Ubiquitin specific peptidase 8

mammalian protein found in Homo sapiens
Protein protein Q21105620
Press Enter · cited answer in seconds

Summary

Ubiquitin specific peptidase 8 is a protein[1]. It is known by 9 alternative names across languages and contexts.[2]

Key Facts

  • Part of: Rhodanese-like domain superfamily[3], Papain-like cysteine peptidase superfamily[4], Peptidase C19, ubiquitin carboxyl-terminal hydrolase family[5], USP8 dimerisation domain, protein family[6], Ubiquitin specific protease domain, protein family[7], Rhodanese-like domain, protein family[8], Ubiquitin specific protease, conserved site, protein family[9]
  • Has part(s): Peptidase C19, ubiquitin carboxyl-terminal hydrolase[10], Ubiquitin specific protease, conserved site[11], USP8 dimerisation domain[12], Rhodanese-like domain[13], Ubiquitin specific protease domain[14]
  • Molecular function: cysteine-type peptidase activity[15], SH3 domain binding[16], thiol-dependent deubiquitinase[17], peptidase activity[18], protein binding[19], cysteine-type endopeptidase activity[20], hydrolase activity[21], cadherin binding[22]
  • Cell component: cytoplasm[23], endosome[24], membrane[25], plasma membrane[26], extrinsic component of endosome membrane[27], midbody[28], endosome membrane[29], extrinsic component of plasma membrane[30], nucleus[31], postsynaptic density[32], dendritic spine[33], early endosome[34], cytosol[35], glutamatergic synapse[36]
  • Biological process: protein K48-linked deubiquitination[37], ubiquitin-dependent protein catabolic process[38], mitotic cytokinesis[39], endosome organization[40], proteolysis[41], protein K63-linked deubiquitination[42], cell cycle[43], cell population proliferation[44], protein deubiquitination[45], cellular response to dexamethasone stimulus[46], cellular response to nerve growth factor stimulus[47], positive regulation of canonical Wnt signaling pathway[48], Ras protein signal transduction[49], regulation of protein stability[50]

References

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

Direct Wikidata claims

  1. [3] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  2. [4] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  3. [5] ↑ . wikidata.org.
  4. [6] ↑ . wikidata.org.
  5. [7] ↑ . wikidata.org.
  6. [8] ↑ . wikidata.org.
  7. [9] ↑ . wikidata.org.
  8. [10] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  9. [11] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  10. [12] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  11. [13] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  12. [14] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  13. [15] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  14. [16] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  15. [17] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  16. [18] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  17. [19] ↑ . Final stages of cytokinesis and midbody ring formation are controlled by BRUCE. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  18. [20] ↑ . Deubiquitinating enzymes: a new class of biological regulators. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  19. [21] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  20. [22] ↑ . E-cadherin interactome complexity and robustness resolved by quantitative proteomics. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  21. [23] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  22. [24] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  23. [25] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  24. [26] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  25. [27] ↑ . Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  26. [28] ↑ . Dynamic regulation of ubiquitylation and deubiquitylation at the central spindle during cytokinesis. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  27. [29] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  28. [30] ↑ . The ubiquitin isopeptidase UBPY regulates endosomal ubiquitin dynamics and is essential for receptor down-regulation. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  29. [31] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  30. [32] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  31. [33] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  32. [34] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  33. [35] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  34. [36] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  35. [37] ↑ . The ubiquitin isopeptidase UBPY regulates endosomal ubiquitin dynamics and is essential for receptor down-regulation. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  36. [38] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  37. [39] ↑ . Dynamic regulation of ubiquitylation and deubiquitylation at the central spindle during cytokinesis. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  38. [40] ↑ . The ubiquitin isopeptidase UBPY regulates endosomal ubiquitin dynamics and is essential for receptor down-regulation. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  39. [41] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  40. [42] ↑ . The ubiquitin isopeptidase UBPY regulates endosomal ubiquitin dynamics and is essential for receptor down-regulation. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  41. [43] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  42. [44] ↑ . UBPY: a growth-regulated human ubiquitin isopeptidase.. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  43. [45] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  44. [46] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  45. [47] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  46. [48] ↑ . Balanced ubiquitylation and deubiquitylation of Frizzled regulate cellular responsiveness to Wg/Wnt. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  47. [49] ↑ . Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  48. [50] ↑ . The Endosome-associated Deubiquitinating Enzyme USP8 Regulates BACE1 Enzyme Ubiquitination and Degradation. 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). Ubiquitin specific peptidase 8. Retrieved May 3, 2026, from https://4ort.xyz/entity/ubiquitin-specific-peptidase-8
MLA “Ubiquitin specific peptidase 8.” 4ort.xyz Knowledge Graph, 4ort.xyz, 3 May. 2026, https://4ort.xyz/entity/ubiquitin-specific-peptidase-8.
BibTeX @misc{4ortxyz_ubiquitin-specific-peptidase-8_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{Ubiquitin specific peptidase 8}}, year = {2026}, url = {https://4ort.xyz/entity/ubiquitin-specific-peptidase-8}, note = {Accessed: 2026-05-03}}
LLM prompt According to 4ort.xyz Knowledge Graph (aggregator of Wikidata, Wikipedia, and authoritative open-data sources): Ubiquitin specific peptidase 8 — https://4ort.xyz/entity/ubiquitin-specific-peptidase-8 (retrieved 2026-05-03)

Canonical URL: https://4ort.xyz/entity/ubiquitin-specific-peptidase-8 · 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. 11w ago · Boghog · 2026-07-24 view diff on Wikidata ↗
    Imported from → —
    Encoded by → USP8
    Wikidata description → mammalian protein found in Homo sapiens
    Molecular function → cysteine-type peptidase activity, SH3 domain binding, thiol-dependent deubiquitinase +8
    + 11 other properties edited (see Wikidata diff for full list)
    "/* wbcreateclaim-create:1| */ Ec enzyme number: 3.4.19.12, [[:toollabs:quickstatements/#/batch/261489|batch #261489]]"
Live feed via Wikidata EventStreams. New edits appear within minutes of being made on Wikidata.