NUDT3

NUDT3
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2FVV, 2Q9P
Identifiers
Aliases	NUDT3, DIPP, DIPP-1, DIPP1, nudix hydrolase 3
External IDs	OMIM: 609228 MGI: 1928484 HomoloGene: 31400 GeneCards: NUDT3
Gene location (Human) Chr. Chromosome 6 (human) Band 6p21.31 Start 34,279,679 bp End 34,392,669 bp
Gene location (Mouse) Chr. Chromosome 17 (mouse) Band 17|17 A3.3 Start 27,798,356 bp End 27,842,469 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in inferior olivary nucleus postcentral gyrus Brodmann area 46 Brodmann area 10 middle frontal gyrus Region I of hippocampus proper external globus pallidus entorhinal cortex internal globus pallidus frontal pole Top expressed in entorhinal cortex superior frontal gyrus cingulate gyrus primary motor cortex prefrontal cortex hippocampus proper cerebellar cortex superior colliculus ganglionic eminence blood More reference expression data BioGPS More reference expression data
Gene ontology Molecular function inositol-3-diphosphate-1,2,4,5,6-pentakisphosphate diphosphatase activity inositol diphosphate tetrakisphosphate diphosphatase activity inositol-3,5-bisdiphosphate-2,3,4,6-tetrakisphosphate 5-diphosphatase activity hydrolase activity diphosphoinositol-polyphosphate diphosphatase activity inositol-5-diphosphate-1,2,3,4,6-pentakisphosphate diphosphatase activity metal ion binding inositol-1,5-bisdiphosphate-2,3,4,6-tetrakisphosphate 1-diphosphatase activity inositol-1,5-bisdiphosphate-2,3,4,6-tetrakisphosphate 5-diphosphatase activity magnesium ion binding inositol-1-diphosphate-2,3,4,5,6-pentakisphosphate diphosphatase activity inositol diphosphate pentakisphosphate diphosphatase activity inositol bisdiphosphate tetrakisphosphate diphosphatase activity endopolyphosphatase activity bis(5'-adenosyl)-hexaphosphatase activity bis(5'-adenosyl)-pentaphosphatase activity m7G(5')pppN diphosphatase activity Cellular component nucleus cytoplasm cytosol Biological process cell-cell signaling diadenosine polyphosphate catabolic process inositol phosphate metabolic process diphosphoinositol polyphosphate catabolic process diadenosine pentaphosphate catabolic process diadenosine hexaphosphate catabolic process adenosine 5'-(hexahydrogen pentaphosphate) catabolic process diphosphoinositol polyphosphate metabolic process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 11165 56409 Ensembl ENSG00000272325 ENSMUSG00000024213 UniProt O95989 Q9JI46 RefSeq (mRNA) NM_006703 NM_001291046 NM_019837 RefSeq (protein) NP_006694 NP_001277975 NP_062811 Location (UCSC) Chr 6: 34.28 – 34.39 Mb Chr 17: 27.8 – 27.84 Mb PubMed search
Wikidata
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Diphosphoinositol polyphosphate phosphohydrolase 1 is an enzyme that in humans is encoded by the NUDT3 gene.

NUDT3 belongs to the MutT, or Nudix, protein family. Nudix proteins act as homeostatic checkpoints at important stages in nucleoside phosphate metabolic pathways, guarding against elevated levels of potentially dangerous intermediates, like 8-oxo-dGTP, which promotes AT-to-CG transversions (Safrany et al., 1998).[supplied by OMIM]

Further reading

• Safrany ST, Ingram SW, Cartwright JL, et al. (1999). "The diadenosine hexaphosphate hydrolases from Schizosaccharomyces pombe and Saccharomyces cerevisiae are homologues of the human diphosphoinositol polyphosphate phosphohydrolase. Overlapping substrate specificities in a MutT-type protein". J. Biol. Chem. 274 (31): 21735–40. doi:10.1074/jbc.274.31.21735. PMID 10419486.
• Yang X, Safrany ST, Shears SB (2000). "Site-directed mutagenesis of diphosphoinositol polyphosphate phosphohydrolase, a dual specificity NUDT enzyme that attacks diadenosine polyphosphates and diphosphoinositol polyphosphates". J. Biol. Chem. 274 (50): 35434–40. doi:10.1074/jbc.274.50.35434. PMID 10585413.
• Fisher DI, Safrany ST, Strike P, et al. (2003). "Nudix hydrolases that degrade dinucleoside and diphosphoinositol polyphosphates also have 5-phosphoribosyl 1-pyrophosphate (PRPP) pyrophosphatase activity that generates the glycolytic activator ribose 1,5-bisphosphate". J. Biol. Chem. 277 (49): 47313–7. doi:10.1074/jbc.M209795200. PMID 12370170.
• 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.
• Mungall AJ, Palmer SA, Sims SK, et al. (2003). "The DNA sequence and analysis of human chromosome 6". Nature. 425 (6960): 805–11. Bibcode:2003Natur.425..805M. doi:10.1038/nature02055. PMID 14574404.
• 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.
• Stelzl U, Worm U, Lalowski M, et al. (2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell. 122 (6): 957–68. doi:10.1016/j.cell.2005.08.029. hdl:11858/00-001M-0000-0010-8592-0. PMID 16169070. S2CID 8235923.
• 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.