Peptidase D

mammalian protein found in Homo sapiens
Protein protein Q21119710
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Peptidase D

Summary

Peptidase D is a protein[1].

Key Facts

  • Peptidase D's instance of is recorded as protein[2].
  • Peptidase D is part of Creatinase/Aminopeptidase P/Spt16, N-terminal[3].
  • Peptidase D is part of Creatinase/aminopeptidase-like[4].
  • Peptidase D is part of Peptidase M24 family[5].
  • Peptidase D is part of Peptidase M24B, X-Pro dipeptidase/aminopeptidase P, conserved site, protein family[6].
  • Peptidase D is part of Aminopeptidase P, N-terminal domain, protein family[7].
  • Peptidase D comprises Peptidase M24[8].
  • Peptidase D comprises Peptidase M24B, X-Pro dipeptidase/aminopeptidase P, conserved site[9].
  • Peptidase D comprises Aminopeptidase P, N-terminal[10].
  • Peptidase D's molecular function is recorded as peptidase activity[11].
  • Peptidase D's molecular function is recorded as aminopeptidase activity[12].
  • Peptidase D's molecular function is recorded as protein binding[13].
  • Peptidase D's molecular function is recorded as hydrolase activity[14].
  • Peptidase D's molecular function is recorded as metallopeptidase activity[15].
  • Peptidase D's molecular function is recorded as dipeptidase activity[16].
  • Peptidase D's molecular function is recorded as manganese ion binding[17].
  • Peptidase D's molecular function is recorded as metal ion binding[18].
  • Peptidase D's molecular function is recorded as metallocarboxypeptidase activity[19].
  • Peptidase D's molecular function is recorded as proline dipeptidase activity[20].
  • Peptidase D's cell component is recorded as extracellular exosome[21].
  • Peptidase D's cell component is recorded as nucleus[22].
  • Peptidase D's cell component is recorded as nucleoplasm[23].
  • Peptidase D's cell component is recorded as extracellular exosome[24].
  • Peptidase D's biological process is recorded as collagen catabolic process[25].
  • Peptidase D's biological process is recorded as cellular amino acid metabolic process[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] ↑ . wikidata.org.
  5. [6] ↑ . wikidata.org.
  6. [7] ↑ . wikidata.org.
  7. [8] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  8. [9] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  9. [10] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  10. [11] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  11. [12] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  12. [13] ↑ . Genome-wide YFP fluorescence complementation screen identifies new regulators for telomere signaling in human cells. 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] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  17. [18] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  18. [19] ↑ . Structural organization of the gene for human prolidase (peptidase D) and demonstration of a partial gene deletion in a patient with prolidase deficiency. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  19. [20] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  20. [21] ↑ . Proteomic analysis of podocyte exosome-enriched fraction from normal human urine. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  21. [22] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  22. [23] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  23. [24] ↑ . Large-scale proteomics and phosphoproteomics of urinary exosomes. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  24. [25] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  25. [26] ↑ . Structural organization of the gene for human prolidase (peptidase D) and demonstration of a partial gene deletion in a patient with prolidase deficiency. 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). Peptidase D. Retrieved May 3, 2026, from https://4ort.xyz/entity/peptidase-d-q21119710
MLA “Peptidase D.” 4ort.xyz Knowledge Graph, 4ort.xyz, 3 May. 2026, https://4ort.xyz/entity/peptidase-d-q21119710.
BibTeX @misc{4ortxyz_peptidase-d-q21119710_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{Peptidase D}}, year = {2026}, url = {https://4ort.xyz/entity/peptidase-d-q21119710}, note = {Accessed: 2026-05-03}}
LLM prompt According to 4ort.xyz Knowledge Graph (aggregator of Wikidata, Wikipedia, and authoritative open-data sources): Peptidase D — https://4ort.xyz/entity/peptidase-d-q21119710 (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. 11w ago · Boghog · 2026-07-24 view diff on Wikidata ↗
    Imported from → —
    Encoded by → PEPD
    Wikidata description → mammalian protein found in Homo sapiens
    Molecular function → peptidase activity, aminopeptidase activity, protein binding +7
    + 11 other properties edited (see Wikidata diff for full list)
    "/* wbcreateclaim-create:1| */ [[Property:P591]]: 3.4.13.9, [[:toollabs:quickstatements/#/batch/261491|batch #261491]]"
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