Selenoprotein S

mammalian protein found in Homo sapiens
Protein protein Q21122067
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Summary

Selenoprotein S is a protein[1].

Key Facts

  • Selenoprotein S's instance of is recorded as protein[2].
  • Selenoprotein S's UniProt protein ID is recorded as Q9BQE4[3].
  • Selenoprotein S's part of is recorded as Selenoprotein S[4].
  • Selenoprotein S's RefSeq protein ID is recorded as NP_060915[5].
  • Selenoprotein S's RefSeq protein ID is recorded as NP_982298[6].
  • Selenoprotein S's PDB structure ID is recorded as 2Q2F[7].
  • Selenoprotein S's molecular function is recorded as ATPase binding[8].
  • Selenoprotein S's molecular function is recorded as antioxidant activity[9].
  • Selenoprotein S's molecular function is recorded as protein binding[10].
  • Selenoprotein S's molecular function is recorded as enzyme binding[11].
  • Selenoprotein S's molecular function is recorded as ubiquitin-specific protease binding[12].
  • Selenoprotein S's molecular function is recorded as signaling receptor activity[13].
  • Selenoprotein S's cell component is recorded as cytoplasm[14].
  • Selenoprotein S's cell component is recorded as integral component of membrane[15].
  • Selenoprotein S's cell component is recorded as membrane[16].
  • Selenoprotein S's cell component is recorded as Derlin-1-VIMP complex[17].
  • Selenoprotein S's cell component is recorded as plasma membrane[18].
  • Selenoprotein S's cell component is recorded as very-low-density lipoprotein particle[19].
  • Selenoprotein S's cell component is recorded as integral component of endoplasmic reticulum membrane[20].
  • Selenoprotein S's cell component is recorded as endoplasmic reticulum[21].
  • Selenoprotein S's cell component is recorded as low-density lipoprotein particle[22].
  • Selenoprotein S's cell component is recorded as Derlin-1 retrotranslocation complex[23].
  • Selenoprotein S's cell component is recorded as cytoplasmic microtubule[24].
  • Selenoprotein S's cell component is recorded as endoplasmic reticulum membrane[25].
  • Selenoprotein S's cell component is recorded as integral component of endoplasmic reticulum membrane[26].

References

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

Direct Wikidata claims

  1. [2] ↑ . UniProt. Retrieved . wikidata.org.
  2. [3] ↑ . UniProt. Retrieved . wikidata.org.
  3. [4] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  4. [5] ↑ . Q20641742. Retrieved . wikidata.org.
  5. [6] ↑ . Q20641742. Retrieved . wikidata.org.
  6. [7] ↑ . UniProt. Retrieved . wikidata.org.
  7. [8] ↑ . USP13 antagonizes gp78 to maintain functionality of a chaperone in ER-associated degradation. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  8. [9] ↑ . Regulation of the selenoprotein SelS by glucose deprivation and endoplasmic reticulum stress - SelS is a novel glucose-regulated protein. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  9. [10] ↑ . A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  10. [11] ↑ . A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  11. [12] ↑ . Regulation of retrotranslocation by p97-associated deubiquitinating enzyme ataxin-3. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  12. [13] ↑ . A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  13. [14] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  14. [15] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  15. [16] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  16. [17] ↑ . A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  17. [18] ↑ . Elevation in Tanis expression alters glucose metabolism and insulin sensitivity in H4IIE cells. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  18. [19] ↑ . Secretion of the glucose-regulated selenoprotein SEPS1 from hepatoma cells. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  19. [20] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  20. [21] ↑ . Recruitment of the p97 ATPase and ubiquitin ligases to the site of retrotranslocation at the endoplasmic reticulum membrane. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  21. [22] ↑ . Secretion of the glucose-regulated selenoprotein SEPS1 from hepatoma cells. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  22. [23] ↑ . A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  23. [24] ↑ . MTR120/KIAA1383, a novel microtubule-associated protein, promotes microtubule stability and ensures cytokinesis. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  24. [25] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  25. [26] ↑ . GOA. 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). Selenoprotein S. Retrieved May 3, 2026, from https://4ort.xyz/entity/selenoprotein-s-q21122067
MLA “Selenoprotein S.” 4ort.xyz Knowledge Graph, 4ort.xyz, 3 May. 2026, https://4ort.xyz/entity/selenoprotein-s-q21122067.
BibTeX @misc{4ortxyz_selenoprotein-s-q21122067_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{Selenoprotein S}}, year = {2026}, url = {https://4ort.xyz/entity/selenoprotein-s-q21122067}, note = {Accessed: 2026-05-03}}
LLM prompt According to 4ort.xyz Knowledge Graph (aggregator of Wikidata, Wikipedia, and authoritative open-data sources): Selenoprotein S — https://4ort.xyz/entity/selenoprotein-s-q21122067 (retrieved 2026-05-03)

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