tripeptidyl peptidase 1

mammalian protein found in Homo sapiens
Protein protein Q21136439
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tripeptidyl peptidase 1

Summary

tripeptidyl peptidase 1 is a protein[1].

Key Facts

  • tripeptidyl peptidase 1's instance of is recorded as protein[2].
  • tripeptidyl peptidase 1's subclass of is recorded as protein[3].
  • tripeptidyl peptidase 1's UniProt protein ID is recorded as O14773[4].
  • tripeptidyl peptidase 1's part of is recorded as Peptidase S8/S53 domain superfamily[5].
  • tripeptidyl peptidase 1's part of is recorded as Peptidase S53, activation domain, protein family[6].
  • tripeptidyl peptidase 1's part of is recorded as Sedolisin domain, protein family[7].
  • tripeptidyl peptidase 1's MeSH descriptor ID is recorded as D000091346[8].
  • tripeptidyl peptidase 1's has part is recorded as Sedolisin domain[9].
  • tripeptidyl peptidase 1's has part is recorded as Peptidase S53, activation domain[10].
  • tripeptidyl peptidase 1's RefSeq protein ID is recorded as NP_000382[11].
  • tripeptidyl peptidase 1's PDB structure ID is recorded as 3EDY[12].
  • tripeptidyl peptidase 1's PDB structure ID is recorded as 3EE6[13].
  • tripeptidyl peptidase 1's MeSH tree code is recorded as D08.811.277.656.350.100.877[14].
  • tripeptidyl peptidase 1's MeSH tree code is recorded as D08.811.277.656.350.350.843[15].
  • tripeptidyl peptidase 1's MeSH tree code is recorded as D08.811.277.656.959.780[16].
  • tripeptidyl peptidase 1's molecular function is recorded as tripeptidyl-peptidase activity[17].
  • tripeptidyl peptidase 1's molecular function is recorded as peptide binding[18].
  • tripeptidyl peptidase 1's molecular function is recorded as endopeptidase activity[19].
  • tripeptidyl peptidase 1's molecular function is recorded as metal ion binding[20].
  • tripeptidyl peptidase 1's molecular function is recorded as peptidase activity[21].
  • tripeptidyl peptidase 1's molecular function is recorded as protein binding[22].
  • tripeptidyl peptidase 1's molecular function is recorded as serine-type peptidase activity[23].
  • tripeptidyl peptidase 1's molecular function is recorded as serine-type endopeptidase activity[24].
  • tripeptidyl peptidase 1's molecular function is recorded as hydrolase activity[25].
  • tripeptidyl peptidase 1's molecular function is recorded as endopeptidase activity[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] . Q905695. Retrieved . wikidata.org.
  3. [4] . Q905695. Retrieved . wikidata.org.
  4. [5] . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  5. [6] . wikidata.org.
  6. [7] . wikidata.org.
  7. [8] . 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] . Q20641742. Retrieved . wikidata.org.
  11. [12] . Q905695. Retrieved . wikidata.org.
  12. [13] . Q905695. Retrieved . wikidata.org.
  13. [14] . wikidata.org.
  14. [15] . wikidata.org.
  15. [16] . wikidata.org.
  16. [17] . Characterization of endopeptidase activity of tripeptidyl peptidase-I/CLN2 protein which is deficient in classical late infantile neuronal ceroid lipofuscinosis. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  17. [18] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  18. [19] . Characterization of endopeptidase activity of tripeptidyl peptidase-I/CLN2 protein which is deficient in classical late infantile neuronal ceroid lipofuscinosis. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  19. [20] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  20. [21] . Association of Mutations in a Lysosomal Protein with Classical Late-Infantile Neuronal Ceroid Lipofuscinosis. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  21. [22] . Neuronal ceroid lipofuscinoses are connected at molecular level: interaction of CLN5 protein with CLN2 and CLN3. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  22. [23] . The human CLN2 protein/tripeptidyl-peptidase I is a serine protease that autoactivates at acidic pH. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  23. [24] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  24. [25] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  25. [26] . Characterization of endopeptidase activity of tripeptidyl peptidase-I/CLN2 protein which is deficient in classical late infantile neuronal ceroid lipofuscinosis. 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). tripeptidyl peptidase 1. Retrieved May 3, 2026, from https://4ort.xyz/entity/tripeptidyl-peptidase-1-q21136439
MLA “tripeptidyl peptidase 1.” 4ort.xyz Knowledge Graph, 4ort.xyz, 3 May. 2026, https://4ort.xyz/entity/tripeptidyl-peptidase-1-q21136439.
BibTeX @misc{4ortxyz_tripeptidyl-peptidase-1-q21136439_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{tripeptidyl peptidase 1}}, year = {2026}, url = {https://4ort.xyz/entity/tripeptidyl-peptidase-1-q21136439}, note = {Accessed: 2026-05-03}}
LLM prompt According to 4ort.xyz Knowledge Graph (aggregator of Wikidata, Wikipedia, and authoritative open-data sources): tripeptidyl peptidase 1 — https://4ort.xyz/entity/tripeptidyl-peptidase-1-q21136439 (retrieved 2026-05-03)

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