Nucleoside-triphosphatase YDL166C

fungal protein found in Saccharomyces cerevisiae S288c
Protein protein Q27552415
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Nucleoside-triphosphatase YDL166C

Summary

Nucleoside-triphosphatase YDL166C is a protein[1].

Key Facts

  • Nucleoside-triphosphatase YDL166C's instance of is recorded as protein[2].
  • Nucleoside-triphosphatase YDL166C's subclass of is recorded as protein[3].
  • Nucleoside-triphosphatase YDL166C's UniProt protein ID is recorded as Eilenburg[4].
  • Nucleoside-triphosphatase YDL166C's RefSeq protein ID is recorded as NP_010115[5].
  • Nucleoside-triphosphatase YDL166C's molecular function is recorded as kinase activity[6].
  • Nucleoside-triphosphatase YDL166C's molecular function is recorded as transferase activity[7].
  • Nucleoside-triphosphatase YDL166C's molecular function is recorded as nucleotide binding[8].
  • Nucleoside-triphosphatase YDL166C's molecular function is recorded as ATP binding[9].
  • Nucleoside-triphosphatase YDL166C's molecular function is recorded as adenylate kinase activity[10].
  • Nucleoside-triphosphatase YDL166C's molecular function is recorded as ATPase activity[11].
  • Nucleoside-triphosphatase YDL166C's molecular function is recorded as protein binding[12].
  • Nucleoside-triphosphatase YDL166C's molecular function is recorded as ATPase activity[13].
  • Nucleoside-triphosphatase YDL166C's cell component is recorded as nucleus[14].
  • Nucleoside-triphosphatase YDL166C's cell component is recorded as cytoplasm[15].
  • Nucleoside-triphosphatase YDL166C's cell component is recorded as cytoplasmic stress granule[16].
  • Nucleoside-triphosphatase YDL166C's cell component is recorded as nucleus[17].
  • Nucleoside-triphosphatase YDL166C's cell component is recorded as cytoplasm[18].
  • Nucleoside-triphosphatase YDL166C's biological process is recorded as ribosome biogenesis[19].
  • Nucleoside-triphosphatase YDL166C's biological process is recorded as transcription, DNA-templated[20].
  • Nucleoside-triphosphatase YDL166C's biological process is recorded as rRNA processing[21].
  • Nucleoside-triphosphatase YDL166C's biological process is recorded as phosphorylation[22].
  • Nucleoside-triphosphatase YDL166C's biological process is recorded as cellular response to oxidative stress[23].
  • Nucleoside-triphosphatase YDL166C's biological process is recorded as regulation of transcription, DNA-templated[24].
  • Nucleoside-triphosphatase YDL166C's biological process is recorded as nucleotide phosphorylation[25].
  • Nucleoside-triphosphatase YDL166C's biological process is recorded as maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA)[26].

References

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

Direct Wikidata claims

  1. [2] ↑ . Q905695. Retrieved . wikidata.org.
  2. [3] ↑ . Q905695. Retrieved . wikidata.org.
  3. [4] ↑ . Q905695. Retrieved . wikidata.org.
  4. [5] ↑ . Q20641742. Retrieved . wikidata.org.
  5. [6] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  6. [7] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  7. [8] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  8. [9] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  9. [10] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  10. [11] ↑ . RNA mimicry by the fap7 adenylate kinase in ribosome biogenesis. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  11. [12] ↑ . An inter-species protein-protein interaction network across vast evolutionary distance. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  12. [13] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  13. [14] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  14. [15] ↑ . The putative NTPase Fap7 mediates cytoplasmic 20S pre-rRNA processing through a direct interaction with Rps14.. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  15. [16] ↑ . ATPase-Modulated Stress Granules Contain a Diverse Proteome and Substructure.. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  16. [17] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  17. [18] ↑ . The putative NTPase Fap7 mediates cytoplasmic 20S pre-rRNA processing through a direct interaction with Rps14.. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  18. [19] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  19. [20] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  20. [21] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  21. [22] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  22. [23] ↑ . The essential protein fap7 is involved in the oxidative stress response of Saccharomyces cerevisiae. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  23. [24] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  24. [25] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  25. [26] ↑ . A panoramic view of yeast noncoding RNA processing. Retrieved . ebi.ac.uk. Provenance: wikidata.org.

Class ancestry

  1. [1] ↑ . Wikidata. wikidata.org.

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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). Nucleoside-triphosphatase YDL166C. Retrieved May 3, 2026, from https://4ort.xyz/entity/nucleoside-triphosphatase-ydl166c
MLA “Nucleoside-triphosphatase YDL166C.” 4ort.xyz Knowledge Graph, 4ort.xyz, 3 May. 2026, https://4ort.xyz/entity/nucleoside-triphosphatase-ydl166c.
BibTeX @misc{4ortxyz_nucleoside-triphosphatase-ydl166c_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{Nucleoside-triphosphatase YDL166C}}, year = {2026}, url = {https://4ort.xyz/entity/nucleoside-triphosphatase-ydl166c}, note = {Accessed: 2026-05-03}}
LLM prompt According to 4ort.xyz Knowledge Graph (aggregator of Wikidata, Wikipedia, and authoritative open-data sources): Nucleoside-triphosphatase YDL166C — https://4ort.xyz/entity/nucleoside-triphosphatase-ydl166c (retrieved 2026-05-03)

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