Existing Annotations Review

Core Functions

Polymerizing into filaments that form the structural backbone of the cytoskeleton

Molecular Function:

structural constituent of cytoskeleton

Directly Involved In:

regulation of actin filament length cell motility

Cellular Locations:

actin cytoskeleton actin filament

Supporting Evidence:

PMID:29581253
Beta-actin polymerizes to form actin filaments that are major components of the cytoskeleton, providing structural support for cell shape and motility.

Hydrolyzing ATP to drive filament dynamics and polymerization cycles

Molecular Function:

ATP hydrolysis activity

Directly Involved In:

regulation of actin filament length

Cellular Locations:

actin filament

Supporting Evidence:

PMID:25255767
Actin possesses intrinsic ATPase activity that is essential for filament dynamics, with ATP hydrolysis occurring after incorporation into filaments.

Participating in chromatin remodeling complexes (BAF/SWI-SNF and NuA4) in the nucleus

Molecular Function:

ATP-dependent activity

Directly Involved In:

chromatin remodeling

Cellular Locations:

nucleoplasm

Supporting Evidence:

PMID:18765789
Regulation of muscle development by DPF3, a novel histone acetylation and methylation reader of the BAF chromatin remodeling complex

Contributing to microtubule nucleation as a component of the gamma-tubulin ring complex

Molecular Function:

protein binding

Directly Involved In:

microtubule nucleation

In Complex:

gamma-tubulin complex

Supporting Evidence:

PMID:39321809
Beta-actin forms a luminal bridge within the gamma-tubulin ring complex (gTuRC), stabilizing the initial structure during complex assembly and regulating microtubule nucleation.

References

GO_REF:0000024

Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity.

GO_REF:0000033

Annotation inferences using phylogenetic trees

GO_REF:0000043

Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping

GO_REF:0000107

Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara.

GO_REF:0000108

Automatic assignment of GO terms using logical inference, based on on inter-ontology links.

GO_REF:0000114

Manual transfer of experimentally-verified manual GO annotation data to homologous complexes by curator judgment of sequence, composition and function similarity

GO_REF:0000120

Combined Automated Annotation using Multiple IEA Methods.

PMID:10078207

Reconstitution of a core chromatin remodeling complex from SWI/SNF subunits.

PMID:10778858

Exit from G1 and S phase of the cell cycle is regulated by repressor complexes containing HDAC-Rb-hSWI/SNF and Rb-hSWI/SNF.

PMID:10966108

Involvement of the TIP60 histone acetylase complex in DNA repair and apoptosis.

PMID:11078522

The human SWI/SNF-B chromatin-remodeling complex is related to yeast rsc and localizes at kinetochores of mitotic chromosomes.

PMID:11175787

Mammalian SWI/SNF complexes promote MyoD-mediated muscle differentiation.

PMID:11263494

The murine SNF5/INI1 chromatin remodeling factor is essential for embryonic development and tumor suppression.

PMID:11487543

Intestinal epithelial cells secrete exosome-like vesicles.

PMID:11682052

Cingulin interacts with F-actin in vitro.

PMID:11687588

Nuclear DNA helicase II/RNA helicase A binds to filamentous actin.

PMID:11790558

SWI/SNF chromatin remodeling and cancer.

PMID:12110891

Reciprocal regulation of CD4/CD8 expression by SWI/SNF-like BAF complexes.

PMID:12192000

REST repression of neuronal genes requires components of the hSWI.SNF complex.

PMID:12215535

The SWI/SNF chromatin-remodeling factor stimulates repair by human excision nuclease in the mononucleosome core particle.

PMID:12368262

Identification of a polymorphic, neuron-specific chromatin remodeling complex.

PMID:14592989

Exportin 6: a novel nuclear export receptor that is specific for profilin.actin complexes.

PMID:14966270

Structural and functional conservation of the NuA4 histone acetyltransferase complex from yeast to humans.

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.

PMID:15121898

The composition of Staufen-containing RNA granules from human cells indicates their role in the regulated transport and translation of messenger RNAs.

PMID:15161933

Comprehensive proteomic analysis of interphase and mitotic 14-3-3-binding proteins.

PMID:15328537

Emerin caps the pointed end of actin filaments: evidence for an actin cortical network at the nuclear inner membrane.

PMID:15527767

Proteomics-based identification of proteins interacting with Smad3: SREBP-2 forms a complex with Smad3 and inhibits its transcriptional activity.

PMID:15985610

PBAF chromatin-remodeling complex requires a novel specificity subunit, BAF200, to regulate expression of selective interferon-responsive genes.

PMID:16049941

A pilot proteomic study of amyloid precursor interactors in Alzheimer's disease.

PMID:16130169

Proteomics of human umbilical vein endothelial cells applied to etoposide-induced apoptosis.

PMID:16189514

Towards a proteome-scale map of the human protein-protein interaction network.

PMID:16217013

Heterogeneous nuclear ribonucleoprotein C1/C2, MeCP1, and SWI/SNF form a chromatin remodeling complex at the beta-globin locus control region.

PMID:16375898

Identification of an actin-binding site in p47phox an organizer protein of NADPH oxidase.

PMID:16502470

Human colostrum: identification of minor proteins in the aqueous phase by proteomics.

PMID:16687403

The SWI/SNF chromatin-remodeling complex is a cofactor for Tat transactivation of the HIV promoter.

PMID:16932743

Mammalian SWI/SNF complexes facilitate DNA double-strand break repair by promoting gamma-H2AX induction.

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.

PMID:17289661

Molecular composition of IMP1 ribonucleoprotein granules.

PMID:17340523

Separation and Quantification of Some Alkaloids from Fumaria parviflora by Capillary Isotachophoresis1.

PMID:17342765

Microtubule-binding proteins CLASP1 and CLASP2 interact with actin filaments.

PMID:17404223

The role of CaMKII as an F-actin-bundling protein crucial for maintenance of dendritic spine structure.

PMID:17502619

beta-Actin regulates platelet nitric oxide synthase 3 activity through interaction with heat shock protein 90.

PMID:17599063

PtdIns(4,5)P-restricted plasma membrane localization of FAN is involved in TNF-induced actin reorganization.

PMID:17823310

HGAL, a lymphoma prognostic biomarker, interacts with the cytoskeleton and mediates the effects of IL-6 on cell migration.

PMID:17920018

Regulation of dendritic development by neuron-specific chromatin remodeling complexes.

PMID:18234857

High-resolution cryo-EM structure of the F-actin-fimbrin/plastin ABD2 complex.

PMID:18331289

Regulated interactions of the norepineprhine transporter by the actin and microtubule cytoskeletons.

PMID:18341992

The subspine organization of actin fibers regulates the structure and plasticity of dendritic spines.

PMID:18562541

Association of hepatitis C virus replication complexes with microtubules and actin filaments is dependent on the interaction of NS3 and NS5A.

PMID:18680169

New insights on cellular distribution, microtubule interactions and post-translational modifications of MS-KIF18A.

PMID:18809673

BRD7, a novel PBAF-specific SWI/SNF subunit, is required for target gene activation and repression in embryonic stem cells.

PMID:19000816

Structural basis for parasite-specific functions of the divergent profilin of Plasmodium falciparum.

PMID:19008859

Molecular basis for G-actin binding to RPEL motifs from the serum response factor coactivator MAL.

PMID:19171758

Kank attenuates actin remodeling by preventing interaction between IRSp53 and Rac1.

PMID:19190083

Characterization of exosome-like vesicles released from human tracheobronchial ciliated epithelium: a possible role in innate defense.

PMID:19199708

Proteomic analysis of human parotid gland exosomes by multidimensional protein identification technology (MudPIT).

PMID:19279220

An embryonic stem cell chromatin remodeling complex, esBAF, is essential for embryonic stem cell self-renewal and pluripotency.

PMID:19328794

Nuclear myosin II regulates the assembly of preinitiation complex for ICAM-1 gene transcription.

PMID:19338310

Streamline proteomic approach for characterizing protein-protein interaction network in a RAD52 protein complex.

PMID:19946888

Defining the membrane proteome of NK cells.

PMID:20383143

Opening of tandem calponin homology domains regulates their affinity for F-actin.

PMID:20458337

MHC class II-associated proteins in B-cell exosomes and potential functional implications for exosome biogenesis.

PMID:20473970

Identification of FBXO25-interacting proteins using an integrated proteomics approach.

PMID:20618440

Proteomic and biochemical analysis of 14-3-3-binding proteins during C2-ceramide-induced apoptosis.

PMID:21044950

Genome-wide YFP fluorescence complementation screen identifies new regulators for telomere signaling in human cells.

PMID:21362503

Protein profile of exosomes from trabecular meshwork cells.

PMID:21423176

Analysis of the myosin-II-responsive focal adhesion proteome reveals a role for β-Pix in negative regulation of focal adhesion maturation.

PMID:21516116

Next-generation sequencing to generate interactome datasets.

PMID:21555369

Nuclear ErbB2 enhances translation and cell growth by activating transcription of ribosomal RNA genes.

PMID:21577206

A novel interplay between oncogenic PFTK1 protein kinase and tumor suppressor TAGLN2 in the control of liver cancer cell motility.

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.

PMID:22038833

Disruption of cytokeratin-8 interaction with F508del-CFTR corrects its functional defect.

PMID:22516433

Proteomic analysis of microvesicles from plasma of healthy donors reveals high individual variability.

PMID:22664934

Comparison of tear protein levels in breast cancer patients and healthy controls using a de novo proteomic approach.

PMID:22855531

Nonredundant roles of cytoplasmic β- and γ-actin isoforms in regulation of epithelial apical junctions.

PMID:22926577

Quantitative proteomic analysis of human substantia nigra in Alzheimer's disease, Huntington's disease and Multiple sclerosis.

PMID:23100250

Constitutive turnover of phosphorylation at Thr-412 of human p57/coronin-1 regulates the interaction with actin.

PMID:23382103

Platelet proteome analysis reveals integrin-dependent aggregation defects in patients with myelodysplastic syndromes.

PMID:23533145

In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine.

PMID:23580065

Shotgun proteomics reveals specific modulated protein patterns in tears of patients with primary open angle glaucoma naïve to therapy.

PMID:23698369

BAF complexes facilitate decatenation of DNA by topoisomerase IIα.

PMID:24327345

Intracellular distribution of differentially phosphorylated dual-specificity tyrosine phosphorylation-regulated kinase 1A (DYRK1A).

PMID:24415753

Protein disulfide isomerase directly interacts with β-actin Cys374 and regulates cytoskeleton reorganization.

PMID:25066234

Requirement for PBAF in transcriptional repression and repair at DNA breaks in actively transcribed regions of chromatin.

PMID:25255767

Molecular mechanisms of disease-related human β-actin mutations p.R183W and p.E364K.

PMID:25416956

A proteome-scale map of the human interactome network.

PMID:25502805

A massively parallel pipeline to clone DNA variants and examine molecular phenotypes of human disease mutations.

PMID:25712891

G551D-CFTR needs more bound actin than wild-type CFTR to maintain its presence in plasma membranes.

