max-2
C. elegans
Serine/threonine-protein kinase max-2;non-specific serine/threonine protein kinase
What the model saw
Gene: max-2 Organism: Caenorhabditis elegans Known functions: Serine/threonine-protein kinase max-2;non-specific serine/threonine protein kinase. ATP binding. mitogen-activated protein kinase kinase kinase binding. protein kinase activity. protein serine kinase activity. protein serine/threonine kinase activity. small GTPase binding.
View unredacted entry
Serine/threonine-protein kinase max-2;non-specific serine/threonine protein kinase. ATP binding. mitogen-activated protein kinase kinase kinase binding. protein kinase activity. protein serine kinase activity. protein serine/threonine kinase activity. small GTPase binding.
Solver output
max-2 encodes a serine/threonine protein kinase in C. elegans that binds small GTPases and MAP kinase kinase kinases (MAP3Ks), placing it in a Ras/MAPK signaling cascade. In C. elegans, max-2 is a PAK (p21-activated kinase) family member that acts downstream of small GTPases (e.g., Rac/Cdc42) and upstream of MAPK modules. MAPK/PAK signaling can intersect with both stress-response pathways (which tend to be pro-longevity) and growth/proliferation pathways (which tend to be anti-longevity). The dual role of max-2 in axon guidance and immune/stress signaling makes it difficult to assign a clear net longevity direction without direct lifespan data. Its MAP3K-binding and small GTPase-binding activities suggest involvement in stress-activated MAPK cascades (e.g., p38/PMK-1), which are generally pro-longevity, but its kinase activity could also promote growth signaling that opposes longevity, leaving the net effect genuinely ambiguous.
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
The model predicted "unclear" while the ground truth is "anti_longevity." The model correctly identified max-2 as a PAK-family serine/threonine kinase involved in small GTPase and MAPK signaling, but failed to commit to the anti-longevity direction. The model's reasoning about stress-activated MAPK pathways being pro-longevity led it to hedge rather than recognize that max-2 loss-of-function likely extends lifespan (making it anti-longevity). The mechanistic reasoning was partially correct in identifying the relevant pathways but drew the wrong directional inference, ultimately landing on "unclear" rather than anti_longevity. The confidence was appropriately low (0.38), reflecting genuine uncertainty, but the answer is still wrong.
Raw API responses
solver
{
"reasoning": "max-2 encodes a serine/threonine protein kinase in C. elegans that binds small GTPases and MAP kinase kinase kinases (MAP3Ks), placing it in a Ras/MAPK signaling cascade. In C. elegans, max-2 is a PAK (p21-activated kinase) family member that acts downstream of small GTPases (e.g., Rac/Cdc42) and upstream of MAPK modules. MAPK/PAK signaling can intersect with both stress-response pathways (which tend to be pro-longevity) and growth/proliferation pathways (which tend to be anti-longevity). The dual role of max-2 in axon guidance and immune/stress signaling makes it difficult to assign a clear net longevity direction without direct lifespan data. Its MAP3K-binding and small GTPase-binding activities suggest involvement in stress-activated MAPK cascades (e.g., p38/PMK-1), which are generally pro-longevity, but its kinase activity could also promote growth signaling that opposes longevity, leaving the net effect genuinely ambiguous.",
"confidence": 0.38,
"key_pathways": [
"Ras/small GTPase-PAK signaling",
"MAP kinase kinase kinase (MAP3K) cascade",
"stress-activated MAPK (p38) pathway"
],
"mechanism_class": "deregulated_nutrient_sensing",
"longevity_influence": "unclear"
}advisor
{
"notes": "The model predicted \"unclear\" while the ground truth is \"anti_longevity.\" The model correctly identified max-2 as a PAK-family serine/threonine kinase involved in small GTPase and MAPK signaling, but failed to commit to the anti-longevity direction. The model's reasoning about stress-activated MAPK pathways being pro-longevity led it to hedge rather than recognize that max-2 loss-of-function likely extends lifespan (making it anti-longevity). The mechanistic reasoning was partially correct in identifying the relevant pathways but drew the wrong directional inference, ultimately landing on \"unclear\" rather than anti_longevity. The confidence was appropriately low (0.38), reflecting genuine uncertainty, but the answer is still wrong.",
"failure_mode": "appropriately_uncertain",
"answer_correct": false,
"mechanism_correct": false,
"reasoning_quality": 2,
"ground_truth_questionable": false
}