BPTF is a large chromatin-recognition subunit of nuclear NURF complexes. Its C-terminal PHD finger recognizes H3K4me3, and the adjacent bromodomain recognizes acetylated H4, including H4K16ac in a coupled nucleosome-recognition mechanism. These contacts help recruit or stabilize NURF at regulatory chromatin. NURF can contain either SMARCA1/SNF2L or SMARCA5/SNF2H as its ATP-hydrolyzing motor; complex activity depends on the motor and its splice form. BPTF supplies histone recognition and regulatory interactions that support transcription at developmental and differentiation-associated loci. Historical FAC1 constructs also display sequence-specific DNA binding, transcriptional repression and regulated nuclear/cytoplasmic localization. Alternative splicing alters internal regions of BPTF.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0000122 negative regulation of transcription by RNA polymerase II | IDA PMID:10727212 Fetal Alz-50 clone 1 (FAC1) protein interacts with the Myc-a... | KEEP AS NON CORE | Summary: FAC1 represses MAZ-dependent reporter activation in the tested cell context. Reason: The cached primary abstract describes recombinant FAC1–MAZ association and dose-dependent inhibition of MAZ-driven SV40 reporter activation; an interaction-defective FAC1 mutant lacks this effect. This supports the existing negative-regulation assertion, retained as a context-specific activity. The legacy FAC1 construct is not assigned to a current numbered BPTF product, and the result does not make transcriptional repression the universal action of full-length NURF. Supporting Evidence: PMID:10727212 Cotransfection with FAC1 reduces the level of ZF87/MAZ-induced activation of the SV40 promoter in a dose dependent manner. |
| GO:0000785 chromatin | IDA PMID:27141965 Setd1a and NURF mediate chromatin dynamics and gene regulati... | ACCEPT | Summary: BPTF occupies chromatin at regulated promoters. Reason: The primary study includes BPTF ChIP and sequential ChIP in human erythroid cells, supporting chromatin association. This is consistent with direct histone recognition and NURF function. The Setd1a conditional-knockout phenotype in the same paper is not attributed to a Bptf knockout or to BPTF histone methyltransferase activity. Supporting Evidence: PMID:27141965 USF1, BPTF, a component of the NURF complex and SETD1A co-occupied the promoters of active erythroid genes |
| GO:0005515 protein binding | IPI PMID:14609955 Isolation of human NURF: a regulator of Engrailed gene expre... | KEEP AS NON CORE | Summary: BPTF associates with the SMARCA1/SNF2L-containing human NURF complex. Reason: PMID:14609955 reports purification of human SNF2L-containing NURF. Its saved official PubMed Figure 2 and 3 captions identify BPTF in endogenous and Flag-BPTF immunoprecipitation/purification material containing SNF2L. This supports the curated association with UniProtKB:P28370 in its complex context; these inspected passages do not establish a purified binary interaction. Retain this supported complex association as non-core; the task-specific binding instruction and its publication link are recorded in the notes. The mechanistic reader and complex-level remodeling functions are represented separately; do not infer autonomous ATP hydrolysis from association. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:14609955 Isolation of human NURF: a regulator of Engrailed gene expre... | KEEP AS NON CORE | Summary: BPTF associates with the RBBP4/RbAp48-containing human NURF complex. Reason: The IPI source names UniProtKB:Q09028. PMID:14609955 and the saved official Figure 3 caption report Flag-BPTF purification with SNF2L, RbAP48 and RbAP46, confirmed by western analysis; the curated Q09028 partner is RBBP4. This supports NURF co-association without proving that every pair contacts directly. Keep this supported interaction as non-core, preserving its original partner and reference; the task-specific instruction is recorded in the notes. A specific catalytic or adaptor activity cannot be assigned from this interaction alone. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:15640247 CECR2, a protein involved in neurulation, forms a novel chro... | KEEP AS NON CORE | Summary: BPTF association with SMARCA1/SNF2L is supported by human NURF isolation. Reason: Human NURF purification and BPTF immunoprecipitation in PMID:14609955 directly support association with the same P28370 partner. Retain the curated pairwise interaction as non-core with that independent corroboration and curator deference. The particular BPTF assay in the CERF comparison remains uninspected; its score, controls and direct-binary interpretation are not certified. No more specific catalytic, chaperone or adaptor function follows from this protein pair alone. |
