Epm2a
entrez
13853
canonical
uniprot
Q9WUA5
canonical
ensembl
ENSMUSG00000055493
resolver
ensp
ENSMUSP00000066050
resolver
enst
ENSMUST00000069106
resolver
genesymbol
Epm2a
resolver
uniprot
G5E8E2
resolver
uniprot
Q8BY80
resolver
uniprot_entry
EPM2A_MOUSE
resolver
uniprot_sec
G5E8E2
resolver
uniprot_sec
Q8BY80
resolver
amino_acid_sequence
MLFRFGVVVPPAVAGARQELLLAGSRPELGRWEPHGAVRLRPAGTAAGAAALALQEPGLWLAEVELEAYEEAGGAEPGRVDTFWYKFLQREPGGELHWEGNGPHHDRCCTYNEDNLVDGVYCLPVGHWIEATGHTNEMKHTTDFYFNIAGHQAMHYSRILPNIWLGSCPRQLEHVTIKLKHELGVTAVMNFQTEWDIIQNSSGCNRYPEPMTPDTMMKLYKEEGLSYIWMPTPDMSTEGRVQMLPQAVCLLHALLENGHTVYVHCNAGVGRSTAAVCGWLHYVIGWNLRKVQYFIMAKRPAVYIDEDALAQAQQDFSQKFGKVHSSICAL
uniprot
proteins
ec_number
3.1.3.-
uniprot
proteins
ec_number
3.1.3.16
uniprot
proteins
ec_number
3.1.3.48
uniprot
proteins
function
FUNCTION: 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:24068615, PubMed:24430976). 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). {ECO:0000269|PubMed:16971387, ECO:0000269|PubMed:18040046, ECO:0000269|PubMed:18852261, ECO:0000269|PubMed:19036738, ECO:0000269|PubMed:19542233, ECO:0000269|PubMed:20453062, ECO:0000269|PubMed:22669944, ECO:0000269|PubMed:23663739, ECO:0000269|PubMed:24068615, ECO:0000269|PubMed:24430976}.
uniprot
proteins
mass_dalton
36958
uniprot
proteins
mutagenesis
MUTAGEN 32; /note="W->G: Loss of glycogen phosphatase activity. Nearly abolishes phosphatase activity."; /evidence="ECO:0000269|PubMed:16971387, ECO:0000269|PubMed:18040046"; MUTAGEN 83; /note="F->L: Abolishes phosphatase activity."; /evidence="ECO:0000269|PubMed:16971387"; MUTAGEN 107; /note="R->C: Abolishes phosphatase activity."; /evidence="ECO:0000269|PubMed:16971387"; MUTAGEN 193; /note="T->I: Nearly abolishes phosphatase activity."; /evidence="ECO:0000269|PubMed:16971387"; MUTAGEN 265; /note="C->S: Loss of phosphatase activity with glycogen and synthetic substrates."; /evidence="ECO:0000269|PubMed:16971387, ECO:0000269|PubMed:18040046, ECO:0000269|PubMed:24430976"; MUTAGEN 292; /note="Q->L: Abolishes phosphatase activity."; /evidence="ECO:0000269|PubMed:16971387"; MUTAGEN 293; /note="Y->N: Nearly abolishes phosphatase activity."; /evidence="ECO:0000269|PubMed:16971387"; MUTAGEN 300; /note="P->L: Abolishes phosphatase activity."; /evidence="ECO:0000269|PubMed:16971387
uniprot
proteins
post_translational_modification
PTM: Polyubiquitinated by NHLRC1/malin. {ECO:0000250|UniProtKB:O95278}.; PTM: Phosphorylation on Ser-25 by AMPK affects the phosphatase activity of the enzyme and its ability to homodimerize and interact with NHLRC1, PPP1R3C or PRKAA2. {ECO:0000250|UniProtKB:O95278}.
uniprot
proteins
protein_family
Protein-tyrosine phosphatase family
uniprot
proteins
pubmed
10092504
uniprot
proteins
pubmed
11355878
uniprot
proteins
pubmed
12019206
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
16971387
uniprot
proteins
pubmed
18040046
uniprot
proteins
pubmed
18852261
uniprot
proteins
pubmed
19036738
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
19542233
uniprot
proteins
pubmed
20453062
uniprot
proteins
pubmed
22669944
uniprot
proteins
pubmed
23624058
uniprot
proteins
pubmed
23663739
uniprot
proteins
pubmed
24068615
uniprot
proteins
pubmed
24430976
uniprot
proteins
sequence_length
330
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O95278}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O95278}; Peripheral membrane protein {ECO:0000250|UniProtKB:O95278}; Cytoplasmic side {ECO:0000250|UniProtKB:O95278}. Cell membrane {ECO:0000250|UniProtKB:O95278}. Note=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. Under glycogenolytic conditions localizes to the nucleus. {ECO:0000250|UniProtKB:O95278}.
uniprot
proteins