YMR276W - Revision history

SGDwikiBot: Automated import of articles

2012-01-23T14:45:38Z

Automated import of articles

SGDwikiBot: Automated import of articles

2011-02-03T21:05:34Z

Automated import of articles

SGDwikiBot: Automated import of articles

2010-02-25T21:05:28Z

Automated import of articles

SGDwikiBot: Automated import of articles

2009-03-31T21:05:32Z

Automated import of articles

SGDwikiBot: Automated import of articles

2007-02-27T15:46:15Z

Automated import of articles

SGDwikiBot: Automated import of articles

2007-02-21T20:02:23Z

Automated import of articles

SGDwikiBot: Automated import of articles

2007-01-30T15:18:06Z

Automated import of articles

SGDwikiBot: Automated import of articles

2007-01-23T15:20:41Z

Automated import of articles

New page

{{PageTop}}
{|{{Prettytable}} align = 'right' width = '200px'
|-
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?locus=YMR276W YMR276W]
|-
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''DSK2 ''
|-
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Aliases''' ||'' ''
|-
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Feature type''' || ORF, Verified[[Category:ORF]][[Category:ORF, Verified]]
|-
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
|nowrap| Chr XIII:818826..819947
|-
|colspan = '3'|{{Don'tEditThisBox}}
|}
 
'''Description of {{PAGENAME}}:''' Nuclear-enriched ubiquitin-like polyubiquitin-binding protein, required for spindle pole body (SPB) duplication and for transit through the G2/M phase of the cell cycle, involved in proteolysis, interacts with the proteasome<ref name='S000070040'>Saeki Y, et al. (2002) Ubiquitin-like proteins and Rpn10 play cooperative roles in ubiquitin-dependent proteolysis. Biochem Biophys Res Commun 293(3):986-92 {{SGDpaper|S000070040}} PMID 12051757</ref><ref name='S000069561'>Rao H and Sastry A (2002) Recognition of specific ubiquitin conjugates is important for the proteolytic functions of the ubiquitin-associated domain proteins Dsk2 and Rad23. J Biol Chem 277(14):11691-5 {{SGDpaper|S000069561}} PMID 11805121</ref><ref name='S000069044'>Funakoshi M, et al. (2002) Budding yeast Dsk2p is a polyubiquitin-binding protein that can interact with the proteasome. Proc Natl Acad Sci U S A 99(2):745-50 {{SGDpaper|S000069044}} PMID 11805328</ref><ref name='S000054506'>Kaye FJ, et al. (2000) A family of ubiquitin-like proteins binds the ATPase domain of Hsp70-like Stch. FEBS Lett 467(2-3):348-55 {{SGDpaper|S000054506}} PMID 10675567</ref><ref name='S000052146'>Khalfan W, et al. (2000) Functional interaction between the PKC1 pathway and CDC31 network of SPB duplication genes. Genetics 155(4):1543-59 {{SGDpaper|S000052146}} PMID 10924456</ref><ref name='S000042382'>Biggins S, et al. (1996) Yeast ubiquitin-like genes are involved in duplication of the microtubule organizing center. J Cell Biol 133(6):1331-46
{{SGDpaper|S000042382}} PMID 8682868</ref>
 
 
 
 

__TOC__
==Community Commentary==
{{CommentaryHelp}}

==References==

{{RefHelp}}

@@ Line 13: / Line 13: @@
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
-|nowrap| Chr XIII:818826..819947
+|nowrap| Chr XIII:818827..819948
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''           || S000004889

