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Beta-1,3-glucuronyltransferase 3

mammalian protein found in Homo sapiens
Protein protein Q21109519
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Summary

Beta-1,3-glucuronyltransferase 3 is a protein[1]. It is known by 9 alternative names across languages and contexts.[2]

Key Facts

  • Beta-1,3-glucuronyltransferase 3's instance of is recorded as protein[3].
  • Beta-1,3-glucuronyltransferase 3 is part of nucleotide-diphospho-sugar transferases[4].
  • Beta-1,3-glucuronyltransferase 3 is part of Glycosyl transferase, family 43[5].
  • Beta-1,3-glucuronyltransferase 3's molecular function is recorded as transferase activity[6].
  • Beta-1,3-glucuronyltransferase 3's molecular function is recorded as protein phosphatase activator activity[7].
  • Beta-1,3-glucuronyltransferase 3's molecular function is recorded as glucuronosyltransferase activity[8].
  • Beta-1,3-glucuronyltransferase 3's molecular function is recorded as metal ion binding[9].
  • Beta-1,3-glucuronyltransferase 3's molecular function is recorded as protein binding[10].
  • Beta-1,3-glucuronyltransferase 3's molecular function is recorded as galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase activity[11].
  • Beta-1,3-glucuronyltransferase 3's molecular function is recorded as galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase activity[12].
  • Beta-1,3-glucuronyltransferase 3's cell component is recorded as integral component of membrane[13].
  • Beta-1,3-glucuronyltransferase 3's cell component is recorded as Golgi apparatus[14].
  • Beta-1,3-glucuronyltransferase 3's cell component is recorded as membrane[15].
  • Beta-1,3-glucuronyltransferase 3's cell component is recorded as cis-Golgi network[16].
  • Beta-1,3-glucuronyltransferase 3's cell component is recorded as extracellular exosome[17].
  • Beta-1,3-glucuronyltransferase 3's cell component is recorded as Golgi membrane[18].
  • Beta-1,3-glucuronyltransferase 3's cell component is recorded as membrane[19].
  • Beta-1,3-glucuronyltransferase 3's cell component is recorded as extracellular exosome[20].
  • Beta-1,3-glucuronyltransferase 3's biological process is recorded as positive regulation of intracellular protein transport[21].
  • Beta-1,3-glucuronyltransferase 3's biological process is recorded as glycosaminoglycan metabolic process[22].
  • Beta-1,3-glucuronyltransferase 3's biological process is recorded as heparan sulfate proteoglycan biosynthetic process[23].
  • Beta-1,3-glucuronyltransferase 3's biological process is recorded as positive regulation of catalytic activity[24].
  • Beta-1,3-glucuronyltransferase 3's biological process is recorded as protein glycosylation[25].
  • Beta-1,3-glucuronyltransferase 3's biological process is recorded as glycosaminoglycan biosynthetic process[26].
  • Beta-1,3-glucuronyltransferase 3's biological process is recorded as chondroitin sulfate proteoglycan biosynthetic process[27].

Why It Matters

Beta-1,3-glucuronyltransferase 3 is known by 9 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] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  3. [5] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  4. [6] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  5. [7] ↑ . Identification of Phosphatase That Dephosphorylates Xylose in the Glycosaminoglycan-Protein Linkage Region of Proteoglycans. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  6. [8] ↑ . Faulty initiation of proteoglycan synthesis causes cardiac and joint defects. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  7. [9] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  8. [10] ↑ . Identification of Phosphatase That Dephosphorylates Xylose in the Glycosaminoglycan-Protein Linkage Region of Proteoglycans. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  9. [11] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  10. [12] ↑ . Structure/function of the human Ga1beta1,3-glucuronosyltransferase. Dimerization and functional activity are mediated by two crucial cysteine residues. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  11. [13] ↑ . Structure/function of the human Ga1beta1,3-glucuronosyltransferase. Dimerization and functional activity are mediated by two crucial cysteine residues. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  12. [14] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  13. [15] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  14. [16] ↑ . Faulty initiation of proteoglycan synthesis causes cardiac and joint defects. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  15. [17] ↑ . Proteomic analysis of podocyte exosome-enriched fraction from normal human urine. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  16. [18] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  17. [19] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  18. [20] ↑ . Proteomic analysis of human parotid gland exosomes by multidimensional protein identification technology (MudPIT). Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  19. [21] ↑ . Identification of Phosphatase That Dephosphorylates Xylose in the Glycosaminoglycan-Protein Linkage Region of Proteoglycans. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  20. [22] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  21. [23] ↑ . Skeletal dysplasia in a consanguineous clan from the island of Nias/Indonesia is caused by a novel mutation in B3GAT3. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  22. [24] ↑ . Identification of Phosphatase That Dephosphorylates Xylose in the Glycosaminoglycan-Protein Linkage Region of Proteoglycans. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  23. [25] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  24. [26] ↑ . Structure/function of the human Ga1beta1,3-glucuronosyltransferase. Dimerization and functional activity are mediated by two crucial cysteine residues. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  25. [27] ↑ . Skeletal dysplasia in a consanguineous clan from the island of Nias/Indonesia is caused by a novel mutation in B3GAT3. Retrieved . ebi.ac.uk. Provenance: wikidata.org.

Class ancestry

  1. [1] ↑ . Wikidata. wikidata.org.

Aggregate / graph-position facts

  1. [2] ↑ . Wikidata aliases. wikidata.org.

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APA 4ort.xyz Knowledge Graph. (2026). Beta-1,3-glucuronyltransferase 3. Retrieved May 3, 2026, from https://4ort.xyz/entity/beta-1-3-glucuronyltransferase-3
MLA “Beta-1,3-glucuronyltransferase 3.” 4ort.xyz Knowledge Graph, 4ort.xyz, 3 May. 2026, https://4ort.xyz/entity/beta-1-3-glucuronyltransferase-3.
BibTeX @misc{4ortxyz_beta-1-3-glucuronyltransferase-3_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{Beta-1,3-glucuronyltransferase 3}}, year = {2026}, url = {https://4ort.xyz/entity/beta-1-3-glucuronyltransferase-3}, 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 → B3GAT3
    Wikidata description → mammalian protein found in Homo sapiens
    Molecular function → transferase activity, protein phosphatase activator activity, glucuronosyltransferase activity +4
    + 10 other properties edited (see Wikidata diff for full list)
    "/* wbcreateclaim-create:1| */ Ec enzyme number: 2.4.1.135, [[:toollabs:quickstatements/#/batch/261491|batch #261491]]"
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