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Protein phosphatase, Mg2+/Mn2+ dependent, 1G
PP2Cgamma, PPM1G, FIN13, protein phosphatase 1gamma, protein phosphatase 1 G
The protein encoded by this gene is a member of the PP2C family of Ser/Thr protein phosphatases. PP2C family members are known to be negative regulators of cell stress response pathways. This phosphatase is found to be responsible for the dephosphorylation of Pre-mRNA splicing factors, which is important for the formation of functional spliceosome. Studies of a similar gene in mice suggested a role of this phosphatase in regulating cell cycle progression. [provided by RefSeq, Apr 2010] (from
NCBI)
Choudhary et al., Copenhagen, Denmark. In Mol Cell, May 2012
We show that the splicing-regulator phosphatase PPM1G is recruited to sites of DNA damage, while the splicing-associated protein THRAP3 is excluded from these regions.
Dianov et al., Oxford, United Kingdom. In Mol Cell, Apr 2012
After ionizing radiation, dephosphorylation of USP7S by the ATM-dependent protein phosphatase PPM1G leads to USP7S downregulation, followed by Mdm2 downregulation and accumulation of p53.
Takai et al., Nagoya, Japan. In Bioorg Med Chem, 2010
Protein phosphatase 1gamma, a serine/threonine phosphatase, is a metalloprotein that coordinates two Mn(2+) in the active site when expressed in Escherichia coli in a buffer containing MnCl(2).
Vaughan et al., Bethesda, United States. In Proc Natl Acad Sci U S A, 2007
Brefeldin A-inhibited guanine nucleotide-exchange proteins (GEPs) BIG1 and BIG2 activate ADP-ribosylation factor (ARF) GTPases, which are required for vesicular trafficking.
Taylor et al., Dublin, Ireland. In J Cell Physiol, 2006
Eukaryotic cells sense decreased oxygen levels and respond by altering their metabolic strategy to sustain non-respiratory ATP production through glycolysis, and thus promote cell survival in a hypoxic environment.
Yano et al., Ponce, Puerto Rico. In Mol Cell Biochem, 2002
Among PKC isozymes examined, PKCzeta was the most effective modulator followed by PKCgamma, and protein phosphatase 1gamma and 2A decreased the catalase activity.
In the mitochondrial inner membrane a PP2Cgamma-type phosphatase has also been immunodetected, which dephosphorylates the 18 kDa subunit, phosphorylated by PKA.