The normal imported source record identifies human BRPF1, UniProt P55201 and HGNC:14255. The review preserves all 36 machine-sourced annotation objects, all 14 reference identifiers/titles, and all four alternative products (P55201-1 through P55201-4). Product sequence notes remain unchanged; none of the experiments reviewed here establishes a distinct function for each named isoform. The import receipt is tmp/BRPF1-hosted-fetch/import-receipt.json. This is a scientific candidate awaiting independent review and authorized application; canonical source files and authored seed are unchanged.
The annotation outcome is 26 ACCEPT, 4 KEEP_AS_NON_CORE, 4 UNDECIDED and 2 MODIFY. There are no REMOVE or NEW rows. The unresolved rows are the three H4-site contributes_to annotations (zero-based indices 24–26) and the original hemopoiesis NAS annotation (35). Completion of annotation review does not resolve these biological and access uncertainties. The normal schema status command computes COMPLETE because all decisions are made and normal validation has no curation warnings.
BRPF1 supplies a chromatin-reader and scaffold/activator role in alternative KAT6A/MOZ, KAT6B/MORF and KAT7/HBO1 assemblies. KAT6A and KAT6B are related alternative catalytic partners; the complex name does not require both enzymes in every particle. BRPF1 bridges the KAT proteins to ING and MEAF6 factors, increases activity on nucleosomal substrates, and helps select substrate context. Acetyl transfer is performed by the KAT subunits. The activator core uses the already sourced GO:0010698 rather than attributing an intrinsic HAT reaction to BRPF1. PMID:18794358(https://pubmed.ncbi.nlm.nih.gov/18794358/), PMID:24065767(https://pmc.ncbi.nlm.nih.gov/articles/PMC3792477/), PMID:27939640(https://pubmed.ncbi.nlm.nih.gov/27939640/).
A second, coupled core captures histone-reader activity. Purified human BRPF1 bromodomain structures and mutagenesis establish recognition of acetylated H2A and H4 peptides. PZP experiments independently show H3 recognition with an unmethylated Lys4 and chromatin engagement by the assembled complex. ING5 is the source of H3K4me3-directed targeting in that complex; this is not intrinsic H3K4me3 recognition by the BRPF1 PZP domain. Two binding rows are refined to GO:0140054 histone H2A reader activity and GO:0140008 histone H4 reader activity; their exact GOA partner IDs are preserved. The peptide structures do not distinguish among genes encoding identical histone sequences. The broad core GO:0140566 covers the complementary recognition modules without multiplying overlapping core entries. PMID:25281266(https://pmc.ncbi.nlm.nih.gov/articles/PMC4252766/), PMID:24065767(https://pmc.ncbi.nlm.nih.gov/articles/PMC3792477/).
The three H4 catalytic labels already carry contributes_to. Their weaker assertion must not be mistaken for independent BRPF1 catalysis. The 2006 original assay remains unavailable beyond the abstract. Later actual Results distinguish BRPF1-complex acetylation of free H3/H4 from preferential H3 acetylation in chromatin, whereas HBO1-JADE complexes target chromatin H4K5/8/12. That distinction justifies uncertainty about the precise original sites, not categorical removal of all possible free-histone contribution. PMID:16387653(https://pubmed.ncbi.nlm.nih.gov/16387653/), PMID:24065767(https://pmc.ncbi.nlm.nih.gov/articles/PMC3792477/).
Nuclear function and chromatin association are directly supported. The 2008 primary indexed Results also show cytoplasmic tagged BRPF1 when expressed alone, with nuclear relocalization on partner coexpression. This is a conditional non-core compartment; it does not establish a separate cytoplasmic biochemical function or quantify endogenous distribution. Runx-responsive reporter coactivation with MOZ is likewise context dependent: Gal4-BRPF1 alone lacked activation potential. The publisher erratum swaps H2A/H2B labels in Fig.5D/E/G and BR2/BR14 labels in Fig.6E; no claim here depends on those uncorrected labels. PMID:18794358(https://pmc.ncbi.nlm.nih.gov/articles/PMC2573306/), publisher erratum.
