YLL002W - Revision history

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{{PageTop}}
{|{{Prettytable}} align = 'right' width = '200px'
|-
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?locus=YLL002W YLL002W]
|-
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''RTT109 ''
|-
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Aliases''' ||''KIM2, REM50''
|-
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Feature type''' || ORF, Verified[[Category:ORF]][[Category:ORF, Verified]]
|-
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
|nowrap| Chr XII:146290..147600
|-
|colspan = '3'|{{Don'tEditThisBox}}
|}
 
'''Description of {{PAGENAME}}:''' Protein with a role in regulation of Ty1 transposition<ref name='S000068874'>Scholes DT, et al. (2001) Multiple regulators of Ty1 transposition in Saccharomyces cerevisiae have conserved roles in genome maintenance. Genetics 159(4):1449-65
{{SGDpaper|S000068874}} PMID 11779788</ref>
 
 
 
 

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==Community Commentary==
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==References==

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@@ Line 13: / Line 13: @@
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
-|nowrap| Chr XII:146290..147600
+|nowrap| Chr XII:146291..147601
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''           || S000003925

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YLL002W:''' Histone acetyltransferase critical for cell survival in the presence of DNA damage during S phase; acetylates H3-K56 and H3-K9; involved in non-homologous end joining and in regulation of Ty1 transposition; interacts physically with Vps75p<ref name='S000068874'>Scholes DT, et al. (2001) Multiple regulators of Ty1 transposition in Saccharomyces cerevisiae have conserved roles in genome maintenance. Genetics 159(4):1449-65 {{SGDpaper|S000068874}} PMID 11779788</ref><ref name='S000120595'>Driscoll R, et al. (2007) Yeast Rtt109 promotes genome stability by acetylating histone H3 on lysine 56. Science 315(5812):649-52 {{SGDpaper|S000120595}} PMID 17272722</ref><ref name='S000120673'>Han J, et al. (2007) Rtt109 acetylates histone H3 lysine 56 and functions in DNA replication. Science 315(5812):653-5 {{SGDpaper|S000120673}} PMID 17272723</ref><ref name='S000124825'>Jessulat M, et al. (2008) Interacting proteins Rtt109 and Vps75 affect the efficiency of non-homologous end-joining in Saccharomyces cerevisiae. Arch Biochem Biophys 469(2):157-64 {{SGDpaper|S000124825}} PMID 18036332</ref><ref name='S000126328'>Fillingham J, et al. (2008) Chaperone control of the activity and specificity of the histone H3 acetyltransferase Rtt109. Mol Cell Biol 28(13):4342-53
+'''Description of YLL002W:''' Histone acetyltransferase critical for cell survival in the presence of DNA damage during S phase; acetylates H3-K56 and H3-K9; involved in non-homologous end joining and in regulation of Ty1 transposition; interacts physically with Vps75p<ref name='S000120595'>Driscoll R, et al. (2007) Yeast Rtt109 promotes genome stability by acetylating histone H3 on lysine 56. Science 315(5812):649-52 {{SGDpaper|S000120595}} PMID 17272722</ref><ref name='S000126328'>Fillingham J, et al. (2008) Chaperone control of the activity and specificity of the histone H3 acetyltransferase Rtt109. Mol Cell Biol 28(13):4342-53 {{SGDpaper|S000126328}} PMID 18458063</ref><ref name='S000120673'>Han J, et al. (2007) Rtt109 acetylates histone H3 lysine 56 and functions in DNA replication. Science 315(5812):653-5 {{SGDpaper|S000120673}} PMID 17272723</ref><ref name='S000124825'>Jessulat M, et al. (2008) Interacting proteins Rtt109 and Vps75 affect the efficiency of non-homologous end-joining in Saccharomyces cerevisiae. Arch Biochem Biophys 469(2):157-64 {{SGDpaper|S000124825}} PMID 18036332</ref><ref name='S000068874'>Scholes DT, et al. (2001) Multiple regulators of Ty1 transposition in Saccharomyces cerevisiae have conserved roles in genome maintenance. Genetics 159(4):1449-65
-  {{SGDpaper|S000126328}} PMID 18458063</ref>
+  {{SGDpaper|S000068874}} PMID 11779788</ref>
 <br>
 <br>

