Human ACTB encodes cytoplasmic beta-actin, an ATP-binding protein that assembles into dynamic filaments. Its polymers provide mechanical support and force for cell motility, cell shape, epithelial junctions and membrane remodeling. ATP hydrolysis and phosphate release alter filament turnover, while actin-binding proteins control assembly and coupling to cellular structures. Nuclear beta-actin also participates in chromatin-remodeling and histone-modifying complexes: the ACTBβACTL6 module helps connect the SWI/SNF motor to the rest of the complex. Distinct structural pools occur in dynactin and non-activated gamma-tubulin ring complexes. Pathogenic ACTB variants can disrupt actin dynamics and cause developmental disease.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0015629 actin cytoskeleton | IBA GO_REF:0000033 | ACCEPT | Summary: ACTB supplies the polymeric backbone of the actin cytoskeleton. Reason: The PAINT assertion at PTN002631484 agrees with the target protein forming cytoplasmic filaments. Human biochemical work and epithelial junction experiments independently support this structural location (PMID:25255767; PMID:22855531). Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN002631484 SUPPORTS TRANSFER The actin-cytoskeleton assertion at PTN002631484 agrees with direct target filament and junctional evidence. |
| GO:0045202 synapse | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Beta-actin forms part of the synaptic cytoskeleton. Reason: The inherited synaptic localization is compatible with beta-actin imaging in hippocampal spines (PMID:18341992). Synapse is retained at the ancestral assertionβs resolution as a neuronal context of actin function. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN007551913 SUPPORTS TRANSFER The PTN007551913 synaptic assertion is consistent with beta-actin imaging in hippocampal spines. |
| GO:0005737 cytoplasm | IBA GO_REF:0000033 | ACCEPT | Summary: Cytoplasmic beta-actin forms soluble and filamentous pools. Reason: PTN007551913 supports the broad compartment, which agrees with human cell and purified-protein observations (PMID:22855531; PMID:25255767). More specific locations do not invalidate this organelle-level assertion. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN007551913 SUPPORTS TRANSFER The PTN007551913 cytoplasmic assertion preserves the broad compartment supported by human experiments. |
| GO:0016020 membrane | IBA GO_REF:0000033 | ACCEPT | Summary: ACTB associates with the cytoplasmic face of cellular membranes. Reason: Membrane-associated actin supports cortical and junctional structures; the PAINT assertion does not imply that ACTB spans a lipid bilayer. Human junctional beta-actin localization supports retention (PMID:22855531). Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN007551913 SUPPORTS TRANSFER The PTN007551913 membrane assertion agrees with human cortical and junctional beta-actin. |
| GO:0030424 axon | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Axonal localization is an inherited neuronal context of beta-actin. Reason: The PTN007551913 placement is retained: there is no target-specific evidence of loss of axonal structural function. This neuronal compartment is contextual relative to the broadly used cytoskeletal protein. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN007551913 SUPPORTS TRANSFER The PTN007551913 axonal assertion is retained as an inherited neuronal location; no target-specific loss is established. |
| GO:0098973 structural constituent of postsynaptic actin cytoskeleton | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: ACTB contributes structural material to the postsynaptic actin cytoskeleton. Reason: GO:0098973 specifically describes structural integrity of the postsynaptic actin cytoskeleton. Beta-actin imaging and perturbation in hippocampal spines support that role (PMID:18341992). Its neuronal scope is a reason to mark it contextual, not to replace it with the already represented general cytoskeletal activity. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN002631586 SUPPORTS TRANSFER The PTN002631586 postsynaptic structural assertion is supported by spine beta-actin experiments and retains their specific structural role. |
| GO:0005884 actin filament | IBA GO_REF:0000033 | ACCEPT | Summary: Beta-actin polymerizes into actin filaments. Reason: The PTN002631586 assertion matches direct polymerization and filament biochemistry (PMID:25255767; PMID:29581253). This is the structural product in which actin functions. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN002631586 SUPPORTS TRANSFER The PTN002631586 actin-filament assertion agrees with target polymerization experiments. |
| GO:0007409 axonogenesis | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Actin supplies the dynamic structural machinery for axon formation. Reason: The inherited axonogenesis assertion is compatible with actin contributing polymer structure and protrusive force. Structural participation is actual work in the process, not merely a downstream consequence; the developmental context is retained as non-core. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN007551913 SUPPORTS TRANSFER The PTN007551913 axonogenesis assertion is consistent with inherited filament structure and protrusive work during axonal development. |
| GO:0019901 protein kinase binding | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Actin binds regulatory protein kinases in cytoskeletal contexts. Reason: Specific kinase interactions are represented by CaMKII and DYRK1A studies (PMID:17404223; PMID:24327345). The PAINT node supports a conserved interaction class; it does not assign protein kinase catalysis to ACTB. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN007551913 SUPPORTS TRANSFER The PTN007551913 kinase-binding assertion agrees with the experimentally represented CaMKII/DYRK1A interaction class. |
| GO:0035267 NuA4 histone acetyltransferase complex | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: ACTB is a subunit of the NuA4/TIP60 histone acetyltransferase complex. Reason: The PTN007551913 placement is consistent with human TIP60/NuA4 complex purification (PMID:10966108; PMID:14966270). Complex membership is retained without attributing KAT5 acetyltransferase chemistry to actin. This complex represents a specialized structural pool outside the filament and SWI/SNF core functions synthesized here. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN007551913 SUPPORTS TRANSFER The PTN007551913 NuA4 assertion is corroborated by human complex purification. |
| GO:0048870 cell motility | IBA GO_REF:0000033 | ACCEPT | Summary: ACTB supplies filament structure and polymerization-dependent force for cell motility. Reason: The inherited process agrees with beta-actin mutant and cytochalasin-resistance experiments (PMID:6202424) and cytoplasmic actin polymer dynamics (PMID:29581253). ACTB performs structural work in motility. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN007551913 SUPPORTS TRANSFER The PTN007551913 motility assertion agrees with beta-actin-dependent filament dynamics and human mutant observations. |
| GO:0000166 nucleotide binding | IEA GO_REF:0000043 | ACCEPT | Summary: ACTB binds adenine nucleotides in monomeric and filamentous states. Reason: The UniProt nucleotide-binding keyword supports this broad molecular function. Both ATP- and ADP-bound actin states are biologically relevant, so replacement by ATP binding alone would discard supported scope (PMID:25255767; PMID:3672117). Propagation Review Root cause: NO FAILURE CORE Sources checked: UniProtKB-KW:KW-0547 SUPPORTS TRANSFER The nucleotide-binding keyword agrees with the actin nucleotide pocket; ATP and ADP states are retained. |
| GO:0005524 ATP binding | IEA GO_REF:0000043 | ACCEPT | Summary: ACTB binds ATP at its conserved nucleotide pocket. Reason: The ATP-binding keyword is supported by human beta-actin nucleotide-binding and polymerization studies (PMID:25255767). ATP binding is retained independently of its subsequent hydrolysis. Propagation Review Root cause: NO FAILURE CORE Sources checked: UniProtKB-KW:KW-0067 SUPPORTS TRANSFER ATP binding is a directly supported actin property. |
| GO:0005634 nucleus | IEA GO_REF:0000120 | ACCEPT | Summary: ACTB has a supported nucleus pool. Reason: The combined UniProt/Ensembl localization inference agrees with human nuclear complex and ribonucleoprotein observations (PMID:11687588; PMID:10966108). The existing UniProt citation PMID:29925947 also reports nuclear actin in a DNA-repair context. Retain the source compartment resolution. Propagation Review Root cause: NO FAILURE CORE Sources checked: UniProtKB:P60710 Β· Actb SUPPORTS TRANSFER Mouse Actb is a traced source of the combined localization inference; independent human evidence supports this target compartment. Ensembl:ENSMUSP00000098066 SUPPORTS TRANSFER This mouse protein accession is also present in the combined inference. It is corroborative mapping context, not an independently counted experiment. UniProtKB-SubCell:SL-0191 SUPPORTS TRANSFER The UniProt subcellular-location mapping supports the broad nucleus compartment; no narrower compartment is substituted. |
| GO:0005856 cytoskeleton | IEA GO_REF:0000120 | ACCEPT | Summary: ACTB has a supported cytoskeleton pool. Reason: The combined UniProt/Ensembl localization inference agrees with human cytoskeletal and junctional experiments (PMID:22855531; PMID:6202424). Retain the source compartment resolution. Propagation Review Root cause: NO FAILURE CORE Sources checked: UniProtKB:P60710 Β· Actb SUPPORTS TRANSFER Mouse Actb is a traced source of the combined localization inference; independent human evidence supports this target compartment. Ensembl:ENSMUSP00000098066 SUPPORTS TRANSFER This mouse protein accession is also present in the combined inference. It is corroborative mapping context, not an independently counted experiment. UniProtKB-SubCell:SL-0090 SUPPORTS TRANSFER The UniProt subcellular-location mapping supports the broad cytoskeleton compartment; no narrower compartment is substituted. |
| GO:0016787 hydrolase activity | IEA GO_REF:0000043 | MODIFY | Summary: ACTB hydrolyzes its bound ATP during filament turnover. Reason: The hydrolase keyword captures real chemistry, but ATP hydrolysis activity describes the directly measured reaction more precisely. Human recombinant beta-actin filament turnover was measured separately from actin-stimulated myosin ATPase (PMID:25255767, Figure 4, https://febs.onlinelibrary.wiley.com/doi/10.1111/febs.13068). That human assay is externally accessible but absent from its local abstract. The cached PMID:3672117 abstract independently describes F-actin ATP hydrolysis at the actin-family level; it is not a human ACTB kinetic measurement. Propagation Review Root cause: TERM SCOPING PROBLEM Sources checked: UniProtKB-KW:KW-0378 SUPPORTS TRANSFER The broad hydrolase keyword can be refined to the measured ATP-hydrolysis reaction. Proposed replacements: ATP hydrolysis activity Supporting Evidence: PMID:3672117 The hydrolysis reaction occurs on the F-actin subsequent to the polymerization reaction in two steps |
| GO:0098974 postsynaptic actin cytoskeleton organization | IEA GO_REF:0000108 | KEEP AS NON CORE | Summary: Postsynaptic actin organization follows from ACTBβs structural role in that network. Reason: GO:0098974 includes assembly, arrangement and disassembly of postsynaptic actin filaments and associated proteins. Its inference from structural constituent of postsynaptic actin cytoskeleton is compatible with beta-actin spine dynamics (PMID:18341992); a generic filament-length regulation term would lose the supported postsynaptic context. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: GO:0098973 SUPPORTS TRANSFER The logical inference starts from postsynaptic structural activity; ACTB supplies the polymer material in this network. |
| GO:0005515 protein binding | IPI PMID:11682052 Cingulin interacts with F-actin in vitro. | REMOVE | Summary: The reported interaction provides association evidence but generic protein binding is uninformative. Reason: Cingulin binding was examined with actin pelleting and cross-linking in the junctional-protein study; the accessible evidence does not resolve an additional ACTB-specific regulatory activity. Remove GO:0005515 under the generic-binding policy; this does not reject the reported pair or infer that ACTB is absent from the experimental complex. Supporting Evidence: PMID:11682052 Cingulin interacts with F-actin in vitro. |
| GO:0005515 protein binding | IPI PMID:15047060 Analysis of proteins copurifying with the CD4/lck complex us... | REMOVE | Summary: The reported interaction provides association evidence but generic protein binding is uninformative. Reason: The CD4/lck biochemical preparation establishes an interaction-screen context; the paper does not establish a distinct ACTB molecular function from the generic association. Remove GO:0005515 under the generic-binding policy; this does not reject the reported pair or infer that ACTB is absent from the experimental complex. Supporting Evidence: PMID:15047060 Analysis of proteins copurifying with the CD4/lck complex using one-dimensional polyacrylamide gel electrophoresis and mass spectrometry: comparison with affinity-tag based protein detection and evaluation of different solubilization methods. |
| GO:0005515 protein binding | IPI PMID:15161933 Comprehensive proteomic analysis of interphase and mitotic 1... | REMOVE | Summary: The reported interaction provides association evidence but generic protein binding is uninformative. Reason: The study surveys proteins associated with 14-3-3; an association in this signaling network does not identify a specific actin effector activity. Remove GO:0005515 under the generic-binding policy; this does not reject the reported pair or infer that ACTB is absent from the experimental complex. Supporting Evidence: PMID:15161933 Comprehensive proteomic analysis of interphase and mitotic 14-3-3-binding proteins. |
| GO:0005515 protein binding | IPI PMID:15328537 Emerin caps the pointed end of actin filaments: evidence for... | REMOVE | Summary: The reported interaction provides association evidence but generic protein binding is uninformative. Reason: The emerin study concerns attachment to actin and nuclear mechanical structure; actinβs general binding label adds no specific activity beyond its structural roles. Remove GO:0005515 under the generic-binding policy; this does not reject the reported pair or infer that ACTB is absent from the experimental complex. Supporting Evidence: PMID:15328537 Emerin caps the pointed end of actin filaments: evidence for an actin cortical network at the nuclear inner membrane. |
| GO:0005515 protein binding | IPI PMID:15527767 Proteomics-based identification of proteins interacting with... | REMOVE | Summary: The reported interaction provides association evidence but generic protein binding is uninformative. Reason: The study detects beta-actin association with Smad3 during cytoskeletal rearrangement; it does not justify assigning the partnerβs transcription-factor activity to actin. Remove GO:0005515 under the generic-binding policy; this does not reject the reported pair or infer that ACTB is absent from the experimental complex. Supporting Evidence: PMID:15527767 Proteomics-based identification of proteins interacting with Smad3: SREBP-2 forms a complex with Smad3 and inhibits its transcriptional activity. |
| GO:0005515 protein binding | IPI PMID:16049941 A pilot proteomic study of amyloid precursor interactors in ... | REMOVE | Summary: The reported interaction provides association evidence but generic protein binding is uninformative. Reason: APP-associated cytoskeletal interactions are the evidence context; a specific biochemical function of ACTB is not established by the broad binding assertion. Remove GO:0005515 under the generic-binding policy; this does not reject the reported pair or infer that ACTB is absent from the experimental complex. Supporting Evidence: PMID:16049941 A pilot proteomic study of amyloid precursor interactors in Alzheimer's disease. |
| GO:0005515 protein binding | IPI PMID:16189514 Towards a proteome-scale map of the human protein-protein in... | REMOVE | Summary: The reported interaction provides association evidence but generic protein binding is uninformative. Reason: The proteome-scale interaction map records association evidence, without resolving a particular biochemical activity for this ACTB edge. Remove GO:0005515 under the generic-binding policy; this does not reject the reported pair or infer that ACTB is absent from the experimental complex. Supporting Evidence: PMID:16189514 Towards a proteome-scale map of the human protein-protein interaction network. |
| GO:0005515 protein binding | IPI PMID:16375898 Identification of an actin-binding site in p47phox an organi... | REMOVE | Summary: The reported interaction provides association evidence but generic protein binding is uninformative. Reason: The p47phox study examines association with cytoskeletal proteins during oxidase assembly; interaction is not evidence that ACTB performs oxidase catalysis. Remove GO:0005515 under the generic-binding policy; this does not reject the reported pair or infer that ACTB is absent from the experimental complex. Supporting Evidence: PMID:16375898 Identification of an actin-binding site in p47phox an organizer protein of NADPH oxidase. |
| GO:0005515 protein binding | IPI PMID:17404223 The role of CaMKII as an F-actin-bundling protein crucial fo... | MODIFY | Summary: Actin binds CaMKII-beta in an F-actin-bundling interaction. Reason: PMID:17404223 describes CaMKII-beta association with F-actin and bundling, rather than an actin kinase active site. Protein kinase binding captures the partner class already independently represented by PAINT; retain the source assay scope without assigning CaMKII catalysis to ACTB. Proposed replacements: protein kinase binding Supporting Evidence: PMID:17404223 Here, we provide biochemical evidence that CaMKII is capable of bundling F-actin through a stoichiometric interaction. |
| GO:0005515 protein binding | IPI PMID:17502619 beta-Actin regulates platelet nitric oxide synthase 3 activi... | REMOVE | Summary: G-actin binds NOS3 in the human platelet study. Reason: PMID:17502619 directly supports G-actin binding to NOS3 and Hsp90-dependent regulation in human platelets. The same-source IPI GO:0050998 nitric-oxide synthase binding annotation already represents the informative interaction. Remove the generic GO:0005515 annotation under the generic-binding policy; this does not reject the interaction or create a duplicate replacement. Supporting Evidence: PMID:17502619 We found that NOS-3 binds to the globular, but not the filamentous, form of beta-actin |
| GO:0005515 protein binding | IPI PMID:17599063 PtdIns(4,5)P-restricted plasma membrane localization of FAN ... | REMOVE | Summary: The reported interaction provides association evidence but generic protein binding is uninformative. Reason: FAN-associated signaling and cytoskeletal effects provide the interaction context; the generic association does not specify a separate ACTB effector activity. Remove GO:0005515 under the generic-binding policy; this does not reject the reported pair or infer that ACTB is absent from the experimental complex. Supporting Evidence: PMID:17599063 PtdIns(4,5)P-restricted plasma membrane localization of FAN is involved in TNF-induced actin reorganization. |
| GO:0005515 protein binding | IPI PMID:19000816 Structural basis for parasite-specific functions of the dive... | REMOVE | Summary: The reported interaction provides association evidence but generic protein binding is uninformative. Reason: PMID:19000816 describes parasite profilin structure and function. The available abstract does not resolve the human actin reagent or assay underlying this IPI association. Remove the uninformative GO:0005515 under the generic-binding policy, without rejecting the interaction or asserting that ACTB was absent from the full study. Supporting Evidence: PMID:19000816 Structural basis for parasite-specific functions of the divergent profilin of Plasmodium falciparum. |
| GO:0005515 protein binding | IPI PMID:19008859 Molecular basis for G-actin binding to RPEL motifs from the ... | MODIFY | Summary: Human beta-actin binds the RPEL-containing transcription coregulator MAL. Reason: PMID:19008859 explicitly uses human FLAG-beta-actin in cell pull-downs with MAL RPEL constructs; the crystal actin preparation is rabbit skeletal actin. The human experiments support transcription coregulator binding, with actinβMAL association controlling availability of the coactivator, rather than an uninformative protein-binding label. Proposed replacements: transcription coregulator binding Supporting Evidence: PMID:19008859 RPEL1MAL and RPEL2MAL recovered exogenous wild-type Ξ²-actin and endogenous Ξ²-actin efficiently from total cell lysates |
| GO:0005515 protein binding | IPI PMID:19171758 Kank attenuates actin remodeling by preventing interaction b... | REMOVE | Summary: The reported interaction provides association evidence but generic protein binding is uninformative. Reason: Kank and IRSp53 organize signaling-linked actin structures; their association does not make ACTB the signaling enzyme. Remove GO:0005515 under the generic-binding policy; this does not reject the reported pair or infer that ACTB is absent from the experimental complex. Supporting Evidence: PMID:19171758 Kank attenuates actin remodeling by preventing interaction between IRSp53 and Rac1. |
| GO:0005515 protein binding | IPI PMID:19328794 Nuclear myosin II regulates the assembly of preinitiation co... | REMOVE | Summary: The reported interaction provides association evidence but generic protein binding is uninformative. Reason: The study identifies nuclear alpha- and beta-actin with myosin-II-associated transcriptional complexes; the generic label adds no defined ACTB activity beyond this complex context. Remove GO:0005515 under the generic-binding policy; this does not reject the reported pair or infer that ACTB is absent from the experimental complex. Supporting Evidence: PMID:19328794 Nuclear myosin II regulates the assembly of preinitiation complex for ICAM-1 gene transcription. |