The ZMYND8-centered paper explicitly reports focal nuclear BRPF1 in its broad bromodomain screen. Its title is not a reason to reject the BRPF1 localization row. The fuller actual Results do not place BRPF1 in the ZMYND8 damage-recruitment class; no ZMYND8 repair mechanism is assigned to BRPF1. The 2013 genomic mapping antibody recognizes both BRPF1 and BRPF2, so the ChIP map is not presented as BRPF1-exclusive. PMID:25593309(https://pmc.ncbi.nlm.nih.gov/articles/PMC4298138/), PMID:24065767(https://pmc.ncbi.nlm.nih.gov/articles/PMC3792477/).
The broad existing developmental annotation is retained as non-core context, supported by the human variant study and disruption of the chromatin machinery. This is not a new instructive-patterning claim. The original hemopoiesis annotation remains UNDECIDED because neither the source-specific BRPF1 mechanism nor the later mouse primary assays were examined sufficiently to settle it. KAT6A phenotypes are not automatically transferred to BRPF1. PMID:27939640(https://pubmed.ncbi.nlm.nih.gov/27939640/).
All six original PMID abstracts were read completely. Canonical PMID:16387653, PMID:18794358, PMID:25281266, PMID:25593309 and PMID:27939640 are abstract-only; only PMID:24065767 has an extensive canonical XML-derived body. A full-text flag never substitutes for reading actual sections.
tmp/BRPF1-artifact-transport/extracted/raw/publications/PMID_25281266.md supplied Methods paragraphs 23/24/27/36 and Results/Discussion 44/47/50–54/69. Purified human bromodomain, peptide structures and binding-pocket experiments were actually read. The canonical abstract was preserved and supplies any YAML quotations.tmp/BRPF1-root-primary-consultation/.The ordinary Falcon research workflow with the documented installed-client override and perplexity-lite fallback was attempted once in an isolated TMP working directory using exact copies of the normal template and UniProt record. Both providers failed, with DNS failure observed; no provider report was produced. provider-attempt-assessment.json stores a filtered outcome. Credential-bearing rich tracebacks were neither displayed nor saved. These notes are manual synthesis and are not labeled as provider-generated research.
GO definitions and parents were checked in the local read-only OAK ontology and selected official AmiGO pages. Chromatin remodeling (GO:0006338) includes chromatin structural reorganization and histone-modifying activity; retaining it does not assert ATP-dependent remodeling by BRPF1. Histone-reader activity is chromatin-adaptor activity, not merely undifferentiated binding. The finer H2A/H4 terms are existing-row replacements supported by original structural evidence. Official chromatin-remodeling definition, official histone-reader definition.
No NEW annotation is proposed. The existing activator, reader, complex and transcription/chromatin rows already cover the main molecular roles; more process rows would add overlapping ancestry or phenotype claims. The local GO-CAM index has no P55201 match; that is a local-cache observation, not proof of global absence. No comparator search is claimed as completed because no new annotation is being advanced. The two generic-binding refinements preserve their original assertions and evidence sources rather than claiming a newly discovered curation gap.
The candidate has nine supporting-text instances, five distinct short quotations, all exact substrings of preserved canonical publications. Counting repeated snippets again, word totals are 19 (PMID:18794358), 16 (PMID:27939640), 15 (PMID:25281266) and 7 (PMID:24065767). Most support entries are reference-only; quotations anchor both cores and selected original decisions. No quote is copied from an alternate-only body. The adjacent quote ledger records every location.
Normal validation includes schema, best practices, references, supporting text, GOA and --terms; no checks were disabled. The first complete run passed with no curation warnings. The normal status command computed COMPLETE on the explicit TMP candidate path. This CLI preserves an existing status and reports a mismatch rather than overwriting it, so only the status line was aligned to its computed value; the repeated status check and final validation verify the result. Adjacent command/result records contain the actual outcomes. The generic-binding removal preference causes no warning here because both binding rows have justified finer replacements; the standing campaign policy would otherwise retain supported binding as non-core.
