Putative metallocarboxypeptidase YHR132C

fungal protein found in Saccharomyces cerevisiae S288c
Protein protein Q27550766
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Putative metallocarboxypeptidase YHR132C

Summary

Putative metallocarboxypeptidase YHR132C is a protein[1].

Key Facts

  • Putative metallocarboxypeptidase YHR132C's instance of is recorded as protein[2].
  • Putative metallocarboxypeptidase YHR132C's subclass of is recorded as protein[3].
  • Putative metallocarboxypeptidase YHR132C's UniProt protein ID is recorded as P38836[4].
  • Putative metallocarboxypeptidase YHR132C's part of is recorded as Peptidase M14, carboxypeptidase A family[5].
  • Putative metallocarboxypeptidase YHR132C's has part is recorded as Peptidase M14, carboxypeptidase A[6].
  • Putative metallocarboxypeptidase YHR132C's RefSeq protein ID is recorded as NP_012000[7].
  • Putative metallocarboxypeptidase YHR132C's molecular function is recorded as zinc ion binding[8].
  • Putative metallocarboxypeptidase YHR132C's molecular function is recorded as metal ion binding[9].
  • Putative metallocarboxypeptidase YHR132C's molecular function is recorded as hydrolase activity[10].
  • Putative metallocarboxypeptidase YHR132C's molecular function is recorded as peptidase activity[11].
  • Putative metallocarboxypeptidase YHR132C's molecular function is recorded as metallocarboxypeptidase activity[12].
  • Putative metallocarboxypeptidase YHR132C's molecular function is recorded as carboxypeptidase activity[13].
  • Putative metallocarboxypeptidase YHR132C's molecular function is recorded as metallopeptidase activity[14].
  • Putative metallocarboxypeptidase YHR132C's molecular function is recorded as metalloendopeptidase activity[15].
  • Putative metallocarboxypeptidase YHR132C's cell component is recorded as vacuole[16].
  • Putative metallocarboxypeptidase YHR132C's cell component is recorded as extracellular space[17].
  • Putative metallocarboxypeptidase YHR132C's cell component is recorded as fungal-type vacuole[18].
  • Putative metallocarboxypeptidase YHR132C's biological process is recorded as cell wall organization[19].
  • Putative metallocarboxypeptidase YHR132C's biological process is recorded as proteolysis[20].
  • Putative metallocarboxypeptidase YHR132C's biological process is recorded as proteolysis[21].
  • Putative metallocarboxypeptidase YHR132C's encoded by is recorded as ECM14[22].
  • Putative metallocarboxypeptidase YHR132C's found in taxon is recorded as Saccharomyces cerevisiae S288c[23].
  • Putative metallocarboxypeptidase YHR132C's Ensembl protein ID is recorded as YHR132C[24].
  • Putative metallocarboxypeptidase YHR132C's Saccharomyces Genome Database ID is recorded as S000001174[25].

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] . wikidata.org.
  5. [6] . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  6. [7] . Q20641742. Retrieved . wikidata.org.
  7. [8] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  8. [9] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  9. [10] . GOA. Retrieved . 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] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  13. [14] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  14. [15] . Enhanced peptide secretion by gene disruption of CYM1, a novel protease in Saccharomyces cerevisiae. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  15. [16] . GOA. 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] . Global analysis of protein localization in budding yeast. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  18. [19] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  19. [20] . Enhanced peptide secretion by gene disruption of CYM1, a novel protease in Saccharomyces cerevisiae. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  20. [21] . Enhanced peptide secretion by gene disruption of CYM1, a novel protease in Saccharomyces cerevisiae. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  21. [22] . Q905695. Retrieved . wikidata.org.
  22. [23] . Q905695. Retrieved . wikidata.org.
  23. [24] . ensembl Release 106. wikidata.org.
  24. [25] . Q20641742. 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). Putative metallocarboxypeptidase YHR132C. Retrieved May 3, 2026, from https://4ort.xyz/entity/putative-metallocarboxypeptidase-yhr132c
MLA “Putative metallocarboxypeptidase YHR132C.” 4ort.xyz Knowledge Graph, 4ort.xyz, 3 May. 2026, https://4ort.xyz/entity/putative-metallocarboxypeptidase-yhr132c.
BibTeX @misc{4ortxyz_putative-metallocarboxypeptidase-yhr132c_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{Putative metallocarboxypeptidase YHR132C}}, year = {2026}, url = {https://4ort.xyz/entity/putative-metallocarboxypeptidase-yhr132c}, note = {Accessed: 2026-05-03}}
LLM prompt According to 4ort.xyz Knowledge Graph (aggregator of Wikidata, Wikipedia, and authoritative open-data sources): Putative metallocarboxypeptidase YHR132C — https://4ort.xyz/entity/putative-metallocarboxypeptidase-yhr132c (retrieved 2026-05-03)

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