ARID1A

UniProt ID: O14497
Organism: Homo sapiens
Review Status: COMPLETE
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Gene Description

ARID1A (BAF250A/p270) is a nuclear DNA-binding and assembly subunit of canonical mammalian SWI/SNF (cBAF) chromatin-remodeling complexes. Its ARID domain binds DNA without an established AT-rich sequence preference, while other regions associate with complex components and transcriptional regulators. ARID1A-containing complexes couple substrate engagement and regulatory recruitment to ATP-driven nucleosome remodeling by SMARCA4 or SMARCA2, supporting context-dependent transcriptional activation and repression. ARID1A and ARID1B occupy alternative positions in cBAF assemblies. ARID1A also participates in TOP2A-associated chromosome decatenation and contributes to developmental gene-regulatory programs; altered ARID1A function is associated with developmental disorders and cancer.

Existing Annotations Review

GO Term Evidence Action Reason
GO:0000785 chromatin
IDA
PMID:17363140
The core component of the mammalian SWI/SNF complex SMARCD3/...
ACCEPT
Summary: Chromatin is supported by the integrated human evidence.
Reason: Human endogenous HIC1/ARID1A association and promoter ChIP-reChIP independently support chromatin occupancy. Retain the original 17363140 IDA and explicitly leave its individual ARID1A assay uninspected.
Supporting Evidence:
PMID:19486893
sequential chromatin immunoprecipitation (ChIP-reChIP) experiments demonstrated that HIC1 represses E2F1 through the recruitment of anti-proliferative SWI/SNF complexes containing ARID1A.
GO:0000785 chromatin
NAS
PMID:12192000
REST repression of neuronal genes requires components of the...
ACCEPT
Summary: Chromatin is supported by the integrated human evidence.
Reason: The same independently observed chromatin recruitment establishes the broad location. The original REST recruitment source is retained; its exact ARID1A experiment remains unresolved.
Supporting Evidence:
PMID:19486893
sequential chromatin immunoprecipitation (ChIP-reChIP) experiments demonstrated that HIC1 represses E2F1 through the recruitment of anti-proliferative SWI/SNF complexes containing ARID1A.
GO:0003677 DNA binding
IDA
PMID:15640446
DNA-binding properties of ARID family proteins.
ACCEPT
Summary: DNA binding β€” accept.
Reason: Target Results and Methods identify human p270 constructs including NP_006006 residues 958–1188 and non-sequence-specific DNA binding; AT-rich preference is not inferred from the domain name.
Supporting Evidence:
PMID:15640446
In contrast to Dri, p270 (ARID1A) binds in a non-specific manner, binding to all fragments offered to it, showing selectivity only for longer fragments (>200 bp) at higher salt concentrations, presumably because longer fragments offer multiple binding sites.
GO:0003677 DNA binding
IDA
PMID:23129809
ARID1a-DNA interactions are required for promoter occupancy ...
ACCEPT
Summary: DNA binding is supported by the integrated human evidence.
Reason: Actual human p270 ARID DNA-binding Results and construct Methods establish the function. Retain the mouse-mutant original reference and explicitly do not relabel it a human IDA experiment.
Supporting Evidence:
PMID:15640446
In contrast to Dri, p270 (ARID1A) binds in a non-specific manner, binding to all fragments offered to it, showing selectivity only for longer fragments (>200 bp) at higher salt concentrations, presumably because longer fragments offer multiple binding sites.
GO:0003677 DNA binding
IEA
GO_REF:0000002
ACCEPT
Summary: DNA binding β€” accept.
Reason: The three actual InterPro source identifiers map a DNA-binding domain and are independently corroborated by direct human p270 assays in PMID:15640446 and PMID:10757798; no sequence preference is invented.
Supporting Evidence:
PMID:15640446
In contrast to Dri, p270 (ARID1A) binds in a non-specific manner, binding to all fragments offered to it, showing selectivity only for longer fragments (>200 bp) at higher salt concentrations, presumably because longer fragments offer multiple binding sites.
GO:0003677 DNA binding
NAS
PMID:10757798
The human SWI-SNF complex protein p270 is an ARID family mem...
ACCEPT
Summary: DNA binding β€” accept.
Reason: The original abstract directly characterizes human p270 DNA binding without preferential AT-rich sequence binding.
Supporting Evidence:
PMID:10757798
In contrast, p270 shows no sequence preference in its DNA binding activity
GO:0003713 transcription coactivator activity
IDA
PMID:12200431
Largest subunits of the human SWI/SNF chromatin-remodeling c...
ACCEPT
Summary: transcription coactivator activity β€” accept.
Reason: Human hOsa1/BAF250 coactivates steroid receptor transcription in the cited study. The gene is an accessory component of an ATPase-containing complex, not itself the ATPase.
Supporting Evidence:
PMID:12200431
In cultured mammalian cells, hOsa1 and hOsa2 stimulate transcription by the glucocorticoid, estrogen, and androgen receptors.
GO:0003713 transcription coactivator activity
NAS
PMID:8804307
Diversity and specialization of mammalian SWI/SNF complexes.
ACCEPT
Summary: Transcription coactivator activity is supported by the integrated human evidence.
Reason: Human hOsa1 receptor-dependent reporter activation establishes coactivator activity independently of the historical 8804307 source-local attribution.
Supporting Evidence:
PMID:12200431
In cultured mammalian cells, hOsa1 and hOsa2 stimulate transcription by the glucocorticoid, estrogen, and androgen receptors.
file:human/ARID1A/ARID1A-notes.md
The original PMID:12200431 human-clone Methods and Figures 3–5 and 8 distinguish native HeLa association, reciprocal C33A coprecipitation and GST/translated-fragment binding to BRG1 or BRM. Figures 9 and 11 show receptor-dependent activation by human hOsa1 in T47D cells; its isolated C terminus does not reproduce the activation. Rat GR and human ER/AR reagents are distinguished. These experiments support coactivator function within SWI/SNF rather than sequence-specific DNA recognition by ARID1A.
GO:0005515 protein binding
IPI
PMID:11780067
Selectivity of chromatin-remodelling cofactors for ligand-ac...
UNDECIDED
Summary: protein binding β€” undecided.
Reason: The exact ARID1A–SMARCA4 experiment from the ligand-activated transcription study remains unread; a plausible complex association does not settle this individual IPI source. Human hOsa1 association with BRG1/BRM is independently supported by PMID:12200431; that does not claim recovery of this original pair-level experiment.
GO:0005515 protein binding
IPI
PMID:11988099
Cloning and characterization of hELD/OSA1, a novel BRG1 inte...
UNDECIDED
Summary: protein binding β€” undecided.
Reason: The cloned hELD/OSA1 EHD2 binds BRG1, but historical alias use and the exact accession-to-ARID1A mapping remain unresolved. Mouse-brain endogenous complexes and human cloned reagent are distinguished; no paralog-error claim is made. The historical hELD/OSA1 naming distinction is discussed in PMID:12200431; the actual source clone mapping still requires resolution.
GO:0005515 protein binding
IPI
PMID:12200431
Largest subunits of the human SWI/SNF chromatin-remodeling c...
MODIFY
Summary: SMARCA2/BRM association supports ATPase binding.
Reason: Same-source human endogenous and reciprocal tagged hOsa1/hBRM association, plus mapped in-vitro fragment binding. ATPase is the partner class; no ATPase activity of ARID1A is inferred.
Proposed replacements: ATPase binding
Supporting Evidence:
PMID:12200431
Co-precipitation studies indicate that hOsa1 and hOsa2 associate with BRG1 and hBRM through the C-terminal domain of hOsa.
file:human/ARID1A/ARID1A-notes.md
The original PMID:12200431 human-clone Methods and Figures 3–5 and 8 distinguish native HeLa association, reciprocal C33A coprecipitation and GST/translated-fragment binding to BRG1 or BRM. Figures 9 and 11 show receptor-dependent activation by human hOsa1 in T47D cells; its isolated C terminus does not reproduce the activation. Rat GR and human ER/AR reagents are distinguished. These experiments support coactivator function within SWI/SNF rather than sequence-specific DNA recognition by ARID1A.
GO:0005515 protein binding
IPI
PMID:12200431
Largest subunits of the human SWI/SNF chromatin-remodeling c...
