Version 5.4
Bos taurus Protein: NUDT16
Summary
InnateDB Protein IDBP-691216.2
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol NUDT16
Protein Name U8 snoRNA-decapping enzyme
Synonyms
Species Bos taurus
Ensembl Protein ENSBTAP00000049112
InnateDB Gene IDBG-639095 (NUDT16)
Protein Structure
UniProt Annotation
Function RNA-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 (By similarity). {ECO:0000250}.
Subcellular Localization Nucleus {ECO:0000250}. Nucleus, nucleoplasm {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Localized predominantly in the cytoplasm. Localized in nucleolus, and in a minor proportion in distinct foci in the nucleoplasm (By similarity). {ECO:0000250}.
Disease Associations
Tissue Specificity
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 0 experimentally validated interaction(s) in this database.
Gene Ontology

Molecular Function
Accession GO Term
GO:0000166 nucleotide binding
GO:0000287 magnesium ion binding
GO:0003723 RNA binding
GO:0003729 mRNA binding
GO:0005525 GTP binding
GO:0008235 metalloexopeptidase activity
GO:0016787 hydrolase activity
GO:0030145 manganese ion binding
GO:0030515 snoRNA binding
GO:0035870 dITP diphosphatase activity
GO:0042803 protein homodimerization activity
GO:0046872 metal ion binding
GO:0050072 m7G(5')pppN diphosphatase activity
GO:0050897 cobalt ion binding
GO:0098519 nucleotide phosphatase activity, acting on free nucleotides
GO:1901640 XTP binding
GO:1901641 ITP binding
Biological Process
GO:0006382 adenosine to inosine editing
GO:0006402 mRNA catabolic process
GO:0006508 proteolysis
GO:0008284 positive regulation of cell proliferation
GO:0009117 nucleotide metabolic process
GO:0016077 snoRNA catabolic process
GO:0016311 dephosphorylation
GO:0035863 dITP catabolic process
GO:0046709 IDP catabolic process
GO:0090068 positive regulation of cell cycle process
GO:1901639 XDP catabolic process
GO:2000233 negative regulation of rRNA processing
GO:2000781 positive regulation of double-strand break repair
Cellular Component
GO:0005634 nucleus
GO:0005654 nucleoplasm
GO:0005730 nucleolus
GO:0005737 cytoplasm
Protein Structure and Domains
PDB ID
InterPro IPR000086 NUDIX hydrolase domain
IPR015797 NUDIX hydrolase domain-like
PFAM PF00293
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt A1A4Q9
PhosphoSite PhosphoSite-
TrEMBL
UniProt Splice Variant
Entrez Gene 512320
UniGene Bt.20950
RefSeq XP_005202022
HUGO
OMIM
CCDS
HPRD
IMGT
EMBL BC126814
GenPept AAI26815

If you use InnateDB for your research, please cite the following publication:

Breuer et al., InnateDB: systems biology of innate immunity and beyond - recent updates and continuing curation. Nucl. Acids Res. (2013) 41 (D1) 

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Funding is currently provided by Allergen and EMBL Australia. Previous funding has been provided by Genome Canada, the Foundation for the National Institutes of Health through the Grand Challenges in Global Health initiative and by Teagasc. InnateDB curated interactions are licensed under the Design Science License. All other data is licensed under the terms of the originating database. Contact: innatedb-mail@sfu.ca