CHD2 is a nuclear ATP-dependent chromatin remodeler with tandem chromodomains and an SNF2-family motor. It binds DNA and histones, uses ATP hydrolysis to organize nucleosomes, and regulates chromatin accessibility and histone H3.3 occupancy. Its recruitment can depend on lineage-specific transcription factors or, at DNA breaks, PARP1-generated poly(ADP-ribose). These chromatin activities contribute to gene-expression programs during development and to an accessible environment for nonhomologous end joining. Human CHD2 haploinsufficiency alters cortical interneuron development and is associated with developmental disorders and epilepsy. MyoD-dependent recruitment supports myogenic chromatin marking before differentiation in mouse cells; FOSL1-associated recruitment supports a distinct transcriptional program in human glioma cells.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0000785 chromatin | IBA GO_REF:0000033 | ACCEPT | Summary: CHD2 performs its remodeling activity on nuclear chromatin. Reason: The PAINT active-in assertion agrees with human chromatin recruitment, ATP-dependent chromatin expansion and purified nucleosome remodeling. It is a functional chromatin location, not simply recovery of a soluble protein. The ancestral node is preserved without reconstructing its historical IBD or judging support by donor count. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN002473914 SUPPORTS TRANSFER The actual curated PAINT assertion at PANTHER:PTN002473914 is accepted as the transfer basis, with human damage-site chromatin recruitment and purified nucleosome remodeling (PMID:26895424; PMID:25384982) corroborating the target capability. This is qualified deference to the curated phylogenetic judgment, not independent reconstruction or validation of its historical IBD placement. Current target evidence alone does not establish that placement; neither donor count nor target self-reference is treated as a defect. |
| GO:0000978 RNA polymerase II cis-regulatory region sequence-specific DNA binding | IEA GO_REF:0000107 | MODIFY | Summary: Refine the inferred motif-specific activity to demonstrated cis-regulatory-region binding. Reason: The exact mouse donor E9PZM4 carries promoter-binding IMP evidence from PMID:22569126. ChIP/re-ChIP and MyoD gain/loss show MyoD-dependent Chd2 recruitment to myogenic promoters, including Ckm, without isolating a CHD2 recognition motif. GO:0000976 explicitly allows non-specific binding to transcription regulatory regions and preserves this experimentally observed regulatory context. Human CHD2 genomic occupancy in PMID:36115870 and FOSL1-dependent regulatory-element recruitment in PMID:38767413 independently corroborate the context. Purified human duplex-DNA binding in PMID:25384982 is a separate capability; it does not by itself encode promoter location. No inability to recognize particular sequences is asserted. Proposed replacements: transcription cis-regulatory region binding Supporting Evidence: PMID:22569126 Chd2 recruitment is MyoD-dependent file:human/CHD2/CHD2-source-evidence.json |
| GO:0000978 RNA polymerase II cis-regulatory region sequence-specific DNA binding | ISS GO_REF:0000024 | MODIFY | Summary: Refine the inferred motif-specific activity to demonstrated cis-regulatory-region binding. Reason: The exact mouse donor E9PZM4 carries promoter-binding IMP evidence from PMID:22569126. ChIP/re-ChIP and MyoD gain/loss show MyoD-dependent Chd2 recruitment to myogenic promoters, including Ckm, without isolating a CHD2 recognition motif. GO:0000976 explicitly allows non-specific binding to transcription regulatory regions and preserves this experimentally observed regulatory context. Human CHD2 genomic occupancy in PMID:36115870 and FOSL1-dependent regulatory-element recruitment in PMID:38767413 independently corroborate the context. Purified human duplex-DNA binding in PMID:25384982 is a separate capability; it does not by itself encode promoter location. No inability to recognize particular sequences is asserted. Proposed replacements: transcription cis-regulatory region binding Supporting Evidence: PMID:22569126 Chd2 is targeted to the Ckm promoter via MyoD file:human/CHD2/CHD2-source-evidence.json |
| GO:0003677 DNA binding | IBA GO_REF:0000033 | ACCEPT | Summary: DNA binding is a substrate-recognition component of CHD2 remodeling. Reason: Purified human full-length CHD2 and domain constructs bind defined double-stranded DNA in EMSA experiments; stronger binding to longer duplexes is not evidence of a sequence-specific transcription-factor motif. This directly corroborates the ancestral DNA-binding assertion. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN002473914 SUPPORTS TRANSFER The actual curated PAINT assertion at PANTHER:PTN002473914 is accepted as the transfer basis, with purified human CHD2 binding to defined duplex DNA (PMID:25384982) corroborating the target capability. This is qualified deference to the curated phylogenetic judgment, not independent reconstruction or validation of its historical IBD placement. Current target evidence alone does not establish that placement; neither donor count nor target self-reference is treated as a defect. |
