3.1.3.52	A193X	single-nucleotide polymorphisms (SNPs) in human PP2Cm: mutant demonstrate basal activity against branched-chain alpha-keto dehydrogenase (BCKD) but impaired responsiveness to branched-chain-alpha-keto acids (BCKAs)	732061	
3.1.3.52	E321K	single-nucleotide polymorphisms (SNPs) in human PP2Cm: mutant demonstrate basal activity against branched-chain alpha-keto dehydrogenase (BCKD) but impaired responsiveness to branched-chain-alpha-keto acids (BCKAs). Mutant is not detected by immunoblot using human PP2Cm antibody. Therefore, it remains unclear whether this mutant is phosphatase dead due to loss-of-function mutations or unstable due to premature truncation	732061	
3.1.3.52	F359X	single-nucleotide polymorphisms (SNPs) in human PP2Cm: frameshift mutant shows no phosphatase activity at basal or after branched-chain-alpha-keto acids (BCKA) treatment. Mutant is not detected by immunoblot using human PP2Cm antibody. Therefore, it remains unclear whether this mutant is phosphatase dead due to loss-of-function mutations or unstable due to premature truncation	732061	
3.1.3.52	I167T	single-nucleotide polymorphisms (SNPs) in human PP2Cm: mutation has no an elevated activity compared to wild-type	732061	
3.1.3.52	additional information	motifs responsible for PP2Cm and E2 interaction: using deletion mutants it is shown that the region between the residues 46 and 61 is critical to the association of PP2Cm with the complex	732061	
3.1.3.52	N94K	missense mutant due to single nucleotide polymorphism. Mutation significantly impairs Mg2+-dependent catalytic activity and induces a conformational change in the key residue in coordinating the Mg2+ in the active site	751367	
3.1.3.52	N94K	single-nucleotide polymorphisms (SNPs) in human PP2Cm: mutation has no impact on PP2Cm activity	732061