Independent scaffold consultation: tmp/BRPF1-scaffold-consultation/consultation.json, authored by /root/bicra_science, assessed the ten complex/activator/H4-contribution rows. Its seven ACCEPT and three UNDECIDED recommendations were integrated, with source-specific complex reasons refined after ROOT's additional primary access. Final whole-candidate scientific review and canonical application remain with ROOT; this file does not claim publication or ownership clearance.
The independently reviewed candidate was applied after checking the exact seeded preimage. Normal canonical validation passed with no errors or curation warnings, and the standard codex/gpt-6 CREATE history was scaffolded and validated. COMPLETE records that all36 assertions were assessed; the three H4-site contributions and hemopoiesis assertion remain explicitly UNDECIDED. All14 reference identities, four products, raw source records, normal publication caches and richer supplemental variants were preserved. Earlier candidate-stage statements above record the prior stage and are superseded by this application entry.
The H2A reader identifier was checked independently against the official ontology views: GO:0140054 is correctly named histone H2A reader activity. The identifier was not inferred from its numerical neighbors. Its more specific child GO:0140130 names histone H2AK5ac reader activity. The corresponding H4 child GO:0140011 names histone H4K12ac reader activity. These definitions and parent relations also agree with the existing local GO snapshot. Direct AmiGO openings for some terms timed out or were rate-limited; the successful indexed official AmiGO/FlyBase views are the stated current external evidence.
The two original protein-binding rows retain MODIFY and their exact H2A/H4 partner accessions, but their replacement terms now capture the specific H2AK5ac and H4K12ac ligands. The canonical PMID:25281266 abstract itself states both crystal structures and binding-pocket mutagenesis. Selected Methods and Results in the authenticated fuller source confirm human BRPF1 residues 629–742, modified peptides and ITC experiments. This refinement does not imply that the bromodomain recognizes only these marks or that isolated-peptide structures establish full-length genome-wide recruitment. The broad reader core remains one coherent unit covering the interacting reader modules; no duplicate parent/child core is added.
The current GO:0006338 definition begins: “A dynamic process of chromatin reorganization resulting in changes to chromatin structure.” The decisive additional ontology assertion is GO:0140993 histone modifying activity part_of GO:0006338. This is a molecular-function-to-biological-process relation, not an is_a claim between two process terms. The older GO:0016570 histone modification is explicitly obsolete because it represents a molecular function. Thus a historical sibling comparison does not justify excluding histone-modifying mechanisms from the current remodeling process.
BRPF1's participation is supported by its own contribution to complex assembly, activation and chromatin engagement. In the inspected PMID:24065767 Results, PZP-domain deletions disrupt histone association and chromatin acetylation while leaving free-histone acetylation intact. The same study distinguishes H3 targeting by BRPF1 complexes from H4 targeting by JADE complexes. The PMID:27939640 abstract independently reports deficient H3K23 acetylation in the pathogenic-variant context. The retained GO:0006338 annotations and core process links therefore refer to a scaffold/reader contribution to histone modification; KAT6A, KAT6B or KAT7 performs acetyl transfer. Neither an intrinsic BRPF1 ATPase nor a direct nucleosome-sliding experiment is claimed. Both core descriptions now state this mechanistic boundary explicitly.
The PZP evidence for recognition of H3 with unmethylated Lys4 remains explicit in the accepted broad histone-reader row and core. It must not be conflated with recognition requiring H3K14 acetylation. A focused question now makes the annotation granularity visible; no extra NEW child assertion is added under the existing broad reader assertion. The four previous uncertainties, including the original H4-site contributes_to claims, remain unchanged. The 2008 source correction and prior access limits remain recorded. All 36 machine source objects, 14 reference records, four products and nine publication-quote instances are preserved, as are historical notes and history records. This entry supersedes the older broader replacement-term wording without rewriting that historical account.
The independently reviewed follow-up was applied after exact preimage checks. Full normal candidate and canonical validation passed with no errors or curation warnings; COMPLETE and the four unresolved annotations remain unchanged. The standard codex/gpt-6 EDIT history was scaffolded and validated. All source objects, reference records, four products, publication quotations, raw sources, caches and prior history records were preserved. The two specific reader replacements and the explicit scaffold/reader rationale for chromatin remodeling are now the current reviewed state; earlier broader wording remains in the historical entries above.