Polyubiquitin-binding protein UFD1 YGR048W

fungal protein found in Saccharomyces cerevisiae S288c
Protein protein Q27548232
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Summary

Polyubiquitin-binding protein UFD1 YGR048W is a protein[1].

Key Facts

  • Polyubiquitin-binding protein UFD1 YGR048W's instance of is recorded as protein[2].
  • Polyubiquitin-binding protein UFD1 YGR048W's subclass of is recorded as protein[3].
  • Polyubiquitin-binding protein UFD1 YGR048W's UniProt protein ID is recorded as P53044[4].
  • Polyubiquitin-binding protein UFD1 YGR048W's part of is recorded as Ubiquitin fusion degradation protein Ufd1-like[5].
  • Polyubiquitin-binding protein UFD1 YGR048W's RefSeq protein ID is recorded as NP_011562[6].
  • Polyubiquitin-binding protein UFD1 YGR048W's molecular function is recorded as polyubiquitin modification-dependent protein binding[7].
  • Polyubiquitin-binding protein UFD1 YGR048W's molecular function is recorded as ubiquitin binding[8].
  • Polyubiquitin-binding protein UFD1 YGR048W's molecular function is recorded as protein binding[9].
  • Polyubiquitin-binding protein UFD1 YGR048W's cell component is recorded as RQC complex[10].
  • Polyubiquitin-binding protein UFD1 YGR048W's cell component is recorded as Doa10p ubiquitin ligase complex[11].
  • Polyubiquitin-binding protein UFD1 YGR048W's cell component is recorded as VCP-NPL4-UFD1 AAA ATPase complex[12].
  • Polyubiquitin-binding protein UFD1 YGR048W's cell component is recorded as nucleus[13].
  • Polyubiquitin-binding protein UFD1 YGR048W's cell component is recorded as Hrd1p ubiquitin ligase ERAD-L complex[14].
  • Polyubiquitin-binding protein UFD1 YGR048W's cell component is recorded as nucleus[15].
  • Polyubiquitin-binding protein UFD1 YGR048W's cell component is recorded as cytosol[16].
  • Polyubiquitin-binding protein UFD1 YGR048W's biological process is recorded as ubiquitin-dependent ERAD pathway[17].
  • Polyubiquitin-binding protein UFD1 YGR048W's biological process is recorded as nonfunctional rRNA decay[18].
  • Polyubiquitin-binding protein UFD1 YGR048W's biological process is recorded as ER-associated misfolded protein catabolic process[19].
  • Polyubiquitin-binding protein UFD1 YGR048W's biological process is recorded as ubiquitin-dependent protein catabolic process[20].
  • Polyubiquitin-binding protein UFD1 YGR048W's biological process is recorded as positive regulation of protein localization to nucleus[21].
  • Polyubiquitin-binding protein UFD1 YGR048W's biological process is recorded as retrograde protein transport, ER to cytosol[22].
  • Polyubiquitin-binding protein UFD1 YGR048W's biological process is recorded as proteasome-mediated ubiquitin-dependent protein catabolic process[23].
  • Polyubiquitin-binding protein UFD1 YGR048W's biological process is recorded as negative regulation of telomerase activity[24].
  • Polyubiquitin-binding protein UFD1 YGR048W's biological process is recorded as cytoplasm protein quality control by the ubiquitin-proteasome system[25].
  • Polyubiquitin-binding protein UFD1 YGR048W's biological process is recorded as ribosome-associated 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] ↑ . UniProt. Retrieved . wikidata.org.
  4. [5] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  5. [6] ↑ . Q20641742. Retrieved . wikidata.org.
  6. [7] ↑ . Ufd1 exhibits the AAA-ATPase fold with two distinct ubiquitin interaction sites. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  7. [8] ↑ . Ufd1 exhibits the AAA-ATPase fold with two distinct ubiquitin interaction sites. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  8. [9] ↑ . Distinct ubiquitin-ligase complexes define convergent pathways for the degradation of ER proteins. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  9. [10] ↑ . A ribosome-bound quality control complex triggers degradation of nascent peptides and signals translation stress. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  10. [11] ↑ . Distinct ubiquitin-ligase complexes define convergent pathways for the degradation of ER proteins. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  11. [12] ↑ . Mobilization of processed, membrane-tethered SPT23 transcription factor by CDC48(UFD1/NPL4), a ubiquitin-selective chaperone. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  12. [13] ↑ . Mobilization of processed, membrane-tethered SPT23 transcription factor by CDC48(UFD1/NPL4), a ubiquitin-selective chaperone. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  13. [14] ↑ . Distinct ubiquitin-ligase complexes define convergent pathways for the degradation of ER proteins. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  14. [15] ↑ . Mobilization of processed, membrane-tethered SPT23 transcription factor by CDC48(UFD1/NPL4), a ubiquitin-selective chaperone. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  15. [16] ↑ . One library to make them all: streamlining the creation of yeast libraries via a SWAp-Tag strategy. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  16. [17] ↑ . HRD4/NPL4Is Required for the Proteasomal Processing of Ubiquitinated ER Proteins. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  17. [18] ↑ . 40S subunit dissociation and proteasome-dependent RNA degradation in nonfunctional 25S rRNA decay. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  18. [19] ↑ . The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  19. [20] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  20. [21] ↑ . Mobilization of processed, membrane-tethered SPT23 transcription factor by CDC48(UFD1/NPL4), a ubiquitin-selective chaperone. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  21. [22] ↑ . The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  22. [23] ↑ . The Cdc48–Ufd1–Npl4 complex is central in ubiquitin–proteasome triggered catabolite degradation of fructose-1,6-bisphosphatase. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  23. [24] ↑ . Proteomics of yeast telomerase identified Cdc48-Npl4-Ufd1 and Ufd4 as regulators of Est1 and telomere length. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  24. [25] ↑ . Degradation of a cytosolic protein requires endoplasmic reticulum-associated degradation machinery.. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  25. [26] ↑ . Cdc48/p97 promotes degradation of aberrant nascent polypeptides bound to the ribosome. Retrieved . ebi.ac.uk. Provenance: wikidata.org.

Class ancestry

  1. [1] ↑ . Wikidata. wikidata.org.

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APA 4ort.xyz Knowledge Graph. (2026). Polyubiquitin-binding protein UFD1 YGR048W. Retrieved May 3, 2026, from https://4ort.xyz/entity/polyubiquitin-binding-protein-ufd1-ygr048w
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BibTeX @misc{4ortxyz_polyubiquitin-binding-protein-ufd1-ygr048w_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{Polyubiquitin-binding protein UFD1 YGR048W}}, year = {2026}, url = {https://4ort.xyz/entity/polyubiquitin-binding-protein-ufd1-ygr048w}, note = {Accessed: 2026-05-03}}
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