| GO:0003677 DNA binding | TAS PMID:9326634 Characterization of the CHD family of proteins. | ACCEPT | Summary: Retain the historical DNA-binding assertion with later direct CHD2 corroboration. Reason: The original 1997 paper establishes human CHD2 sequence/domain relationships, whereas much of its direct DNA-binding precedent concerns CHD1. Later purified human CHD2 experiments directly establish duplex DNA binding. Retain the correct TAS capability without redescribing the old family-comparison paper as a human CHD2 biochemical assay. |
| GO:0003682 chromatin binding | IBA GO_REF:0000033 | ACCEPT | Summary: CHD2 binds and remodels chromatin. Reason: Human-cell chromatin occupancy, damage-site recruitment and purified nucleosome-remodeling experiments independently support this conserved substrate-binding function. The PAINT inference is retained as an ancestral judgment rather than treated as a collection of pairwise transfers. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN002473914 SUPPORTS TRANSFER The actual curated PAINT assertion at PANTHER:PTN002473914 is accepted as the transfer basis, with human chromatin occupancy and purified nucleosome remodeling (PMID:36115870; PMID:25384982) corroborating the target capability. This is qualified deference to the curated phylogenetic judgment, not independent reconstruction or validation of its historical IBD placement. Current target evidence alone does not establish that placement; neither donor count nor target self-reference is treated as a defect. |
| GO:0003723 RNA binding | HDA PMID:22658674 Insights into RNA biology from an atlas of mammalian mRNA-bi... | KEEP AS NON CORE | Summary: CHD2 is a source-verified HeLa mRNA-interactome hit, outside the remodeling core. Reason: The recovered original Table S1 identifies CHD2 in crosslinked capture but not controls. Ion-count adjusted p=0.00218 meets the study threshold, whereas spectral-count p=0.713 does not; either method could qualify a protein. Gene-level peptide grouping does not resolve an isoform, RNA target or regulatory mechanism. Retain the non-core capability, with the separate Baltz result as corroboration. |
| GO:0003723 RNA binding | HDA PMID:22681889 The mRNA-bound proteome and its global occupancy profile on ... | KEEP AS NON CORE | Summary: CHD2 is a positive RNA-capture hit, outside its established remodeling core. Reason: The original author thesis Table S1 lists CHD2 in class II. Its two measured light-crosslinked experiments are enriched after applying the actual raw H/L convention; the reverse-label experiment is unavailable, not a negative result. This supports RNA association at capture scope. The gene-level table does not identify an RNA target, a unique CHD2 isoform or a specific RNA-processing function. |
| GO:0005515 protein binding | IPI PMID:21516116 Next-generation sequencing to generate interactome datasets. | MODIFY | Summary: The verified TRIM41 pair supports E3-ligase binding at two-hybrid scope. Reason: BioGRID interaction 1438345 identifies human CHD2 bait and TRIM41 prey in the PMID:21516116 two-hybrid screen. The official TRIM41 record establishes an E3 ubiquitin-protein ligase with experimentally supported catalytic annotation. GO:0031625 describes binding to that partner class, not ubiquitin transfer by CHD2. The exact tested isoform and pair-specific orthogonal mammalian validation remain unverified. This refinement carries the same screen-level evidence as the generic assertion; no native ubiquitination-regulatory mechanism or ligase activity of CHD2 is inferred. Proposed replacements: ubiquitin protein ligase binding |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | KEEP AS NON CORE | Summary: Retain the exact CHD2–BEND7 screen association. Reason: Positive records intact:EBI-10589158, intact:EBI-10181192, intact:EBI-10339223 match human CHD2 O14647 and Q8N7W2-2 in array, pooling and validated yeast two-hybrid stages of PMID:25416956. The curated partner feature is sufficient binding region:10-374. These stages belong to one study, not independent physiological replications. Retain the association at the tested product/fragment scope under the project binding instruction; the screen does not establish a native regulatory mechanism or transfer the partner's activity to CHD2. Supported generic binding remains non-core under the standing ClinGen project instruction; no more informative activity is inferred solely from the partner name. