CYLD lysine 63 deubiquitinase

mammalian protein found in Homo sapiens
Protein protein Q21117462
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Summary

CYLD lysine 63 deubiquitinase is a protein[1]. It is known by 10 alternative names across languages and contexts.[2]

Key Facts

  • Part of: CAP Gly-rich domain superfamily[3], Papain-like cysteine peptidase superfamily[4], Peptidase C19, ubiquitin carboxyl-terminal hydrolase family[5], CAP Gly-rich domain, protein family[6], Ubiquitin specific protease domain, protein family[7], Ubiquitin specific protease, conserved site, protein family[8]
  • Has part(s): CAP Gly-rich domain[9], Ubiquitin specific protease, conserved site[10], Ubiquitin specific protease domain[11], Peptidase C19, ubiquitin carboxyl-terminal hydrolase[12]
  • Molecular function: cysteine-type peptidase activity[13], zinc ion binding[14], metal ion binding[15], peptidase activity[16], protein binding[17], thiol-dependent deubiquitinase[18], proline-rich region binding[19], hydrolase activity[20], protein kinase binding[21], Lys63-specific deubiquitinase activity[22], Lys48-specific deubiquitinase activity[23], structural constituent of ribosome[24]
  • Cell component: cytoplasm[25], cytosol[26], centrosome[27], cell projection[28], membrane[29], extrinsic component of cytoplasmic side of plasma membrane[30], plasma membrane[31], spindle[32], microtubule organizing center[33], midbody[34], perinuclear region of cytoplasm[35], cytoplasmic microtubule[36], cytoskeleton[37], microtubule[38]
  • Biological process: regulation of intrinsic apoptotic signaling pathway[39], ubiquitin-dependent protein catabolic process[40], regulation of microtubule cytoskeleton organization[41], Wnt signaling pathway[42], proteolysis[43], protein K63-linked deubiquitination[44], regulation of mitotic cell cycle[45], positive regulation of extrinsic apoptotic signaling pathway[46], cell cycle[47], negative regulation of type I interferon production[48]

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] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: 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] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  12. [14] ↑ . The structure of the CYLD USP domain explains its specificity for Lys63-linked polyubiquitin and reveals a B box module. Retrieved . 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] ↑ . SPATA2-Mediated Binding of CYLD to HOIP Enables CYLD Recruitment to Signaling Complexes. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  16. [18] ↑ . The structure of the CYLD USP domain explains its specificity for Lys63-linked polyubiquitin and reveals a B box module. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  17. [19] ↑ . The CAP-Gly domain of CYLD associates with the proline-rich sequence in NEMO/IKKgamma. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  18. [20] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  19. [21] ↑ . The tumour suppressor CYLD is a negative regulator of RIG-I-mediated antiviral response. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  20. [22] ↑ . GOA. 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] ↑ . The deubiquitinating enzyme CYLD controls apical docking of basal bodies in ciliated epithelial cells. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  26. [28] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  27. [29] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  28. [30] ↑ . CYLD regulates angiogenesis by mediating vascular endothelial cell migration. 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] ↑ . The tumor suppressor CYLD regulates entry into mitosis. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  33. [35] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  34. [36] ↑ . The tumor suppressor CYLD regulates entry into mitosis. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  35. [37] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  36. [38] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  37. [39] ↑ . TWEAK Induces Apoptosis through a Death-signaling Complex Comprising Receptor-interacting Protein 1 (RIP1), Fas-associated Death Domain (FADD), and Caspase-8. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  38. [40] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  39. [41] ↑ . CYLD regulates angiogenesis by mediating vascular endothelial cell migration. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  40. [42] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  41. [43] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  42. [44] ↑ . The tumour suppressor CYLD is a negative regulator of RIG-I-mediated antiviral response. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  43. [45] ↑ . The tumor suppressor CYLD regulates entry into mitosis. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  44. [46] ↑ . TWEAK Induces Apoptosis through a Death-signaling Complex Comprising Receptor-interacting Protein 1 (RIP1), Fas-associated Death Domain (FADD), and Caspase-8. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  45. [47] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  46. [48] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.

Class ancestry

  1. [1] ↑ . Wikidata. wikidata.org.

Aggregate / graph-position facts

  1. [2] ↑ . Wikidata aliases. wikidata.org.

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APA 4ort.xyz Knowledge Graph. (2026). CYLD lysine 63 deubiquitinase. Retrieved May 3, 2026, from https://4ort.xyz/entity/cyld-lysine-63-deubiquitinase
MLA “CYLD lysine 63 deubiquitinase.” 4ort.xyz Knowledge Graph, 4ort.xyz, 3 May. 2026, https://4ort.xyz/entity/cyld-lysine-63-deubiquitinase.
BibTeX @misc{4ortxyz_cyld-lysine-63-deubiquitinase_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{CYLD lysine 63 deubiquitinase}}, year = {2026}, url = {https://4ort.xyz/entity/cyld-lysine-63-deubiquitinase}, note = {Accessed: 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. 13w ago · Boghog · 2026-07-24 view diff on Wikidata ↗
    Found in taxon → Homo sapiens
    Mesh tree code → D08.811.037.375, D12.776.624.776.482
    Wikidata description → mammalian protein found in Homo sapiens
    Pdb structure id → 1IXD, 1WHL, 1WHM +1
    + 14 other properties edited (see Wikidata diff for full list)
    "/* wbcreateclaim-create:1| */ Ec enzyme number: 3.4.19.12, [[:toollabs:quickstatements/#/batch/261491|batch #261491]]"
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