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YMR276W:''' Nuclear-enriched ubiquitin-like polyubiquitin-binding protein, required for spindle pole body (SPB) duplication and for transit through the G2/M phase of the cell cycle, involved in proteolysis, interacts with the proteasome<ref name='S000042382'>Biggins S, et al. (1996) Yeast ubiquitin-like genes are involved in duplication of the microtubule organizing center. J Cell Biol 133(6):1331-46 {{SGDpaper|S000042382}} PMID 8682868</ref><ref name='S000052146'>Khalfan W, et al. (2000) Functional interaction between the PKC1 pathway and CDC31 network of SPB duplication genes. Genetics 155(4):1543-59 {{SGDpaper|S000052146}} PMID 10924456</ref><ref name='S000054506'>Kaye FJ, et al. (2000) A family of ubiquitin-like proteins binds the ATPase domain of Hsp70-like Stch. FEBS Lett 467(2-3):348-55 {{SGDpaper|S000054506}} PMID 10675567</ref><ref name='S000069044'>Funakoshi M, et al. (2002) Budding yeast Dsk2p is a polyubiquitin-binding protein that can interact with the proteasome. Proc Natl Acad Sci U S A 99(2):745-50 {{SGDpaper|S000069044}} PMID 11805328</ref><ref name='S000070040'>Saeki Y, et al. (2002) Ubiquitin-like proteins and Rpn10 play cooperative roles in ubiquitin-dependent proteolysis. Biochem Biophys Res Commun 293(3):986-92 {{SGDpaper|S000070040}} PMID 12051757</ref><ref name='S000069561'>Rao H and Sastry A (2002) Recognition of specific ubiquitin conjugates is important for the proteolytic functions of the ubiquitin-associated domain proteins Dsk2 and Rad23. J Biol Chem 277(14):11691-5
+'''Description of YMR276W:''' Nuclear-enriched ubiquitin-like polyubiquitin-binding protein, required for spindle pole body (SPB) duplication and for transit through the G2/M phase of the cell cycle, involved in proteolysis, interacts with the proteasome<ref name='S000042382'>Biggins S, et al. (1996) Yeast ubiquitin-like genes are involved in duplication of the microtubule organizing center. J Cell Biol 133(6):1331-46 {{SGDpaper|S000042382}} PMID 8682868</ref><ref name='S000069044'>Funakoshi M, et al. (2002) Budding yeast Dsk2p is a polyubiquitin-binding protein that can interact with the proteasome. Proc Natl Acad Sci U S A 99(2):745-50 {{SGDpaper|S000069044}} PMID 11805328</ref><ref name='S000054506'>Kaye FJ, et al. (2000) A family of ubiquitin-like proteins binds the ATPase domain of Hsp70-like Stch. FEBS Lett 467(2-3):348-55 {{SGDpaper|S000054506}} PMID 10675567</ref><ref name='S000052146'>Khalfan W, et al. (2000) Functional interaction between the PKC1 pathway and CDC31 network of SPB duplication genes. Genetics 155(4):1543-59 {{SGDpaper|S000052146}} PMID 10924456</ref><ref name='S000069561'>Rao H and Sastry A (2002) Recognition of specific ubiquitin conjugates is important for the proteolytic functions of the ubiquitin-associated domain proteins Dsk2 and Rad23. J Biol Chem 277(14):11691-5 {{SGDpaper|S000069561}} PMID 11805121</ref><ref name='S000070040'>Saeki Y, et al. (2002) Ubiquitin-like proteins and Rpn10 play cooperative roles in ubiquitin-dependent proteolysis. Biochem Biophys Res Commun 293(3):986-92
-  {{SGDpaper|S000069561}} PMID 11805121</ref>
+  {{SGDpaper|S000070040}} PMID 12051757</ref>
 <br>
 <br>