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | MODIFY | Summary: Refine the exact TRIM41 association to E3-ligase binding with its fragment limit. Reason: Positive IntAct EBI-10181204, EBI-10339235 and EBI-10500882 match human CHD2 and TRIM41 Q8WV44 in the array, pooling and validated two-hybrid stages of PMID:25416956. The array record specifies sufficient binding region 86–630; the authentic parent TRIM41 is an E3 ligase, but this region excludes its RING segment 20–61. Binding to a noncatalytic portion can support a protein-class binding annotation without requiring contact with the catalytic domain. It does not show that the assayed fragment itself retains E3 catalysis. GO:0031625 is therefore applied at the preserved interaction/construct scope only; related screen stages are not independent physiological replications, and no native ubiquitination mechanism or activity transfer to CHD2 is claimed. Proposed replacements: ubiquitin protein ligase binding |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | KEEP AS NON CORE | Summary: Retain the exact CHD2–TEKT1 screen association. Reason: Positive records intact:EBI-10181216, intact:EBI-10339247, intact:EBI-10500892 match human CHD2 O14647 and Q969V4 in array, pooling and validated yeast two-hybrid stages of PMID:25416956. No partner residue-range feature occurs in these exact records. These stages belong to one study, not independent physiological replications. Retain the association at the tested product/fragment scope under the project binding instruction; the screen does not establish a native regulatory mechanism or transfer the partner's activity to CHD2. Supported generic binding remains non-core under the standing ClinGen project instruction; no more informative activity is inferred solely from the partner name. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | MODIFY | Summary: The exact THAP1 association supports DNA-binding transcription factor binding at screen scope. Reason: Three positive IntAct records match human CHD2 and THAP1 Q9NVV9 in the array, pooling and validated yeast two-hybrid stages of PMID:25416956. Official partner annotation identifies THAP1 as a sequence-specific DNA-binding transcription regulator. The verified GO:0140297 definition therefore supports this partner-class refinement. It does not require a measured transcriptional consequence of CHD2 binding. All stages belong to one screen, not independent physiological replication; no stronger native mechanism, transcriptional activity transfer or new core is inferred. Proposed replacements: DNA-binding transcription factor binding |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | MODIFY | Summary: Refine the MID2 isoform-2 association to E3-ligase binding at screen scope. Reason: Positive IntAct EBI-10181236, EBI-10339267 and EBI-10500912 match CHD2 and MID2 Q9UJV3-2 in the three related yeast two-hybrid stages of PMID:25416956. Official MID2 is an E3 ubiquitin-protein ligase. Exact VSP_009009 reconstruction removes canonical residues 450–479 to form the 705-residue isoform 2; its RING segment 30–80 is retained and lies within the recorded sufficient binding region 21–705. This supports GO:0031625 at partner-class binding scope. It does not establish a catalytic assay of the tested isoform/fusion, native colocalization, CHD2 ubiquitination or transfer of MID2 activity to CHD2. Proposed replacements: ubiquitin protein ligase binding |
| GO:0005515 protein binding | IPI PMID:29153328 TDP-43 Promotes Neurodegeneration by Impairing Chromatin Rem... | KEEP AS NON CORE | Summary: Human endogenous CHD2 associates with TDP-43. Reason: The genuine full primary Results report selective CHD2 recovery with endogenous TDP-43 and reciprocal endogenous CHD2 immunoprecipitation in HEK293 cells, with IgG and beta-tubulin controls. RNase treatment also increased nonspecific association, so it is not used to assert a purified or RNA-independent binary interface. The paper's Drosophila Chd1 functional experiments are distinguished from this human CHD2 association. Supported generic binding remains non-core under the standing ClinGen project instruction; no more informative activity is inferred solely from the partner name. |
| GO:0005524 ATP binding | IEA GO_REF:0000002 | ACCEPT | Summary: ATP binding is integral to the CHD2 remodeling motor. Reason: The conserved SNF2-related domain mapping is corroborated by purified human ATP hydrolysis and ATP-dependent nucleosome assembly/remodeling. Active-site mutants and nonhydrolysable-nucleotide controls distinguish motor function from a generic family-name inference. Supporting Evidence: |
