SIC1 Antibody

1. Studies propose that Sic1, Cdc37, and Hsp82 may orchestrate parts of the cellular starvation response by regulating transcription factor- and kinase activities. PMID: 24909858
2. Data indicate that Sic1 function in analogy to its human counterpart p27(Kip1), whose deregulation leads to failure in timing of kinase activation and, therefore, to cancer. PMID: 22161326
3. Ime2 does not directly catalyze Sic1 phosphorylation to target it for destabilization as Cln1,-2/Cdk1 do during the cell cycle PMID: 22393365
4. We analyse oscillations of B-type (Clb) cyclins, focusing on the role of their inhibitor Sic1. PMID: 21963604
5. Individually weak dispersed Sic1 phospho sites engage Cdc4 in a dynamic equilibrium. The multisite nature of this interaction confers cooperative dependence on kinase activity for Sic1 recognition & ubiquitination at equilibrium. PMID: 22328159
6. Sic1 regulates waves of Clbs, acting as a timer in their appearance, thus controlling Cdk1-Clbs activation. The molecular mechanism is not yet fully understood but is hypothesized to occur via stoichiometric binding of Sic1 to Cdk1-Clb complexes. PMID: 22002907
7. Computational simulation revealed that an increased amount of SIC1 mRNAs lead to an amplified dispersion of Sic1 protein levels, suggesting mRNA control being critical to set timing of Sic1 downregulation and, therefore, S phase onset PMID: 21717009
8. we discovered previously unrecognized levels of regulation of the Ace2 transcription factor and the cyclin-dependent protein kinase inhibitor Sic1 PMID: 21196523
9. CK2 plays a role in the regulation of Sic1 activity. PMID: 16168390
10. These data indicate a previously unrecognized inhibitor/activator dual role for Sic1 and put it among key molecules whose activity is regulated by their nuclear-cytoplasmic localization. PMID: 16294029
11. Ime2 is necessary but not sufficient to promote Sic1 destruction during sporulation. PMID: 16776651
12. CK2 phosphorylates Sic1 in vivo PMID: 16777072
13. Sic1 phosphorylation provides a sharp link between G(1) cyclin activation and Clb kinase activation, but failure of Sic1 phosphorylation and proteolysis imposes a variable cell cycle delay and extreme sensitivity to B-type cyclin dosage PMID: 17483408
14. Here we show that CK2 inactivation up-regulates Sic1 level resulting in severe down-regulation of Clb5-Cdc28 kinase activity. PMID: 17574209
15. Accumulation of SIC1 mutated at multiple phosphorylation sites (stabilized version) led to significant DNA rereplication in the absence of normal chromosome segregation PMID: 19116279
16. Data concluded that the molecule exists in a highly disordered state but displays some content in secondary and tertiary structure. The mutations S201A and S201E do not have significant effects on the conformational properties of the pure protein. PMID: 19280601

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KEGG: sce:YLR079W

STRING: 4932.YLR079W