Human WEE1 is a nuclear CDK-inhibitory tyrosine kinase. Direct assays distinguish CDK1 Tyr15 phosphorylation from Thr14 phosphorylation. Mouse egg-activation experiments distinguish WEE2/Wee1B from WEE1/Wee1A: WEE2 depletion blocks pronuclear formation, whereas WEE1 depletion does not in that assay.
The full646-residue horse protein closely matches human WEE1 at95.4% identity. Nuclear phosphorylation is supported. The specific female-pronucleus prediction has a plausible paralog-transfer explanation, but remains UNC: differential necessity does not exclude redundant participation. Broad meiotic claims likewise remain unresolved. Electronic Ser/Thr assignments are refined to the demonstrated tyrosine activity.
The reproducible alignment, source paths and hashes are in the paired comparison. Current UniProt sequences have not been proven identical to the original ProtNLM input sequences. Sequence anomalies are therefore recorded as model/transfer limitations, not as proven wrong-input pipeline errors.
The2023Wee2 knockouts retain substantial fertility and support possible biological redundancy, so do not claim WEE2 is universally essential or WEE1 can never compensate. Check horse oocyte expression/perturbation before scoring broad meiosis. Separate kinase catalysis from regulation of a different phosphorylation reaction.
Every seeded annotation receives a current assessment. UNDECIDED marks unresolved source-specific or biological evidence; these are initial reviews rather than a claim that every original experimental assay has been independently reproduced or verified. The human Edison report is retained as a research synthesis and source-finding aid; decisive YAML excerpts cite primary publications, source records or reproducible analysis. The validator advisory to cite the deep-research file is deliberately not satisfied by citing AI prose as biological proof.