superfamily. Proc Natl Acad Sci U S A 101(6):1531-6 {{SGDpaper|S000074850}} PMID 14745011</ref><ref name='S000074191'>Samanta MP and Liang S (2003) Predicting protein functions from redundancies in large-scale protein interaction networks. Proc Natl Acad Sci U S A 100(22):12579-83
+'''Description of YMR322C:''' Possible chaperone and cysteine protease, similar to bacterial Hsp31 and yeast Hsp31p, Hsp32p, and Hsp33p; DJ-1/ThiJ/PfpI superfamily member; predicted involvement in pyridoxine metabolism; induced by mild heat stress and copper deprivation<ref name='S000114240'>Sakaki K, et al. (2003) Response of genes associated with mitochondrial function to mild heat stress in yeast Saccharomyces cerevisiae. J Biochem 134(3):373-84 {{SGDpaper|S000114240}} PMID 14561723</ref><ref name='S000081637'>van Bakel H, et al. (2005) Gene expression profiling and phenotype analyses of S. cerevisiae in response to changing copper reveals six genes with new roles in copper and iron metabolism. Physiol Genomics 22(3):356-67 {{SGDpaper|S000081637}} PMID 15886332</ref><ref name='S000074850'>Wilson MA, et al. (2004) The 1.8-A resolution crystal structure of YDR533Cp from Saccharomyces cerevisiae: A member of the DJ-1/ThiJ/PfpI superfamily. Proc Natl Acad Sci U S A 101(6):1531-6 {{SGDpaper|S000074850}} PMID 14745011</ref><ref name='S000074191'>Samanta MP and Liang S (2003) Predicting protein functions from redundancies in large-scale protein interaction networks. Proc Natl Acad Sci U S A 100(22):12579-83
   {{SGDpaper|S000074191}} PMID 14566057</ref>
 <br>

← Older revision		Revision as of 20:02, 21 February 2007
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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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 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
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