NUDT2

Nudix (nucleoside diphosphate linked moiety X)-type motif 2
File:PBB Protein NUDT2 image.jpg PDB rendering based on 1xsa.
Available structures PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB List of PDB id codes 1xsa​, 1xsb​, 1xsc​
Identifiers
Symbols	NUDT2 ; APAH1; MGC10404
External IDs	Template:OMIM5 Template:MGI HomoloGene: 896
Gene ontology Molecular function Template:GNF GO Template:GNF GO Template:GNF GO Biological process Template:GNF GO Template:GNF GO
RNA expression pattern
File:PBB GE NUDT2 218609 s at tn.png
More reference expression data
Orthologs
Template:GNF Ortholog box
Species	Human	Mouse
Entrez	n/a	n/a
Ensembl	n/a	n/a
UniProt	n/a	n/a
RefSeq (mRNA)	n/a	n/a
RefSeq (protein)	n/a	n/a
Location (UCSC)	n/a	n/a
PubMed search	n/a	n/a

Nudix (nucleoside diphosphate linked moiety X)-type motif 2, also known as NUDT2, is a human gene.

This gene encodes a member of the MutT family of nucleotide pyrophosphatases, a subset of the larger NUDIX hydrolase family. The gene product possesses a modification of the MutT sequence motif found in certain nucleotide pyrophosphatases. The enzyme asymmetrically hydrolyzes Ap4A to yield AMP and ATP and is responsible for maintaining the intracellular level of the dinucleotide Ap4A, the function of which has yet to be established. This gene may be a candidate tumor suppressor gene. Alternative splicing has been observed at this locus and three transcript variants, all encoding the same protein, have been identified.

Further reading

• Bessman MJ, Frick DN, O'Handley SF (1996). "The MutT proteins or "Nudix" hydrolases, a family of versatile, widely distributed, "housecleaning" enzymes". J. Biol. Chem. 271 (41): 25059–62. PMID 8810257.CS1 maint: Multiple names: authors list (link)
• Pinto RM, Costas MJ, Fernández A; et al. (1991). "Dinucleoside tetraphosphatase from human blood cells. Purification and characterization as a high specific activity enzyme recognized by an anti-rat tetraphosphatase antibody". FEBS Lett. 287 (1–2): 85–8. PMID 1652465.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Thorne NM, Hankin S, Wilkinson MC; et al. (1995). "Human diadenosine 5',5"'-P1,P4-tetraphosphate pyrophosphohydrolase is a member of the MutT family of nucleotide pyrophosphatases". Biochem. J. 311 ( Pt 3): 717–21. PMID 7487923.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Hankin S, Matthew N, Thorne H, McLennan AG (1995). "Diadenosine 5',5"'-P1,P4-tetraphosphate hydrolase is present in human erythrocytes, leukocytes and platelets". Int. J. Biochem. Cell Biol. 27 (2): 201–6. PMID 7767787.CS1 maint: Multiple names: authors list (link)
• Lazewska D, Starzyńska E, Guranowski A (1993). "Human placental (Asymmetrical) diadenosine 5',5-P1,P4-tetraphosphate hydrolase: purification to homogeneity and some properties". Protein Expr. Purif. 4 (1): 45–51. doi:10.1006/prep.1993.1007. PMID 8381042.CS1 maint: Multiple names: authors list (link)
• McLennan AG, Flannery AV, Morten JE, Ridanpää M (1998). "Chromosomal localization of the human diadenosine 5',5"'-P1,P4-tetraphosphate pyrophosphohydrolase (Ap4A hydrolase) gene (APAH1) to 9p13". Genomics. 47 (2): 307–9. doi:10.1006/geno.1997.5092. PMID 9479504.CS1 maint: Multiple names: authors list (link)
• Rotllán P, Rodríguez-Ferrer CR, Asensio AC, Oaknin S (1998). "Potent inhibition of specific diadenosine polyphosphate hydrolases by suramin". FEBS Lett. 429 (2): 143–6. PMID 9650578.CS1 maint: Multiple names: authors list (link)
• Vartanian A, Alexandrov I, Prudowski I; et al. (1999). "Ap4A induces apoptosis in human cultured cells". FEBS Lett. 456 (1): 175–80. PMID 10452553.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Guranowski A, Galbas M, Hartmann R, Justesen J (2000). "Selective degradation of 2'-adenylated diadenosine tri- and tetraphosphates, Ap(3)A and Ap(4)A, by two specific human dinucleoside polyphosphate hydrolases". Arch. Biochem. Biophys. 373 (1): 218–24. doi:10.1006/abbi.1999.1556. PMID 10620341.CS1 maint: Multiple names: authors list (link)
• Abdelghany HM, Gasmi L, Cartwright JL; et al. (2002). "Cloning, characterisation and crystallisation of a diadenosine 5',5"'-P(1),P(4)-tetraphosphate pyrophosphohydrolase from Caenorhabditis elegans". Biochim. Biophys. Acta. 1550 (1): 27–36. PMID 11738085.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Guranowski A, Sillero A, Günther Sillero MA (2003). "Selective splitting of 3'-adenylated dinucleoside polyphosphates by specific enzymes degrading dinucleoside polyphosphates". Acta Biochim. Pol. 50 (1): 123–30. doi:035001123 . PMID 12673352.CS1 maint: Multiple names: authors list (link)
• Pitcher WH, Kirby TW, DeRose EF, London RE (2003). "Metabolic transformation of AZTp4A by Ap4A hydrolase regenerates AZT triphosphate". Antiviral Res. 58 (3): 227–33. PMID 12767470.CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Swarbrick JD, Buyya S, Gunawardana D; et al. (2005). "Structure and substrate-binding mechanism of human Ap4A hydrolase". J. Biol. Chem. 280 (9): 8471–81. doi:10.1074/jbc.M412318200. PMID 15596429.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Swarbrick JD, Buyya S, Gunawardana D; et al. (2005). "1H, 13C, and 15N resonance assignments of the 17 kDa Ap4A hydrolase from Homo sapiens in the presence and absence of ATP". J. Biomol. NMR. 31 (2): 181–2. doi:10.1007/s10858-004-7440-4. PMID 15772762.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)