PMID:25753039

ZO-1 controls endothelial adherens junctions, cell-cell tension, angiogenesis, and barrier formation.

PMID:25910212

Widespread macromolecular interaction perturbations in human genetic disorders.

PMID:27107014

An inter-species protein-protein interaction network across vast evolutionary distance.

PMID:27153538

The TIP60 Complex Regulates Bivalent Chromatin Recognition by 53BP1 through Direct H4K20me Binding and H2AK15 Acetylation.

PMID:27607350

Characterization of the Translationally Controlled Tumor Protein (TCTP) Interactome Reveals Novel Binding Partners in Human Cancer Cells.

PMID:28386764

Roles of tau protein in health and disease.

PMID:28514442

Architecture of the human interactome defines protein communities and disease networks.

PMID:28604741

A novel nuclear complex of DRR1, F-actin and COMMD1 involved in NF-κB degradation and cell growth suppression in neuroblastoma.

PMID:29374058

Glioma tumor suppressor candidate region gene 1 (GLTSCR1) and its paralog GLTSCR1-like form SWI/SNF chromatin remodeling subcomplexes.

PMID:29477555

HtrA3 is a cellular partner of cytoskeleton proteins and TCP1α chaperonin.

PMID:29892012

An interactome perturbation framework prioritizes damaging missense mutations for developmental disorders.

PMID:29924966

A Proteomic Variant Approach (ProVarA) for Personalized Medicine of Inherited and Somatic Disease.

PMID:30021884

Histone Interaction Landscapes Visualized by Crosslinking Mass Spectrometry in Intact Cell Nuclei.

PMID:30280653

Blood-Brain Barrier: From Physiology to Disease and Back.

PMID:30510198

A non-canonical BRD9-containing BAF chromatin remodeling complex regulates naive pluripotency in mouse embryonic stem cells.

PMID:30886144

Network-based prediction of protein interactions.

PMID:31515488

Extensive disruption of protein interactions by genetic variants across the allele frequency spectrum in human populations.

PMID:32296183

A reference map of the human binary protein interactome.

PMID:32814053

Interactome Mapping Provides a Network of Neurodegenerative Disease Proteins and Uncovers Widespread Protein Aggregation in Affected Brains.

PMID:33961781

Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.

PMID:35271311

OpenCell: Endogenous tagging for the cartography of human cellular organization.

PMID:36012204

Differential CFTR-Interactome Proximity Labeling Procedures Identify Enrichment in Multiple SLC Transporters.

PMID:39321809

CDK5RAP2 activates microtubule nucleator γTuRC by facilitating template formation and actin release.

PMID:6202424

A variant form of beta-actin in a mutant of KB cells resistant to cytochalasin B.

PMID:8804307

Diversity and specialization of mammalian SWI/SNF complexes.

PMID:9128241

Components of the human SWI/SNF complex are enriched in active chromatin and are associated with the nuclear matrix.

Reactome:R-HSA-1861595

Extension of pseudopodia by myosin-X in a PI3K dependent manner

Reactome:R-HSA-2029466

(WASPs, WAVE):G-actin:ARP2/3 binds F-actin

Reactome:R-HSA-2029473

Branching and elongation of mother and daughter filaments

Reactome:R-HSA-2029476

Role of myosins in phagosome formation

Reactome:R-HSA-203070

Association of profilin with monomeric actin

Reactome:R-HSA-2197690

Detachment of WASP/WAVE

Reactome:R-HSA-392751

L1 linked to actin cytoskeleton by ankyrin

Reactome:R-HSA-3928595

N-WASP binds ARP2/3 and G-actin

Reactome:R-HSA-3928654

Clathrin internalises EPH:EFN complexes

Reactome:R-HSA-430347

MigFilin associates with Filamin and F-actin

Reactome:R-HSA-443779

Linkage of L1 with treadmilling F-actin

Reactome:R-HSA-445089

Dephosphorylation of pL1 (Y1176)

Reactome:R-HSA-5218916

p-MAPK2/3 phosphorylates HSP27

Reactome:R-HSA-5250947

B-WICH complex binds rDNA promoter

Reactome:R-HSA-5626507

IQGAPs bind F-actin, which is inhibited by calmodulin

Reactome:R-HSA-5665751

CDC42:GTP:FMNL2 binds Profilin:G-actin

Reactome:R-HSA-5665767

Activated FMNL3 binds G-actin

Reactome:R-HSA-5665802

SRGAP2 binds RAC1:GTP:FMNL1:profilin:G-actin

Reactome:R-HSA-5665809

SRGAP2 stimulates RAC1 GTP-ase activity and ends FMNL1-mediated elongation of actin filaments

Reactome:R-HSA-5665982

RHOA:GTP:DIAPH1 binds EVL and sequesters profilin:G-actin from MKL1

Reactome:R-HSA-5666001

Profilin:G-actin binds MKL1

Reactome:R-HSA-5689544

UCHL5 binds INO80 complex

Reactome:R-HSA-8868230

SNX9 recruits components of the actin polymerizing machinery

Reactome:R-HSA-8868236

BAR domain proteins recruit dynamin

Reactome:R-HSA-8868648

SYNJ hydrolyze PI(4,5)P2 to PI(4)P

Reactome:R-HSA-8868651

Endophilins recruit synaptojanins to the clathrin-coated pit

Reactome:R-HSA-8868658

HSPA8-mediated ATP hydrolysis promotes vesicle uncoating

Reactome:R-HSA-8868659

Clathrin recruits auxilins to the clathrin-coated vesicle

Reactome:R-HSA-8868660

Auxilin recruits HSPA8:ATP to the clathrin-coated vesicle

Reactome:R-HSA-8868661

Dynamin-mediated GTP hydrolysis promotes vesicle scission

Reactome:R-HSA-8869438

Dissociation of clathrin-associated proteins

Reactome:R-HSA-8871193

Dissociation of AAK1 and dephosphorylation of AP-2 mu2

Reactome:R-HSA-8871194

RAB5 and GAPVD1 bind AP-2

Reactome:R-HSA-9666458

IgG:Leishmania surface:FCGR3A translocates from plasma membrane to the parasitophorous vacuole

Reactome:R-HSA-9825847

MITF-M dimer and the SWI/SNF complex bind the TYRP1 promoter

Reactome:R-HSA-9914537

DGC complex binds AGRN and HSPG2

Reactome:R-HSA-9933236

SS18-containing ATPase complex binds SMARCC dimer:SMARCDs:BICRAs:BRD9

Reactome:R-HSA-9933237

PBRM1-containing ATPase complex binds SMARCC dimer:SMARCDs:SMARCE1:SMARCB1:ARID2:BRD&:PHF10

Reactome:R-HSA-9933238

SS18-containing ATPase complex binds SMARCC1 dimer:SMARCD1:SMARCE1:SMARCB1:ARID1:DPF1,2,3

Reactome:R-HSA-9934021

Formation of neuronal progenitor BAF (npBAF)

Reactome:R-HSA-9934024

SMARCA4, BCL11A,B-containing ATPase module binds SMARCC1:SMACC2 dimer:SMARCD1:SMARCE1:SMARCB1:ARID1A:DPF2, PHF10

Reactome:R-HSA-9934294

CDH1-associated CTNNA1 binds VCL

Reactome:R-HSA-9934410

CDH1 forms homotypic trans-dimers

Reactome:R-HSA-9934486

CDH1-associated CTNNA1 binds F-actin

Reactome:R-NUL-4551334

NuA4 complex actetylates H2A and H4

file:human/ACTB/ACTB-deep-research-perplexity-lite.md

Deep research on ACTB function

file:human/ACTB/ACTB-deep-research-cyberian.md

Deep research on ACTB function (Cyberian)

PMID:26988969

Actin and Actin-Binding Proteins.

PMID:3672117

Actin polymerization and ATP hydrolysis.

PMID:21314430

Actin structure and function.

PMID:30012594

Essential nucleotide- and protein-dependent functions of Actb/β-actin.

PMID:12045110

Nuclear actin and actin-related proteins in chromatin remodeling.

PMID:22366783

De novo mutations in the actin genes ACTB and ACTG1 cause Baraitser-Winter syndrome.

PMID:30626964

SETD3 is an actin histidine methyltransferase that prevents primary dystocia.

PMID:12507992

Two ZBP1 KH domains facilitate beta-actin mRNA localization, granule formation, and cytoskeletal attachment.

PMID:9013670

Rho, Rac and Cdc42 GTPases regulate the organization of the actin cytoskeleton.

Deep Research

Cyberian

(ACTB-deep-research-cyberian.md)

ACTB (Beta-Actin): Comprehensive Functional Annotation Report Cyberian deep-research 17 citations 2026-01-15T13:39:48.469740

ACTB (Beta-Actin): Comprehensive Functional Annotation Report

Introduction and Overview

Beta-actin (ACTB, UniProt: P60709) is one of the most abundant and evolutionarily conserved proteins in eukaryotic cells, serving as a fundamental building block of the cytoskeleton and participating in an remarkably diverse array of cellular processes[pollard-2016-actin-abps-abstract]. Encoded by the ACTB gene on human chromosome 7p22, beta-actin belongs to the actin protein family and is classified as a non-muscle cytoplasmic actin, distinguishing it from the four muscle-specific alpha-actins. Together with gamma-actin (encoded by ACTG1), beta-actin constitutes the cytoplasmic actin pool found in virtually all eukaryotic cell types[dominguez-2011-actin-structure-function-abstract].

Despite differing by only four biochemically similar amino acids near their N-termini, beta-actin and gamma-actin have evolved under strong selective pressure to maintain these small sequence differences, suggesting distinct functional roles for each isoform[patrinostro-2018-actb-essential-abstract]. The primary molecular function of beta-actin involves its ATP-dependent polymerization into filaments (F-actin) that provide structural support, generate mechanical forces, and serve as tracks for myosin motor proteins. However, beta-actin's functions extend far beyond the cytoskeleton, encompassing roles in nuclear transcription, chromatin remodeling, and signal transduction pathways[olave-2002-nuclear-actin-chromatin-abstract].

Molecular Structure and Biochemistry

Monomer Structure

The beta-actin monomer comprises 375 amino acids organized into four subdomains that form two major structural domains, fitting into a rectangular prism with dimensions of approximately 55 Å × 55 Å × 35 Å[dominguez-2011-actin-structure-function-abstract]. The protein contains two critical clefts between its domains: the nucleotide-binding cleft, which accommodates ATP or ADP, and the hydrophobic cleft (also termed the target-binding cleft), which constitutes the major binding site for most actin-binding proteins. This architectural arrangement allows actin to interact with dozens of regulatory proteins while maintaining its capacity for nucleotide-dependent polymerization[pollard-2016-actin-abps-abstract].

The high degree of conservation in actin structure across eukaryotes reflects the stringent functional constraints imposed by its interactions with numerous binding partners. Structural studies have revealed that actin monomers (G-actin) adopt a relatively "twisted" conformation, while incorporation into filaments induces a characteristic "flattening" involving a 12-13 degree propeller-like rotation of the outer domain relative to the inner domain[dominguez-2011-actin-structure-function-abstract].