MODIFY
Summary: SMARCA4/BRG1 association supports ATPase binding.
Reason: Same-source human endogenous/reciprocal tagged association and in-vitro fragment binding support the more informative partner-class term.
Proposed replacements: ATPase binding
Supporting Evidence:
PMID:12200431
Co-precipitation studies indicate that hOsa1 and hOsa2 associate with BRG1 and hBRM through the C-terminal domain of hOsa.
file:human/ARID1A/ARID1A-notes.md
The original PMID:12200431 human-clone Methods and Figures 3–5 and 8 distinguish native HeLa association, reciprocal C33A coprecipitation and GST/translated-fragment binding to BRG1 or BRM. Figures 9 and 11 show receptor-dependent activation by human hOsa1 in T47D cells; its isolated C terminus does not reproduce the activation. Rat GR and human ER/AR reagents are distinguished. These experiments support coactivator function within SWI/SNF rather than sequence-specific DNA recognition by ARID1A.
GO:0005515 protein binding
IPI
PMID:12368262
Identification of a polymorphic, neuron-specific chromatin r...
UNDECIDED
Summary: protein binding β€” undecided.
Reason: The inspected source concerns murine neuronal complexes and discusses BAF250a/b combinatorial assembly as an assumption. The exact human ARID1A–BRG1 IPI experiment remains unresolved. Human hOsa1 association with BRG1/BRM is independently supported by PMID:12200431; that does not claim recovery of this original pair-level experiment.
GO:0005515 protein binding
IPI
PMID:15985610
PBAF chromatin-remodeling complex requires a novel specifici...
UNDECIDED
Summary: protein binding β€” undecided.
Reason: The PBAF/BAF200-centered abstract does not establish which ARID1A control or complex interaction was assayed. Preserve the IPI assertion while its target result is unread. Human hOsa1 association with BRG1/BRM is independently supported by PMID:12200431; that does not claim recovery of this original pair-level experiment.
GO:0005515 protein binding
IPI
PMID:17363140
The core component of the mammalian SWI/SNF complex SMARCD3/...
UNDECIDED
Summary: protein binding β€” undecided.
Reason: SRC1-dependent BAF60c coactivation is reported, but the actual ARID1A–SRC1 pair evidence is not exposed in the inspected abstract.
GO:0005515 protein binding
IPI
PMID:19486893
HIC1 interacts with a specific subunit of SWI/SNF complexes,...
MODIFY
Summary: HIC1 association supports DNA-binding transcription factor binding.
Reason: Original abstract explicitly reports endogenous target coIP and HIC1-dependent ARID1A recruitment. Official HIC1 record verifies sequence-specific transcriptional repressor identity. No purified binary interface claim.
Supporting Evidence:
PMID:19486893
Co-immunoprecipitation assays in WI38 fibroblasts and in BRG1-/- SW13 cells showed that endogenous HIC1 and ARID1A proteins interact in a BRG1-dependent manner.
GO:0005515 protein binding
IPI
PMID:23540691
Reversible disruption of mSWI/SNF (BAF) complexes by the SS1...
MODIFY
Summary: SMARCA4/BRG1 association supports ATPase binding.
Reason: Read original BAF-subunit coIP Results including BAF250a in human and mouse study contexts; retain the IPI coassociation scope rather than upgrade to an isolated interface. Human 12200431 corroborates the partner relationship.
Proposed replacements: ATPase binding
Supporting Evidence:
PMID:23540691
Immunoprecipitation studies using anti-Brg as well as antibodies specific to other established mSWI/SNF complex components including BAF250a, BAF155 and BAF47 confirmed the association of SS18 with native BAF complexes
GO:0005515 protein binding
IPI
O14497-1
PMID:23698369
BAF complexes facilitate decatenation of DNA by topoisomeras...
MODIFY
Summary: TOP2A association supports enzyme binding.
Reason: Read actual Fig4 heterologous BAF250a fragment/coIP Results and targeted Methods. TOP2A association is positive and supports enzyme binding; construct accession/species for that particular heterologous BAF250a panel remains unresolved. Preserve O14497-1 source isoform and IPI. Do not call all experiments human or purified binary binding. GO0044547 has a general text definition but its official parent table includes RO0004009 to type-IB topoisomerase PR000016542; that unresolved ontology inconsistency motivates using the unambiguous enzyme-binding parent rather than assuming the child.
Proposed replacements: enzyme binding
Supporting Evidence:
PMID:23698369
TopoIIΞ± associated with full-length BAF250a and BAF250a (aa1-1758), but not BAF250a (aa1759-2285) in a heterologous expression system
GO:0005515 protein binding
IPI
PMID:30021884
Histone Interaction Landscapes Visualized by Crosslinking Ma...
UNDECIDED
Summary: protein binding β€” undecided.
Reason: The exact ARID1A–SMARCD2 crosslink and its identifiers have not been inspected in the human-nucleus XL-MS inventory.
GO:0005515 protein binding
IPI
PMID:31759698
Recurrent SMARCB1 Mutations Reveal a Nucleosome Acidic Patch...
UNDECIDED
Summary: protein binding β€” undecided.
Reason: Methods show ARID1A immunopurification of canonical BAF for activity assays, but the exact ARID1A–SMARCA4 pair evidence underlying this IPI assertion remains uninspected. Human hOsa1 association with BRG1/BRM is independently supported by PMID:12200431; that does not claim recovery of this original pair-level experiment.
GO:0005515 protein binding
IPI
PMID:34591612
A protein interaction landscape of breast cancer.
UNDECIDED
Summary: protein binding β€” undecided.
Reason: The breast-cancer interactome's ARID1A–SMARCA2 pair, bait context and confidence record remain unread. Human hOsa1 association with BRG1/BRM is independently supported by PMID:12200431; that does not claim recovery of this original pair-level experiment.
GO:0005515 protein binding
IPI
PMID:34591612
A protein interaction landscape of breast cancer.
UNDECIDED
Summary: protein binding β€” undecided.
Reason: The breast-cancer interactome's ARID1A–SMARCA4 pair and source-specific detection remain unread. Human hOsa1 association with BRG1/BRM is independently supported by PMID:12200431; that does not claim recovery of this original pair-level experiment.
GO:0005515 protein binding
IPI
PMID:34591612
A protein interaction landscape of breast cancer.
UNDECIDED
Summary: protein binding β€” undecided.
Reason: The breast-cancer interactome's ARID1A–SMARCD2 pair and source-specific detection remain unread.
GO:0005515 protein binding
IPI
PMID:35271311
OpenCell: Endogenous tagging for the cartography of human ce...
UNDECIDED
Summary: protein binding β€” undecided.
Reason: The OpenCell endogenous ARID1A–SMARCA2 interaction record remains uninspected; platform-level methods do not resolve the pair. Human hOsa1 association with BRG1/BRM is independently supported by PMID:12200431; that does not claim recovery of this original pair-level experiment.
GO:0005515 protein binding
IPI
PMID:35271311
OpenCell: Endogenous tagging for the cartography of human ce...
UNDECIDED
Summary: protein binding β€” undecided.
Reason: The OpenCell endogenous ARID1A–SMARCA4 interaction record remains uninspected. Human hOsa1 association with BRG1/BRM is independently supported by PMID:12200431; that does not claim recovery of this original pair-level experiment.
GO:0005515 protein binding
IPI
PMID:35271311
OpenCell: Endogenous tagging for the cartography of human ce...
UNDECIDED
Summary: protein binding β€” undecided.
Reason: The OpenCell endogenous ARID1A–SMARCD2 interaction record remains uninspected.
GO:0005515 protein binding
IPI
PMID:36931659
Pioneer factor ASCL1 cooperates with the mSWI/SNF complex at...
MODIFY
Summary: ASCL1 association supports bHLH transcription factor binding.
Reason: Actual Fig5A Results describe reciprocal ASCL1/ARID1A coIP in human DIV24 neural cultures. Official GO0043425 is a specific child of GO0140297 and ASCL1 is a bHLH transcription factor. The separate fetal PLA panels test other BAF subunits and are not ARID1A evidence.
Supporting Evidence:
PMID:36931659
Immunoprecipitation followed by Western blot analysis in DIV24 neural cultures showing reciprocal coimmunoprecipitation of ASCL1 and SMARCC1 or ARID1A.
GO:0005634 nucleus
EXP
PMID:26614907
Identification and functional characterization of a novel bi...
ACCEPT
Summary: nucleus β€” accept.
