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MGP006518

UniProt Annotations

Entry Information
Gene Namenudix (nucleoside diphosphate linked moiety X)-type motif 16
Protein EntryNUD16_HUMAN
UniProt IDQ96DE0
SpeciesHuman
Comments
Comment typeDescription
Alternative ProductsEvent=Alternative splicing; Named isoforms=4; Name=1; IsoId=Q96DE0-1; Sequence=Displayed; Name=2; IsoId=Q96DE0-2; Sequence=VSP_045450, VSP_045451; Note=No experimental confirmation available.; Name=3; IsoId=Q96DE0-3; Sequence=VSP_045449, VSP_045452; Note=No experimental confirmation available. Ref.2 (BP199028) sequence is in conflict in position: 128:A->Missing. {ECO:0000305}; Name=4; IsoId=Q96DE0-4; Sequence=VSP_045451;
Biophysicochemical PropertiesKinetic parameters: KM=0.062 uM for IDP (at 37 degrees Celsius) {ECO:0000269|PubMed:20385596}; KM=0.088 uM for dIDP (at 37 degrees Celsius) {ECO:0000269|PubMed:20385596}; KM=0.330 uM for GDP (at 37 degrees Celsius) {ECO:0000269|PubMed:20385596}; KM=0.319 mM for dGDP (at 37 degrees Celsius) {ECO:0000269|PubMed:20385596}; KM=15.7 mM for XDP (at 37 degrees Celsius) {ECO:0000269|PubMed:20385596}; KM=22.1 mM for ITP (at 37 degrees Celsius) {ECO:0000269|PubMed:20385596}; KM=24.1 mM for dITP (at 37 degrees Celsius) {ECO:0000269|PubMed:20385596}; Note=kcat is 0.931 sec(-1) with IDP. kcat is 0.966 sec(-1) with dIDP. kcat is 0.518 sec(-1) with GDP. kcat is 0.492 sec(-1) with dGDP. kcat is 2.6 sec(-1) with XDP. kcat is 3.06 sec(-1) with ITP. kcat is 3.2 sec(-1) with dITP. The catalytic efficiency for IDP is at least 1.3-fold higher than for dIDP, 9.6-fold higher than for GDP and dGDP, 100-fold higher than for XDP, ITP and dITP.; pH dependence: Gradually increased from pH 6.5 to 8.5 in its IDP hydrolyzing activity. {ECO:0000269|PubMed:20385596}; Temperature dependence: Exhibited a temperature-dependent increase in its IDP hydrolyzing activity up to 60 degrees Celsius. {ECO:0000269|PubMed:20385596};
Catalytic Activity5'-(N(7)-methylguanosine 5'-triphospho)-(mRNA) + H(2)O = N(7)-methylguanosine 5'-diphosphate + 5'-phospho-(mRNA).
Catalytic ActivityIDP + H(2)O = IMP + phosphate.
CofactorName=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:17567574, ECO:0000269|PubMed:21337011}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:17567574, ECO:0000269|PubMed:21337011}; Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000269|PubMed:17567574, ECO:0000269|PubMed:21337011}; Note=Binds 3 or 4 divalent metal cations. Acts specifically on U8 snoRNA with magnesium as cofactor. Has broad substrate specificity with bound manganese or cobalt (in vitro). {ECO:0000269|PubMed:17567574, ECO:0000269|PubMed:21337011};
FunctionRNA-binding and decapping enzyme that catalyzes the cleavage of the cap structure of snoRNAs and mRNAs in a metal- dependent manner. Part of the U8 snoRNP complex that is required for the accumulation of mature 5.8S and 28S rRNA. Has diphosphatase activity and removes m7G and/or m227G caps from U8 snoRNA and leaves a 5'monophosphate on the RNA. Catalyzes also the cleavage of the cap structure on mRNAs. Does not hydrolyze cap analog structures like 7-methylguanosine nucleoside triphosphate (m7GpppG). Also hydrolysis m7G- and m227G U3-capped RNAs but with less efficiencies. Has broad substrate specificity with manganese or cobalt as cofactor and can act on various RNA species. Binds to the U8 snoRNA; metal is not required for RNA-binding. May play a role in the regulation of snoRNAs and mRNAs degradation. Acts also as a phosphatase; hydrolyzes the non-canonical purine nucleotides inosine diphosphate (IDP) and deoxyinosine diphosphate (dITP) as well as guanosine diphosphate (GDP), deoxyguanosine diphosphate (dGDP), xanthine diphosphate (XDP), inosine triphosphate (ITP) and deoxyinosine triphosphate (ITP) to their respective monophosphate derivatives and does not distinguish between the deoxy- and ribose forms. The order of activity with different substrates is IDP > dIDP >> GDP = dGDP > XDP = ITP = dITP. Binds strongly to GTP, ITP and XTP. Participates in the hydrolysis of dIDP/IDP and probably excludes non-canonical purines from RNA and DNA precursor pools, thus preventing their incorporation into RNA and DNA and avoiding chromosomal lesions. {ECO:0000269|PubMed:15053875, ECO:0000269|PubMed:17567574, ECO:0000269|PubMed:18820299, ECO:0000269|PubMed:20385596, ECO:0000269|PubMed:21070968, ECO:0000269|PubMed:21337011}.
Sequence CautionSequence=BAB71024.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
SimilarityBelongs to the Nudix hydrolase family. NUDT16 subfamily. {ECO:0000305}.
SimilarityContains 1 nudix hydrolase domain. {ECO:0000255|PROSITE-ProRule:PRU00794}.
Subcellular LocationNucleus. Nucleus, nucleoplasm {ECO:0000250}. Nucleus, nucleolus. Cytoplasm. Note=Localized predominantly in the cytoplasm. Localized in nucleolus, and in a minor proportion in distinct foci in the nucleoplasm (By similarity). {ECO:0000250}.
SubunitHomodimer. {ECO:0000269|PubMed:17567574, ECO:0000269|PubMed:18820299, ECO:0000269|Ref.14}.
Tissue SpecificityExpressed strongly in lung, kidney, adrenal gland, testis, heart and brain. {ECO:0000269|PubMed:20385596}.
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