Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on curation of intracellular localizations of expressed fusion proteins in living cells
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Automatic Gene Ontology annotation based on Rhea mapping
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
The gene encoding hydroxypyruvate reductase (GRHPR) is mutated in patients with primary hyperoxaluria type II.
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GRHPR encodes the enzyme that reduces hydroxypyruvate to D-glycerate, reduces glyoxylate to glycolate, and oxidizes D-glycerate; its deficiency causes primary hyperoxaluria type 2 with elevated urinary oxalate and L-glycerate.
"characterized by a lack of the enzyme that catalyzes the reduction of hydroxypyruvate to D-glycerate, the reduction of glyoxylate to glycolate and the oxidation of D-glycerate to hydroxypyruvate"
Identification and expression of a cDNA for human hydroxypyruvate/glyoxylate reductase.
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Cloning and expression of the human liver GRHPR (GLXR) cDNA showed the 328-residue protein has glyoxylate and hydroxypyruvate reductase activities.
"a human liver cDNA encoding a 40-kDa protein with glyoxylate and hydroxypyruvate reductase activities"
Structural basis of substrate specificity in human glyoxylate reductase/hydroxypyruvate reductase.
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Crystal structure of human GRHPR shows a homodimer that binds NADPH and substrate; the enzyme prefers glyoxylate and hydroxypyruvate but not pyruvate, with Trp141 from the neighbouring subunit shaping specificity.
"A tryptophan residue (Trp141) from the neighbouring subunit of the dimer is projected into the active site region and appears to contribute to the selectivity for hydroxypyruvate."
A novel mutation in the GRHPR gene in a Japanese patient with primary hyperoxaluria type 2.
Large-scale proteomics and phosphoproteomics of urinary exosomes.
MHC class II-associated proteins in B-cell exosomes and potential functional implications for exosome biogenesis.
In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine.
Glyoxalate reductase/hydroxypyruvate reductase interacts with the sodium-dependent vitamin C transporter-1 to regulate cellular vitamin C homeostasis.
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GRHPR physically interacts with the sodium-dependent vitamin C transporter SLC23A1 (hSVCT1), and this interaction modulates ascorbate uptake, coupling vitamin C transport to control of cellular oxalate production.
"we identify the enzyme human glyoxalate reductase/hydroxypyruvate reductase (hGR/HPR) as an hSVCT1 associated protein by yeast two-hybrid (Y2H) screening of a human liver cDNA library"
Quantitative high-confidence human mitochondrial proteome and its dynamics in cellular context.
glyoxylate + NADPH + H+ => glycolate + NADP+
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Reactome describes GRHPR catalyzing the NADPH-dependent reduction of glyoxylate to glycolate; it labels the enzyme peroxisomal and links its mutations to primary hyperoxaluria type II.
"Peroxisomal GRHPR catalyzes the reaction of glyoxylate and NADPH + H+ to form glycolate and NADP+."
UniProt entry GRHPR_HUMAN (Q9UBQ7)
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UniProt records GRHPR as a hydroxypyruvate reductase, glyoxylate reductase and D-glycerate dehydrogenase (EC 1.1.1.79, EC 1.1.1.81), a homodimer of the D-isomer specific 2-hydroxyacid dehydrogenase family, most abundant in liver, whose deficiency causes primary hyperoxaluria type 2.
"hydroxypyruvate to D-glycerate, glyoxylate to glycolate"