NUDT3

From Wikipedia, the free encyclopedia

Nudix (nucleoside diphosphate linked moiety X)-type motif 3

PDB rendering based on 2fvv.

Available structures: 2fvv

Identifiers

Symbol(s)

NUDT3; DIPP; DIPP1

External IDs

OMIM: 609228 MGI: 1928484 HomoloGene: 31400

Gene ontology
Molecular Function:	• magnesium ion binding • diphosphoinositol-polyphosphate diphosphatase activity • hydrolase activity
Biological Process:	• cell-cell signaling • diadenosine polyphosphate catabolic process

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_006703 (mRNA)
NP_006694 (protein)

XM_992328 (mRNA)
XP_997422 (protein)

Location

Chr 6: 34.36 - 34.47 Mb

Chr 17: 27.31 - 27.35 Mb

Pubmed search

[1]

[2]

Nudix (nucleoside diphosphate linked moiety X)-type motif 3, also known as NUDT3, is a human gene.^[1]

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]^[1]

[edit] References

^ ^a ^b Entrez Gene: NUDT3 nudix (nucleoside diphosphate linked moiety X)-type motif 3.

[edit] Further reading

Safrany ST, Caffrey JJ, Yang X, et al. (1999). "A novel context for the 'MutT' module, a guardian of cell integrity, in a diphosphoinositol polyphosphate phosphohydrolase.". EMBO J. 17 (22): 6599-607. doi:10.1093/emboj/17.22.6599. PMID 9822604.
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. 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. 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. doi:10.1073/pnas.242603899. 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. 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. 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. PMID 16169070.
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.