| GO:0005515 protein binding | IPI PMID:19338310 Streamline proteomic approach for characterizing protein-pro... | REMOVE | Summary: The reported interaction provides association evidence but generic protein binding is uninformative. Reason: RAD52-associated actin evidence does not make actin a DNA-recombination enzyme; a more specific ACTB function is not established by this generic association. Remove GO:0005515 under the generic-binding policy; this does not reject the reported pair or infer that ACTB is absent from the experimental complex. Supporting Evidence: PMID:19338310 Streamline proteomic approach for characterizing protein-protein interaction network in a RAD52 protein complex. |
| GO:0005515 protein binding | IPI PMID:20473970 Identification of FBXO25-interacting proteins using an integ... | REMOVE | Summary: The reported interaction provides association evidence but generic protein binding is uninformative. Reason: FBXO25 interacts with beta-actin and associates with actin-dependent nuclear domains; the interaction does not assign ubiquitin-ligase activity to ACTB. Remove GO:0005515 under the generic-binding policy; this does not reject the reported pair or infer that ACTB is absent from the experimental complex. Supporting Evidence: PMID:20473970 Identification of FBXO25-interacting proteins using an integrated proteomics approach. |
| GO:0005515 protein binding | IPI PMID:20618440 Proteomic and biochemical analysis of 14-3-3-binding protein... | REMOVE | Summary: The reported interaction provides association evidence but generic protein binding is uninformative. Reason: The 14-3-3/ceramide study examines cytoskeletal interaction changes; no separate specific ACTB molecular activity follows from the generic interaction. Remove GO:0005515 under the generic-binding policy; this does not reject the reported pair or infer that ACTB is absent from the experimental complex. Supporting Evidence: PMID:20618440 Proteomic and biochemical analysis of 14-3-3-binding proteins during C2-ceramide-induced apoptosis. |
| GO:0005515 protein binding | IPI PMID:21044950 Genome-wide YFP fluorescence complementation screen identifi... | REMOVE | Summary: The reported interaction provides association evidence but generic protein binding is uninformative. Reason: The protein-association screen concerns telomeric complexes; detection of ACTB alone does not identify a telomerase or DNA-remodeling activity. Remove GO:0005515 under the generic-binding policy; this does not reject the reported pair or infer that ACTB is absent from the experimental complex. Supporting Evidence: PMID:21044950 Genome-wide YFP fluorescence complementation screen identifies new regulators for telomere signaling in human cells. |
| GO:0005515 protein binding | IPI PMID:21516116 Next-generation sequencing to generate interactome datasets. | REMOVE | Summary: The reported interaction provides association evidence but generic protein binding is uninformative. Reason: The Stitch-seq assay detects binary interactions; it establishes an interaction-map context rather than a biochemical ACTB role for each edge. Remove GO:0005515 under the generic-binding policy; this does not reject the reported pair or infer that ACTB is absent from the experimental complex. Supporting Evidence: PMID:21516116 Next-generation sequencing to generate interactome datasets. |
| GO:0005515 protein binding | IPI PMID:21555369 Nuclear ErbB2 enhances translation and cell growth by activa... | REMOVE | Summary: The reported interaction provides association evidence but generic protein binding is uninformative. Reason: The study reports nuclear ErbB2 association with beta-actin and RNA polymerase I; it does not attribute ErbB2 kinase chemistry to actin. Remove GO:0005515 under the generic-binding policy; this does not reject the reported pair or infer that ACTB is absent from the experimental complex. Supporting Evidence: PMID:21555369 Nuclear ErbB2 enhances translation and cell growth by activating transcription of ribosomal RNA genes. |
| GO:0005515 protein binding | IPI PMID:21577206 A novel interplay between oncogenic PFTK1 protein kinase and... | REMOVE | Summary: The reported interaction provides association evidence but generic protein binding is uninformative. Reason: The PFTK1/TAGLN2 study includes ACTB-associated signaling and phosphorylation; a substrate or partner relationship is not protein-kinase activity. Remove GO:0005515 under the generic-binding policy; this does not reject the reported pair or infer that ACTB is absent from the experimental complex. Supporting Evidence: PMID:21577206 A novel interplay between oncogenic PFTK1 protein kinase and tumor suppressor TAGLN2 in the control of liver cancer cell motility. |
| GO:0005515 protein binding | IPI PMID:22038833 Disruption of cytokeratin-8 interaction with F508del-CFTR co... | REMOVE | Summary: The reported interaction provides association evidence but generic protein binding is uninformative. Reason: The CFTR/keratin interaction context supports association evidence without resolving an additional ACTB molecular function. Remove GO:0005515 under the generic-binding policy; this does not reject the reported pair or infer that ACTB is absent from the experimental complex. Supporting Evidence: PMID:22038833 Disruption of cytokeratin-8 interaction with F508del-CFTR corrects its functional defect. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: The reported interaction provides association evidence but generic protein binding is uninformative. Reason: The systematic human interaction map provides pairwise association evidence, not a mechanism specific to every ACTB edge. Remove GO:0005515 under the generic-binding policy; this does not reject the reported pair or infer that ACTB is absent from the experimental complex. Supporting Evidence: PMID:25416956 A proteome-scale map of the human interactome network. |
| GO:0005515 protein binding | IPI PMID:25712891 G551D-CFTR needs more bound actin than wild-type CFTR to mai... | REMOVE | Summary: The reported interaction provides association evidence but generic protein binding is uninformative. Reason: The study reports altered association of mutant CFTR with actin and effects of actin disruption; the generic binding label is less informative than the measured cytoskeletal regulation context. Remove GO:0005515 under the generic-binding policy; this does not reject the reported pair or infer that ACTB is absent from the experimental complex. Supporting Evidence: PMID:25712891 G551D-CFTR needs more bound actin than wild-type CFTR to maintain its presence in plasma membranes. |
| GO:0005515 protein binding | IPI PMID:25910212 Widespread macromolecular interaction perturbations in human... | REMOVE | Summary: The reported interaction provides association evidence but generic protein binding is uninformative. Reason: The disease-variant interaction study measures changes in protein interactions; generic ACTB association alone does not identify a distinct molecular activity. Remove GO:0005515 under the generic-binding policy; this does not reject the reported pair or infer that ACTB is absent from the experimental complex. Supporting Evidence: PMID:25910212 Widespread macromolecular interaction perturbations in human genetic disorders. |
| GO:0005515 protein binding | IPI PMID:27107014 An inter-species protein-protein interaction network across ... | REMOVE | Summary: The reported interaction provides association evidence but generic protein binding is uninformative. Reason: The human-yeast interaction map is a cross-species association screen; no ACTB enzymatic activity is implied by a detected pair. Remove GO:0005515 under the generic-binding policy; this does not reject the reported pair or infer that ACTB is absent from the experimental complex. Supporting Evidence: PMID:27107014 An inter-species protein-protein interaction network across vast evolutionary distance. |
| GO:0005515 protein binding | IPI PMID:27607350 Characterization of the Translationally Controlled Tumor Pro... | REMOVE | Summary: The reported interaction provides association evidence but generic protein binding is uninformative. Reason: The TCTP study provides a cytoskeletal-interaction context without establishing an additional ACTB-specific activity. Remove GO:0005515 under the generic-binding policy; this does not reject the reported pair or infer that ACTB is absent from the experimental complex. Supporting Evidence: PMID:27607350 Characterization of the Translationally Controlled Tumor Protein (TCTP) Interactome Reveals Novel Binding Partners in Human Cancer Cells. |
| GO:0005515 protein binding | IPI PMID:28514442 Architecture of the human interactome defines protein commun... | REMOVE | Summary: The reported interaction provides association evidence but generic protein binding is uninformative. Reason: BioPlex affinity-purification mass spectrometry supports complex association; an individual edge is not necessarily direct binding or a distinct ACTB activity. Remove GO:0005515 under the generic-binding policy; this does not reject the reported pair or infer that ACTB is absent from the experimental complex. Supporting Evidence: PMID:28514442 Architecture of the human interactome defines protein communities and disease networks. |
| GO:0005515 protein binding | IPI PMID:29477555 HtrA3 is a cellular partner of cytoskeleton proteins and TCP... | REMOVE | Summary: The reported interaction provides association evidence but generic protein binding is uninformative. Reason: HtrA3 cleavage of actin places ACTB in a substrate relationship; it does not make ACTB a peptidase. Remove GO:0005515 under the generic-binding policy; this does not reject the reported pair or infer that ACTB is absent from the experimental complex. Supporting Evidence: PMID:29477555 HtrA3 is a cellular partner of cytoskeleton proteins and TCP1Ξ± chaperonin. |
| GO:0005515 protein binding | IPI PMID:29892012 An interactome perturbation framework prioritizes damaging m... | REMOVE | Summary: The reported interaction provides association evidence but generic protein binding is uninformative. Reason: The variant interaction framework assays protein pairs and variant effects; a generic association does not define ACTBβs biochemical role. Remove GO:0005515 under the generic-binding policy; this does not reject the reported pair or infer that ACTB is absent from the experimental complex. Supporting Evidence: PMID:29892012 An interactome perturbation framework prioritizes damaging missense mutations for developmental disorders. |
| GO:0005515 protein binding | IPI PMID:29924966 A Proteomic Variant Approach (ProVarA) for Personalized Medi... | REMOVE | Summary: The reported interaction provides association evidence but generic protein binding is uninformative. Reason: The ProVarA study assesses interaction changes in protein variants; the generic label does not convey a distinct ACTB mechanism. Remove GO:0005515 under the generic-binding policy; this does not reject the reported pair or infer that ACTB is absent from the experimental complex. Supporting Evidence: PMID:29924966 A Proteomic Variant Approach (ProVarA) for Personalized Medicine of Inherited and Somatic Disease. |
| GO:0005515 protein binding | IPI PMID:30021884 Histone Interaction Landscapes Visualized by Crosslinking Ma... | REMOVE | Summary: The reported interaction provides association evidence but generic protein binding is uninformative. Reason: Histone cross-linking mass spectrometry establishes proximity or association in a chromatin context; it does not by itself assign histone modification chemistry to ACTB. Remove GO:0005515 under the generic-binding policy; this does not reject the reported pair or infer that ACTB is absent from the experimental complex. Supporting Evidence: PMID:30021884 Histone Interaction Landscapes Visualized by Crosslinking Mass Spectrometry in Intact Cell Nuclei. |
| GO:0005515 protein binding | IPI PMID:30886144 Network-based prediction of protein interactions. | REMOVE | Summary: The reported interaction provides association evidence but generic protein binding is uninformative. Reason: The interaction-network study combines prediction with experimental investigation; the generic ACTB label does not establish a specific molecular activity, irrespective of the edge-discovery method. Remove GO:0005515 under the generic-binding policy; this does not reject the reported pair or infer that ACTB is absent from the experimental complex. Supporting Evidence: PMID:30886144 Network-based prediction of protein interactions. |
| GO:0005515 protein binding | IPI PMID:31515488 Extensive disruption of protein interactions by genetic vari... | REMOVE | Summary: The reported interaction provides association evidence but generic protein binding is uninformative. Reason: The variant interaction study identifies association differences without defining a separate ACTB biochemical activity for this edge. Remove GO:0005515 under the generic-binding policy; this does not reject the reported pair or infer that ACTB is absent from the experimental complex. Supporting Evidence: PMID:31515488 Extensive disruption of protein interactions by genetic variants across the allele frequency spectrum in human populations. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: The reported interaction provides association evidence but generic protein binding is uninformative. Reason: HuRI systematically measures binary protein interactions; the generic term does not describe which structural or regulatory work ACTB performs. Remove GO:0005515 under the generic-binding policy; this does not reject the reported pair or infer that ACTB is absent from the experimental complex. Supporting Evidence: PMID:32296183 A reference map of the human binary protein interactome. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: The reported interaction provides association evidence but generic protein binding is uninformative. Reason: The interaction resource uses repeated screening, pair retesting and validation of a subset; generic binding remains functionally uninformative even when an association is reproducible. Remove GO:0005515 under the generic-binding policy; this does not reject the reported pair or infer that ACTB is absent from the experimental complex. Supporting Evidence: PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative Disease Proteins and Uncovers Widespread Protein Aggregation in Affected Brains. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: The reported interaction provides association evidence but generic protein binding is uninformative. Reason: BioPlex surveys associations by affinity purification and mass spectrometry; complex coassociation is retained as evidence, without inventing an ACTB-specific function. Remove GO:0005515 under the generic-binding policy; this does not reject the reported pair or infer that ACTB is absent from the experimental complex. Supporting Evidence: PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling of the human interactome. |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | REMOVE | Summary: The reported interaction provides association evidence but generic protein binding is uninformative. Reason: OpenCell combines endogenous protein tagging, imaging and interaction proteomics; the generic binding annotation does not specify the activity of ACTB within a detected association. Remove GO:0005515 under the generic-binding policy; this does not reject the reported pair or infer that ACTB is absent from the experimental complex. Supporting Evidence: PMID:35271311 OpenCell: Endogenous tagging for the cartography of human cellular organization. |
| GO:0005515 protein binding | IPI PMID:36012204 Differential CFTR-Interactome Proximity Labeling Procedures ... | REMOVE | Summary: The reported interaction provides association evidence but generic protein binding is uninformative. Reason: The CFTR proximity-proteomics context identifies nearby proteins; it does not establish a new catalytic or regulatory ACTB activity for every hit. Remove GO:0005515 under the generic-binding policy; this does not reject the reported pair or infer that ACTB is absent from the experimental complex. Supporting Evidence: PMID:36012204 Differential CFTR-Interactome Proximity Labeling Procedures Identify Enrichment in Multiple SLC Transporters. |
| GO:0042802 identical protein binding | IPI PMID:16189514 Towards a proteome-scale map of the human protein-protein in... | ACCEPT | Summary: Actin self-association supports its filament-forming structural function. Reason: PMID:16189514 describes a human two-hybrid interaction map; its exact ACTBβACTB assay record was not independently recovered. Retain the curated self-association function on independent direct human beta-actin assembly evidence: recombinant wild-type ACTB formed filaments in PMID:25255767, Results/Figure 4A. The original IPI attribution is preserved, without claiming that its source-specific experiment was independently verified. The original publisher Results/Figure evidence is documented in the notes; the local abstract does not contain this specific assay result. Supporting Evidence: PMID:16189514 Using a stringent, high-throughput yeast two-hybrid system, we tested pairwise interactions among the products of approximately 8,100 currently available Gateway-cloned open reading frames and detected approximately 2,800 interactions. |
| GO:0042802 identical protein binding | IPI PMID:17404223 The role of CaMKII as an F-actin-bundling protein crucial fo... | ACCEPT | Summary: Actin self-association supports its filament-forming structural function. Reason: PMID:17404223 directly reports CaMKII-dependent bundling of F-actin; this is positive filament evidence but does not by itself resolve the actin reagent as human ACTB. Retain the curated self-association function on independent direct human beta-actin assembly evidence: recombinant wild-type ACTB formed filaments in PMID:25255767, Results/Figure 4A. The original IPI attribution is preserved, without claiming that its source-specific experiment was independently verified. The original publisher Results/Figure evidence is documented in the notes; the local abstract does not contain this specific assay result. Supporting Evidence: PMID:17404223 Here, we provide biochemical evidence that CaMKII is capable of bundling F-actin through a stoichiometric interaction. |
| GO:0042802 identical protein binding | IPI PMID:18234857 High-resolution cryo-EM structure of the F-actin-fimbrin/pla... | ACCEPT | Summary: Actin self-association supports its filament-forming structural function. Reason: PMID:18234857 directly reconstructs F-actin alone and with fimbrin, including adjacent actin protomers; the accessible abstract does not identify the actin isoform and species. Retain the curated self-association function on independent direct human beta-actin assembly evidence: recombinant wild-type ACTB formed filaments in PMID:25255767, Results/Figure 4A. The original IPI attribution is preserved, without claiming that its source-specific experiment was independently verified. The original publisher Results/Figure evidence is documented in the notes; the local abstract does not contain this specific assay result. Supporting Evidence: PMID:18234857 we have generated 12-A-resolution maps of F-actin alone and F-actin decorated with a fragment of human fimbrin (L-plastin) containing tandem CH-domains. |
| GO:0042802 identical protein binding | IPI PMID:19000816 Structural basis for parasite-specific functions of the dive... | ACCEPT | Summary: Actin self-association supports its filament-forming structural function. Reason: PMID:19000816 describes parasite profilin structures and genetics. The available abstract does not resolve the actin reagent or the particular homotypic assay underlying this IPI annotation. Retain the curated self-association function on independent direct human beta-actin assembly evidence: recombinant wild-type ACTB formed filaments in PMID:25255767, Results/Figure 4A. The original IPI attribution is preserved, without claiming that its source-specific experiment was independently verified. The original publisher Results/Figure evidence is documented in the notes; the local abstract does not contain this specific assay result. Supporting Evidence: PMID:19000816 We present the first crystal structure of an apicomplexan profilin, that of the malaria parasite Plasmodium falciparum, alone and in complex with a polyproline ligand peptide. |
| GO:0042802 identical protein binding | IPI PMID:20383143 Opening of tandem calponin homology domains regulates their ... | ACCEPT | Summary: Actin self-association supports its filament-forming structural function. Reason: PMID:20383143 directly resolves alpha-actinin domains on F-actin. The recovered body establishes the filament context, while the actin isoform and source attribution remain unresolved. Retain the curated self-association function on independent direct human beta-actin assembly evidence: recombinant wild-type ACTB formed filaments in PMID:25255767, Results/Figure 4A. The original IPI attribution is preserved, without claiming that its source-specific experiment was independently verified. The original publisher Results/Figure evidence is documented in the notes; the local abstract does not contain this specific assay result. Supporting Evidence: PMID:20383143 We show that the tandem CH domains of alpha-actinin bind F-actin in an open conformation |
| GO:0042802 identical protein binding | IPI PMID:21516116 Next-generation sequencing to generate interactome datasets. | ACCEPT | Summary: Actin self-association supports its filament-forming structural function. Reason: PMID:21516116 reports Stitch-seq human interaction mapping; the exact ACTBβACTB supplemental assay record was not independently recovered. Retain the curated self-association function on independent direct human beta-actin assembly evidence: recombinant wild-type ACTB formed filaments in PMID:25255767, Results/Figure 4A. The original IPI attribution is preserved, without claiming that its source-specific experiment was independently verified. The original publisher Results/Figure evidence is documented in the notes; the local abstract does not contain this specific assay result. Supporting Evidence: PMID:21516116 We describe a massively parallel interactome-mapping pipeline, Stitch-seq, that combines PCR stitching with next-generation sequencing and used it to generate a new human interactome dataset. |
