Aspartyl protease YDR144C

fungal protein found in Saccharomyces cerevisiae S288c
Protein protein Q27551397
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Aspartyl protease YDR144C

Summary

Aspartyl protease YDR144C is a protein[1].

Key Facts

  • Aspartyl protease YDR144C's instance of is recorded as protein[2].
  • Aspartyl protease YDR144C's UniProt protein ID is recorded as P53379[3].
  • Aspartyl protease YDR144C's part of is recorded as Aspartic peptidase A1 family[4].
  • Aspartyl protease YDR144C's part of is recorded as Aspartic peptidase domain superfamily[5].
  • Aspartyl protease YDR144C's part of is recorded as membrane protein[6].
  • Aspartyl protease YDR144C's part of is recorded as Secreted aspartic endopeptidase family[7].
  • Aspartyl protease YDR144C's part of is recorded as Peptidase family A1 domain[8].
  • Aspartyl protease YDR144C's part of is recorded as Aspartic peptidase, active site, protein family[9].
  • Aspartyl protease YDR144C's has part is recorded as Secreted aspartic endopeptidase[10].
  • Aspartyl protease YDR144C's has part is recorded as Peptidase family A1 domain[11].
  • Aspartyl protease YDR144C's has part is recorded as Aspartic peptidase, active site[12].
  • Aspartyl protease YDR144C's RefSeq protein ID is recorded as NP_010428[13].
  • Aspartyl protease YDR144C's molecular function is recorded as aspartic-type endopeptidase activity[14].
  • Aspartyl protease YDR144C's molecular function is recorded as hydrolase activity[15].
  • Aspartyl protease YDR144C's molecular function is recorded as peptidase activity[16].
  • Aspartyl protease YDR144C's molecular function is recorded as aspartic-type endopeptidase activity[17].
  • Aspartyl protease YDR144C's cell component is recorded as anchored component of membrane[18].
  • Aspartyl protease YDR144C's cell component is recorded as plasma membrane[19].
  • Aspartyl protease YDR144C's cell component is recorded as fungal-type cell wall[20].
  • Aspartyl protease YDR144C's cell component is recorded as membrane[21].
  • Aspartyl protease YDR144C's cell component is recorded as extracellular region[22].
  • Aspartyl protease YDR144C's cell component is recorded as anchored component of external side of plasma membrane[23].
  • Aspartyl protease YDR144C's cell component is recorded as fungal-type cell wall[24].
  • Aspartyl protease YDR144C's cell component is recorded as fungal-type vacuole[25].
  • Aspartyl protease YDR144C's biological process is recorded as fungal-type cell wall organization[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] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  5. [6] ↑ . wikidata.org.
  6. [7] ↑ . wikidata.org.
  7. [8] ↑ . wikidata.org.
  8. [9] ↑ . 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] ↑ . 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] ↑ . Amino acid residues in the omega-minus region participate in cellular localization of yeast glycosylphosphatidylinositol-attached proteins. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  20. [21] ↑ . GOA. 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] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  23. [24] ↑ . Amino acid residues in the omega-minus region participate in cellular localization of yeast glycosylphosphatidylinositol-attached proteins. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  24. [25] ↑ . One library to make them all: streamlining the creation of yeast libraries via a SWAp-Tag strategy. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  25. [26] ↑ . Yapsins are a family of aspartyl proteases required for cell wall integrity in Saccharomyces cerevisiae.. 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). Aspartyl protease YDR144C. Retrieved May 3, 2026, from https://4ort.xyz/entity/aspartyl-protease-ydr144c
MLA “Aspartyl protease YDR144C.” 4ort.xyz Knowledge Graph, 4ort.xyz, 3 May. 2026, https://4ort.xyz/entity/aspartyl-protease-ydr144c.
BibTeX @misc{4ortxyz_aspartyl-protease-ydr144c_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{Aspartyl protease YDR144C}}, year = {2026}, url = {https://4ort.xyz/entity/aspartyl-protease-ydr144c}, note = {Accessed: 2026-05-03}}
LLM prompt According to 4ort.xyz Knowledge Graph (aggregator of Wikidata, Wikipedia, and authoritative open-data sources): Aspartyl protease YDR144C — https://4ort.xyz/entity/aspartyl-protease-ydr144c (retrieved 2026-05-03)

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