ARID1B is HGNC:18040, UniProt Q8NFD5. The imported Seed11 review contains 51 original assertions and four alternative-product records. All 22 cited PMID records and five Reactome records are present. Raw UniProt, GOA and normal publication/event caches are immutable. The configured Falcon research attempt with Perplexity fallback exited unsuccessfully after 3.9 seconds and produced no provider report; its original receipt is tmp/ARID1B-initial/deep-research-attempt.json. No repeated source or research fetch was performed.
Historical names require accession-level care. The current UniProt record maps p250R, hELD/OSA1, hOsa2 and BAF250B to ARID1B. Inoue's hOsa1 is ARID1A, whereas Wang's hELD/OSA1 is ARID1B: the shared name alone cannot resolve a paper. The actual introduction of PMID:15170388(https://pmc.ncbi.nlm.nih.gov/articles/PMC1134073/) explicitly connects these ARID1B aliases. UniProt also records AF468300/AAL76077.1 for PMID11988099 and AF259792/AAG36928.1 for PMID11734557 as historical N-terminally incomplete sequences. The imported four product identities remain unchanged; old constructs are not assigned a modern isoform merely from their names.
For PMID15170388, I read the original antibody and DNA-assay Methods, target Results, Figures 1, 4, 5, 7 and 8 legends, and relevant Discussion. Distinct monoclonal antibodies resolve ARID1A and ARID1B in human cells; reciprocal native-complex immunoprecipitation supports alternative assemblies containing either protein. Recombinant ARID1B DNA-fragment selection and DNA-cellulose assays establish DNA binding without an inferred AT-rich preference. Native coassociation by itself is not a purified binary-contact measurement. The normal cache contains the abstract only, so external body access does not change its availability flag. PMID:15170388, Two related ARID family proteins are alternative subunits of human SWI/SNF complexes.
For PMID:12200431, original author-uploaded article, I read the targeted construct/assay Methods and hOsa2 Results and Figures 3, 6–8, 10–11 legends. Human-library hOsa2 associates with native HeLa complexes; C33A reciprocal assays and GST-bait/in-vitro-translated partner assays resolve BRG1 and BRM association. Longer hOsa2 enhances steroid-receptor reporters, unlike its isolated C terminus or ARID deletion in the GR assay. Receptors were rat GR and human ER/AR. Historical clone lengths are not modern full-length isoform identities. These are source-local grounds for ATPase-binding refinement of the two original IPI rows and for coactivation; they do not confer a mechanism on uninspected screen pairs. The cache remains abstract-only.
The PMID11734557 correction, JBC 277:14350 was read directly. It corrects funding and a peptide's residue numbering; it is not a retraction or an altered functional conclusion. The original complete abstract explicitly identifies p250R in human complexes. Its SSX1 histone-binding experiment is not reassigned to ARID1B. Original full Methods remain unread; independently inspected PMID12200431 supports coactivation. PMID11988099's complete abstract establishes cloned human hELD/OSA1 and mouse-brain endogenous association; its exact localization experiment remains unread. Independent human nuclear extracts and HPA establish the broad nuclear pool.
The current Human Protein Atlas ARID1B subcellular table was inspected: nucleoplasm is supported; the listed plasma-membrane and cytosolic signals are uncertain. I did not reinterpret image pixels or infer new compartments. Broad nucleus/nucleoplasm assertions are supported independently of any unresolved individual historical source.
All five cached Reactome summaries were read. R-HSA-9932437 explicitly distinguishes ARID1A- and ARID1B-containing cBAF assembly; 9932836 describes DPF recruitment; 9933238 joins the ATPase module; 9934021 describes neural-progenitor assemblies with a mouse experimental basis. R-HSA-9825847 concerns MITF/TYRP1 recruitment. Their exact entity graphs were not reconstructed. The broad nucleoplasmic location is retained using independent human localization, without presenting every event as a direct human localization assay or assigning DPF histone-reading chemistry to ARID1B.
The original PAINT nodes PTN000291886 and PTN002652024 are preserved. Their complete IBD/tree/MSA placement has not been traced. Broad inherited localization, transcription and SWI/SNF membership have independent target corroboration; donor counts and target self-inclusion are not criticisms. The nucleosome-binding row already uses contributes_to, consistent with cooperative engagement by an ARID1B-containing remodeling complex, without asserting an isolated ARID1B histone interface. Specialized nBAF placement remains unresolved at the exact inherited-node scope.