Reason: The original ARID1A NLS study reports functional GFP fusion tests and nuclear wild-type protein. Exact isoform-specific distributions are not extrapolated.
Supporting Evidence:
PMID:26614907
We further show that cyto-nuclear localized, bipartite NLS mutant ARID1A exhibits greater stability than nuclear-localized, wild-type ARID1A.
GO:0005634 nucleus
IEA
GO_REF:0000044
ACCEPT
Summary: nucleus β€” accept.
Reason: The UniProt nuclear-location mapping agrees with ARID1A's nuclear import study and current human antibody-based nucleoplasm localization.
Supporting Evidence:
PMID:26614907
We further show that cyto-nuclear localized, bipartite NLS mutant ARID1A exhibits greater stability than nuclear-localized, wild-type ARID1A.
GO:0005634 nucleus
TAS
PMID:12200431
Largest subunits of the human SWI/SNF chromatin-remodeling c...
ACCEPT
Summary: nucleus β€” accept.
Reason: The human hOsa1 source purifies SWI/SNF-A from HeLa and tests transcriptional coactivation; nuclear residence is also corroborated independently by the NLS and HPA data.
Supporting Evidence:
PMID:12200431
Mass spectrometric analysis, and immunoblotting with antibodies specific to hOsa1 or hOsa2 demonstrate the presence of both proteins in SWI/SNF-A but not in the related polybromo-BRG1-associated factors complex purified from HeLa cells.
PMID:26614907
We further show that cyto-nuclear localized, bipartite NLS mutant ARID1A exhibits greater stability than nuclear-localized, wild-type ARID1A.
GO:0005654 nucleoplasm
IBA
GO_REF:0000033
ACCEPT
Summary: nucleoplasm β€” accept.
Reason: PAINT's inherited nucleoplasm assignment is corroborated by current human HPA localization. Target self-inclusion is legitimate descendant evidence; exact PTN000291886 placement was not reconstructed.
Propagation Review
Root cause: NO FAILURE CORE
Sources checked:
PANTHER:PTN000291886 Β· PTN000291886 UNRESOLVED
Original PAINT ancestral node preserved. Exact target-to-node topology, MSA and IBD assay scope were not independently reconstructed; donor count and target self-inclusion are not treated as defects. Independent target evidence and specialized-complex limits are evaluated in the annotation rationale.
Supporting Evidence:
file:human/ARID1A/ARID1A-notes.md
The current Human Protein Atlas ARID1A page reports supported nucleoplasm localization, with HPA005456 and CAB016334 in A-431, U-251MG and U2OS cells and HPA005456 in KOLF2.1J cells. The antibody-based location table was read; image pixels were not independently reinterpreted, and this does not establish an exclusive compartment.
GO:0005654 nucleoplasm
IDA
GO_REF:0000052
ACCEPT
Summary: nucleoplasm β€” accept.
Reason: The current original HPA target page reports supported nucleoplasm localization with HPA005456/CAB016334 in A-431, U-251MG, U2OS and HPA005456 in KOLF2.1J. Images were not independently reinterpreted and exclusivity is not asserted.
Supporting Evidence:
file:human/ARID1A/ARID1A-notes.md
The current Human Protein Atlas ARID1A page reports supported nucleoplasm localization, with HPA005456 and CAB016334 in A-431, U-251MG and U2OS cells and HPA005456 in KOLF2.1J cells. The antibody-based location table was read; image pixels were not independently reinterpreted, and this does not establish an exclusive compartment.
GO:0005654 nucleoplasm
TAS
Reactome:R-HSA-9766293
ACCEPT
Summary: nucleoplasm β€” accept.
Reason: The exact Reactome event places ARID1A at the human CDH1 promoter, agreeing with the nucleoplasmic active pool.
Supporting Evidence:
Reactome:R-HSA-9766293
ARID1A, a component of the SWI/SNF complex, binds to the CDH1 gene promoter (Yan et al. 2014, Baldi et al. 2022), likely recruiting the SWI/SNF chromatin remodeling complex to the CDH1 gene promoter.
GO:0005654 nucleoplasm
TAS
Reactome:R-HSA-9825847
ACCEPT
Summary: Nucleoplasm is supported by the integrated human evidence.
Reason: Human HPA nucleoplasm evidence and human nuclear-extract experiments independently support the location. The MITF Reactome target inventory remains UNVERIFIED; acceptance is not a claim that its exact graph entity was inspected.
Supporting Evidence:
file:human/ARID1A/ARID1A-notes.md
The current Human Protein Atlas ARID1A page reports supported nucleoplasm localization, with HPA005456 and CAB016334 in A-431, U-251MG and U2OS cells and HPA005456 in KOLF2.1J cells. The antibody-based location table was read; image pixels were not independently reinterpreted, and this does not establish an exclusive compartment.
GO:0005654 nucleoplasm
TAS
Reactome:R-HSA-9932437
ACCEPT
Summary: nucleoplasm β€” accept.
Reason: The exact event identifies ARID1A/ARID1B assembly into cBAF, contacts with the ATPase module and nonspecific DNA interaction; its nuclear complex context agrees with direct human localization.
Supporting Evidence:
Reactome:R-HSA-9932437
Recruitment of ARID1A or ARID1B to the forming cBAF complex represent a branching point that distinguishes it from pBAF, which contains ARID2 (Mashtalir et al, 2018; Mashtalir et al, 2020; He et al, 2020; Euskirchen et al, 2012). ARID1A and ARID1B extensively cross-link with core components of the assembling complex including SMARCC, SMARCD, SMARCB1 and SMARCE1 (Mashtalir et al, 2018). The ARID subunit in turn is responsible for making many of the contacts with the catalytic ATPase module as well as non-specifically with DNA (Mashtalir et al, 2018; Mashtalir et al 2020; reviewed in Euskirchen et al, 2012). <br>The functions of ARID1A- versus ARID1B -containing complexes are overlapping yet distinct, with both shared and unique genomic targets and different expression patterns. ARID1A expression is high in embryonic stem cells and ARID1B expression is activated during differentiation (Staahl et al, 2013; Staahl and Crabtree, 2013; Raab et al, 2015; reviewed in Pagliaroli and Trizzino, 2021). ARID1A and ARID1B are highly mutated in many cancers and in a range of neurodevelopmental disorders (reviewed in Bogershausen and Wollnick, 2018; Pagliaroli and Trizzino, 2021; Cenik and Shilatifard, 2021; Wang and Tang, 2023)
file:human/ARID1A/ARID1A-notes.md
The current Human Protein Atlas ARID1A page reports supported nucleoplasm localization, with HPA005456 and CAB016334 in A-431, U-251MG and U2OS cells and HPA005456 in KOLF2.1J cells. The antibody-based location table was read; image pixels were not independently reinterpreted, and this does not establish an exclusive compartment.
GO:0005654 nucleoplasm
TAS
Reactome:R-HSA-9932836
ACCEPT
Summary: nucleoplasm β€” accept.
Reason: The event title includes ARID1 and the summary describes DPF recruitment through ARID/SMARCC interactions in assembling cBAF. This supports the nuclear complex pool, without assigning DPF histone reading to ARID1A.
Supporting Evidence:
Reactome:R-HSA-9932836
cBAF assembly continues with the addition of a DPF protein (Double PHD Finger), a defining constituent of the complex (Mashtalir et al, 2018; Mashtalir et al, 2020). Three mutually exclusive DPF proteins may form part of the cBAF complex, DPF1 (also known as BAF45B), DPF2 (BAF45D) or DPF3 (BAF45C). The DPF subunit forms part of the base module of the SWI/SNF complex that contacts the nucleosome, and DPF proteins are recruited through interaction with ARID and SMARCC proteins (He et al, 2020). DPF proteins bind to acetylated tails of histone H3 and H4 (Hyun et al, 2024; Lange et al, 2008; Huber et al, 2017). Selective incorporation of DPF1, 2 or 3 in the cBAF complex may reflect cell type specificity or stage in development (Lange et al, 2008 Lessard et al, 2007).
file:human/ARID1A/ARID1A-notes.md
The current Human Protein Atlas ARID1A page reports supported nucleoplasm localization, with HPA005456 and CAB016334 in A-431, U-251MG and U2OS cells and HPA005456 in KOLF2.1J cells. The antibody-based location table was read; image pixels were not independently reinterpreted, and this does not establish an exclusive compartment.
GO:0005654 nucleoplasm
TAS
Reactome:R-HSA-9933238
ACCEPT
Summary: nucleoplasm β€” accept.
Reason: The exact event joins the ATPase module to an ARID1-containing cBAF core. Nucleoplasmic residence is consistent with independently observed human localization; ATP hydrolysis belongs to SMARCA2/4.
Supporting Evidence:
Reactome:R-HSA-9933238
