ID:DUT_HUMAN DESCRIPTION: RecName: Full=Deoxyuridine 5'-triphosphate nucleotidohydrolase, mitochondrial; Short=dUTPase; EC=3.6.1.23; AltName: Full=dUTP pyrophosphatase; Flags: Precursor; FUNCTION: This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA. CATALYTIC ACTIVITY: dUTP + H(2)O = dUMP + diphosphate. COFACTOR: Magnesium. ENZYME REGULATION: Phosphorylation is necessary for activity. BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.5 uM for dUTP; Note=for both isoform 2 and isoform 3; PATHWAY: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 2/2. SUBUNIT: Homotrimer. INTERACTION: Q6ZVK8:NUDT18; NbExp=3; IntAct=EBI-353224, EBI-740486; SUBCELLULAR LOCATION: Isoform 2: Nucleus. SUBCELLULAR LOCATION: Isoform 3: Mitochondrion. TISSUE SPECIFICITY: Found in a variety of tissues. Isoform 3 expression is constitutive, while isoform 2 expression correlates with the onset of DNA replication (at protein level). Isoform 2 degradation coincides with the cessation of nuclear DNA replication (at protein level). PTM: Nuclear isoform 2 is phosphorylated in vivo on Ser-11, a reaction that can be catalyzed in vitro by CDC2. Phosphorylation in mature T-cells occurs in a cell cycle-dependent manner. Isoform 3 is not phosphorylated. PTM: The initiator methionine is cleaved in isoform 2. MISCELLANEOUS: Each trimer binds three substrate molecules. The ligands are bound between subunits, and for each substrate molecule, residues from adjacent subunits contribute to the binding interactions. SIMILARITY: Belongs to the dUTPase family. SEQUENCE CAUTION: Sequence=AAB71393.1; Type=Frameshift; Positions=29, 47; Sequence=AAB93866.1; Type=Frameshift; Positions=29, 47; Sequence=AAB94642.1; Type=Frameshift; Positions=29, 47; WEB RESOURCE: Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/dut/";
Protein Domain and Structure Information
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