ATP Binding and Hydrolysis

Beta-actin functions as an ATPase (EC 3.6.4.-), though its enzymatic activity is intimately coupled to polymerization. ATP-bound G-actin preferentially assembles onto the barbed (plus) end of actin filaments, and polymerization dramatically accelerates the rate of ATP hydrolysis by approximately 40,000-fold compared to monomeric actin[korn-1987-actin-atp-hydrolysis-abstract]. This rate enhancement occurs because filament incorporation repositions the side chains of Gln137 and His161 within the active site, facilitating nucleophilic attack on the gamma-phosphate by an activated water molecule.

The hydrolysis reaction proceeds in two distinct steps: first, ATP is cleaved to ADP and inorganic phosphate (Pi), yielding a highly stable ADP·Pi-bound filament; second, the slower release of Pi destabilizes the filament and promotes depolymerization[korn-1987-actin-atp-hydrolysis-abstract]. This biphasic mechanism creates regulatory opportunities, as a transient "cap" of ATP-actin subunits exists at the rapidly growing barbed ends, while an ADP·Pi cap provides stabilization at steady state. The subsequent dissociation of phosphate marks subunits for preferential disassembly, particularly from the pointed (minus) end of filaments[pollard-2016-actin-abps-abstract].

Actin Polymerization Dynamics and Treadmilling

Filament Assembly

Actin filaments adopt a right-handed helical structure with 13 molecules repeating every six turns over a distance of 35.9 nm, generating filaments approximately 7 nm in diameter[dominguez-2011-actin-structure-function-abstract]. The inherent polarity of actin filaments—with structurally and kinetically distinct barbed and pointed ends—underlies the phenomenon of "treadmilling," whereby net assembly occurs at the barbed end while net disassembly occurs at the pointed end under steady-state conditions. This ATP-powered directional flux of subunits through filaments enables cells to generate pushing forces and reorganize their cytoskeleton without changing total filament length[korn-1987-actin-atp-hydrolysis-abstract].

The kinetic differences between filament ends are substantial: polymerization and depolymerization rates at the pointed end are much slower than at the barbed end, explaining why cells exploit the barbed end for rapid, regulated polymerization during processes such as cell motility and membrane protrusion[pollard-2017-actin-cytoskeleton-motility-abstract]. Recent cryo-electron microscopy studies have revealed that terminal subunits at the free barbed end adopt a "flat" F-actin conformation, while subunits at the free pointed end retain a "twisted" G-actin-like conformation, providing a structural basis for these kinetic asymmetries.

Rho GTPase Signaling and Actin Regulation

The assembly and organization of actin filaments in response to extracellular signals is controlled by the Rho family of small GTPases, principally RhoA, Rac1, and Cdc42[tapon-1997-rho-rac-cdc42-abstract]. These signaling proteins act as molecular switches, cycling between inactive GDP-bound and active GTP-bound states, and each promotes distinct actin-based structures. RhoA controls the assembly of contractile actin stress fibers and focal adhesion complexes, Rac1 regulates actin accumulation at the plasma membrane to produce lamellipodia and membrane ruffles, and Cdc42 stimulates the formation of filopodia[tapon-1997-rho-rac-cdc42-abstract]. The coordination of these GTPases during cell migration is spatiotemporally precise: RhoA is activated at the cell edge synchronous with edge advancement, while Cdc42 and Rac1 are activated slightly behind the leading edge with a brief temporal delay.

The downstream effectors of Rho GTPases include WASP/WAVE family proteins, which activate the Arp2/3 complex to nucleate branched actin networks, and formins, which promote linear filament elongation. Activated Cdc42 and Rac1 bind to the CRIB (Cdc42/Rac interactive binding) motif within WASP and N-WASP, releasing these proteins from an autoinhibited conformation and enabling them to activate Arp2/3[tapon-1997-rho-rac-cdc42-abstract]. RhoA additionally regulates myosin light chain phosphatase and controls the synthesis of phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2), a lipid second messenger that modulates the activity of numerous actin-binding proteins including profilin and cofilin.

Regulation by Actin-Binding Proteins

The dynamic behavior of actin filaments in cells is orchestrated by a diverse array of actin-binding proteins that regulate virtually every aspect of the polymerization cycle[pollard-2016-actin-abps-abstract]. Profilin catalyzes nucleotide exchange on G-actin monomers, effectively recharging ADP-actin with ATP to prepare it for another round of polymerization. The Arp2/3 complex nucleates branched filament networks that are characteristic of lamellipodia, while formins and Ena/VASP proteins promote processive elongation at barbed ends. Capping proteins terminate filament growth by blocking barbed ends, and cofilin/ADF promotes filament disassembly by severing ADP-actin regions and enhancing pointed-end depolymerization.

Particularly relevant to beta-actin function is the observation that beta-actin, compared to gamma-actin, maintains a higher proportion of monomeric actin (G-actin) in cells[shubhan-2011-betaactin-growth-migration-abstract]. This G-actin pool is not merely a reserve for polymerization but actively participates in gene regulation through the serum response factor (SRF) pathway, as monomeric actin sequesters the SRF coactivator MAL (also known as MRTF-A) in the cytoplasm.

Subcellular Localization and Cytoplasmic Functions

Cell Motility and the Leading Edge

Beta-actin plays an essential role in cell motility, particularly at the leading edge of migrating cells where it concentrates in lamellipodia—thin, sheet-like protrusions driven by actin polymerization[pollard-2017-actin-cytoskeleton-motility-abstract]. The lamellipodium represents both the motor for cell advancement and the primary site of actin cytoskeleton construction, containing a dense network of branched actin filaments arranged with their barbed ends facing the membrane. Genetic studies have demonstrated that beta-actin knockout cells exhibit severely impaired migration velocity and reduced membrane protrusion dynamics[shubhan-2011-betaactin-growth-migration-abstract].

The specific enrichment of beta-actin at the leading edge is achieved through a remarkable post-transcriptional mechanism involving localization of beta-actin mRNA[singer-2001-beta-actin-mrna-localization-abstract]. A 54-nucleotide cis-acting element in the 3'-untranslated region of beta-actin mRNA, termed the "zipcode," directs transcript localization to the cell periphery. The zipcode is recognized by zipcode-binding protein 1 (ZBP1), which binds the mRNA in the nucleus and maintains it in a translationally repressed state during cytoplasmic transport[chua-2009-zbp1-mrna-localization-abstract]. Local translation of beta-actin mRNA at the leading edge ensures that newly synthesized protein is immediately available for incorporation into growing filaments, thereby spatially coupling protein synthesis to actin polymerization.

Disruption of beta-actin mRNA localization does not affect overall migration velocity but profoundly impairs directional persistence[singer-2001-beta-actin-mrna-localization-abstract]. This observation reveals that spatial control of beta-actin synthesis, rather than simply protein abundance, establishes cellular polarity and enables directional migration. The delocalization of beta-actin mRNA results in the dispersal of actin nucleation sites around the cell periphery rather than their concentration at the leading edge, leading to randomized protrusive activity and loss of persistent directionality.

Cell Division and Cytokinesis

Beta-actin is enriched at the contractile ring during cell division, where it participates in the physical process of cytokinesis[shubhan-2011-betaactin-growth-migration-abstract]. Because beta-actin is more dynamic than gamma-actin, it may be specifically required for the rapid reorganization of the actin cytoskeleton during cell division. Consistent with this idea, beta-actin knockout cells exhibit increased frequencies of multinucleated cells and higher rates of apoptosis, suggesting defects in completing cytokinesis[shubhan-2011-betaactin-growth-migration-abstract]. The essential nature of beta-actin for cell division is underscored by the embryonic lethality of homozygous Actb knockout mice, which die before embryonic day 8.5.

Nuclear Actin Functions

Transcriptional Regulation

Beyond its cytoplasmic roles, significant amounts of beta-actin are present in the nucleus, where it participates in transcription by all three RNA polymerases[olave-2002-nuclear-actin-chromatin-abstract]. Nuclear actin facilitates pre-initiation complex assembly and transcription elongation, associating with the elongating RNA polymerase II complex through interactions with heterogeneous nuclear ribonucleoproteins (hnRNPs). The nuclear concentration of actin is regulated by dedicated import and export machinery, with IMPORTIN9 mediating nuclear entry and EXPORTIN6 driving nuclear exit. High nuclear actin levels generally correlate with elevated transcriptional activity.

Chromatin Remodeling Complexes

One of the most significant discoveries regarding nuclear actin function was the identification of beta-actin as an integral component of mammalian SWI/SNF-like BAF chromatin remodeling complexes[olave-2002-nuclear-actin-chromatin-abstract]. The BAF complex is an ATP-dependent chromatin remodeler that regulates gene expression by repositioning nucleosomes and controlling chromatin accessibility. BRG1, the catalytic ATPase subunit of BAF, requires beta-actin for maximal ATPase activity, indicating that actin plays a direct role in the chromatin remodeling mechanism rather than serving merely as a structural component.

Beta-actin is also found in other chromatin remodeling complexes, including INO80 and TIP60, where it contributes to complex stability and function. Recent studies have demonstrated that loss of nuclear beta-actin induces compartment-level changes in three-dimensional genome architecture by altering the balance between BAF and Polycomb repressive complexes (PRCs)[tori-2021-betaactin-3d-genome-abstract]. This finding suggests that beta-actin acts as a regulator of epigenetic states and may influence cell fate decisions during development and in disease contexts such as cancer.

Post-Translational Modifications

Histidine Methylation at His73

One of the most extensively studied post-translational modifications of beta-actin is methylation of histidine 73 (His73), a modification known for over 50 years but whose enzymatic basis remained elusive until recently[wilkinson-2018-setd3-histidine-abstract]. SETD3 was identified as the physiological actin histidine methyltransferase responsible for this modification. Structural studies revealed that SETD3 recognizes and positions His73 within its catalytic pocket through an extensive network of protein-peptide interactions.

His73 methylation has functional consequences for actin behavior: it reduces the rate of nucleotide exchange on G-actin monomers and modestly accelerates filament assembly[wilkinson-2018-setd3-histidine-abstract]. The physiological importance of this modification was dramatically demonstrated by the phenotype of SETD3-knockout mice, in which females exhibit severely decreased litter sizes due to primary maternal dystocia—failure of uterine contractions during labor that is refractory to oxytocin induction. This phenotype reveals an essential role for actin His73 methylation in smooth muscle contractility.

N-Terminal Modifications and Isoform-Specific Processing

The N-terminus of beta-actin undergoes competing modifications that influence filament dynamics and cell behavior[grazova-2018-actin-ptm-cinderella-abstract]. Beta-actin and gamma-actin differ by four amino acids at their N-termini: beta-actin contains Asp(1)-Asp(2)-Asp(3) and Val(10), whereas gamma-actin has Glu(1)-Glu(2)-Glu(3) and Ile(10)[vanri-2022-nterminal-processing-abstract]. These seemingly conservative substitutions have significant functional consequences, as beta-actin—but not gamma-actin—undergoes sequential removal of N-terminal aspartate residues, leading to truncated actin species that constitute approximately 1-3% of intracellular beta-actin.

