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Ring finger and FYVE like domain containing E3 ubiquitin protein ligase

mammalian protein found in Homo sapiens
Protein protein Q21123828
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Ring finger and FYVE like domain containing E3 ubiquitin protein ligase

Summary

Ring finger and FYVE like domain containing E3 ubiquitin protein ligase is a protein[1].

Key Facts

  • Ring finger and FYVE like domain containing E3 ubiquitin protein ligase's instance of is recorded as protein[2].
  • Ring finger and FYVE like domain containing E3 ubiquitin protein ligase is part of Zinc finger, FYVE/PHD-type[3].
  • Ring finger and FYVE like domain containing E3 ubiquitin protein ligase is part of Zinc finger, RING/FYVE/PHD-type[4].
  • Ring finger and FYVE like domain containing E3 ubiquitin protein ligase is part of SAP domain superfamily[5].
  • Ring finger and FYVE like domain containing E3 ubiquitin protein ligase is part of Zinc finger, RING-type, protein family[6].
  • Ring finger and FYVE like domain containing E3 ubiquitin protein ligase comprises Zinc finger, RING-type[7].
  • Ring finger and FYVE like domain containing E3 ubiquitin protein ligase's molecular function is recorded as p53 binding[8].
  • Ring finger and FYVE like domain containing E3 ubiquitin protein ligase's molecular function is recorded as metal ion binding[9].
  • Ring finger and FYVE like domain containing E3 ubiquitin protein ligase's molecular function is recorded as protease binding[10].
  • Ring finger and FYVE like domain containing E3 ubiquitin protein ligase's molecular function is recorded as protein binding[11].
  • Ring finger and FYVE like domain containing E3 ubiquitin protein ligase's molecular function is recorded as protein kinase binding[12].
  • Ring finger and FYVE like domain containing E3 ubiquitin protein ligase's molecular function is recorded as ubiquitin protein ligase binding[13].
  • Ring finger and FYVE like domain containing E3 ubiquitin protein ligase's molecular function is recorded as ubiquitin protein ligase activity[14].
  • Ring finger and FYVE like domain containing E3 ubiquitin protein ligase's molecular function is recorded as transferase activity[15].
  • Ring finger and FYVE like domain containing E3 ubiquitin protein ligase's molecular function is recorded as ubiquitin protein ligase activity[16].
  • Ring finger and FYVE like domain containing E3 ubiquitin protein ligase's cell component is recorded as cytoplasm[17].
  • Ring finger and FYVE like domain containing E3 ubiquitin protein ligase's cell component is recorded as cytosol[18].
  • Ring finger and FYVE like domain containing E3 ubiquitin protein ligase's cell component is recorded as endosome[19].
  • Ring finger and FYVE like domain containing E3 ubiquitin protein ligase's cell component is recorded as membrane[20].
  • Ring finger and FYVE like domain containing E3 ubiquitin protein ligase's cell component is recorded as plasma membrane[21].
  • Ring finger and FYVE like domain containing E3 ubiquitin protein ligase's cell component is recorded as Golgi membrane[22].
  • Ring finger and FYVE like domain containing E3 ubiquitin protein ligase's cell component is recorded as tumor necrosis factor receptor superfamily complex[23].
  • Ring finger and FYVE like domain containing E3 ubiquitin protein ligase's cell component is recorded as recycling endosome membrane[24].
  • Ring finger and FYVE like domain containing E3 ubiquitin protein ligase's cell component is recorded as lysosome[25].
  • Ring finger and FYVE like domain containing E3 ubiquitin protein ligase's cell component is recorded as endosome membrane[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] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  3. [4] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  4. [5] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  5. [6] ↑ . wikidata.org.
  6. [7] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  7. [8] ↑ . CARPs enhance p53 turnover by degrading 14-3-3sigma and stabilizing MDM2. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  8. [9] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  9. [10] ↑ . Suppression of caspase-8- and -10-associated RING proteins results in sensitization to death ligands and inhibition of tumor cell growth. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  10. [11] ↑ . PRR5L degradation promotes mTORC2-mediated PKC-δ phosphorylation and cell migration downstream of Gα12. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  11. [12] ↑ . CARP-2 is an endosome-associated ubiquitin ligase for RIP and regulates TNF-induced NF-kappaB activation. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  12. [13] ↑ . CARPs enhance p53 turnover by degrading 14-3-3sigma and stabilizing MDM2. 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] ↑ . CARPs are ubiquitin ligases that promote MDM2-independent p53 and phospho-p53ser20 degradation. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  16. [17] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  17. [18] ↑ . GOA. 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] ↑ . CARP-2 is an endosome-associated ubiquitin ligase for RIP and regulates TNF-induced NF-kappaB activation. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  22. [23] ↑ . CARP-2 is an endosome-associated ubiquitin ligase for RIP and regulates TNF-induced NF-kappaB activation. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  23. [24] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  24. [25] ↑ . CARP-2 is an endosome-associated ubiquitin ligase for RIP and regulates TNF-induced NF-kappaB activation. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  25. [26] ↑ . CARP-2 is an endosome-associated ubiquitin ligase for RIP and regulates TNF-induced NF-kappaB activation. Retrieved . ebi.ac.uk. Provenance: wikidata.org.

Class ancestry

  1. [1] ↑ . Wikidata. 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). Ring finger and FYVE like domain containing E3 ubiquitin protein ligase. Retrieved May 3, 2026, from https://4ort.xyz/entity/ring-finger-and-fyve-like-domain-containing-e3-ubiquitin-protein-ligase-q21123828
MLA “Ring finger and FYVE like domain containing E3 ubiquitin protein ligase.” 4ort.xyz Knowledge Graph, 4ort.xyz, 3 May. 2026, https://4ort.xyz/entity/ring-finger-and-fyve-like-domain-containing-e3-ubiquitin-protein-ligase-q21123828.
BibTeX @misc{4ortxyz_ring-finger-and-fyve-like-domain-containing-e3-ubiquitin-protein-ligase-q21123828_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{Ring finger and FYVE like domain containing E3 ubiquitin protein ligase}}, year = {2026}, url = {https://4ort.xyz/entity/ring-finger-and-fyve-like-domain-containing-e3-ubiquitin-protein-ligase-q21123828}, note = {Accessed: 2026-05-03}}
LLM prompt According to 4ort.xyz Knowledge Graph (aggregator of Wikidata, Wikipedia, and authoritative open-data sources): Ring finger and FYVE like domain containing E3 ubiquitin protein ligase — https://4ort.xyz/entity/ring-finger-and-fyve-like-domain-containing-e3-ubiquitin-protein-ligase-q21123828 (retrieved 2026-05-03)

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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. 18d ago · Boghog · 2026-07-24 view diff on Wikidata ↗
    Imported from → —
    Encoded by → RFFL
    Wikidata description → mammalian protein found in Homo sapiens
    Molecular function → p53 binding, metal ion binding, protease binding +6
    + 11 other properties edited (see Wikidata diff for full list)
    "/* wbcreateclaim-create:1| */ [[Property:P591]]: 2.3.2.27, [[:toollabs:quickstatements/#/batch/261491|batch #261491]]"
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