Overview
| Uniprot ID | A6NDG6 |
|---|
| Protein Name | Phosphoglycolate phosphatase |
|---|
| Gene Name | PGP |
|---|
| Organism | Homo sapiens |
|---|
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 290 |
VSTLGDVKNNQESDC |
| 72 |
FITNNSSKTRAAYAE |
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:26755581, PubMed:27294321). This controls triosephosphate isomerase activity, glycerolipid partitioning and cell proliferation in the embryo and is required for embryonic development (By similarity). 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 (PubMed:27294321). 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 (PubMed:27294321). 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 (By similarity)
Protein Sequence
10
MAAAEAGGDD
20
ARCVRLSAER
30
AQALLADVDT
40
LLFDCDGVLW
50
RGETAVPGAP
60
EALRALRARG
70
KRLGFITNNS
80
SKTRAAYAEK
90
LRRLGFGGPA
100
GPGASLEVFG
110
TAYCTALYLR
120
QRLAGAPAPK
130
AYVLGSPALA
140
AELEAVGVAS
150
VGVGPEPLQG
160
EGPGDWLHAP
170
LEPDVRAVVV
180
GFDPHFSYMK
190
LTKALRYLQQ
200
PGCLLVGTNM
210
DNRLPLENGR
220
FIAGTGCLVR
230
AVEMAAQRQA
240
DIIGKPSRFI
250
FDCVSQEYGI
260
NPERTVMVGD
270
RLDTDILLGA
280
TCGLKTILTL
290
TGVSTLGDVK
300
NNQESDCVSK
310
KKMVPDFYVD
320
SIADLLPALQ
G
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0005737 |
cytoplasm |
| Cellular Component |
GO:0005829 |
cytosol |
| Molecular Function |
GO:0043262 |
ADP phosphatase activity |
| Molecular Function |
GO:0000287 |
magnesium ion binding |
| Molecular Function |
GO:0008967 |
phosphoglycolate phosphatase activity |
| Molecular Function |
GO:0004725 |
protein tyrosine phosphatase activity |
| Molecular Function |
GO:0000121 |
sn-glycerol 1-phosphatase activity |
| Molecular Function |
GO:0043136 |
sn-glycerol 3-phosphatase activity |
| Biological Process |
GO:0006114 |
glycerol biosynthetic process |
| Biological Process |
GO:0006650 |
glycerophospholipid metabolic process |
| Biological Process |
GO:0045721 |
negative regulation of gluconeogenesis |
| Biological Process |
GO:0110052 |
toxic metabolite repair |
Reference
[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.