| GO:0005515 protein binding | IPI PMID:21596426 Recognition of a mononucleosomal histone modification patter... | MODIFY | Summary: The BPTF bromodomain reads H4K16ac in a coupled histone-recognition mechanism. Reason: The 2011 study measures direct acetyl-H4 recognition and enhanced binding of the PHD–bromodomain module to H3K4me3/H4K16ac mononucleosomes. Reader-pocket and linker mutations reduce full-length BPTF recruitment at HOXA9. This supports histone H4K16ac reader activity for the original H4 partner P62805. The isolated bromodomain also binds other acetyl-H4 peptides; the nucleosome preference is not universal mark exclusivity. H3K4me3 recognition is a separately supported PHD activity in the core synthesis, not an added H3 assertion on this H4 source object. Proposed replacements: histone H4K16ac reader activity Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:22729083 Diverse epigenetic strategies interact to control epidermal ... | KEEP AS NON CORE | Summary: BPTF associates with SMARCA5/SNF2H in endogenous cellular complexes. Reason: Endogenous SMARCA5 immunoprecipitation and reciprocal BPTF antibody precipitation in PMID:28801535 support cellular association with the same O60264 partner. UniProt calls the BPTF–SMARCA5 complex NURF-5. Retain this association as non-core with independent corroboration and curator deference; the original target-level assay in the epidermal differentiation study remains uninspected. The 2017 recombinant panel explicitly excludes BPTF, so its direct-interaction, ATPase and nucleosome-sliding results do not establish a reconstituted BPTF complex. Supporting Evidence: file:human/BPTF/BPTF-uniprot.txt PMID:28801535 precipitation with antibodies against the regulatory subunits BAZ1A, BPTF, or CECR2 enriched both ATPases |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | KEEP AS NON CORE | Summary: BPTF associates with SMARCA5/SNF2H in endogenous cellular complexes. Reason: Endogenous SMARCA5 immunoprecipitation and reciprocal BPTF antibody precipitation in PMID:28801535 support cellular association with the same O60264 partner. UniProt calls the BPTF–SMARCA5 complex NURF-5. Retain this association as non-core with independent corroboration and curator deference; the original target-level assay in the OpenCell screen remains uninspected. The 2017 recombinant panel explicitly excludes BPTF, so its direct-interaction, ATPase and nucleosome-sliding results do not establish a reconstituted BPTF complex. |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | KEEP AS NON CORE | Summary: BPTF association with SMARCA1/SNF2L is supported by human NURF isolation. Reason: Human NURF purification and BPTF immunoprecipitation in PMID:14609955 directly support association with the same P28370 partner. Retain the curated pairwise interaction as non-core with that independent corroboration and curator deference. The particular BPTF assay in the OpenCell screen remains uninspected; its score, controls and direct-binary interpretation are not certified. No more specific catalytic, chaperone or adaptor function follows from this protein pair alone. |
| GO:0005634 nucleus | EXP PMID:10727212 Fetal Alz-50 clone 1 (FAC1) protein interacts with the Myc-a... | ACCEPT | Summary: Nuclear localization is consistent with FAC1–MAZ transcriptional regulation. Reason: The primary abstract reports the FAC1–MAZ interaction, nuclear localization/export regions and transcriptional reporter effects. Nuclear function is independently supported by BPTF chromatin occupancy and NURF purification. Retain the experimental curator assertion without assigning the legacy FAC1 experiment to a specific current product. Supporting Evidence: |
