Pgp
entrez
67078
canonical
uniprot
Q8CHP8
canonical
ensembl
ENSMUSG00000043445
resolver
ensp
ENSMUSP00000052866
resolver
enst
ENSMUST00000053024
resolver
genesymbol
Pgp
resolver
uniprot_entry
PGP_MOUSE
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by orthovanadate, beryllium trifluoride, Ca(2+) and EDTA (PubMed:24338473). Inhibited by reversible oxidation in response to EGFR activation which induces conformational changes (PubMed:27179418). {ECO:0000269|PubMed:24338473, ECO:0000269|PubMed:27179418}.
uniprot
proteins
amino_acid_sequence
MAEAEAGGDEARCVRLSAERAKLLLAEVDTLLFDCDGVLWRGETAVPGAPETLRALRARGKRLGFITNNSSKTRTAYAEKLRRLGFGGPVGPEAGLEVFGTAYCSALYLRQRLAGVPDPKAYVLGSPALAAELEAVGVTSVGVGPDVLHGDGPSDWLAVPLEPDVRAVVVGFDPHFSYMKLTKAVRYLQQPDCLLVGTNMDNRLPLENGRFIAGTGCLVRAVEMAAQRQADIIGKPSRFIFDCVSQEYGINPERTVMVGDRLDTDILLGSTCSLKTILTLTGVSSLEDVKSNQESDCMFKKKMVPDFYVDSIADLLPALQG
uniprot
proteins
ec_number
3.1.3.18
uniprot
proteins
ec_number
3.1.3.21
uniprot
proteins
ec_number
3.1.3.48
uniprot
proteins
function
FUNCTION: Phosphatase with activity against multiple substrates (PubMed:27294321). Acts as a metabolite repair enzyme which eliminates toxic glycolytic side products (PubMed:27294321). Dephosphorylates 2-phosphoglycolate which is generated during the repair of oxidative DNA lesions (PubMed:27179418, PubMed:27294321, PubMed:27731369). This controls triosephosphate isomerase activity, glycerolipid partitioning and cell proliferation in the embryo and is required for embryonic development (PubMed:27731369). Dephosphorylates 4-phosphoerythronate, a side product which is produced by GAPDH and which inhibits 6-phosphogluconate dehydrogenase (PubMed:27294321). Dephosphorylation of 4-phosphoerythronate prevents the accumulation of high 4-phosphoerythronate levels which would otherwise inhibit the pentose phosphate pathway (By similarity). Dephosphorylates 2-phospho-L-lactate which is a product of a pyruvate kinase side reaction (PubMed:27294321). This prevents the inhibition of fructose-2,6-bisphosphate production and allows glycolysis to occur (By similarity). Has glycerol-3-phosphate phosphatase activity, hydrolyzing glycerol-3-phosphate into glycerol and thereby regulating the cellular levels of glycerol-3-phosphate, a metabolic intermediate of glucose, lipid and energy metabolism (PubMed:26755581). Has been shown to have tyrosine-protein phosphatase activity although the physiological relevance is unclear (PubMed:26755581). In vitro, has phosphatase activity toward ADP, ATP, GDP and GTP (PubMed:24338473). {ECO:0000250|UniProtKB:A6NDG6, ECO:0000269|PubMed:24338473, ECO:0000269|PubMed:26755581, ECO:0000269|PubMed:27179418, ECO:0000269|PubMed:27294321, ECO:0000269|PubMed:27731369}.
uniprot
proteins
mass_dalton
34541
uniprot
proteins
mutagenesis
MUTAGEN 13; /note="C->S: Reduces basal activity."; /evidence="ECO:0000269|PubMed:27179418"; MUTAGEN 34; /note="D->N: Abolishes tyrosine-protein phosphatase activity. Abolishes phosphoglycolate phosphatase activity."; /evidence="ECO:0000269|PubMed:24338473, ECO:0000269|PubMed:27179418"; MUTAGEN 35; /note="C->S: Reduces basal activity."; /evidence="ECO:0000269|PubMed:27179418"; MUTAGEN 41; /note="R->N: Slightly increases phosphatase activity with p-nitrophenylphosphate; when associated with R-44 and I-45."; /evidence="ECO:0000269|PubMed:24338473"; MUTAGEN 44; /note="T->R: Slightly increases phosphatase activity with p-nitrophenylphosphate; when associated with N-41 and I-45."; /evidence="ECO:0000269|PubMed:24338473"; MUTAGEN 45; /note="A->I: Slightly increases phosphatase activity with p-nitrophenylphosphate; when associated with N-41 and R-44."; /evidence="ECO:0000269|PubMed:24338473"; MUTAGEN 67; /note="T->S: Strongly reduces phosphatase activity; when associated with R-71; R-72 and A-73. Abolishes phosphatase activity; when associated with R-72 and A-73."; /evidence="ECO:0000269|PubMed:24338473"; MUTAGEN 71; /note="S->R: Mildly reduces phosphatase activity; when associated with R-72 and A-73. Strongly reduces phosphatase activity; when associated with S-67; R-72 and A-73."; /evidence="ECO:0000269|PubMed:24338473"; MUTAGEN 72; /note="K->R: Mildly reduces phosphatase activity; when associated with R-71 and A-73. Strongly reduces phosphatase activity; when associated with S-67; R-71 and A-73. Abolishes phosphatase activity; when associated with S-67 and A-73."; /evidence="ECO:0000269|PubMed:24338473"; MUTAGEN 73; /note="T->A: Abolishes phosphatase activity. Abolishes phosphatase activity; when associated with S-67 and R-72. Strongly reduces phosphatase activity; when associated with S-67; R-71 and R-72. Mildly reduces phosphatase activity; when associated with R-71 and R-72."; /evidence="ECO:0000269|PubMed:24338473"; MUTAGEN 104; /note="C->S: Increases basal activity. Desensitizes protein to oxidation-mediated inhibition."; /evidence="ECO:0000269|PubMed:27179418"; MUTAGEN 193; /note="C->S: Reduces basal activity."; /evidence="ECO:0000269|PubMed:27179418"; MUTAGEN 204; /note="L->H: Strongly increases activity with pyridoxal phosphate."; /evidence="ECO:0000269|PubMed:24338473"; MUTAGEN 217; /note="C->S: Reduces basal activity. No effect on oligomerization."; /evidence="ECO:0000269|PubMed:27179418"; MUTAGEN 243; /note="C->S: Reduces basal activity. Desensitizes protein to oxidation-mediated inhibition."; /evidence="ECO:0000269|PubMed:27179418"; MUTAGEN 272; /note="C->S: Reduces basal activity."; /evidence="ECO:0000269|PubMed:27179418"; MUTAGEN 297; /note="C->S: Reduces basal activity. Abolishes tetramerization."; /evidence="ECO:0000269|PubMed:27179418
uniprot
proteins
protein_family
CbbY/CbbZ/Gph/YieH family
uniprot
proteins
protein_family
HAD-like hydrolase superfamily
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
24338473
uniprot
proteins
pubmed
26755581
uniprot
proteins
pubmed
27179418
uniprot
proteins
pubmed
27294321
uniprot
proteins
pubmed
27731369
uniprot
proteins
pubmed
36369173
uniprot
proteins
sequence_length
321
uniprot
proteins