Difference between revisions of "YER151C"

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{|{{Prettytable}} align = 'right' width = '200px'
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000000953 YER151C]  
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000000953 YER151C]  
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''UBP3 ''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''UBP3 ''
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
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|nowrap| Chr V:472419..469681
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|nowrap| Chr V:472424..469686
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''          || S000000953
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''          || S000000953
 
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'''Description of YER151C:''' Ubiquitin-specific protease that interacts with Bre5p to co-regulate anterograde and retrograde transport between endoplasmic reticulum and Golgi compartments; inhibitor of gene silencing; cleaves ubiquitin fusions but not polyubiquitin<ref name='S000075076'>Cohen M, et al. (2003) Deubiquitination, a new player in Golgi to endoplasmic reticulum retrograde transport. J Biol Chem 278(52):51989-92 {{SGDpaper|S000075076}} PMID 14593109</ref><ref name='S000073727'>Cohen M, et al. (2003) Ubp3 requires a cofactor, Bre5, to specifically de-ubiquitinate the COPII protein, Sec23. Nat Cell Biol 5(7):661-7 {{SGDpaper|S000073727}} PMID 12778054</ref><ref name='S000051791'>Moazed D and Johnson D (1996) A deubiquitinating enzyme interacts with SIR4 and regulates silencing in S. cerevisiae. Cell 86(4):667-77 {{SGDpaper|S000051791}} PMID 8752220</ref><ref name='S000051210'>Baker RT, et al. (1992) Ubiquitin-specific proteases of Saccharomyces cerevisiae. Cloning of UBP2 and UBP3, and functional analysis of the UBP gene family. J Biol Chem 267(32):23364-75
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'''Description of YER151C:''' Ubiquitin-specific protease involved in transport and osmotic response; interacts with Bre5p to co-regulate anterograde and retrograde transport between the ER and Golgi; involved in transcription elongation in response to osmostress through phosphorylation at Ser695 by Hog1p; inhibitor of gene silencing; cleaves ubiquitin fusions but not polyubiquitin; also has mRNA binding activity<ref name='S000051210'>Baker RT, et al. (1992) Ubiquitin-specific proteases of Saccharomyces cerevisiae. Cloning of UBP2 and UBP3, and functional analysis of the UBP gene family. J Biol Chem 267(32):23364-75 {{SGDpaper|S000051210}} PMID 1429680</ref><ref name='S000075076'>Cohen M, et al. (2003) Deubiquitination, a new player in Golgi to endoplasmic reticulum retrograde transport. J Biol Chem 278(52):51989-92 {{SGDpaper|S000075076}} PMID 14593109</ref><ref name='S000073727'>Cohen M, et al. (2003) Ubp3 requires a cofactor, Bre5, to specifically de-ubiquitinate the COPII protein, Sec23. Nat Cell Biol 5(7):661-7 {{SGDpaper|S000073727}} PMID 12778054</ref><ref name='S000051791'>Moazed D and Johnson D (1996) A deubiquitinating enzyme interacts with SIR4 and regulates silencing in S. cerevisiae. Cell 86(4):667-77 {{SGDpaper|S000051791}} PMID 8752220</ref><ref name='S000146056'>Sole C, et al. (2011) Control of Ubp3 ubiquitin protease activity by the Hog1 SAPK modulates transcription upon osmostress.LID - 10.1038/emboj.2011.227 [doi] EMBO J () {{SGDpaper|S000146056}} PMID 21743437</ref><ref name='S000136456'>Tsvetanova NG, et al. (2010) Proteome-Wide Search Reveals Unexpected RNA-Binding Proteins in Saccharomyces cerevisiae.LID - e12671 [pii] PLoS One 5(9)
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  {{SGDpaper|S000051210}} PMID 1429680</ref>
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  {{SGDpaper|S000136456}} PMID 20844764</ref>
 
