GRHPR

GRHPR
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2GCG, 2H1S, 2Q50, 2WWR
Identifiers
Aliases	GRHPR , GLXR, GLYD, PH2, glyoxylate reductase/hydroxypyruvate reductase, glyoxylate and hydroxypyruvate reductase
External IDs	OMIM: 604296; MGI: 1923488; HomoloGene: 49088; GeneCards: GRHPR; OMA:GRHPR - orthologs
Gene location (Human) Chr. Chromosome 9 (human) [1] Band 9p13.2 Start 37,422,666 bp [1] End 37,436,990 bp [1]
Gene location (Mouse) Chr. Chromosome 4 (mouse) [2] Band 4|4 B1 Start 44,981,395 bp [2] End 44,990,734 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in right lobe of liver right adrenal gland left adrenal gland right adrenal cortex left adrenal cortex tendon of biceps brachii human kidney muscle of thigh apex of heart C1 segment Top expressed in left lobe of liver right kidney proximal tubule Ileal epithelium human kidney adrenal gland yolk sac cumulus cell epithelium of stomach brown adipose tissue More reference expression data BioGPS More reference expression data
Gene ontology Molecular function glycerate dehydrogenase activity oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor protein homodimerization activity NAD binding carboxylic acid binding NADP binding NADPH binding oxidoreductase activity hydroxypyruvate reductase activity glyoxylate reductase (NADP+) activity Cellular component cytoplasm peroxisomal matrix extracellular exosome cytosol Biological process dicarboxylic acid metabolic process excretion protein complex oligomerization metabolism cellular nitrogen compound metabolic process glyoxylate metabolic process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 9380 76238 Ensembl ENSG00000137106 ENSMUSG00000035637 UniProt Q9UBQ7 Q91Z53 RefSeq (mRNA) NM_012203 NM_080289 NM_001312880 RefSeq (protein) NP_036335 NP_001299809 NP_525028 Location (UCSC) Chr 9: 37.42 – 37.44 Mb Chr 4: 44.98 – 44.99 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Glyoxylate reductase/hydroxypyruvate reductase is an enzyme that in humans is encoded by the GRHPR gene. ^{[5] [6] [7]}

This gene encodes an enzyme with hydroxypyruvate reductase, glyoxylate reductase, and D-glycerate dehydrogenase enzymatic activities. The enzyme has widespread tissue expression and has a role in metabolism. Type II hyperoxaluria is caused by mutations in this gene. ^[7] GRHPR mutation analysis needs to pay attention to primer design, because allele dropout can cause false-positive result. ^[8]

References

1. GRCh38: Ensembl release 89: ENSG00000137106 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000035637 – Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Rumsby G, Cregeen DP (Nov 1999). "Identification and expression of a cDNA for human hydroxypyruvate/glyoxylate reductase". Biochim Biophys Acta. 1446 (3): 383–8. doi:10.1016/S0167-4781(99)00105-0. PMID   10524214.
6. Cramer SD, Ferree PM, Lin K, Milliner DS, Holmes RP (Dec 1999). "The gene encoding hydroxypyruvate reductase (GRHPR) is mutated in patients with primary hyperoxaluria type II". Hum Mol Genet. 8 (11): 2063–9. doi:10.1093/hmg/8.11.2063. PMID   10484776.
7. "Entrez Gene: GRHPR glyoxylate reductase/hydroxypyruvate reductase".
8. Takaoka N, Takayama T, Miyazaki M, Nagata M, Ozono S (Dec 2008). "Modification of primers for GRHPR genotyping: avoiding allele dropout by single nucleotide polymorphisms and homology sequence". Urol Res. 36 (6): 297–302. doi:10.1007/s00240-008-0159-z. PMID   18982322. S2CID   12234158.

External links

• GeneReviews/NCBI/NIH/UW entry on Primary Hyperoxaluria Type 2

Further reading

• Takayama T, Nagata M, Ozono S, et al. (2007). "A novel mutation in the GRHPR gene in a Japanese patient with primary hyperoxaluria type 2". Nephrol. Dial. Transplant. 22 (8): 2371–4. doi:10.1093/ndt/gfm271. PMC   2413148 . PMID   17510093.
• Booth MP, Conners R, Rumsby G, Brady RL (2006). "Structural basis of substrate specificity in human glyoxylate reductase/hydroxypyruvate reductase". J. Mol. Biol. 360 (1): 178–89. doi:10.1016/j.jmb.2006.05.018. PMID   16756993.
• Mehrle A, Rosenfelder H, Schupp I, et al. (2006). "The LIFEdb database in 2006". Nucleic Acids Res. 34 (Database issue): D415–8. doi:10.1093/nar/gkj139. PMC   1347501 . PMID   16381901.
• Wiemann S, Arlt D, Huber W, et al. (2004). "From ORFeome to Biology: A Functional Genomics Pipeline". Genome Res. 14 (10B): 2136–44. doi:10.1101/gr.2576704. PMC   528930 . PMID   15489336.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC   528928 . PMID   15489334.
• Lehner B, Sanderson CM (2004). "A Protein Interaction Framework for Human mRNA Degradation". Genome Res. 14 (7): 1315–23. doi:10.1101/gr.2122004. PMC   442147 . PMID   15231747.
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi: 10.1038/ng1285 . PMID   14702039.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi: 10.1073/pnas.242603899 . PMC   139241 . PMID   12477932.
• Simpson JC, Wellenreuther R, Poustka A, et al. (2001). "Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing". EMBO Rep. 1 (3): 287–92. doi:10.1093/embo-reports/kvd058. PMC   1083732 . PMID   11256614.
• Hartley JL, Temple GF, Brasch MA (2001). "DNA Cloning Using In Vitro Site-Specific Recombination". Genome Res. 10 (11): 1788–95. doi:10.1101/gr.143000. PMC   310948 . PMID   11076863.
• Webster KE, Ferree PM, Holmes RP, Cramer SD (2000). "Identification of missense, nonsense, and deletion mutations in the GRHPR gene in patients with primary hyperoxaluria type II (PH2)". Hum. Genet. 107 (2): 176–85. doi:10.1007/s004390000351. PMID   11030416. S2CID   10574729.
• Huang T, Yang W, Pereira AC, et al. (2000). "Cloning and characterization of a putative human d-2-hydroxyacid dehydrogenase in chromosome 9q". Biochem. Biophys. Res. Commun. 268 (2): 298–301. doi:10.1006/bbrc.2000.2122. PMID   10679197.