SHQ1 has four IBA annotations, all propagated through PANTHER:PTN000311574 in
the PTHR12967 SHQ1 homolog family. The current cached PAINT export for
PTHR12967 still places GO:0005654 nucleoplasm, GO:0005737 cytoplasm, and
GO:0000493 box H/ACA snoRNP assembly on PTN000311574; yeast SHQ1
(P40486), human SHQ1 (Q6PI26), and the other representative eukaryotic SHQ1
proteins in the local entries table all sit in the single PTHR12967:SF0
subfamily. I added explicit propagation_review blocks treating the nucleoplasm
and box H/ACA snoRNP assembly IBAs as core transfers and the cytoplasm IBA as a
defensible but secondary localization transfer.
The fourth IBA, GO:0051082 unfolded protein binding, is still present in the
local GOA file as a 2017 row from PTN000311574, but the current
PTHR12967-paint.tsv cache no longer lists the molecular-function assertion.
The existing MODIFY call remains right biologically: the source biology is
Cbf5/dyskerin carrier-chaperone activity, not a generic unfolded-protein-binding
claim. I added TERM_SCOPING_PROBLEM / GRANULARITY_MISMATCH propagation
metadata and marked the ancestral node source as SOURCE_STALE_OR_MISSING
because the exact MF assertion cannot be recovered from the current cached PAINT
table.
The cached experimental papers support the existing action set. Yang et al.
identified Yil104c/Shq1p as essential for stable box H/ACA snoRNP accumulation
and pre-rRNA processing, and reported that Shq1p is nuclear and interacts with
Cbf5p and Nhp2p PMID:12228251. Godin et al. showed that Shq1p binds the
pseudouridylating enzyme Cbf5p and has stand-alone in vitro chaperone activity,
supporting the MODIFY of unfolded protein binding to GO:0140597 protein
carrier chaperone PMID:19426738. The oxygen-regulation localization paper
lists YIL104C/SHQ1 among nuclear proteins that relocalize to the cytosol during
hypoxia and return to the nucleus after reoxygenation, so the cytosol/cytoplasm
rows should be retained as non-core/contextual rather than removed
PMID:22932476.
I searched for 2023-2026 SHQ1/yeast literature. Most newer SHQ1 papers are human
neurodevelopmental-disease or cancer reports that do not change the yeast GO
review. The relevant newer experimental paper is Alidou-D'Anjou et al. 2023,
which expressed human SHQ1 R335C and A426V variants in a conditional yeast
SHQ1-depletion strain and showed weakened Cbf5 interaction, loss of H/ACA
snoRNAs, pre-rRNA processing defects, and reduced ribosome production
PMID:37818102. This reinforces the conserved SHQ1-Cbf5 carrier-chaperone
model but does not require a new GO term for the yeast protein.