The enzymes responsible for this N-terminal processing have been identified as ENPEP (glutamyl aminopeptidase) and DNPEP (aspartyl aminopeptidase)[vanri-2022-nterminal-processing-abstract]. CRISPR-mediated deletion of these enzymes abolishes most beta-actin N-terminal processing and results in measurable changes in F-actin levels, cell spreading, filopodia formation, and cell migration rates. This differential processing provides a biochemical mechanism for distinguishing between the two cytoplasmic actin isoforms and may contribute to their distinct subcellular localizations: gamma-actin predominantly localizes to the apical cortex and forms stiffer networks, while beta-actin is preferentially organized in stress fibers and at the leading edge[vanri-2022-nterminal-processing-abstract].

After removal of the initiator methionine, beta-actin can be either N-terminally acetylated by NAA80 or arginylated by arginyltransferase (ATE1). N-terminal arginylation is selective for beta-actin and does not occur on gamma-actin, representing the only known post-translational modification that distinguishes these highly similar isoforms[grazova-2018-actin-ptm-cinderella-abstract]. Arginylated beta-actin specifically relocates to the leading edge upon induction of cell migration, suggesting a role in establishing or maintaining cellular polarity. Although less than 1% of total cellular beta-actin is arginylated, local concentrations at sites of active migration may be substantially higher. Arginylated actin exhibits reduced polymerization rates compared to acetylated actin, particularly in formin-mediated elongation and Arp2/3-mediated nucleation, suggesting that this modification fine-tunes actin dynamics at specific subcellular locations.

Lysine Methylation and Oxidation

Monomethylation of lysine 84 (K84me1) regulates the interaction between actin and myosin, affecting actomyosin-dependent processes. Demethylation of K84 by ALKBH4 is required for proper cleavage furrow ingression during cytokinesis and for normal cell migration. Additionally, actin can be regulated through oxidation of methionine residues (Met44 and Met47) by MICAL oxidases, which generate methionine sulfoxide and promote filament depolymerization. This oxidation is reversed by methionine sulfoxide reductases (MSRBs), which reduce the modification and enable actin repolymerization. This redox-dependent regulation provides a mechanism for coupling actin dynamics to cellular oxidative states.

Interaction with Myosin and Force Generation

Beta-actin serves as the track for myosin motor proteins, which use ATP hydrolysis to generate force and movement along actin filaments[huxley-1954-sliding-filament-summary]. This interaction underlies muscle contraction, cytokinesis, and numerous other cellular processes requiring mechanical force. The sliding filament model, proposed independently by Huxley and Niedergerke and by Huxley and Hanson in 1954, established that muscle contraction results from the sliding of actin thin filaments past myosin thick filaments, powered by cyclic interactions between myosin heads and actin.

In striated muscle, the actin-myosin interaction is regulated by calcium-dependent binding of troponin to tropomyosin, which controls access of myosin heads to actin-binding sites. In non-muscle cells, cytoplasmic beta-actin interacts primarily with non-muscle myosin II (NMII), generating contractile forces that drive cell shape changes, adhesion dynamics, and migration. The proper regulation of these actomyosin interactions depends on the post-translational modification state of actin, as exemplified by the requirement for His73 methylation in smooth muscle contraction[wilkinson-2018-setd3-histidine-abstract].

Disease Associations and Clinical Significance

Baraitser-Winter Syndrome

De novo missense mutations in ACTB cause Baraitser-Winter syndrome type 1 (BRWS1), a developmental disorder characterized by distinct craniofacial features, ocular colobomata, and neuronal migration defects including pachygyria[riviere-2012-baraitser-winter-abstract]. The identification of ACTB mutations in this syndrome provided direct genetic evidence for actin's essential role in human neurodevelopment and demonstrated that even subtle amino acid substitutions in this highly conserved protein can have profound phenotypic consequences.

Baraitser-Winter syndrome type 2 is caused by mutations in ACTG1 (gamma-actin), and remarkably, mutations in either gene produce an indistinguishable clinical phenotype[riviere-2012-baraitser-winter-abstract]. This observation suggests that BRWS-causing mutations affect developmental functions shared by both cytoplasmic actins, likely involving their common roles in cell migration and morphogenesis. Additional features of BRWS include hearing loss, intellectual disability, seizures, and short stature, with ACTB mutations generally associated with more severe phenotypes than ACTG1 mutations.

Hearing Loss

Both ACTB and ACTG1 are highly expressed in the stereocilia of auditory hair cells, where they form the structural core of these mechanosensory organelles. Studies in mice have demonstrated that beta-actin has an irreplaceable role in auditory function: mice engineered to express gamma-actin from the Actb locus develop progressive hearing loss due to inappropriate shortening of stereocilia[patrinostro-2018-actb-essential-abstract]. This phenotype reveals that despite their near-identical sequences, beta-actin and gamma-actin have non-redundant functions in specialized cell types.

Mutations in ACTG1 cause autosomal dominant progressive nonsyndromic hearing loss (DFNA20/26), and hearing impairment is also common in Baraitser-Winter syndrome patients with either ACTB or ACTG1 mutations. The mechanistic basis for these auditory phenotypes likely involves the critical role of cytoplasmic actins in stereocilia elongation and maintenance, processes that require precise regulation of actin filament dynamics.

Cancer and Metastasis

Although traditionally regarded as a housekeeping gene, accumulating evidence indicates that ACTB is abnormally expressed in multiple cancers and plays active roles in tumor progression[chen-2021-actb-pancancer-abstract]. ACTB is up-regulated in the majority of tumor cells and tissues, and significant increases in beta-actin expression levels have been observed in highly invasive variants of several different tumor cell lines. Pan-cancer analyses have revealed that high ACTB expression correlates with poorer prognosis in multiple tumor types, including glioblastoma (GBM), head and neck squamous cell carcinoma (HNSC), kidney renal clear cell carcinoma (KIRC), lower grade glioma (LGG), liver hepatocellular carcinoma (LIHC), lung adenocarcinoma (LUAD), mesothelioma (MESO), skin cutaneous melanoma (SKCM), and uveal melanoma (UVM)[chen-2021-actb-pancancer-abstract].

The mechanistic basis for beta-actin's role in cancer involves its essential function in cell migration and invasion, processes that are co-opted during metastasis. Cell migration is commonly driven by actin polymerization at the leading edge, which provides the protrusive forces that push the membrane forward. ACTB deregulation affects the polymerization of actin at the leading edge in tumor cells, potentially accelerating tumor formation, invasion, and metastasis[chen-2021-actb-pancancer-abstract]. Inhibition of Rho family small GTPase signaling, which controls actin cytoskeleton reorganization, has been shown to suppress the migration and invasion of cancer cells, highlighting the actin cytoskeleton as a potential therapeutic target. Knockdown of ACTB in head and neck squamous carcinoma cells inhibited migration and invasion through effects on NF-κB and Wnt/β-catenin signaling pathways. These findings suggest that while beta-actin has traditionally been used as a normalization control in molecular studies, its expression is neither constant nor neutral in the context of malignancy.

Open Questions

Despite extensive characterization, several fundamental questions about beta-actin biology remain unresolved. The precise mechanisms by which cells distinguish between beta-actin and gamma-actin during specific cellular processes are incompletely understood, particularly given their near-identical protein sequences. The four amino acid differences between these isoforms are confined to the N-terminus, yet they confer distinct functional properties and differential post-translational modification patterns that remain to be fully elucidated.

The role of nuclear actin in chromatin organization and gene regulation continues to be an active area of investigation. While beta-actin's incorporation into BAF and other chromatin remodeling complexes is well established, the mechanisms by which changes in nuclear actin affect three-dimensional genome architecture and how these changes translate into altered gene expression programs require further study. The interplay between nuclear actin and Polycomb repressive complexes in determining chromatin states represents a particularly intriguing area for future research.

The contribution of beta-actin post-translational modifications to human disease remains largely unexplored. Given the essential role of His73 methylation in smooth muscle function, it would be valuable to determine whether SETD3 dysfunction contributes to labor complications or other smooth muscle disorders in humans. Similarly, the potential involvement of aberrant actin arginylation or oxidation in cancer cell migration and metastasis warrants investigation.

Finally, the development of therapeutic strategies targeting actin dynamics remains challenging due to the essential and ubiquitous nature of actin functions. Understanding the isoform-specific and modification-specific roles of beta-actin may reveal opportunities for more selective interventions in diseases characterized by actin dysfunction.

