Home › Entities › protein › Nudix hydrolase 16

Nudix hydrolase 16

mammalian protein found in Homo sapiens
Protein protein Q21120178
Press Enter · cited answer in seconds

Nudix hydrolase 16

Summary

Nudix hydrolase 16 is a protein[1]. It is known by 13 alternative names across languages and contexts.[2]

Key Facts

  • Nudix hydrolase 16's instance of is recorded as protein[3].
  • Nudix hydrolase 16 is part of NUDIX hydrolase-like domain superfamily[4].
  • Nudix hydrolase 16 is part of NUDIX hydrolase domain, protein family[5].
  • Nudix hydrolase 16 comprises NUDIX hydrolase domain[6].
  • Nudix hydrolase 16's EC enzyme number is recorded as 3.6.1.64[7].
  • Nudix hydrolase 16's molecular function is recorded as cobalt ion binding[8].
  • Nudix hydrolase 16's molecular function is recorded as nucleotide binding[9].
  • Nudix hydrolase 16's molecular function is recorded as dIDP diphosphatase activity[10].
  • Nudix hydrolase 16's molecular function is recorded as m7G(5')pppN diphosphatase activity[11].
  • Nudix hydrolase 16's molecular function is recorded as manganese ion binding[12].
  • Nudix hydrolase 16's molecular function is recorded as protein homodimerization activity[13].
  • Nudix hydrolase 16's molecular function is recorded as XTP binding[14].
  • Nudix hydrolase 16's molecular function is recorded as GTP binding[15].
  • Nudix hydrolase 16's molecular function is recorded as metal ion binding[16].
  • Nudix hydrolase 16's molecular function is recorded as ITP binding[17].
  • Nudix hydrolase 16's molecular function is recorded as RNA binding[18].
  • Nudix hydrolase 16's molecular function is recorded as identical protein binding[19].
  • Nudix hydrolase 16's molecular function is recorded as metalloexopeptidase activity[20].
  • Nudix hydrolase 16's molecular function is recorded as hydrolase activity[21].
  • Nudix hydrolase 16's molecular function is recorded as mRNA binding[22].
  • Nudix hydrolase 16's molecular function is recorded as magnesium ion binding[23].
  • Nudix hydrolase 16's molecular function is recorded as snoRNA binding[24].
  • Nudix hydrolase 16's molecular function is recorded as inosine-diphosphatase activity[25].
  • Nudix hydrolase 16's molecular function is recorded as dITP diphosphatase activity[26].
  • Nudix hydrolase 16's molecular function is recorded as chloride ion binding[27].

Why It Matters

Nudix hydrolase 16 is known by 13 alternative names across languages and contexts.[2]

References

Programmatic citations — every numbered marker resolves to a verifiable graph row below.

Direct Wikidata claims

  1. [3] ↑ . Q905695. Retrieved . wikidata.org.
  2. [4] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  3. [5] ↑ . wikidata.org.
  4. [6] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  5. [7] ↑ . Swiss-Prot. Retrieved . uniprot.org. Provenance: wikidata.org.
  6. [8] ↑ . Metal determines efficiency and substrate specificity of the nuclear NUDIX decapping proteins X29 and H29K (Nudt16). Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  7. [9] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  8. [10] ↑ . NUDT16 is a (deoxy)inosine diphosphatase, and its deficiency induces accumulation of single-strand breaks in nuclear DNA and growth arrest. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  9. [11] ↑ . Evolutionary conservation supports ancient origin for Nudt16, a nuclear-localized, RNA-binding, RNA-decapping enzyme. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  10. [12] ↑ . Metal determines efficiency and substrate specificity of the nuclear NUDIX decapping proteins X29 and H29K (Nudt16). Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  11. [13] ↑ . Evolutionary conservation supports ancient origin for Nudt16, a nuclear-localized, RNA-binding, RNA-decapping enzyme. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  12. [14] ↑ . NUDT16 is a (deoxy)inosine diphosphatase, and its deficiency induces accumulation of single-strand breaks in nuclear DNA and growth arrest. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  13. [15] ↑ . NUDT16 is a (deoxy)inosine diphosphatase, and its deficiency induces accumulation of single-strand breaks in nuclear DNA and growth arrest. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  14. [16] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  15. [17] ↑ . NUDT16 is a (deoxy)inosine diphosphatase, and its deficiency induces accumulation of single-strand breaks in nuclear DNA and growth arrest. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  16. [18] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  17. [19] ↑ . Structural Basis for the Specificity of Human NUDT16 and Its Regulation by Inosine Monophosphate. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  18. [20] ↑ . hNUDT16: a universal decapping enzyme for small nucleolar RNA and cytoplasmic mRNA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  19. [21] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  20. [22] ↑ . hNUDT16: a universal decapping enzyme for small nucleolar RNA and cytoplasmic mRNA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  21. [23] ↑ . Hydrolytic activity of human Nudt16 enzyme on dinucleotide cap analogs and short capped oligonucleotides. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  22. [24] ↑ . Evolutionary conservation supports ancient origin for Nudt16, a nuclear-localized, RNA-binding, RNA-decapping enzyme. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  23. [25] ↑ . NUDT16 is a (deoxy)inosine diphosphatase, and its deficiency induces accumulation of single-strand breaks in nuclear DNA and growth arrest. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  24. [26] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  25. [27] ↑ . Hydrolytic activity of human Nudt16 enzyme on dinucleotide cap analogs and short capped oligonucleotides. Retrieved . ebi.ac.uk. Provenance: wikidata.org.

Class ancestry

  1. [1] ↑ . Wikidata. wikidata.org.

Aggregate / graph-position facts

  1. [2] ↑ . Wikidata aliases. wikidata.org.

📑 Cite this page

Use these citations when quoting this entity in research, articles, AI prompts, or wherever provenance matters. We aggregate Wikidata + Wikipedia + authoritative open-data sources; the stitched, scored, cross-referenced view is what 4ort.xyz contributes.

APA 4ort.xyz Knowledge Graph. (2026). Nudix hydrolase 16. Retrieved May 3, 2026, from https://4ort.xyz/entity/nudix-hydrolase-16
MLA “Nudix hydrolase 16.” 4ort.xyz Knowledge Graph, 4ort.xyz, 3 May. 2026, https://4ort.xyz/entity/nudix-hydrolase-16.
BibTeX @misc{4ortxyz_nudix-hydrolase-16_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{Nudix hydrolase 16}}, year = {2026}, url = {https://4ort.xyz/entity/nudix-hydrolase-16}, note = {Accessed: 2026-05-03}}
LLM prompt According to 4ort.xyz Knowledge Graph (aggregator of Wikidata, Wikipedia, and authoritative open-data sources): Nudix hydrolase 16 — https://4ort.xyz/entity/nudix-hydrolase-16 (retrieved 2026-05-03)

Canonical URL: https://4ort.xyz/entity/nudix-hydrolase-16 · Last refreshed:

Edit History

Rolling log of changes to this entity's Wikidata record. Values shown reflect the current state of each edited property — follow the history link to see the precise diff for any edit.

  1. 10w ago · Boghog · 2026-07-24 view diff on Wikidata ↗
    Ec enzyme number → 3.6.1.64
    Imported from → —
    Wikidata description → mammalian protein found in Homo sapiens
    Encoded by → NUDT16
    + 11 other properties edited (see Wikidata diff for full list)
    "/* wbcreateclaim-create:1| */ [[Property:P591]]: 3.6.1.62, [[:toollabs:quickstatements/#/batch/261491|batch #261491]]"
Live feed via Wikidata EventStreams. New edits appear within minutes of being made on Wikidata.