| GO:0005634 nucleus | EXP PMID:9225734 FAC1 expression and localization in motor neurons of develop... | ACCEPT | Summary: FAC1 is detected in motor-neuron nuclei in developmental and disease contexts. Reason: The cached abstract explicitly reports predominant nuclear and cell-body localization during spinal-cord development and nuclear/cytoplasmic staining in surviving ALS motor neurons. Nuclear localization is a core location of BPTF, although its distribution varies with tissue and state. These observations do not establish that BPTF causes ALS or identify the numbered product detected by the historical antibody. Supporting Evidence: PMID:9225734 FAC1 protein was localized predominately in nuclei and the cell body of motor neurons during early stages of spinal cord development. |
| GO:0005634 nucleus | IDA PMID:10403843 DNA binding activity of the fetal Alz-50 clone 1 (FAC1) prot... | ACCEPT | Summary: Nuclear FAC1 DNA-binding activity supports the nuclear location. Reason: The cached primary abstract describes neuroblastoma nuclear extracts and phosphorylation-sensitive FAC1 DNA binding. Nuclear localization also agrees with direct BPTF chromatin/NURF evidence. Retain the source assertion without equating the historical FAC1 reagent with every current BPTF isoform. Supporting Evidence: |
| GO:0005634 nucleus | IDA PMID:14609955 Isolation of human NURF: a regulator of Engrailed gene expre... | ACCEPT | Summary: Human BPTF-containing NURF is recovered from nuclear material. Reason: The human NURF study identifies BPTF in a nuclear chromatin-remodeling complex. Official primary figure captions additionally identify HEK293 nuclear preparations and tagged-BPTF purification. The canonical cache is abstract-only; the supplemental caption reading is documented in the notes, not inserted into the cache. Supporting Evidence: |
| GO:0005634 nucleus | IDA PMID:25593309 Screen identifies bromodomain protein ZMYND8 in chromatin re... | ACCEPT | Summary: BPTF is nuclear and can accumulate at DNA-damage sites. Reason: The longer authenticated supplemental source Results explicitly include BPTF among bromodomain proteins recruited to DNA damage. This supports the nuclear-location assertion despite the title foregrounding ZMYND8. The existing canonical cache remains abstract-only; no supplemental passage is quoted as canonical support and no ZMYND8-specific repair mechanism is transferred to BPTF. Supporting Evidence: |
| GO:0005634 nucleus | IEA GO_REF:0000044 | ACCEPT | Summary: The electronic nuclear-location mapping agrees with direct BPTF evidence. Reason: The UniProt nuclear-location mapping is corroborated by nuclear NURF isolation and human BPTF chromatin occupancy. Retain the source mapping as a core location; its evidence code and source accession remain unchanged. |
| GO:0005634 nucleus | NAS PMID:14609955 Isolation of human NURF: a regulator of Engrailed gene expre... | ACCEPT | Summary: The NURF study supports BPTF nuclear localization. Reason: The source describes human NURF and primary captions identify its isolation from nuclear material with BPTF as a subunit. Nuclear localization is independently consistent with BPTF histone recognition and chromatin occupancy. The NAS source assertion is retained without upgrading its evidence code. Supporting Evidence: |
| GO:0005654 nucleoplasm | IDA GO_REF:0000052 | ACCEPT | Summary: Nucleoplasmic localization is consistent with BPTF chromatin function. Reason: Retain the curated immunofluorescence location in light of independent nuclear/chromatin evidence. The source image was not independently reanalyzed, so no cell-line distribution or isoform specificity is asserted. BPTF functions in nuclear chromatin-remodeling complexes. |
| GO:0005737 cytoplasm | EXP PMID:15379550 Fetal Alz-50 clone 1 interacts with the human orthologue of ... | KEEP AS NON CORE | Summary: FAC1 has a demonstrated cytoplasmic pool associated with KEAP1. Reason: The cached abstract explicitly reports FAC1 colocalization with endogenous KEAP1 in the cytoplasm of PT67 cells and redistribution with an introduced KEAP1 fusion. Retain this experimentally supported, context-dependent location outside the dominant nuclear chromatin function. The historical FAC1 construct is not assigned to a current numbered product. Supporting Evidence: PMID:15379550 FAC1 colocalizes with endogenous Keap1 within the cytoplasm of PT67 cells. |
| GO:0005737 cytoplasm | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: Cytoplasmic localization is supported in developmental and FAC1 interaction contexts. Reason: The electronic UniProt location mapping is consistent with primary FAC1 cytoplasmic staining and KEAP1 colocalization. Retain the biologically supported secondary location without making it the principal site of NURF action or asserting that all BPTF products share the same distribution. |