| GO:0042802 identical protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | ACCEPT | Summary: Actin self-association supports its filament-forming structural function. Reason: PMID:25416956 reports a human binary interaction map; the exact ACTBβACTB supplemental assay record was not independently recovered. Retain the curated self-association function on independent direct human beta-actin assembly evidence: recombinant wild-type ACTB formed filaments in PMID:25255767, Results/Figure 4A. The original IPI attribution is preserved, without claiming that its source-specific experiment was independently verified. The original publisher Results/Figure evidence is documented in the notes; the local abstract does not contain this specific assay result. Supporting Evidence: PMID:25416956 Here, we describe a systematic map of ?14,000 high-quality human binary protein-protein interactions. |
| GO:0042802 identical protein binding | IPI PMID:25502805 A massively parallel pipeline to clone DNA variants and exam... | ACCEPT | Summary: Actin self-association supports its filament-forming structural function. Reason: PMID:25502805 reports Clone-seq and comparative interaction assays for human variants; the exact ACTBβACTB assay and allele assignment were not independently recovered. Retain the curated self-association function on independent direct human beta-actin assembly evidence: recombinant wild-type ACTB formed filaments in PMID:25255767, Results/Figure 4A. The original IPI attribution is preserved, without claiming that its source-specific experiment was independently verified. The original publisher Results/Figure evidence is documented in the notes; the local abstract does not contain this specific assay result. Supporting Evidence: PMID:25502805 we further develop a comparative interactome-scanning pipeline integrating high-throughput GFP, yeast two-hybrid (Y2H), and mass spectrometry assays to systematically evaluate the functional impact of mutations on protein stability and interactions. |
| GO:0042802 identical protein binding | IPI PMID:25910212 Widespread macromolecular interaction perturbations in human... | ACCEPT | Summary: Actin self-association supports its filament-forming structural function. Reason: PMID:25910212 reports interaction profiling of human disease variants; the exact ACTBβACTB assay and allele assignment were not independently recovered. Retain the curated self-association function on independent direct human beta-actin assembly evidence: recombinant wild-type ACTB formed filaments in PMID:25255767, Results/Figure 4A. The original IPI attribution is preserved, without claiming that its source-specific experiment was independently verified. The original publisher Results/Figure evidence is documented in the notes; the local abstract does not contain this specific assay result. Supporting Evidence: PMID:25910212 Here we functionally profile several thousand missense mutations across a spectrum of Mendelian disorders using various interaction assays. |
| GO:0042802 identical protein binding | IPI PMID:29892012 An interactome perturbation framework prioritizes damaging m... | ACCEPT | Summary: Actin self-association supports its filament-forming structural function. Reason: PMID:29892012 reports interaction perturbations associated with developmental-disorder variants; the exact ACTBβACTB assay and allele assignment were not independently recovered. Retain the curated self-association function on independent direct human beta-actin assembly evidence: recombinant wild-type ACTB formed filaments in PMID:25255767, Results/Figure 4A. The original IPI attribution is preserved, without claiming that its source-specific experiment was independently verified. The original publisher Results/Figure evidence is documented in the notes; the local abstract does not contain this specific assay result. Supporting Evidence: PMID:29892012 Here we establish an experimentally and computationally integrated approach to investigate the functional impact of missense mutations in the context of the human interactome network |
| GO:0042802 identical protein binding | IPI PMID:31515488 Extensive disruption of protein interactions by genetic vari... | ACCEPT | Summary: Actin self-association supports its filament-forming structural function. Reason: PMID:31515488 reports human variant effects on binary interactions; the exact ACTBβACTB assay and allele assignment were not independently recovered. Retain the curated self-association function on independent direct human beta-actin assembly evidence: recombinant wild-type ACTB formed filaments in PMID:25255767, Results/Figure 4A. The original IPI attribution is preserved, without claiming that its source-specific experiment was independently verified. The original publisher Results/Figure evidence is documented in the notes; the local abstract does not contain this specific assay result. Supporting Evidence: PMID:31515488 we leverage the ExAC database of 60,706 human exomes to investigate experimentally the impact of 2009 missense single nucleotide variants (SNVs) across 2185 protein-protein interactions |
| GO:0042802 identical protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | ACCEPT | Summary: Actin self-association supports its filament-forming structural function. Reason: PMID:32296183 reports the HuRI human binary interaction map; the exact ACTBβACTB supplemental assay record was not independently recovered. Retain the curated self-association function on independent direct human beta-actin assembly evidence: recombinant wild-type ACTB formed filaments in PMID:25255767, Results/Figure 4A. The original IPI attribution is preserved, without claiming that its source-specific experiment was independently verified. The original publisher Results/Figure evidence is documented in the notes; the local abstract does not contain this specific assay result. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' reference interactome map of human binary protein interactions, or 'HuRI'. |
| GO:0005737 cytoplasm | IEA GO_REF:0000107 | ACCEPT | Summary: The mouse Actb transfer supports cytoplasm. Reason: The cytoplasmic pool agrees with human beta-actin localization. The ortholog inference is consistent with human ACTBβs conserved structural role; neuronal and apical specializations are retained as contextual. Propagation Review Root cause: NO FAILURE CORE Sources checked: UniProtKB:P60710 SUPPORTS TRANSFER Mouse Actb is the traced source, with Ensembl ENSMUSP00000098066 also in the inference. The cytoplasmic pool agrees with human beta-actin localization. |
| GO:0005829 cytosol | IEA GO_REF:0000107 | ACCEPT | Summary: The mouse Actb transfer supports cytosol. Reason: Soluble cytosolic actin coexists with filamentous actin and supports dynamic exchange. The ortholog inference is consistent with human ACTBβs conserved structural role; neuronal and apical specializations are retained as contextual. Propagation Review Root cause: NO FAILURE CORE Sources checked: UniProtKB:P60710 SUPPORTS TRANSFER Mouse Actb is the traced source, with Ensembl ENSMUSP00000098066 also in the inference. Soluble cytosolic actin coexists with filamentous actin and supports dynamic exchange. |
| GO:0005903 brush border | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: The mouse Actb transfer supports brush border. Reason: Brush-border association is a specialized apical epithelial context; no claim of ACTB-specific microvillar enzyme activity is made. The ortholog inference is consistent with human ACTBβs conserved structural role; neuronal and apical specializations are retained as contextual. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: UniProtKB:P60710 SUPPORTS TRANSFER Mouse Actb is the traced source, with Ensembl ENSMUSP00000098066 also in the inference. Brush-border association is a specialized apical epithelial context; no claim of ACTB-specific microvillar enzyme activity is made. |
| GO:0030863 cortical cytoskeleton | IEA GO_REF:0000107 | ACCEPT | Summary: The mouse Actb transfer supports cortical cytoskeleton. Reason: The cortical network is directly compatible with human junctional beta-actin localization. The ortholog inference is consistent with human ACTBβs conserved structural role; neuronal and apical specializations are retained as contextual. Propagation Review Root cause: NO FAILURE CORE Sources checked: UniProtKB:P60710 SUPPORTS TRANSFER Mouse Actb is the traced source, with Ensembl ENSMUSP00000098066 also in the inference. The cortical network is directly compatible with human junctional beta-actin localization. |
| GO:0044305 calyx of Held | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: The mouse Actb transfer supports calyx of Held. Reason: SynGO traces mouse Actb evidence to calyx-type synapses in PMID:27840001, where beta- and gamma-actin are examined separately. The ortholog inference is consistent with human ACTBβs conserved structural role; neuronal and apical specializations are retained as contextual. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: UniProtKB:P60710 SUPPORTS TRANSFER Mouse Actb is the traced source, with Ensembl ENSMUSP00000098066 also in the inference. SynGO traces mouse Actb evidence to calyx-type synapses in PMID:27840001, where beta- and gamma-actin are examined separately. Supporting Evidence: PMID:27840001 Polymerized actin provides mechanical force to form endocytic pits. |
| GO:0098685 Schaffer collateral - CA1 synapse | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: The mouse Actb transfer supports Schaffer collateral - CA1 synapse. Reason: The mouse source includes hippocampal synaptic actin. Preserve the curated Schaffer collateralβCA1 location as a neuronal context; the paper also studies calyx synapses. The ortholog inference is consistent with human ACTBβs conserved structural role; neuronal and apical specializations are retained as contextual. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: UniProtKB:P60710 SUPPORTS TRANSFER Mouse Actb is the traced source, with Ensembl ENSMUSP00000098066 also in the inference. The mouse source includes hippocampal synaptic actin. Preserve the curated Schaffer collateralβCA1 location as a neuronal context; the paper also studies calyx synapses. Supporting Evidence: PMID:27840001 Polymerized actin provides mechanical force to form endocytic pits. |
| GO:1900242 regulation of synaptic vesicle endocytosis | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: The mouse Actb transfer supports regulation of synaptic vesicle endocytosis. Reason: PMID:27840001 combines isoform knockout with capacitance, vesicle imaging and ultrastructure. Polymerized actin supplies mechanical force for endocytic pit formation, establishing actual structural participation rather than a merely downstream requirement. The ortholog inference is consistent with human ACTBβs conserved structural role; neuronal and apical specializations are retained as contextual. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: UniProtKB:P60710 SUPPORTS TRANSFER Mouse Actb is the traced source, with Ensembl ENSMUSP00000098066 also in the inference. PMID:27840001 combines isoform knockout with capacitance, vesicle imaging and ultrastructure. Polymerized actin supplies mechanical force for endocytic pit formation, establishing actual structural participation rather than a merely downstream requirement. Supporting Evidence: PMID:27840001 Polymerized actin provides mechanical force to form endocytic pits. |
| GO:0000776 kinetochore | NAS PMID:11078522 The human SWI/SNF-B chromatin-remodeling complex is related ... | KEEP AS NON CORE | Summary: Human SWI/SNF-B is detected at mitotic kinetochores. Reason: PMID:11078522 localizes the complex using BAF180 immunofluorescence. The NAS statement is retained as localization of an actin-containing complex, not as a direct beta-actin antibody experiment. Supporting Evidence: PMID:11078522 Immunofluorescence studies with a BAF180 antibody revealed that SWI/SNF-B localizes at the kinetochores of chromosomes during mitosis. |
| GO:0000785 chromatin | NAS PMID:12192000 REST repression of neuronal genes requires components of the... | ACCEPT | Summary: Chromatin-associated BAF complexes support this ACTB localization. Reason: PMID:12192000 demonstrates REST/CoREST recruitment of BAF components to a neuronal promoter. ACTBβs established membership supports the NAS complex localization without attributing REST DNA recognition to actin. Supporting Evidence: PMID:12192000 In vivo, BAF57 occupies the neuronal sodium channel gene (Nav1.2) promoter, and targeting to this gene requires REST. Reactome:R-HSA-9933238 a dimer of ACTB and ACTL6A/B (which together form the actin-related protein or ARP module linking the catalytic core of the SWI/SNF complex to the core/base module) |
| GO:0000785 chromatin | NAS PMID:29374058 Glioma tumor suppressor candidate region gene 1 (GLTSCR1) an... | ACCEPT | Summary: ACTB belongs to chromatin-associated GBAF remodeling machinery. Reason: PMID:29374058 measures GBAF bulk chromatin affinity and remodeling-complex properties. The broad chromatin location is compatible with structural participation by the ACTBβACTL6 module. Supporting Evidence: PMID:29374058 Even without these subunits, GBAF displayed in vitro ATPase activity and bulk chromatin affinity comparable to those of BAF. Reactome:R-HSA-9933238 a dimer of ACTB and ACTL6A/B (which together form the actin-related protein or ARP module linking the catalytic core of the SWI/SNF complex to the core/base module) |
| GO:0000786 nucleosome | IDA PMID:27153538 The TIP60 Complex Regulates Bivalent Chromatin Recognition b... | UNDECIDED | Summary: The precise nucleosome annotation requires resolution of the ACTB-related assay. Reason: GO:0000786 includes histones, wrapped DNA and associated proteins, so lack of histone identity is not grounds for rejection. PMID:27153538 establishes TIP60/MBTD1 interactions with nucleosomal chromatin, but the recovered material does not resolve the particular ACTB localization experiment supporting this IDA row. Supporting Evidence: PMID:27153538 The TIP60 Complex Regulates Bivalent Chromatin Recognition by 53BP1 through Direct H4K20me Binding and H2AK15 Acetylation. |
| GO:0000930 gamma-tubulin complex | NAS PMID:39321809 CDK5RAP2 activates microtubule nucleator Ξ³TuRC by facilitati... | KEEP AS NON CORE | Summary: Luminal actin is a component of non-activated gamma-TuRC. Reason: PMID:39321809 explicitly reports actin in the non-activated complex and its release during CDK5RAP2 activation. Retain complex membership with this assembly-state limitation. This complex represents a specialized structural pool outside the filament and SWI/SNF core functions synthesized here. Supporting Evidence: PMID:39321809 CM1 binding promotes lateral interactions between GCP subunits to facilitate microtubule-like conformations and release of luminal actin that is integral to non-activated Ξ³TuRC. |
| GO:0005869 dynactin complex | ISO GO_REF:0000114 | KEEP AS NON CORE | Summary: ACTB contributes to the short actin-related filament of dynactin. Reason: The ISO donor is ComplexPortal:CPX-26390, a dynactin complex. UniProt describes a filament containing one ACTB and eight ACTR1A subunits that supports dynactin-dependent dynein transport. This source is distinct from gamma-TuRC. This complex represents a specialized structural pool outside the filament and SWI/SNF core functions synthesized here. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: ComplexPortal:CPX-26390 SUPPORTS TRANSFER The ISO source is dynactin, whose short ACTR1A/ACTB filament supports dynein-mediated transport. It is not a gamma-TuRC donor. |
| GO:0006338 chromatin remodeling | NAS PMID:10078207 Reconstitution of a core chromatin remodeling complex from S... | ACCEPT | Summary: ACTB contributes structurally to native SWI/SNF chromatin remodeling. Reason: PMID:10078207 reconstitutes remodeling with BRG1/BRM and a minimal subset of other subunits; it does not identify ACTB as the ATPase. Retain the NAS process on established native ACTB complex participation, corroborated by the ACTBβACTL6 module in Reactome:R-HSA-9933238. Supporting Evidence: PMID:10078207 The addition of INI1, BAF155, and BAF170 to BRG1 increases remodeling activity to a level comparable to that of the whole hSWI/SNF complex. Reactome:R-HSA-9933238 a dimer of ACTB and ACTL6A/B (which together form the actin-related protein or ARP module linking the catalytic core of the SWI/SNF complex to the core/base module) |
| GO:0006338 chromatin remodeling | NAS PMID:29374058 Glioma tumor suppressor candidate region gene 1 (GLTSCR1) an... | ACCEPT | Summary: ACTB contributes within chromatin-remodeling GBAF complexes. Reason: PMID:29374058 demonstrates GBAF biochemical activity and chromatin affinity. ACTB supplies part of the structural module connecting the remodeling motor to the core; BRG1/BRM supplies the ATP-dependent motor chemistry. Supporting Evidence: PMID:29374058 Even without these subunits, GBAF displayed in vitro ATPase activity and bulk chromatin affinity comparable to those of BAF. Reactome:R-HSA-9933238 a dimer of ACTB and ACTL6A/B (which together form the actin-related protein or ARP module linking the catalytic core of the SWI/SNF complex to the core/base module) |
| GO:0006357 regulation of transcription by RNA polymerase II | NAS PMID:11263494 The murine SNF5/INI1 chromatin remodeling factor is essentia... | KEEP AS NON CORE | Summary: SWI/SNF-dependent gene regulation supports this contextual transcription process. Reason: PMID:11263494 uses mouse Snf5 loss to investigate mammalian remodeling complexes. Retain the NAS process for structural ACTB participation in functional SWI/SNF complexes, without presenting it as a human ACTB knockout experiment. Supporting Evidence: PMID:11263494 To investigate the function of two closely related mammalian SWI/SNF complexes in vivo, we inactivated the murine SNF5/INI1 gene, a common subunit of these two complexes. Reactome:R-HSA-9933238 a dimer of ACTB and ACTL6A/B (which together form the actin-related protein or ARP module linking the catalytic core of the SWI/SNF complex to the core/base module) |
| GO:0006357 regulation of transcription by RNA polymerase II | NAS PMID:17340523 Separation and Quantification of Some Alkaloids from Fumaria... | UNDECIDED | Summary: The recorded PMID resolves to an unrelated alkaloid paper. Reason: PMID:17340523 was independently checked in PubMed and matches the cached Fumaria separation paper. The source identifier is preserved, but the intended transcription reference remains unknown. The general ACTB process is plausible from other sources; this particular NAS assertion cannot be adjudicated from the miscited source. Propagation Review Root cause: SOURCE BAD Sources checked: PMID:17340523 UNRESOLVED The live PubMed record and local cache identify an unrelated alkaloid paper. Intended source unresolved. Supporting Evidence: PMID:17340523 Separation and Quantification of Some Alkaloids from Fumaria parviflora by Capillary Isotachophoresis1. |
| GO:0006357 regulation of transcription by RNA polymerase II | NAS PMID:17920018 Regulation of dendritic development by neuron-specific chrom... | KEEP AS NON CORE | Summary: Neuronal BAF complexes regulate transcriptional programs for dendrite development. Reason: PMID:17920018 establishes nBAF recruitment to target genes and cooperation with CREST. ACTBβs structural membership supports contextual complex participation, without assigning ACTL6B/BAF53b-specific targeting determinants to beta-actin. Supporting Evidence: PMID:17920018 nBAF complexes bind tightly to the Ca(2+)-responsive dendritic regulator CREST and directly regulate genes essential for dendritic outgrowth. Reactome:R-HSA-9933238 a dimer of ACTB and ACTL6A/B (which together form the actin-related protein or ARP module linking the catalytic core of the SWI/SNF complex to the core/base module) |
| GO:0006357 regulation of transcription by RNA polymerase II | NAS PMID:18809673 BRD7, a novel PBAF-specific SWI/SNF subunit, is required for... | KEEP AS NON CORE | Summary: PBAF and BAF complexes regulate target-gene transcription in stem cells. Reason: PMID:18809673 shows promoter-specific effects on transcription and preinitiation-complex recruitment. Retain structural ACTB participation at the broad regulation level; direction and specificity depend on the assembled complex and target. Supporting Evidence: PMID:18809673 We found that SWI/SNF affects recruitment of components of the preinitiation complex in a promoter-specific manner to modulate transcription positively or negatively. Reactome:R-HSA-9933238 a dimer of ACTB and ACTL6A/B (which together form the actin-related protein or ARP module linking the catalytic core of the SWI/SNF complex to the core/base module) |
| GO:0006357 regulation of transcription by RNA polymerase II | NAS PMID:29374058 Glioma tumor suppressor candidate region gene 1 (GLTSCR1) an... | KEEP AS NON CORE | Summary: GBAF supports context-dependent transcriptional regulation. Reason: PMID:29374058 defines the GLTSCR1/GLTSCR1L-containing remodeling complex. ACTB participates through the structural actin-related module; the annotation does not imply direct sequence-specific promoter recognition by actin. Supporting Evidence: PMID:29374058 Even without these subunits, GBAF displayed in vitro ATPase activity and bulk chromatin affinity comparable to those of BAF. Reactome:R-HSA-9933238 a dimer of ACTB and ACTL6A/B (which together form the actin-related protein or ARP module linking the catalytic core of the SWI/SNF complex to the core/base module) |