| GO:0005634 nucleus | IBA GO_REF:0000033 | ACCEPT | Summary: CHD2 has an established nuclear chromatin-remodeling role. Reason: Human CHD2 is recruited to nuclear chromatin and DNA-damage tracks, and human developmental chromatin profiling independently confirms genomic occupancy. Mouse Chd2 nuclear localization is directly reported in PMID:22569126. These target data support the preserved IBA localization; no exclusive localization of all three products is inferred. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN002473914 SUPPORTS TRANSFER The actual curated PAINT assertion at PANTHER:PTN002473914 is accepted as the transfer basis, with human nuclear chromatin occupancy and DNA-damage recruitment (PMID:36115870; PMID:26895424) corroborating the target capability. This is qualified deference to the curated phylogenetic judgment, not independent reconstruction or validation of its historical IBD placement. Current target evidence alone does not establish that placement; neither donor count nor target self-reference is treated as a defect. Supporting Evidence: file:human/CHD2/CHD2-source-evidence.json |
| GO:0005634 nucleus | IEA GO_REF:0000120 | ACCEPT | Summary: CHD2 has an established nuclear chromatin-remodeling role. Reason: Human CHD2 is recruited to nuclear chromatin and DNA-damage tracks, and human developmental chromatin profiling independently confirms genomic occupancy. Mouse Chd2 nuclear localization is directly reported in PMID:22569126. These target data support the preserved IEA localization; no exclusive localization of all three products is inferred. Supporting Evidence: file:human/CHD2/CHD2-source-evidence.json |
| GO:0005634 nucleus | ISS GO_REF:0000024 | ACCEPT | Summary: CHD2 has an established nuclear chromatin-remodeling role. Reason: Human CHD2 is recruited to nuclear chromatin and DNA-damage tracks, and human developmental chromatin profiling independently confirms genomic occupancy. Mouse Chd2 nuclear localization is directly reported in PMID:22569126. These target data support the preserved ISS localization; no exclusive localization of all three products is inferred. Supporting Evidence: file:human/CHD2/CHD2-source-evidence.json |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9943412 | KEEP AS NON CORE | Summary: Retain the curated nucleoplasmic reaction context. Reason: The official Reactome event places the CHD1/CHD2 set in nucleoplasm during modeled nucleosome binding. Human-cell experiments also recover a soluble nuclear CHD2 pool. The shared event is a curated context, not an independent direct compartment assay or evidence that every cited CHD1-specific mechanism applies to CHD2. The defining active location in the core is nuclear chromatin. |
| GO:0006338 chromatin remodeling | IEA GO_REF:0000117 | ACCEPT | Summary: CHD2 directly performs chromatin remodeling. Reason: Purified human CHD2 hydrolyses ATP and changes nucleosomal DNA accessibility, with inactive motor controls. Human-cell tethering and damage experiments additionally show ATPase-dependent chromatin expansion. This is performed remodeling, not solely a downstream perturbation phenotype. |
| GO:0007517 muscle organ development | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Retain the developmental role at its experimentally supported mouse scope. Reason: The exact mouse donor has IMP evidence from C2C12 myogenesis. Chd2 depletion disrupts myogenic gene activation and myotube formation, with rescue by full-length Chd2; MyoD-dependent recruitment and H3.3 deposition provide an actual chromatin contribution. Retain the existing human orthology-based muscle-development assertion as context, while distinguishing these mouse-cell experiments from a direct human muscle-organ assay. Supporting Evidence: PMID:22569126 restored MHC expression and myotube formation file:human/CHD2/CHD2-source-evidence.json |
| GO:0007517 muscle organ development | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Retain the developmental role at its experimentally supported mouse scope. Reason: The exact mouse donor has IMP evidence from C2C12 myogenesis. Chd2 depletion disrupts myogenic gene activation and myotube formation, with rescue by full-length Chd2; MyoD-dependent recruitment and H3.3 deposition provide an actual chromatin contribution. Retain the existing human orthology-based muscle-development assertion as context, while distinguishing these mouse-cell experiments from a direct human muscle-organ assay. |
