ATP citrate lyase

mammalian protein found in Homo sapiens
Protein protein Q21096258
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Summary

ATP citrate lyase is a protein[1]. It is known by 6 alternative names across languages and contexts.[2]

Key Facts

  • ATP citrate lyase's instance of is recorded as protein[3].
  • ATP citrate lyase's physically interacts with is recorded as bempedoic acid[4].
  • ATP citrate lyase is part of NAD(P)-binding domain superfamily[5].
  • ATP citrate lyase is part of Citrate synthase superfamily[6].
  • ATP citrate lyase is part of ATP-citrate synthase, eukaryotic[7].
  • ATP citrate lyase is part of Citrate synthase-like, small alpha subdomain[8].
  • ATP citrate lyase is part of Succinyl-CoA synthetase-like[9].
  • ATP citrate lyase is part of ATP-citrate synthase, citrate-binding domain, protein family[10].
  • ATP citrate lyase is part of CoA-binding domain, protein family[11].
  • ATP citrate lyase is part of ATP-citrate lyase/succinyl-CoA ligase, active site, protein family[12].
  • ATP citrate lyase is part of ATP-citrate lyase/succinyl-CoA ligase family[13].
  • ATP citrate lyase is part of Succinyl-CoA synthetase, beta subunit, conserved site, protein family[14].
  • ATP citrate lyase is part of ATP-citrate lyase/succinyl-CoA ligase, conserved site, protein family[15].
  • ATP citrate lyase comprises CoA-binding[16].
  • ATP citrate lyase comprises Succinyl-CoA synthetase, beta subunit, conserved site[17].
  • ATP citrate lyase comprises ATP-citrate lyase/succinyl-CoA ligase[18].
  • ATP citrate lyase comprises ATP-citrate lyase/succinyl-CoA ligase, active site[19].
  • ATP citrate lyase comprises ATP-citrate synthase, citrate-binding domain[20].
  • ATP citrate lyase comprises ATP-citrate lyase/succinyl-CoA ligase, conserved site[21].
  • ATP citrate lyase's molecular function is recorded as transferase activity[22].
  • ATP citrate lyase's molecular function is recorded as ATP citrate synthase activity[23].
  • ATP citrate lyase's molecular function is recorded as nucleotide binding[24].
  • ATP citrate lyase's molecular function is recorded as metal ion binding[25].
  • ATP citrate lyase's molecular function is recorded as acyltransferase, acyl groups converted into alkyl on transfer[26].
  • ATP citrate lyase's molecular function is recorded as protein binding[27].

Why It Matters

ATP citrate lyase is known by 6 alternative names across languages and contexts.[2]

References

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

Direct Wikidata claims

  1. [3] ↑ . UniProt. Retrieved . wikidata.org.
  2. [4] ↑ . Open Targets Platform. Retrieved . platform.opentargets.org. Provenance: wikidata.org.
  3. [5] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  4. [6] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  5. [7] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  6. [8] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  7. [9] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  8. [10] ↑ . wikidata.org.
  9. [11] ↑ . wikidata.org.
  10. [12] ↑ . wikidata.org.
  11. [13] ↑ . wikidata.org.
  12. [14] ↑ . wikidata.org.
  13. [15] ↑ . wikidata.org.
  14. [16] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  15. [17] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  16. [18] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  17. [19] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  18. [20] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  19. [21] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  20. [22] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  21. [23] ↑ . Acetylation Stabilizes ATP-Citrate Lyase to Promote Lipid Biosynthesis and Tumor Growth. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  22. [24] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  23. [25] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  24. [26] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  25. [27] ↑ . Acetylation Stabilizes ATP-Citrate Lyase to Promote Lipid Biosynthesis and Tumor Growth. Retrieved . ebi.ac.uk. Provenance: wikidata.org.

Class ancestry

  1. [1] ↑ . Wikidata. wikidata.org.

Aggregate / graph-position facts

  1. [2] ↑ . Wikidata aliases. 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). ATP citrate lyase. Retrieved May 3, 2026, from https://4ort.xyz/entity/atp-citrate-lyase-q21096258
MLA “ATP citrate lyase.” 4ort.xyz Knowledge Graph, 4ort.xyz, 3 May. 2026, https://4ort.xyz/entity/atp-citrate-lyase-q21096258.
BibTeX @misc{4ortxyz_atp-citrate-lyase-q21096258_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{ATP citrate lyase}}, year = {2026}, url = {https://4ort.xyz/entity/atp-citrate-lyase-q21096258}, note = {Accessed: 2026-05-03}}
LLM prompt According to 4ort.xyz Knowledge Graph (aggregator of Wikidata, Wikipedia, and authoritative open-data sources): ATP citrate lyase — https://4ort.xyz/entity/atp-citrate-lyase-q21096258 (retrieved 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. 12w ago · Boghog · 2026-07-23 view diff on Wikidata ↗
    Uniprot protein id → P53396
    Umls cui → C0004199
    Imported from → —
    Mesh descriptor id → D001275
    + 15 other properties edited (see Wikidata diff for full list)
    "/* wbcreateclaim-create:1| */ Ec enzyme number: 2.3.3.8, [[:toollabs:quickstatements/#/batch/261457|batch #261457]]"
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