| GO:0007017 microtubule-based process | ISO GO_REF:0000114 | ACCEPT | Summary: The dynactin-associated ACTB filament contributes to a microtubule-based process. Reason: The traced ISO donor is dynactin ComplexPortal:CPX-26390, which supports processive dynein transport. Retain the sourceβs broad process; replacement with microtubule nucleation would substitute an unrelated gamma-TuRC mechanism for the actual donor. Propagation Review Root cause: NO FAILURE CORE Sources checked: ComplexPortal:CPX-26390 SUPPORTS TRANSFER The ISO source is dynactin, whose short ACTR1A/ACTB filament supports dynein-mediated transport. It is not a gamma-TuRC donor. |
| GO:0007020 microtubule nucleation | NAS PMID:39321809 CDK5RAP2 activates microtubule nucleator Ξ³TuRC by facilitati... | UNDECIDED | Summary: Actin occupies non-activated gamma-TuRC; its contribution to the tubulin nucleation step needs source-level resolution. Reason: The accessible PMID:39321809 abstract identifies luminal actin in non-activated gamma-TuRC and its release during CM1-dependent activation. GO:0007020 concerns formation of an oligomeric tubulin seed. Stable assembly of the precursor complex alone does not establish that ACTB supplies structure to that step; conversely, release during activation does not by itself prove that ACTB never contributes. The full source and ACTB-specific mechanistic evidence were not recovered, so leave this NAS process unresolved while retaining the directly reported complex membership. Supporting Evidence: PMID:39321809 CM1 binding promotes lateral interactions between GCP subunits to facilitate microtubule-like conformations and release of luminal actin that is integral to non-activated Ξ³TuRC. |
| GO:0008284 positive regulation of cell population proliferation | NAS PMID:29374058 Glioma tumor suppressor candidate region gene 1 (GLTSCR1) an... | KEEP AS NON CORE | Summary: GBAF supports proliferation in the tested prostate cancer context. Reason: PMID:29374058 reports loss of PC3 proliferation and colony formation after GLTSCR1 or GLTSCR1L knockout, with different dependence in LNCaP cells. ACTBβs structural contribution to the functioning complex makes contextual participation defensible; this is not a universal pro-proliferative property of actin. The proliferation experiment perturbs GLTSCR1/GLTSCR1L, not ACTB; its ACTB attribution is a complex-level inference anchored to ACTB structural membership, not an ACTB-specific necessity test. Supporting Evidence: PMID:29374058 GLTSCR1 or GLTSCR1L knockouts in the metastatic prostate cancer cell line PC3 resulted in a loss in proliferation and colony-forming ability. Reactome:R-HSA-9933238 a dimer of ACTB and ACTL6A/B (which together form the actin-related protein or ARP module linking the catalytic core of the SWI/SNF complex to the core/base module) |
| GO:0016363 nuclear matrix | NAS PMID:9128241 Components of the human SWI/SNF complex are enriched in acti... | KEEP AS NON CORE | Summary: A nuclear-matrix-associated SWI/SNF pool supports this location. Reason: PMID:9128241 fractionates active chromatin and nuclear matrix while detecting SWI/SNF subunits. Retain the NAS location at complex level; the source does not establish every nuclear ACTB molecule as matrix-bound. Supporting Evidence: PMID:9128241 hSWI/SNF proteins were also found to be associated with the nuclear matrix or nuclear scaffold |
| GO:0016514 SWI/SNF complex | NAS PMID:8804307 Diversity and specialization of mammalian SWI/SNF complexes. | ACCEPT | Summary: ACTB is a structural subunit of mammalian SWI/SNF complexes. Reason: PMID:8804307 establishes heterogeneous mammalian BAF assemblies. Subsequent ACTB complex evidence and the ACTBβACTL6 linkage described in Reactome:R-HSA-9933238 support membership without assigning the remodeling motor activity independently to actin. Supporting Evidence: PMID:8804307 We demonstrate that in mammals SWI/SNF complexes are present in multiple forms made up of 9-12 proteins that we refer to as BRG1-associated factors (BAFs) Reactome:R-HSA-9933238 a dimer of ACTB and ACTL6A/B (which together form the actin-related protein or ARP module linking the catalytic core of the SWI/SNF complex to the core/base module) |
| GO:0016586 RSC-type complex | NAS PMID:8804307 Diversity and specialization of mammalian SWI/SNF complexes. | ACCEPT | Summary: The RSC-type complex term includes mammalian PBAF. Reason: GO:0016586 explicitly encompasses mammalian PBAF, including its BAF180-containing form. Human SWI/SNF-B/PBAF evidence (PMID:11078522) corroborates ACTB complex membership; this term is not restricted to a yeast counterpart. Supporting Evidence: PMID:8804307 We demonstrate that in mammals SWI/SNF complexes are present in multiple forms made up of 9-12 proteins that we refer to as BRG1-associated factors (BAFs) Reactome:R-HSA-9933238 a dimer of ACTB and ACTL6A/B (which together form the actin-related protein or ARP module linking the catalytic core of the SWI/SNF complex to the core/base module) |
| GO:0030071 regulation of mitotic metaphase/anaphase transition | NAS PMID:23698369 BAF complexes facilitate decatenation of DNA by topoisomeras... | UNDECIDED | Summary: BAF-assisted decatenation is established, but the exact metaphase/anaphase regulatory assertion remains unresolved. Reason: PMID:23698369 shows TOP2A recruitment via BAF250A and BRG1 activity, with G2/M decatenation-checkpoint delay and anaphase bridges. These results support chromosome-segregation-related complex work; they do not by themselves resolve the narrower transition-control mechanism attributed in this NAS row. Supporting Evidence: PMID:23698369 BAF complexes facilitate decatenation of DNA by topoisomerase IIΞ±. |
| GO:0030071 regulation of mitotic metaphase/anaphase transition | NAS PMID:25066234 Requirement for PBAF in transcriptional repression and repai... | UNDECIDED | Summary: The exact mitotic-transition claim was not established from the recovered source. Reason: PMID:25066234 directly studies PBAF-dependent transcriptional silencing near DNA breaks and early repair in G0/G1. Discussion of sister-chromatid cohesion does not settle this separate metaphase/anaphase assertion; retain the original source and record the evidentiary gap. Supporting Evidence: PMID:25066234 Requirement for PBAF in transcriptional repression and repair at DNA breaks in actively transcribed regions of chromatin. |
| GO:0035060 brahma complex | NAS PMID:8804307 Diversity and specialization of mammalian SWI/SNF complexes. | ACCEPT | Summary: ACTB occurs in the BRM-containing form of the SWI/SNF machinery. Reason: GO:0035060 specifically denotes a brahma/BRM-containing complex. Mammalian complexes can use SMARCA2/BRM or SMARCA4/BRG1; the term is retained for the BRM-bearing assembly, not treated as a synonym for every BAF complex (PMID:8804307; Reactome:R-HSA-9933238). Supporting Evidence: PMID:8804307 We demonstrate that in mammals SWI/SNF complexes are present in multiple forms made up of 9-12 proteins that we refer to as BRG1-associated factors (BAFs) Reactome:R-HSA-9933238 a dimer of ACTB and ACTL6A/B (which together form the actin-related protein or ARP module linking the catalytic core of the SWI/SNF complex to the core/base module) |
| GO:0035267 NuA4 histone acetyltransferase complex | IDA PMID:27153538 The TIP60 Complex Regulates Bivalent Chromatin Recognition b... | KEEP AS NON CORE | Summary: ACTB is a component of the human NuA4/TIP60 complex. Reason: PMID:27153538 characterizes the TIP60/MBTD1 complex, while independent purification sources (PMID:14966270; PMID:10966108) substantiate actin membership. Retain the curated IDA membership without attributing the complexβs histone acetylation or methyl-lysine recognition to ACTB. This complex represents a specialized structural pool outside the filament and SWI/SNF core functions synthesized here. Supporting Evidence: PMID:27153538 MBTD1 allows TIP60 to associate with specific gene promoters and to promote the repair of DNA double-strand breaks by homologous recombination. |
| GO:0042981 regulation of apoptotic process | NAS PMID:14966270 Structural and functional conservation of the NuA4 histone a... | KEEP AS NON CORE | Summary: The ACTB-containing TIP60 complex contributes to apoptotic signaling. Reason: PMID:14966270 identifies the conserved human NuA4 assembly and discusses its apoptotic signaling context. The earlier primary PMID:10966108 reports that a catalytically inactive TIP60 complex impairs double-strand-break repair and apoptotic competence. Retain the NAS complex-level process as contextual structural participation, without assigning TIP60 acetyltransferase chemistry or a universal regulatory direction to ACTB. Supporting Evidence: PMID:14966270 Tip60 and its splice variant Tip60b/PLIP were purified as stable HAT complexes associated with identical polypeptides |
| GO:0045582 positive regulation of T cell differentiation | NAS PMID:12110891 Reciprocal regulation of CD4/CD8 expression by SWI/SNF-like ... | KEEP AS NON CORE | Summary: BAF complexes contribute to T-cell lineage differentiation through chromatin regulation. Reason: PMID:12110891 demonstrates BAF occupancy of the CD4 silencer and regulation of CD4/CD8 lineage genes. ACTB contributes complex structure, making the contextual process defensible; this is not an ACTB-specific DNA-recognition or lineage-instruction claim. Supporting Evidence: PMID:12110891 BAF complexes directly bind the CD4 silencer Reactome:R-HSA-9933238 a dimer of ACTB and ACTL6A/B (which together form the actin-related protein or ARP module linking the catalytic core of the SWI/SNF complex to the core/base module) |
| GO:0045596 negative regulation of cell differentiation | NAS PMID:30510198 A non-canonical BRD9-containing BAF chromatin remodeling com... | KEEP AS NON CORE | Summary: GBAF supports maintenance of the naive stem-cell transcriptional state. Reason: PMID:30510198 places GBAF at chromatin features governing naive pluripotency in mouse embryonic stem cells. The negative-differentiation context is retained through ACTBβs contribution to the functional complex, bounded to this cell state. Supporting Evidence: PMID:30510198 GBAF and esBAF complexes are targeted to different genomic features, with GBAF co-localizing with key regulators of naive pluripotency, which is consistent with its specific function in maintaining naive pluripotency gene expression. Reactome:R-HSA-9933238 a dimer of ACTB and ACTL6A/B (which together form the actin-related protein or ARP module linking the catalytic core of the SWI/SNF complex to the core/base module) |
| GO:0045597 positive regulation of cell differentiation | NAS PMID:11790558 SWI/SNF chromatin remodeling and cancer. | UNDECIDED | Summary: The specific positive-differentiation assertion requires the underlying evidence. Reason: PMID:11790558 is a review of SWI/SNF and cancer; the accessible abstract gives broad context-dependent transcription and tumor-suppression roles. It does not resolve the exact differentiation setting of this NAS row, so no biological contradiction is asserted. Supporting Evidence: PMID:11790558 SWI/SNF chromatin remodeling and cancer. |
| GO:0045597 positive regulation of cell differentiation | NAS PMID:12368262 Identification of a polymorphic, neuron-specific chromatin r... | UNDECIDED | Summary: bBAF membership is secure, while the particular positive-differentiation inference remains uncertain. Reason: Recovered full Results of PMID:12368262 identify beta-actin by Western blot in brain and HeLa complexes. The discussed developmental function remains a model, which is insufficient to settle the specific positive-differentiation process attributed here. Supporting Evidence: PMID:12368262 Identification of a polymorphic, neuron-specific chromatin remodeling complex. |
| GO:0045663 positive regulation of myoblast differentiation | NAS PMID:11175787 Mammalian SWI/SNF complexes promote MyoD-mediated muscle dif... | KEEP AS NON CORE | Summary: SWI/SNF remodeling promotes MyoD-dependent differentiation in the experimental fibroblast system. Reason: PMID:11175787 connects dominant-negative BRG1/BRM to failed remodeling of a muscle-gene promoter and blocked myogenesis. ACTB contributes to the remodeling complex, rather than acting as the MyoD transcription factor; the process is retained as contextual. Supporting Evidence: PMID:11175787 SWI/SNF enzymes promote MyoD-mediated muscle differentiation and indicate that these enzymes function by altering chromatin structure in promoter regions of endogenous, differentiation-specific loci. Reactome:R-HSA-9933238 a dimer of ACTB and ACTL6A/B (which together form the actin-related protein or ARP module linking the catalytic core of the SWI/SNF complex to the core/base module) |
| GO:0045663 positive regulation of myoblast differentiation | NAS PMID:15985610 PBAF chromatin-remodeling complex requires a novel specifici... | UNDECIDED | Summary: The precise myoblast-differentiation claim was not resolved from this source. Reason: PMID:15985610 establishes PBAF/BAF200-dependent selective interferon-responsive gene regulation. Recovered material does not settle the separate myoblast result. The annotation is left unresolved instead of declaring a wrong-gene error from the paperβs emphasis. Supporting Evidence: PMID:15985610 PBAF chromatin-remodeling complex requires a novel specificity subunit, BAF200, to regulate expression of selective interferon-responsive genes. |
| GO:0045893 positive regulation of DNA-templated transcription | NAS PMID:27153538 The TIP60 Complex Regulates Bivalent Chromatin Recognition b... | KEEP AS NON CORE | Summary: TIP60-associated chromatin regulation can support positive transcription in the tested context. Reason: PMID:27153538 links MBTD1/TIP60 recruitment to chromatin and transcriptional effects. ACTBβs structural contribution to the functional complex supports contextual participation; it is not the histone-reader or acetyltransferase subunit. Supporting Evidence: PMID:27153538 MBTD1 allows TIP60 to associate with specific gene promoters and to promote the repair of DNA double-strand breaks by homologous recombination. |
| GO:0051726 regulation of cell cycle | IMP PMID:27153538 The TIP60 Complex Regulates Bivalent Chromatin Recognition b... | UNDECIDED | Summary: The ACTB-specific cell-cycle interpretation of this IMP row remains unresolved. Reason: The recovered PMID:27153538 material examines TIP60/MBTD1 functions and checks cell-cycle distribution as a potential confound of repair assays. It does not resolve the particular experiment underlying ACTB regulation of cell cycle. The original experimental assertion is not overruled from partial access. Supporting Evidence: PMID:27153538 The TIP60 Complex Regulates Bivalent Chromatin Recognition by 53BP1 through Direct H4K20me Binding and H2AK15 Acetylation. |
| GO:0070316 regulation of G0 to G1 transition | NAS PMID:11790558 SWI/SNF chromatin remodeling and cancer. | UNDECIDED | Summary: The exact G0-to-G1 transition assertion needs more specific source evidence. Reason: The accessible PMID:11790558 review abstract establishes broad SWI/SNF effects on transcription and tumor suppression, but not the specific transition mechanism of this row. Retain the source without substituting evidence for the distinct G1/S transition. Supporting Evidence: PMID:11790558 SWI/SNF chromatin remodeling and cancer. |
| GO:0071564 npBAF complex | NAS PMID:8804307 Diversity and specialization of mammalian SWI/SNF complexes. | ACCEPT | Summary: ACTB participates in neural-progenitor BAF complexes. Reason: The early mammalian complex study PMID:8804307 provides historical BAF context; neural-progenitor composition is corroborated by the distinct progenitor versus neuronal complexes described in PMID:17920018 and the ACTB-containing npBAF event Reactome:R-HSA-9934021. Supporting Evidence: PMID:8804307 We demonstrate that in mammals SWI/SNF complexes are present in multiple forms made up of 9-12 proteins that we refer to as BRG1-associated factors (BAFs) Reactome:R-HSA-9933238 a dimer of ACTB and ACTL6A/B (which together form the actin-related protein or ARP module linking the catalytic core of the SWI/SNF complex to the core/base module) Reactome:R-HSA-9934021 npBAF complexes contain either SMARCA4 or SMARCA2 as catalytic subunits |
| GO:0071565 nBAF complex | NAS PMID:17920018 Regulation of dendritic development by neuron-specific chrom... | ACCEPT | Summary: ACTB is a structural component of neuronal BAF complexes. Reason: PMID:17920018 characterizes nBAF complexes distinguished by BAF53b. ACTB membership is compatible with the actin-related structural module, while ACTL6B-specific determinants are not assigned to ACTB. Supporting Evidence: PMID:17920018 nBAF complexes bind tightly to the Ca(2+)-responsive dendritic regulator CREST and directly regulate genes essential for dendritic outgrowth. Reactome:R-HSA-9933238 a dimer of ACTB and ACTL6A/B (which together form the actin-related protein or ARP module linking the catalytic core of the SWI/SNF complex to the core/base module) |
| GO:0140092 bBAF complex | NAS PMID:12368262 Identification of a polymorphic, neuron-specific chromatin r... | ACCEPT | Summary: Beta-actin is experimentally detected in brain-derived BAF complexes. Reason: The externally recovered Results and Figure 3A of PMID:12368262 report beta-actin Western detection in purified mouse-brain and HeLa complexes. This directly supports the complex membership even though a developmental process discussed by the authors is less firmly established. The primary Results are accessible at https://pmc.ncbi.nlm.nih.gov/articles/PMC187451/; the local extraction contains the abstract and Discussion but omits this Western-blot passage. The Reactome description independently names ACTB in the ACTBβACTL6A/B module. Supporting Evidence: Reactome:R-HSA-9933238 a dimer of ACTB and ACTL6A/B (which together form the actin-related protein or ARP module linking the catalytic core of the SWI/SNF complex to the core/base module) |
| GO:0140288 GBAF complex | NAS PMID:29374058 Glioma tumor suppressor candidate region gene 1 (GLTSCR1) an... | ACCEPT | Summary: ACTB contributes to the GLTSCR1-containing GBAF assembly. Reason: PMID:29374058 defines GBAF and distinguishes it from canonical BAF/PBAF; Reactome:R-HSA-9933236 describes the ACTBβACTL6-containing module. Retain membership without assuming all SWI/SNF subunits occur in every assembly. Supporting Evidence: PMID:29374058 Even without these subunits, GBAF displayed in vitro ATPase activity and bulk chromatin affinity comparable to those of BAF. Reactome:R-HSA-9933238 a dimer of ACTB and ACTL6A/B (which together form the actin-related protein or ARP module linking the catalytic core of the SWI/SNF complex to the core/base module) Reactome:R-HSA-9933236 a dimer of ACTB and ACTL6A/B/C (which together form the actin-related protein or ARP module linking the catalytic core of the SWI/SNF complex to the core/base module) |
| GO:1902459 positive regulation of stem cell population maintenance | NAS PMID:19279220 An embryonic stem cell chromatin remodeling complex, esBAF, ... | KEEP AS NON CORE | Summary: esBAF supports stem-cell self-renewal and pluripotency. Reason: PMID:19279220 establishes specialized mouse esBAF composition and its requirement in the stem-cell state. Structural ACTB contribution to the complex supports this contextual process, without converting an esBAF-specific effect into a universal ACTB activity. Supporting Evidence: PMID:19279220 Here, we show that BAF complexes are required for the self-renewal and pluripotency of mouse ES cells but not for the proliferation of fibroblasts or other cells. Reactome:R-HSA-9933238 a dimer of ACTB and ACTL6A/B (which together form the actin-related protein or ARP module linking the catalytic core of the SWI/SNF complex to the core/base module) |
| GO:1902459 positive regulation of stem cell population maintenance | NAS PMID:30510198 A non-canonical BRD9-containing BAF chromatin remodeling com... | KEEP AS NON CORE | Summary: GBAF maintains a naive pluripotency program in mouse embryonic stem cells. Reason: PMID:30510198 connects complex recruitment to the transcriptional network maintaining naive pluripotency. ACTB supplies complex structure; BRD9/BRD4-dependent targeting remains a property of the corresponding subunits. Supporting Evidence: PMID:30510198 GBAF and esBAF complexes are targeted to different genomic features, with GBAF co-localizing with key regulators of naive pluripotency, which is consistent with its specific function in maintaining naive pluripotency gene expression. Reactome:R-HSA-9933238 a dimer of ACTB and ACTL6A/B (which together form the actin-related protein or ARP module linking the catalytic core of the SWI/SNF complex to the core/base module) |
| GO:1905168 positive regulation of double-strand break repair via homologous recombination | IDA PMID:27153538 The TIP60 Complex Regulates Bivalent Chromatin Recognition b... | KEEP AS NON CORE | Summary: TIP60-complex activity supports homologous-recombination repair in the tested chromatin context. Reason: The recovered full primary Results of PMID:27153538 include repair reporters and competition between chromatin marks. Retain the curated contextual contribution of ACTB-containing TIP60 complexes, without ascribing MBTD1 histone reading or KAT5 acetylation to ACTB. Supporting Evidence: PMID:27153538 MBTD1 allows TIP60 to associate with specific gene promoters and to promote the repair of DNA double-strand breaks by homologous recombination. |
| 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... | KEEP AS NON CORE | Summary: Rb-associated SWI/SNF regulates cell-cycle transcription at G1/S. Reason: PMID:10778858 links HDACβRbβSWI/SNF complexes to cyclin E/A repression and ordered progression. ACTB contributes to the remodeling machinery used in that regulation; the direction depends on the assembled repressor and cell-cycle stage. Supporting Evidence: PMID:10778858 Rb forms a repressor containing histone deacetylase (HDAC) and the hSWI/SNF nucleosome remodeling complex, which inhibits transcription of genes for cyclins E and A and arrests cells in the G1 phase of the cell cycle. Reactome:R-HSA-9933238 a dimer of ACTB and ACTL6A/B (which together form the actin-related protein or ARP module linking the catalytic core of the SWI/SNF complex to the core/base module) |