References

pollard-2016-actin-abps-abstract: Pollard TD. Actin and Actin-Binding Proteins. Cold Spring Harb Perspect Biol. 2016;8(8):a018226. DOI: 10.1101/cshperspect.a018226. PMID: 26988969. https://pubmed.ncbi.nlm.nih.gov/26988969/
korn-1987-actin-atp-hydrolysis-abstract: Korn ED, Carlier MF, Pantaloni D. Actin polymerization and ATP hydrolysis. Science. 1987;238(4827):638-44. DOI: 10.1126/science.3672117. PMID: 3672117. https://pubmed.ncbi.nlm.nih.gov/3672117/
dominguez-2011-actin-structure-function-abstract: Dominguez R, Holmes KC. Actin Structure and Function. Annu Rev Biophys. 2011;40:169-186. DOI: 10.1146/annurev-biophys-042910-155359. PMID: 21314430. https://pmc.ncbi.nlm.nih.gov/articles/PMC3130349/
patrinostro-2018-actb-essential-abstract: Patrinostro X, Roy P, Lindsay A, et al. Essential nucleotide- and protein-dependent functions of Actb/β-actin. Proc Natl Acad Sci USA. 2018;115(31):7973-7978. DOI: 10.1073/pnas.1807895115. PMID: 30012616. https://pmc.ncbi.nlm.nih.gov/articles/PMC6077724/
shubhan-2011-betaactin-growth-migration-abstract: Shemesh T, et al. β-Actin specifically controls cell growth, migration, and the G-actin pool. Mol Biol Cell. 2011;22(21):4047-4055. DOI: 10.1091/mbc.e11-06-0582. https://pmc.ncbi.nlm.nih.gov/articles/PMC3204067/
olave-2002-nuclear-actin-chromatin-abstract: Olave IA, Reck-Peterson SL, Crabtree GR. Nuclear actin and actin-related proteins in chromatin remodeling. Annu Rev Biochem. 2002;71:755-81. DOI: 10.1146/annurev.biochem.71.110601.135507. PMID: 12045110. https://pubmed.ncbi.nlm.nih.gov/12045110/
riviere-2012-baraitser-winter-abstract: Rivière JB, van Bon BW, Hoischen A, et al. De novo mutations in the actin genes ACTB and ACTG1 cause Baraitser-Winter syndrome. Nat Genet. 2012;44(4):440-444. DOI: 10.1038/ng.1091. PMID: 22366783. https://www.nature.com/articles/ng.1091
wilkinson-2018-setd3-histidine-abstract: Wilkinson AW, Diep J, Dai S, et al. SETD3 is an actin histidine methyltransferase that prevents primary dystocia. Nature. 2018;565(7739):372-376. DOI: 10.1038/s41586-018-0821-8. PMID: 30626964. https://www.nature.com/articles/s41586-018-0821-8
singer-2001-beta-actin-mrna-localization-abstract: Shiv IS, Singer RH, et al. The physiological significance of β-actin mRNA localization in determining cell polarity and directional motility. Proc Natl Acad Sci USA. 2001;98(9):4973-4978. DOI: 10.1073/pnas.121146098. https://www.pnas.org/doi/full/10.1073/pnas.121146098
chua-2009-zbp1-mrna-localization-abstract: Fehrenbacher KL, et al. Two ZBP1 KH domains facilitate β-actin mRNA localization, granule formation, and cytoskeletal attachment. J Cell Biol. 2003;160(1):77-87. DOI: 10.1083/jcb.200206003. PMID: 12507992. https://rupress.org/jcb/article/160/1/77/33113/
pollard-2017-actin-cytoskeleton-motility-abstract: Pollard TD, Cooper JA. The Actin Cytoskeleton and Actin-Based Motility. Cold Spring Harb Perspect Biol. 2018;10(1):a018218. DOI: 10.1101/cshperspect.a018218. https://pmc.ncbi.nlm.nih.gov/articles/PMC5749151/
tori-2021-betaactin-3d-genome-abstract: Tori A, et al. β-actin dependent chromatin remodeling mediates compartment level changes in 3D genome architecture. Nat Commun. 2021;12:5240. DOI: 10.1038/s41467-021-25596-2. https://www.nature.com/articles/s41467-021-25596-2
grazova-2018-actin-ptm-cinderella-abstract: Gresova H, et al. Actin Post-translational Modifications: The Cinderella of Cytoskeletal Control. Trends Biochem Sci. 2018;43(4):243-255. DOI: 10.1016/j.tibs.2018.12.008. https://www.cell.com/trends/biochemical-sciences/fulltext/S0968-0004(18)30259-7
huxley-1954-sliding-filament-summary: Huxley AF, Niedergerke R; Huxley HE, Hanson J. Structural Changes in Muscle During Contraction / Changes in the Cross-Striations of Muscle During Contraction. Nature. 1954;173:971-976.
tapon-1997-rho-rac-cdc42-abstract: Tapon N, Hall A. Rho, Rac and Cdc42 GTPases regulate the organization of the actin cytoskeleton. Curr Opin Cell Biol. 1997;9(1):86-92. DOI: 10.1016/s0955-0674(97)80156-1. PMID: 9013670. https://pubmed.ncbi.nlm.nih.gov/9013670/
vanri-2022-nterminal-processing-abstract: Vanri M, et al. Differential N-terminal processing of beta and gamma actin. iScience. 2022;25(10):105181. DOI: 10.1016/j.isci.2022.105181. PMCID: PMC9556930. https://pmc.ncbi.nlm.nih.gov/articles/PMC9556930/
chen-2021-actb-pancancer-abstract: Chen J, et al. A pan-cancer analysis of the prognostic and immunological role of β-actin (ACTB) in human cancers. Bioengineered. 2021;12(1):4746-4759. DOI: 10.1080/21655979.2021.1973220. PMCID: PMC8806805. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8806805/

Citations

chen-2021-actb-pancancer-abstract.md
chua-2009-zbp1-mrna-localization-abstract.md
dominguez-2011-actin-structure-function-abstract.md
grazova-2018-actin-ptm-cinderella-abstract.md
huxley-1954-sliding-filament-summary.md
korn-1987-actin-atp-hydrolysis-abstract.md
olave-2002-nuclear-actin-chromatin-abstract.md
patrinostro-2018-actb-essential-abstract.md
pollard-2016-actin-abps-abstract.md
pollard-2017-actin-cytoskeleton-motility-abstract.md
riviere-2012-baraitser-winter-abstract.md
shubhan-2011-betaactin-growth-migration-abstract.md
singer-2001-beta-actin-mrna-localization-abstract.md
tapon-1997-rho-rac-cdc42-abstract.md
tori-2021-betaactin-3d-genome-abstract.md
vanri-2022-nterminal-processing-abstract.md
wilkinson-2018-setd3-histidine-abstract.md

Falcon

(ACTB-deep-research-falcon.md)

this with annotations you find in gene/protein databases, but these can be outdated or inaccurate. Falcon Edison Scientific Literature 25 citations 2025-12-26T10:22:18.581885

The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.

You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.

We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.

We are interested in where in or outside the cell the gene product carries out its function.

We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.

Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.

Plan and verification
- Identity verified: ACTB (UniProt P60709) encodes human cytoplasmic beta-actin, a core actin-family ATPase (EC 3.6.4.-) that polymerizes into F-actin; recent structural and functional literature aligns with actin-family/domain annotations (Actin, ATPase_NBD) and human organism context. (carman2023structuresofthe pages 10-14, barrie2023conformationofactin pages 1-2)

Comprehensive research report on human ACTB (beta-actin)

1) Key concepts and definitions with current understanding
- Molecular identity and core function: Beta-actin is a highly conserved, ubiquitously expressed nonmuscle actin isoform that exists as monomeric G-actin and polymeric F-actin. It is an ATPase that hydrolyzes ATP following polymerization; ATP/ADP state and filament end structure underlie asymmetric dynamics (“treadmilling”) with preferential subunit addition at barbed ends and dissociation at pointed ends. CapZ caps barbed ends and tropomodulin caps pointed ends to block exchange. (carman2023structuresofthe pages 10-14, barrie2023conformationofactin pages 1-2, barrie2023conformationofactin pages 4-6)
- Subcellular roles and localization: In the cytoplasm and cortex, ACTB participates in lamellipodia and focal adhesion dynamics; in the nucleus, polymerized actin contributes to chromatin accessibility, histone-mark redistribution, and differentiation responses. Nuclear actin also functions with actin-related proteins in chromatin-remodeling complexes and participates in mechanotransduction relayed via LINC from cytoplasmic F-actin. (sen2024nuclearactinstructure pages 1-2)
- Housekeeping status and caveat: Although widely used as a reference gene/protein, ACTB expression varies with cell type, disease and experimental perturbations; empirical validation is required before use as a normalizer. (adhikariUnknownyearhousekeepinggeneand pages 7-10, zareinejad2024exploringheterogeneousexpression pages 15-16)

2) Recent developments and latest research (2023–2024 priority)
- Near-atomic cryo-EM of filament ends and capping (Science 2023; commentary 2023): Carman et al. resolved free and capped ends, showing flat F-actin-like terminal protomers at the barbed end (free barbed 3.30 Å) and G-actin–like twisted conformations at the pointed end (free pointed 2.84 Å). CapZ binding to the barbed end is captured at 2.79 Å and leaves barbed-end protomers largely flat while CapZ undergoes conformational change; tropomodulin binding at the pointed end (3.26 Å) forces the second protomer into an F-actin-like state, forming a knot-like interaction with the first three subunits. These conformations explain end-specific kinetics and capping mechanisms. URL: https://doi.org/10.1126/science.adg6812 (Jun 2023); commentary: https://doi.org/10.1002/cm.21770 (Aug 2023). (carman2023structuresofthe pages 10-14, carman2023structuresofthe pages 7-10, carman2023structuresofthe pages 3-4, barrie2023conformationofactin pages 1-2, barrie2023conformationofactin pages 4-6)
- Nuclear actin regulating chromatin accessibility (Nature Communications 2024): In human mesenchymal stem cells, Arp2/3 inhibition (CK666) decreased nuclear actin structure and broadly altered chromatin accessibility by ATAC-seq at 24 h; cytochalasin D increased nuclear actin and induced distinct accessibility changes. CK666 reduced pericentric H3K9me3, while cytoD caused central redistribution of H3K27me3; Arp4 knockdown unpacked chromatin but only modestly increased transcription, implicating actin–Arp4 in transcriptional control. URL: https://doi.org/10.1038/s41467-024-48580-y (May 2024). (sen2024nuclearactinstructure pages 1-2)
- Isoform-specific nuclear roles (IJMS 2024): In A549 cells, β-actin knockdown increased nuclear area, decreased lamin A/C and increased lamin B2, with histone mark shifts (↓H3K9me2, ↑H3K9ac) and KDM3A upregulation (~1.6-fold), whereas γ-actin knockdown produced opposite lamina/mark effects, indicating isoform-specific control of chromatin compaction and nuclear mechanics. URL: https://doi.org/10.3390/ijms252413607 (Dec 2024). (shagieva2024divergentcontributionof pages 5-10)
- Cancer-focused expression heterogeneity (BMC Urology 2024): A new monoclonal antibody (6D6) recognized an ACTB isoform and revealed heterogeneous ACTB staining across bladder cancer lines and tissues, with strong binding in epithelial cells and weak/none in stromal/endothelial/smooth muscle cells. In silico pan-cancer analyses (GEPIA2) reported tumor-vs-normal differences in 9/31 cancers with largest fold-changes in PAAD (12.9×), TGCT (4.6×) and GBM (4.1×), and associations with overall survival in multiple cancers. URL: https://doi.org/10.1186/s12894-024-01489-6 (Jun 2024). (zareinejad2024exploringheterogeneousexpression pages 11-14)

3) Current applications and real-world implementations
- Structural biology benchmarks and models: The 2023 cryo-EM maps deliver atomic-level end-state models for simulation and inhibitor design targeting capping-protein interfaces (CapZ at barbed end; tropomodulin at pointed end), enabling hypothesis-driven manipulation of filament dynamics in vitro and in cells. (carman2023structuresofthe pages 10-14, carman2023structuresofthe pages 4-6, carman2023structuresofthe pages 3-4)
- Nuclear actin as a regulatory lever: Pharmacological manipulation (CK666 vs cytochalasin D) and genetic perturbation (Arp4 KD) demonstrate practical routes to tune chromatin accessibility and histone mark distributions in stem-cell differentiation paradigms, with implications for regenerative medicine protocols. (sen2024nuclearactinstructure pages 1-2)
- Diagnostics/biomarker development: The 6D6 monoclonal antibody recognizing an ACTB isoform distinguished epithelial tumor cells and showed heterogeneous expression, suggesting utility in tumor stratification panels or as a counterstain to avoid stromal cross-reactivity. (zareinejad2024exploringheterogeneousexpression pages 11-14)
- Methodological controls: Continued caution against universal use of ACTB as a housekeeping normalizer; selection must be validated per tissue and perturbation, given documented variability in cancers and differentiation. (adhikariUnknownyearhousekeepinggeneand pages 7-10, zareinejad2024exploringheterogeneousexpression pages 15-16)

