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ZFP36 ring finger protein

mammalian protein found in Homo sapiens
Protein protein Q21110024
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Summary

ZFP36 ring finger protein is a protein[1].

Key Facts

  • ZFP36 ring finger protein's instance of is recorded as protein[2].
  • ZFP36 ring finger protein's UniProt protein ID is recorded as P26651[3].
  • ZFP36 ring finger protein's part of is recorded as Zinc finger, CCCH-type superfamily[4].
  • ZFP36 ring finger protein's part of is recorded as Zinc finger, CCCH-type, protein family[5].
  • ZFP36 ring finger protein's MeSH descriptor ID is recorded as D051816[6].
  • ZFP36 ring finger protein's has part is recorded as Zinc finger, CCCH-type[7].
  • ZFP36 ring finger protein's RefSeq protein ID is recorded as NP_003398[8].
  • ZFP36 ring finger protein's PDB structure ID is recorded as 4J8S[9].
  • ZFP36 ring finger protein's MeSH tree code is recorded as D12.776.260.790[10].
  • ZFP36 ring finger protein's MeSH tree code is recorded as D12.776.460.762[11].
  • ZFP36 ring finger protein's MeSH tree code is recorded as D12.776.930.960[12].
  • ZFP36 ring finger protein's molecular function is recorded as DNA binding[13].
  • ZFP36 ring finger protein's molecular function is recorded as C-C chemokine binding[14].
  • ZFP36 ring finger protein's molecular function is recorded as 14-3-3 protein binding[15].
  • ZFP36 ring finger protein's molecular function is recorded as metal ion binding[16].
  • ZFP36 ring finger protein's molecular function is recorded as protein binding[17].
  • ZFP36 ring finger protein's molecular function is recorded as single-stranded RNA binding[18].
  • ZFP36 ring finger protein's molecular function is recorded as mRNA 3'-UTR AU-rich region binding[19].
  • ZFP36 ring finger protein's molecular function is recorded as enzyme binding[20].
  • ZFP36 ring finger protein's molecular function is recorded as mRNA binding[21].
  • ZFP36 ring finger protein's molecular function is recorded as protein kinase binding[22].
  • ZFP36 ring finger protein's molecular function is recorded as RNA binding[23].
  • ZFP36 ring finger protein's molecular function is recorded as heat shock protein binding[24].
  • ZFP36 ring finger protein's molecular function is recorded as RNA polymerase binding[25].
  • ZFP36 ring finger protein's molecular function is recorded as RNA binding[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] ↑ . wikidata.org.
  5. [6] ↑ . wikidata.org.
  6. [7] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  7. [8] ↑ . Q20641742. Retrieved . wikidata.org.
  8. [9] ↑ . UniProt. Retrieved . wikidata.org.
  9. [10] ↑ . wikidata.org.
  10. [11] ↑ . wikidata.org.
  11. [12] ↑ . wikidata.org.
  12. [13] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  13. [14] ↑ . Zinc finger protein tristetraprolin interacts with CCL3 mRNA and regulates tissue inflammation. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  14. [15] ↑ . MK2-induced tristetraprolin:14-3-3 complexes prevent stress granule association and ARE-mRNA decay. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  15. [16] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  16. [17] ↑ . Protor-2 interacts with tristetraprolin to regulate mRNA stability during stress. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  17. [18] ↑ . Feedback Inhibition of Macrophage Tumor Necrosis Factor-α Production by Tristetraprolin. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  18. [19] ↑ . The role of mRNA turnover in the regulation of tristetraprolin expression: evidence for an extracellular signal-regulated kinase-specific, AU-rich element-dependent, autoregulatory pathway. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  19. [20] ↑ . CNOT7/hCAF1 is involved in ICAM-1 and IL-8 regulation by tristetraprolin. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  20. [21] ↑ . Recruitment and activation of mRNA decay enzymes by two ARE-mediated decay activation domains in the proteins TTP and BRF-1. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  21. [22] ↑ . MK2-induced tristetraprolin:14-3-3 complexes prevent stress granule association and ARE-mRNA decay. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  22. [23] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  23. [24] ↑ . Phosphorylation of Human Tristetraprolin in Response to Its Interaction with the Cbl Interacting Protein CIN85. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  24. [25] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  25. [26] ↑ . GOA. 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). ZFP36 ring finger protein. Retrieved May 3, 2026, from https://4ort.xyz/entity/zfp36-ring-finger-protein-q21110024
MLA “ZFP36 ring finger protein.” 4ort.xyz Knowledge Graph, 4ort.xyz, 3 May. 2026, https://4ort.xyz/entity/zfp36-ring-finger-protein-q21110024.
BibTeX @misc{4ortxyz_zfp36-ring-finger-protein-q21110024_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{ZFP36 ring finger protein}}, year = {2026}, url = {https://4ort.xyz/entity/zfp36-ring-finger-protein-q21110024}, note = {Accessed: 2026-05-03}}
LLM prompt According to 4ort.xyz Knowledge Graph (aggregator of Wikidata, Wikipedia, and authoritative open-data sources): ZFP36 ring finger protein — https://4ort.xyz/entity/zfp36-ring-finger-protein-q21110024 (retrieved 2026-05-03)

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