| GO:2000779 regulation of double-strand break repair | NAS PMID:14966270 Structural and functional conservation of the NuA4 histone a... | KEEP AS NON CORE | Summary: The ACTB-containing TIP60 complex contributes to double-strand-break repair. Reason: PMID:14966270 identifies the conserved human NuA4 assembly and discusses its double-strand-break repair context. The earlier primary PMID:10966108 reports that a catalytically inactive TIP60 complex impairs double-strand-break repair and apoptotic competence. Retain the NAS complex-level process as contextual structural participation, without assigning TIP60 acetyltransferase chemistry or a universal regulatory direction to ACTB. Supporting Evidence: PMID:14966270 Tip60 and its splice variant Tip60b/PLIP were purified as stable HAT complexes associated with identical polypeptides |
| GO:2000781 positive regulation of double-strand break repair | NAS PMID:16932743 Mammalian SWI/SNF complexes facilitate DNA double-strand bre... | KEEP AS NON CORE | Summary: SWI/SNF promotes DNA-break repair through chromatin remodeling. Reason: PMID:16932743 shows recruitment near breaks, impaired H2AX phosphorylation and inefficient repair when remodeling activity is disrupted. ACTB contributes structural support to this complex; it is not the kinase phosphorylating H2AX. Supporting Evidence: PMID:16932743 these results suggest that the SWI/SNF complexes facilitate DSB repair, at least in part, by promoting H2AX phosphorylation by directly acting on chromatin. Reactome:R-HSA-9933238 a dimer of ACTB and ACTL6A/B (which together form the actin-related protein or ARP module linking the catalytic core of the SWI/SNF complex to the core/base module) |
| GO:2000781 positive regulation of double-strand break repair | NAS PMID:25066234 Requirement for PBAF in transcriptional repression and repai... | KEEP AS NON CORE | Summary: PBAF promotes repair in actively transcribed regions by silencing transcription near breaks. Reason: PMID:25066234 links PBAF-mediated local silencing to early repair of a subset of double-strand breaks. ACTBβs complex contribution supports the contextual process without claiming a repair-enzyme active site in actin. Supporting Evidence: PMID:25066234 the PBAF remodeling complex is important for DSB-induced transcriptional silencing and promotes repair of a subset of DNA DSBs at early time points, which can be rescued by inhibiting transcription globally. Reactome:R-HSA-9933238 a dimer of ACTB and ACTL6A/B (which together form the actin-related protein or ARP module linking the catalytic core of the SWI/SNF complex to the core/base module) |
| GO:2000819 regulation of nucleotide-excision repair | NAS PMID:12215535 The SWI/SNF chromatin-remodeling factor stimulates repair by... | UNDECIDED | Summary: Remodeling-assisted excision repair is demonstrated, but the transfer to human ACTB remains unresolved. Reason: The full Methods of PMID:12215535 use yeast SWI/SNF with six purified human excision-repair factors. The experiment establishes complex-assisted lesion access; it is not a direct human ACTB assay. The NAS transfer and complex-composition scope need resolution before an ACTB assignment can be adjudicated. Supporting Evidence: PMID:12215535 The SWI/SNF chromatin-remodeling factor stimulates repair by human excision nuclease in the mononucleosome core particle. |
| GO:0030235 nitric-oxide synthase regulator activity | IDA PMID:17502619 beta-Actin regulates platelet nitric oxide synthase 3 activi... | KEEP AS NON CORE | Summary: G-actin regulates NOS3 activity in human platelets. Reason: PMID:17502619 reports NOS3 association with G-actin and increased NO/cGMP output dependent on Hsp90. The monomeric-state and platelet context matter; ACTB is a regulator rather than the nitric-oxide-producing enzyme. Supporting Evidence: PMID:17502619 Formation of this ternary complex among NOS-3, globular beta-actin, and Hsp90, in turn, results in an increase in both NOS activity and cyclic guanosine-3',5'-monophosphate |
| GO:0007010 cytoskeleton organization | ISS GO_REF:0000024 | ACCEPT | Summary: ACTB contributes structural material to cytoskeletal organization. Reason: The ISS donor is rat Actb P60711. Conserved cytoplasmic actin polymerization and target human junctional experiments (PMID:22855531) support actual organization of the network, not merely a phenotype following protein depletion. Propagation Review Root cause: NO FAILURE CORE Sources checked: UniProtKB:P60711 SUPPORTS TRANSFER Rat Actb is the source; conserved filament-forming structural work supports transfer. |
| GO:0141108 transporter regulator activity | IGI PMID:18331289 Regulated interactions of the norepineprhine transporter by ... | KEEP AS NON CORE | Summary: Actin-dependent interactions regulate norepinephrine-transporter function. Reason: PMID:18331289 examines the actinβalpha-synucleinβNET system with transporter uptake and cytoskeletal perturbations. Effects depend on alpha-synuclein dosage and preparation, so the general transporter-regulator term is appropriate without a universal activating or inhibiting sign. Supporting Evidence: PMID:18331289 Protein interactions between NET, beta-actin, and alpha-Syn were modified, along with levels of surface transporters. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5250947 | ACCEPT | Summary: The curated event places ACTB in the nucleoplasm. Reason: Reactome:R-HSA-5250947 describes a context in which B-WICH-associated actin and MYO1C participate in nuclear transcriptional machinery. Retain the eventβs compartment resolution. Actin can be monomeric or polymeric here; membership does not transfer a partnerβs kinase, GTPase, motor or acetyltransferase chemistry to ACTB. Supporting Evidence: Reactome:R-HSA-5250947 Active rRNA genes are bound by the BβWICH multiprotein complex (Cavellan et al. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5689544 | ACCEPT | Summary: The curated event places ACTB in the nucleoplasm. Reason: Reactome:R-HSA-5689544 describes a context in which INO80-associated nuclear actin is present in the complex context of UCHL5 regulation. Retain the eventβs compartment resolution. Actin can be monomeric or polymeric here; membership does not transfer a partnerβs kinase, GTPase, motor or acetyltransferase chemistry to ACTB. Supporting Evidence: Reactome:R-HSA-5689544 The C-terminal extension of UCHL5 (UCH37) binds NFRKB within the INO80 chromatin remodeling complex (Yao et al. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9825847 | ACCEPT | Summary: The curated event places ACTB in the nucleoplasm. Reason: Reactome:R-HSA-9825847 describes a context in which MITF engages nuclear SWI/SNF machinery containing the actin-related module. Retain the eventβs compartment resolution. Actin can be monomeric or polymeric here; membership does not transfer a partnerβs kinase, GTPase, motor or acetyltransferase chemistry to ACTB. Supporting Evidence: Reactome:R-HSA-9825847 MITF-M binds to the promoter of the TYRP1 gene to stimulate expression as assessed by reporter gene assay, electrophoretic mobility shift assay (EMSA) and chromatin immunoprecipitation (ChIP) (Bertolotto et al, 1998a, b; Fang et al, 2002; De la Serna et al, 2006; reviewed in Cheli et al, 2010). |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9933236 | ACCEPT | Summary: The curated event places ACTB in the nucleoplasm. Reason: Reactome:R-HSA-9933236 describes a context in which the GBAF ATPase module includes an ACTBβACTL6 dimer linking catalytic and core modules. Retain the eventβs compartment resolution. Actin can be monomeric or polymeric here; membership does not transfer a partnerβs kinase, GTPase, motor or acetyltransferase chemistry to ACTB. Supporting Evidence: Reactome:R-HSA-9933236 Isolation of SMARC4A-containing complexes suggests that the ATPase module of cBAF, pBAF and ncBAF complexes exist as discrete, isolatable complexes. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9933237 | ACCEPT | Summary: The curated event places ACTB in the nucleoplasm. Reason: Reactome:R-HSA-9933237 describes a context in which the PBAF ATPase module contains the ACTBβACTL6 structural linkage. Retain the eventβs compartment resolution. Actin can be monomeric or polymeric here; membership does not transfer a partnerβs kinase, GTPase, motor or acetyltransferase chemistry to ACTB. Supporting Evidence: Reactome:R-HSA-9933237 Cryo-EM studies of the pBAF complex bound to a nucleosome support a model where the catalytic core of the complex SMARCA2/4, is linked to the core or base module through a regulatory actin-related protein (ARP) module consisting of ACTB and ACTL6 that interacts with the HSA (helicase-SANT-associated) region of SMARCA2/3 (Yuan et al, 2022; Wang et al, 2022; He et al, 2020). |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9933238 | ACCEPT | Summary: The curated event places ACTB in the nucleoplasm. Reason: Reactome:R-HSA-9933238 describes a context in which the BAF ATPase module contains the ACTBβACTL6 structural linkage. Retain the eventβs compartment resolution. Actin can be monomeric or polymeric here; membership does not transfer a partnerβs kinase, GTPase, motor or acetyltransferase chemistry to ACTB. Supporting Evidence: Reactome:R-HSA-9933238 Isolation of SMARC4A-containing complexes suggests that the ATPase module of cBAF, pBAF and ncBAF complexes exist as discrete, isolatable complexes. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9934021 | ACCEPT | Summary: The curated event places ACTB in the nucleoplasm. Reason: Reactome:R-HSA-9934021 describes a context in which neural-progenitor BAF assembly includes nuclear actin. Retain the eventβs compartment resolution. Actin can be monomeric or polymeric here; membership does not transfer a partnerβs kinase, GTPase, motor or acetyltransferase chemistry to ACTB. 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). |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9934024 | ACCEPT | Summary: The curated event places ACTB in the nucleoplasm. Reason: Reactome:R-HSA-9934024 describes a context in which embryonic-stem-cell BAF assembly includes the actin-related structural module. Retain the eventβs compartment resolution. Actin can be monomeric or polymeric here; membership does not transfer a partnerβs kinase, GTPase, motor or acetyltransferase chemistry to ACTB. Supporting Evidence: Reactome:R-HSA-9934024 The ATPase module of the esBAF complex contains SMARCA4/BRG1 to the exclusion of SMARCA2/BRM (Zhang et al, 2014; Ho et al, 2009; reviewed in Kadoch and Crabtree, 2015; Innis and Cabot, 2020 Cenik and Shilatifard, 2021). |
| GO:0005654 nucleoplasm | TAS Reactome:R-NUL-4551334 | ACCEPT | Summary: The curated event places ACTB in the nucleoplasm. Reason: Reactome:R-NUL-4551334 describes a context in which NuA4 contains ACTB while histone acetylation is performed by its catalytic subunit. Retain the eventβs compartment resolution. Actin can be monomeric or polymeric here; membership does not transfer a partnerβs kinase, GTPase, motor or acetyltransferase chemistry to ACTB. Supporting Evidence: Reactome:R-NUL-4551334 The NuA4 complex contains the histone acetyltransferase (HAT) KAT5 (TIP60), a member of the MYST family. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1861595 | ACCEPT | Summary: The curated event places ACTB in the cytosol. Reason: Reactome:R-HSA-1861595 describes a context in which myosin-X engages the cytoplasmic actin network. Retain the eventβs compartment resolution. Actin can be monomeric or polymeric here; membership does not transfer a partnerβs kinase, GTPase, motor or acetyltransferase chemistry to ACTB. Supporting Evidence: Reactome:R-HSA-1861595 Myosin-X (Myosin 10) is one of the downstream effectors of PI3K in FCGR-phagocytosis and is involved in pseudopod extension and closure of phagocytic cups. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2029466 | ACCEPT | Summary: The curated event places ACTB in the cytosol. Reason: Reactome:R-HSA-2029466 describes a context in which WASP/Arp2/3 interactions recruit actin for filament assembly. Retain the eventβs compartment resolution. Actin can be monomeric or polymeric here; membership does not transfer a partnerβs kinase, GTPase, motor or acetyltransferase chemistry to ACTB. Supporting Evidence: Reactome:R-HSA-2029466 Once activated, the ARP2/3 complex nucleates new actin filaments that extend from the sides of pre-existing mother actin filaments at a 70-degree angle to form Y-branched networks (Firat-Karalar & Welch 2010). |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2029473 | ACCEPT | Summary: The curated event places ACTB in the cytosol. Reason: Reactome:R-HSA-2029473 describes a context in which actin supplies polymer subunits in branching and elongation. Retain the eventβs compartment resolution. Actin can be monomeric or polymeric here; membership does not transfer a partnerβs kinase, GTPase, motor or acetyltransferase chemistry to ACTB. Supporting Evidence: Reactome:R-HSA-2029473 ATP bound G-actin monomers are added to the fast growing barbed ends of both mother and daughter filaments. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2029476 | ACCEPT | Summary: The curated event places ACTB in the cytosol. Reason: Reactome:R-HSA-2029476 describes a context in which actin filaments provide a substrate for myosin-dependent phagosome movement. Retain the eventβs compartment resolution. Actin can be monomeric or polymeric here; membership does not transfer a partnerβs kinase, GTPase, motor or acetyltransferase chemistry to ACTB. Supporting Evidence: Reactome:R-HSA-2029476 In addition to the membrane remodeling for pseudopod extension, particle internalization requires a contractility force pulling the forming phagosome into the cytoplasm. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-203070 | ACCEPT | Summary: The curated event places ACTB in the cytosol. Reason: Reactome:R-HSA-203070 describes a context in which profilin binds cytoplasmic monomeric actin. Retain the eventβs compartment resolution. Actin can be monomeric or polymeric here; membership does not transfer a partnerβs kinase, GTPase, motor or acetyltransferase chemistry to ACTB. Supporting Evidence: Reactome:R-HSA-203070 Profilins PFN1 and PFN2 bind to monomeric actin (G-actin), forming a 1:1 complex and subsequently regulate actin filament barbed end assembly downstream of various signaling pathways (Pring et al. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2197690 | ACCEPT | Summary: The curated event places ACTB in the cytosol. Reason: Reactome:R-HSA-2197690 describes a context in which WASP dissociation occurs in the context of assembled cytoplasmic actin machinery. Retain the eventβs compartment resolution. Actin can be monomeric or polymeric here; membership does not transfer a partnerβs kinase, GTPase, motor or acetyltransferase chemistry to ACTB. Supporting Evidence: Reactome:R-HSA-2197690 After incorporation at the branch, the actin bound to VCA domain of WASP/WAVE undergoes ATP hydrolysis and this destabilizes its interaction with WASP/WAVE. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-392751 | ACCEPT | Summary: The curated event places ACTB in the cytosol. Reason: Reactome:R-HSA-392751 describes a context in which L1/ankyrin signaling engages the cortical actin network. Retain the eventβs compartment resolution. Actin can be monomeric or polymeric here; membership does not transfer a partnerβs kinase, GTPase, motor or acetyltransferase chemistry to ACTB. Supporting Evidence: Reactome:R-HSA-392751 Ankyrins are bifunctional linker proteins that tether L1 to the membrane associated, spectrin based actin cytoskeleton. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-3928595 | ACCEPT | Summary: The curated event places ACTB in the cytosol. Reason: Reactome:R-HSA-3928595 describes a context in which N-WASP recruits actin-polymerization machinery. Retain the eventβs compartment resolution. Actin can be monomeric or polymeric here; membership does not transfer a partnerβs kinase, GTPase, motor or acetyltransferase chemistry to ACTB. Supporting Evidence: Reactome:R-HSA-3928595 Once neural Wiskott-Aldrich syndrome protein (WASL, N-WASP) is activated its VCA region becomes available for binding to actin-related protein (ARP2/3) complex and actin monomer. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-430347 | ACCEPT | Summary: The curated event places ACTB in the cytosol. Reason: Reactome:R-HSA-430347 describes a context in which migfilin connects adhesion-associated proteins to cytoplasmic actin structures. Retain the eventβs compartment resolution. Actin can be monomeric or polymeric here; membership does not transfer a partnerβs kinase, GTPase, motor or acetyltransferase chemistry to ACTB. Supporting Evidence: Reactome:R-HSA-430347 Migfilin associates with actin filaments as a result of its interaction with filamin (Tu et al., 2003). |
| GO:0005829 cytosol | TAS Reactome:R-HSA-443779 | ACCEPT | Summary: The curated event places ACTB in the cytosol. Reason: Reactome:R-HSA-443779 describes a context in which L1-dependent treadmilling uses cytoplasmic actin. Retain the eventβs compartment resolution. Actin can be monomeric or polymeric here; membership does not transfer a partnerβs kinase, GTPase, motor or acetyltransferase chemistry to ACTB. Supporting Evidence: Reactome:R-HSA-443779 The COOH termini of all ERM proteins have sequence motifs that bind directly to F-actin. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-445089 | ACCEPT | Summary: The curated event places ACTB in the cytosol. Reason: Reactome:R-HSA-445089 describes a context in which L1 phosphorylation-state changes affect coupling to the actin network. Retain the eventβs compartment resolution. Actin can be monomeric or polymeric here; membership does not transfer a partnerβs kinase, GTPase, motor or acetyltransferase chemistry to ACTB. Supporting Evidence: Reactome:R-HSA-445089 L1 translocated to the non raft membranes of the C-domain is dephosphorylated. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5218916 | ACCEPT | Summary: The curated event places ACTB in the cytosol. Reason: Reactome:R-HSA-5218916 describes a context in which HSP27 modulates actin assembly in the cytoplasmic network. Retain the eventβs compartment resolution. Actin can be monomeric or polymeric here; membership does not transfer a partnerβs kinase, GTPase, motor or acetyltransferase chemistry to ACTB. Supporting Evidence: Reactome:R-HSA-5218916 Activated MAP kinase-activated protein kinase (MAPK/MAPKAPK) 2 and 3 in turn phosphorylate heat shock protein beta 1 (HSPB1, HSP27). |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5626507 | ACCEPT | Summary: The curated event places ACTB in the cytosol. Reason: Reactome:R-HSA-5626507 describes a context in which IQGAP associates with cytoplasmic actin structures. Retain the eventβs compartment resolution. Actin can be monomeric or polymeric here; membership does not transfer a partnerβs kinase, GTPase, motor or acetyltransferase chemistry to ACTB. Supporting Evidence: Reactome:R-HSA-5626507 IQGAP proteins IQGAP1, IQGAP2 and IQGAP3 bind F-actin filaments through their calponin homology (CH) domain (Pelikan-Conchaudron et al. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5665751 | ACCEPT | Summary: The curated event places ACTB in the cytosol. Reason: Reactome:R-HSA-5665751 describes a context in which FMNL2 promotes actin assembly in the cytosol. Retain the eventβs compartment resolution. Actin can be monomeric or polymeric here; membership does not transfer a partnerβs kinase, GTPase, motor or acetyltransferase chemistry to ACTB. Supporting Evidence: Reactome:R-HSA-5665751 Once activated by binding to GTP-bound CDC42, FMNL2 interacts with actin bound profilin(s) and drives elongation but not nucleation of actin filaments (Block et al. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5665767 | ACCEPT | Summary: The curated event places ACTB in the cytosol. Reason: Reactome:R-HSA-5665767 describes a context in which FMNL3 promotes actin assembly in the cytosol. Retain the eventβs compartment resolution. Actin can be monomeric or polymeric here; membership does not transfer a partnerβs kinase, GTPase, motor or acetyltransferase chemistry to ACTB. Supporting Evidence: Reactome:R-HSA-5665767 Activated FMNL3 (presumably associated with RHOC:GTP) has the ability to directly bind G-actin through knob and coiled-coil subdomains of the FMNL3 FH2 domain. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5665802 | ACCEPT | Summary: The curated event places ACTB in the cytosol. Reason: Reactome:R-HSA-5665802 describes a context in which SRGAP2 signaling is coupled to the cytoplasmic actin network. Retain the eventβs compartment resolution. Actin can be monomeric or polymeric here; membership does not transfer a partnerβs kinase, GTPase, motor or acetyltransferase chemistry to ACTB. Supporting Evidence: Reactome:R-HSA-5665802 SRGAP2 binds FMNL1 activated by RAC1:GTP by simultaneously interacting with RAC1 and FMNL1. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5665809 | ACCEPT | Summary: The curated event places ACTB in the cytosol. Reason: Reactome:R-HSA-5665809 describes a context in which Rac GTPase regulation controls actin-network organization. Retain the eventβs compartment resolution. Actin can be monomeric or polymeric here; membership does not transfer a partnerβs kinase, GTPase, motor or acetyltransferase chemistry to ACTB. Supporting Evidence: Reactome:R-HSA-5665809 SRGAP2 is a GTPase activating protein that stimulates the GTPase activity of RAC1 bound to FMNL1. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5665982 | ACCEPT | Summary: The curated event places ACTB in the cytosol. Reason: Reactome:R-HSA-5665982 describes a context in which DIAPH1/EVL/MKL interactions involve actin assemblies and actin-responsive signaling. Retain the eventβs compartment resolution. Actin can be monomeric or polymeric here; membership does not transfer a partnerβs kinase, GTPase, motor or acetyltransferase chemistry to ACTB. Supporting Evidence: Reactome:R-HSA-5665982 Once activated by binding to RHOA:GTP, DIAPH1 binds profilin:G-actin complexes together with EVL (VASP) homotetramers and promotes elongation of actin filaments (Copeland and Treisman 2002, Grosse et al. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5666001 | ACCEPT | Summary: The curated event places ACTB in the cytosol. Reason: Reactome:R-HSA-5666001 describes a context in which profilin/MKL interactions involve soluble actin and its regulated availability. Retain the eventβs compartment resolution. Actin can be monomeric or polymeric here; membership does not transfer a partnerβs kinase, GTPase, motor or acetyltransferase chemistry to ACTB. Supporting Evidence: Reactome:R-HSA-5666001 MKL1 (MAL) transcription cofactor is negatively regulated by binding to nonpolymerized actin (G-actin) (Miralles et al. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9666458 | ACCEPT | Summary: The curated event places ACTB in the cytosol. Reason: Reactome:R-HSA-9666458 describes a context in which Leishmania-associated remodeling involves host cytoplasmic actin. Retain the eventβs compartment resolution. Actin can be monomeric or polymeric here; membership does not transfer a partnerβs kinase, GTPase, motor or acetyltransferase chemistry to ACTB. Supporting Evidence: Reactome:R-HSA-9666458 In addition to the membrane remodeling for pseudopod extension, particle internalization requires a contractility force pulling the forming phagosome into the cytoplasm. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9914537 | ACCEPT | Summary: The curated event places ACTB in the cytosol. Reason: Reactome:R-HSA-9914537 describes a context in which dystrophin-associated glycoprotein complexes anchor cytoplasmic actin to the membrane. Retain the eventβs compartment resolution. Actin can be monomeric or polymeric here; membership does not transfer a partnerβs kinase, GTPase, motor or acetyltransferase chemistry to ACTB. Supporting Evidence: Reactome:R-HSA-9914537 Alpha-dystroglycan (DAG1(30-653)) binds G domain-like sequences in other extracellular matrix molecules such as AGRN (agrin) (Gee et al. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9934294 | ACCEPT | Summary: The curated event places ACTB in the cytosol. Reason: Reactome:R-HSA-9934294 describes a context in which E-cadherin adhesion complexes engage cytoplasmic actin. Retain the eventβs compartment resolution. Actin can be monomeric or polymeric here; membership does not transfer a partnerβs kinase, GTPase, motor or acetyltransferase chemistry to ACTB. Supporting Evidence: Reactome:R-HSA-9934294 Vinculin (VCL) was first shown to be recruited to the CDH1 complex through its interaction with CTNNA1 (alpha-catenin) in human colon carcinoma cell line (Watabe-Uchida et al. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9934410 | ACCEPT | Summary: The curated event places ACTB in the cytosol. Reason: Reactome:R-HSA-9934410 describes a context in which E-cadherin trans-dimer context includes the cortical actin network without requiring actin for the initiating trans interaction. Retain the eventβs compartment resolution. Actin can be monomeric or polymeric here; membership does not transfer a partnerβs kinase, GTPase, motor or acetyltransferase chemistry to ACTB. Supporting Evidence: Reactome:R-HSA-9934410 CDH1 (E-cadherin) forms a homotypic trans-complex with CDH1 presented on the plasma membrane of a neighbouring cell, where two CDH1 molecules interact through their extracellular domains in a calcium (Ca2+)-dependent manner and catenin-dependent manner (Chitaev and Troyanovski 1998). |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9934486 | ACCEPT | Summary: The curated event places ACTB in the cytosol. Reason: Reactome:R-HSA-9934486 describes a context in which E-cadherin junction organization is coupled to cytoplasmic actin. Retain the eventβs compartment resolution. Actin can be monomeric or polymeric here; membership does not transfer a partnerβs kinase, GTPase, motor or acetyltransferase chemistry to ACTB. Supporting Evidence: Reactome:R-HSA-9934486 CTNNA1 (alpha-catenin) is responsible for the recruitment of F-actin polymers to the CDH1 complex (Watabe-Uchida et al. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-3928654 | ACCEPT | Summary: The curated event places ACTB in the plasma membrane. Reason: Reactome:R-HSA-3928654 describes a context in which EPH/ephrin internalization uses membrane-associated actin machinery. Retain the eventβs compartment resolution. Actin can be monomeric or polymeric here; membership does not transfer a partnerβs kinase, GTPase, motor or acetyltransferase chemistry to ACTB. Supporting Evidence: Reactome:R-HSA-3928654 During endocytosis the EPH-ephrin (EFN) intact complex and, possibly, associated cytoplasmic proteins, together with the surrounding plasma membrane, can be internalized into the EPH- or EFN-expressing cell. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8868230 | ACCEPT | Summary: The curated event places ACTB in the plasma membrane. Reason: Reactome:R-HSA-8868230 describes a context in which SNX9 couples membrane curvature to actin-dependent pit maturation. Retain the eventβs compartment resolution. Actin can be monomeric or polymeric here; membership does not transfer a partnerβs kinase, GTPase, motor or acetyltransferase chemistry to ACTB. Supporting Evidence: Reactome:R-HSA-8868230 Actin polymerization is not absolutely required for clathrin-mediated endocytosis, and disruption of actin does not interfere with the early stages of clathrin-coated pit formation. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8868236 | ACCEPT | Summary: The curated event places ACTB in the plasma membrane. Reason: Reactome:R-HSA-8868236 describes a context in which BAR-domain proteins and dynamin work with membrane-associated actin during endocytosis. Retain the eventβs compartment resolution. Actin can be monomeric or polymeric here; membership does not transfer a partnerβs kinase, GTPase, motor or acetyltransferase chemistry to ACTB. Supporting Evidence: Reactome:R-HSA-8868236 Dynamin is a large GTPase whose GTP hydrolysis activity is required for the scission of clathrin-coated vesicles from the plasma membrane (reviewed in Ferguson and De Camilli, 2012). |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8868648 | ACCEPT | Summary: The curated event places ACTB in the plasma membrane. Reason: Reactome:R-HSA-8868648 describes a context in which synaptojanin-mediated lipid remodeling occurs around actin-associated endocytic structures. Retain the eventβs compartment resolution. Actin can be monomeric or polymeric here; membership does not transfer a partnerβs kinase, GTPase, motor or acetyltransferase chemistry to ACTB. Supporting Evidence: Reactome:R-HSA-8868648 Inositol-5-phosphatases like SYNJs and OCRL hydrolyze PI(4,5)P2 to PI(4)P. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8868651 | ACCEPT | Summary: The curated event places ACTB in the plasma membrane. Reason: Reactome:R-HSA-8868651 describes a context in which synaptojanin recruitment occurs at actin-associated membrane trafficking sites. Retain the eventβs compartment resolution. Actin can be monomeric or polymeric here; membership does not transfer a partnerβs kinase, GTPase, motor or acetyltransferase chemistry to ACTB. Supporting Evidence: Reactome:R-HSA-8868651 Synaptojanin (SYNJ) 1 and 2 are inositol-5-phosphatases that sequentially convert PI(4,5)P2 to PI(4)P and PI (Cremona et al 1999; reviewed in Billcliff and Lowe, 2014). |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8868658 | ACCEPT | Summary: The curated event places ACTB in the plasma membrane. Reason: Reactome:R-HSA-8868658 describes a context in which HSPA-mediated uncoating occurs in a membrane-trafficking assembly with actin. Retain the eventβs compartment resolution. Actin can be monomeric or polymeric here; membership does not transfer a partnerβs kinase, GTPase, motor or acetyltransferase chemistry to ACTB. Supporting Evidence: Reactome:R-HSA-8868658 HSPA8 hydrolyzes ATP to promote dissociation of the clathrin coat from the vesicle (reviewed in Sousa and Lafer, 2015). |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8868659 | ACCEPT | Summary: The curated event places ACTB in the plasma membrane. Reason: Reactome:R-HSA-8868659 describes a context in which auxilin recruitment occurs in the actin-associated endocytic machinery. Retain the eventβs compartment resolution. Actin can be monomeric or polymeric here; membership does not transfer a partnerβs kinase, GTPase, motor or acetyltransferase chemistry to ACTB. Supporting Evidence: Reactome:R-HSA-8868659 After fission from the plasma membrane, auxilin proteins DNAJC6 and GAK are recruited to the vesicle through interaction with clathrin and phosphoinositides, in particular PI4P (Greener et al, 2000; Lee et al, 2006; Massol et al, 2006; Taylor et al, 2011; Scheele et al, 2001; Fotin et al, 2004a; Fotin et al, 2004b; Guan et al, 2010; reviewed in McMahon and Boucrot, 2011; Sousa and Lafer, 2015). |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8868660 | ACCEPT | Summary: The curated event places ACTB in the plasma membrane. Reason: Reactome:R-HSA-8868660 describes a context in which HSPA recruitment occurs around the actin-associated endocytic apparatus. Retain the eventβs compartment resolution. Actin can be monomeric or polymeric here; membership does not transfer a partnerβs kinase, GTPase, motor or acetyltransferase chemistry to ACTB. Supporting Evidence: Reactome:R-HSA-8868660 HSPA8 (also known as HSC70) is recruited to the clathrin-coated vesicle through interaction with DNA J proteins GAK and DNAJC6 (Rapoport et al, 2008; Xing et al, 2010; reviewed in Sousa and Lafer, 2015). |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8868661 | ACCEPT | Summary: The curated event places ACTB in the plasma membrane. Reason: Reactome:R-HSA-8868661 describes a context in which dynamin-dependent fission is coupled to the endocytic actin network. Retain the eventβs compartment resolution. Actin can be monomeric or polymeric here; membership does not transfer a partnerβs kinase, GTPase, motor or acetyltransferase chemistry to ACTB. Supporting Evidence: Reactome:R-HSA-8868661 Self-assembly of dynamin around the neck of the emerging clathrin-coated vesicle stimulates its GTPase activity. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8869438 | ACCEPT | Summary: The curated event places ACTB in the plasma membrane. Reason: Reactome:R-HSA-8869438 describes a context in which endocytic-complex dissociation includes previously membrane-associated actin machinery. Retain the eventβs compartment resolution. Actin can be monomeric or polymeric here; membership does not transfer a partnerβs kinase, GTPase, motor or acetyltransferase chemistry to ACTB. Supporting Evidence: Reactome:R-HSA-8869438 After the removal of the clathrin coat, it is likely that many of the proteins that contributed to vesicle formation are lost, although the timing and mechanism of this step are poorly understood (reviewed in McMahon and Boucrot, 2011; Lemmon, 2001). |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8871193 | ACCEPT | Summary: The curated event places ACTB in the plasma membrane. Reason: Reactome:R-HSA-8871193 describes a context in which AAK1/AP2 regulation occurs in an actin-associated coated-pit context. Retain the eventβs compartment resolution. Actin can be monomeric or polymeric here; membership does not transfer a partnerβs kinase, GTPase, motor or acetyltransferase chemistry to ACTB. Supporting Evidence: Reactome:R-HSA-8871193 GAPVD1 binds the alpha adaptin ear domain of AP-2 mu2, activating its RAB5-directed GEF activity and displacing AAK1. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8871194 | ACCEPT | Summary: The curated event places ACTB in the plasma membrane. Reason: Reactome:R-HSA-8871194 describes a context in which RAB5/AP2-dependent trafficking involves the membrane-associated actin network. Retain the eventβs compartment resolution. Actin can be monomeric or polymeric here; membership does not transfer a partnerβs kinase, GTPase, motor or acetyltransferase chemistry to ACTB. Supporting Evidence: Reactome:R-HSA-8871194 RAB5 is a small GTPase that is implicated in clathrin-mediated endocytosis (Chavrier et al, 1990; McLauchlan et al, 1998; Shin et al, 2002; Taylor et al, 2011; reviewed in Stenmark, 2009; Wandiger-Ness and Zerial, 2014). |
| GO:0098871 postsynaptic actin cytoskeleton | IDA PMID:18341992 The subspine organization of actin fibers regulates the stru... | KEEP AS NON CORE | Summary: Beta-actin is a structural component of the postsynaptic spine network. Reason: PMID:18341992 uses photoactivatable GFPβbeta-actin in rat CA1 hippocampal slices to distinguish dynamic and stable actin pools and connect remodeling to spine shape and plasticity. Retain postsynaptic actin cytoskeleton in this neuronal context. The specific postsynaptic structural activity is supported; general cytoskeletal activity elsewhere does not negate it. Full construct details are not inferred beyond the available report. Supporting Evidence: PMID:18341992 Using two-photon photoactivation of green fluorescent protein fused to beta-actin, we found that a dynamic pool of F-actin at the tip of the spine quickly treadmilled to generate an expansive force. |
| GO:0098871 postsynaptic actin cytoskeleton | IMP PMID:18341992 The subspine organization of actin fibers regulates the stru... | KEEP AS NON CORE | Summary: Beta-actin is a structural component of the postsynaptic spine network. Reason: PMID:18341992 uses photoactivatable GFPβbeta-actin in rat CA1 hippocampal slices to distinguish dynamic and stable actin pools and connect remodeling to spine shape and plasticity. Retain postsynaptic actin cytoskeleton in this neuronal context. The specific postsynaptic structural activity is supported; general cytoskeletal activity elsewhere does not negate it. Full construct details are not inferred beyond the available report. Supporting Evidence: PMID:18341992 Using two-photon photoactivation of green fluorescent protein fused to beta-actin, we found that a dynamic pool of F-actin at the tip of the spine quickly treadmilled to generate an expansive force. |
| GO:0098973 structural constituent of postsynaptic actin cytoskeleton | IDA PMID:18341992 The subspine organization of actin fibers regulates the stru... | KEEP AS NON CORE | Summary: Beta-actin is a structural component of the postsynaptic spine network. Reason: PMID:18341992 uses photoactivatable GFPβbeta-actin in rat CA1 hippocampal slices to distinguish dynamic and stable actin pools and connect remodeling to spine shape and plasticity. Retain structural constituent of postsynaptic actin cytoskeleton in this neuronal context. The specific postsynaptic structural activity is supported; general cytoskeletal activity elsewhere does not negate it. Full construct details are not inferred beyond the available report. Supporting Evidence: PMID:18341992 Using two-photon photoactivation of green fluorescent protein fused to beta-actin, we found that a dynamic pool of F-actin at the tip of the spine quickly treadmilled to generate an expansive force. |
| GO:0098973 structural constituent of postsynaptic actin cytoskeleton | EXP PMID:18341992 The subspine organization of actin fibers regulates the stru... | KEEP AS NON CORE | Summary: Beta-actin is a structural component of the postsynaptic spine network. Reason: PMID:18341992 uses photoactivatable GFPβbeta-actin in rat CA1 hippocampal slices to distinguish dynamic and stable actin pools and connect remodeling to spine shape and plasticity. Retain structural constituent of postsynaptic actin cytoskeleton in this neuronal context. The specific postsynaptic structural activity is supported; general cytoskeletal activity elsewhere does not negate it. Full construct details are not inferred beyond the available report. Supporting Evidence: PMID:18341992 Using two-photon photoactivation of green fluorescent protein fused to beta-actin, we found that a dynamic pool of F-actin at the tip of the spine quickly treadmilled to generate an expansive force. |
| GO:0098973 structural constituent of postsynaptic actin cytoskeleton | IMP PMID:18341992 The subspine organization of actin fibers regulates the stru... | KEEP AS NON CORE | Summary: Beta-actin is a structural component of the postsynaptic spine network. Reason: PMID:18341992 uses photoactivatable GFPβbeta-actin in rat CA1 hippocampal slices to distinguish dynamic and stable actin pools and connect remodeling to spine shape and plasticity. Retain structural constituent of postsynaptic actin cytoskeleton in this neuronal context. The specific postsynaptic structural activity is supported; general cytoskeletal activity elsewhere does not negate it. Full construct details are not inferred beyond the available report. Supporting Evidence: PMID:18341992 Using two-photon photoactivation of green fluorescent protein fused to beta-actin, we found that a dynamic pool of F-actin at the tip of the spine quickly treadmilled to generate an expansive force. |
| GO:0098978 glutamatergic synapse | IDA PMID:18341992 The subspine organization of actin fibers regulates the stru... | KEEP AS NON CORE | Summary: Beta-actin is a structural component of the postsynaptic spine network. Reason: PMID:18341992 uses photoactivatable GFPβbeta-actin in rat CA1 hippocampal slices to distinguish dynamic and stable actin pools and connect remodeling to spine shape and plasticity. Retain glutamatergic synapse in this neuronal context. The specific postsynaptic structural activity is supported; general cytoskeletal activity elsewhere does not negate it. Full construct details are not inferred beyond the available report. Supporting Evidence: PMID:18341992 Using two-photon photoactivation of green fluorescent protein fused to beta-actin, we found that a dynamic pool of F-actin at the tip of the spine quickly treadmilled to generate an expansive force. |
| GO:0098978 glutamatergic synapse | EXP PMID:18341992 The subspine organization of actin fibers regulates the stru... | KEEP AS NON CORE | Summary: Beta-actin is a structural component of the postsynaptic spine network. Reason: PMID:18341992 uses photoactivatable GFPβbeta-actin in rat CA1 hippocampal slices to distinguish dynamic and stable actin pools and connect remodeling to spine shape and plasticity. Retain glutamatergic synapse in this neuronal context. The specific postsynaptic structural activity is supported; general cytoskeletal activity elsewhere does not negate it. Full construct details are not inferred beyond the available report. Supporting Evidence: PMID:18341992 Using two-photon photoactivation of green fluorescent protein fused to beta-actin, we found that a dynamic pool of F-actin at the tip of the spine quickly treadmilled to generate an expansive force. |
| GO:0098978 glutamatergic synapse | IMP PMID:18341992 The subspine organization of actin fibers regulates the stru... | KEEP AS NON CORE | Summary: Beta-actin is a structural component of the postsynaptic spine network. Reason: PMID:18341992 uses photoactivatable GFPβbeta-actin in rat CA1 hippocampal slices to distinguish dynamic and stable actin pools and connect remodeling to spine shape and plasticity. Retain glutamatergic synapse in this neuronal context. The specific postsynaptic structural activity is supported; general cytoskeletal activity elsewhere does not negate it. Full construct details are not inferred beyond the available report. Supporting Evidence: PMID:18341992 Using two-photon photoactivation of green fluorescent protein fused to beta-actin, we found that a dynamic pool of F-actin at the tip of the spine quickly treadmilled to generate an expansive force. |
| GO:0005515 protein binding | IPI PMID:25255767 Molecular mechanisms of disease-related human Ξ²-actin mutati... | MODIFY | Summary: Human beta-actin interacts functionally with nonmuscle myosin-2A. Reason: The externally read Results and Figure 6 of PMID:25255767 measure actin-dependent activation of nonmuscle myosin-2A ATP turnover with human WT/variant beta-actin preparations. Myosin binding is an informative interaction function supported by this assay. The preparations contain 5β15% endogenous insect actin; ACTBβs own ATP turnover is separately measured in Figure 4. The primary Results/Figure 6 at https://febs.onlinelibrary.wiley.com/doi/10.1111/febs.13068 report approximately 15-fold stimulation of human NM-2A by 30 micromolar WT beta-actin. This externally read functional interaction assay is absent from the local abstract; the general F-actin hydrolysis review does not substitute for it. Proposed replacements: myosin binding Supporting Evidence: |
| GO:0016887 ATP hydrolysis activity | IDA PMID:25255767 Molecular mechanisms of disease-related human Ξ²-actin mutati... | ACCEPT | Summary: Recombinant human beta-actin filaments hydrolyze ATP. Reason: PMID:25255767 Figure 4 reports intrinsic ATP turnover of WT and variant beta-actin filaments using a coupled assay. WT turnover was approximately 2.1 per hour. This is separate from Figure 6βs myosin ATPase assay; the authors report 5β15% insect actin in recombinant preparations. The primary Results and Figure 4 at https://febs.onlinelibrary.wiley.com/doi/10.1111/febs.13068 are externally accessible, but this assay is absent from the local abstract. PMID:3672117 supplies cached actin-family evidence for F-actin ATP hydrolysis, not independent verification of the human kinetic value. Supporting Evidence: PMID:3672117 The hydrolysis reaction occurs on the F-actin subsequent to the polymerization reaction in two steps |
| GO:0006338 chromatin remodeling | HDA PMID:16217013 Heterogeneous nuclear ribonucleoprotein C1/C2, MeCP1, and SW... | ACCEPT | Summary: Actin is present in a chromatin-remodeling assembly purified from K562 cells. Reason: The full PMID:16217013 identifies actin in the 45-kDa band of the LCR-associated remodeling complex by mass spectrometry. Structural ACTB participation in a remodeling assembly supports the process, without assigning all enzymatic activities of LARC to actin. Supporting Evidence: PMID:16217013 The LC-MS/MS analysis of the tryptic digest of the 45-kDa band revealed the presence of actin and requiem |
