RPE (gene)

Ribulose-5-phosphate-3-epimerase
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 3OVP​, 3OVQ​, 3OVR​, 3QC3​
Identifiers
Symbols	RPE ; RPE2-1
External IDs	OMIM: 180480 MGI: 1913896 HomoloGene: 12005 GeneCards: RPE Gene
EC number	5.1.3.1
Gene ontology Molecular function • ribulose-phosphate 3-epimerase activity • identical protein binding • protein homodimerization activity • metal ion binding Cellular component • cytosol • extracellular exosome Biological process • carbohydrate metabolic process • pentose-phosphate shunt • pentose-phosphate shunt, non-oxidative branch • pentose catabolic process • cellular carbohydrate metabolic process • small molecule metabolic process Sources: Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	6120	66646
Ensembl	ENSG00000197713	ENSMUSG00000026005
UniProt	Q96AT9	Q8VEE0
RefSeq (mRNA)	NM_001278282	NM_025683
RefSeq (protein)	NP_001265211	NP_079959
Location (UCSC)	Chr 2: 210 – 210.02 Mb	Chr 1: 66.7 – 66.72 Mb
PubMed search

Ribulose-phosphate 3-epimerase is an enzyme that in humans is encoded by the RPE gene.^[1]

References

1. "Entrez Gene: RPE ribulose-5-phosphate-3-epimerase".

Further reading

• Boss GR, Pilz RB (1985). "Phosphoribosylpyrophosphate synthesis from glucose decreases during amino acid starvation of human lymphoblasts.". J. Biol. Chem. 260 (10): 6054–9. PMID 2581946.
• Miyazaki K, Yamanaka T, Ogasawara N (1989). "Interstitial deletion 2q32.1----q34 in a child with half normal activity of ribulose 5-phosphate 3-epimerase (RPE).". J. Med. Genet. 25 (12): 850–1. doi:10.1136/jmg.25.12.850. PMC 1051616. PMID 3236368.
• Dallapiccola B, Novelli G, Giannotti A (1988). "Deletion 2q31.3----2q33.3: gene dosage effect of ribulose 5-phosphate 3-epimerase.". Hum. Genet. 79 (1): 92. doi:10.1007/BF00291721. PMID 3366467.
• Spencer N, Hopkinson DA (1980). "Biochemical genetics of the pentose phosphate cycle: human ribose 5-phosphate isomerase (RPI) and ribulose 5-phosphate 3-epimerase (RPE).". Ann. Hum. Genet. 43 (4): 335–42. doi:10.1111/j.1469-1809.1980.tb01567.x. PMID 7396409.
• Stanchi F, Bertocco E, Toppo S, et al. (2001). "Characterization of 16 novel human genes showing high similarity to yeast sequences.". Yeast 18 (1): 69–80. doi:10.1002/1097-0061(200101)18:1<69::AID-YEA647>3.0.CO;2-H. PMID 11124703.
• 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. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• 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.
• 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.
• 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.
• Krull M, Brosius J, Schmitz J (2005). "Alu-SINE exonization: en route to protein-coding function.". Mol. Biol. Evol. 22 (8): 1702–11. doi:10.1093/molbev/msi164. PMID 15901843.
• 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. doi:10.1038/nature04209. PMID 16189514.