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YMR276W:''' Nuclear-enriched ubiquitin-like polyubiquitin-binding protein, required for spindle pole body (SPB) duplication and for transit through the G2/M phase of the cell cycle, involved in proteolysis, interacts with the proteasome<ref name='S000070040'>Saeki Y, et al. (2002) Ubiquitin-like proteins and Rpn10 play cooperative roles in ubiquitin-dependent proteolysis. Biochem Biophys Res Commun 293(3):986-92 {{SGDpaper|S000070040}} PMID 12051757</ref><ref name='S000069561'>Rao H and Sastry A (2002) Recognition of specific ubiquitin conjugates is important for the proteolytic functions of the ubiquitin-associated domain proteins Dsk2 and Rad23. J Biol Chem 277(14):11691-5 {{SGDpaper|S000069561}} PMID 11805121</ref><ref name='S000069044'>Funakoshi M, et al. (2002) Budding yeast Dsk2p is a polyubiquitin-binding protein that can interact with the proteasome. Proc Natl Acad Sci U S A 99(2):745-50 {{SGDpaper|S000069044}} PMID 11805328</ref><ref name='S000054506'>Kaye FJ, et al. (2000) A family of ubiquitin-like proteins binds the ATPase domain of Hsp70-like Stch. FEBS Lett 467(2-3):348-55 {{SGDpaper|S000054506}} PMID 10675567</ref><ref name='S000052146'>Khalfan W, et al. (2000) Functional interaction between the PKC1 pathway and CDC31 network of SPB duplication genes. Genetics 155(4):1543-59 {{SGDpaper|S000052146}} PMID 10924456</ref><ref name='S000042382'>Biggins S, et al. (1996) Yeast ubiquitin-like genes are involved in duplication of the microtubule organizing center. J Cell Biol 133(6):1331-46
+'''Description of YMR276W:''' Nuclear-enriched ubiquitin-like polyubiquitin-binding protein, required for spindle pole body (SPB) duplication and for transit through the G2/M phase of the cell cycle, involved in proteolysis, interacts with the proteasome<ref name='S000042382'>Biggins S, et al. (1996) Yeast ubiquitin-like genes are involved in duplication of the microtubule organizing center. J Cell Biol 133(6):1331-46 {{SGDpaper|S000042382}} PMID 8682868</ref><ref name='S000052146'>Khalfan W, et al. (2000) Functional interaction between the PKC1 pathway and CDC31 network of SPB duplication genes. Genetics 155(4):1543-59 {{SGDpaper|S000052146}} PMID 10924456</ref><ref name='S000054506'>Kaye FJ, et al. (2000) A family of ubiquitin-like proteins binds the ATPase domain of Hsp70-like Stch. FEBS Lett 467(2-3):348-55 {{SGDpaper|S000054506}} PMID 10675567</ref><ref name='S000069044'>Funakoshi M, et al. (2002) Budding yeast Dsk2p is a polyubiquitin-binding protein that can interact with the proteasome. Proc Natl Acad Sci U S A 99(2):745-50 {{SGDpaper|S000069044}} PMID 11805328</ref><ref name='S000070040'>Saeki Y, et al. (2002) Ubiquitin-like proteins and Rpn10 play cooperative roles in ubiquitin-dependent proteolysis. Biochem Biophys Res Commun 293(3):986-92 {{SGDpaper|S000070040}} PMID 12051757</ref><ref name='S000069561'>Rao H and Sastry A (2002) Recognition of specific ubiquitin conjugates is important for the proteolytic functions of the ubiquitin-associated domain proteins Dsk2 and Rad23. J Biol Chem 277(14):11691-5
-  {{SGDpaper|S000042382}} PMID 8682868</ref>
+  {{SGDpaper|S000069561}} PMID 11805121</ref>
 <br>
 <br>

← Older revision		Revision as of 20:02, 21 February 2007
Line 28:		Line 28:
	{{CommentaryHelp}}		{{CommentaryHelp}}

		+
		+
		+
		+	<!-- PLEASE ADD Community Commentary ABOVE THIS MESSAGE. See below for an example of community annotation -->
		+	<!--
		+	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>
		+	-->

	<protect>		<protect>

@@ 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=S000004889 YMR276W]
+|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000004889 YMR276W]
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''         ||''DSK2 ''

@@ Line 1: / Line 1: @@
 <!-- PLEASE DO NOT EDIT HERE. USE THE SECTION EDIT LINKS ON THE RIGHT MARGIN-->
 {{PageTop}}
 {|{{Prettytable}} align = 'right' width = '200px'
 |-
@@ Line 13: / Line 14: @@
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
 |nowrap| Chr XIII:818826..819947
 |}
 <br>
@@ Line 23: / Line 22: @@
 <br>
 <br>
+<br>
 __TOC__
 ==Community Commentary==
 {{CommentaryHelp}}
 ==References==
 <!-- REFERENCES ARE AUTOMATICALLY GENERATED.  PLEASE DON'T EDIT THIS SECTION-->
 {{RefHelp}}