Plays an important role in preventing glycogen hyperphosphorylation and the formation of insoluble aggregates, via its activity as glycogen phosphatase, and by promoting the ubiquitination of proteins involved in glycogen metabolism via its interaction with the E3 ubiquitin ligase NHLRC1/malin. Shows strong phosphatase activity towards complex carbohydrates in vitro, avoiding glycogen hyperphosphorylation which is associated with reduced branching and formation of insoluble aggregates (  ). Dephosphorylates phosphotyrosine and synthetic substrates, such as para-nitrophenylphosphate (pNPP), and has low activity with phosphoserine and phosphothreonine substrates (in vitro) (    ). Has been shown to dephosphorylate MAPT (By similarity). Forms a complex with NHLRC1/malin and HSP70, which suppresses the cellular toxicity of misfolded proteins by promoting their degradation through the ubiquitin-proteasome system (UPS). Acts as a scaffold protein to facilitate PPP1R3C/PTG ubiquitination by NHLRC1/malin . Also promotes proteasome-independent protein degradation through the macroautophagy pathway .
Does not bind to glycogen . Lacks phosphatase activity and might function as a dominant-negative regulator for the phosphatase activity of isoform 1 and isoform 7 (, ).
Has phosphatase activity (in vitro).
Subcellular locations: Cytoplasm
Under glycogenolytic conditions localizes to the nucleus.
Subcellular locations: Cytoplasm, Endoplasmic reticulum membrane, Cell membrane
Colocalizes with glycogen synthase in punctate structures in the cytoplasm (, ). Primarily associated with polyribosomes at the rough endoplasmic reticulum, and also detected at the plasma membrane ( , ).
Subcellular locations: Cytoplasm, Endoplasmic reticulum membrane, Cell membrane, Nucleus
Also found in the nucleus.
Subcellular locations: Cytoplasm, Nucleus
Subcellular locations: Cytoplasm, Nucleus
Subcellular locations: Cytoplasm
Expressed in heart, skeletal muscle, kidney, pancreas and brain. Isoform 4 is also expressed in the placenta.