The DCAF11/WDR-23 identity and qualified substrate-receptor prediction are supported by direct worm studies and preservation of the common WD-repeat region. The nucleus prediction requires isoform-specific evidence; the two ribosome-related GO predictions derive from RACK1 rather than WDR-23 evidence.
S6FN32/D2030.9d is exactly residues 74–571 of the longer P90794 WDR-23A sequence and residues 33–530 of P90794-2/WDR-23B. It therefore is not identical to either tested isoform. Every annotated WD repeat is retained. The missing isoform-specific N termini matter because primary experiments establish different nuclear and cytoplasmic behavior. The GO donor P69103 is trypanosome small ribosomal subunit protein RACK1, a different WD-repeat protein.
WDR-23, which interacts with the
CUL-4/DDB-1 ubiquitin ligase
These opposing roles are mediated by two distinct isoforms: WDR-23A
in the cytoplasm and WDR-23B in the nucleus.we identify
GEN-1, a Holliday junction resolvase, as an evolutionarily conserved WDR-23
substratethe N-terminal domain of WDR-23B that mediates nuclear localization does not interfere with binding of GEN-1 in vitro.
The complete emitted record is preserved in wdr-23-protnlm-source.json. Assessments below address the selected protein product; evidence on longer products is identified explicitly.
DDB1- and CUL4-associated factor 11
CNN (CS 2). DDB1- and CUL4-associated factor 11 correctly identifies the WDR-23 lineage, independently supported by direct C. elegans interaction and substrate-regulation experiments. It does not specify the untested isoform localization.
May function as a substrate receptor for CUL4-DDB1 E3 ubiquitin-protein ligase complex
CNN (CS 2). The qualified “may function as a substrate receptor” wording is consistent with preservation of the complete common WD-repeat region and direct worm evidence for WDR-23–CUL-4/DDB-1 association. The prediction does not establish that the short product has all regulatory effects measured for WDR-23A or WDR-23B. PMID:19273594(https://pubmed.ncbi.nlm.nih.gov/19273594/); PMID:31409866(https://pubmed.ncbi.nlm.nih.gov/31409866/).
Nucleus
UNC (CS 1). Both nuclear and cytoplasmic WDR-23 isoforms are experimentally documented. S6FN32 starts downstream of the distinctive N termini of both tested products, so it cannot simply inherit the WDR-23B localization. The missing N terminus does not by itself prove exclusion from the nucleus. Isoform comparison; primary localization study.
All 2 emitted GO claims are individually assessed in wdr-23-protnlm-predictions-review.yaml.
PTHR19847/SF7 identifies the DCAF11/WDR23 substrate-receptor lineage. A WD-repeat fold alone is insufficient to transfer the ribosome-associated functions of RACK1. Substrate identity and compartmental effects require finer resolution than family membership; nuclear inhibition and cytoplasmic activation of substrates are both compatible with a common adaptor architecture.
The 2019 report is available in full text; the 2009 cache is abstract-only. Neither directly assays D2030.9d/S6FN32. The genuine Falcon report provides useful primary leads, but its gene-level nuclear and SKN-1 conclusions require the exact isoform boundary documented here. No NEW experimental annotation is assigned to an untested protein product. No direct assay was found either establishing or refuting ribosome association.
Exact sequence mapping: wdr-23-bioinformatics/RESULTS.md. Global alignments can place nonhomologous alternative tails opposite gaps or distant residues; only conserved segments and explicitly retained feature intervals support functional transfer.