Tif11p YMR260C

fungal protein found in Saccharomyces cerevisiae S288c
Protein protein Q27547343
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Tif11p YMR260C

Summary

Tif11p YMR260C is a protein[1].

Key Facts

  • Tif11p YMR260C's instance of is recorded as protein[2].
  • Tif11p YMR260C's subclass of is recorded as protein[3].
  • Tif11p YMR260C's UniProt protein ID is recorded as P38912[4].
  • Tif11p YMR260C's part of is recorded as Nucleic acid-binding, OB-fold[5].
  • Tif11p YMR260C's part of is recorded as Translation initiation factor 1A (eIF-1A)[6].
  • Tif11p YMR260C's part of is recorded as Translation initiation factor 1A (eIF-1A), conserved site, protein family[7].
  • Tif11p YMR260C's part of is recorded as RNA-binding domain, S1, IF1 type, protein family[8].
  • Tif11p YMR260C's has part is recorded as RNA-binding domain, S1, IF1 type[9].
  • Tif11p YMR260C's has part is recorded as Translation initiation factor 1A (eIF-1A), conserved site[10].
  • Tif11p YMR260C's RefSeq protein ID is recorded as NP_013987[11].
  • Tif11p YMR260C's molecular function is recorded as double-stranded RNA binding[12].
  • Tif11p YMR260C's molecular function is recorded as ribosomal small subunit binding[13].
  • Tif11p YMR260C's molecular function is recorded as translation initiation factor activity[14].
  • Tif11p YMR260C's molecular function is recorded as translation initiation factor binding[15].
  • Tif11p YMR260C's molecular function is recorded as RNA binding[16].
  • Tif11p YMR260C's molecular function is recorded as protein kinase binding[17].
  • Tif11p YMR260C's cell component is recorded as eukaryotic 43S preinitiation complex[18].
  • Tif11p YMR260C's cell component is recorded as eukaryotic 48S preinitiation complex[19].
  • Tif11p YMR260C's cell component is recorded as cytoplasmic stress granule[20].
  • Tif11p YMR260C's biological process is recorded as formation of translation preinitiation complex[21].
  • Tif11p YMR260C's biological process is recorded as formation of cytoplasmic translation initiation complex[22].
  • Tif11p YMR260C's biological process is recorded as protein biosynthesis[23].
  • Tif11p YMR260C's biological process is recorded as translational initiation[24].
  • Tif11p YMR260C's encoded by is recorded as TIF11[25].
  • Tif11p YMR260C's found in taxon is recorded as Saccharomyces cerevisiae S288c[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] . Q20641742. Retrieved . wikidata.org.
  3. [4] . Q905695. Retrieved . wikidata.org.
  4. [5] . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  5. [6] . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  6. [7] . wikidata.org.
  7. [8] . wikidata.org.
  8. [9] . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  9. [10] . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  10. [11] . Q20641742. Retrieved . wikidata.org.
  11. [12] . Translation initiation factor eIF1A possesses RNA annealing activity in its oligonucleotide-binding fold. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  12. [13] . The eukaryotic translation initiation factors eIF1 and eIF1A induce an open conformation of the 40S ribosome. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  13. [14] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  14. [15] . Physical and functional interaction between the eukaryotic orthologs of prokaryotic translation initiation factors IF1 and IF2. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  15. [16] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  16. [17] . Evidence that eukaryotic translation elongation factor 1A (eEF1A) binds the Gcn2 protein C terminus and inhibits Gcn2 activity. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  17. [18] . Communication between eukaryotic translation initiation factors 5 and 1A within the ribosomal pre-initiation complex plays a role in start site selection. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  18. [19] . Coupled release of eukaryotic translation initiation factors 5B and 1A from 80S ribosomes following subunit joining.. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  19. [20] . ATPase-Modulated Stress Granules Contain a Diverse Proteome and Substructure.. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  20. [21] . Study of translational control of eukaryotic gene expression using yeast.. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  21. [22] . Interaction between eukaryotic initiation factors 1A and 5B is required for efficient ribosomal subunit joining.. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  22. [23] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  23. [24] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  24. [25] . Q905695. Retrieved . wikidata.org.
  25. [26] . Q905695. Retrieved . 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). Tif11p YMR260C. Retrieved May 3, 2026, from https://4ort.xyz/entity/tif11p-ymr260c
MLA “Tif11p YMR260C.” 4ort.xyz Knowledge Graph, 4ort.xyz, 3 May. 2026, https://4ort.xyz/entity/tif11p-ymr260c.
BibTeX @misc{4ortxyz_tif11p-ymr260c_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{Tif11p YMR260C}}, year = {2026}, url = {https://4ort.xyz/entity/tif11p-ymr260c}, note = {Accessed: 2026-05-03}}
LLM prompt According to 4ort.xyz Knowledge Graph (aggregator of Wikidata, Wikipedia, and authoritative open-data sources): Tif11p YMR260C — https://4ort.xyz/entity/tif11p-ymr260c (retrieved 2026-05-03)

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