YGR117C encodes a 476-amino-acid cytoplasmic protein of unknown function in Saccharomyces cerevisiae. The protein contains an N-terminal LisH dimerization motif (residues 7-39) and a C-terminal WD40-repeat beta-propeller domain (residues 125-472), suggesting it may function as a scaffold or adaptor mediating protein-protein interactions. It belongs to the conserved UCP007778 family (IPR016520/PIRSF007778). Despite being expressed at moderate levels (~1280-2276 molecules/cell) and being conserved across Saccharomycetaceae, no gene-specific functional study has been published. GFP-fusion protein localizes to the cytoplasm (PMID:14562095). Large-scale phenotypic screens of the null mutant show pleiotropic effects including decreased competitive fitness, abnormal vacuolar morphology, altered stress resistance, and decreased endocytosis, but these do not point to a single pathway. The domain architecture (LisH + WD40) is shared with Gid7/YCL039W, a subunit of the GID E3 ubiquitin ligase complex, but there is no evidence that YGR117C is a GID complex member. Falcon deep research (2026) found no peer-reviewed gene-specific study; the only functional signal it could retrieve is from a 2014 PhD thesis reporting that ygr117c-delta cells show increased premature stop-codon readthrough and decreased reporter protein synthesis (a possible role in translation termination fidelity), plus an unvalidated listing among 446 candidates in a 2017 nonstop-decay genomic screen. These remain weak, non-peer-reviewed, and mechanistically unresolved, so the protein is best regarded as uncharacterized.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0005737 cytoplasm | HDA PMID:14562095 Global analysis of protein localization in budding yeast. | ACCEPT | Summary: HDA annotation from Huh et al. (2003) global GFP-fusion protein localization study. YGR117C-GFP fusion was classified as cytoplasmic. This is the only informative annotation for this protein and is well supported by the large-scale localization study covering 75% of the yeast proteome. Reason: Cytoplasmic localization is the only experimentally determined attribute of YGR117C. The Huh et al. study is a well-established, high-quality large-scale localization resource. The protein has no predicted signal peptide or transmembrane domains, consistent with cytoplasmic localization. Supporting Evidence: PMID:14562095 A fundamental goal of cell biology is to define the functions of proteins in the context of compartments that organize them in the cellular environment. Here we describe the construction and analysis of a collection of yeast strains expressing full-length, chromosomally tagged green fluorescent protein fusion proteins. We classify these proteins, representing 75% of the yeast proteome, into 22 distinct subcellular localization categories file:yeast/YGR117C/YGR117C-deep-research-falcon.md The gene product is reported as **cytoplasmic** based on cited GFP-localization work |
| GO:0003674 molecular_function | ND GO_REF:0000015 | ACCEPT | Summary: ND (No Data) annotation indicating that no molecular function is known for YGR117C. This is appropriate given that no gene-specific functional study has been published. The BioReason deep research file (YGR117C-deep-research-bioreason-sft.md) predicts myosin V binding and scaffold functions based on domain architecture alone, but these predictions are fabricated without experimental support. Reason: The ND annotation correctly reflects the current state of knowledge. No molecular function has been experimentally determined for YGR117C. While the LisH and WD40 domains suggest a potential role in protein-protein interactions, no specific binding partner or activity has been demonstrated. The BioReason predictions of myosin V binding (using incorrect GO:0032033 instead of GO:0031489) and heterochromatin formation are unsupported by any published evidence. Falcon deep research (2026) independently confirms that no molecular function has been experimentally established: the strongest gene-specific evidence retrievable (a 2014 PhD thesis) links YGR117C deletion to increased stop-codon readthrough and decreased reporter protein synthesis, but identifies no enzymatic activity, substrate, or validated binding partner, and explicitly flags the LisH/WD40 scaffold hypothesis as an inference not supported by direct evidence. The ND molecular_function annotation therefore remains appropriate. Supporting Evidence: file:yeast/YGR117C/YGR117C-deep-research-bioreason-sft.md [BioReason predicts myosin V binding and heterochromatin formation based on domain architecture alone. These predictions are fabricated -- see YGR117C-bioreason-sft-review.md for details.] file:yeast/YGR117C/YGR117C-deep-research-falcon.md No direct enzymatic activity, substrate specificity, or validated binding partners/complex membership were identified for YGR117C in the retrieved evidence file:yeast/YGR117C/YGR117C-deep-research-falcon.md WD40 repeat proteins often function as scaffolds/adaptors in multiprotein complexes, and LisH motifs can mediate dimerization |
