YDR143C - 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=S000002550 YDR143C]
+|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000002550 YDR143C]
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''         ||''SAN1 ''

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YDR143C:''' Ubiquitin-protein ligase, involved in the proteasome-dependent degradation of aberrant nuclear proteins; contains intrinsically disordered regions that contribute to substrate recognition<ref name='S000058946'>Dasgupta A, et al. (2004) Sir Antagonist 1 (San1) is a ubiquitin ligase. J Biol Chem 279(26):26830-8 {{SGDpaper|S000058946}} PMID 15078868</ref><ref name='S000081200'>Gardner RG, et al. (2005) Degradation-mediated protein quality control in the nucleus. Cell 120(6):803-15 {{SGDpaper|S000081200}} PMID 15797381</ref><ref name='S000142868'>Rosenbaum JC, et al. (2011) Disorder targets misorder in nuclear quality control degradation: a disordered ubiquitin ligase directly recognizes its misfolded substrates. Mol Cell 41(1):93-106
+'''Description of YDR143C:''' Ubiquitin-protein ligase; involved in the proteasome-dependent degradation of aberrant nuclear proteins; targets substrates with regions of exposed hydrophobicity containing 5 or more contiguous hydrophobic residues; contains intrinsically disordered regions that contribute to substrate recognition<ref name='S000058946'>Dasgupta A, et al. (2004) Sir Antagonist 1 (San1) is a ubiquitin ligase. J Biol Chem 279(26):26830-8 {{SGDpaper|S000058946}} PMID 15078868</ref><ref name='S000145368'>Fredrickson EK, et al. (2011) Exposed hydrophobicity is a key determinant of nuclear quality control degradation. Mol Biol Cell () {{SGDpaper|S000145368}} PMID 21551067</ref><ref name='S000081200'>Gardner RG, et al. (2005) Degradation-mediated protein quality control in the nucleus. Cell 120(6):803-15 {{SGDpaper|S000081200}} PMID 15797381</ref><ref name='S000142868'>Rosenbaum JC, et al. (2011) Disorder targets misorder in nuclear quality control degradation: a disordered ubiquitin ligase directly recognizes its misfolded substrates. Mol Cell 41(1):93-106
   {{SGDpaper|S000142868}} PMID 21211726</ref>
 <br>

@@ Line 13: / Line 13: @@
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
-|nowrap| Chr IV:743872..742040
+|nowrap| Chr IV:743874..742042
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''           || S000002550

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YDR143C:''' Ubiquitin-protein ligase, involved in the proteasome-dependent degradation of aberrant nuclear proteins<ref name='S000058946'>Dasgupta A, et al. (2004) Sir Antagonist 1 (San1) is a ubiquitin ligase. J Biol Chem 279(26):26830-8 {{SGDpaper|S000058946}} PMID 15078868</ref><ref name='S000081200'>Gardner RG, et al. (2005) Degradation-mediated protein quality control in the nucleus. Cell 120(6):803-15
+'''Description of YDR143C:''' Ubiquitin-protein ligase, involved in the proteasome-dependent degradation of aberrant nuclear proteins; contains intrinsically disordered regions that contribute to substrate recognition<ref name='S000058946'>Dasgupta A, et al. (2004) Sir Antagonist 1 (San1) is a ubiquitin ligase. J Biol Chem 279(26):26830-8 {{SGDpaper|S000058946}} PMID 15078868</ref><ref name='S000081200'>Gardner RG, et al. (2005) Degradation-mediated protein quality control in the nucleus. Cell 120(6):803-15 {{SGDpaper|S000081200}} PMID 15797381</ref><ref name='S000142868'>Rosenbaum JC, et al. (2011) Disorder targets misorder in nuclear quality control degradation: a disordered ubiquitin ligase directly recognizes its misfolded substrates. Mol Cell 41(1):93-106
-  {{SGDpaper|S000081200}} PMID 15797381</ref>
+  {{SGDpaper|S000142868}} PMID 21211726</ref>
 <br>
 <br>