| GO:0005737 cytoplasm | TAS PMID:7621746 FAC1, a novel gene identified with the monoclonal antibody A... | KEEP AS NON CORE | Summary: The developmental FAC1 study reports cytoplasmic localization in human fetal brain. Reason: The abstract explicitly describes nuclear and cytoplasmic FAC1 staining throughout developing cortex, with predominantly nuclear staining in adult neocortex. This supports a context-specific cytoplasmic location. It is an observation of localization and expression, not a mechanism of neuronal development. Supporting Evidence: PMID:7621746 the protein is located both in the nucleus and the cytoplasm of cells throughout the developing cortex. |
| GO:0005829 cytosol | IDA GO_REF:0000052 | KEEP AS NON CORE | Summary: A cytosolic pool is retained as a secondary localization. Reason: Retain the curated immunofluorescence assertion in the context of independent cytoplasmic FAC1 evidence. The underlying image was not independently examined; the review does not infer a soluble enzymatic role, cell-line pattern or product specificity from this location alone. |
| GO:0006338 chromatin remodeling | IDA PMID:14609955 Isolation of human NURF: a regulator of Engrailed gene expre... | ACCEPT | Summary: BPTF contributes directly to NURF chromatin remodeling as a regulatory subunit. Reason: BPTF is a component of purified human NURF, whose ATP-dependent remodeling is measured at the complex level. Its histone-recognition module supplies a direct chromatin-targeting contribution to remodeling. BPTF is not itself established as the ATP-hydrolyzing motor; that distinction does not negate its participation in the remodeling process. |
| GO:0006338 chromatin remodeling | IEA GO_REF:0000117 | ACCEPT | Summary: The electronic chromatin-remodeling assertion agrees with NURF biology. Reason: Human NURF purification and BPTF histone-recognition experiments independently support direct participation in chromatin remodeling. Retain the ARBA-derived process assertion without representing the rule as experimental evidence or assigning intrinsic ATPase catalysis to BPTF. |
| GO:0006355 regulation of DNA-templated transcription | IDA PMID:14609955 Isolation of human NURF: a regulator of Engrailed gene expre... | ACCEPT | Summary: BPTF-containing NURF regulates transcription through chromatin remodeling. Reason: The human NURF study links the BPTF-containing complex to Engrailed expression; official figure captions separately describe BPTF depletion and promoter occupancy. Chromatin targeting and remodeling provide a direct regulatory role. This is transcriptional regulation by a chromatin complex, not RNA synthesis catalysis by BPTF. Supporting Evidence: |
| GO:0006357 regulation of transcription by RNA polymerase II | IBA GO_REF:0000033 | ACCEPT | Summary: The phylogenetic assertion of RNA polymerase II transcriptional regulation is coherent with human BPTF function. Reason: Human BPTF/NURF promoter occupancy and transcriptional effects support this conserved regulatory role. The PAINT assertion is a phylogenetic judgment; the target's appearance among descendant evidence is expected and is not circularity. No independent reconstruction of the IBD node or alignment is claimed. |
| GO:0006357 regulation of transcription by RNA polymerase II | IEA GO_REF:0000002 | ACCEPT | Summary: The InterPro transcription-regulation mapping matches BPTF's chromatin role. Reason: The domain/family-derived assertion is corroborated by human NURF and BPTF promoter experiments. Retain the broad RNA polymerase II regulatory function without inferring that a domain match alone proves a particular target gene or direction of regulation. |
| GO:0006357 regulation of transcription by RNA polymerase II | IMP PMID:10575013 Fetal Alz-50 clone 1, a novel zinc finger protein, binds a s... | KEEP AS NON CORE | Summary: Legacy FAC1 DNA binding can repress a sequence-containing transcriptional reporter. Reason: The primary abstract reports binding-site selection, loss of binding on site mutation, and repression of a CACAACAC-containing reporter in NIH3T3 cells. This supports the existing regulatory assertion in that assay context. The historical FAC1 construct is not equated with a current full-length BPTF product, and its sequence-specific repression is not treated as the defining mechanism of all NURF complexes. Supporting Evidence: |
