NUDT4

NUDT4
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2DUK
Identifiers
Aliases	NUDT4, DIPP2, DIPP2alpha, DIPP2beta, HDCMB47P, nudix hydrolase 4, DIPP-2B, NUDT4B
External IDs	OMIM: 609229 MGI: 1918457 HomoloGene: 41726 GeneCards: NUDT4
Gene location (Human) Chr. Chromosome 12 (human) Band 12q22 Start 93,377,883 bp End 93,408,146 bp
Gene location (Mouse) Chr. Chromosome 10 (mouse) Band 10|10 C2 Start 95,382,869 bp End 95,400,008 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in right ventricle parotid gland renal medulla caput epididymis corpus epididymis gallbladder trabecular bone urethra ganglionic eminence secondary oocyte Top expressed in molar ciliary body endocardial cushion submandibular gland left colon seminiferous tubule atrium quadriceps femoris muscle knee joint spermatid More reference expression data BioGPS More reference expression data
Gene ontology Molecular function inositol diphosphate tetrakisphosphate diphosphatase activity inositol-1-diphosphate-2,3,4,5,6-pentakisphosphate diphosphatase activity inositol-3,5-bisdiphosphate-2,3,4,6-tetrakisphosphate 5-diphosphatase activity inositol-5-diphosphate-1,2,3,4,6-pentakisphosphate diphosphatase activity metal ion binding protein binding RNA binding inositol-3-diphosphate-1,2,4,5,6-pentakisphosphate diphosphatase activity hydrolase activity diphosphoinositol-polyphosphate diphosphatase activity inositol-1,5-bisdiphosphate-2,3,4,6-tetrakisphosphate 1-diphosphatase activity inositol-1,5-bisdiphosphate-2,3,4,6-tetrakisphosphate 5-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 snoRNA binding Cellular component intracellular anatomical structure nucleus cytoplasm cytosol Biological process intracellular signal transduction cyclic nucleotide metabolic process inositol phosphate metabolic process cyclic-nucleotide-mediated signaling calcium-mediated signaling diphosphoinositol polyphosphate metabolic process diadenosine pentaphosphate catabolic process diadenosine hexaphosphate catabolic process adenosine 5'-(hexahydrogen pentaphosphate) catabolic process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 11163 71207 Ensembl ENSG00000173598 ENSMUSG00000020029 UniProt Q9NZJ9 Q8R2U6 RefSeq (mRNA) NM_001301022 NM_001301023 NM_001301024 NM_019094 NM_199040 NM_027722 NM_001358996 RefSeq (protein) NP_001287951 NP_001287952 NP_001287953 NP_061967 NP_950241 NP_081998 NP_001345925 Location (UCSC) Chr 12: 93.38 – 93.41 Mb Chr 10: 95.38 – 95.4 Mb PubMed search
Wikidata
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Diphosphoinositol polyphosphate phosphohydrolase 2 is an enzyme that in humans is encoded by the NUDT4 gene.

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.

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. doi:10.1016/0378-1119(94)90802-8. 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. doi:10.1016/S0378-1119(97)00411-3. 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. doi:10.1093/dnares/4.5.345. PMID 9455484.
• Leslie NR, McLennan AG, Safrany ST (2002). "Cloning and characterisation of hAps1 and hAps2, human diadenosine polyphosphate-metabolising Nudix hydrolases". BMC Biochem. 3: 20. doi:10.1186/1471-2091-3-20. PMC 117780. 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. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. 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. PMC 449870. 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. PMC 528928. PMID 15489334.