EPM2A

Laforin, isoform 9

344 amino acids

35.169 kDa

MHPKEGAEQHVFSPVPGAPTPPPNRCGRLVLGPRLPAAGTPGPGIRAAAARHALPLWGGGATRRGRRPAGAAGGGVAARAGALGAARCRPPEAGRHRGGRRGPGPAGAGPVARGGGAGGRGGGAGRGGAGPRGHVLVQVPEAGAGRRALLGRYCQQTPAPGAERELRPAPPTGASASGRPRRPRRRASRAFCPRPCALPGRPGLTLLCRPRCRRQPRLRLPTDSLDPYSAPGRLPAHSVACPSDLVSAHPVLSFFPTAPASRASALRLPPGAPFALRVPLDLRVPPFAGPLAARPRAADGFNSPTPPWLGFVSSFSCSNSLKKTQNDPTNETSVFANPRQQCAT

EPM2A

Laforin

331 amino acids

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.

36.9 kDa

MRFRFGVVVPPAGAGAAPELLVVGSRPELGRWEPRGAVRLRPAGSAAGGGARALQEPGLWLGEVELAPGEAARDGAEPARVDTFWYKFLKREPGGALSWEGNGPHHDRCCTYNENNLVDGVYCLPIGHWIEATGHTNEMKHTTDFYFNIAGHQAMHYSRILPNIWLGSCPRQVEHITIKLKHELGITAVMNFQTEWDIVQNSSGCNRYPEPMTPDTMIKLYKEEGLVYIWMPTPDMSTEGRVQMLPQAVCLLHALLENGHTVYVHCNAGVGRSTAAVCGWLQYVMGWNLRKVQYFLMAKRPAVYIDEDALARAEEDFFQKFGKVRSSVCSV

EPM2A

Laforin

331 amino acids

Isoform 7: has phosphatase activity (in vitro).

Belongs to the protein-tyrosine phosphatase family.

37.158 kDa

MRFRFGVVVPPAVAGARPELLVVGSRPELGRWEPRGAVRLRPAGTAAGDGALALQEPGLWLGEVELAAEEAAQDGAEPGRVDTFWYKFLKREPGGELSWEGNGPHHDRCCTYNENNLVDGVYCLPIGHWIEATGHTNEMKHTTDFYFNIAGHQAMHYSRILPNIWLGSCPRQVEHVTIKLKHELGITAVMNFQTEWDIVQNSSGCNRYPEPMTPDTMIKLYREEGLAYIWMPTPDMSTEGRVQMLPQAVCLLHALLEKGHIVYVHCNAGVGRSTAAVCGWLQYVMGWNLRKVQYFLMAKRPAVYIDEEALARAQEDFFQKFGKVRSSVCSL

Epm2a

Laforin

331 amino acids

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.

37.144 kDa

MLFRFGVVVPPAVAGTRLELLLAGSRPELGRWEPRGAVRLRPAGTAAGAAALALQEPGLWLAEVELAPEEEAADGAEPGRIDTFWYKFLQREPGGELHWEGNGPHHDRCCTYNENNLVDGVYCLPVGHWIEATGHTNEMKHTTDFYFNIAGHQAMHYSRILPNIWLGSCPRQLEHVTIKLKHELGITAVMNFQTEWDIIQNSSGCNRYPEPMTPDTMMKLYKEEGLAYIWMPTPDMSTEGRVQMLPQAVCLLHALLENGHTVYVHCNAGVGRSTAAVCGWLHYVIGWSLRKVQYFIMAKRPAVYIDEEALAQAQQDFFQKFGKVHSSICTL

Epm2a

Laforin

330 amino acids

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 (PubMed:18040046, PubMed:18852261, PubMed:19036738, PubMed:23663739, PubMed:24430976, PubMed:24068615). Dephosphorylates phosphotyrosine and synthetic substrates, such as para-nitrophenylphosphate (pNPP), and has low activity with phosphoserine and phosphothreonine substrates (in vitro) (PubMed:16971387, PubMed:24430976). Has also been shown to dephosphorylate MAPT (PubMed:19542233). Shows strong phosphatase activity towards complex carbohydrates in vitro, avoiding glycogen hyperphosphorylation which is associated with reduced branching and formation of insoluble aggregates (PubMed:18040046, PubMed:18852261, PubMed:23663739). 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) (PubMed:19036738, PubMed:24068615). Acts as a scaffold protein to facilitate PPP1R3C/PTG ubiquitination by NHLRC1/malin. Also promotes proteasome-independent protein degradation through the macroautophagy pathway (PubMed:20453062).

Belongs to the protein-tyrosine phosphatase family.

36.958 kDa

MLFRFGVVVPPAVAGARQELLLAGSRPELGRWEPHGAVRLRPAGTAAGAAALALQEPGLWLAEVELEAYEEAGGAEPGRVDTFWYKFLQREPGGELHWEGNGPHHDRCCTYNEDNLVDGVYCLPVGHWIEATGHTNEMKHTTDFYFNIAGHQAMHYSRILPNIWLGSCPRQLEHVTIKLKHELGVTAVMNFQTEWDIIQNSSGCNRYPEPMTPDTMMKLYKEEGLSYIWMPTPDMSTEGRVQMLPQAVCLLHALLENGHTVYVHCNAGVGRSTAAVCGWLHYVIGWNLRKVQYFIMAKRPAVYIDEDALAQAQQDFSQKFGKVHSSICAL