Serpin family A member 3

mammalian protein found in Homo sapiens
Protein protein Q4734974
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Serpin family A member 3

Summary

Serpin family A member 3 is a protein[1].

Key Facts

  • Serpin family A member 3's instance of is recorded as protein[2].
  • Serpin family A member 3's UniProt protein ID is recorded as P01011[3].
  • Serpin family A member 3's part of is recorded as Serpin superfamily[4].
  • Serpin family A member 3's part of is recorded as serpin family[5].
  • Serpin family A member 3's part of is recorded as Serpin, conserved site, protein family[6].
  • Serpin family A member 3's part of is recorded as Serpin domain, protein family[7].
  • Serpin family A member 3's has part is recorded as Serpin domain[8].
  • Serpin family A member 3's has part is recorded as Serpin, conserved site[9].
  • Serpin family A member 3's RefSeq protein ID is recorded as NP_001076[10].
  • Serpin family A member 3's PDB structure ID is recorded as 1AS4[11].
  • Serpin family A member 3's PDB structure ID is recorded as 1QMN[12].
  • Serpin family A member 3's PDB structure ID is recorded as 2ACH[13].
  • Serpin family A member 3's PDB structure ID is recorded as 3CAA[14].
  • Serpin family A member 3's PDB structure ID is recorded as 3DLW[15].
  • Serpin family A member 3's PDB structure ID is recorded as 4CAA[16].
  • Serpin family A member 3's Freebase ID is recorded as /m/025zd63[17].
  • Serpin family A member 3's molecular function is recorded as peptidase inhibitor activity[18].
  • Serpin family A member 3's molecular function is recorded as DNA binding[19].
  • Serpin family A member 3's molecular function is recorded as protein binding[20].
  • Serpin family A member 3's molecular function is recorded as serine-type endopeptidase inhibitor activity[21].
  • Serpin family A member 3's molecular function is recorded as serine-type endopeptidase inhibitor activity[22].
  • Serpin family A member 3's cell component is recorded as blood microparticle[23].
  • Serpin family A member 3's cell component is recorded as extracellular exosome[24].
  • Serpin family A member 3's cell component is recorded as intracellular anatomical structure[25].
  • Serpin family A member 3's cell component is recorded as nucleus[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] . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  8. [9] . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  9. [10] . Q20641742. Retrieved . wikidata.org.
  10. [11] . Q905695. Retrieved . wikidata.org.
  11. [12] . Q905695. Retrieved . wikidata.org.
  12. [13] . Q905695. Retrieved . wikidata.org.
  13. [14] . Q905695. Retrieved . wikidata.org.
  14. [15] . Q905695. Retrieved . wikidata.org.
  15. [16] . Q905695. Retrieved . wikidata.org.
  16. [17] . Freebase Data Dumps. wikidata.org.
  17. [18] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  18. [19] . The SANT2 domain of the murine tumor cell DnaJ-like protein 1 human homologue interacts with alpha1-antichymotrypsin and kinetically interferes with its serpin inhibitory activity. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  19. [20] . Purification of human kallikrein 6 from biological fluids and identification of its complex with alpha(1)-antichymotrypsin. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  20. [21] . Cloning, expression, purification, and biological activity of recombinant native and variant human alpha 1-antichymotrypsins. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  21. [22] . Cloning, expression, purification, and biological activity of recombinant native and variant human alpha 1-antichymotrypsins. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  22. [23] . Proteomic analysis of microvesicles from plasma of healthy donors reveals high individual variability. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  23. [24] . Proteomic analysis of podocyte exosome-enriched fraction from normal human urine. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  24. [25] . Molecular studies define the primary structure of alpha1-antichymotrypsin (ACT) protease inhibitor in Alzheimer's disease brains. Comparison of act in hippocampus and liver. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  25. [26] . The SANT2 domain of the murine tumor cell DnaJ-like protein 1 human homologue interacts with alpha1-antichymotrypsin and kinetically interferes with its serpin inhibitory activity. Retrieved . ebi.ac.uk. Provenance: wikidata.org.

Class ancestry

  1. [1] . Wikidata. wikidata.org.

📑 Cite this page

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). Serpin family A member 3. Retrieved May 3, 2026, from https://4ort.xyz/entity/serpin-family-a-member-3
MLA “Serpin family A member 3.” 4ort.xyz Knowledge Graph, 4ort.xyz, 3 May. 2026, https://4ort.xyz/entity/serpin-family-a-member-3.
BibTeX @misc{4ortxyz_serpin-family-a-member-3_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{Serpin family A member 3}}, year = {2026}, url = {https://4ort.xyz/entity/serpin-family-a-member-3}, note = {Accessed: 2026-05-03}}
LLM prompt According to 4ort.xyz Knowledge Graph (aggregator of Wikidata, Wikipedia, and authoritative open-data sources): Serpin family A member 3 — https://4ort.xyz/entity/serpin-family-a-member-3 (retrieved 2026-05-03)

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