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Carboxylesterase 1C

mammalian protein found in Mus musculus
Protein protein Q21421187
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Carboxylesterase 1C

Summary

Carboxylesterase 1C is a protein[1].

Key Facts

  • Carboxylesterase 1C's instance of is recorded as protein[2].
  • Carboxylesterase 1C's subclass of is recorded as protein[3].
  • Carboxylesterase 1C's UniProt protein ID is recorded as P23953[4].
  • Carboxylesterase 1C's part of is recorded as Alpha/Beta hydrolase fold[5].
  • Carboxylesterase 1C's part of is recorded as Carboxylesterase type B[6].
  • Carboxylesterase 1C's part of is recorded as Carboxylesterase type B, active site, protein family[7].
  • Carboxylesterase 1C's part of is recorded as Carboxylesterase type B, conserved site, protein family[8].
  • Carboxylesterase 1C's has part is recorded as carboxylesterase, type B[9].
  • Carboxylesterase 1C's has part is recorded as carboxylesterase type B, conserved site[10].
  • Carboxylesterase 1C's has part is recorded as carboxylesterase type B, active site[11].
  • Carboxylesterase 1C's RefSeq protein ID is recorded as NP_031980[12].
  • Carboxylesterase 1C's molecular function is recorded as hydrolase activity, acting on ester bonds[13].
  • Carboxylesterase 1C's molecular function is recorded as carboxylic ester hydrolase activity[14].
  • Carboxylesterase 1C's molecular function is recorded as hydrolase activity[15].
  • Carboxylesterase 1C's molecular function is recorded as sterol esterase activity[16].
  • Carboxylesterase 1C's molecular function is recorded as triglyceride lipase activity[17].
  • Carboxylesterase 1C's molecular function is recorded as carboxylic ester hydrolase activity[18].
  • Carboxylesterase 1C's molecular function is recorded as methyl indole-3-acetate esterase activity[19].
  • Carboxylesterase 1C's cell component is recorded as endoplasmic reticulum lumen[20].
  • Carboxylesterase 1C's cell component is recorded as endoplasmic reticulum[21].
  • Carboxylesterase 1C's cell component is recorded as extracellular space[22].
  • Carboxylesterase 1C's cell component is recorded as extracellular space[23].
  • Carboxylesterase 1C's biological process is recorded as response to bacterium[24].
  • Carboxylesterase 1C's biological process is recorded as lipid catabolic process[25].
  • Carboxylesterase 1C's encoded by is recorded as Ces1c[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] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  11. [12] ↑ . Q20641742. Retrieved . wikidata.org.
  12. [13] ↑ . Esterase-6 (Es-6) in laboratory mice: Hormone-influenced expression and linkage relationship to oligosyndactylism (Os), esterase-1 (Es-1), and esterase-2 (Es-2) in chromosome 8. 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] ↑ . Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  16. [17] ↑ . Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  17. [18] ↑ . GOA. 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] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  21. [22] ↑ . Biochemistry and genetics of esterase-20 (ES-20), a second trimeric carboxylesterase of the house mouse (Mus musculus). II. A unique recombination reveals ES-20 as a hybrid enzyme. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  22. [23] ↑ . Biochemistry and genetics of esterase-20 (ES-20), a second trimeric carboxylesterase of the house mouse (Mus musculus). II. A unique recombination reveals ES-20 as a hybrid enzyme. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  23. [24] ↑ . Impact of lactobacilli on orally acquired listeriosis. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  24. [25] ↑ . Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  25. [26] ↑ . Q905695. Retrieved . 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). Carboxylesterase 1C. Retrieved May 3, 2026, from https://4ort.xyz/entity/carboxylesterase-1c
MLA “Carboxylesterase 1C.” 4ort.xyz Knowledge Graph, 4ort.xyz, 3 May. 2026, https://4ort.xyz/entity/carboxylesterase-1c.
BibTeX @misc{4ortxyz_carboxylesterase-1c_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{Carboxylesterase 1C}}, year = {2026}, url = {https://4ort.xyz/entity/carboxylesterase-1c}, note = {Accessed: 2026-05-03}}
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