id: A0A9L0T4W6
gene_symbol: PTPRN2
taxon:
  id: NCBITaxon:9796
  label: Equus caballus
status: COMPLETE
description: 'Protein dephosphorylation remains uncertain: loss of intrinsic phosphoprotein catalysis
  does not exclude a regulatory contribution to that process.'
source_documents:
- projects/PROTNLM_EVALUATION/mammal-benchmark/horse40-predictions.csv
- projects/PROTNLM_EVALUATION/mammal-benchmark/predictions.jsonl.gz
- projects/PROTNLM_EVALUATION/mammal-benchmark/paired-sequences/PTPRN2.json
references:
- id: PMID:26620550
  title: PTPRN2 and PLCβ1 promote metastatic breast cancer cell migration through PI(4,5)P2-dependent
    actin remodeling.
  full_text_unavailable: false
  findings: []
- id: file:HORSE/PTPRN2/PTPRN2-bioinformatics/RESULTS.md
  title: HORSE/PTPRN2/PTPRN2-bioinformatics/RESULTS.md
  findings: []
predictions:
- source_method: ProtNLM2
  source_version: UniProt API snapshot 2026-09-08
  predicted_term:
    id: GO:0006470
    label: protein dephosphorylation
  predicted_term_type: GO_BP
  review:
    assessment: UNC
    confidence_score: 1
    summary: Human PTPRN2 lacks conventional phosphoprotein-substrate activity, while lipid phosphatase
      activity and possible regulation of active protein phosphatases are distinct mechanisms. The predicted
      biological process does not require PTPRN2 itself to catalyze protein dephosphorylation. Evidence
      for that specific regulatory participation in horse is missing, and the selected horse phosphatase-like
      domain has a divergent C terminus. Thus catalytic inactivity alone does not justify an incorrect-process
      verdict.
    supported_by:
    - reference_id: PMID:26620550
      supporting_text: PTPRN2 belongs to the protein tyrosine phosphatase family, but does not exhibit
        activity against phosphoprotein substrates due to several critical amino acid variations in the
        PTP domain (Magistrelli et al, 1996).
    - reference_id: file:HORSE/PTPRN2/PTPRN2-bioinformatics/RESULTS.md
      supporting_text: The selected horse sequence has a divergent C-terminal region, including deletion
        of human residues 989–1003 within the annotated phosphatase domain. The N-terminal signal sequence
        and transmembrane segment are retained. Substrate-specific enzymatic activity requires more than
        the global homology assignment.