DPYS

DPYS
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2VR2
Identifiers
Aliases	DPYS , dihydropyrimidinase, DHP, DHPase
External IDs	OMIM: 613326 MGI: 1928679 HomoloGene: 20359 GeneCards: DPYS
Gene location (Human) Chr. Chromosome 8 (human) [1] Band 8q22.3 Start 104,330,324 bp [1] End 104,467,055 bp [1]
Gene location (Mouse) Chr. Chromosome 15 (mouse) [2] Band 15|15 B3.1 Start 39,631,883 bp [2] End 39,720,866 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in right lobe of liver kidney tubule kidney glomerulus metanephric glomerulus gallbladder renal medulla parietal pleura germinal epithelium prefrontal cortex Top expressed in left lobe of liver proximal tubule respiratory epithelium olfactory epithelium secondary oocyte spermatid sexually immature organism spermatocyte kidney mirror More reference expression data BioGPS More reference expression data
Gene ontology Molecular function amino acid binding zinc ion binding metal ion binding dihydropyrimidinase activity phosphoprotein binding hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds thymine binding uracil binding hydrolase activity Cellular component cytoplasm cytosol extracellular exosome Biological process beta-alanine metabolic process uracil catabolic process pyrimidine nucleoside catabolic process uracil metabolic process pyrimidine nucleobase catabolic process protein homooligomerization protein homotetramerization thymine catabolic process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 1807 64705 Ensembl ENSG00000147647 ENSMUSG00000022304 UniProt Q14117 Q9EQF5 RefSeq (mRNA) NM_001385 NM_001164466 NM_022722 RefSeq (protein) NP_001376 NP_001157938 NP_073559 Location (UCSC) Chr 8: 104.33 – 104.47 Mb Chr 15: 39.63 – 39.72 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Dihydropyrimidinase is an enzyme that in humans is encoded by the DPYS gene. ^{[5] [6]}

Dihydropyrimidinase catalyzes the conversion of 5,6-dihydrouracil to 3-ureidopropionate in pyrimidine metabolism. Dihydropyrimidinase is expressed at a high level in liver and kidney as a major 2.5-kb transcript and a minor 3.8-kb transcript. Defects in the DPYS gene are linked to dihydropyrimidinuria. ^[6]

Interactive pathway map

Click on genes, proteins and metabolites below to link to respective articles. ^{[§ 1]}

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|alt=Fluorouracil (5-FU) Activity edit]]

Fluorouracil (5-FU) Activity edit

1. The interactive pathway map can be edited at WikiPathways: "FluoropyrimidineActivity_WP1601".

References

1. GRCh38: Ensembl release 89: ENSG00000147647 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000022304 - 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. Hamajima N, Matsuda K, Sakata S, Tamaki N, Sasaki M, Nonaka M (Jan 1997). "A novel gene family defined by human dihydropyrimidinase and three related proteins with differential tissue distribution". Gene. 180 (1–2): 157–63. doi:10.1016/S0378-1119(96)00445-3. PMID   8973361.
6. "Entrez Gene: DPYS dihydropyrimidinase".

Further reading

• Thomas HR, Ezzeldin HH, Guarcello V, et al. (2008). "Genetic regulation of beta-ureidopropionase and its possible implication in altered uracil catabolism". Pharmacogenet. Genomics. 18 (1): 25–35. doi:10.1097/FPC.0b013e3282f2f134. PMID   18216719. S2CID   10940058.
• Thomas HR, Ezzeldin HH, Guarcello V, et al. (2008). "Genetic regulation of dihydropyrimidinase and its possible implication in altered uracil catabolism". Pharmacogenet. Genomics. 17 (11): 973–87. doi:10.1097/FPC.0b013e3282f01788. PMID   18075467. S2CID   23490646.
• van Kuilenburg AB, Meijer J, Dobritzsch D, et al. (2007). "Clinical, biochemical and genetic findings in two siblings with a dihydropyrimidinase deficiency". Mol. Genet. Metab. 91 (2): 157–64. doi:10.1016/j.ymgme.2007.02.008. PMID   17383919.
• Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID   16189514. S2CID   4427026.
• 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.
• 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.
• Fukada M, Watakabe I, Yuasa-Kawada J, et al. (2001). "Molecular characterization of CRMP5, a novel member of the collapsin response mediator protein family". J. Biol. Chem. 275 (48): 37957–65. doi: 10.1074/jbc.M003277200 . PMID   10956643.
• Hamajima N, Kouwaki M, Vreken P, et al. (1998). "Dihydropyrimidinase deficiency: structural organization, chromosomal localization, and mutation analysis of the human dihydropyrimidinase gene". Am. J. Hum. Genet. 63 (3): 717–26. doi:10.1086/302022. PMC   1377410 . PMID   9718352.
• Naguib FN, el Kouni MH, Cha S (1985). "Enzymes of uracil catabolism in normal and neoplastic human tissues". Cancer Res. 45 (11 Pt 1): 5405–12. PMID   3931905.