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Serine-type carboxypeptidase YGL203C

fungal protein found in Saccharomyces cerevisiae S288c
Protein protein Q27550821
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Summary

Serine-type carboxypeptidase YGL203C is a protein[1].

Key Facts

  • Serine-type carboxypeptidase YGL203C's instance of is recorded as protein[2].
  • Serine-type carboxypeptidase YGL203C's UniProt protein ID is recorded as P09620[3].
  • Serine-type carboxypeptidase YGL203C's part of is recorded as Peptidase S10, serine carboxypeptidase[4].
  • Serine-type carboxypeptidase YGL203C's part of is recorded as Alpha/Beta hydrolase fold[5].
  • Serine-type carboxypeptidase YGL203C's part of is recorded as membrane protein[6].
  • Serine-type carboxypeptidase YGL203C's part of is recorded as Serine carboxypeptidase, serine active site, protein family[7].
  • Serine-type carboxypeptidase YGL203C's part of is recorded as Serine carboxypeptidases, histidine active site, protein family[8].
  • Serine-type carboxypeptidase YGL203C's has part is recorded as Serine carboxypeptidase, serine active site[9].
  • Serine-type carboxypeptidase YGL203C's has part is recorded as Serine carboxypeptidases, histidine active site[10].
  • Serine-type carboxypeptidase YGL203C's RefSeq protein ID is recorded as NP_011312[11].
  • Serine-type carboxypeptidase YGL203C's molecular function is recorded as carboxypeptidase activity[12].
  • Serine-type carboxypeptidase YGL203C's molecular function is recorded as hydrolase activity[13].
  • Serine-type carboxypeptidase YGL203C's molecular function is recorded as peptidase activity[14].
  • Serine-type carboxypeptidase YGL203C's molecular function is recorded as serine-type carboxypeptidase activity[15].
  • Serine-type carboxypeptidase YGL203C's molecular function is recorded as serine-type carboxypeptidase activity[16].
  • Serine-type carboxypeptidase YGL203C's cell component is recorded as membrane[17].
  • Serine-type carboxypeptidase YGL203C's cell component is recorded as Golgi apparatus[18].
  • Serine-type carboxypeptidase YGL203C's cell component is recorded as integral component of membrane[19].
  • Serine-type carboxypeptidase YGL203C's cell component is recorded as trans-Golgi network[20].
  • Serine-type carboxypeptidase YGL203C's cell component is recorded as trans-Golgi network[21].
  • Serine-type carboxypeptidase YGL203C's cell component is recorded as fungal-type vacuole[22].
  • Serine-type carboxypeptidase YGL203C's biological process is recorded as proteolysis[23].
  • Serine-type carboxypeptidase YGL203C's biological process is recorded as apoptotic process[24].
  • Serine-type carboxypeptidase YGL203C's biological process is recorded as proteolysis involved in cellular protein catabolic process[25].
  • Serine-type carboxypeptidase YGL203C's biological process is recorded as apoptotic process[26].

References

Programmatic citations — every numbered marker resolves to a verifiable graph row below.

Direct Wikidata claims

  1. [2] ↑ . UniProt. Retrieved . wikidata.org.
  2. [3] ↑ . UniProt. Retrieved . wikidata.org.
  3. [4] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: 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] ↑ . 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] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  16. [17] ↑ . GOA. 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] ↑ . Immunoisolation of Kex2p-containing organelles from yeast demonstrates colocalisation of three processing proteinases to a single Golgi compartment. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  20. [21] ↑ . Immunoisolation of Kex2p-containing organelles from yeast demonstrates colocalisation of three processing proteinases to a single Golgi compartment. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  21. [22] ↑ . One library to make them all: streamlining the creation of yeast libraries via a SWAp-Tag strategy. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  22. [23] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  23. [24] ↑ . The cell death protease Kex1p is essential for hypochlorite-induced apoptosis in yeast.. 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] ↑ . The cell death protease Kex1p is essential for hypochlorite-induced apoptosis in yeast.. Retrieved . ebi.ac.uk. Provenance: wikidata.org.

Class ancestry

  1. [1] ↑ . Wikidata. wikidata.org.

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APA 4ort.xyz Knowledge Graph. (2026). Serine-type carboxypeptidase YGL203C. Retrieved May 3, 2026, from https://4ort.xyz/entity/serine-type-carboxypeptidase-ygl203c
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BibTeX @misc{4ortxyz_serine-type-carboxypeptidase-ygl203c_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{Serine-type carboxypeptidase YGL203C}}, year = {2026}, url = {https://4ort.xyz/entity/serine-type-carboxypeptidase-ygl203c}, note = {Accessed: 2026-05-03}}
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