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NUDT16 nudix hydrolase 16 [ Homo sapiens (human) ]

Gene ID: 131870, updated on 25-Nov-2021

Summary

Official Symbol
NUDT16provided by HGNC
Official Full Name
nudix hydrolase 16provided by HGNC
Primary source
HGNC:HGNC:26442
See related
Ensembl:ENSG00000198585 MIM:617381
Gene type
protein coding
RefSeq status
VALIDATED
Organism
Homo sapiens
Lineage
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
Expression
Ubiquitous expression in fat (RPKM 14.5), kidney (RPKM 13.4) and 25 other tissues See more
Orthologs
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Genomic context

See NUDT16 in Genome Data Viewer
Location:
3q22.1
Exon count:
5
Annotation release Status Assembly Chr Location
109.20211119 current GRCh38.p13 (GCF_000001405.39) 3 NC_000003.12 (131381671..131388830)
105.20201022 previous assembly GRCh37.p13 (GCF_000001405.25) 3 NC_000003.11 (131100515..131107674)

Chromosome 3 - NC_000003.12Genomic Context describing neighboring genes Neighboring gene NIMA related kinase 11 Neighboring gene RNA, U6 small nuclear 726, pseudogene Neighboring gene NUDT16 divergent transcript Neighboring gene nudix hydrolase 16 like 2, pseudogene Neighboring gene uncharacterized LOC107986025 Neighboring gene uncharacterized LOC105374110

Genomic regions, transcripts, and products

Expression

  • Project title: HPA RNA-seq normal tissues
  • Description: RNA-seq was performed of tissue samples from 95 human individuals representing 27 different tissues in order to determine tissue-specificity of all protein-coding genes
  • BioProject: PRJEB4337
  • Publication: PMID 24309898
  • Analysis date: Wed Apr 4 07:08:55 2018

Bibliography

GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Pathways from PubChem

Interactions

Products Interactant Other Gene Complex Source Pubs Description

General gene information

Markers

Homology

Clone Names

  • FLJ31265, FLJ34034, FLJ36248

Gene Ontology Provided by GOA

Function Evidence Code Pubs
enables GTP binding IDA
Inferred from Direct Assay
more info
PubMed 
enables ITP binding IDA
Inferred from Direct Assay
more info
PubMed 
enables RNA NAD-cap (NMN-forming) hydrolase activity IEA
Inferred from Electronic Annotation
more info
 
enables XTP binding IDA
Inferred from Direct Assay
more info
PubMed 
enables chloride ion binding IDA
Inferred from Direct Assay
more info
PubMed 
enables cobalt ion binding IDA
Inferred from Direct Assay
more info
PubMed 
enables dIDP diphosphatase activity IEA
Inferred from Electronic Annotation
more info
 
enables dITP diphosphatase activity ISS
Inferred from Sequence or Structural Similarity
more info
 
enables identical protein binding IPI
Inferred from Physical Interaction
more info
PubMed 
enables inosine-diphosphatase activity IEA
Inferred from Electronic Annotation
more info
 
enables m7G(5')pppN diphosphatase activity IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
enables m7G(5')pppN diphosphatase activity IDA
Inferred from Direct Assay
more info
PubMed 
enables mRNA binding IDA
Inferred from Direct Assay
more info
PubMed 
enables magnesium ion binding IDA
Inferred from Direct Assay
more info
PubMed 
enables manganese ion binding IDA
Inferred from Direct Assay
more info
PubMed 
enables metalloexopeptidase activity IDA
Inferred from Direct Assay
more info
PubMed 
enables nucleotide phosphatase activity, acting on free nucleotides IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
enables nucleotide phosphatase activity, acting on free nucleotides IDA
Inferred from Direct Assay
more info
PubMed 
enables phosphodiesterase decapping endonuclease activity IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
enables phosphodiesterase decapping endonuclease activity IDA
Inferred from Direct Assay
more info
PubMed 
enables protein homodimerization activity IDA
Inferred from Direct Assay
more info
PubMed 
enables snoRNA binding IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
enables snoRNA binding IDA
Inferred from Direct Assay
more info
PubMed 
Process Evidence Code Pubs
involved_in IDP catabolic process IDA
Inferred from Direct Assay
more info
PubMed 
involved_in NAD-cap decapping IDA
Inferred from Direct Assay
more info
PubMed 
involved_in RNA phosphodiester bond hydrolysis, endonucleolytic IDA
Inferred from Direct Assay
more info
PubMed 
involved_in adenosine to inosine editing IMP
Inferred from Mutant Phenotype
more info
PubMed 
involved_in dITP catabolic process ISS
Inferred from Sequence or Structural Similarity
more info
 
