id: O13769
gene_symbol: ulp2
taxon:
  id: NCBITaxon:284812
  label: Schizosaccharomyces pombe (strain 972 / ATCC 24843)
status: COMPLETE
description: Both broad peptidase predictions are supported but lose the experimentally established SUMO-deconjugating
  specificity.
source_documents:
- genes/SCHPO/ulp2/ulp2-protnlm-source.xml
- genes/SCHPO/ulp2/ulp2-uniprot-source.json
- genes/SCHPO/ulp2/ulp2-uniprot.txt
predictions:
- source_method: ProtNLM2
  source_version: pre-release post-processed-2026_02_28k.xml
  source_reference_id: file:SCHPO/ulp2/ulp2-protnlm-source.xml
  predicted_term:
    id: GO:0019783
    label: ubiquitin-like protein peptidase activity
  predicted_term_type: GO_MF
  review:
    assessment: LSP
    confidence_score: 2
    summary: Purified fission-yeast Ulp2 directly deconjugates SUMO from high-molecular-weight species,
      and the study identifies it as a cysteine protease. SUMO is a ubiquitin-like modifier, so the broad
      ubiquitin-like protein peptidase term is biologically correct. The more specific deSUMOylase activity
      GO:0016929 is experimentally established and already annotated; the XML records hydration from that
      term. This prediction loses substrate specificity and is therefore LSP. It does not imply a demonstrated
      ability to remove ubiquitin itself.
    supported_by:
    - &id001
      reference_id: PMID:24818994
      supporting_text: These results confirm that like S. cerevisiae Ulp2, S. pombe Ulp2 is a cysteine
        protease whose main function is in deconjugating SUMO from target proteins.
- source_method: ProtNLM2
  source_version: pre-release post-processed-2026_02_28k.xml
  source_reference_id: file:SCHPO/ulp2/ulp2-protnlm-source.xml
  predicted_term:
    id: GO:0008234
    label: cysteine-type peptidase activity
  predicted_term_type: GO_MF
  review:
    assessment: LSP
    confidence_score: 2
    summary: Direct biochemical experiments establish Ulp2 as a SUMO-deconjugating cysteine protease,
      including sensitivity to N-ethylmaleimide. The conserved C48 catalytic domain is consistent with
      that mechanism. Cysteine-type peptidase activity is true but less precise than the already annotated
      deSUMOylase activity and its SUMO substrate specificity.
    supported_by:
    - *id001
references:
- id: PMID:24818994
  title: The S. pombe translation initiation factor eIF4G is Sumoylated and associates with the SUMO protease
    Ulp2.
  findings: []
  full_text_unavailable: false