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==Community Commentary==
 
==Community Commentary==
 
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blm3-1 is an allele of UBP3 and BLM10 does not act as a suppressor of blm3-1. Further, blm10 null mutants are not sensitive to DNA damaging agents. The original error in cloning Blm10/Blm3 has caused enormous confusion in the proteasome field.
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<ref>McCullock S, Kinard T, McCullough L, Formosa T (2006) blm3-1 Is an Allele of UBP3, a Ubiquitin Protease that Appears to Act During Transcription of Damaged DNA. J Mol Biol 363(3):660-72</ref>
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<ref>Iwanczyk J, Sadre-Bazzaz K, Ferrell K, Kondrashkina E, Formosa T, Hill CP, Ortega J (2006) Structure of the Blm10-20 S proteasome complex by cryo-electron microscopy. Insights into the mechanism of activation of mature yeast proteasomes. J Mol Biol 363(3):648-59</ref>
  
  
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==References==
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==References==
 
==References==

Latest revision as of 06:45, 23 January 2012

Share your knowledge...Edit this entry! <protect>

Systematic name YER151C
Gene name UBP3
Aliases BLM3
Feature type ORF, Verified
Coordinates Chr V:472424..469686
Primary SGDID S000000953


Description of YER151C: Ubiquitin-specific protease involved in transport and osmotic response; interacts with Bre5p to co-regulate anterograde and retrograde transport between the ER and Golgi; involved in transcription elongation in response to osmostress through phosphorylation at Ser695 by Hog1p; inhibitor of gene silencing; cleaves ubiquitin fusions but not polyubiquitin; also has mRNA binding activity[1][2][3][4][5][6]




</protect>

Community Commentary

About Community Commentary. Please share your knowledge!

blm3-1 is an allele of UBP3 and BLM10 does not act as a suppressor of blm3-1. Further, blm10 null mutants are not sensitive to DNA damaging agents. The original error in cloning Blm10/Blm3 has caused enormous confusion in the proteasome field. [7] [8]




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References

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  1. ↑ Baker RT, et al. (1992) Ubiquitin-specific proteases of Saccharomyces cerevisiae. Cloning of UBP2 and UBP3, and functional analysis of the UBP gene family. J Biol Chem 267(32):23364-75 SGD PMID 1429680
  2. ↑ Cohen M, et al. (2003) Deubiquitination, a new player in Golgi to endoplasmic reticulum retrograde transport. J Biol Chem 278(52):51989-92 SGD PMID 14593109
  3. ↑ Cohen M, et al. (2003) Ubp3 requires a cofactor, Bre5, to specifically de-ubiquitinate the COPII protein, Sec23. Nat Cell Biol 5(7):661-7 SGD PMID 12778054
  4. ↑ Moazed D and Johnson D (1996) A deubiquitinating enzyme interacts with SIR4 and regulates silencing in S. cerevisiae. Cell 86(4):667-77 SGD PMID 8752220
  5. ↑ Sole C, et al. (2011) Control of Ubp3 ubiquitin protease activity by the Hog1 SAPK modulates transcription upon osmostress.LID - 10.1038/emboj.2011.227 [doi] EMBO J () SGD PMID 21743437
  6. ↑ Tsvetanova NG, et al. (2010) Proteome-Wide Search Reveals Unexpected RNA-Binding Proteins in Saccharomyces cerevisiae.LID - e12671 [pii] PLoS One 5(9) SGD PMID 20844764
  7. ↑ McCullock S, Kinard T, McCullough L, Formosa T (2006) blm3-1 Is an Allele of UBP3, a Ubiquitin Protease that Appears to Act During Transcription of Damaged DNA. J Mol Biol 363(3):660-72
  8. ↑ Iwanczyk J, Sadre-Bazzaz K, Ferrell K, Kondrashkina E, Formosa T, Hill CP, Ortega J (2006) Structure of the Blm10-20 S proteasome complex by cryo-electron microscopy. Insights into the mechanism of activation of mature yeast proteasomes. J Mol Biol 363(3):648-59

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References

See Help:References on how to add references

See Help:Categories on how to add the wiki page for this gene to a Category </protect>

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