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YDR143C:''' Ubiquitin-protein ligase, involved in the proteasome-dependent degradation of aberrant nuclear proteins<ref name='S000081200'>Gardner RG, et al. (2005) Degradation-mediated protein quality control in the nucleus. Cell 120(6):803-15 {{SGDpaper|S000081200}} PMID 15797381</ref><ref name='S000058946'>Dasgupta A, et al. (2004) Sir Antagonist 1 (San1) is a ubiquitin ligase. J Biol Chem 279(26):26830-8
+'''Description of YDR143C:''' Ubiquitin-protein ligase, involved in the proteasome-dependent degradation of aberrant nuclear proteins<ref name='S000058946'>Dasgupta A, et al. (2004) Sir Antagonist 1 (San1) is a ubiquitin ligase. J Biol Chem 279(26):26830-8 {{SGDpaper|S000058946}} PMID 15078868</ref><ref name='S000081200'>Gardner RG, et al. (2005) Degradation-mediated protein quality control in the nucleus. Cell 120(6):803-15
-  {{SGDpaper|S000058946}} PMID 15078868</ref>
+  {{SGDpaper|S000081200}} PMID 15797381</ref>
 <br>
 <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=YDR143C YDR143C]
+|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000002550 YDR143C]
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''         ||''SAN1 ''
@@ Line 14: / Line 14: @@
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
 |nowrap| Chr IV:743871..742039
 |}
 <br>
-'''Description of {{PAGENAME}}:''' Ubiquitin-protein ligase, involved in the proteasome-dependent degradation of aberrant nuclear proteins; san1 mutations suppress sir4, spt16, and cdc68 mutations, suggesting a role in chromatin silencing<ref name='S000081200'>Gardner RG, et al. (2005) Degradation-mediated protein quality control in the nucleus. Cell 120(6):803-15 {{SGDpaper|S000081200}} PMID 15797381</ref><ref name='S000058946'>Dasgupta A, et al. (2004) Sir Antagonist 1 (San1) is a ubiquitin ligase. J Biol Chem 279(26):26830-8 {{SGDpaper|S000058946}} PMID 15078868</ref><ref name='S000049062'>Xu Q, et al. (1993) The Saccharomyces cerevisiae Cdc68 transcription activator is antagonized by San1, a protein implicated in transcriptional silencing. Mol Cell Biol 13(12):7553-65 {{SGDpaper|S000049062}} PMID 8246972</ref><ref name='S000045142'>Schnell R, et al. (1989) Genetic and molecular characterization of suppressors of SIR4 mutations in Saccharomyces cerevisiae. Genetics 122(1):29-46
+'''Description of YDR143C:''' Ubiquitin-protein ligase, involved in the proteasome-dependent degradation of aberrant nuclear proteins; san1 mutations suppress sir4, spt16, and cdc68 mutations, suggesting a role in chromatin silencing<ref name='S000081200'>Gardner RG, et al. (2005) Degradation-mediated protein quality control in the nucleus. Cell 120(6):803-15 {{SGDpaper|S000081200}} PMID 15797381</ref><ref name='S000058946'>Dasgupta A, et al. (2004) Sir Antagonist 1 (San1) is a ubiquitin ligase. J Biol Chem 279(26):26830-8 {{SGDpaper|S000058946}} PMID 15078868</ref><ref name='S000049062'>Xu Q, et al. (1993) The Saccharomyces cerevisiae Cdc68 transcription activator is antagonized by San1, a protein implicated in transcriptional silencing. Mol Cell Biol 13(12):7553-65 {{SGDpaper|S000049062}} PMID 8246972</ref><ref name='S000045142'>Schnell R, et al. (1989) Genetic and molecular characterization of suppressors of SIR4 mutations in Saccharomyces cerevisiae. Genetics 122(1):29-46
   {{SGDpaper|S000045142}} PMID 2471670</ref>
 <br>
@@ Line 44: / Line 46: @@
 J Biol Chem 278(5):3265-74</ref>
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