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YLL002W:''' Histone acetyltransferase critical for cell survival in the presence of DNA damage during S phase; acetylates H3-K56 and H3-K9; involved in non-homologous end joining and in regulation of Ty1 transposition; interacts physically with Vps75p<ref name='S000126328'>Fillingham J, et al. (2008) Chaperone control of the activity and specificity of the histone H3 acetyltransferase Rtt109. Mol Cell Biol 28(13):4342-53 {{SGDpaper|S000126328}} PMID 18458063</ref><ref name='S000124825'>Jessulat M, et al. (2008) Interacting proteins Rtt109 and Vps75 affect the efficiency of non-homologous end-joining in Saccharomyces cerevisiae. Arch Biochem Biophys 469(2):157-64 {{SGDpaper|S000124825}} PMID 18036332</ref><ref name='S000120673'>Han J, et al. (2007) Rtt109 acetylates histone H3 lysine 56 and functions in DNA replication. Science 315(5812):653-5 {{SGDpaper|S000120673}} PMID 17272723</ref><ref name='S000120595'>Driscoll R, et al. (2007) Yeast Rtt109 promotes genome stability by acetylating histone H3 on lysine 56. Science 315(5812):649-52 {{SGDpaper|S000120595}} PMID 17272722</ref><ref name='S000068874'>Scholes DT, et al. (2001) Multiple regulators of Ty1 transposition in Saccharomyces cerevisiae have conserved roles in genome maintenance. Genetics 159(4):1449-65
+'''Description of YLL002W:''' Histone acetyltransferase critical for cell survival in the presence of DNA damage during S phase; acetylates H3-K56 and H3-K9; involved in non-homologous end joining and in regulation of Ty1 transposition; interacts physically with Vps75p<ref name='S000068874'>Scholes DT, et al. (2001) Multiple regulators of Ty1 transposition in Saccharomyces cerevisiae have conserved roles in genome maintenance. Genetics 159(4):1449-65 {{SGDpaper|S000068874}} PMID 11779788</ref><ref name='S000120595'>Driscoll R, et al. (2007) Yeast Rtt109 promotes genome stability by acetylating histone H3 on lysine 56. Science 315(5812):649-52 {{SGDpaper|S000120595}} PMID 17272722</ref><ref name='S000120673'>Han J, et al. (2007) Rtt109 acetylates histone H3 lysine 56 and functions in DNA replication. Science 315(5812):653-5 {{SGDpaper|S000120673}} PMID 17272723</ref><ref name='S000124825'>Jessulat M, et al. (2008) Interacting proteins Rtt109 and Vps75 affect the efficiency of non-homologous end-joining in Saccharomyces cerevisiae. Arch Biochem Biophys 469(2):157-64 {{SGDpaper|S000124825}} PMID 18036332</ref><ref name='S000126328'>Fillingham J, et al. (2008) Chaperone control of the activity and specificity of the histone H3 acetyltransferase Rtt109. Mol Cell Biol 28(13):4342-53
-  {{SGDpaper|S000068874}} PMID 11779788</ref>
+  {{SGDpaper|S000126328}} PMID 18458063</ref>
 <br>
 <br>

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YLL002W:''' Histone acetyltransferase critical for cell survival in the presence of DNA damage during S phase, acetylates H3-K56; plays a role in regulation of Ty1 transposition<ref name='S000120673'>Han J, et al. (2007) Rtt109 acetylates histone H3 lysine 56 and functions in DNA replication. Science 315(5812):653-5 {{SGDpaper|S000120673}} PMID 17272723</ref><ref name='S000120595'>Driscoll R, et al. (2007) Yeast Rtt109 promotes genome stability by acetylating histone H3 on lysine 56. Science 315(5812):649-52 {{SGDpaper|S000120595}} PMID 17272722</ref><ref name='S000068874'>Scholes DT, et al. (2001) Multiple regulators of Ty1 transposition in Saccharomyces cerevisiae have conserved roles in genome maintenance. Genetics 159(4):1449-65
+'''Description of YLL002W:''' Histone acetyltransferase critical for cell survival in the presence of DNA damage during S phase; acetylates H3-K56 and H3-K9; involved in non-homologous end joining and in regulation of Ty1 transposition; interacts physically with Vps75p<ref name='S000126328'>Fillingham J, et al. (2008) Chaperone control of the activity and specificity of the histone H3 acetyltransferase Rtt109. Mol Cell Biol 28(13):4342-53 {{SGDpaper|S000126328}} PMID 18458063</ref><ref name='S000124825'>Jessulat M, et al. (2008) Interacting proteins Rtt109 and Vps75 affect the efficiency of non-homologous end-joining in Saccharomyces cerevisiae. Arch Biochem Biophys 469(2):157-64 {{SGDpaper|S000124825}} PMID 18036332</ref><ref name='S000120673'>Han J, et al. (2007) Rtt109 acetylates histone H3 lysine 56 and functions in DNA replication. Science 315(5812):653-5 {{SGDpaper|S000120673}} PMID 17272723</ref><ref name='S000120595'>Driscoll R, et al. (2007) Yeast Rtt109 promotes genome stability by acetylating histone H3 on lysine 56. Science 315(5812):649-52 {{SGDpaper|S000120595}} PMID 17272722</ref><ref name='S000068874'>Scholes DT, et al. (2001) Multiple regulators of Ty1 transposition in Saccharomyces cerevisiae have conserved roles in genome maintenance. Genetics 159(4):1449-65
   {{SGDpaper|S000068874}} PMID 11779788</ref>
 <br>

