These computational predictions are reviewed separately from the GOA annotation set used for this review. The assessments below are from this project and do not constitute official GO annotations or endorsement by GO/UniProt. They are not included in the existing annotation review above.
ProtNLM2 External predictions
View prediction review YAML ยท PEA15-protnlm-predictions-review.yaml ยท Review status: COMPLETE
PEA15 has experimentally supported regulatory effects on glucose-transporter trafficking. Whether the exact carbohydrate-transport process annotation is justified for the selected horse protein remains uncertain.
Source documents: genes/HORSE/PEA15/PEA15-bioinformatics/RESULTS.md ยท genes/human/PEA15/PEA15-uniprot.txt ยท publications/PMID_9670003.md
Review score: 2 = concordant with evidence; 1 = uncertain; 0 = discordant with evidence. This is an assessment score, not a model probability.
Prediction method: ProtNLM2 ยท Version: UniProt API snapshot 2026-09-08
Review rationale: Human PEA15 changes GLUT1/GLUT4 surface recruitment and insulin-stimulated glucose transport, so this prediction must not be rejected merely because PEA15 lacks a transporter fold. The selected horse protein retains the complete human core at 100% identity with a 46-residue N-terminal extension. However, the inspected experimental evidence supports regulation of transport, whereas GO:0008643 denotes directed carbohydrate movement; regulation is not automatically the same biological-process assertion. The exact horse process has no target GOA overlap and neither direct horse transport evidence nor a demonstrated mechanistic participation beyond regulation is available. The prediction remains uncertain rather than being classified as a nonparalog error.
Supporting Evidence: - PMID:9670003: "Transfection of PED/PEA-15 in differentiating L6 skeletal muscle cells increases the content of Glut1 transporters on the plasma membrane and inhibits insulin-stimulated glucose transport and cell-surface recruitment of Glut4"
- file:HORSE/PEA15/PEA15-bioinformatics/RESULTS.md: "Global alignment of cached UniProt sequences gives **130/130 identical paired residues (100.0%)**."