Current official ontology pages were checked for ATPase binding GO:0051117, brahma complex GO:0035060, nucleosome binding GO:0031491, ATP-dependent chromatin remodeler activity GO:0140658 and transcription coactivator activity GO:0003713. The brahma term includes mammalian BRM-containing complexes. ATP hydrolysis belongs to SMARCA2/4; ARID1B supplies DNA/assembly contacts and contributes to the complex activity.
All 22 complete cached abstracts were read, plus the five event summaries. Cache full_text_available records retrieval availability, not proof that an entire paper and every supplement were inspected. Targeted cached body reads included PMID11263494, 12368262, 16932743, 23698369 and the ARID1B/antibody passages of 36950384. Eight screen-specific interactions from 33961781, 35271311, 36950384 and 40205054 have uninspected target tables/records. UniProt's positive interaction summaries are corroboration, not substitutes for those particular assay records. The requested actions follow the user's explicit ActionEnum: lack of access does not justify REMOVE.
PMID12368262's available Discussion explicitly treats BAF250a/b combinatorial assembly in murine neurons as an assumption and says definitive demonstration is difficult. It does not close the precise bBAF or differentiation assertions. PMID17920018 emphasizes BAF53b-dependent neuronal complexes; the target-specific ARID1B subcomplex evidence remains untraced. Early PMID8804307 establishes heterogeneous BAF complexes, but does not identify every modern ARID1B-containing neural assembly in its abstract.
PMID23698369 actually uses BAF250b antibodies, so it must not be described as wholly lacking ARID1B. The inspected interaction/deletion and chromosome-decatenation mechanism is resolved for BAF250a; ARID1B's specific metaphase/anaphase role remains uncertain. PMID16932743's inspected Results perturb BRG1/BRM and test double-strand-break repair; that does not by itself identify ARID1B's particular repair contribution. PMID12215535 is available as an abstract-only cache with preserved duplicated content; the yeast remodeling/human repair-factor context does not establish an isolated human ARID1B repair assay. No normal cache was repaired or overwritten.
PMID10778858, 11175787, 11790558 and 12110891 leave specific ARID1B cell-cycle, myoblast, differentiation and T-cell mechanisms unresolved in the inspected scope. In contrast, broad transcription/remodeling membership is independently demonstrated by the human target studies and can be retained without claiming those older sources were fully adjudicated. Official PubMed PMID17340523 confirms a Fumaria alkaloid-separation article. Its source assertion is retained UNDECIDED and the reference flagged WRONG_IDENTIFIER; there is no verified replacement.
The planned core synthesis separates DNA/complex remodeling contribution from demonstrated transcriptional coactivation. No new annotation or process is proposed. Native complex composition, exact developmental assemblies and isoform-specific effects remain distinct open questions.
Prospective consultation refined the core representation: transcription-initiation-coupled remodeling is attached to the DNA/complex remodeling core, while the reporter-supported coactivator core links to positive transcription. The reporter alone is not presented as a direct chromatin-remodeling measurement.
The inspected Human Protein Atlas ARID1B table reports supported nucleoplasm localization; plasma-membrane and cytosolic signals are uncertain. This supports a human nuclear pool without assigning exclusive localization or reinterpreting image pixels.
Historical hELD/OSA1 in PMID:11988099 is mapped to ARID1B by the alias discussion in PMID:15170388 and UniProt AF468300/AAL76077.1 provenance. Inoue hOsa1 is ARID1A, whereas Inoue hOsa2 is ARID1B; historical constructs are not assigned a modern isoform from the shared names.
The independently consulted all-51 map is now authored: 27 ACCEPT, two MODIFY and 22 UNDECIDED, with no NEW annotations. All original source objects and four alternative products are preserved. Only the two own-source ATPase pair assertions are refined; uninspected screen records remain uncertain. The DNA/remodeling core includes the established coupled-remodeling process as a synthesis, while the separate reporter-supported coactivator core links to positive transcription. SMARCA2/4 supplies ATP hydrolysis; no autonomous ARID1B enzyme activity is added.
Reference correctness distinguishes verified target support from metadata identity. External Methods access does not turn an abstract-only normal cache into full text. The user-supplied ActionEnum takes precedence over genericity-only removal preferences: unclear source evidence remains UNDECIDED, and positive interaction correctness is not rejected merely because protein binding is uninformative. Prospective consultation by alx3 checked all 51 decisions and the selected human source scopes before authorship. Final preservation, literal evidence and validation checks are recorded in the new history and tmp receipts.
The initial full validation passed with one deliberate action-consistency advisory: the unrelated PMID:17340523 leaves its Pol II transcription assertion UNDECIDED while independently supported assertions for that broad term are ACCEPT. Literal evidence checks passed for 57 quoted instances and 59 availability flags, with 22 PMID titles and five Reactome titles matched to immutable caches. All 51 source objects, four products and 29 raw/cache files remain unchanged. Final status validation, rendering, history validation and independent authored consultation are bound separately in the completion receipts.