SS18-containing ATPase complex binds SMARCC1 dimer:SMARCD1:SMARCE1:SMARCB1:ARID1:DPF1,2,3
file:human/ARID1A/ARID1A-notes.md
The current Human Protein Atlas ARID1A page reports supported nucleoplasm localization, with HPA005456 and CAB016334 in A-431, U-251MG and U2OS cells and HPA005456 in KOLF2.1J cells. The antibody-based location table was read; image pixels were not independently reinterpreted, and this does not establish an exclusive compartment.
GO:0005654 nucleoplasm
TAS
Reactome:R-HSA-9934021
ACCEPT
Summary: nucleoplasm β€” accept.
Reason: Reactome explicitly includes ARID1A/B in npBAF while identifying mouse studies as its basis. The inferred specialized assembly is not claimed as a new human experiment; broad nucleoplasmic residence has independent human support.
Supporting Evidence:
Reactome:R-HSA-9934021
Studies in mice identified a neural progenitor (np) BAF complex that is required for the proliferation of neural stem and progenitor cells (Lessard et al, 2007; Staahl et al, 2013). These complexes differ slightly from esBAF complexes in subunit composition. npBAF complexes contain either SMARCA4 or SMARCA2 as catalytic subunits, may contain either ARID1A or ARID1B, and contain SMARCD1 and SMARCD3 but not SMARCD2 (Lessard et al, 2007; Stahl et al, 2013; reviewed in Staahl and Crabtree, 2013; Kadoch and Crabtree, 2015; Cenik and Shilatifard, 2021; Innis and Cabot, 2020).
file:human/ARID1A/ARID1A-notes.md
The current Human Protein Atlas ARID1A page reports supported nucleoplasm localization, with HPA005456 and CAB016334 in A-431, U-251MG and U2OS cells and HPA005456 in KOLF2.1J cells. The antibody-based location table was read; image pixels were not independently reinterpreted, and this does not establish an exclusive compartment.
GO:0005654 nucleoplasm
TAS
Reactome:R-HSA-9934022
ACCEPT
Summary: nucleoplasm β€” accept.
Reason: The exact Reactome event title names ARID1A in the recipient esBAF complex. The summary retains its mouse-purification basis, while independent human HPA nucleoplasm localization supports this broad compartment annotation; no new human assembly assay is inferred.
Supporting Evidence:
Reactome:R-HSA-9934022
DPF2, PHF10 bind SMARCC1:SMARCC2 dimer:SMARD1:ARID1A
file:human/ARID1A/ARID1A-notes.md
The current Human Protein Atlas ARID1A page reports supported nucleoplasm localization, with HPA005456 and CAB016334 in A-431, U-251MG and U2OS cells and HPA005456 in KOLF2.1J cells. The antibody-based location table was read; image pixels were not independently reinterpreted, and this does not establish an exclusive compartment.
GO:0005654 nucleoplasm
TAS
Reactome:R-HSA-9934024
ACCEPT
Summary: nucleoplasm β€” accept.
Reason: The exact event title names an ARID1A-containing recipient esBAF complex, and independent human HPA data support the nucleoplasmic pool. Preserve the source’s model and ATPase-composition scope without transferring BRG1 activity to ARID1A or calling it a direct localization experiment.
Supporting Evidence:
Reactome:R-HSA-9934024
SMARCA4, BCL11A,B-containing ATPase module binds SMARCC1:SMACC2 dimer:SMARCD1:SMARCE1:SMARCB1:ARID1A:DPF2, PHF10
file:human/ARID1A/ARID1A-notes.md
The current Human Protein Atlas ARID1A page reports supported nucleoplasm localization, with HPA005456 and CAB016334 in A-431, U-251MG and U2OS cells and HPA005456 in KOLF2.1J cells. The antibody-based location table was read; image pixels were not independently reinterpreted, and this does not establish an exclusive compartment.
GO:0005654 nucleoplasm
TAS
Reactome:R-HSA-9934028
ACCEPT
Summary: nucleoplasm β€” accept.
Reason: The exact human esBAF summary explicitly identifies abundant ARID1A relative to ARID1B/ARID2, supporting its nuclear complex pool; cell-state expression differences are retained.
Supporting Evidence:
Reactome:R-HSA-9934028
ARID1A appears to be the most abundant ARID subunit in human esBAF complexes, although ARID1B and ARID2 have been identified in low amounts in some human and mouse purifications (Ho, Jothi et al, 2009; Ho, Ronan et al, 2009; Zhang et al, 2014; reviewed in Kadoch and Crabtree, 2015; Innis and Cabot, 2020; Cenik and Shilatifard, 2021).
file:human/ARID1A/ARID1A-notes.md
The current Human Protein Atlas ARID1A page reports supported nucleoplasm localization, with HPA005456 and CAB016334 in A-431, U-251MG and U2OS cells and HPA005456 in KOLF2.1J cells. The antibody-based location table was read; image pixels were not independently reinterpreted, and this does not establish an exclusive compartment.
GO:0006338 chromatin remodeling
IDA
PMID:11726552
Fanconi anemia protein, FANCA, associates with BRG1, a compo...
ACCEPT
Summary: Chromatin remodeling is supported by the integrated human evidence.
Reason: Purified human SWI/SNF remodeling together with identified human p270/hOsa1 complex participation supports the broad process. The original FANCA-centered target assay remains uninspected, not refuted.
Supporting Evidence:
PMID:8895581
Complexes containing BRG1 can disrupt nucleosomes and facilitate the binding of GAL4-VP16 to a nucleosomal template similar to the yeast SWI-SNF complex.
PMID:9584200
Purification and analysis of various proteins in this group reveals that they are components of the human SWI/SNF complex and that p270 is an integral member of this complex.
file:human/ARID1A/ARID1A-notes.md
The original PMID:8895581 Results and Figure 7 caption report ATP-dependent nucleosome disruption and improved GAL4-VP16 access by purified human YT complexes. The authors state: β€œBoth activities require the presence of hydrolyzable ATP”. This establishes activity of the complex; identified human p270/hOsa1 membership in later studies supplies the ARID1A attribution, without assigning ATP hydrolysis to ARID1A.
GO:0006338 chromatin remodeling
IDA
PMID:8895581
Purification and biochemical heterogeneity of the mammalian ...
ACCEPT
Summary: chromatin remodeling β€” accept.
Reason: The original source reports ATP-dependent nucleosome disruption by purified mammalian BRG1-associated complexes. Independent human p270 membership and assembly contacts support ARID1A's structural contribution to remodeling, without claiming it hydrolyzes ATP.
Supporting Evidence:
PMID:8895581
Complexes containing BRG1 can disrupt nucleosomes and facilitate the binding of GAL4-VP16 to a nucleosomal template similar to the yeast SWI-SNF complex.
PMID:9584200
Purification and analysis of various proteins in this group reveals that they are components of the human SWI/SNF complex and that p270 is an integral member of this complex.
GO:0006338 chromatin remodeling
IEA
GO_REF:0000002
ACCEPT
Summary: chromatin remodeling β€” accept.
Reason: The actual IPR021906 mapping agrees with direct p270 complex membership and DNA/recruitment work. A contributing structural subunit participates in remodeling even though SMARCA2/4 supplies the ATPase.
Supporting Evidence:
PMID:15640446
In contrast to Dri, p270 (ARID1A) binds in a non-specific manner, binding to all fragments offered to it, showing selectivity only for longer fragments (>200 bp) at higher salt concentrations, presumably because longer fragments offer multiple binding sites.
PMID:9584200
Purification and analysis of various proteins in this group reveals that they are components of the human SWI/SNF complex and that p270 is an integral member of this complex.
GO:0006338 chromatin remodeling
NAS
PMID:10078207
Reconstitution of a core chromatin remodeling complex from S...
ACCEPT
Summary: Chromatin remodeling is supported by the integrated human evidence.
Reason: The same direct complex-activity and human membership synthesis supports remodeling participation. Minimal reconstitution without ARID1A in the original abstract is not proof that a native ARID1A complex lacks the function.
Supporting Evidence:
PMID:8895581
Complexes containing BRG1 can disrupt nucleosomes and facilitate the binding of GAL4-VP16 to a nucleosomal template similar to the yeast SWI-SNF complex.
PMID:9584200
Purification and analysis of various proteins in this group reveals that they are components of the human SWI/SNF complex and that p270 is an integral member of this complex.
file:human/ARID1A/ARID1A-notes.md
