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Protein phosphatase 3 catalytic subunit alpha

mammalian protein found in Homo sapiens
Protein protein Q21132155
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Summary

Protein phosphatase 3 catalytic subunit alpha is a protein[1].

Key Facts

  • Protein phosphatase 3 catalytic subunit alpha's instance of is recorded as protein[2].
  • Protein phosphatase 3 catalytic subunit alpha is part of Metallo-dependent phosphatase-like[3].
  • Protein phosphatase 3 catalytic subunit alpha is part of Serine/threonine-specific protein phosphatase/bis(5-nucleosyl)-tetraphosphatase family[4].
  • Protein phosphatase 3 catalytic subunit alpha is part of Calcineurin-like phosphoesterase[5].
  • Protein phosphatase 3 catalytic subunit alpha comprises Serine/threonine-specific protein phosphatase/bis(5-nucleosyl)-tetraphosphatase[6].
  • Protein phosphatase 3 catalytic subunit alpha comprises Calcineurin-like phosphoesterase domain, ApaH type[7].
  • Protein phosphatase 3 catalytic subunit alpha's molecular function is recorded as calcium ion binding[8].
  • Protein phosphatase 3 catalytic subunit alpha's molecular function is recorded as phosphoprotein phosphatase activity[9].
  • Protein phosphatase 3 catalytic subunit alpha's molecular function is recorded as protein dimerization activity[10].
  • Protein phosphatase 3 catalytic subunit alpha's molecular function is recorded as protein serine/threonine phosphatase activity[11].
  • Protein phosphatase 3 catalytic subunit alpha's molecular function is recorded as metal ion binding[12].
  • Protein phosphatase 3 catalytic subunit alpha's molecular function is recorded as calmodulin binding[13].
  • Protein phosphatase 3 catalytic subunit alpha's molecular function is recorded as protein binding[14].
  • Protein phosphatase 3 catalytic subunit alpha's molecular function is recorded as protein heterodimerization activity[15].
  • Protein phosphatase 3 catalytic subunit alpha's molecular function is recorded as enzyme binding[16].
  • Protein phosphatase 3 catalytic subunit alpha's molecular function is recorded as calcium-dependent protein serine/threonine phosphatase activity[17].
  • Protein phosphatase 3 catalytic subunit alpha's molecular function is recorded as hydrolase activity[18].
  • Protein phosphatase 3 catalytic subunit alpha's molecular function is recorded as cyclosporin A binding[19].
  • Protein phosphatase 3 catalytic subunit alpha's molecular function is recorded as calmodulin-dependent protein phosphatase activity[20].
  • Protein phosphatase 3 catalytic subunit alpha's molecular function is recorded as calmodulin binding[21].
  • Protein phosphatase 3 catalytic subunit alpha's molecular function is recorded as calmodulin-dependent protein phosphatase activity[22].
  • Protein phosphatase 3 catalytic subunit alpha's molecular function is recorded as protein serine/threonine phosphatase activity[23].
  • Protein phosphatase 3 catalytic subunit alpha's cell component is recorded as membrane[24].
  • Protein phosphatase 3 catalytic subunit alpha's cell component is recorded as plasma membrane[25].
  • Protein phosphatase 3 catalytic subunit alpha's cell component is recorded as calcineurin complex[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] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  3. [4] ↑ . wikidata.org.
  4. [5] ↑ . wikidata.org.
  5. [6] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  6. [7] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  7. [8] ↑ . Molecular cloning of a full-length cDNA encoding the catalytic subunit of human calmodulin-dependent protein phosphatase (calcineurin A alpha). Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  8. [9] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  9. [10] ↑ . Genetic conservation of the immunophilin-binding domains of human calcineurin A1 and A2. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  10. [11] ↑ . Molecular cloning of a full-length cDNA encoding the catalytic subunit of human calmodulin-dependent protein phosphatase (calcineurin A alpha). Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  11. [12] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  12. [13] ↑ . Molecular cloning of a full-length cDNA encoding the catalytic subunit of human calmodulin-dependent protein phosphatase (calcineurin A alpha). Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  13. [14] ↑ . Investigating the human Calcineurin Interaction Network using the πɸLxVP SLiM.. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  14. [15] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  15. [16] ↑ . Genetic conservation of the immunophilin-binding domains of human calcineurin A1 and A2. 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] ↑ . Crystal structure of calcineurin-cyclophilin-cyclosporin shows common but distinct recognition of immunophilin-drug complexes. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  19. [20] ↑ . Cloning of human calcineurin A: evidence for two isozymes and identification of a polyproline structural domain. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  20. [21] ↑ . Molecular cloning of a full-length cDNA encoding the catalytic subunit of human calmodulin-dependent protein phosphatase (calcineurin A alpha). Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  21. [22] ↑ . Cloning of human calcineurin A: evidence for two isozymes and identification of a polyproline structural domain. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  22. [23] ↑ . Molecular cloning of a full-length cDNA encoding the catalytic subunit of human calmodulin-dependent protein phosphatase (calcineurin A alpha). Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  23. [24] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  24. [25] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  25. [26] ↑ . Molecular cloning of a full-length cDNA encoding the catalytic subunit of human calmodulin-dependent protein phosphatase (calcineurin A alpha). 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). Protein phosphatase 3 catalytic subunit alpha. Retrieved May 3, 2026, from https://4ort.xyz/entity/protein-phosphatase-3-catalytic-subunit-alpha
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BibTeX @misc{4ortxyz_protein-phosphatase-3-catalytic-subunit-alpha_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{Protein phosphatase 3 catalytic subunit alpha}}, year = {2026}, url = {https://4ort.xyz/entity/protein-phosphatase-3-catalytic-subunit-alpha}, note = {Accessed: 2026-05-03}}
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Edit History

Rolling log of changes to this entity's Wikidata record. Values shown reflect the current state of each edited property — follow the history link to see the precise diff for any edit.

  1. 11w ago · Boghog · 2026-07-24 view diff on Wikidata ↗
    Imported from → —
    Encoded by → PPP3CA
    Wikidata description → mammalian protein found in Homo sapiens
    Molecular function → calcium ion binding, phosphoprotein phosphatase activity, protein dimerization activity +13
    + 11 other properties edited (see Wikidata diff for full list)
    "/* wbcreateclaim-create:1| */ Ec enzyme number: 3.1.3.16, [[:toollabs:quickstatements/#/batch/261491|batch #261491]]"
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