The preceding counts and core-assignment statements describe the initial published review. The current decisions are 29 ACCEPT, two MODIFY and 20 UNDECIDED, with two cores and no NEW annotation. All 51 original annotation objects and four alternative products remain unchanged. The four action changes are acceptance of three nBAF/npBAF assertions and uncertainty for the specific initiation-coupled remodeling assertion.
The exact GOA provenance census is 19 ComplexPortal NAS records using ECO:0005547 and two UniProt NAS records using ECO:0000303. The latter are the original coactivator and initiation-coupled remodeling assertions. ComplexPortal NAS is curator reconstruction, not a claim that each referenced paper directly assayed every individual subunit. The official ComplexPortal manual, indexed sections 2.6.10.1–2.6.10.8, explains reconstruction from background knowledge and experimental information about components. Those sections were inspected; the direct PDF route failed, and no whole-manual or figure-pixel reading is claimed.
The inspected human Reactome ARID1B entity R-HSA-5225635 places ARID1B beneath the ARID1A,B component in both nBAF and npBAF membership branches. These are curated target-specific assembly statements, with the neural experimental and UniProt subunit basis explicitly retaining mouse orthology; they are not newly inspected human isolation assays.
The public locator is the human ARID1B entity, Locations in the PathwayBrowser. The actual identity and both membership branches were read, without reconstructing every linked reaction or original experiment. The cached npBAF formation event R-HSA-9934021 explicitly permits ARID1A or ARID1B and names a mouse experimental basis. Current UniProt neural-complex membership is also marked by similarity. This independently corroborated target membership supports the existing npBAF and nBAF assertions while preserving their original references and the unresolved PTN002652024 ancestry. The original BAF53b-focused PMID:17920018 experiment is not redescribed as a newly inspected ARID1B assay.
The current npBAF definition and nBAF definition include alternative ARID1A or ARID1B subunits. In contrast, bBAF GO:0140092 is distinguished by component composition. Its original PMID:12368262 Discussion presents BAF250a/b combinatorial assembly as an assumption and acknowledges difficulty demonstrating it. The separately resolved nBAF membership therefore does not automatically close this historical bBAF record.
A gene product can participate in a process by contributing within its complex; an isolated subunit assay is not required. The retained uncertainties for specialized cell-cycle, repair and differentiation records concern the relevant ARID1B-containing assembly, biological context, process direction or unreconstructed curator derivation. They are not a blanket rejection of ComplexPortal or an assertion that the experimental curators were wrong. Broad human DNA binding, complex remodeling and transcriptional coactivation remain independently established. The uninspected exact screen pairs remain uncertain under the user's ActionEnum; genericity alone is not grounds to remove an experimental assertion.
The current GO:0045815 definition and parents describe epigenetic remodeling that permits gene expression and relate it to initiation. The term is a descendant of broad chromatin remodeling. Direct human assembly/DNA contacts and receptor reporters support the broader activities, but the inspected PMID:11734557 abstract and independent reporter experiments do not close this more specific chromatin mechanism. Its original UniProt NAS record is now UNDECIDED, and the redundant specific child is removed from the remodeling core. The independent coactivator core remains linked to positive transcription. No ATPase activity is assigned to ARID1B.
Independent prospective consultation read all 51 decisions, the four changes, the official membership branches and ontology definitions, and the bounded ComplexPortal manual sections. Full original source limitations and the verified unrelated PMID:17340523 remain explicit. Historical observations and original source caches have not been rewritten.
The three existing npBAF/nBAF ACCEPT decisions now cite exact SUBUNIT passages in the preserved ARID1B UniProt record. The npBAF row additionally retains its exact cached Reactome R-HSA-9934021 passage. The nBAF quote explicitly includes “By similarity”; these curated statements do not establish a newly inspected human neural-complex isolation experiment or reconstruct the PAINT node.
The earlier inspection of the external Reactome ARID1B entity remains a bounded observation in this journal. Its uncached entity description is no longer used as a supporting-text attachment for these three rows. The other notes attachments report the previously inspected Human Protein Atlas localization table or the separately documented historical-alias analysis; UniProt's general nucleus statement does not replace the more specific nucleoplasm observation. No additional source retrieval or new biological claim is introduced.
All 51 original annotation objects, four alternative products, 29 ACCEPT/two MODIFY/20 UNDECIDED decisions and both cores remain unchanged. The original publication and all prior histories and normal source files are preserved.