involved_in dephosphorylation IEA
Inferred from Electronic Annotation
more info
 
involved_in mRNA catabolic process IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
involved_in mRNA catabolic process IDA
Inferred from Direct Assay
more info
PubMed 
involved_in negative regulation of rRNA processing ISS
Inferred from Sequence or Structural Similarity
more info
 
involved_in positive regulation of cell cycle process IMP
Inferred from Mutant Phenotype
more info
PubMed 
involved_in proteolysis IEA
Inferred from Electronic Annotation
more info
 
involved_in sno(s)RNA catabolic process IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
involved_in sno(s)RNA catabolic process IDA
Inferred from Direct Assay
more info
PubMed 
Component Evidence Code Pubs
located_in cytoplasm IDA
Inferred from Direct Assay
more info
PubMed 
located_in nucleolus IDA
Inferred from Direct Assay
more info
PubMed 
located_in nucleoplasm IDA
Inferred from Direct Assay
more info
 
located_in nucleoplasm TAS
Traceable Author Statement
more info
 
located_in nucleus HDA PubMed 
is_active_in nucleus IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
located_in nucleus IDA
Inferred from Direct Assay
more info
PubMed 

General protein information

Preferred Names
U8 snoRNA-decapping enzyme
Names
IDP phosphatase
IDPase
U8 snoRNA-binding protein H29K
inosine diphosphate phosphatase
m7GpppN-mRNA hydrolase
nucleoside diphosphate-linked moiety X motif 16
nudix (nucleoside diphosphate linked moiety X)-type motif 16
nudix motif 16
testicular tissue protein Li 129
NP_001165376.1
NP_001165377.1
NP_689608.2

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

  1. NM_001171905.2NP_001165376.1  U8 snoRNA-decapping enzyme isoform 3

    Status: VALIDATED

    Description
    Transcript Variant: This variant (3) has multiple differences, compared to variant 1. The encoded isoform (3) is shorter at the N-terminus and has a distinct C-terminus, compared to isoform 1.
    Source sequence(s)
    AC010210, BP199028
    Consensus CDS
    CCDS54641.1
    UniProtKB/Swiss-Prot
    Q96DE0
    Related
    ENSP00000440230.1, ENST00000537561.5
    Conserved Domains (1) summary
    cl00447
    Location:736
    Nudix_Hydrolase; Nudix hydrolase is a superfamily of enzymes found in all three kingdoms of life, and it catalyzes the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+ ...
  2. NM_001171906.2NP_001165377.1  U8 snoRNA-decapping enzyme isoform 1

    Status: VALIDATED

    Description
    Transcript Variant: This variant (1) encodes the longest isoform (1).
    Source sequence(s)
    AC010210, AK304650, BP219080
    Consensus CDS
    CCDS54640.1
    UniProtKB/Swiss-Prot
    Q96DE0
    Related
    ENSP00000422375.1, ENST00000502852.1
    Conserved Domains (1) summary
    cl00447
    Location:5382
    Nudix_Hydrolase; Nudix hydrolase is a superfamily of enzymes found in all three kingdoms of life, and it catalyzes the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+ ...
  3. NM_152395.3NP_689608.2  U8 snoRNA-decapping enzyme isoform 2

    See identical proteins and their annotated locations for NP_689608.2

    Status: VALIDATED

    Description
    Transcript Variant: This variant (2) differs in the 3' UTR and 3' coding region, compared to variant 1. The encoded isoform (2) is shorter and has a distinct C-terminus compared to isoform 1.
    Source sequence(s)
    AC010210, CB121755
    Consensus CDS
    CCDS3070.2
    UniProtKB/Swiss-Prot
    Q96DE0
    Related
    ENSP00000429274.2, ENST00000521288.2
    Conserved Domains (2) summary
    PRK05379
    Location:53131
    PRK05379; bifunctional nicotinamide-nucleotide adenylyltransferase/Nudix hydroxylase
    cl00447
    Location:5382
    Nudix_Hydrolase; Nudix hydrolase is a superfamily of enzymes found in all three kingdoms of life, and it catalyzes the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+ ...

RNA

  1. NR_033268.2 RNA Sequence

    Status: VALIDATED

    Description
    Transcript Variant: This variant (4) has multiple differences, compared to variant 1. This variant is represented as non-coding because the use of the 5'-most supported translational start codon, as used in variant 1, renders the transcript a candidate for nonsense-mediated mRNA decay (NMD).
    Source sequence(s)
    AC010210, AK295852, DC343245

RefSeqs of Annotated Genomes: Homo sapiens Updated Annotation Release 109.20211119

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference GRCh38.p13 Primary Assembly

Genomic

  1. NC_000003.12 Reference GRCh38.p13 Primary Assembly

    Range
    131381671..131388830
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)
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