Difference between revisions of "YGL208W"

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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000003176 YGL208W]  
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000003176 YGL208W]  
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''SIP2 ''
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
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|nowrap| Chr VII:97342..98589
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|nowrap| Chr VII:97338..98585
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''          || S000003176
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''          || S000003176
 
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'''Description of YGL208W:''' One of three beta subunits of the Snf1 serine/threonine protein kinase complex involved in the response to glucose starvation; null mutants exhibit accelerated aging; N-myristoylprotein localized to the cytoplasm and the plasma membrane<ref name='S000049850'>Ashrafi K, et al. (2000) Sip2p and its partner snf1p kinase affect aging in S. cerevisiae. Genes Dev 14(15):1872-85 {{SGDpaper|S000049850}} PMID 10921902</ref><ref name='S000059161'>Schmidt MC and McCartney RR (2000) beta-subunits of Snf1 kinase are required for kinase function and substrate definition. EMBO J 19(18):4936-43 {{SGDpaper|S000059161}} PMID 10990457</ref><ref name='S000060188'>Vincent O, et al. (2001) Subcellular localization of the Snf1 kinase is regulated by specific beta subunits and a novel glucose signaling mechanism. Genes Dev 15(9):1104-14 {{SGDpaper|S000060188}} PMID 11331606</ref><ref name='S000072977'>Lin SS, et al. (2003) Sip2, an N-myristoylated beta subunit of Snf1 kinase, regulates aging in Saccharomyces cerevisiae by affecting cellular histone kinase activity, recombination at rDNA loci, and silencing. J Biol Chem 278(15):13390-7
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'''Description of YGL208W:''' One of three beta subunits of the Snf1 serine/threonine protein kinase complex involved in the response to glucose starvation; null mutants exhibit accelerated aging; N-myristoylprotein localized to the cytoplasm and the plasma membrane<ref name='S000049850'>Ashrafi K, et al. (2000) Sip2p and its partner snf1p kinase affect aging in S. cerevisiae. Genes Dev 14(15):1872-85 {{SGDpaper|S000049850}} PMID 10921902</ref><ref name='S000072977'>Lin SS, et al. (2003) Sip2, an N-myristoylated beta subunit of Snf1 kinase, regulates aging in Saccharomyces cerevisiae by affecting cellular histone kinase activity, recombination at rDNA loci, and silencing. J Biol Chem 278(15):13390-7 {{SGDpaper|S000072977}} PMID 12562756</ref><ref name='S000059161'>Schmidt MC and McCartney RR (2000) beta-subunits of Snf1 kinase are required for kinase function and substrate definition. EMBO J 19(18):4936-43 {{SGDpaper|S000059161}} PMID 10990457</ref><ref name='S000060188'>Vincent O, et al. (2001) Subcellular localization of the Snf1 kinase is regulated by specific beta subunits and a novel glucose signaling mechanism. Genes Dev 15(9):1104-14
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{{SGDpaper|S000072977}} PMID 12562756</ref>
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{{SGDpaper|S000060188}} PMID 11331606</ref>
 
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Latest revision as of 06:45, 23 January 2012

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

Systematic name YGL208W
Gene name SIP2
Aliases SPM2
Feature type ORF, Verified
Coordinates Chr VII:97338..98585
Primary SGDID S000003176


Description of YGL208W: One of three beta subunits of the Snf1 serine/threonine protein kinase complex involved in the response to glucose starvation; null mutants exhibit accelerated aging; N-myristoylprotein localized to the cytoplasm and the plasma membrane[1][2][3][4]




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Community Commentary

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Alleles, Strains, and Phenotypes

Multiple Knockout Strains

Strain Background: Sigma1278b (Sigma2000 series)
Genotype: MCY 4597
Together with: NRG2, NRG1, SIP1, GAL83
Phenotype(s): Loss of function (Null)

sip2 gal83 double mutants are more defective for invasive growth in response to limiting glucose than gal83 single mutants. [5] [6]

Strain Background: Sigma1278b (Sigma2000 series)
Genotype: MCY4600
Together with: REG1, SIP1, GAL83, MUC1
Phenotype(s): Loss of function (Null)

