Alpha-1,6-mannosyltransferase YJL183W

fungal protein found in Saccharomyces cerevisiae S288c
Protein protein Q27549723
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Summary

Alpha-1,6-mannosyltransferase YJL183W is a protein[1].

Key Facts

  • Alpha-1,6-mannosyltransferase YJL183W's instance of is recorded as protein[2].
  • Alpha-1,6-mannosyltransferase YJL183W's UniProt protein ID is recorded as P46985[3].
  • Alpha-1,6-mannosyltransferase YJL183W's part of is recorded as Glycosyltransferase 34[4].
  • Alpha-1,6-mannosyltransferase YJL183W's part of is recorded as membrane protein[5].
  • Alpha-1,6-mannosyltransferase YJL183W's RefSeq protein ID is recorded as NP_012352[6].
  • Alpha-1,6-mannosyltransferase YJL183W's molecular function is recorded as transferase activity[7].
  • Alpha-1,6-mannosyltransferase YJL183W's molecular function is recorded as glycosyltransferase activity[8].
  • Alpha-1,6-mannosyltransferase YJL183W's molecular function is recorded as alpha-1,6-mannosyltransferase activity[9].
  • Alpha-1,6-mannosyltransferase YJL183W's molecular function is recorded as protein binding[10].
  • Alpha-1,6-mannosyltransferase YJL183W's molecular function is recorded as alpha-1,6-mannosyltransferase activity[11].
  • Alpha-1,6-mannosyltransferase YJL183W's cell component is recorded as membrane[12].
  • Alpha-1,6-mannosyltransferase YJL183W's cell component is recorded as Golgi apparatus[13].
  • Alpha-1,6-mannosyltransferase YJL183W's cell component is recorded as integral component of membrane[14].
  • Alpha-1,6-mannosyltransferase YJL183W's cell component is recorded as mannan polymerase complex[15].
  • Alpha-1,6-mannosyltransferase YJL183W's cell component is recorded as mannan polymerase complex[16].
  • Alpha-1,6-mannosyltransferase YJL183W's cell component is recorded as Golgi membrane[17].
  • Alpha-1,6-mannosyltransferase YJL183W's cell component is recorded as endoplasmic reticulum[18].
  • Alpha-1,6-mannosyltransferase YJL183W's biological process is recorded as protein glycosylation[19].
  • Alpha-1,6-mannosyltransferase YJL183W's biological process is recorded as protein N-linked glycosylation[20].
  • Alpha-1,6-mannosyltransferase YJL183W's biological process is recorded as cell wall mannoprotein biosynthetic process[21].
  • Alpha-1,6-mannosyltransferase YJL183W's biological process is recorded as mannosylation[22].
  • Alpha-1,6-mannosyltransferase YJL183W's biological process is recorded as protein N-linked glycosylation[23].
  • Alpha-1,6-mannosyltransferase YJL183W's encoded by is recorded as MNN11[24].
  • Alpha-1,6-mannosyltransferase YJL183W's found in taxon is recorded as Saccharomyces cerevisiae S288c[25].
  • Alpha-1,6-mannosyltransferase YJL183W's Ensembl protein ID is recorded as YJL183W[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] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  8. [9] ↑ . Multi-protein complexes in the cis Golgi of Saccharomyces cerevisiae with alpha-1,6-mannosyltransferase activity. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  9. [10] ↑ . Proteome survey reveals modularity of the yeast cell machinery. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  10. [11] ↑ . Multi-protein complexes in the cis Golgi of Saccharomyces cerevisiae with alpha-1,6-mannosyltransferase activity. 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] ↑ . Multi-protein complexes in the cis Golgi of Saccharomyces cerevisiae with alpha-1,6-mannosyltransferase activity. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  15. [16] ↑ . Multi-protein complexes in the cis Golgi of Saccharomyces cerevisiae with alpha-1,6-mannosyltransferase activity. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  16. [17] ↑ . Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  17. [18] ↑ . One library to make them all: streamlining the creation of yeast libraries via a SWAp-Tag strategy. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  18. [19] ↑ . Interaction among the subunits of Golgi membrane mannosyltransferase complexes of the yeast Saccharomyces cerevisiae. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  19. [20] ↑ . Proper protein glycosylation promotes mitogen-activated protein kinase signal fidelity. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  20. [21] ↑ . The Saccharomyces cerevisiae protein Mnn10p/Bed1p is a subunit of a Golgi mannosyltransferase complex. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  21. [22] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  22. [23] ↑ . Proper protein glycosylation promotes mitogen-activated protein kinase signal fidelity. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  23. [24] ↑ . UniProt. Retrieved . wikidata.org.
  24. [25] ↑ . UniProt. Retrieved . wikidata.org.
  25. [26] ↑ . ensembl Release 106. wikidata.org.

Class ancestry

  1. [1] ↑ . Wikidata. wikidata.org.

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APA 4ort.xyz Knowledge Graph. (2026). Alpha-1,6-mannosyltransferase YJL183W. Retrieved May 3, 2026, from https://4ort.xyz/entity/alpha-1-6-mannosyltransferase-yjl183w
MLA “Alpha-1,6-mannosyltransferase YJL183W.” 4ort.xyz Knowledge Graph, 4ort.xyz, 3 May. 2026, https://4ort.xyz/entity/alpha-1-6-mannosyltransferase-yjl183w.
BibTeX @misc{4ortxyz_alpha-1-6-mannosyltransferase-yjl183w_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{Alpha-1,6-mannosyltransferase YJL183W}}, year = {2026}, url = {https://4ort.xyz/entity/alpha-1-6-mannosyltransferase-yjl183w}, note = {Accessed: 2026-05-03}}
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