YDR212W - 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=S000002620 YDR212W]
+|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000002620 YDR212W]
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''         ||''TCP1 ''

@@ Line 13: / Line 13: @@
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
-|nowrap| Chr IV:887230..888909
+|nowrap| Chr IV:887232..888911
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''           || S000002620

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YDR212W:''' Alpha subunit of chaperonin-containing T-complex, which mediates protein folding in the cytosol; involved in actin cytoskeleton maintenance; overexpression in neurons suppresses formation of pathogenic conformations of huntingtin protein<ref name='S000042926'>Ursic D and Culbertson MR (1991) The yeast homolog to mouse Tcp-1 affects microtubule-mediated processes. Mol Cell Biol 11(5):2629-40 {{SGDpaper|S000042926}} PMID 1901944</ref><ref name='S000043581'>Ursic D, et al. (1994) The essential yeast Tcp1 protein affects actin and microtubules. Mol Biol Cell 5(10):1065-80 {{SGDpaper|S000043581}} PMID 7865875</ref><ref name='S000061049'>Siegers K, et al. (1999) Compartmentation of protein folding in vivo: sequestration of non-native polypeptide by the chaperonin-GimC system. EMBO J 18(1):75-84 {{SGDpaper|S000061049}} PMID 9878052</ref><ref name='S000118957'>Tam S, et al. (2006) The chaperonin TRiC controls polyglutamine aggregation and toxicity through subunit-specific interactions. Nat Cell Biol 8(10):1155-62 {{SGDpaper|S000118957}} PMID 16980959</ref><ref name='S000075049'>Siegers K, et al. (2003) TRiC/CCT cooperates with different upstream chaperones in the folding of distinct protein classes. EMBO J 22(19):5230-40
+'''Description of YDR212W:''' Alpha subunit of chaperonin-containing T-complex, which mediates protein folding in the cytosol; involved in actin cytoskeleton maintenance; overexpression in neurons suppresses formation of pathogenic conformations of huntingtin protein<ref name='S000061049'>Siegers K, et al. (1999) Compartmentation of protein folding in vivo: sequestration of non-native polypeptide by the chaperonin-GimC system. EMBO J 18(1):75-84 {{SGDpaper|S000061049}} PMID 9878052</ref><ref name='S000075049'>Siegers K, et al. (2003) TRiC/CCT cooperates with different upstream chaperones in the folding of distinct protein classes. EMBO J 22(19):5230-40 {{SGDpaper|S000075049}} PMID 14517260</ref><ref name='S000118957'>Tam S, et al. (2006) The chaperonin TRiC controls polyglutamine aggregation and toxicity through subunit-specific interactions. Nat Cell Biol 8(10):1155-62 {{SGDpaper|S000118957}} PMID 16980959</ref><ref name='S000042926'>Ursic D and Culbertson MR (1991) The yeast homolog to mouse Tcp-1 affects microtubule-mediated processes. Mol Cell Biol 11(5):2629-40 {{SGDpaper|S000042926}} PMID 1901944</ref><ref name='S000043581'>Ursic D, et al. (1994) The essential yeast Tcp1 protein affects actin and microtubules. Mol Biol Cell 5(10):1065-80
-  {{SGDpaper|S000075049}} PMID 14517260</ref>
+  {{SGDpaper|S000043581}} PMID 7865875</ref>
 <br>
 <br>

