SIP2/YGL208W Literature Guide Help

Other names published for SIP2: SPM2, YGL208W

SIP2 - Protein Processing/Modification/Regulation (10)

ReferenceOther Genes Addressed
Galdieri L and Vancura A  (2012) Acetyl-CoA carboxylase regulates global histone acetylation. J Biol Chem 287(28):23865-76
Lu JY, et al.  (2011) Acetylation of yeast AMPK controls intrinsic aging independently of caloric restriction. Cell 146(6):969-79
Zhang Y, et al.  (2011) Reg1 protein regulates phosphorylation of all three Snf1 isoforms but preferentially associates with the Gal83 isoform. Eukaryot Cell 10(12):1628-36
Mangat S, et al.  (2010) Differential roles of the glycogen-binding domains of beta subunits in regulation of the Snf1 kinase complex. Eukaryot Cell 9(1):173-83
Lin YY, et al.  (2009) Protein acetylation microarray reveals that NuA4 controls key metabolic target regulating gluconeogenesis. Cell 136(6):1073-84
Amodeo GA, et al.  (2007) Crystal structure of the heterotrimer core of Saccharomyces cerevisiae AMPK homologue SNF1. Nature 449(7161):492-5
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
Ashrafi K, et al.  (1998) A role for Saccharomyces cerevisiae fatty acid activation protein 4 in regulating protein N-myristoylation during entry into stationary phase. J Biol Chem 273(40):25864-74
Lesage P, et al.  (1996) Yeast SNF1 protein kinase interacts with SIP4, a C6 zinc cluster transcriptional activator: a new role for SNF1 in the glucose response. Mol Cell Biol 16(5):1921-8
Yang X, et al.  (1994) A family of proteins containing a conserved domain that mediates interaction with the yeast SNF1 protein kinase complex. EMBO J 13(24):5878-86