NUDT16
entrez
131870
canonical
uniprot
Q96DE0
canonical
ensembl
ENSG00000198585
resolver
ensp
ENSP00000422375
resolver
ensp
ENSP00000429274
resolver
ensp
ENSP00000440230
resolver
genesymbol
NUDT16
resolver
hgnc
HGNC:26442
resolver
uniprot
B4E3B4
resolver
uniprot
E9PED4
resolver
uniprot
F5GYJ1
resolver
uniprot
Q96N82
resolver
uniprot_entry
NUD16_HUMAN
resolver
uniprot_sec
B4E3B4
resolver
uniprot_sec
E9PED4
resolver
uniprot_sec
F5GYJ1
resolver
uniprot_sec
Q96N82
resolver
activity_regulation
ACTIVITY REGULATION: The phosphatase activity is inhibited by the product IMP. {ECO:0000269|PubMed:26121039}.
uniprot
proteins
amino_acid_sequence
MAGARRLELGEALALGSGWRHACHALLYAPDPGMLFGRIPLRYAILMQMRFDGRLGFPGGFVDTQDRSLEDGLNRELREELGEAAAAFRVERTDYRSSHVGSGPRVVAHFYAKRLTLEELLAVEAGATRAKDHGLEVLGLVRVPLYTLRDGVGGLPTFLENSFIGSAREQLLEALQDLGLLQSGSISGLKIPAHH
uniprot
proteins
ec_number
3.6.1.62
uniprot
proteins
ec_number
3.6.1.64
uniprot
proteins
function
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. Also catalyzes 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. Also acts 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 (PubMed:20385596, PubMed:26121039). The order of activity with different substrates is IDP > dIDP >> GDP = dGDP > XDP = ITP = dITP (PubMed:20385596). 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 (PubMed:20385596). Exhibits decapping activity towards NAD-capped RNAs and FAD-capped RNAs (PubMed:32432673). Exhibits decapping activity towards dpCoA-capped RNAs in vitro (By similarity). {ECO:0000250|UniProtKB:Q6P3D0, ECO:0000269|PubMed:15053875, ECO:0000269|PubMed:17567574, ECO:0000269|PubMed:18820299, ECO:0000269|PubMed:20385596, ECO:0000269|PubMed:21070968, ECO:0000269|PubMed:21337011, ECO:0000269|PubMed:26121039, ECO:0000269|PubMed:32432673}.
uniprot
proteins
mass_dalton
21273
uniprot
proteins
protein_family
NUDT16 subfamily
uniprot
proteins
protein_family
Nudix hydrolase family
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15053875
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16344560
uniprot
proteins
pubmed
16641997
uniprot
proteins
pubmed
17567574
uniprot
proteins
pubmed
18607096
uniprot
proteins
pubmed
18820299
uniprot
proteins
pubmed
20385596
uniprot
proteins
pubmed
21070968
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21337011
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
26121039
uniprot
proteins
pubmed
32432673
uniprot
proteins
sequence_length
195
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20385596, ECO:0000269|PubMed:21337011}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q6TEC1}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q6TEC1}. Cytoplasm {ECO:0000269|PubMed:21070968, ECO:0000269|PubMed:21337011}. Note=Localized predominantly in the cytoplasm (PubMed:21070968). Localized in nucleolus, and in a minor proportion in distinct foci in the nucleoplasm (By similarity). {ECO:0000250|UniProtKB:Q6TEC1, ECO:0000269|PubMed:21070968}.
uniprot
proteins