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. Dephosphorylates phosphotyrosine and synthetic substrates, such as para-nitrophenylphosphate (pNPP), and has low activity with phosphoserine and phosphothreonine substrates (in vitro). Has also been shown to dephosphorylate MAPT. Shows strong phosphatase activity towards complex carbohydrates in vitro, avoiding glycogen hyperphosphorylation which is associated with reduced branching and formation of insoluble aggregates. 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.

Belongs to the protein-tyrosine phosphatase family.

331 amino acids

MRFRFGVVVPPAGAGAAPELLVVGSRPELGRWEPRGAVRLRPAGSAAGGGARALQEPGLWLGEVELAPGEAARDGAEPARVDTFWYKFLKREPGGALSWEGNGPHHDRCCTYNENNLVDGVYCLPIGHWIEATGHTNEMKHTTDFYFNIAGHQAMHYSRILPNIWLGSCPRQVEHITIKLKHELGITAVMNFQTEWDIVQNSSGCNRYPEPMTPDTMIKLYKEEGLVYIWMPTPDMSTEGRVQMLPQAVCLLHALLENGHTVYVHCNAGVGRSTAAVCGWLQYVMGWNLRKVQYFLMAKRPAVYIDEDALARAEEDFFQKFGKVRSSVCSV

36.9 kDa

(Note: Representative image - actual molecular weight may vary depending on tag type and expression method)

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