The ubiquitin ligase complex annotation on MOH1 is a phylogenetically propagated (IBA) inference from PANTHER family PTHR13848, seeded by human YPEL5 (UniProtKB:P62699). YPEL5 is curated as an ancillary subunit of the human CTLH E3 ubiquitin ligase, and the single yeast ortholog Moh1 has yeast AP-MS evidence for association with core GID E3-ligase subunits.

MOH1 is included among 582 known or potential zinc-binding proteins identified by a proteome-wide bioinformatic domain/motif survey; this is the basis of the RCA zinc ion binding annotation, a prediction rather than a direct metal-binding assay of Moh1.

moh1 deletion increases cell viability under multiple lethal stresses (UV, MMS, camptothecin, heat, hyperosmotic shock), and Moh1 is stress-induced; human YPEL genes partially complement moh1delta. Framed by the authors as involvement in DNA-damage-induced, mitochondria-dependent regulated cell death.

moh1 deletion causes stress-specific phenotypes, increases hydrogen-peroxide and acetic-acid resistance, increases sodium-azide and sulfuric-acid sensitivity, remodels the cell envelope, and reduces intracellular hydrogen-peroxide accumulation by decreased uptake rather than by altered mitochondrial ROS production. These findings reinforce MOH1 as a stress and cell-envelope regulator without identifying its direct molecular activity.

Olgun et al. summarize prior AP-MS evidence that Moh1 co-purifies with CCT2, CCT3, and multiple core GID E3-ligase subunits, and suggest that Moh1 might connect CCT-mediated protein folding with GID-mediated degradation during stress adaptation.

Moh1 also has reported AP-MS association with CCT/TRiC, especially CCT2 and CCT3, although that association has not yet been functionally validated.

Lampert et al. identified human YPEL5 as a GID/CTLH subunit and directly tested yeast Moh1 in the canonical Fbp1 GID-substrate degradation assay, where moh1delta cells degraded Fbp1 with wild-type kinetics while gid4delta cells did not; this supports a human source-side complex role for YPEL5, but argues that Moh1 is dispensable for core catalytic yeast GID activity.

Moh1 is dispensable for yeast GID-dependent degradation of Fbp1 after a switch from non-fermentable carbon to glucose, so any Moh1-GID association is not required for the canonical Fbp1 proteolysis assay.

YBL049W (MOH1) was identified as one of nine putative N-myristoylproteins whose deletion reproduces the stationary-phase survival defect of nmt1 mutant cells, linking MOH1 phenotypically to maintenance of proliferative potential during stationary phase.

Defines the Yippee family as a highly conserved eukaryotic family bearing a putative zinc-finger-like metal-binding domain; even at the family's founding the molecular function was left open.

Genome-wide screen that identified MOH1 as one of the stationary-phase-essential genes: moh1 deletion causes a large loss of viability during long-term stationary phase at 37C, yet MOH1 is not required for growth on nonfermentable carbon sources, indicating a specific quiescence-survival role rather than a generic respiratory defect.

Synthesis concluding MOH1 is a small conserved Yippee-family regulatory/adaptor protein with a zinc-stabilized beta-tent fold and cradle-shaped binding pocket, required for stationary-phase survival, whose precise biochemical activity, substrate, and dedicated pathway remain unresolved in the retrievable literature.

Independently confirms the Yippee zinc signature (C45-x2-C48 ... C101-x2-C104, 52-residue spacer) matching the UniProt Zn-binding features, ~37-45% identity to human YPEL1-5 with all four Zn-cysteines perfectly conserved, and no sequence-level evidence for catalytic activity.