Deletion of SIP1 in a gal83 sip2 double mutant causes an increase in invasion, suggesting Sip1 negatively regulates invasive growth. [5] [6]

Strain Background: Sigma1278b (Sigma 2000 series)
Genotype: MCY4633
Together with: REG1, SIP1, GAL83, MUC1
Phenotype(s): Loss of function (Null)

Deletion of both SIP2 and GAL83 in a reg1 mutant suppresses its constitutive filamentous phenotype. [5] [6]

Strain Background: Sigma1278b (Sigma2000 series)
Genotype: MCY4600
Together with: REG1, SIP1, GAL83, MUC1
Phenotype(s): Loss of function (Null)

Deletion of SIP1 in a gal83 sip2 double mutant causes an increase in invasion, suggesting Sip1 negatively regulates invasive growth. [5] [6]

Strain Background: Sigma1278b (Sigma 2000 series)
Genotype: MCY4597
Together with: NRG2, NRG1, SIP1, GAL83
Phenotype(s): Loss of function (Null)

sip2 gal83 double mutants are defective for filamentation in response to glucose depletion. [5] [6]

Strain Background: Sigma1278b (Sigma2000 series)
Genotype: MCY 4597
Together with: NRG2, NRG1, SIP1, GAL83
Phenotype(s): Loss of function (Null)

sip2 gal83 double mutants are more defective for invasive growth in response to limiting glucose than gal83 single mutants. [5] [6]

Strain Background: Sigma1278b (Sigma 2000 series)
Genotype: MCY4633
Together with: REG1, SIP1, GAL83, MUC1
Phenotype(s): Loss of function (Null)

Deletion of both SIP2 and GAL83 in a reg1 mutant suppresses its constitutive filamentous phenotype. [5] [6]

Strain Background: Sigma1278b (Sigma 2000 series)
Genotype: MCY4597
Together with: NRG2, NRG1, SIP1, GAL83
Phenotype(s): Loss of function (Null)

sip2 gal83 double mutants are defective for filamentation in response to glucose depletion. [5] [6]

DNA and RNA Details

Other DNA and RNA Details

Other Topic: expression

Specifically higher expression in carbon limited chemostat cultures versus carbon excess. [7] [8]

Protein Details

Protein Function/Process

One of three alternative beta subunits of the Snf1 kinase complex [3] [9]




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References

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  1. ↑ Ashrafi K, et al. (2000) Sip2p and its partner snf1p kinase affect aging in S. cerevisiae. Genes Dev 14(15):1872-85 SGD PMID 10921902
  2. ↑ Lin SS, et al. (2003) Sip2, an N-myristoylated beta subunit of Snf1 kinase, regulates aging in Saccharomyces cerevisiae by affecting cellular histone kinase activity, recombination at rDNA loci, and silencing. J Biol Chem 278(15):13390-7 SGD PMID 12562756
  3. ↑ 3.0 3.1 Schmidt MC and McCartney RR (2000) beta-subunits of Snf1 kinase are required for kinase function and substrate definition. EMBO J 19(18):4936-43 SGD PMID 10990457
  4. ↑ Vincent O, et al. (2001) Subcellular localization of the Snf1 kinase is regulated by specific beta subunits and a novel glucose signaling mechanism. Genes Dev 15(9):1104-14 SGD PMID 11331606
  5. ↑ 5.0 5.1 5.2 5.3 5.4 5.5 5.6 5.7 Vyas VK, et al. (2003) Snf1 kinases with different beta-subunit isoforms play distinct roles in regulating haploid invasive growth. Mol Cell Biol 23(4):1341-8 SGD PMID 12556493
  6. ↑ 6.0 6.1 6.2 6.3 6.4 6.5 6.6 6.7 submitted by Valmik K. Vyas on 2003-03-27
  7. ↑ 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 SGD PMID 12414795
  8. ↑ submitted by Viktor Boer on 2003-07-25
  9. ↑ submitted by Martin C. Schmidt on 2003-02-17

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