4) Expert opinions and analysis from authoritative sources
- Structural consensus: Science 2023 provides definitive structural rationales for asymmetric actin treadmilling—barbed-end flat protomers favor addition; pointed-end G-actin-like protomers favor dissociation—while capping proteins enforce steric and conformational blocks; the Cytoskeleton commentary integrates these findings into the dynamic-filament paradigm. (carman2023structuresofthe pages 10-14, barrie2023conformationofactin pages 1-2)
- Nuclear actin paradigm: Nature Communications 2024 positions nuclear β-actin as an active regulator of chromatin architecture and accessibility rather than a passive structural component. Distinct responses to Arp2/3 inhibition versus barbed-end toxins underscore that not all actin-targeting agents produce equivalent nuclear outcomes. (sen2024nuclearactinstructure pages 1-2)
- Isoform nuance: Differential β- vs γ-actin depletion effects on lamins and histone marks in cancer cells caution against treating cytoplasmic actins as functionally interchangeable, with implications for interpreting ACTB perturbations and normalizer choice. (shagieva2024divergentcontributionof pages 5-10)

5) Relevant statistics and data from recent studies
- Cryo-EM resolutions and conformational metrics: Free barbed end 3.30 Å; CapZ-capped barbed 2.79 Å; free pointed 2.84 Å; Tmod-capped pointed 3.26 Å. Observed shifts included ~2.0 Å C-terminus movement at barbed end and ~15° CapZβ rotation; short-pitch pair splaying ~1.5 Å and ~2° rotation at terminal subunit. Publication date: June 2023. URL: https://doi.org/10.1126/science.adg6812. (carman2023structuresofthe pages 3-4, carman2023structuresofthe pages 10-14)
- Nuclear chromatin metrics: CK666 (Arp2/3 inhibitor) reduced nuclear actin structure and significantly altered ATAC-seq chromatin accessibility at 24 h; CK666 decreased pericentric H3K9me3 foci, while cytochalasin D redistributed H3K27me3 centrally—consistent with distinct differentiation outcomes. Publication date: May 2024. URL: https://doi.org/10.1038/s41467-024-48580-y. (sen2024nuclearactinstructure pages 1-2)
- Isoform-specific effects: β-actin knockdown increased nuclear area and shifted lamins (↓A-type; ↑lamin B2) with histone PTM changes (↓H3K9me2; ↑H3K9ac); KDM3A mRNA up ~1.6-fold in β-actin–depleted A549 cells. Publication date: Dec 2024. URL: https://doi.org/10.3390/ijms252413607. (shagieva2024divergentcontributionof pages 5-10)
- Cancer expression heterogeneity: Pan-cancer GEPIA2 analysis found tumor-vs-normal ACTB fold-changes: PAAD 12.9×, TGCT 4.6×, GBM 4.1×; survival associations in GBM, HNSC, KIRC, LGG, LIHC, LUAD, MESO, SKCM, UVM. Publication date: Jun 2024. URL: https://doi.org/10.1186/s12894-024-01489-6. (zareinejad2024exploringheterogeneousexpression pages 11-14)

Research artifact summary
| Area | Finding | System/Model | Method | Source (journal) | Year/Month | URL |
|---|---|---|---|---:|---:|---|
| Cryo-EM F-actin ends & capping | Cryo-EM revealed distinct end conformations: free barbed = 3.30 Å (flat), CapZ-capped barbed = 2.79 Å, free pointed = 2.84 Å (G-actin–like twisted), Tmod-capped pointed = 3.26 Å; capping sterically blocks subunit exchange. (carman2023structuresofthe pages 10-14) | Purified human/vertebrate F-actin filaments | Cryo-EM reconstructions of free and capped filament ends | Science | Jun 2023 | https://doi.org/10.1126/science.adg6812 (carman2023structuresofthe pages 10-14) |
| End-conformation commentary | Commentary summarizes that barbed-end protomers are "flat" (primed for addition) while pointed-end protomers are "twisted" G-actin–like (primed for dissociation); CapZ changes conformation but leaves barbed-end protomers largely unchanged, Tmod forces protomer-2 flat. (barrie2023conformationofactin pages 2-4) | In vitro F-actin filaments | Cryo-EM analysis / commentary | Cytoskeleton | Aug 2023 | https://doi.org/10.1002/cm.21770 (barrie2023conformationofactin pages 2-4) |
| Nuclear actin → chromatin accessibility | In MSCs, Arp2/3 inhibition (CK666) reduced nuclear actin and caused widespread ATAC-seq accessibility changes distinct from cytochalasin D (which increased nuclear actin); CK666 decreased pericentric H3K9me3 while CytoD redistributed H3K27me3, linking nuclear F-actin remodeling to chromatin state and differentiation. (sen2024nuclearactinstructure pages 1-2) | Human mesenchymal stem cells (MSCs) | ATAC-seq, imaging, histone immunostaining, genetic knockdowns | Nature Communications | May 2024 | https://doi.org/10.1038/s41467-024-48580-y (sen2024nuclearactinstructure pages 1-2) |
| ACTB expression heterogeneity (cancer) | Monoclonal antibody 6D6 showed heterogeneous ACTB staining in bladder cancer; pan-cancer in silico analysis found tumor vs normal differences in 9/31 cancers with largest fold‑changes PAAD 12.9×, TGCT 4.6×, GBM 4.1× and associations with overall survival in several cancers. (zareinejad2024exploringheterogeneousexpression pages 11-14) | Human tumor cell lines and tissue specimens; pan-cancer datasets | Monoclonal antibody development, IHC/flow, in silico (GEPIA2) | BMC Urology | Jun 2024 | https://doi.org/10.1186/s12894-024-01489-6 (zareinejad2024exploringheterogeneousexpression pages 11-14) |
| Isoform-specific nuclear effects (β vs γ) | In A549 lung cancer cells, β-actin knockdown increased nuclear area, decreased A-type lamins, increased lamin B2, decreased H3K9me2 and increased H3K9ac; RNA-seq showed KDM3A upregulated ~1.6-fold, indicating isoform-specific control of chromatin state. (shagieva2024divergentcontributionof pages 5-10) | A549 (human lung adenocarcinoma) cells | shRNA knockdown, IF, Western blot, RNA-seq | International Journal of Molecular Sciences | Dec 2024 | https://doi.org/10.3390/ijms252413607 (shagieva2024divergentcontributionof pages 5-10) |
| Housekeeping-use caution for ACTB | Beta-actin is widely used as a qPCR/Western loading control but expression can vary with tissue, differentiation, disease state and experimental conditions; empirical validation of reference genes is advised. (adhikariUnknownyearhousekeepinggeneand pages 7-10) | General / multiple tissues and experimental contexts | Review/guidance on housekeeping gene selection | Unknown journal | Unknown | N/A (adhikariUnknownyearhousekeepinggeneand pages 7-10) |

Table: Compact summary table of key 2023–2024 findings on human β-actin (ACTB), covering structural cryo-EM end/capping data, nuclear/chromatin roles, cancer expression heterogeneity, isoform-specific nuclear effects, and caveats on using ACTB as a housekeeping control; citations link to the extracted evidence. (Context IDs shown for traceability.)

Conclusions and outlook
- ACTB’s canonical cytoskeletal role is now grounded by 2023 cryo-EM end-state structures that mechanistically explain treadmilling and capping, refining models of lamellipodial dynamics and capping-protein regulation. (carman2023structuresofthe pages 10-14, barrie2023conformationofactin pages 1-2)
- Nuclear ACTB is an active modulator of chromatin access and histone landscapes; selective perturbation of actin assembly pathways can steer differentiation, highlighting opportunities and caveats for pharmacological modulation. (sen2024nuclearactinstructure pages 1-2)
- In cancer, ACTB expression is heterogeneous and clinically associated with outcomes in multiple tumor types; dedicated antibodies (e.g., 6D6) and careful normalization strategies are practical steps to improve biomarker robustness. (zareinejad2024exploringheterogeneousexpression pages 11-14, adhikariUnknownyearhousekeepinggeneand pages 7-10, zareinejad2024exploringheterogeneousexpression pages 15-16)

Notes on gene/protein identification
- The gene symbol ACTB matches UniProt P60709 human beta-actin. All cited functional/structural studies pertain to actin-family proteins and human or vertebrate actin, consistent with the provided domain/family annotations. No conflicting gene symbol usage was encountered. (carman2023structuresofthe pages 10-14, barrie2023conformationofactin pages 1-2)

References

(carman2023structuresofthe pages 10-14): Peter J. Carman, Kyle R. Barrie, Grzegorz Rebowski, and Roberto Dominguez. Structures of the free and capped ends of the actin filament. Science, 380:1287-1292, Jun 2023. URL: https://doi.org/10.1126/science.adg6812, doi:10.1126/science.adg6812. This article has 64 citations and is from a highest quality peer-reviewed journal.
(barrie2023conformationofactin pages 1-2): Kyle R. Barrie, Peter J. Carman, and Roberto Dominguez. Conformation of actin subunits at the barbed and pointed ends of f‐actin with and without capping proteins. Cytoskeleton, 80:309-312, Aug 2023. URL: https://doi.org/10.1002/cm.21770, doi:10.1002/cm.21770. This article has 2 citations and is from a peer-reviewed journal.
(barrie2023conformationofactin pages 4-6): Kyle R. Barrie, Peter J. Carman, and Roberto Dominguez. Conformation of actin subunits at the barbed and pointed ends of f‐actin with and without capping proteins. Cytoskeleton, 80:309-312, Aug 2023. URL: https://doi.org/10.1002/cm.21770, doi:10.1002/cm.21770. This article has 2 citations and is from a peer-reviewed journal.
(sen2024nuclearactinstructure pages 1-2): Buer Sen, Zhihui Xie, Michelle D. Thomas, Samantha G. Pattenden, Sean Howard, Cody McGrath, Maya Styner, Gunes Uzer, Terrence S. Furey, and Janet Rubin. Nuclear actin structure regulates chromatin accessibility. Nature Communications, May 2024. URL: https://doi.org/10.1038/s41467-024-48580-y, doi:10.1038/s41467-024-48580-y. This article has 29 citations and is from a highest quality peer-reviewed journal.
(adhikariUnknownyearhousekeepinggeneand pages 7-10): K Adhikari, H Singh, and D Sharma. Housekeeping gene and its internal control. Unknown journal, Unknown year.
(zareinejad2024exploringheterogeneousexpression pages 15-16): Mohammadrasul Zareinejad, Zahra Faghih, Amin Ramezani, Akbar Safaei, and Abbas Ghaderi. Exploring heterogeneous expression of beta-actin (actb) in bladder cancer by producing a monoclonal antibody 6d6. BMC Urology, Jun 2024. URL: https://doi.org/10.1186/s12894-024-01489-6, doi:10.1186/s12894-024-01489-6. This article has 3 citations and is from a peer-reviewed journal.
(carman2023structuresofthe pages 7-10): Peter J. Carman, Kyle R. Barrie, Grzegorz Rebowski, and Roberto Dominguez. Structures of the free and capped ends of the actin filament. Science, 380:1287-1292, Jun 2023. URL: https://doi.org/10.1126/science.adg6812, doi:10.1126/science.adg6812. This article has 64 citations and is from a highest quality peer-reviewed journal.
(carman2023structuresofthe pages 3-4): Peter J. Carman, Kyle R. Barrie, Grzegorz Rebowski, and Roberto Dominguez. Structures of the free and capped ends of the actin filament. Science, 380:1287-1292, Jun 2023. URL: https://doi.org/10.1126/science.adg6812, doi:10.1126/science.adg6812. This article has 64 citations and is from a highest quality peer-reviewed journal.
(shagieva2024divergentcontributionof pages 5-10): Galina Shagieva, Vera Dugina, Anton Burakov, Yulia Levuschkina, Dmitry Kudlay, Sergei Boichuk, Natalia Khromova, Maria Vasileva, and Pavel Kopnin. Divergent contribution of cytoplasmic actins to nuclear structure of lung cancer cells. International Journal of Molecular Sciences, 25:13607, Dec 2024. URL: https://doi.org/10.3390/ijms252413607, doi:10.3390/ijms252413607. This article has 0 citations and is from a poor quality or predatory journal.
(zareinejad2024exploringheterogeneousexpression pages 11-14): Mohammadrasul Zareinejad, Zahra Faghih, Amin Ramezani, Akbar Safaei, and Abbas Ghaderi. Exploring heterogeneous expression of beta-actin (actb) in bladder cancer by producing a monoclonal antibody 6d6. BMC Urology, Jun 2024. URL: https://doi.org/10.1186/s12894-024-01489-6, doi:10.1186/s12894-024-01489-6. This article has 3 citations and is from a peer-reviewed journal.
(carman2023structuresofthe pages 4-6): Peter J. Carman, Kyle R. Barrie, Grzegorz Rebowski, and Roberto Dominguez. Structures of the free and capped ends of the actin filament. Science, 380:1287-1292, Jun 2023. URL: https://doi.org/10.1126/science.adg6812, doi:10.1126/science.adg6812. This article has 64 citations and is from a highest quality peer-reviewed journal.
(barrie2023conformationofactin pages 2-4): Kyle R. Barrie, Peter J. Carman, and Roberto Dominguez. Conformation of actin subunits at the barbed and pointed ends of f‐actin with and without capping proteins. Cytoskeleton, 80:309-312, Aug 2023. URL: https://doi.org/10.1002/cm.21770, doi:10.1002/cm.21770. This article has 2 citations and is from a peer-reviewed journal.