| GO:0007420 brain development | IMP PMID:14609955 Isolation of human NURF: a regulator of Engrailed gene expre... | KEEP AS NON CORE | Summary: BPTF contributes to developmental gene regulation through NURF. Reason: BPTF-containing NURF occupies Engrailed promoters, and BPTF depletion reduces en-1 expression in the primary study. Reviewed UniProt explicitly connects this NURF function to brain development. Retain the existing broad developmental annotation as a context-dependent role, with curator deference for its process-level interpretation. The directly inspected neurite-outgrowth perturbation is SNF2L, not BPTF; no BPTF-specific neurite or whole-brain phenotype is claimed from that experiment. |
| GO:0007420 brain development | NAS PMID:14609955 Isolation of human NURF: a regulator of Engrailed gene expre... | KEEP AS NON CORE | Summary: BPTF contributes to developmental gene regulation through NURF. Reason: BPTF-containing NURF occupies Engrailed promoters, and BPTF depletion reduces en-1 expression in the primary study. Reviewed UniProt explicitly connects this NURF function to brain development. Retain the existing broad developmental annotation as a context-dependent role, with curator deference for its process-level interpretation. The directly inspected neurite-outgrowth perturbation is SNF2L, not BPTF; no BPTF-specific neurite or whole-brain phenotype is claimed from that experiment. |
| GO:0008094 ATP-dependent activity, acting on DNA | IDA PMID:14609955 Isolation of human NURF: a regulator of Engrailed gene expre... | MODIFY | Summary: BPTF contributes to the ATP-dependent chromatin-remodeling activity of NURF. Reason: The original contributes_to annotation correctly distinguishes complex activity from intrinsic BPTF catalysis. The more specific remodeler term captures the nucleosome remodeling measured for purified human NURF. Histone recognition by BPTF supplies a regulatory chromatin-targeting contribution, whereas the ISWI motor supplies ATP hydrolysis. Preserve the original term and qualifier as source fields and propose only the supported activity refinement. Proposed replacements: ATP-dependent chromatin remodeler activity |
| GO:0016589 NURF complex | IBA GO_REF:0000033 | ACCEPT | Summary: BPTF is a conserved NURF-complex subunit. Reason: Human NURF purification independently establishes BPTF membership and is coherent with the PAINT-derived complex annotation. The PTN and descendant sources are preserved. Target-derived experimental support within the WITH/FROM list is not circular evidence, and no new tree-node analysis is claimed. |
| GO:0016589 NURF complex | IDA PMID:20850016 Quantitative interaction proteomics and genome-wide profilin... | ACCEPT | Summary: NURF membership is biologically established for BPTF. Reason: The source is a quantitative histone-reader/complex-proteomics study; its cached abstract does not expose the exact BPTF target table. Retain the experimental curator assertion because independent human NURF purification directly verifies membership. This is explicit curator deference for the original target-level experiment, not a claim that its full table was inspected. |
| GO:0016589 NURF complex | IEA GO_REF:0000120 | ACCEPT | Summary: The combined electronic NURF mapping agrees with direct human complex isolation. Reason: BPTF membership in NURF is independently supported by the human purification study. Retain the ARBA/InterPro source assertion and its provenance without elevating computational evidence to an experimental code. |
| GO:0016589 NURF complex | IPI PMID:14609955 Isolation of human NURF: a regulator of Engrailed gene expre... | ACCEPT | Summary: Human NURF purification directly identifies BPTF as a subunit. Reason: The source identifies the human SNF2L-containing complex, and official figure captions describe BPTF co-purification with SNF2L and RbAP46/48, including tagged-BPTF purification. These data support complex membership without claiming every subunit pair is a direct binary interaction. Supporting Evidence: PMID:14609955 The subunit composition suggests that it represents the human ortholog of the Drosophila nucleosome-remodeling factor (NURF) complex. |
