NUDT4

From Wikipedia, the free encyclopedia

Nudix (nucleoside diphosphate linked moiety X)-type motif 4

PDB rendering based on 2duk.

Available structures: 2duk

Identifiers

Symbol(s)

NUDT4; DIPP2; DIPP2alpha; DIPP2beta; DKFZp686I1281; HDCMB47P; KIAA0487

External IDs

OMIM: 609229 MGI: 1918457 HomoloGene: 41726

Gene ontology
Molecular Function:	• magnesium ion binding • diphosphoinositol-polyphosphate diphosphatase activity • hydrolase activity • manganese ion binding
Cellular Component:	• intracellular
Biological Process:	• intracellular signaling cascade • cyclic nucleotide metabolic process • calcium-mediated signaling • cyclic-nucleotide-mediated signaling • regulation of RNA export from nucleus • intracellular transport

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_019094 (mRNA)
NP_061967 (protein)

XM_991360 (mRNA)
XP_996454 (protein)

Location

Chr 12: 92.3 - 92.32 Mb

Chr 10: 94.98 - 94.99 Mb

Pubmed search

[1]

[2]

Nudix (nucleoside diphosphate linked moiety X)-type motif 4, also known as NUDT4, is a human gene.^[1]

The protein encoded by this gene regulates the turnover of diphosphoinositol polyphosphates. The turnover of these high-energy diphosphoinositol polyphosphates represents a molecular switching activity with important regulatory consequences. Molecular switching by diphosphoinositol polyphosphates may contribute to regulating intracellular trafficking. Several alternatively spliced transcript variants have been described, but the full-length nature of some variants has not been determined. Isoforms DIPP2alpha and DIPP2beta are distinguishable from each other solely by DIPP2beta possessing one additional amino acid due to intron boundary skidding in alternate splicing.^[1]

[edit] References

^ ^a ^b Entrez Gene: NUDT4 nudix (nucleoside diphosphate linked moiety X)-type motif 4.

[edit] Further reading

Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1-2): 171-4. PMID 8125298.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene 200 (1-2): 149-56. PMID 9373149.
Seki N, Ohira M, Nagase T, et al. (1998). "Characterization of cDNA clones in size-fractionated cDNA libraries from human brain.". DNA Res. 4 (5): 345-9. PMID 9455484.
Caffrey JJ, Safrany ST, Yang X, Shears SB (2000). "Discovery of molecular and catalytic diversity among human diphosphoinositol-polyphosphate phosphohydrolases. An expanding Nudt family.". J. Biol. Chem. 275 (17): 12730-6. PMID 10777568.
Caffrey JJ, Shears SB (2001). "Genetic rationale for microheterogeneity of human diphosphoinositol polyphosphate phosphohydrolase type 2.". Gene 269 (1-2): 53-60. PMID 11376937.
Leslie NR, McLennan AG, Safrany ST (2002). "Cloning and characterisation of hAps1 and hAps2, human diadenosine polyphosphate-metabolising Nudix hydrolases.". BMC Biochem. 3: 20. PMID 12121577.
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.
Fortna A, Kim Y, MacLaren E, et al. (2006). "Lineage-specific gene duplication and loss in human and great ape evolution.". PLoS Biol. 2 (7): E207. doi:10.1371/journal.pbio.0020207. PMID 15252450.
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.