Ribosomal protein L17

mammalian protein found in Rattus norvegicus
Protein protein Q28557667
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Ribosomal protein L17

Summary

Ribosomal protein L17 is a protein[1].

Key Facts

  • Ribosomal protein L17's instance of is recorded as protein[2].
  • Ribosomal protein L17's subclass of is recorded as protein[3].
  • Ribosomal protein L17's UniProt protein ID is recorded as P24049[4].
  • Ribosomal protein L17's part of is recorded as Ribosomal protein L22/L17, eukaryotic/archaeal[5].
  • Ribosomal protein L17's part of is recorded as Ribosomal protein L22/L17 superfamily[6].
  • Ribosomal protein L17's part of is recorded as Ribosomal protein L22/L17, conserved site, protein family[7].
  • Ribosomal protein L17's has part is recorded as Ribosomal protein L22/L17, conserved site[8].
  • Ribosomal protein L17's RefSeq protein ID is recorded as NP_958818[9].
  • Ribosomal protein L17's RefSeq protein ID is recorded as XP_038952567[10].
  • Ribosomal protein L17's molecular function is recorded as molecular function[11].
  • Ribosomal protein L17's molecular function is recorded as structural constituent of ribosome[12].
  • Ribosomal protein L17's molecular function is recorded as large ribosomal subunit rRNA binding[13].
  • Ribosomal protein L17's cell component is recorded as nucleus[14].
  • Ribosomal protein L17's cell component is recorded as ribosome[15].
  • Ribosomal protein L17's cell component is recorded as polysome[16].
  • Ribosomal protein L17's cell component is recorded as large ribosomal subunit[17].
  • Ribosomal protein L17's cell component is recorded as cytosolic large ribosomal subunit[18].
  • Ribosomal protein L17's cell component is recorded as A band[19].
  • Ribosomal protein L17's biological process is recorded as cytoplasmic translation[20].
  • Ribosomal protein L17's biological process is recorded as protein biosynthesis[21].
  • Ribosomal protein L17's biological process is recorded as cellular response to amino acid starvation[22].
  • Ribosomal protein L17's biological process is recorded as positive regulation of G1/S transition of mitotic cell cycle[23].
  • Ribosomal protein L17's biological process is recorded as response to amino acid starvation[24].
  • Ribosomal protein L17's encoded by is recorded as Rpl17[25].
  • Ribosomal protein L17's found in taxon is recorded as brown rat[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] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  5. [6] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  6. [7] ↑ . wikidata.org.
  7. [8] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  8. [9] ↑ . Q20641742. Retrieved . wikidata.org.
  9. [10] ↑ . Q20641742. Retrieved . wikidata.org.
  10. [11] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  11. [12] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  12. [13] ↑ . Carbodiimide-induced protein--RNA crosslinking in mammalian ribosomal subunits. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  13. [14] ↑ . Nuclear retention of the induced mRNA following amino acid-dependent transcriptional regulation of mammalian ribosomal proteins L17 and S25. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  14. [15] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  15. [16] ↑ . Nuclear retention of the induced mRNA following amino acid-dependent transcriptional regulation of mammalian ribosomal proteins L17 and S25. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  16. [17] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  17. [18] ↑ . Identification of an amino acid-regulated mRNA from rat liver as the mammalian equivalent of bacterial ribosomal protein L22. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  18. [19] ↑ . Immunological localization of ribosomes in striated rat muscle. Evidence for myofibrillar association and ontological changes in the subsarcolemmal:myofibrillar distribution. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  19. [20] ↑ . Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  20. [21] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  21. [22] ↑ . Nuclear retention of the induced mRNA following amino acid-dependent transcriptional regulation of mammalian ribosomal proteins L17 and S25. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  22. [23] ↑ . Ribosomal protein L17, RpL17, is an inhibitor of vascular smooth muscle growth and carotid intima formation. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  23. [24] ↑ . Liver-specific induction of ribosomal protein gene expression by amino acid starvation in rats. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  24. [25] ↑ . Q905695. Retrieved . wikidata.org.
  25. [26] ↑ . Q905695. Retrieved . wikidata.org.

Class ancestry

  1. [1] ↑ . Wikidata. wikidata.org.

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APA 4ort.xyz Knowledge Graph. (2026). Ribosomal protein L17. Retrieved May 3, 2026, from https://4ort.xyz/entity/ribosomal-protein-l17
MLA “Ribosomal protein L17.” 4ort.xyz Knowledge Graph, 4ort.xyz, 3 May. 2026, https://4ort.xyz/entity/ribosomal-protein-l17.
BibTeX @misc{4ortxyz_ribosomal-protein-l17_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{Ribosomal protein L17}}, year = {2026}, url = {https://4ort.xyz/entity/ribosomal-protein-l17}, note = {Accessed: 2026-05-03}}
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