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BMH2

S. cerevisiae

14-3-3 family protein BMH2

What the model saw

Gene: BMH2
Organism: Saccharomyces cerevisiae
Known functions: 14-3-3 family protein BMH2. DNA replication origin binding. phosphoserine residue binding. protein binding.
View unredacted entry
14-3-3 family protein BMH2. DNA replication origin binding. phosphoserine residue binding. protein binding.

Solver output

Predicted influence
Pro-longevity
Confidence
65%
Mechanism
Deregulated nutrient sensing
Reasoning

BMH2 encodes a yeast 14-3-3 family protein, which are conserved phosphoserine/phosphothreonine-binding scaffold proteins that regulate multiple signaling pathways. In yeast, 14-3-3 proteins (Bmh1/Bmh2) are key regulators of the TORC1 and Ras/PKA nutrient-sensing pathways by binding phosphorylated client proteins and modulating their activity or localization. Specifically, Bmh2 interacts with phosphorylated forms of regulators such as Sch9 and components of the Ras/cAMP/PKA axis, helping to restrain pro-aging nutrient-sensing signals. Loss of BMH2 function has been associated with shortened chronological lifespan in yeast, consistent with a pro-longevity role. Additionally, its DNA replication origin binding activity may contribute to genomic stability, further supporting survival. The 14-3-3 family is broadly conserved as a longevity-associated protein class across eukaryotes.

Key pathways
TORC1/nutrient-sensing signalingRas/cAMP/PKA pathwayDNA replication origin regulation
Longevity influence
Pro-longevity
Lifespan effect
Increase

GenAge curators classify each gene's normal function as promoting (Pro-Longevity) or opposing (Anti-Longevity) longevity, based on synthesis across studies. Loss-of-function effects can vary from this depending on the manipulation.

Advisor judgment

Answer
Correct
Mechanism
Correct
Reasoning quality
4/5
Failure mode
Correct
Notes

The model correctly predicted pro_longevity for BMH2. The mechanistic reasoning is solid - 14-3-3 proteins in yeast are indeed involved in nutrient-sensing pathways (TORC1, Ras/PKA), and BMH2 loss has been associated with shortened lifespan. The model correctly identifies the phosphoserine-binding scaffold role and its connection to longevity regulation. The confidence of 0.65 is reasonable given the complexity. The mechanism class of "deregulated_nutrient_sensing" is plausible though the actual mechanism may be more nuanced. Overall a well-reasoned correct prediction.

Raw API responses

solver

{
  "reasoning": "BMH2 encodes a yeast 14-3-3 family protein, which are conserved phosphoserine/phosphothreonine-binding scaffold proteins that regulate multiple signaling pathways. In yeast, 14-3-3 proteins (Bmh1/Bmh2) are key regulators of the TORC1 and Ras/PKA nutrient-sensing pathways by binding phosphorylated client proteins and modulating their activity or localization. Specifically, Bmh2 interacts with phosphorylated forms of regulators such as Sch9 and components of the Ras/cAMP/PKA axis, helping to restrain pro-aging nutrient-sensing signals. Loss of BMH2 function has been associated with shortened chronological lifespan in yeast, consistent with a pro-longevity role. Additionally, its DNA replication origin binding activity may contribute to genomic stability, further supporting survival. The 14-3-3 family is broadly conserved as a longevity-associated protein class across eukaryotes.",
  "confidence": 0.65,
  "key_pathways": [
    "TORC1/nutrient-sensing signaling",
    "Ras/cAMP/PKA pathway",
    "DNA replication origin regulation"
  ],
  "mechanism_class": "deregulated_nutrient_sensing",
  "longevity_influence": "pro_longevity"
}

advisor

{
  "notes": "The model correctly predicted pro_longevity for BMH2. The mechanistic reasoning is solid - 14-3-3 proteins in yeast are indeed involved in nutrient-sensing pathways (TORC1, Ras/PKA), and BMH2 loss has been associated with shortened lifespan. The model correctly identifies the phosphoserine-binding scaffold role and its connection to longevity regulation. The confidence of 0.65 is reasonable given the complexity. The mechanism class of \"deregulated_nutrient_sensing\" is plausible though the actual mechanism may be more nuanced. Overall a well-reasoned correct prediction.",
  "failure_mode": "correct",
  "answer_correct": true,
  "mechanism_correct": true,
  "reasoning_quality": 4,
  "ground_truth_questionable": false
}