| GO:0030425 dendrite | IEA GO_REF:0000107 | UNDECIDED | Summary: The precise dendritic localization transferred from the rat source needs donor-level verification. Reason: Human FAC1 studies describe neuronal cell bodies and neurites, but the accessed material does not distinguish the exact dendritic compartment asserted by this Ensembl transfer. The rat accession and original source are preserved without guessing a donor product name or treating unspecified neurites as proven dendrites. This is an unresolved localization boundary, not evidence that dendritic localization is false. Supporting Evidence: GO_REF:0000107 |
| GO:0043565 sequence-specific DNA binding | IDA PMID:10403843 DNA binding activity of the fetal Alz-50 clone 1 (FAC1) prot... | KEEP AS NON CORE | Summary: Historical FAC1 experiments support phosphorylation-regulated sequence-specific DNA binding. Reason: The primary abstract explicitly measures FAC1 affinity for an identified DNA sequence and its dependence on phosphorylation, with phosphatase treatment and inhibition. Retain the experimental DNA-binding assertion in the reported construct context. BPTF is the regulated binding species, not the kinase, and the legacy FAC1 activity is not assigned to every current full-length product. Supporting Evidence: PMID:10403843 the affinity of FAC1 for the identified DNA sequence is dramatically enhanced when FAC1 is phosphorylated. |
| GO:0043565 sequence-specific DNA binding | IMP PMID:10575013 Fetal Alz-50 clone 1, a novel zinc finger protein, binds a s... | KEEP AS NON CORE | Summary: FAC1 binds a selected DNA sequence in the historical construct assay. Reason: The primary abstract describes recombinant binding-site selection, mutational specificity and corresponding extract binding. The separately accessed PubMed caption specifies GST-FAC1 residues 1–398. This directly supports the existing binding assertion while leaving the mapping to current named BPTF products unresolved; it does not replace BPTF's defining histone-reader role. Supporting Evidence: PMID:10575013 Mutation of any 2 adjacent base pairs in the identified binding site dramatically reduced the binding preference of FAC1 |
| GO:0044297 cell body | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Neuronal cell-body localization is supported in human FAC1 studies. Reason: The transferred cell-body assertion is corroborated by explicit FAC1 staining in spinal-cord motor-neuron cell bodies. Retain it as a tissue-dependent secondary location. The original rat accession is not normalized to a guessed human isoform, and the donor-specific experiment has not been independently reconstructed. |
| GO:0045892 negative regulation of DNA-templated transcription | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: Negative transcriptional regulation is supported in FAC1 reporter contexts. Reason: The electronic assertion is consistent with the direct FAC1 binding-site reporter repression and MAZ-dependent repression experiments. Retain that context-specific regulatory direction rather than making repression universal across BPTF/NURF targets or claiming an ARBA rule audit. |
| GO:0045944 positive regulation of transcription by RNA polymerase II | IEA GO_REF:0000117 | ACCEPT | Summary: BPTF-containing NURF can positively regulate RNA polymerase II transcription. Reason: The electronic assertion is consistent with NURF regulation of human Engrailed and the BPTF depletion/promoter experiments described in the original primary captions. BPTF contributes chromatin recognition and remodeling, rather than catalyzing transcription itself. Positive regulation is target/context dependent and coexists with the distinct FAC1 repression observations. |
| GO:0045944 positive regulation of transcription by RNA polymerase II | IMP PMID:14609955 Isolation of human NURF: a regulator of Engrailed gene expre... | ACCEPT | Summary: BPTF depletion reduces Engrailed expression in the human NURF study. Reason: The cached abstract establishes NURF-dependent Engrailed regulation; the separately inspected primary figure captions identify BPTF depletion and promoter occupancy. This supports the positive transcription-regulation assertion for BPTF in that context, without treating the SNF2L neurite assay as a separate BPTF result. Supporting Evidence: |
| GO:0048471 perinuclear region of cytoplasm | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: FAC1 can accumulate in perinuclear cytoplasmic structures in an interaction context. Reason: Human FAC1/KEAP1 experiments explicitly report redistribution into perinuclear spherical structures with introduced KEAP1. This corroborates the transferred compartment as a context-dependent secondary location. It does not prove identical endogenous localization in every tissue or product, and the original rat transfer accession is preserved. |