| GO:0035633 maintenance of blood-brain barrier | NAS PMID:30280653 Blood-Brain Barrier: From Physiology to Disease and Back. | KEEP AS NON CORE | Summary: Junction-associated actin supplies structural support to the blood-brain barrier. Reason: The externally recovered junction section and Figure 2 of PMID:30280653 describe tight-junction coupling to actin filaments through ZO proteins and endothelial cytoskeletal anchoring. This is a statement-level barrier-maintenance context, not an ACTB-specific transport or signaling enzyme assay; retain it as non-core. The primary review section and Figure 2 are accessible at https://pmc.ncbi.nlm.nih.gov/articles/PMC6335099/. The local extraction includes the abstract and Introduction, but omits the actin-containing junction section; a generic endothelial-barrier description is not evidence for actin's structural contribution. Supporting Evidence: |
| GO:0001738 morphogenesis of a polarized epithelium | IMP PMID:22855531 Nonredundant roles of cytoplasmic Ξ²- and Ξ³-actin isoforms in... | KEEP AS NON CORE | Summary: Beta-actin contributes to epithelial morphology and lumen formation. Reason: PMID:22855531 examines human SK-CO15 and Caco-2 BBE epithelial cells with isoform-specific staining and perturbation. Beta-actin depletion disrupts actomyosin organization and three-dimensional cyst morphogenesis. Supporting Evidence: PMID:22855531 Both actin isoforms are essential for normal barrier function of epithelial monolayers, rapid AJ/TJ reassembly, and formation of three-dimensional cysts. |
| GO:0007163 establishment or maintenance of cell polarity | IMP PMID:22855531 Nonredundant roles of cytoplasmic Ξ²- and Ξ³-actin isoforms in... | KEEP AS NON CORE | Summary: Beta-actin supports apicobasal epithelial polarity. Reason: PMID:22855531 examines human SK-CO15 and Caco-2 BBE epithelial cells with isoform-specific staining and perturbation. Beta-actin depletion mislocalizes apical EBP50 and junctional Par3, while beta-catenin becomes abnormally apical. Supporting Evidence: PMID:22855531 Both actin isoforms are essential for normal barrier function of epithelial monolayers, rapid AJ/TJ reassembly, and formation of three-dimensional cysts. |
| GO:0034333 adherens junction assembly | IMP PMID:22855531 Nonredundant roles of cytoplasmic Ξ²- and Ξ³-actin isoforms in... | ACCEPT | Summary: Beta-actin supplies structural support for adherens-junction assembly. Reason: PMID:22855531 examines human SK-CO15 and Caco-2 BBE epithelial cells with isoform-specific staining and perturbation. Isoform-specific perturbations and calcium-repletion experiments connect beta-actin filaments to junction reassembly. Supporting Evidence: PMID:22855531 Both actin isoforms are essential for normal barrier function of epithelial monolayers, rapid AJ/TJ reassembly, and formation of three-dimensional cysts. |
| GO:0043296 apical junction complex | IDA PMID:22855531 Nonredundant roles of cytoplasmic Ξ²- and Ξ³-actin isoforms in... | ACCEPT | Summary: Beta-actin is present at the apical junction complex. Reason: PMID:22855531 examines human SK-CO15 and Caco-2 BBE epithelial cells with isoform-specific staining and perturbation. Beta-actin colocalizes with junctional markers in the apical belt of polarized epithelia. Supporting Evidence: PMID:22855531 Both actin isoforms are essential for normal barrier function of epithelial monolayers, rapid AJ/TJ reassembly, and formation of three-dimensional cysts. |
| GO:0045176 apical protein localization | IMP PMID:22855531 Nonredundant roles of cytoplasmic Ξ²- and Ξ³-actin isoforms in... | KEEP AS NON CORE | Summary: Beta-actin-dependent epithelial structure positions apical proteins. Reason: PMID:22855531 examines human SK-CO15 and Caco-2 BBE epithelial cells with isoform-specific staining and perturbation. Beta-actin depletion disrupts apical EBP50 localization, supporting a contextual protein-localization process. Supporting Evidence: PMID:22855531 Both actin isoforms are essential for normal barrier function of epithelial monolayers, rapid AJ/TJ reassembly, and formation of three-dimensional cysts. |
| GO:0071896 protein localization to adherens junction | IMP PMID:22855531 Nonredundant roles of cytoplasmic Ξ²- and Ξ³-actin isoforms in... | KEEP AS NON CORE | Summary: Beta-actin supports localization of proteins to apical junctions. Reason: PMID:22855531 examines human SK-CO15 and Caco-2 BBE epithelial cells with isoform-specific staining and perturbation. Beta-actin depletion redistributes junctional polarity and adhesion proteins, supporting a structural positioning role. Supporting Evidence: PMID:22855531 Both actin isoforms are essential for normal barrier function of epithelial monolayers, rapid AJ/TJ reassembly, and formation of three-dimensional cysts. |
| GO:0150111 regulation of transepithelial transport | IMP PMID:22855531 Nonredundant roles of cytoplasmic Ξ²- and Ξ³-actin isoforms in... | KEEP AS NON CORE | Summary: Junctional beta-actin contributes to epithelial barrier control. Reason: PMID:22855531 examines human SK-CO15 and Caco-2 BBE epithelial cells with isoform-specific staining and perturbation. Isoform-specific depletion reduces transepithelial electrical resistance and increases dextran flux. ACTB supplies junctional structure that controls paracellular passage, rather than itself transporting the tracer. Supporting Evidence: PMID:22855531 Both actin isoforms are essential for normal barrier function of epithelial monolayers, rapid AJ/TJ reassembly, and formation of three-dimensional cysts. |
| GO:0005912 adherens junction | IDA PMID:22855531 Nonredundant roles of cytoplasmic Ξ²- and Ξ³-actin isoforms in... | ACCEPT | Summary: Beta-actin localizes to adherens junctions. Reason: PMID:22855531 examines human SK-CO15 and Caco-2 BBE epithelial cells with isoform-specific staining and perturbation. Early calcium-repletion experiments show beta-actin bundles with beta-catenin-containing junctions. Supporting Evidence: PMID:22855531 Both actin isoforms are essential for normal barrier function of epithelial monolayers, rapid AJ/TJ reassembly, and formation of three-dimensional cysts. |
| GO:0070160 tight junction | IDA PMID:22855531 Nonredundant roles of cytoplasmic Ξ²- and Ξ³-actin isoforms in... | ACCEPT | Summary: Beta-actin also localizes at tight-junction regions in mature polarized cells. Reason: PMID:22855531 examines human SK-CO15 and Caco-2 BBE epithelial cells with isoform-specific staining and perturbation. At the later time point beta-actin colocalizes with ZO-1 as well as adherens-junction markers. Different beta- versus gamma-actin depletion phenotypes do not negate this observed tight-junction localization. Supporting Evidence: PMID:22855531 Both actin isoforms are essential for normal barrier function of epithelial monolayers, rapid AJ/TJ reassembly, and formation of three-dimensional cysts. |
| GO:0005515 protein binding | IPI PMID:24415753 Protein disulfide isomerase directly interacts with Ξ²-actin ... | REMOVE | Summary: PDIβbeta-actin association is more informative as source context than as generic binding. Reason: PMID:24415753 reports PDI interaction with beta-actin in MEG-01 cells, including a disulfide-linked complex. The generic MF adds no specific ACTB activity; removal does not deny the association or the retained complex localization. ACTB is not thereby a disulfide-isomerase enzyme. Supporting Evidence: PMID:24415753 Protein disulfide isomerase directly interacts with Ξ²-actin Cys374 and regulates cytoskeleton reorganization. |
| GO:0030027 lamellipodium | IDA PMID:24415753 Protein disulfide isomerase directly interacts with Ξ²-actin ... | ACCEPT | Summary: Beta-actin localizes to lamellipodia in the studied megakaryocytic cells. Reason: PMID:24415753 places beta-actin and PDI in lamellipodial structures. This supports a canonical protrusive actin location, independent of which partner catalyzes redox chemistry. Supporting Evidence: PMID:24415753 PDI colocalizes with Ξ²-actin in adhering MEG-01 cells and predominantly in areas close to the membrane in the lamellipodial protrusions |
| GO:0032991 protein-containing complex | IDA PMID:24415753 Protein disulfide isomerase directly interacts with Ξ²-actin ... | KEEP AS NON CORE | Summary: ACTB participates in the reported PDI-associated protein complex. Reason: PMID:24415753 describes a disulfide-linked PDIβbeta-actin assembly. Retain the broad CC at the sourceβs resolution; a generic complex location is not subject to the removal policy for uninformative protein-binding MF. Supporting Evidence: PMID:24415753 PDI forms a disulfide-bonded complex with Ξ²-actin with a molecular mass of 110 kDa. |
| GO:0005911 cell-cell junction | IMP PMID:25753039 ZO-1 controls endothelial adherens junctions, cell-cell tens... | ACCEPT | Summary: ACTB contributes to cell-cell junction structure. Reason: PMID:25753039 provides junctional perturbation evidence; human beta-actin structural participation at junctions is independently established by PMID:22855531. Retain the curated junction annotation without converting the perturbation evidence into a new catalytic function. Supporting Evidence: PMID:25753039 ZO-1 depletion led to tight junction disruption, redistribution of active myosin II from junctions to stress fibers PMID:22855531 Ξ²-CYA bundles were enriched in very close proximity of these nascent AJs and significantly colocalized with Ξ²-catenin |
| GO:0048156 tau protein binding | NAS PMID:28386764 Roles of tau protein in health and disease. | KEEP AS NON CORE | Summary: Actin interacts with tau in the neuronal cytoskeleton. Reason: PMID:28386764 Table 1 lists cytoplasmic actin as a tau partner and discusses F-actin contacts through tau repeat domains. Retain this statement-level contextual interaction, without inferring that ACTB has tauβs microtubule-binding activity. Supporting Evidence: PMID:28386764 Binding of filamentous actin occurs through a minimum of two microtubule binding repeats in tau |
| GO:0005515 protein binding | IPI PMID:28604741 A novel nuclear complex of DRR1, F-actin and COMMD1 involved... | REMOVE | Summary: The reported protein association does not specify an additional ACTB function. Reason: PMID:28604741 identifies a DRR1/F-actin/COMMD1 nuclear complex associated with NF-kappaB degradation and growth suppression. The source supports association; generic protein binding does not identify which structural or regulatory work ACTB performs. Removal does not deny the complex or assign its protein-degradation mechanism to actin. Supporting Evidence: PMID:28604741 A novel nuclear complex of DRR1, F-actin and COMMD1 involved in NF-ΞΊB degradation and cell growth suppression in neuroblastoma. |
| GO:0005515 protein binding | IPI PMID:21969592 Tumor suppressor down-regulated in renal cell carcinoma 1 (D... | REMOVE | Summary: The source interaction remains evidence, while generic protein binding adds no mechanism. Reason: PMID:21969592 identifies DRR1 as an actin-bundling factor and studies neuronal effects. ACTB supplies the filament substrate for bundling; the generic binding assertion does not specify a separate activity and its removal does not deny the interaction. Supporting Evidence: PMID:21969592 Tumor suppressor down-regulated in renal cell carcinoma 1 (DRR1) is a stress-induced actin bundling factor that modulates synaptic efficacy and cognition. |
| GO:0005515 protein binding | IPI PMID:18331289 Regulated interactions of the norepineprhine transporter by ... | REMOVE | Summary: The actinβNET/alpha-synuclein interaction is captured more usefully by its functional regulator annotation. Reason: PMID:18331289 directly examines transporter uptake and actin-dependent effects. The generic binding term adds no mechanism beyond the retained transporter-regulator and contextual uptake-process annotations; removal does not deny the interaction. Supporting Evidence: PMID:18331289 Regulated interactions of the norepineprhine transporter by the actin and microtubule cytoskeletons. |
| GO:0051621 regulation of norepinephrine uptake | ISS PMID:18331289 Regulated interactions of the norepineprhine transporter by ... | KEEP AS NON CORE | Summary: The rat Actb evidence supports contextual regulation of norepinephrine uptake. Reason: PMID:18331289 investigates actin/alpha-synuclein effects on NET. Retain the ISS transfer from rat P60711 at the general regulatory level, with preparation- and dosage-dependent effects rather than a universal sign. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: UniProtKB:P60711 SUPPORTS TRANSFER Rat Actb is the traced donor; source-specific NET regulation is contextual and concentration-dependent. Supporting Evidence: PMID:18331289 Protein interactions between NET, beta-actin, and alpha-Syn were modified, along with levels of surface transporters. |
| GO:0051621 regulation of norepinephrine uptake | IGI PMID:18331289 Regulated interactions of the norepineprhine transporter by ... | KEEP AS NON CORE | Summary: Actin-dependent interactions modulate norepinephrine uptake. Reason: PMID:18331289 combines alpha-synuclein expression with cytoskeletal perturbation and uptake assays. ACTB can contribute structural regulation of NET; the direction varies with alpha-synuclein abundance and the preparation. Supporting Evidence: PMID:18331289 Protein interactions between NET, beta-actin, and alpha-Syn were modified, along with levels of surface transporters. |
| GO:1903076 regulation of protein localization to plasma membrane | IMP PMID:18331289 Regulated interactions of the norepineprhine transporter by ... | KEEP AS NON CORE | Summary: Actin-associated NET regulation includes altered plasma-membrane transporter localization. Reason: PMID:18331289 links the actinβalpha-synucleinβNET system to transporter distribution and uptake. Retain this contextual positioning function without generalizing to every membrane protein. Supporting Evidence: PMID:18331289 Protein interactions between NET, beta-actin, and alpha-Syn were modified, along with levels of surface transporters. |
| GO:0005737 cytoplasm | IDA PMID:24327345 Intracellular distribution of differentially phosphorylated ... | ACCEPT | Summary: ACTB has a cytoplasmic pool associated with cytoskeletal kinase interactions. Reason: PMID:24327345 examines DYRK1A with cytoskeletal F-actin. The source compartment agrees with the directly established cytoplasmic distribution of human beta-actin. Supporting Evidence: PMID:24327345 Coimmunoprecipitation revealed that DYRK1A in the brain cytoskeleton fraction forms complexes with filamentous actin, neurofilaments, and tubulin. PMID:22855531 Ξ²-CYA bundles were enriched in very close proximity of these nascent AJs and significantly colocalized with Ξ²-catenin |
| GO:0005856 cytoskeleton | ISS GO_REF:0000024 | ACCEPT | Summary: Conserved vertebrate actin supports the broad cytoskeleton location. Reason: The ISS donors include rat P60711 and chicken P60706. Human cytoplasmic beta-actin experiments independently corroborate the target compartment (PMID:22855531), so the broad source localization is retained. Propagation Review Root cause: NO FAILURE CORE Sources checked: UniProtKB:P60711 SUPPORTS TRANSFER Rat and chicken actin donors support broad cytoskeletal localization; independent human evidence corroborates the target. UniProtKB:P60706 SUPPORTS TRANSFER Chicken beta-actin is the additional traced ISS donor; human target evidence independently supports cytoskeletal localization. |
| GO:0051623 positive regulation of norepinephrine uptake | TAS PMID:18331289 Regulated interactions of the norepineprhine transporter by ... | KEEP AS NON CORE | Summary: In the specified preparation actin-dependent regulation can increase norepinephrine uptake. Reason: PMID:18331289 includes positive uptake effects in primary brainstem/synaptosomal preparations and concentration-dependent effects in expression systems. Retain the curated positive statement for its tested context; it is not a universal sign for actinβNET regulation. Supporting Evidence: PMID:18331289 Protein interactions between NET, beta-actin, and alpha-Syn were modified, along with levels of surface transporters. |
| GO:0098793 presynapse | TAS PMID:18331289 Regulated interactions of the norepineprhine transporter by ... | KEEP AS NON CORE | Summary: The source places actin-associated NET regulation in a presynaptic context. Reason: PMID:18331289 examines transporter biology including synaptosomal preparations. Retain the statement-level location as specialized neuronal context rather than a distinct general biochemical activity. Supporting Evidence: PMID:18331289 Protein interactions between NET, beta-actin, and alpha-Syn were modified, along with levels of surface transporters. |
| GO:0048870 cell motility | IMP PMID:6202424 A variant form of beta-actin in a mutant of KB cells resista... | ACCEPT | Summary: Beta-actin supports cell motility. Reason: PMID:6202424 associates a beta-actin alteration with cytochalasin-B resistance and altered motile behavior in KB cells. ACTB performs structural work in motility, consistent with filament dynamics. Supporting Evidence: PMID:6202424 the primary site of action of cytochalasin B on cellular motility processes is beta-actin. |
| GO:0072749 cellular response to cytochalasin B | IMP PMID:6202424 A variant form of beta-actin in a mutant of KB cells resista... | KEEP AS NON CORE | Summary: The beta-actin/cytochalasin-B relationship supports a specific chemical-response annotation. Reason: PMID:6202424 studies resistant KB-cell beta-actin and its motility-related phenotype. Retain the response in the tested drug context, without defining cytochalasin response as the proteinβs main evolved function. Supporting Evidence: PMID:6202424 the primary site of action of cytochalasin B on cellular motility processes is beta-actin. |
| GO:0019901 protein kinase binding | IPI PMID:24327345 Intracellular distribution of differentially phosphorylated ... | KEEP AS NON CORE | Summary: ACTB associates with the protein kinase DYRK1A. Reason: PMID:24327345 identifies DYRK1A in association with cytoskeletal F-actin. The specific partner class is more informative than generic binding; it does not assign kinase catalysis to ACTB. Supporting Evidence: PMID:24327345 Coimmunoprecipitation revealed that DYRK1A in the brain cytoskeleton fraction forms complexes with filamentous actin, neurofilaments, and tubulin. |
| GO:0005856 cytoskeleton | IDA PMID:24327345 Intracellular distribution of differentially phosphorylated ... | ACCEPT | Summary: The DYRK1A study supports a cytoskeletal actin pool. Reason: PMID:24327345 examines kinase association with F-actin-containing cytoskeletal structures. Retain the broad experimentally curated cytoskeleton location. Supporting Evidence: PMID:24327345 Coimmunoprecipitation revealed that DYRK1A in the brain cytoskeleton fraction forms complexes with filamentous actin, neurofilaments, and tubulin. |
| GO:0005515 protein binding | IPI PMID:17192268 Mutation analysis of the short cytoplasmic domain of the cel... | REMOVE | Summary: The reported association does not resolve an additional ACTB molecular function. Reason: PMID:17192268 mutates the short CEACAM1 cytoplasmic domain and links actin binding to epithelial lumen formation. The reported association is preserved as evidence, while generic ACTB protein binding gives no additional molecular mechanism. Supporting Evidence: PMID:17192268 Mutation analysis of the short cytoplasmic domain of the cell-cell adhesion molecule CEACAM1 identifies residues that orchestrate actin binding and lumen formation. |
| GO:0005515 protein binding | IPI PMID:11687588 Nuclear DNA helicase II/RNA helicase A binds to filamentous ... | REMOVE | Summary: Nuclear actin association with NDHII-containing assemblies is retained as source evidence. Reason: PMID:11687588 reports NDHII/DHX9 interaction with nuclear actin and hnRNP C. Generic protein binding adds little functional information; ACTB is not thereby an RNA helicase. Its nuclear and complex localizations are retained separately. Supporting Evidence: PMID:11687588 Nuclear DNA helicase II/RNA helicase A binds to filamentous actin. |
| GO:0005634 nucleus | IDA PMID:11687588 Nuclear DNA helicase II/RNA helicase A binds to filamentous ... | ACCEPT | Summary: The NDHII study identifies a nuclear actin pool. Reason: PMID:11687588 uses biochemical and localization approaches in HeLa cells to associate nuclear actin with NDHII-containing assemblies. Retain the observed compartment. Supporting Evidence: PMID:11687588 Electron microscopy indicated a close spatial proximity among NDH II, hnRNP C, and F-actin within the HeLa nucleus. |
| GO:0015629 actin cytoskeleton | IDA PMID:11687588 Nuclear DNA helicase II/RNA helicase A binds to filamentous ... | ACCEPT | Summary: ACTB is present in actin cytoskeletal structures in the NDHII study. Reason: PMID:11687588 provides the curated localization evidence, compatible with ACTBβs independently established polymeric structural role. Nuclear actin does not exclude the cytoplasmic cytoskeleton pool. Supporting Evidence: PMID:11687588 Electron microscopy indicated a close spatial proximity among NDH II, hnRNP C, and F-actin within the HeLa nucleus. |
| GO:0032991 protein-containing complex | IDA PMID:11687588 Nuclear DNA helicase II/RNA helicase A binds to filamentous ... | KEEP AS NON CORE | Summary: Nuclear ACTB is part of an NDHII/hnRNP-C-associated assembly. Reason: PMID:11687588 describes a biochemical complex involving nuclear actin. Retain protein-containing-complex CC at the measured resolution rather than deleting it under the unrelated generic-binding MF policy. Supporting Evidence: PMID:11687588 Electron microscopy indicated a close spatial proximity among NDH II, hnRNP C, and F-actin within the HeLa nucleus. |