The original PMID:8895581 Results and Figure 7 caption report ATP-dependent nucleosome disruption and improved GAL4-VP16 access by purified human YT complexes. The authors state: β€œBoth activities require the presence of hydrolyzable ATP”. This establishes activity of the complex; identified human p270/hOsa1 membership in later studies supplies the ARID1A attribution, without assigning ATP hydrolysis to ARID1A.
GO:0006357 regulation of transcription by RNA polymerase II
IBA
GO_REF:0000033
ACCEPT
Summary: regulation of transcription by RNA polymerase II β€” accept.
Reason: The inherited transcription-regulation assertion is corroborated by human hOsa1 coactivation and ARID1A/HIC1 repressive recruitment. Exact PTN000291886 placement is unresolved; donor count is not a quality measure.
Propagation Review
Root cause: NO FAILURE CORE
Sources checked:
PANTHER:PTN000291886 Β· PTN000291886 UNRESOLVED
Original PAINT ancestral node preserved. Exact target-to-node topology, MSA and IBD assay scope were not independently reconstructed; donor count and target self-inclusion are not treated as defects. Independent target evidence and specialized-complex limits are evaluated in the annotation rationale.
Supporting Evidence:
PMID:12200431
In cultured mammalian cells, hOsa1 and hOsa2 stimulate transcription by the glucocorticoid, estrogen, and androgen receptors.
PMID:19486893
sequential chromatin immunoprecipitation (ChIP-reChIP) experiments demonstrated that HIC1 represses E2F1 through the recruitment of anti-proliferative SWI/SNF complexes containing ARID1A.
GO:0006357 regulation of transcription by RNA polymerase II
NAS
PMID:11263494
The murine SNF5/INI1 chromatin remodeling factor is essentia...
ACCEPT
Summary: Regulation of transcription by RNA polymerase II is supported by the integrated human evidence.
Reason: Actual human coactivation and endogenous repressive recruitment establish unsigned Pol-II transcription regulation. Preserve the original murine SNF5 reference and unresolved target derivation.
Supporting Evidence:
PMID:12200431
In cultured mammalian cells, hOsa1 and hOsa2 stimulate transcription by the glucocorticoid, estrogen, and androgen receptors.
PMID:19486893
sequential chromatin immunoprecipitation (ChIP-reChIP) experiments demonstrated that HIC1 represses E2F1 through the recruitment of anti-proliferative SWI/SNF complexes containing ARID1A.
GO:0006357 regulation of transcription by RNA polymerase II
NAS
PMID:17340523
Separation and Quantification of Some Alkaloids from Fumaria...
UNDECIDED
Summary: regulation of transcription by RNA polymerase II β€” undecided.
Reason: Official PubMed PMID:17340523 is an alkaloid-separation study in Fumaria parviflora, not an established ARID1A source. Preserve original_reference_id and flag WRONG_IDENTIFIER; no replacement is known, and the citation error does not refute transcription regulation itself.
GO:0006357 regulation of transcription by RNA polymerase II
NAS
PMID:17920018
Regulation of dendritic development by neuron-specific chrom...
ACCEPT
Summary: Regulation of transcription by RNA polymerase II is supported by the integrated human evidence.
Reason: Accept broad transcription regulation from independent human evidence, without transferring the original specialized neuronal BAF/BAF53b experiment to ARID1A. Its separate nBAF row remains UNC.
Supporting Evidence:
PMID:12200431
In cultured mammalian cells, hOsa1 and hOsa2 stimulate transcription by the glucocorticoid, estrogen, and androgen receptors.
PMID:19486893
sequential chromatin immunoprecipitation (ChIP-reChIP) experiments demonstrated that HIC1 represses E2F1 through the recruitment of anti-proliferative SWI/SNF complexes containing ARID1A.
GO:0006357 regulation of transcription by RNA polymerase II
NAS
PMID:18809673
BRD7, a novel PBAF-specific SWI/SNF subunit, is required for...
ACCEPT
Summary: regulation of transcription by RNA polymerase II β€” accept.
Reason: The source explicitly reports ARID1A knockdown effects on SWI/SNF target transcription, distinct from BRD7/PBAF. It supports transcriptional regulation while the inspected R1 ESC context is kept separate from direct human hOsa1 evidence.
Supporting Evidence:
PMID:18809673
Knockdown studies of PBAF-specific BRD7 and of a signature subunit within the BAF complex, ARID1A, showed that these two subcomplexes affect SWI/SNF target genes differentially, in some cases even antagonistically.
GO:0006357 regulation of transcription by RNA polymerase II
NAS
PMID:8804307
Diversity and specialization of mammalian SWI/SNF complexes.
ACCEPT
Summary: Regulation of transcription by RNA polymerase II is supported by the integrated human evidence.
Reason: Human coactivation and repressive recruitment support this broad function, while the historical 8804307 individual-target attribution remains explicitly unresolved.
Supporting Evidence:
PMID:12200431
In cultured mammalian cells, hOsa1 and hOsa2 stimulate transcription by the glucocorticoid, estrogen, and androgen receptors.
PMID:19486893
sequential chromatin immunoprecipitation (ChIP-reChIP) experiments demonstrated that HIC1 represses E2F1 through the recruitment of anti-proliferative SWI/SNF complexes containing ARID1A.
GO:0016514 SWI/SNF complex
IBA
GO_REF:0000033
ACCEPT
Summary: SWI/SNF complex β€” accept.
Reason: Inherited SWI/SNF membership agrees with direct human p270 isolation and hOsa1 mass-spectrometric/immunoblot identification. Target self-inclusion is legitimate; detailed IBD placement is uninspected.
Propagation Review
Root cause: NO FAILURE CORE
Sources checked:
PANTHER:PTN000291886 Β· PTN000291886 UNRESOLVED
Original PAINT ancestral node preserved. Exact target-to-node topology, MSA and IBD assay scope were not independently reconstructed; donor count and target self-inclusion are not treated as defects. Independent target evidence and specialized-complex limits are evaluated in the annotation rationale.
Supporting Evidence:
PMID:9584200
Purification and analysis of various proteins in this group reveals that they are components of the human SWI/SNF complex and that p270 is an integral member of this complex.
GO:0016514 SWI/SNF complex
IDA
PMID:11078522
The human SWI/SNF-B chromatin-remodeling complex is related ...
ACCEPT
Summary: SWI/SNF complex is supported by the integrated human evidence.
Reason: Identified human p270/hOsa1 is a SWI/SNF-A component. Keep the original comparative PBAF/BAF source and its uninspected target-specific Results distinct.
Supporting Evidence:
PMID:9584200
Purification and analysis of various proteins in this group reveals that they are components of the human SWI/SNF complex and that p270 is an integral member of this complex.
PMID:12200431
Mass spectrometric analysis, and immunoblotting with antibodies specific to hOsa1 or hOsa2 demonstrate the presence of both proteins in SWI/SNF-A but not in the related polybromo-BRG1-associated factors complex purified from HeLa cells.
GO:0016514 SWI/SNF complex
IDA
PMID:12200431
Largest subunits of the human SWI/SNF chromatin-remodeling c...
ACCEPT
Summary: SWI/SNF complex β€” accept.
Reason: The source explicitly detects human hOsa1 in SWI/SNF-A and distinguishes it from PBAF; this is direct complex membership.
Supporting Evidence:
PMID:12200431
Mass spectrometric analysis, and immunoblotting with antibodies specific to hOsa1 or hOsa2 demonstrate the presence of both proteins in SWI/SNF-A but not in the related polybromo-BRG1-associated factors complex purified from HeLa cells.
GO:0016514 SWI/SNF complex
IDA
PMID:8804307
Diversity and specialization of mammalian SWI/SNF complexes.
ACCEPT
Summary: SWI/SNF complex is supported by the integrated human evidence.
Reason: Accept established human SWI/SNF membership; do not equate the historical unidentified 250-kDa band alone with a sequenced modern ARID1A reagent.
Supporting Evidence:
PMID:9584200
Purification and analysis of various proteins in this group reveals that they are components of the human SWI/SNF complex and that p270 is an integral member of this complex.
PMID:12200431
Mass spectrometric analysis, and immunoblotting with antibodies specific to hOsa1 or hOsa2 demonstrate the presence of both proteins in SWI/SNF-A but not in the related polybromo-BRG1-associated factors complex purified from HeLa cells.
GO:0016514 SWI/SNF complex
IDA
PMID:8895581
