Glucose-induced degradation complex subunit VID24 YBR105C

fungal protein found in Saccharomyces cerevisiae S288c
Protein protein Q27548989
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Summary

Glucose-induced degradation complex subunit VID24 YBR105C is a protein[1].

Key Facts

  • Glucose-induced degradation complex subunit VID24 YBR105C's instance of is recorded as protein[2].
  • Glucose-induced degradation complex subunit VID24 YBR105C's UniProt protein ID is recorded as P38263[3].
  • Glucose-induced degradation complex subunit VID24 YBR105C's part of is recorded as Vacuolar import/degradation protein Vid24[4].
  • Glucose-induced degradation complex subunit VID24 YBR105C's part of is recorded as membrane protein[5].
  • Glucose-induced degradation complex subunit VID24 YBR105C's RefSeq protein ID is recorded as NP_009663[6].
  • Glucose-induced degradation complex subunit VID24 YBR105C's molecular function is recorded as molecular function[7].
  • Glucose-induced degradation complex subunit VID24 YBR105C's molecular function is recorded as protein binding[8].
  • Glucose-induced degradation complex subunit VID24 YBR105C's cell component is recorded as cytoplasmic vesicle membrane[9].
  • Glucose-induced degradation complex subunit VID24 YBR105C's cell component is recorded as extrinsic component of membrane[10].
  • Glucose-induced degradation complex subunit VID24 YBR105C's cell component is recorded as membrane[11].
  • Glucose-induced degradation complex subunit VID24 YBR105C's cell component is recorded as GID complex[12].
  • Glucose-induced degradation complex subunit VID24 YBR105C's cell component is recorded as vacuole[13].
  • Glucose-induced degradation complex subunit VID24 YBR105C's cell component is recorded as cytoplasmic vesicle[14].
  • Glucose-induced degradation complex subunit VID24 YBR105C's cell component is recorded as extrinsic component of membrane[15].
  • Glucose-induced degradation complex subunit VID24 YBR105C's cell component is recorded as GID complex[16].
  • Glucose-induced degradation complex subunit VID24 YBR105C's cell component is recorded as cytosol[17].
  • Glucose-induced degradation complex subunit VID24 YBR105C's biological process is recorded as protein transport[18].
  • Glucose-induced degradation complex subunit VID24 YBR105C's biological process is recorded as negative regulation of gluconeogenesis[19].
  • Glucose-induced degradation complex subunit VID24 YBR105C's biological process is recorded as protein catabolic process in the vacuole[20].
  • Glucose-induced degradation complex subunit VID24 YBR105C's biological process is recorded as protein targeting to vacuole[21].
  • Glucose-induced degradation complex subunit VID24 YBR105C's biological process is recorded as proteasome-mediated ubiquitin-dependent protein catabolic process[22].
  • Glucose-induced degradation complex subunit VID24 YBR105C's biological process is recorded as ubiquitin-dependent protein catabolic process via the N-end rule pathway[23].
  • Glucose-induced degradation complex subunit VID24 YBR105C's biological process is recorded as protein targeting to vacuole[24].
  • Glucose-induced degradation complex subunit VID24 YBR105C's biological process is recorded as protein catabolic process in the vacuole[25].
  • Glucose-induced degradation complex subunit VID24 YBR105C's biological process is recorded as proteasome-mediated ubiquitin-dependent protein catabolic process[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] ↑ . Q20641742. Retrieved . wikidata.org.
  6. [7] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  7. [8] ↑ . Global landscape of protein complexes in the yeast Saccharomyces cerevisiae. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  8. [9] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  9. [10] ↑ . Vid24p, a Novel Protein Localized to the Fructose-1,6-bisphosphatase–containing Vesicles, Regulates Targeting of Fructose-1,6-bisphosphatase from the Vesicles to the Vacuole for Degradation. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  10. [11] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  11. [12] ↑ . The yeast GID complex, a novel ubiquitin ligase (E3) involved in the regulation of carbohydrate metabolism. 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] ↑ . Vid24p, a Novel Protein Localized to the Fructose-1,6-bisphosphatase–containing Vesicles, Regulates Targeting of Fructose-1,6-bisphosphatase from the Vesicles to the Vacuole for Degradation. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  15. [16] ↑ . PIPE: a protein-protein interaction prediction engine based on the re-occurring short polypeptide sequences between known interacting protein pairs. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  16. [17] ↑ . One library to make them all: streamlining the creation of yeast libraries via a SWAp-Tag strategy. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  17. [18] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  18. [19] ↑ . An N-end rule pathway that recognizes proline and destroys gluconeogenic enzymes. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  19. [20] ↑ . Degradation of the gluconeogenic enzymes fructose-1,6-bisphosphatase and malate dehydrogenase is mediated by distinct proteolytic pathways and signaling events. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  20. [21] ↑ . Vid24p, a Novel Protein Localized to the Fructose-1,6-bisphosphatase–containing Vesicles, Regulates Targeting of Fructose-1,6-bisphosphatase from the Vesicles to the Vacuole for Degradation. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  21. [22] ↑ . Degradation of the gluconeogenic enzymes fructose-1,6-bisphosphatase and malate dehydrogenase is mediated by distinct proteolytic pathways and signaling events. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  22. [23] ↑ . An N-end rule pathway that recognizes proline and destroys gluconeogenic enzymes. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  23. [24] ↑ . The Vid Vesicle to Vacuole Trafficking Event Requires Components of the SNARE Membrane Fusion Machinery. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  24. [25] ↑ . Degradation of the gluconeogenic enzymes fructose-1,6-bisphosphatase and malate dehydrogenase is mediated by distinct proteolytic pathways and signaling events. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  25. [26] ↑ . Catabolite degradation of fructose-1,6-bisphosphatase in the yeast Saccharomyces cerevisiae: a genome-wide screen identifies eight novel GID genes and indicates the existence of two degradation pathways. Retrieved . ebi.ac.uk. Provenance: wikidata.org.

Class ancestry

  1. [1] ↑ . Wikidata. wikidata.org.

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APA 4ort.xyz Knowledge Graph. (2026). Glucose-induced degradation complex subunit VID24 YBR105C. Retrieved May 3, 2026, from https://4ort.xyz/entity/glucose-induced-degradation-complex-subunit-vid24-ybr105c
MLA “Glucose-induced degradation complex subunit VID24 YBR105C.” 4ort.xyz Knowledge Graph, 4ort.xyz, 3 May. 2026, https://4ort.xyz/entity/glucose-induced-degradation-complex-subunit-vid24-ybr105c.
BibTeX @misc{4ortxyz_glucose-induced-degradation-complex-subunit-vid24-ybr105c_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{Glucose-induced degradation complex subunit VID24 YBR105C}}, year = {2026}, url = {https://4ort.xyz/entity/glucose-induced-degradation-complex-subunit-vid24-ybr105c}, note = {Accessed: 2026-05-03}}
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