| GO:0010467 gene expression | IEA GO_REF:0000107 | MODIFY | Summary: Refine broad gene expression to transcription regulation, with the donor citation defect explicit. Reason: The mouse donor E9PZM4 has a current IMP GO:0010467 record citing PMID:27783602. Its actual Table S1 row 28 and Supplementary Note S5 page 8 test linc2025 promoter deletion and measure neighboring Chd2 RNA; they do not perturb CHD2 protein or establish its gene-expression function. This is a source-citation role problem, not a wrong ortholog or failed similarity transfer. Independently, mouse MyoD-dependent CHD2 recruitment/H3.3 incorporation and human CHD2 promoter occupancy, loss-of-function expression changes and FOSL1-dependent recruitment establish its performed chromatin contribution to transcription regulation (PMID:22569126; PMID:36115870; PMID:38767413). GO:0006357 captures that supported RNA-polymerase-II transcriptional context more precisely than general gene-product production. These studies do not make CHD2 an RNA polymerase, direct DNA-motif recognizer or histone writer. Propagation Review Root cause: SOURCE BAD Failure modes: ROLE CONFLATION Sources checked: UniProtKB:E9PZM4 · Chd2 SOURCE BAD The actual current mouse IMP annotation cites PMID:27783602, whose inspected original Table S1 row 28 and Note S5 page 8 identify Chd2 as a neighboring transcript readout after linc2025 promoter deletion. This citation does not establish CHD2 protein function. Independent mouse and human CHD2 protein experiments support the replacement; the source-citation defect is not evidence against orthology. Proposed replacements: regulation of transcription by RNA polymerase II Supporting Evidence: PMID:38767413 helps recruit CHD2 to gene regulatory elements file:human/CHD2/CHD2-source-evidence.json |
| GO:0016887 ATP hydrolysis activity | IBA GO_REF:0000033 | ACCEPT | Summary: CHD2 directly hydrolyses ATP to power its remodeling activity. Reason: Purified human CHD2 releases phosphate from ATP; DNA and chromatin stimulate this activity, and the D617A/E618A motor mutant is inactive. This target-specific assay independently supports the preserved IBA assertion. The donor CHD3 in the ISS record is not substituted for CHD2, and ATP hydrolysis is represented within the remodeling core rather than as a second unrelated core. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN002473914 SUPPORTS TRANSFER The actual curated PAINT assertion at PANTHER:PTN002473914 is accepted as the transfer basis, with purified human ATP hydrolysis with motor-mutant controls (PMID:25384982) corroborating the target capability. This is qualified deference to the curated phylogenetic judgment, not independent reconstruction or validation of its historical IBD placement. Current target evidence alone does not establish that placement; neither donor count nor target self-reference is treated as a defect. |
| GO:0016887 ATP hydrolysis activity | IEA GO_REF:0000116 | ACCEPT | Summary: CHD2 directly hydrolyses ATP to power its remodeling activity. Reason: Purified human CHD2 releases phosphate from ATP; DNA and chromatin stimulate this activity, and the D617A/E618A motor mutant is inactive. This target-specific assay independently supports the preserved IEA assertion. The donor CHD3 in the ISS record is not substituted for CHD2, and ATP hydrolysis is represented within the remodeling core rather than as a second unrelated core. |
| GO:0016887 ATP hydrolysis activity | ISS GO_REF:0000024 | ACCEPT | Summary: CHD2 directly hydrolyses ATP to power its remodeling activity. Reason: Purified human CHD2 releases phosphate from ATP; DNA and chromatin stimulate this activity, and the D617A/E618A motor mutant is inactive. This target-specific assay independently supports the preserved ISS assertion. The donor CHD3 in the ISS record is not substituted for CHD2, and ATP hydrolysis is represented within the remodeling core rather than as a second unrelated core. |
| GO:0034728 nucleosome organization | IBA GO_REF:0000033 | ACCEPT | Summary: CHD2 performs nucleosome organization. Reason: Purified human CHD2, NAP1, histones, DNA and ATP assemble periodic nucleosome arrays, whereas motor-mutant and nonhydrolysable-nucleotide controls do not. The motor contributes to nucleosome organization itself. Human-cell H3.3-deposition results provide additional context without claiming that CHD2 is an autonomous histone chaperone. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN001326511 SUPPORTS TRANSFER The actual curated PAINT assertion at PANTHER:PTN001326511 is accepted as the transfer basis, with purified human CHD2-dependent nucleosome-array assembly with NAP1, histones and ATP (PMID:25384982) corroborating the target capability. This is qualified deference to the curated phylogenetic judgment, not independent reconstruction or validation of its historical IBD placement. Current target evidence alone does not establish that placement; neither donor count nor target self-reference is treated as a defect. |
