Carboxypeptidase E

mammalian protein found in Rattus norvegicus
Protein protein Q28556386
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Carboxypeptidase E

Summary

Carboxypeptidase E is a protein[1].

Key Facts

  • Carboxypeptidase E's instance of is recorded as protein[2].
  • Carboxypeptidase E's UniProt protein ID is recorded as P15087[3].
  • Carboxypeptidase E's part of is recorded as Carboxypeptidase-like, regulatory domain superfamily[4].
  • Carboxypeptidase E's part of is recorded as membrane protein[5].
  • Carboxypeptidase E's part of is recorded as Peptidase M14, carboxypeptidase A family[6].
  • Carboxypeptidase E's has part is recorded as Peptidase M14, carboxypeptidase A[7].
  • Carboxypeptidase E's RefSeq protein ID is recorded as NP_037260[8].
  • Carboxypeptidase E's molecular function is recorded as carboxypeptidase activity[9].
  • Carboxypeptidase E's molecular function is recorded as metallocarboxypeptidase activity[10].
  • Carboxypeptidase E's molecular function is recorded as protein binding[11].
  • Carboxypeptidase E's molecular function is recorded as peptidase activity[12].
  • Carboxypeptidase E's molecular function is recorded as metallopeptidase activity[13].
  • Carboxypeptidase E's molecular function is recorded as zinc ion binding[14].
  • Carboxypeptidase E's molecular function is recorded as hydrolase activity[15].
  • Carboxypeptidase E's molecular function is recorded as protein domain specific binding[16].
  • Carboxypeptidase E's molecular function is recorded as metal ion binding[17].
  • Carboxypeptidase E's molecular function is recorded as cobalt ion binding[18].
  • Carboxypeptidase E's molecular function is recorded as metallocarboxypeptidase activity[19].
  • Carboxypeptidase E's cell component is recorded as extracellular region[20].
  • Carboxypeptidase E's cell component is recorded as extracellular space[21].
  • Carboxypeptidase E's cell component is recorded as Golgi apparatus[22].
  • Carboxypeptidase E's cell component is recorded as membrane[23].
  • Carboxypeptidase E's cell component is recorded as secretory granule[24].
  • Carboxypeptidase E's cell component is recorded as dendrite[25].
  • Carboxypeptidase E's cell component is recorded as transport vesicle 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] ↑ . Q905695. Retrieved . wikidata.org.
  3. [4] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  4. [5] ↑ . wikidata.org.
  5. [6] ↑ . wikidata.org.
  6. [7] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  7. [8] ↑ . Q20641742. Retrieved . wikidata.org.
  8. [9] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  9. [10] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  10. [11] ↑ . Membrane-bound carboxypeptidase E facilitates the entry of eosinophil cationic protein into neuroendocrine cells. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  11. [12] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  12. [13] ↑ . GOA. 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] ↑ . NOS1AP regulates dendrite patterning of hippocampal neurons through a carboxypeptidase E-mediated pathway. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  16. [17] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  17. [18] ↑ . The insulin-secretory-granule carboxypeptidase H. Purification and demonstration of involvement in proinsulin processing. 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] ↑ . Glu300 of rat carboxypeptidase E is essential for enzymatic activity but not substrate binding or routing to the regulated secretory pathway. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  21. [22] ↑ . The pro region is not required for the expression or intracellular routeing of carboxypeptidase E. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  22. [23] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  23. [24] ↑ . The insulin-secretory-granule carboxypeptidase H. Purification and demonstration of involvement in proinsulin processing. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  24. [25] ↑ . Immunohistochemical expression and colocalization of somatostatin, carboxypeptidase-E and prohormone convertases 1 and 2 in rat brain. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  25. [26] ↑ . GOA. 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). Carboxypeptidase E. Retrieved May 3, 2026, from https://4ort.xyz/entity/carboxypeptidase-e-q28556386
MLA “Carboxypeptidase E.” 4ort.xyz Knowledge Graph, 4ort.xyz, 3 May. 2026, https://4ort.xyz/entity/carboxypeptidase-e-q28556386.
BibTeX @misc{4ortxyz_carboxypeptidase-e-q28556386_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{Carboxypeptidase E}}, year = {2026}, url = {https://4ort.xyz/entity/carboxypeptidase-e-q28556386}, note = {Accessed: 2026-05-03}}
LLM prompt According to 4ort.xyz Knowledge Graph (aggregator of Wikidata, Wikipedia, and authoritative open-data sources): Carboxypeptidase E — https://4ort.xyz/entity/carboxypeptidase-e-q28556386 (retrieved 2026-05-03)

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