Purification and biochemical heterogeneity of the mammalian ...
ACCEPT
Summary: SWI/SNF complex β€” accept.
Reason: The source purifies tightly associated mammalian SWI/SNF complexes; human p270 membership is independently established by PMID:9584200. Preserve the experimentally curated broad membership without treating every early 250 kDa band as an identified sequence isoform.
Supporting Evidence:
PMID:8895581
this group of proteins associates tightly and is likely to be the mammalian equivalent of the yeast SWI-SNF complex.
PMID:9584200
Purification and analysis of various proteins in this group reveals that they are components of the human SWI/SNF complex and that p270 is an integral member of this complex.
GO:0016514 SWI/SNF complex
IDA
PMID:9584200
p300/CREB binding protein-related protein p270 is a componen...
ACCEPT
Summary: SWI/SNF complex β€” accept.
Reason: The source explicitly identifies human p270 as an integral SWI/SNF member, distinct from p300/CBP despite antibody cross-reactivity.
Supporting Evidence:
PMID:9584200
Purification and analysis of various proteins in this group reveals that they are components of the human SWI/SNF complex and that p270 is an integral member of this complex.
GO:0016514 SWI/SNF complex
IEA
GO_REF:0000120
ACCEPT
Summary: SWI/SNF complex β€” accept.
Reason: The ARBA/IPR021906 combined membership mapping is directly corroborated by human p270/BAF250 isolation and hOsa1 SWI/SNF-A identification.
Supporting Evidence:
PMID:9584200
Purification and analysis of various proteins in this group reveals that they are components of the human SWI/SNF complex and that p270 is an integral member of this complex.
GO:0016514 SWI/SNF complex
NAS
PMID:8804307
Diversity and specialization of mammalian SWI/SNF complexes.
ACCEPT
Summary: SWI/SNF complex is supported by the integrated human evidence.
Reason: Same independently established human membership supports the NAS assertion. Original source identity/evidence are preserved and not silently replaced.
Supporting Evidence:
PMID:9584200
Purification and analysis of various proteins in this group reveals that they are components of the human SWI/SNF complex and that p270 is an integral member of this complex.
PMID:12200431
Mass spectrometric analysis, and immunoblotting with antibodies specific to hOsa1 or hOsa2 demonstrate the presence of both proteins in SWI/SNF-A but not in the related polybromo-BRG1-associated factors complex purified from HeLa cells.
GO:0016922 nuclear receptor binding
IPI
PMID:17363140
The core component of the mammalian SWI/SNF complex SMARCD3/...
UNDECIDED
Summary: nuclear receptor binding β€” undecided.
Reason: Exact ARID1A–estrogen receptor binding is not exposed in the BAF60c-centered abstract; coactivation alone is not a direct receptor-binding assay.
GO:0016922 nuclear receptor binding
IPI
PMID:17363140
The core component of the mammalian SWI/SNF complex SMARCD3/...
UNDECIDED
Summary: nuclear receptor binding β€” undecided.
Reason: Exact ARID1A–retinoic acid receptor binding remains unread; the BAF60c/RAR finding cannot be reassigned to ARID1A.
GO:0030071 regulation of mitotic metaphase/anaphase transition
NAS
PMID:23698369
BAF complexes facilitate decatenation of DNA by topoisomeras...
KEEP AS NON CORE
Summary: regulation of mitotic metaphase/anaphase transition β€” keep as non core.
Reason: The targeted BAF250a knockdown work shows chromosome bridges and mitotic defects in mouse MEFs, consistent with its role in TOP2A-associated decatenation. Retain the developmental/cell-cycle context with explicit model-species scope rather than claim direct human experiments or ATPase activity.
GO:0030071 regulation of mitotic metaphase/anaphase transition
NAS
PMID:25066234
Requirement for PBAF in transcriptional repression and repai...
UNDECIDED
Summary: regulation of mitotic metaphase/anaphase transition β€” undecided.
Reason: Inspected PBAF/BAF180 Results and human cell Methods do not expose ARID1A-dependent metaphase/anaphase control. Supplemental targeting records remain unread; absence from a bounded search is not proof of wrong attribution.
GO:0031491 nucleosome binding
IBA
GO_REF:0000033
ACCEPT
Summary: nucleosome binding β€” accept.
Reason: This IBA already records contribution to nucleosome binding. Mouse domain-mutant evidence and human ARID DNA-binding/complex-contact evidence fit cooperative substrate engagement; exact PTN000291886 placement remains uninspected.
Propagation Review
Root cause: NO FAILURE CORE
Sources checked:
PANTHER:PTN000291886 Β· PTN000291886 UNRESOLVED
Original PAINT ancestral node preserved. Exact target-to-node topology, MSA and IBD assay scope were not independently reconstructed; donor count and target self-inclusion are not treated as defects. Independent target evidence and specialized-complex limits are evaluated in the annotation rationale.
GO:0035060 brahma complex
IEA
GO_REF:0000002
ACCEPT
Summary: brahma complex β€” accept.
Reason: Current GO:0035060 explicitly includes mammalian SMARCA2/BRM-containing SWI/SNF complexes. Human hOsa1 association with hBRM corroborates the InterPro mapping; it is not treated as a fly-only complex.
Supporting Evidence:
PMID:12200431
Co-precipitation studies indicate that hOsa1 and hOsa2 associate with BRG1 and hBRM through the C-terminal domain of hOsa.
GO:0035060 brahma complex
NAS
PMID:8804307
Diversity and specialization of mammalian SWI/SNF complexes.
ACCEPT
Summary: Brahma complex is supported by the integrated human evidence.
Reason: Original human endogenous hOsa1/hBRM coprecipitation and hOsa1-BRM association support membership in a BRM-containing SWI/SNF assembly, consistent with the actual GO0035060 definition. Do not conflate BRM and BRG1 assemblies.
Supporting Evidence:
PMID:12200431
Co-precipitation studies indicate that hOsa1 and hOsa2 associate with BRG1 and hBRM through the C-terminal domain of hOsa.
file:human/ARID1A/ARID1A-notes.md
The original PMID:12200431 human-clone Methods and Figures 3–5 and 8 distinguish native HeLa association, reciprocal C33A coprecipitation and GST/translated-fragment binding to BRG1 or BRM. Figures 9 and 11 show receptor-dependent activation by human hOsa1 in T47D cells; its isolated C terminus does not reproduce the activation. Rat GR and human ER/AR reagents are distinguished. These experiments support coactivator function within SWI/SNF rather than sequence-specific DNA recognition by ARID1A.
GO:0045582 positive regulation of T cell differentiation
NAS
PMID:12110891
Reciprocal regulation of CD4/CD8 expression by SWI/SNF-like ...
UNDECIDED
Summary: positive regulation of T cell differentiation β€” undecided.
Reason: The T-cell source identifies BAF57 and Brg perturbations. ARID1A-specific work supporting positive T-cell differentiation is not resolved; it is not inferred from mere membership.
GO:0045597 positive regulation of cell differentiation
NAS
PMID:11790558
SWI/SNF chromatin remodeling and cancer.
UNDECIDED
Summary: positive regulation of cell differentiation β€” undecided.
Reason: The broad cancer/remodeling review does not expose the ARID1A-specific differentiation basis of this NAS row.
GO:0045597 positive regulation of cell differentiation
NAS
PMID:12368262
Identification of a polymorphic, neuron-specific chromatin r...
UNDECIDED
Summary: positive regulation of cell differentiation β€” undecided.
Reason: The neuron-specific complex study establishes BAF53b and discusses BAF250 combinatorial assembly, but ARID1A-performed positive differentiation regulation remains unresolved.
GO:0045663 positive regulation of myoblast differentiation
NAS
PMID:11175787
Mammalian SWI/SNF complexes promote MyoD-mediated muscle dif...
UNDECIDED
Summary: positive regulation of myoblast differentiation β€” undecided.
Reason: The MyoD/SWI-SNF study's exact ARID1A-dependent myoblast differentiation result is uninspected; a complex-level phenotype alone is not assigned wholesale to the subunit.
GO:0045815 transcription initiation-coupled chromatin remodeling
TAS
PMID:12200431
Largest subunits of the human SWI/SNF chromatin-remodeling c...
ACCEPT
Summary: transcription initiation-coupled chromatin remodeling β€” accept.
Reason: Human hOsa1's promoter-coactivation role in an ATP-dependent SWI/SNF-A complex supports its structural/recruitment contribution to transcription-coupled remodeling. It is not assigned autonomous ATP hydrolysis.
