id: S6FN32
gene_symbol: wdr-23
taxon:
  id: NCBITaxon:6239
  label: Caenorhabditis elegans
status: COMPLETE
description: The emitted ribosome-binding and translation-regulator terms are not validated by the direct
  WDR-23 substrate-receptor experiments. The exact product retains its WD-repeat core but has a distinct
  N-terminal boundary.
source_documents:
- genes/worm/wdr-23/wdr-23-protnlm-source.json
- genes/worm/wdr-23/wdr-23-notes.md
references:
- id: PMID:19273594
  title: The WD40 repeat protein WDR-23 functions with the CUL4/DDB1 ubiquitin ligase to regulate nuclear
    abundance and activity of SKN-1 in Caenorhabditis elegans.
  findings:
  - statement: The primary worm study establishes association of WDR-23 with CUL-4/DDB-1 and regulation
      of SKN-1 abundance and activity.
    supporting_text: "WDR-23, which interacts with the \nCUL-4/DDB-1 ubiquitin ligase"
  full_text_unavailable: true
  reference_review:
    relevance: HIGH
    correctness: VERIFIED
    review_notes: Primary report checked against the cached abstract/full text; the evidence scope is
      stated in the finding.
- id: PMID:31409866
  title: Nuclear and cytoplasmic WDR-23 isoforms mediate differential effects on GEN-1 and SKN-1 substrates.
  findings:
  - statement: Primary worm isoform experiments show that compartment and regulatory outcome cannot be
      assigned independently of the N terminus.
    supporting_text: 'These opposing roles are mediated by two distinct isoforms: WDR-23A

      in the cytoplasm and WDR-23B in the nucleus.'
  - statement: The primary study identifies GEN-1 as a WDR-23 substrate; its DNA repair role does not
      make WDR-23 a nuclease.
    supporting_text: 'we identify

      GEN-1, a Holliday junction resolvase, as an evolutionarily conserved WDR-23

      substrate'
  - statement: The tested alternative N termini permit GEN-1 interaction, supporting a shared substrate-binding
      mechanism without establishing localization of the shorter target.
    supporting_text: the N-terminal domain of WDR-23B that mediates nuclear localization does not interfere
      with binding of GEN-1 in vitro.
  full_text_unavailable: false
  reference_review:
    relevance: HIGH
    correctness: VERIFIED
    review_notes: Primary report checked against the cached abstract/full text; the evidence scope is
      stated in the finding.
- id: file:worm/wdr-23/wdr-23-bioinformatics/RESULTS.md
  title: WDR-23 exact-product sequence and repeat conservation
- id: file:worm/wdr-23/wdr-23-bioinformatics/isoform-b-comparison.json
  title: Reproducible comparison against the independently retrieved WDR-23B sequence
- id: file:worm/wdr-23/wdr-23-prediction-donor.json
  title: UniProt identification of the ribosome-related prediction donor
- id: file:worm/wdr-23/wdr-23-protnlm-source.json
  title: Frozen exact-input ProtNLM output and UniProt sequence for S6FN32
predictions:
- source_method: ProtNLM2
  source_version: UniProt API snapshot 2026-09-10
  source_reference_id: file:worm/wdr-23/wdr-23-protnlm-source.json
  predicted_term:
    id: GO:0045182
    label: translation regulator activity
  predicted_term_type: GO_MF
  review:
    assessment: UNC
    confidence_score: 1
    summary: The donor is RACK1, whereas direct worm studies establish WDR-23 substrate recruitment and
      SKN-1/GEN-1 regulation. WD-repeat architecture alone cannot transfer direct translational regulation.
      Effects of related WDR23 proteins on other regulatory substrates do not demonstrate this GO activity
      in S6FN32; an additional role is not experimentally excluded.
    supported_by:
    - &id001
      reference_id: file:worm/wdr-23/wdr-23-prediction-donor.json
      supporting_text: '"value": "Small ribosomal subunit protein RACK1"'
    - &id002
      reference_id: PMID:19273594
      supporting_text: "WDR-23, which interacts with the \nCUL-4/DDB-1 ubiquitin ligase"
    - reference_id: PMID:31409866
      supporting_text: 'we identify

        GEN-1, a Holliday junction resolvase, as an evolutionarily conserved WDR-23

        substrate'
    - &id003
      reference_id: file:worm/wdr-23/wdr-23-bioinformatics/RESULTS.md
      supporting_text: '| 74–571 | 1–498 | 498 |'
- source_method: ProtNLM2
  source_version: UniProt API snapshot 2026-09-10
  source_reference_id: file:worm/wdr-23/wdr-23-protnlm-source.json
  predicted_term:
    id: GO:0043022
    label: ribosome binding
  predicted_term_type: GO_MF
  review:
    assessment: UNC
    confidence_score: 1
    summary: The weak sequence match to ribosomal RACK1 does not establish a ribosome-binding interface
      or ribosome association in this DCAF11/WDR-23 product. Direct WDR-23 studies support a different
      molecular system, but do not provide a negative ribosome-binding assay.
    supported_by:
    - *id001
    - *id002
    - *id003