| GO:0031982 vesicle | HDA PMID:19190083 Characterization of exosome-like vesicles released from huma... | KEEP AS NON CORE | Summary: Actin is detected in an extracellular vesicle preparation. Reason: The full PMID:19190083 reports actin and associated cytoskeletal proteins in airway epithelial vesicle fractions with preparation controls. Retain the measured vesicle association as contextual, without calling it a constitutive secretion mechanism or contamination. Supporting Evidence: PMID:19190083 Several cytoskeletal-related proteins, such as tubulin and actin and its interacting/organizing proteins |
| GO:0070062 extracellular exosome | HDA PMID:11487543 Intestinal epithelial cells secrete exosome-like vesicles. | UNDECIDED | Summary: The source-specific extracellular detection requires access to the ACTB identification evidence. Reason: The HDA row from PMID:11487543 records extracellular exosome. The accessible abstract or incomplete cached body does not expose the relevant ACTB identification table and preparation evidence. This is an access-limited decision, not a contamination claim or a rejection of experimental curation. Supporting Evidence: PMID:11487543 Intestinal epithelial cells secrete exosome-like vesicles. |
| GO:0005886 plasma membrane | ISS GO_REF:0000024 | ACCEPT | Summary: Conserved vertebrate actin supports membrane association. Reason: The ISS sources include chicken beta-actin P60706 and accessions G1NS52/Q58J72. Human cortical and junctional actin independently supports the targetβs broad membrane location; no membrane-spanning topology is implied. Propagation Review Root cause: NO FAILURE CORE Sources checked: UniProtKB:P60706 SUPPORTS TRANSFER Chicken beta-actin is one traced donor; independent human cortical localization supports broad membrane association. UniProtKB:G1NS52 UNRESOLVED This additional source accession is preserved from donor tracing; its underlying experiment and organism were not established here. Independent human cortical/junctional evidence supports the broad target location. UniProtKB:Q58J72 UNRESOLVED This additional source accession is preserved from donor tracing; its underlying experiment and organism were not established here. Independent human cortical/junctional evidence supports the broad target location. |
| GO:0097433 dense body | ISS GO_REF:0000024 | UNDECIDED | Summary: The dense-body donor localization was not resolved to its underlying experiment. Reason: The traced source includes chicken beta-actin P60706. GO:0097433 denotes an electron-dense body that may contain granules; it is not restricted to smooth-muscle dense bodies. Without the source experiment, transfer to human ACTB remains unresolved rather than biologically disproven. Propagation Review Root cause: UNRESOLVED Sources checked: UniProtKB:P60706 UNRESOLVED The chicken beta-actin donor was identified, but the underlying dense-body experiment and transfer context remain unresolved. |
| GO:0005515 protein binding | IPI PMID:23100250 Constitutive turnover of phosphorylation at Thr-412 of human... | REMOVE | Summary: The reported protein association is not a specific ACTB molecular activity. Reason: PMID:23100250 links coronin-1 Thr-412 phosphorylation turnover to its interaction with actin. This establishes regulated partner association without specifying a separate ACTB activity; removal of generic binding does not reject the reported interaction. Supporting Evidence: PMID:23100250 Constitutive turnover of phosphorylation at Thr-412 of human p57/coronin-1 regulates the interaction with actin. |
| GO:0005515 protein binding | IPI PMID:18562541 Association of hepatitis C virus replication complexes with ... | REMOVE | Summary: Generic binding does not explain ACTBβs role in the reported association. Reason: PMID:18562541 places hepatitis-C replication complexes on actin/microtubule structures in an NS3/NS5A-dependent interaction context. Generic protein binding is uninformative about ACTBβs structural contribution; the association is not being called false. Supporting Evidence: PMID:18562541 Association of hepatitis C virus replication complexes with microtubules and actin filaments is dependent on the interaction of NS3 and NS5A. |
| GO:0070527 platelet aggregation | HMP PMID:23382103 Platelet proteome analysis reveals integrin-dependent aggreg... | UNDECIDED | Summary: The exact platelet-aggregation assertion requires the underlying ACTB-specific evidence. Reason: PMID:23382103 examines myelodysplastic platelets with proteomic and functional changes. The locally recovered abstract/discussion links cytoskeletal proteins to platelet abnormalities, but does not expose the particular evidence for this HMP assertion. Do not overrule the curator from a partial cache or call the result a mere downstream effect without the assay. Supporting Evidence: PMID:23382103 Platelet proteome analysis reveals integrin-dependent aggregation defects in patients with myelodysplastic syndromes. |
| GO:0005925 focal adhesion | HDA PMID:21423176 Analysis of the myosin-II-responsive focal adhesion proteome... | ACCEPT | Summary: ACTB is detected in purified focal-adhesion preparations. Reason: PMID:21423176 Methods explicitly describe actin immunoblotting of isolated HFF-1 focal adhesions, followed by actin/fibronectin immunodepletion before MudPIT. The enrichment and removal protocol supports localization; absence after depletion would not refute it. Supporting Evidence: PMID:21423176 FAs were collected, solubilized, denatured, and the abundant proteins actin and fibronectin removed by immunodepletion. |
| GO:0070062 extracellular exosome | HDA PMID:23533145 In-depth proteomic analyses of exosomes isolated from expres... | UNDECIDED | Summary: The source-specific extracellular detection requires access to the ACTB identification evidence. Reason: The HDA row from PMID:23533145 records extracellular exosome. The accessible abstract or incomplete cached body does not expose the relevant ACTB identification table and preparation evidence. This is an access-limited decision, not a contamination claim or a rejection of experimental curation. Supporting Evidence: PMID:23533145 In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine. |
| GO:0016020 membrane | HDA PMID:19946888 Defining the membrane proteome of NK cells. | ACCEPT | Summary: ACTB has a membrane-associated pool in the curated proteomic source. Reason: PMID:19946888 supplies the HDA membrane assertion. This broad location agrees with independently demonstrated cortical and junctional beta-actin. Retain at the sourceβs resolution and defer to the curator for the target peptide assignment; no claim of integral membrane topology is made. Supporting Evidence: PMID:19946888 The remaining species were largely involved in cellular processes and molecular functions that could be predicted to be transiently associated with membranes. PMID:22855531 Ξ²-CYA bundles were enriched in very close proximity of these nascent AJs and significantly colocalized with Ξ²-catenin |
| GO:0036464 cytoplasmic ribonucleoprotein granule | IDA PMID:15121898 The composition of Staufen-containing RNA granules from huma... | KEEP AS NON CORE | Summary: Actin associates with Staufen-containing ribonucleoprotein granules. Reason: PMID:15121898 reports actin in Staufen-containing complexes and colocalization in neuroblastoma cells. Retain this contextual granule association without assigning actin the RNA-recognition specificity of Staufen. Supporting Evidence: PMID:15121898 as well as elements of the cytoskeleton (tubulins, tau, actin and internexin) |
| GO:0005615 extracellular space | HDA PMID:16502470 Human colostrum: identification of minor proteins in the aqu... | UNDECIDED | Summary: The source-specific extracellular detection requires access to the ACTB identification evidence. Reason: The HDA row from PMID:16502470 records extracellular space. The accessible abstract or incomplete cached body does not expose the relevant ACTB identification table and preparation evidence. This is an access-limited decision, not a contamination claim or a rejection of experimental curation. Supporting Evidence: PMID:16502470 Human colostrum: identification of minor proteins in the aqueous phase by proteomics. |
| GO:0000785 chromatin | HDA PMID:16217013 Heterogeneous nuclear ribonucleoprotein C1/C2, MeCP1, and SW... | ACCEPT | Summary: ACTB is associated with the purified chromatin-remodeling assembly. Reason: PMID:16217013 identifies actin in the K562 LARC preparation by mass spectrometry and characterizes complex interaction with chromatin. The broad chromatin location is supported at complex level. Supporting Evidence: PMID:16217013 The LC-MS/MS analysis of the tryptic digest of the 45-kDa band revealed the presence of actin and requiem |
| GO:0031492 nucleosomal DNA binding | HDA PMID:16217013 Heterogeneous nuclear ribonucleoprotein C1/C2, MeCP1, and SW... | UNDECIDED | Summary: The nucleosomal-DNA binding contribution of ACTB requires more specific resolution. Reason: PMID:16217013 recovers actin in a DNA-associated remodeling complex but assigns sequence-specific recognition to hnRNP C1/C2. The whole-complex assay does not resolve the particular actin binding contribution behind this HDA row. Preserve the assertion pending resolution rather than declaring the complex unable to bind DNA. Supporting Evidence: PMID:16217013 The LC-MS/MS analysis of the tryptic digest of the 45-kDa band revealed the presence of actin and requiem |
| GO:0032991 protein-containing complex | HDA PMID:16217013 Heterogeneous nuclear ribonucleoprotein C1/C2, MeCP1, and SW... | KEEP AS NON CORE | Summary: ACTB belongs to the purified LCR-associated remodeling complex. Reason: The full PMID:16217013 identifies the actin band by LC-MS/MS. Retain broad protein-containing-complex CC because the mixed LARC assembly is not safely replaced by a single named constituent remodeler; this is positive complex-membership evidence. Supporting Evidence: PMID:16217013 The LC-MS/MS analysis of the tryptic digest of the 45-kDa band revealed the presence of actin and requiem |
| GO:0021762 substantia nigra development | HEP PMID:22926577 Quantitative proteomic analysis of human substantia nigra in... | UNDECIDED | Summary: The substantia-nigra developmental assertion cannot be resolved from the accessible source. Reason: PMID:22926577 provides adult substantia-nigra proteomic/expression context. The specific developmental interpretation behind the HEP annotation was not recoverable from the abstract. This access limit does not establish that the curator confused development with adult expression. Supporting Evidence: PMID:22926577 Quantitative proteomic analysis of human substantia nigra in Alzheimer's disease, Huntington's disease and Multiple sclerosis. |
| GO:0072562 blood microparticle | HDA PMID:22516433 Proteomic analysis of microvesicles from plasma of healthy d... | UNDECIDED | Summary: The source-specific extracellular detection requires access to the ACTB identification evidence. Reason: The HDA row from PMID:22516433 records blood microparticle. The accessible abstract or incomplete cached body does not expose the relevant ACTB identification table and preparation evidence. This is an access-limited decision, not a contamination claim or a rejection of experimental curation. Supporting Evidence: PMID:22516433 Proteomic analysis of microvesicles from plasma of healthy donors reveals high individual variability. |
| GO:0005615 extracellular space | HDA PMID:22664934 Comparison of tear protein levels in breast cancer patients ... | UNDECIDED | Summary: The source-specific extracellular detection requires access to the ACTB identification evidence. Reason: The HDA row from PMID:22664934 records extracellular space. The accessible abstract or incomplete cached body does not expose the relevant ACTB identification table and preparation evidence. This is an access-limited decision, not a contamination claim or a rejection of experimental curation. Supporting Evidence: PMID:22664934 Comparison of tear protein levels in breast cancer patients and healthy controls using a de novo proteomic approach. |
| GO:0005615 extracellular space | HDA PMID:23580065 Shotgun proteomics reveals specific modulated protein patter... | UNDECIDED | Summary: The source-specific extracellular detection requires access to the ACTB identification evidence. Reason: The HDA row from PMID:23580065 records extracellular space. The accessible abstract or incomplete cached body does not expose the relevant ACTB identification table and preparation evidence. This is an access-limited decision, not a contamination claim or a rejection of experimental curation. Supporting Evidence: PMID:23580065 Shotgun proteomics reveals specific modulated protein patterns in tears of patients with primary open angle glaucoma naΓ―ve to therapy. |
| GO:0070062 extracellular exosome | HDA PMID:19199708 Proteomic analysis of human parotid gland exosomes by multid... | UNDECIDED | Summary: The source-specific extracellular detection requires access to the ACTB identification evidence. Reason: The HDA row from PMID:19199708 records extracellular exosome. The accessible abstract or incomplete cached body does not expose the relevant ACTB identification table and preparation evidence. This is an access-limited decision, not a contamination claim or a rejection of experimental curation. Supporting Evidence: PMID:19199708 Proteomic analysis of human parotid gland exosomes by multidimensional protein identification technology (MudPIT). |
| GO:0070062 extracellular exosome | HDA PMID:20458337 MHC class II-associated proteins in B-cell exosomes and pote... | UNDECIDED | Summary: The source-specific extracellular detection requires access to the ACTB identification evidence. Reason: The HDA row from PMID:20458337 records extracellular exosome. The accessible abstract or incomplete cached body does not expose the relevant ACTB identification table and preparation evidence. This is an access-limited decision, not a contamination claim or a rejection of experimental curation. Supporting Evidence: PMID:20458337 MHC class II-associated proteins in B-cell exosomes and potential functional implications for exosome biogenesis. |
| GO:0070062 extracellular exosome | HDA PMID:21362503 Protein profile of exosomes from trabecular meshwork cells. | KEEP AS NON CORE | Summary: Beta-actin is identified in trabecular-meshwork extracellular vesicles. Reason: The full PMID:21362503 lists beta-actin among detected vesicle proteins and provides fraction characterization. Retain the measured extracellular-vesicle association as contextual, without claiming constitutive secretion or dismissing the detection as contamination. Supporting Evidence: PMID:21362503 commonly observed exosomal markers such as GAPDH, Ξ²-actin, moesin |
| GO:0005515 protein binding | IPI PMID:14592989 Exportin 6: a novel nuclear export receptor that is specific... | REMOVE | Summary: The reported interaction does not specify a distinct ACTB function. Reason: PMID:14592989 identifies exportin-6 as a receptor for profilinβactin cargo. ACTB is cargo in this relationship, rather than the export receptor; the generic binding label adds no specific molecular function. Supporting Evidence: PMID:14592989 Exportin 6: a novel nuclear export receptor that is specific for profilin.actin complexes. |
| GO:0005515 protein binding | IPI PMID:17823310 HGAL, a lymphoma prognostic biomarker, interacts with the cy... | REMOVE | Summary: The protein association is retained as evidence but generic binding adds no mechanism. Reason: PMID:17823310 links HGAL to cytoskeletal associations and IL-6-dependent migration effects. The association can be real while generic ACTB binding remains uninformative; no unmeasured ACTB regulatory activity is invented. Supporting Evidence: PMID:17823310 HGAL, a lymphoma prognostic biomarker, interacts with the cytoskeleton and mediates the effects of IL-6 on cell migration. |
| GO:0030957 Tat protein binding | IPI PMID:16687403 The SWI/SNF chromatin-remodeling complex is a cofactor for T... | KEEP AS NON CORE | Summary: ACTB occurs in Tat-associated nuclear complexes. Reason: PMID:16687403 reports Tat association with beta-actin and SWI/SNF components. Retain the curated specific binding context, with the biochemical-complex assay distinguished from purified pairwise binding and from actinβs independent enzymatic activities. Supporting Evidence: PMID:16687403 Tat was co-immunoprecipitated with several SWI/SNF subunits, including INI-1, BRG-1, and beta-actin. |
| GO:0019894 kinesin binding | IPI PMID:18680169 New insights on cellular distribution, microtubule interacti... | KEEP AS NON CORE | Summary: Actin is associated with kinesin in the studied interaction system. Reason: PMID:18680169 provides KIF18A/actin interaction evidence. Retain kinesin binding as a contextual partner interaction; ACTB is not assigned the kinesin motor ATPase activity. Supporting Evidence: PMID:18680169 Multiple assays including metabolic labeling, cell fractionation and IP with anti-MS-KIF18A antibody demonstrated an association with actin that was prominent in the cell cytoplasm. |
| GO:1990904 ribonucleoprotein complex | IDA PMID:17289661 Molecular composition of IMP1 ribonucleoprotein granules. | UNDECIDED | Summary: The particular ACTB component of the IMP1 ribonucleoprotein assembly requires source resolution. Reason: PMID:17289661 describes IMP1-containing granules, but the accessible abstract does not expose the ACTB assay or component list. Preserve the IDA assertion as unresolved rather than rejecting it because the abstract foregrounds IMP1. Supporting Evidence: PMID:17289661 Molecular composition of IMP1 ribonucleoprotein granules. |
| GO:0050998 nitric-oxide synthase binding | IPI PMID:17502619 beta-Actin regulates platelet nitric oxide synthase 3 activi... | KEEP AS NON CORE | Summary: G-actin binds nitric-oxide synthase in human platelets. Reason: PMID:17502619 directly links G-actinβNOS3 association to Hsp90-dependent regulation. Retain the specific binding function and the monomer-state context; it is distinct from NOS catalytic activity. Supporting Evidence: PMID:17502619 We found that NOS-3 binds to the globular, but not the filamentous, form of beta-actin |
| GO:0005515 protein binding | IPI PMID:17342765 Microtubule-binding proteins CLASP1 and CLASP2 interact with... | REMOVE | Summary: The source interaction remains evidence while the generic MF is uninformative. Reason: PMID:17342765 reports CLASP1/CLASP2 interactions with actin filaments. This associates two cytoskeletal systems without making actin a CLASP microtubule-binding protein. Remove the generic MF while preserving the reported association. Supporting Evidence: PMID:17342765 Microtubule-binding proteins CLASP1 and CLASP2 interact with actin filaments. |
| GO:0005200 structural constituent of cytoskeleton | TAS PMID:6202424 A variant form of beta-actin in a mutant of KB cells resista... | ACCEPT | Summary: ACTB forms a structural constituent of the cytoskeleton. Reason: PMID:6202424 links beta-actin properties to cell motility and cytochalasin response. Direct human beta-actin polymerization and junctional studies corroborate the structural activity (PMID:25255767; PMID:22855531). Supporting Evidence: PMID:6202424 the primary site of action of cytochalasin B on cellular motility processes is beta-actin. |
| GO:0005737 cytoplasm | TAS PMID:16130169 Proteomics of human umbilical vein endothelial cells applied... | ACCEPT | Summary: ACTB has a cytoplasmic pool in endothelial-cell proteomic observations. Reason: PMID:16130169 provides the source-level endothelial proteomic context. The broad cytoplasmic location is independently established and retained without inferring that every detected actin molecule is soluble. Supporting Evidence: PMID:16130169 The overall functional characterization of the 162 identified proteins from primary cultures of HUVECs confirms the metabolic capabilities of endothelium PMID:22855531 Ξ²-CYA bundles were enriched in very close proximity of these nascent AJs and significantly colocalized with Ξ²-catenin |
| GO:0005856 cytoskeleton | TAS PMID:16130169 Proteomics of human umbilical vein endothelial cells applied... | ACCEPT | Summary: ACTB is a component of the endothelial cytoskeleton. Reason: PMID:16130169 provides the curated source context, consistent with beta-actinβs directly established structural role. Retain the broad cytoskeleton annotation rather than forcing a more precise substructure not resolved by this source. Supporting Evidence: PMID:16130169 The overall functional characterization of the 162 identified proteins from primary cultures of HUVECs confirms the metabolic capabilities of endothelium PMID:22855531 Ξ²-CYA bundles were enriched in very close proximity of these nascent AJs and significantly colocalized with Ξ²-catenin |
| GO:0035267 NuA4 histone acetyltransferase complex | IDA PMID:10966108 Involvement of the TIP60 histone acetylase complex in DNA re... | KEEP AS NON CORE | Summary: ACTB is a component of the TIP60/NuA4 complex. Reason: PMID:10966108 purifies the multimeric TIP60 complex, and PMID:14966270 corroborates conserved human NuA4 subunit composition. Retain actin membership, while acetyltransferase, helicase and DNA-binding activities of the whole preparation are not all assigned independently to ACTB. This complex represents a specialized structural pool outside the filament and SWI/SNF core functions synthesized here. Supporting Evidence: PMID:10966108 These results indicate that the histone acetylase TIP60-containing complex plays a role in DNA repair and apoptosis. |
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Download this section (compressed HTML)Q: What intended primary reference supports the NAS regulation-of-RNA-polymerase-II-transcription assertion recorded as PMID:17340523, which resolves to an alkaloid paper?
Q: Does luminal ACTB contribute structurally to tubulin seed formation, or specifically to assembly and regulation of the precursor gamma-TuRC, and how does this vary with activation state?
Q: Which original ACTBβACTB interaction records and actin reagents underlie the retained IPI self-association annotations, especially the filamentβpartner structural studies and variant interaction screens?
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