Supporting Evidence:
PMID:12200431
In cultured mammalian cells, hOsa1 and hOsa2 stimulate transcription by the glucocorticoid, estrogen, and androgen receptors.
GO:0045893 positive regulation of DNA-templated transcription
IBA
GO_REF:0000033
ACCEPT
Summary: positive regulation of DNA-templated transcription β€” accept.
Reason: PAINT's positive transcription-regulation assertion is independently corroborated by human steroid-receptor coactivation. Target inclusion in the source list is legitimate; uninspected IBD placement is not described as circular.
Propagation Review
Root cause: NO FAILURE CORE
Sources checked:
PANTHER:PTN000291886 Β· PTN000291886 UNRESOLVED
Original PAINT ancestral node preserved. Exact target-to-node topology, MSA and IBD assay scope were not independently reconstructed; donor count and target self-inclusion are not treated as defects. Independent target evidence and specialized-complex limits are evaluated in the annotation rationale.
Supporting Evidence:
PMID:12200431
In cultured mammalian cells, hOsa1 and hOsa2 stimulate transcription by the glucocorticoid, estrogen, and androgen receptors.
GO:0045893 positive regulation of DNA-templated transcription
IDA
PMID:12200431
Largest subunits of the human SWI/SNF chromatin-remodeling c...
ACCEPT
Summary: positive regulation of DNA-templated transcription β€” accept.
Reason: The original study reports stimulation of steroid receptor-mediated transcription by human hOsa1; this is active co-regulatory work, not simply gene expression correlation.
Supporting Evidence:
PMID:12200431
In cultured mammalian cells, hOsa1 and hOsa2 stimulate transcription by the glucocorticoid, estrogen, and androgen receptors.
GO:0070316 regulation of G0 to G1 transition
NAS
PMID:11790558
SWI/SNF chromatin remodeling and cancer.
UNDECIDED
Summary: regulation of G0 to G1 transition β€” undecided.
Reason: The review-level source does not expose a target-specific ARID1A mechanism regulating G0-to-G1 transition.
GO:0071564 npBAF complex
ISS
GO_REF:0000024
UNDECIDED
Summary: npBAF complex β€” undecided.
Reason: The actual ISS donor A2BH40 is retained, but its exact npBAF source experiment has not been traced. Human progenitor association is compatible without closing the original donor record.
Propagation Review
Root cause: UNRESOLVED
Sources checked:
UniProtKB:A2BH40 UNRESOLVED
Original donor retained; exact source experiment and specialized neuronal assembly have not been traced.
GO:0071564 npBAF complex
NAS
PMID:8804307
Diversity and specialization of mammalian SWI/SNF complexes.
UNDECIDED
Summary: npBAF complex β€” undecided.
Reason: The early complex-diversity source does not expose a neuronal-progenitor-specific ARID1A assembly. No absence is inferred solely from its publication date.
GO:0071565 nBAF complex
IBA
GO_REF:0000033
UNDECIDED
Summary: nBAF complex β€” undecided.
Reason: The nBAF IBA's PTN002652024 and exact donor experiments have not been reconstructed; neural-progenitor evidence does not alone establish the mature-neuronal subcomplex. No phylogenetic failure or weak-donor-count claim is made.
Propagation Review
Root cause: UNRESOLVED
Sources checked:
PANTHER:PTN002652024 Β· PTN002652024 UNRESOLVED
Original PAINT ancestral node preserved. Exact target-to-node topology, MSA and IBD assay scope were not independently reconstructed; donor count and target self-inclusion are not treated as defects. Independent target evidence and specialized-complex limits are evaluated in the annotation rationale.
GO:0071565 nBAF complex
ISS
GO_REF:0000024
UNDECIDED
Summary: nBAF complex β€” undecided.
Reason: The A2BH40 ISS donor's mature neuronal nBAF evidence remains untraced; preserve the source rather than equate nBAF with npBAF.
Propagation Review
Root cause: UNRESOLVED
Sources checked:
UniProtKB:A2BH40 UNRESOLVED
Original donor retained; exact source experiment and specialized neuronal assembly have not been traced.
GO:0071565 nBAF complex
NAS
PMID:17920018
Regulation of dendritic development by neuron-specific chrom...
UNDECIDED
Summary: nBAF complex β€” undecided.
Reason: The source establishes neuron-specific BAF53b functions, but the exact ARID1A-containing nBAF measurement underlying this NAS assertion is uninspected.
GO:0140092 bBAF complex
NAS
PMID:12368262
Identification of a polymorphic, neuron-specific chromatin r...
UNDECIDED
Summary: bBAF complex β€” undecided.
Reason: The paper's discussion explicitly assumes BAF250a/b combinatorial assembly in murine neurons; exact ARID1A membership in the defined bBAF assembly has not been established in the inspected source scope.
GO:0140658 ATP-dependent chromatin remodeler activity
IDA
PMID:8895581
Purification and biochemical heterogeneity of the mammalian ...
ACCEPT
Summary: ATP-dependent chromatin remodeler activity is supported by the integrated human evidence.
Reason: Actual original human YT complex Results/Fig7 demonstrate ATP-dependent nucleosome disruption and facilitated activator access; later identified human p270/hOsa1 membership supplies target attribution. Preserve enables, do not infer intrinsic ARID1A ATP hydrolysis, and retain contributes_to in the core. Qualifier alone is not a reason to reject complex participation.
Supporting Evidence:
PMID:8895581
Complexes containing BRG1 can disrupt nucleosomes and facilitate the binding of GAL4-VP16 to a nucleosomal template similar to the yeast SWI-SNF complex.
PMID:9584200
Purification and analysis of various proteins in this group reveals that they are components of the human SWI/SNF complex and that p270 is an integral member of this complex.
file:human/ARID1A/ARID1A-notes.md
The original PMID:8895581 Results and Figure 7 caption report ATP-dependent nucleosome disruption and improved GAL4-VP16 access by purified human YT complexes. The authors state: β€œBoth activities require the presence of hydrolyzable ATP”. This establishes activity of the complex; identified human p270/hOsa1 membership in later studies supplies the ARID1A attribution, without assigning ATP hydrolysis to ARID1A.
GO:1902459 positive regulation of stem cell population maintenance
NAS
PMID:19279220
An embryonic stem cell chromatin remodeling complex, esBAF, ...
UNDECIDED
Summary: positive regulation of stem cell population maintenance β€” undecided.
Reason: The esBAF source explicitly concerns mouse ES self-renewal and specialized complex composition; the ARID1A-specific positive stem-population mechanism is not resolved from the inspected abstract.
GO:2000045 regulation of G1/S transition of mitotic cell cycle
NAS
PMID:10778858
Exit from G1 and S phase of the cell cycle is regulated by r...
UNDECIDED
Summary: regulation of G1/S transition of mitotic cell cycle β€” undecided.
Reason: The source describes Rb/HDAC/SWI-SNF repression and cyclin timing, but the ARID1A-specific G1/S role is not exposed in the available abstract.
GO:2000781 positive regulation of double-strand break repair
NAS
PMID:16932743
Mammalian SWI/SNF complexes facilitate DNA double-strand bre...
UNDECIDED
Summary: positive regulation of double-strand break repair β€” undecided.
Reason: The repair source reports SWI/SNF catalytic-core perturbations and gamma-H2AX effects; exact ARID1A-specific repair regulation requires its target experiment.
GO:2000781 positive regulation of double-strand break repair
NAS
PMID:25066234
Requirement for PBAF in transcriptional repression and repai...
UNDECIDED
Summary: positive regulation of double-strand break repair β€” undecided.
Reason: Targeted full-text PBAF Results assign the studied repair effects to BAF180/BRG1. ARID1A's source-local evidence remains unresolved, including unread supplements; no categorical paralog misattribution is asserted.
GO:2000819 regulation of nucleotide-excision repair
NAS
PMID:12215535
The SWI/SNF chromatin-remodeling factor stimulates repair by...
UNDECIDED
Summary: regulation of nucleotide-excision repair β€” undecided.
Reason: Indexed primary Methods use a yeast SWI/SNF complex with human excision factors. This does not directly assay human ARID1A; the human NAS derivation remains unresolved without claiming the biological repair role is impossible.