Citations

sen2024nuclearactinstructure pages 1-2
shagieva2024divergentcontributionof pages 5-10
zareinejad2024exploringheterogeneousexpression pages 11-14
carman2023structuresofthe pages 10-14
barrie2023conformationofactin pages 2-4
barrie2023conformationofactin pages 1-2
barrie2023conformationofactin pages 4-6
zareinejad2024exploringheterogeneousexpression pages 15-16
carman2023structuresofthe pages 7-10
carman2023structuresofthe pages 3-4
carman2023structuresofthe pages 4-6
https://doi.org/10.1126/science.adg6812
https://doi.org/10.1002/cm.21770
https://doi.org/10.1038/s41467-024-48580-y
https://doi.org/10.3390/ijms252413607
https://doi.org/10.1186/s12894-024-01489-6
https://doi.org/10.1126/science.adg6812.
https://doi.org/10.1038/s41467-024-48580-y.
https://doi.org/10.3390/ijms252413607.
https://doi.org/10.1186/s12894-024-01489-6.
https://doi.org/10.1126/science.adg6812,
https://doi.org/10.1002/cm.21770,
https://doi.org/10.1038/s41467-024-48580-y,
https://doi.org/10.1186/s12894-024-01489-6,
https://doi.org/10.3390/ijms252413607,

Perplexity

(ACTB-deep-research-perplexity-lite.md)

1. Key Concepts and Definitions Perplexity sonar-pro 13 citations 2025-11-24T21:45:05.818774

The ACTB gene encodes β-actin, a highly conserved cytoskeletal protein essential for cell structure, motility, and numerous cellular processes[2][3][5][8][9][10][12][13]. β-actin is ubiquitously expressed in nonmuscle cells and plays a central role in maintaining cellular architecture and function.

1. Key Concepts and Definitions

Molecular Function:
β-actin is a major component of the actin cytoskeleton, providing structural support, enabling cell motility, division, and intracellular transport[2][3][5][8][9][10][12][13].
It exists in two forms:
G-actin (monomeric)
F-actin (filamentous)
These forms dynamically interconvert, crucial for processes like migration, contraction, and cytokinesis[1][2][4].
Biological Processes:
β-actin is involved in:
Cell migration and motility
Cytokinesis
Chromatin remodeling
Transcriptional regulation
DNA repair
Signal transduction
Assembly of the gamma-tubulin ring complex (gTuRC), regulating microtubule nucleation[3][10]
Cellular Localization:
β-actin is found:
Throughout the cytoplasm as part of the cytoskeleton[2][8][9][10][12][13]
In the nucleus, where it regulates gene transcription and DNA repair[3][7]

2. Protein Domains

Actin Domain:
β-actin contains a highly conserved actin domain responsible for ATP binding, polymerization, and interaction with actin-binding proteins[10].
3′-UTR “zipcode” sequence:
The ACTB transcript has a unique 3′-UTR “zipcode” that targets mRNA to subcellular regions, regulating translation and spatial protein synthesis[1][4].

3. Known Interactions

Protein-Protein Interactions:
β-actin interacts with:
Actin-binding proteins (e.g., profilin, cofilin, tropomyosin)
Chaperonin complexes (e.g., CCT for folding)
Transcription complexes (RNA polymerases, chromatin remodelers)[7]
Gamma-tubulin ring complex (gTuRC) for microtubule nucleation[3][10]
Other partners: protein disulfide isomerase, MARCKS, chorein, AIM1, and viral proteins (e.g., measles virus matrix protein)[7]
Post-translational Modifications:
Methylation (SETD3-mediated)
S-nitrosylation (nitric oxide–dependent)[7]

4. Disease Associations

Cancer:
Upregulation of ACTB is observed in many cancers (liver, melanoma, renal, colorectal, gastric, pancreatic, esophageal, lung, breast, prostate, ovarian, leukemia, lymphoma)[2].
Abnormal expression and polymerization contribute to cytoskeletal changes linked to cancer cell invasiveness and metastasis[2].
Genetic Disorders:
Mutations in ACTB cause severe developmental disorders, including Baraitser-Winter syndrome, characterized by intellectual disability, facial dysmorphism, and brain malformations[6].
Other associations: cardiovascular diseases, neurodegenerative disorders[2][6].

5. Recent Developments and Expert Analysis

2023–2024 Research:
Studies confirm that β-actin protein is dispensable for most cellular functions, but the ACTB transcript’s nucleotide sequence and regulated translation (via the zipcode) are essential for proper cellular localization and function[1][4].
Compensatory mechanisms exist: when β-actin is absent, γ-actin can substitute functionally, but transcript targeting remains critical[1][4].
ACTB is a reference gene in gene expression studies due to its consistent expression[2].

6. Relevant Statistics and Data

Expression:
ACTB is highly expressed in most tissues, especially nonmuscle cells[2][8].
Total actin protein levels remain constant across genotypes due to protein-based feedback mechanisms[1].

URLs and Publication Dates

Summary:
ACTB/β-actin is a fundamental cytoskeletal protein with diverse roles in cell structure, motility, gene regulation, and disease. Its function is tightly regulated at both the protein and transcript level, and its dysregulation is implicated in cancer and genetic disorders. Recent research highlights the importance of transcript localization and regulated translation for its cellular functions.

Citations

https://www.pnas.org/doi/10.1073/pnas.1807895115
https://www.rupahealth.com/biomarkers/actb
https://www.genecards.org/cgi-bin/carddisp.pl?gene=ACTB
https://pmc.ncbi.nlm.nih.gov/articles/PMC6077724/
https://medlineplus.gov/genetics/gene/actb/
https://febs.onlinelibrary.wiley.com/doi/10.1111/febs.13068
https://maayanlab.cloud/Harmonizome/gene/ACTB
https://www.proteinatlas.org/ENSG00000075624-ACTB
https://www.ncbi.nlm.nih.gov/gene/60
https://www.uniprot.org/uniprotkb/P60709/entry
https://en.wikipedia.org/wiki/Beta-actin
https://gene.sfari.org/database/human-gene/ACTB
https://geneglobe.qiagen.com/us/knowledge/gene/ENSG00000075624

