Difference between revisions of "YLR430W"
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− | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http:// | + | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000004422 YLR430W] |
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''SEN1 '' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''SEN1 '' | ||
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | ||
− | |nowrap| Chr XII: | + | |nowrap| Chr XII:993434..1000129 |
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− | | | + | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID''' || S000004422 |
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− | '''Description of | + | '''Description of YLR430W:''' Presumed helicase and subunit of the Nrd1 complex (Nrd1p-Nab3p-Sen1p); complex interacts with the exosome to mediate 3' end formation of some mRNAs, snRNAs, snoRNAs, and CUTs; homolog of Senataxin which causes Ataxia-Oculomotor Apraxia 2 and a dominant form of amyotrophic lateral sclerosis<ref name='S000115270'>Chen YZ, et al. (2006) Senataxin, the yeast Sen1p orthologue: characterization of a unique protein in which recessive mutations cause ataxia and dominant mutations cause motor neuron disease. Neurobiol Dis 23(1):97-108 {{SGDpaper|S000115270}} PMID 16644229</ref><ref name='S000047324'>Rasmussen TP and Culbertson MR (1998) The putative nucleic acid helicase Sen1p is required for formation and stability of termini and for maximal rates of synthesis and levels of accumulation of small nucleolar RNAs in Saccharomyces cerevisiae. Mol Cell Biol 18(12):6885-96 {{SGDpaper|S000047324}} PMID 9819377</ref><ref name='S000071624'>Steinmetz EJ, et al. (2001) RNA-binding protein Nrd1 directs poly(A)-independent 3'-end formation of RNA polymerase II transcripts. Nature 413(6853):327-31 {{SGDpaper|S000071624}} PMID 11565036</ref><ref name='S000119984'>Steinmetz EJ, et al. (2006) Genome-wide distribution of yeast RNA polymerase II and its control by Sen1 helicase. Mol Cell 24(5):735-46 {{SGDpaper|S000119984}} PMID 17157256</ref><ref name='S000046278'>Ursic D, et al. (1997) The yeast SEN1 gene is required for the processing of diverse RNA classes. Nucleic Acids Res 25(23):4778-85 |
{{SGDpaper|S000046278}} PMID 9365256</ref> | {{SGDpaper|S000046278}} PMID 9365256</ref> | ||
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==Community Commentary== | ==Community Commentary== | ||
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+ | === Protein Details === | ||
+ | [[Category:Topic:Protein Details]] | ||
+ | ==== Protein Modification ==== | ||
+ | [[Category:Topic:Protein Details:Protein Modification]] | ||
+ | '''Modification(s)''': Phosphorylation [[Category:Modification:Phosphorylation]] | ||
+ | |||
+ | Identified as an efficient substrate of Clb2-Cdk1-as1 in a screen of a proteomic GST-fusion library. <ref name='S000074306'>Ubersax JA, et al. (2003) Targets of the cyclin-dependent kinase Cdk1. Nature 425(6960):859-64 {{SGDpaper|S000074306}} PMID 14574415</ref> <ref name = 'CAset7903-2004-01-29'>submitted by [http://db.yeastgenome.org/cgi-bin/colleague/colleagueSearch?id=7903 Jeff Ubersax] on 2004-01-29</ref> | ||
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+ | 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> | ||
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==References== | ==References== | ||
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Latest revision as of 14:05, 10 May 2012
Share your knowledge...Edit this entry! <protect>
Systematic name | YLR430W |
Gene name | SEN1 |
Aliases | CIK3, NRD2 |
Feature type | ORF, Verified |
Coordinates | Chr XII:993434..1000129 |
Primary SGDID | S000004422 |
Description of YLR430W: Presumed helicase and subunit of the Nrd1 complex (Nrd1p-Nab3p-Sen1p); complex interacts with the exosome to mediate 3' end formation of some mRNAs, snRNAs, snoRNAs, and CUTs; homolog of Senataxin which causes Ataxia-Oculomotor Apraxia 2 and a dominant form of amyotrophic lateral sclerosis[1][2][3][4][5]
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Community Commentary
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Protein Details
Protein Modification
Modification(s): Phosphorylation
Identified as an efficient substrate of Clb2-Cdk1-as1 in a screen of a proteomic GST-fusion library. [6] [7]
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References
See Help:References on how to add references
- ↑ Chen YZ, et al. (2006) Senataxin, the yeast Sen1p orthologue: characterization of a unique protein in which recessive mutations cause ataxia and dominant mutations cause motor neuron disease. Neurobiol Dis 23(1):97-108 SGD PMID 16644229
- ↑ Rasmussen TP and Culbertson MR (1998) The putative nucleic acid helicase Sen1p is required for formation and stability of termini and for maximal rates of synthesis and levels of accumulation of small nucleolar RNAs in Saccharomyces cerevisiae. Mol Cell Biol 18(12):6885-96 SGD PMID 9819377
- ↑ Steinmetz EJ, et al. (2001) RNA-binding protein Nrd1 directs poly(A)-independent 3'-end formation of RNA polymerase II transcripts. Nature 413(6853):327-31 SGD PMID 11565036
- ↑ Steinmetz EJ, et al. (2006) Genome-wide distribution of yeast RNA polymerase II and its control by Sen1 helicase. Mol Cell 24(5):735-46 SGD PMID 17157256
- ↑ Ursic D, et al. (1997) The yeast SEN1 gene is required for the processing of diverse RNA classes. Nucleic Acids Res 25(23):4778-85 SGD PMID 9365256
- ↑ Ubersax JA, et al. (2003) Targets of the cyclin-dependent kinase Cdk1. Nature 425(6960):859-64 SGD PMID 14574415
- ↑ submitted by Jeff Ubersax on 2004-01-29
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