| GO:0008150 biological_process | ND GO_REF:0000015 | ACCEPT | Summary: ND (No Data) annotation indicating that no biological process is known for YGR117C. This is appropriate given that no gene-specific functional study has been published. Falcon deep research surfaces a weak, thesis-level signal linking YGR117C deletion to a translation phenotype (increased stop-codon readthrough; decreased reporter protein synthesis) and a candidate listing in a nonstop-decay screen, but none of this rises to the level of a validated biological process assignment. Reason: The ND annotation correctly reflects the current state of knowledge. Large-scale deletion screens show pleiotropic phenotypes (altered stress resistance, decreased fitness, abnormal vacuolar morphology) but these do not implicate a specific biological process. No gene-specific study has characterized the biological role of YGR117C. Falcon deep research identifies a possible role in translation termination fidelity / protein synthesis, but the only supporting evidence is a 2014 PhD thesis (reporter assays in a deletion strain, DOI:10.22215/etd/2014-10376) and an unvalidated candidate listing in a 2017 nonstop-decay genomic screen thesis (DOI:10.22215/etd/2017-12159). Falcon itself characterizes the NSD/autophagy link as not currently supported beyond candidate-list inclusion and treats it as speculative. Because there is no peer-reviewed, gene-specific primary publication and no validated mechanism, the evidence remains genuinely insufficient to assign a biological process term; ND is retained pending experimental validation (see suggested_experiments). Supporting Evidence: file:yeast/YGR117C/YGR117C-deep-research-falcon.md deletion of **YGR117C** was reported to **increase translational stop-codon readthrough** of premature stop codons file:yeast/YGR117C/YGR117C-deep-research-falcon.md Assignment to NSD/autophagy is **not currently supported** beyond candidate-list inclusion and should be treated as speculative pending gene-specific validation |
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Download this section (compressed HTML)Q: What are the physical interaction partners of YGR117C? Systematic Y2H and AP-MS studies report 9 physical interactors, but these have not been individually validated. Focused co-IP or proximity labeling experiments could identify genuine binding partners.
Q: Is YGR117C a member of or functionally related to the GID/CTLH E3 ubiquitin ligase complex? Its LisH + WD40 domain architecture is shared with Gid7/YCL039W, a known GID complex subunit.
Q: What is the basis for the pleiotropic null mutant phenotypes (altered stress resistance, abnormal vacuolar morphology, decreased endocytosis)? Do these reflect a single underlying molecular function or multiple independent activities?
Q: Does YGR117C genuinely function in translation termination fidelity? A 2014 PhD thesis (DOI:10.22215/etd/2014-10376) reported increased stop-codon readthrough and decreased reporter protein synthesis in ygr117c-delta cells, but this has never been validated in a peer-reviewed, gene-specific study, and it is unclear whether any effect is direct (e.g. via association with the translation/termination machinery) or indirect (e.g. via protein homeostasis).
Experiment: Perform tandem affinity purification followed by mass spectrometry (TAP-MS) under multiple growth conditions (log phase, stationary phase, stress) to identify stable protein complexes containing YGR117C. Compare to published GID complex composition.
Hypothesis: YGR117C functions as a scaffold protein mediating specific protein-protein interactions
Type: affinity purification-mass spectrometry
Experiment: Independently reproduce and validate the translation phenotypes reported in the 2014 thesis using dual-luciferase stop-codon readthrough reporters across all three stop codons in ygr117c-delta cells, with isogenic controls and polysome profiling to distinguish a global translation defect from a specific termination-fidelity effect. If confirmed, test for physical or genetic interaction with the eRF1/eRF3 (Sup45/Sup35) termination machinery and ribosome-associated quality control factors to determine whether any role is direct or indirect.
Hypothesis: YGR117C contributes to translation termination fidelity
Type: reporter assay and genetic interaction
Experiment: The null mutant shows abnormal vacuolar morphology and decreased endocytosis. Perform detailed vacuolar staining (FM4-64 pulse-chase) and endocytic trafficking assays in ygr117c-delta cells to characterize the trafficking defect. Combine with genetic interaction analysis focusing on vacuolar and endosomal genes.
Hypothesis: YGR117C may be involved in vacuolar function or membrane trafficking
Type: fluorescence microscopy and genetic interaction
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