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YDR212W:''' Alpha subunit of chaperonin-containing T-complex, which mediates protein folding in the cytosol; involved in actin cytoskeleton maintenance; overexpression in neurons suppresses formation of pathogenic conformations of huntingtin protein<ref name='S000118957'>Tam S, et al. (2006) The chaperonin TRiC controls polyglutamine aggregation and toxicity through subunit-specific interactions. Nat Cell Biol 8(10):1155-62 {{SGDpaper|S000118957}} PMID 16980959</ref><ref name='S000075049'>Siegers K, et al. (2003) TRiC/CCT cooperates with different upstream chaperones in the folding of distinct protein classes. EMBO J 22(19):5230-40 {{SGDpaper|S000075049}} PMID 14517260</ref><ref name='S000061049'>Siegers K, et al. (1999) Compartmentation of protein folding in vivo: sequestration of non-native polypeptide by the chaperonin-GimC system. EMBO J 18(1):75-84 {{SGDpaper|S000061049}} PMID 9878052</ref><ref name='S000043581'>Ursic D, et al. (1994) The essential yeast Tcp1 protein affects actin and microtubules. Mol Biol Cell 5(10):1065-80 {{SGDpaper|S000043581}} PMID 7865875</ref><ref name='S000042926'>Ursic D and Culbertson MR (1991) The yeast homolog to mouse Tcp-1 affects microtubule-mediated processes. Mol Cell Biol 11(5):2629-40
+'''Description of YDR212W:''' Alpha subunit of chaperonin-containing T-complex, which mediates protein folding in the cytosol; involved in actin cytoskeleton maintenance; overexpression in neurons suppresses formation of pathogenic conformations of huntingtin protein<ref name='S000042926'>Ursic D and Culbertson MR (1991) The yeast homolog to mouse Tcp-1 affects microtubule-mediated processes. Mol Cell Biol 11(5):2629-40 {{SGDpaper|S000042926}} PMID 1901944</ref><ref name='S000043581'>Ursic D, et al. (1994) The essential yeast Tcp1 protein affects actin and microtubules. Mol Biol Cell 5(10):1065-80 {{SGDpaper|S000043581}} PMID 7865875</ref><ref name='S000061049'>Siegers K, et al. (1999) Compartmentation of protein folding in vivo: sequestration of non-native polypeptide by the chaperonin-GimC system. EMBO J 18(1):75-84 {{SGDpaper|S000061049}} PMID 9878052</ref><ref name='S000118957'>Tam S, et al. (2006) The chaperonin TRiC controls polyglutamine aggregation and toxicity through subunit-specific interactions. Nat Cell Biol 8(10):1155-62 {{SGDpaper|S000118957}} PMID 16980959</ref><ref name='S000075049'>Siegers K, et al. (2003) TRiC/CCT cooperates with different upstream chaperones in the folding of distinct protein classes. EMBO J 22(19):5230-40
-  {{SGDpaper|S000042926}} PMID 1901944</ref>
+  {{SGDpaper|S000075049}} PMID 14517260</ref>
 <br>
 <br>

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YDR212W:''' Alpha subunit of chaperonin-containing T-complex, which mediates protein folding in the cytosol; involved in maintenance of actin cytoskeleton; homolog to Drosophila melanogaster and mouse tailless complex polypeptide<ref name='S000075049'>Siegers K, et al. (2003) TRiC/CCT cooperates with different upstream chaperones in the folding of distinct protein classes. EMBO J 22(19):5230-40 {{SGDpaper|S000075049}} PMID 14517260</ref><ref name='S000061049'>Siegers K, et al. (1999) Compartmentation of protein folding in vivo: sequestration of non-native polypeptide by the chaperonin-GimC system. EMBO J 18(1):75-84 {{SGDpaper|S000061049}} PMID 9878052</ref><ref name='S000043581'>Ursic D, et al. (1994) The essential yeast Tcp1 protein affects actin and microtubules. Mol Biol Cell 5(10):1065-80 {{SGDpaper|S000043581}} PMID 7865875</ref><ref name='S000042926'>Ursic D and Culbertson MR (1991) The yeast homolog to mouse Tcp-1 affects microtubule-mediated processes. Mol Cell Biol 11(5):2629-40
+'''Description of YDR212W:''' Alpha subunit of chaperonin-containing T-complex, which mediates protein folding in the cytosol; involved in actin cytoskeleton maintenance; overexpression in neurons suppresses formation of pathogenic conformations of huntingtin protein<ref name='S000118957'>Tam S, et al. (2006) The chaperonin TRiC controls polyglutamine aggregation and toxicity through subunit-specific interactions. Nat Cell Biol 8(10):1155-62 {{SGDpaper|S000118957}} PMID 16980959</ref><ref name='S000075049'>Siegers K, et al. (2003) TRiC/CCT cooperates with different upstream chaperones in the folding of distinct protein classes. EMBO J 22(19):5230-40 {{SGDpaper|S000075049}} PMID 14517260</ref><ref name='S000061049'>Siegers K, et al. (1999) Compartmentation of protein folding in vivo: sequestration of non-native polypeptide by the chaperonin-GimC system. EMBO J 18(1):75-84 {{SGDpaper|S000061049}} PMID 9878052</ref><ref name='S000043581'>Ursic D, et al. (1994) The essential yeast Tcp1 protein affects actin and microtubules. Mol Biol Cell 5(10):1065-80 {{SGDpaper|S000043581}} PMID 7865875</ref><ref name='S000042926'>Ursic D and Culbertson MR (1991) The yeast homolog to mouse Tcp-1 affects microtubule-mediated processes. Mol Cell Biol 11(5):2629-40
   {{SGDpaper|S000042926}} PMID 1901944</ref>
 <br>

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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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