| GO:0070062 extracellular exosome | HDA PMID:18570454 Proteomic analysis of exosomes from human neural stem cells ... | MARK AS OVER ANNOTATED | Summary: Detected in an extracellular-vesicle proteome, but the detection does not establish that this protein is an EV constituent. Reason: Nuclear chromatin-remodelling subunit. Mainly resident in an intracellular compartment that MISEV2018 (PMID:30637094) lists as not enriched in small EVs of plasma-membrane/endosomal origin (category 4), and its own review keeps no experimental cell-surface or plasma-membrane pool; an exosome annotation from a bulk EV proteome is not supported. (Manual re-review for OMICS_EVIDENCE, 2026-10-10; previous action: UNDECIDED.) Supporting Evidence: |
| GO:1904949 ATPase complex | IDA PMID:14609955 Isolation of human NURF: a regulator of Engrailed gene expre... | ACCEPT | Summary: BPTF belongs to an ATPase-containing chromatin-remodeling complex. Reason: Purified human NURF contains BPTF and an ISWI ATPase and exhibits ATP-dependent remodeling. The ATPase-complex location is therefore correct without assigning ATP hydrolysis to BPTF itself. The more specific NURF membership is separately represented in the existing source annotations and core synthesis. Supporting Evidence: |
| GO:1990090 cellular response to nerve growth factor stimulus | IEA GO_REF:0000107 | UNDECIDED | Summary: The transferred nerve-growth-factor response requires the original donor experiment. Reason: The accessed human sources establish NURF-related transcription and FAC1 developmental localization but do not resolve the specific NGF-response assay behind the rat orthology transfer. Preserve the donor accession and source fields, and leave this process unresolved rather than inferring it from generic neuronal expression or SNF2L-associated neurite outgrowth. Supporting Evidence: GO_REF:0000107 |
| GO:0140002 histone H3K4me3 reader activity | IDA PMID:16728978 Molecular basis for site-specific read-out of histone H3K4me... | NEW | Summary: Human BPTF recognizes H3K4me3 through its bromodomain-proximal PHD finger and couples this recognition to NURF chromatin engagement. Reason: The human BPTF PHD finger is directly assayed in PMID:16728978: the cached abstract reports free and H3K4me3-bound structures, binding measurements and specificity-determining mutations. PMID:16728976 independently links H3K4me3 recognition to BPTF chromatin association and recruitment of the associated NURF motor; its Xenopus developmental phenotype is not the basis for this molecular-function assertion. The full-length recruitment and coupled-domain experiments in PMID:21596426 support the chromatin-adaptor role beyond isolated peptide binding. This is a proposed new assertion, not a previously seeded GOA row. It is distinct from the H4K16ac replacement on the preserved H4-partner row. Wild-type preference for H3K4me3 is not absolute exclusion of H3K4me2, and neither engineered mutant specificity, an unverified present-day isoform assignment nor intrinsic ATPase activity is inferred. Supporting Evidence: PMID:16728978 specific recognition of H3(1-15)K4me3 |
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Download this section (compressed HTML)Q: How do the historical FAC1 constructs and antibody epitopes map to the current BPTF products 1, 2 and 4, and which reported activities extend to each complete product?
Q: What target-specific assays or screen rows establish the BPTF interactions assigned to the CERF comparison, epidermal differentiation study and OpenCell?
Q: Can the original rat donor experiments resolve dendritic localization and the cellular response to nerve growth factor, and can the BPTF exosome peptide record be recovered?
Q: How do histone-tail accessibility, combined modifications and the composition of intact NURF complexes shape the substrate preferences measured with isolated BPTF reader modules?
Q: How do BPTF dosage and the choice of active or inactive ISWI motor variants alter NURF targeting during neurodevelopment, and which biochemical deficits underlie NEDDFL haploinsufficiency?
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