Carboxypeptidase N subunit 2

mammalian protein found in Homo sapiens
Protein protein Q21115690
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Carboxypeptidase N subunit 2

Summary

Carboxypeptidase N subunit 2 is a protein[1].

Key Facts

  • Carboxypeptidase N subunit 2's instance of is recorded as protein[2].
  • Carboxypeptidase N subunit 2's UniProt protein ID is recorded as P22792[3].
  • Carboxypeptidase N subunit 2's part of is recorded as Leucine-rich repeat domain superfamily[4].
  • Carboxypeptidase N subunit 2's part of is recorded as Leucine-rich repeat N-terminal domain, protein family[5].
  • Carboxypeptidase N subunit 2's part of is recorded as Cysteine-rich flanking region, C-terminal domain, protein family[6].
  • Carboxypeptidase N subunit 2's part of is recorded as Leucine-rich repeat, typical subtype, protein family[7].
  • Carboxypeptidase N subunit 2's part of is recorded as Leucine-rich repeat, protein family[8].
  • Carboxypeptidase N subunit 2's has part is recorded as leucine-rich repeat N-terminal domain[9].
  • Carboxypeptidase N subunit 2's has part is recorded as leucine-rich repeat, typical subtype[10].
  • Carboxypeptidase N subunit 2's has part is recorded as cysteine-rich flanking region, C-terminal[11].
  • Carboxypeptidase N subunit 2's has part is recorded as Leucine-rich repeat[12].
  • Carboxypeptidase N subunit 2's RefSeq protein ID is recorded as NP_001073982[13].
  • Carboxypeptidase N subunit 2's RefSeq protein ID is recorded as NP_001278917[14].
  • Carboxypeptidase N subunit 2's RefSeq protein ID is recorded as XP_005269337[15].
  • Carboxypeptidase N subunit 2's molecular function is recorded as enzyme regulator activity[16].
  • Carboxypeptidase N subunit 2's molecular function is recorded as metallocarboxypeptidase activity[17].
  • Carboxypeptidase N subunit 2's cell component is recorded as blood microparticle[18].
  • Carboxypeptidase N subunit 2's cell component is recorded as extracellular exosome[19].
  • Carboxypeptidase N subunit 2's cell component is recorded as extracellular region[20].
  • Carboxypeptidase N subunit 2's cell component is recorded as extracellular space[21].
  • Carboxypeptidase N subunit 2's cell component is recorded as extracellular matrix[22].
  • Carboxypeptidase N subunit 2's cell component is recorded as extracellular exosome[23].
  • Carboxypeptidase N subunit 2's cell component is recorded as blood microparticle[24].
  • Carboxypeptidase N subunit 2's biological process is recorded as protein stabilization[25].
  • Carboxypeptidase N subunit 2's biological process is recorded as regulation of catalytic 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] . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  4. [5] . 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] . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  11. [12] . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  12. [13] . Q20641742. Retrieved . wikidata.org.
  13. [14] . Q20641742. Retrieved . wikidata.org.
  14. [15] . Q20641742. Retrieved . wikidata.org.
  15. [16] . The deduced protein sequence of the human carboxypeptidase N high molecular weight subunit reveals the presence of leucine-rich tandem repeats. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  16. [17] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  17. [18] . Proteomic analysis of microvesicles from plasma of healthy donors reveals high individual variability. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  18. [19] . Proteomic analysis of podocyte exosome-enriched fraction from normal human urine. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  19. [20] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  20. [21] . Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  21. [22] . Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  22. [23] . In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  23. [24] . Proteomic analysis of microvesicles from plasma of healthy donors reveals high individual variability. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  24. [25] . The deduced protein sequence of the human carboxypeptidase N high molecular weight subunit reveals the presence of leucine-rich tandem repeats. 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 N subunit 2. Retrieved May 3, 2026, from https://4ort.xyz/entity/carboxypeptidase-n-subunit-2
MLA “Carboxypeptidase N subunit 2.” 4ort.xyz Knowledge Graph, 4ort.xyz, 3 May. 2026, https://4ort.xyz/entity/carboxypeptidase-n-subunit-2.
BibTeX @misc{4ortxyz_carboxypeptidase-n-subunit-2_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{Carboxypeptidase N subunit 2}}, year = {2026}, url = {https://4ort.xyz/entity/carboxypeptidase-n-subunit-2}, note = {Accessed: 2026-05-03}}
LLM prompt According to 4ort.xyz Knowledge Graph (aggregator of Wikidata, Wikipedia, and authoritative open-data sources): Carboxypeptidase N subunit 2 — https://4ort.xyz/entity/carboxypeptidase-n-subunit-2 (retrieved 2026-05-03)

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