| GO:0042393 histone binding | IBA GO_REF:0000033 | ACCEPT | Summary: Histone association is a supported substrate-recognition component of CHD2 remodeling. Reason: Mouse Chd2 co-immunoprecipitates with H3.3 and shows proximity/localization evidence in myogenic cells; chromodomain deletion compromises association. Human CHD2–H3.3 co-immunoprecipitation and nucleosome remodeling independently corroborate the general histone-binding capability. This does not establish an isolated binary interface, universal methyl-mark specificity, or intrinsic histone-modification catalysis. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN002473914 SUPPORTS TRANSFER The actual curated PAINT assertion at PANTHER:PTN002473914 is accepted as the transfer basis, with mouse Chd2–H3.3 association and independent human CHD2–H3.3 recovery (PMID:22569126; PMID:26895424) corroborating the target capability. This is qualified deference to the curated phylogenetic judgment, not independent reconstruction or validation of its historical IBD placement. Current target evidence alone does not establish that placement; neither donor count nor target self-reference is treated as a defect. Supporting Evidence: file:human/CHD2/CHD2-source-evidence.json |
| GO:0042393 histone binding | IEA GO_REF:0000107 | ACCEPT | Summary: Histone association is a supported substrate-recognition component of CHD2 remodeling. Reason: Mouse Chd2 co-immunoprecipitates with H3.3 and shows proximity/localization evidence in myogenic cells; chromodomain deletion compromises association. Human CHD2–H3.3 co-immunoprecipitation and nucleosome remodeling independently corroborate the general histone-binding capability. This does not establish an isolated binary interface, universal methyl-mark specificity, or intrinsic histone-modification catalysis. Supporting Evidence: file:human/CHD2/CHD2-source-evidence.json |
| GO:0042393 histone binding | ISS GO_REF:0000024 | ACCEPT | Summary: Histone association is a supported substrate-recognition component of CHD2 remodeling. Reason: Mouse Chd2 co-immunoprecipitates with H3.3 and shows proximity/localization evidence in myogenic cells; chromodomain deletion compromises association. Human CHD2–H3.3 co-immunoprecipitation and nucleosome remodeling independently corroborate the general histone-binding capability. This does not establish an isolated binary interface, universal methyl-mark specificity, or intrinsic histone-modification catalysis. Supporting Evidence: file:human/CHD2/CHD2-source-evidence.json |
| GO:0140658 ATP-dependent chromatin remodeler activity | IBA GO_REF:0000033 | ACCEPT | Summary: ATP-dependent chromatin remodeler activity is the defining CHD2 molecular function. Reason: Defined biochemical reconstitution with purified human CHD2 demonstrates ATP-dependent nucleosome assembly and remodeling. ATPase-mutant controls, nucleosomal accessibility and chromatin-expansion assays connect hydrolysis to histone–DNA reorganization, matching the verified GO definition. No intrinsic duplex-unwinding or histone writer/eraser activity is inferred from the protein name or downstream chromatin marks. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN002473914 SUPPORTS TRANSFER The actual curated PAINT assertion at PANTHER:PTN002473914 is accepted as the transfer basis, with purified human ATP-dependent remodeling plus motor-dependent cellular chromatin expansion (PMID:25384982; PMID:26895424) corroborating the target capability. This is qualified deference to the curated phylogenetic judgment, not independent reconstruction or validation of its historical IBD placement. Current target evidence alone does not establish that placement; neither donor count nor target self-reference is treated as a defect. Supporting Evidence: PMID:25384982 CHD2 catalyzes the efficient ATP-dependent assembly file:human/CHD2/CHD2-source-evidence.json |
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Download this section (compressed HTML)Q: Which RNA species contact endogenous CHD2, and do those contacts alter its chromatin remodeling rather than simply accompany poly(A)-RNA capture?
Q: How do the three human CHD2 products differ in motor activity, chromatin recruitment and RNA association under endogenous expression?
Q: Does CHD2 recognize any DNA sequence independently of recruiting transcription factors, or do DNA length/structure and partner recruitment explain its genomic specificity?
Q: During H3.3 assembly at DNA breaks and developmental genes, which histone chaperones cooperate with CHD2 and which physical step does its motor perform?
Q: Should CHD2 motor-dependent chromatin expansion and KU/XRCC4 recruitment at double-strand breaks be annotated directly to nonhomologous end joining or to its regulation? The actual human mechanism exceeds a necessity-only phenotype, but the small human remodeler comparator set does not resolve the annotation convention for this preparatory chromatin step.
Experiment: Compare sequence-verified human CHD2 products in purified ATPase, nucleosome-remodeling and DNA-sequence/shape panels, retaining motor-mutant and histone-chaperone controls.
Experiment: Map endogenous CHD2 RNA contacts with orthogonal crosslinking assays and test separation-of-function mutants for RNA binding, factor recruitment and chromatin remodeling without changing protein abundance.
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