apolipoprotein B mRNA editing enzyme catalytic subunit 3G

mammalian protein found in Homo sapiens
Protein protein Q296209
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apolipoprotein B mRNA editing enzyme catalytic subunit 3G

Summary

apolipoprotein B mRNA editing enzyme catalytic subunit 3G is a protein[1].

Key Facts

  • apolipoprotein B mRNA editing enzyme catalytic subunit 3G's instance of is recorded as protein[2].
  • apolipoprotein B mRNA editing enzyme catalytic subunit 3G is part of Cytidine deaminase-like[3].
  • apolipoprotein B mRNA editing enzyme catalytic subunit 3G is part of Cytidine and deoxycytidylate deaminase domain, protein family[4].
  • apolipoprotein B mRNA editing enzyme catalytic subunit 3G is part of APOBEC/CMP deaminase, zinc-binding domain, protein family[5].
  • apolipoprotein B mRNA editing enzyme catalytic subunit 3G comprises Cytidine and deoxycytidylate deaminase domain[6].
  • apolipoprotein B mRNA editing enzyme catalytic subunit 3G comprises APOBEC/CMP deaminase, zinc-binding[7].
  • apolipoprotein B mRNA editing enzyme catalytic subunit 3G's molecular function is recorded as protein homodimerization activity[8].
  • apolipoprotein B mRNA editing enzyme catalytic subunit 3G's molecular function is recorded as cytidine deaminase activity[9].
  • apolipoprotein B mRNA editing enzyme catalytic subunit 3G's molecular function is recorded as protein binding[10].
  • apolipoprotein B mRNA editing enzyme catalytic subunit 3G's molecular function is recorded as catalytic activity[11].
  • apolipoprotein B mRNA editing enzyme catalytic subunit 3G's molecular function is recorded as hydrolase activity[12].
  • apolipoprotein B mRNA editing enzyme catalytic subunit 3G's molecular function is recorded as hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines[13].
  • apolipoprotein B mRNA editing enzyme catalytic subunit 3G's molecular function is recorded as metal ion binding[14].
  • apolipoprotein B mRNA editing enzyme catalytic subunit 3G's molecular function is recorded as deoxycytidine deaminase activity[15].
  • apolipoprotein B mRNA editing enzyme catalytic subunit 3G's molecular function is recorded as RNA binding[16].
  • apolipoprotein B mRNA editing enzyme catalytic subunit 3G's molecular function is recorded as zinc ion binding[17].
  • apolipoprotein B mRNA editing enzyme catalytic subunit 3G's molecular function is recorded as dCTP deaminase activity[18].
  • apolipoprotein B mRNA editing enzyme catalytic subunit 3G's molecular function is recorded as identical protein binding[19].
  • apolipoprotein B mRNA editing enzyme catalytic subunit 3G's molecular function is recorded as RNA binding[20].
  • apolipoprotein B mRNA editing enzyme catalytic subunit 3G's molecular function is recorded as cytidine deaminase activity[21].
  • apolipoprotein B mRNA editing enzyme catalytic subunit 3G's molecular function is recorded as cytidine deaminase activity[22].
  • apolipoprotein B mRNA editing enzyme catalytic subunit 3G's cell component is recorded as nucleus[23].
  • apolipoprotein B mRNA editing enzyme catalytic subunit 3G's cell component is recorded as apolipoprotein B mRNA editing enzyme complex[24].
  • apolipoprotein B mRNA editing enzyme catalytic subunit 3G's cell component is recorded as cytosol[25].
  • apolipoprotein B mRNA editing enzyme catalytic subunit 3G's cell component is recorded as cytoplasm[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] . 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] . An anthropoid-specific locus of orphan C to U RNA-editing enzymes on chromosome 22. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  8. [9] . APOBEC3F can inhibit the accumulation of HIV-1 reverse transcription products in the absence of hypermutation. Comparisons with APOBEC3G. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  9. [10] . HIV-1 Replication and APOBEC3 Antiviral Activity Are Not Regulated by P Bodies. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  10. [11] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  11. [12] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  12. [13] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  13. [14] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  14. [15] . The cytidine deaminase CEM15 induces hypermutation in newly synthesized HIV-1 DNA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  15. [16] . An anthropoid-specific locus of orphan C to U RNA-editing enzymes on chromosome 22. 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 the APOBEC3G catalytic domain reveals potential oligomerization interfaces. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  19. [20] . An anthropoid-specific locus of orphan C to U RNA-editing enzymes on chromosome 22. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  20. [21] . APOBEC3F can inhibit the accumulation of HIV-1 reverse transcription products in the absence of hypermutation. Comparisons with APOBEC3G. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  21. [22] . APOBEC3F can inhibit the accumulation of HIV-1 reverse transcription products in the absence of hypermutation. Comparisons with APOBEC3G. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  22. [23] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  23. [24] . APOBEC3F can inhibit the accumulation of HIV-1 reverse transcription products in the absence of hypermutation. Comparisons with APOBEC3G. 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). apolipoprotein B mRNA editing enzyme catalytic subunit 3G. Retrieved May 3, 2026, from https://4ort.xyz/entity/apolipoprotein-b-mrna-editing-enzyme-catalytic-subunit-3g
MLA “apolipoprotein B mRNA editing enzyme catalytic subunit 3G.” 4ort.xyz Knowledge Graph, 4ort.xyz, 3 May. 2026, https://4ort.xyz/entity/apolipoprotein-b-mrna-editing-enzyme-catalytic-subunit-3g.
BibTeX @misc{4ortxyz_apolipoprotein-b-mrna-editing-enzyme-catalytic-subunit-3g_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{apolipoprotein B mRNA editing enzyme catalytic subunit 3G}}, year = {2026}, url = {https://4ort.xyz/entity/apolipoprotein-b-mrna-editing-enzyme-catalytic-subunit-3g}, note = {Accessed: 2026-05-03}}
LLM prompt According to 4ort.xyz Knowledge Graph (aggregator of Wikidata, Wikipedia, and authoritative open-data sources): apolipoprotein B mRNA editing enzyme catalytic subunit 3G — https://4ort.xyz/entity/apolipoprotein-b-mrna-editing-enzyme-catalytic-subunit-3g (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. 4w ago · Boghog · 2026-07-23 view diff on Wikidata ↗
    Uniprot protein id Q9HC16
    Umls cui C4255227
    Exact match http://purl.uniprot.org/uniprot/Q9HC16
    Imported from
    + 15 other properties edited (see Wikidata diff for full list)
    "/* wbcreateclaim-create:1| */ [[Property:P591]]: 3.5.4.38, [[:toollabs:quickstatements/#/batch/261446|batch #261446]]"
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