CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-015163
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 U8 snoRNA-decapping enzyme 
Protein Synonyms/Alias
 IDP phosphatase; IDPase; Inosine diphosphate phosphatase; Nucleoside diphosphate-linked moiety X motif 16; Nudix motif 16; m7GpppN-mRNA hydrolase 
Gene Name
 Nudt16 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
188LDPGIIAKLKIPDSKubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023
Functional Description
 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. 
Sequence Annotation
 DOMAIN 18 173 Nudix hydrolase.
 MOTIF 61 82 Nudix box.
 METAL 59 59 Magnesium or manganese 1; via carbonyl
 METAL 76 76 Magnesium or manganese 2 (By similarity).
 METAL 76 76 Magnesium or manganese 3 (By similarity).
 METAL 80 80 Magnesium or manganese 1 (By similarity).
 METAL 80 80 Magnesium or manganese 3 (By similarity).
 METAL 136 136 Magnesium or manganese 3 (By similarity).
 METAL 136 136 Magnesium or manganese 4 (By similarity).
 BINDING 24 24 Substrate (By similarity).
 BINDING 50 50 Substrate (By similarity).
 BINDING 170 170 Substrate (By similarity).  
Keyword
 Complete proteome; Cytoplasm; Hydrolase; Magnesium; Manganese; Metal-binding; Nucleotide metabolism; Nucleotide-binding; Nucleus; Reference proteome; RNA-binding. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 195 AA 
Protein Sequence
MEGHRKVELS EALALGPDWR HACHALLYAP DPRKLFGRIP MRFAVLMQMR FDGRLGFPGG 60
FVDAQDSCLE DGLNRELREE LGEAMSAFRV ERSDYRSSHI AARPRVVAHF YAKRLTLEQL 120
QAVEARAPQA KDHGLEVLGL VRVPLYVLRD GEGGLPAFLE NSFIGAAREQ LLEALQDLKL 180
LDPGIIAKLK IPDSK 195 
Gene Ontology
 GO:0005737; C:cytoplasm; ISS:UniProtKB.
 GO:0005730; C:nucleolus; ISS:UniProtKB.
 GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
 GO:0050897; F:cobalt ion binding; ISS:UniProtKB.
 GO:0035870; F:dITP diphosphatase activity; IMP:MGI.
 GO:0005525; F:GTP binding; ISS:UniProtKB.
 GO:1901641; F:ITP binding; ISS:UniProtKB.
 GO:0050072; F:m7G(5')pppN diphosphatase activity; ISS:UniProtKB.
 GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
 GO:0030145; F:manganese ion binding; ISS:UniProtKB.
 GO:0008235; F:metalloexopeptidase activity; ISS:UniProtKB.
 GO:0003729; F:mRNA binding; ISS:UniProtKB.
 GO:0019204; F:nucleotide phosphatase activity; IDA:UniProtKB.
 GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
 GO:0030515; F:snoRNA binding; ISS:UniProtKB.
 GO:1901640; F:XTP binding; ISS:UniProtKB.
 GO:0006382; P:adenosine to inosine editing; ISS:UniProtKB.
 GO:0051276; P:chromosome organization; IGI:MGI.
 GO:0035863; P:dITP catabolic process; IGI:MGI.
 GO:0046709; P:IDP catabolic process; ISS:UniProtKB.
 GO:0006402; P:mRNA catabolic process; IMP:UniProtKB.
 GO:2000233; P:negative regulation of rRNA processing; ISS:UniProtKB.
 GO:0090068; P:positive regulation of cell cycle process; ISS:UniProtKB.
 GO:0008284; P:positive regulation of cell proliferation; ISS:UniProtKB.
 GO:2000781; P:positive regulation of double-strand break repair; ISS:UniProtKB.
 GO:0016077; P:snoRNA catabolic process; ISS:UniProtKB.
 GO:1901639; P:XDP catabolic process; ISS:UniProtKB. 
Interpro
 IPR000086; NUDIX_hydrolase_dom.
 IPR015797; NUDIX_hydrolase_dom-like. 
Pfam
 PF00293; NUDIX 
SMART
  
PROSITE
 PS51462; NUDIX
 PS00893; NUDIX_BOX 
PRINTS