Difference between revisions of "YER151C"
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| − | '''Description of YER151C:''' Ubiquitin-specific protease that interacts with Bre5p to co-regulate anterograde and retrograde transport between | + | '''Description of YER151C:''' Ubiquitin-specific protease that interacts with Bre5p to co-regulate anterograde and retrograde transport between the ER and Golgi; 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='S000136456'>Tsvetanova NG, et al. (2010) Proteome-Wide Search Reveals Unexpected RNA-Binding Proteins in Saccharomyces cerevisiae.LID - e12671 [pii] PLoS One 5(9) |
| − | {{SGDpaper| | + | {{SGDpaper|S000136456}} PMID 20844764</ref> |
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Revision as of 13:05, 2 February 2011
Share your knowledge...Edit this entry! <protect>
| Systematic name | YER151C |
| Gene name | UBP3 |
| Aliases | BLM3 |
| Feature type | ORF, Verified |
| Coordinates | Chr V:472419..469681 |
| Primary SGDID | S000000953 |
Description of YER151C: Ubiquitin-specific protease that interacts with Bre5p to co-regulate anterograde and retrograde transport between the ER and Golgi; inhibitor of gene silencing; cleaves ubiquitin fusions but not polyubiquitin; also has mRNA binding activity[1][2][3][4][5]
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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. [6] [7]
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References
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- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 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
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See Help:Categories on how to add the wiki page for this gene to a Category </protect>