@@ Line 4: / Line 4: @@
 {|{{Prettytable}} align = 'right' width = '200px'
 |-
-|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?locus=YLL002W YLL002W]
+|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000003925 YLL002W]
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''         ||''RTT109 ''
@@ Line 14: / Line 14: @@
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
 |nowrap| Chr XII:146290..147600
 |}
 <br>
-'''Description of {{PAGENAME}}:''' Histone acetyltransferase critical for cell survival in the presence of DNA damage during S phase, acetylates H3-K56; plays a role in regulation of Ty1 transposition<ref name='S000120673'>Han J, et al. (2007) Rtt109 acetylates histone H3 lysine 56 and functions in DNA replication. Science 315(5812):653-5 {{SGDpaper|S000120673}} PMID 17272723</ref><ref name='S000120595'>Driscoll R, et al. (2007) Yeast Rtt109 promotes genome stability by acetylating histone H3 on lysine 56. Science 315(5812):649-52 {{SGDpaper|S000120595}} PMID 17272722</ref><ref name='S000068874'>Scholes DT, et al. (2001) Multiple regulators of Ty1 transposition in Saccharomyces cerevisiae have conserved roles in genome maintenance. Genetics 159(4):1449-65
+'''Description of YLL002W:''' Histone acetyltransferase critical for cell survival in the presence of DNA damage during S phase, acetylates H3-K56; plays a role in regulation of Ty1 transposition<ref name='S000120673'>Han J, et al. (2007) Rtt109 acetylates histone H3 lysine 56 and functions in DNA replication. Science 315(5812):653-5 {{SGDpaper|S000120673}} PMID 17272723</ref><ref name='S000120595'>Driscoll R, et al. (2007) Yeast Rtt109 promotes genome stability by acetylating histone H3 on lysine 56. Science 315(5812):649-52 {{SGDpaper|S000120595}} PMID 17272722</ref><ref name='S000068874'>Scholes DT, et al. (2001) Multiple regulators of Ty1 transposition in Saccharomyces cerevisiae have conserved roles in genome maintenance. Genetics 159(4):1449-65
   {{SGDpaper|S000068874}} PMID 11779788</ref>
 <br>
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 J Biol Chem 278(5):3265-74</ref>
 -->
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 |}
 <br>
-'''Description of {{PAGENAME}}:''' Protein with a role in regulation of Ty1 transposition<ref name='S000068874'>Scholes DT, et al. (2001) Multiple regulators of Ty1 transposition in Saccharomyces cerevisiae have conserved roles in genome maintenance. Genetics 159(4):1449-65
+'''Description of {{PAGENAME}}:''' Histone acetyltransferase critical for cell survival in the presence of DNA damage during S phase, acetylates H3-K56; plays a role in regulation of Ty1 transposition<ref name='S000120673'>Han J, et al. (2007) Rtt109 acetylates histone H3 lysine 56 and functions in DNA replication. Science 315(5812):653-5 {{SGDpaper|S000120673}} PMID 17272723</ref><ref name='S000120595'>Driscoll R, et al. (2007) Yeast Rtt109 promotes genome stability by acetylating histone H3 on lysine 56. Science 315(5812):649-52 {{SGDpaper|S000120595}} PMID 17272722</ref><ref name='S000068874'>Scholes DT, et al. (2001) Multiple regulators of Ty1 transposition in Saccharomyces cerevisiae have conserved roles in genome maintenance. Genetics 159(4):1449-65
   {{SGDpaper|S000068874}} PMID 11779788</ref>
 <br>
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 {|{{Prettytable}} align = 'right' width = '200px'
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 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
 |nowrap| Chr XII:146290..147600
 |}
 <br>
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 __TOC__
 ==Community Commentary==
 {{CommentaryHelp}}
 ==References==
 <!-- REFERENCES ARE AUTOMATICALLY GENERATED.  PLEASE DON'T EDIT THIS SECTION-->
 {{RefHelp}}