Core Functions

Bind DNA and supply structural and recruitment contacts within ARID1A-containing cBAF complexes, contributing to nucleosome remodeling and transcriptional regulation. ARID1A does not itself supply the SMARCA2/4 ATPase activity.

Supporting Evidence:
  • PMID:15640446
    In contrast to Dri, p270 (ARID1A) binds in a non-specific manner, binding to all fragments offered to it, showing selectivity only for longer fragments (>200 bp) at higher salt concentrations, presumably because longer fragments offer multiple binding sites.
  • PMID:12200431
    In cultured mammalian cells, hOsa1 and hOsa2 stimulate transcription by the glucocorticoid, estrogen, and androgen receptors.
  • PMID:9584200
    Purification and analysis of various proteins in this group reveals that they are components of the human SWI/SNF complex and that p270 is an integral member of this complex.
  • PMID:19486893
    sequential chromatin immunoprecipitation (ChIP-reChIP) experiments demonstrated that HIC1 represses E2F1 through the recruitment of anti-proliferative SWI/SNF complexes containing ARID1A.
  • Reactome:R-HSA-9932437
    The ARID subunit in turn is responsible for making many of the contacts with the catalytic ATPase module as well as non-specifically with DNA
  • PMID:8895581
    Complexes containing BRG1 can disrupt nucleosomes and facilitate the binding of GAL4-VP16 to a nucleosomal template similar to the yeast SWI-SNF complex.
  • file:human/ARID1A/ARID1A-notes.md
    The original PMID:8895581 Results and Figure 7 caption report ATP-dependent nucleosome disruption and improved GAL4-VP16 access by purified human YT complexes. The authors state: β€œBoth activities require the presence of hydrolyzable ATP”. This establishes activity of the complex; identified human p270/hOsa1 membership in later studies supplies the ARID1A attribution, without assigning ATP hydrolysis to ARID1A.

Promote receptor-dependent transcription as a coactivator within human SWI/SNF complexes. Human hOsa1 enhances steroid-receptor reporter activation in the inspected cellular assays; this function cooperates with DNA engagement and complex recruitment, and does not imply activation of every ARID1A target.

Supporting Evidence:
  • PMID:12200431
    In cultured mammalian cells, hOsa1 and hOsa2 stimulate transcription by the glucocorticoid, estrogen, and androgen receptors.
  • file:human/ARID1A/ARID1A-notes.md
    The original PMID:12200431 human-clone Methods and Figures 3–5 and 8 distinguish native HeLa association, reciprocal C33A coprecipitation and GST/translated-fragment binding to BRG1 or BRM. Figures 9 and 11 show receptor-dependent activation by human hOsa1 in T47D cells; its isolated C terminus does not reproduce the activation. Rat GR and human ER/AR reagents are distinguished. These experiments support coactivator function within SWI/SNF rather than sequence-specific DNA recognition by ARID1A.

References

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Suggested Questions for Experts

Q: How do ARID1A DNA contacts and transcription-factor recruitment divide locus selection between ARID1A- and ARID1B-containing assemblies?

Q: Which native human cell contexts switch ARID1A-containing complexes between receptor coactivation and HIC1-dependent repression?

Q: How does the BAF250a-TOP2A interface influence decatenation independently of global chromatin accessibility?

Suggested Experiments

Experiment: Compare defined endogenous ARID1A and ARID1B assemblies in neural progenitors and differentiated neurons, retaining isoform identity, quantitative subunit composition and chromatin-recruitment measurements.

πŸ“š Additional Documentation

Notes

(ARID1A-notes.md)

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πŸ“„ View Raw YAML

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