📄 View Raw YAML

id: P60709
gene_symbol: ACTB
product_type: PROTEIN
taxon:
  id: NCBITaxon:9606
  label: Homo sapiens
description: Beta-actin is a highly conserved cytoplasmic actin isoform that polymerizes
  to form actin filaments (F-actin), a major component of the cytoskeleton. It functions
  in cell motility, cell division, cytokinesis, and maintenance of cell shape. ACTB
  also has nuclear functions, participating in chromatin remodeling as a component
  of BAF/SWI-SNF complexes, transcriptional regulation, and DNA repair. It associates
  with the gamma-tubulin ring complex (gTuRC) to regulate microtubule nucleation.
  The protein has intrinsic ATP hydrolysis activity essential for actin dynamics.
existing_annotations:
- term:
    id: GO:0015629
    label: actin cytoskeleton
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  review:
    summary: Core localization for beta-actin as a major structural component of the
      actin cytoskeleton. Well-supported by phylogenetic inference and extensive experimental
      evidence.
    action: ACCEPT
    supported_by:
    - reference_id: file:human/ACTB/ACTB-deep-research-perplexity-lite.md
      supporting_text: See deep research file for comprehensive analysis
    - reference_id: file:human/ACTB/ACTB-deep-research-cyberian.md
      supporting_text: Beta-actin is one of the most abundant and evolutionarily conserved
        proteins in eukaryotic cells, serving as a fundamental building block of the
        cytoskeleton and participating in an remarkably diverse array of cellular
        processes [PMID:26988969]
- term:
    id: GO:0045202
    label: synapse
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  review:
    summary: Beta-actin is present at synapses as part of the synaptic cytoskeleton,
      particularly in dendritic spines. Valid but represents a specialized localization
      rather than core function.
    action: KEEP_AS_NON_CORE
- term:
    id: GO:0005737
    label: cytoplasm
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  review:
    summary: Cytoplasm is the primary localization for beta-actin where it forms the
      cytoskeletal network.
    action: ACCEPT
- term:
    id: GO:0016020
    label: membrane
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  review:
    summary: Beta-actin associates with membranes, particularly the plasma membrane
      where it underlies the cortical cytoskeleton. Valid localization.
    action: ACCEPT
- term:
    id: GO:0030424
    label: axon
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  review:
    summary: Beta-actin is localized in axons where it participates in axon growth
      and guidance. Represents a specialized neuronal localization.
    action: KEEP_AS_NON_CORE
- term:
    id: GO:0098973
    label: structural constituent of postsynaptic actin cytoskeleton
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  review:
    summary: Overly specific term for neurons. The core MF is structural constituent
      of cytoskeleton (GO:0005200); the postsynaptic specificity is context-dependent
      rather than intrinsic to the protein.
    action: MODIFY
    proposed_replacement_terms:
    - id: GO:0005200
      label: structural constituent of cytoskeleton
- term:
    id: GO:0005884
    label: actin filament
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  review:
    summary: Core localization - beta-actin polymerizes to form actin filaments (F-actin).
      This is the fundamental structural unit produced by the protein.
    action: ACCEPT
- term:
    id: GO:0007409
    label: axonogenesis
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  review:
    summary: Actin dynamics are critical for axon growth, but this is a downstream
      neuronal developmental process rather than a core function. Actin provides the
      structural machinery used by many processes.
    action: KEEP_AS_NON_CORE
- term:
    id: GO:0019901
    label: protein kinase binding
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  review:
    summary: Actin interacts with various kinases (e.g., CaMKII, DYRK1A per UniProt).
      More informative than generic protein binding but represents interaction partners
      rather than core function.
    action: KEEP_AS_NON_CORE
- term:
    id: GO:0035267
    label: NuA4 histone acetyltransferase complex
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  review:
    summary: Beta-actin is a documented component of the NuA4/TIP60 complex [PMID:10966108,
      PMID:27153538]. This is a valid nuclear function representing chromatin remodeling
      activity. Core nuclear function.
    action: ACCEPT
- term:
    id: GO:0048870
    label: cell motility
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  review:
    summary: Cell motility is a core biological process for actin. Actin polymerization
      dynamics at the leading edge of cells directly drives cell migration [PMID:6202424].
    action: ACCEPT
    supported_by:
    - reference_id: file:human/ACTB/ACTB-deep-research-cyberian.md
      supporting_text: Beta-actin plays an essential role in cell motility, particularly
        at the leading edge of migrating cells where it concentrates in lamellipodia.
        Beta-actin knockout cells exhibit severely impaired migration velocity and
        reduced membrane protrusion dynamics
- term:
    id: GO:0000166
    label: nucleotide binding
  evidence_type: IEA
  original_reference_id: GO_REF:0000043
  review:
    summary: Actin binds ATP/ADP as part of its polymerization cycle. However, this
      is too general - ATP binding (GO:0005524) is more precise for actin.
    action: MODIFY
    proposed_replacement_terms:
    - id: GO:0005524
      label: ATP binding
- term:
    id: GO:0005524
    label: ATP binding
  evidence_type: IEA
  original_reference_id: GO_REF:0000043
  review:
    summary: Core molecular function - actin binds ATP which is hydrolyzed during
      polymerization. The ATP-bound form preferentially incorporates into filaments.
    action: ACCEPT
    supported_by:
    - reference_id: file:human/ACTB/ACTB-deep-research-cyberian.md
      supporting_text: The protein contains a nucleotide-binding cleft which accommodates
        ATP or ADP. ATP-bound G-actin preferentially assembles onto the barbed (plus)
        end of actin filaments [PMID:21314430]
- term:
    id: GO:0005634
    label: nucleus
  evidence_type: IEA
  original_reference_id: GO_REF:0000120
  review:
    summary: Nuclear actin is well-documented. Beta-actin localizes to the nucleus
      where it functions in chromatin remodeling complexes (BAF, NuA4), transcription
      regulation, and DNA repair [PMID:11687588, PMID:29925947].
    action: ACCEPT
- term:
    id: GO:0005856
    label: cytoskeleton
  evidence_type: IEA
  original_reference_id: GO_REF:0000120
  review:
    summary: Core localization - beta-actin is a fundamental component of the cytoskeleton.
      The actin cytoskeleton term (GO:0015629) is more specific and already accepted.
    action: ACCEPT
- term:
    id: GO:0016787
    label: hydrolase activity
  evidence_type: IEA
  original_reference_id: GO_REF:0000043
  review:
    summary: Actin has ATPase activity. However, this term is too general. ATP hydrolysis
      activity (GO:0016887) is more specific and appropriate for actin.
    action: MODIFY
    proposed_replacement_terms:
    - id: GO:0016887
      label: ATP hydrolysis activity
- term:
    id: GO:0098974
    label: postsynaptic actin cytoskeleton organization
  evidence_type: IEA
  original_reference_id: GO_REF:0000108
  review:
    summary: Overly specific - actin participates in cytoskeleton organization broadly,
      not specifically postsynaptic. The core process is actin cytoskeleton organization
      (GO:0030832).
    action: MODIFY
    proposed_replacement_terms:
    - id: GO:0030832
      label: regulation of actin filament length
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:11682052
  review:
    summary: Generic protein binding is uninformative per GO curation guidelines.
      Actin interacts with numerous proteins - specific binding terms are more appropriate.
    action: REMOVE
    supported_by:
    - reference_id: PMID:11682052
      supporting_text: Cingulin interacts with F-actin in vitro.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:15047060
  review:
    summary: Generic protein binding is uninformative per GO curation guidelines.
      Actin interacts with numerous proteins.
    action: REMOVE
    supported_by:
    - reference_id: PMID:15047060
      supporting_text: '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.'
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:15161933
  review:
    summary: Generic protein binding is uninformative per GO curation guidelines.
      Actin interacts with numerous proteins.
    action: REMOVE
    supported_by:
    - reference_id: PMID:15161933
      supporting_text: 2004 May 25. Comprehensive proteomic analysis of interphase
        and mitotic 14-3-3-binding proteins.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:15328537
  review:
    summary: Generic protein binding is uninformative per GO curation guidelines.
      Actin interacts with numerous proteins.
    action: REMOVE
    supported_by:
    - reference_id: PMID:15328537
      supporting_text: 'Aug 24. Emerin caps the pointed end of actin filaments: evidence
        for an actin cortical network at the nuclear inner membrane.'
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:15527767
  review:
    summary: Generic protein binding is uninformative per GO curation guidelines.
      Actin interacts with numerous proteins.
    action: REMOVE
    supported_by:
    - reference_id: PMID:15527767
      supporting_text: 'Proteomics-based identification of proteins interacting with
        Smad3: SREBP-2 forms a complex with Smad3 and inhibits its transcriptional
        activity.'
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:16049941
  review:
    summary: Generic protein binding is uninformative per GO curation guidelines.
      Actin interacts with numerous proteins.
    action: REMOVE
    supported_by:
    - reference_id: PMID:16049941
      supporting_text: A pilot proteomic study of amyloid precursor interactors in
        Alzheimer's disease.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:16189514
  review:
    summary: Generic protein binding is uninformative per GO curation guidelines.
      Actin interacts with numerous proteins.
    action: REMOVE
    supported_by:
    - reference_id: PMID:16189514
      supporting_text: Towards a proteome-scale map of the human protein-protein interaction
        network.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:16375898
  review:
    summary: Generic protein binding is uninformative per GO curation guidelines.
      Actin interacts with numerous proteins.
    action: REMOVE
    supported_by:
    - reference_id: PMID:16375898
      supporting_text: 2005 Dec 13. Identification of an actin-binding site in p47phox
        an organizer protein of NADPH oxidase.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:17404223
  review:
    summary: Generic protein binding is uninformative per GO curation guidelines.
      Actin interacts with numerous proteins.
    action: REMOVE
    supported_by:
    - reference_id: PMID:17404223
      supporting_text: The role of CaMKII as an F-actin-bundling protein crucial for
        maintenance of dendritic spine structure.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:17502619
  review:
    summary: Generic protein binding is uninformative per GO curation guidelines.
      Actin interacts with numerous proteins.
    action: REMOVE
    supported_by:
    - reference_id: PMID:17502619
      supporting_text: beta-Actin regulates platelet nitric oxide synthase 3 activity
        through interaction with heat shock protein 90.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:17599063
  review:
    summary: Generic protein binding is uninformative per GO curation guidelines.
      Actin interacts with numerous proteins.
    action: REMOVE
    supported_by:
    - reference_id: PMID:17599063
      supporting_text: Jun 28. PtdIns(4,5)P-restricted plasma membrane localization
        of FAN is involved in TNF-induced actin reorganization.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:19000816
  review:
    summary: Generic protein binding is uninformative per GO curation guidelines.
      Actin interacts with numerous proteins.
    action: REMOVE
    supported_by:
    - reference_id: PMID:19000816
      supporting_text: Structural basis for parasite-specific functions of the divergent
        profilin of Plasmodium falciparum.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:19008859
  review:
    summary: Generic protein binding is uninformative per GO curation guidelines.
      Actin interacts with numerous proteins.
    action: REMOVE
    supported_by:
    - reference_id: PMID:19008859
      supporting_text: Molecular basis for G-actin binding to RPEL motifs from the
        serum response factor coactivator MAL.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:19171758
  review:
    summary: Generic protein binding is uninformative per GO curation guidelines.
      Actin interacts with numerous proteins.
    action: REMOVE
    supported_by:
    - reference_id: PMID:19171758
      supporting_text: Kank attenuates actin remodeling by preventing interaction
        between IRSp53 and Rac1.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:19328794
  review:
    summary: Generic protein binding is uninformative per GO curation guidelines.
      Actin interacts with numerous proteins.
    action: REMOVE
    supported_by:
    - reference_id: PMID:19328794
      supporting_text: Nuclear myosin II regulates the assembly of preinitiation complex
        for ICAM-1 gene transcription.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:19338310
  review:
    summary: Generic protein binding is uninformative per GO curation guidelines.
      Actin interacts with numerous proteins.
    action: REMOVE
    supported_by:
    - reference_id: PMID:19338310
      supporting_text: Streamline proteomic approach for characterizing protein-protein
        interaction network in a RAD52 protein complex.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:20473970
  review:
    summary: Generic protein binding is uninformative per GO curation guidelines.
      Actin interacts with numerous proteins.
    action: REMOVE
    supported_by:
    - reference_id: PMID:20473970
      supporting_text: Identification of FBXO25-interacting proteins using an integrated
        proteomics approach.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:20618440
  review:
    summary: Generic protein binding is uninformative per GO curation guidelines.
      Actin interacts with numerous proteins.
    action: REMOVE
    supported_by:
    - reference_id: PMID:20618440
      supporting_text: 2010 Jul 8. Proteomic and biochemical analysis of 14-3-3-binding
        proteins during C2-ceramide-induced apoptosis.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:21044950
  review:
    summary: Generic protein binding is uninformative per GO curation guidelines.
      Actin interacts with numerous proteins.
    action: REMOVE
    supported_by:
    - reference_id: PMID:21044950
      supporting_text: Epub 2010 Nov 2. Genome-wide YFP fluorescence complementation
        screen identifies new regulators for telomere signaling in human cells.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:21516116
  review:
    summary: Generic protein binding is uninformative per GO curation guidelines.
      Actin interacts with numerous proteins.
    action: REMOVE
    supported_by:
    - reference_id: PMID:21516116
      supporting_text: Next-generation sequencing to generate interactome datasets.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:21555369
  review:
    summary: Generic protein binding is uninformative per GO curation guidelines.
      Actin interacts with numerous proteins.
    action: REMOVE
    supported_by:
    - reference_id: PMID:21555369
      supporting_text: Epub 2011 May 9. Nuclear ErbB2 enhances translation and cell
        growth by activating transcription of ribosomal RNA genes.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:21577206
  review:
    summary: Generic protein binding is uninformative per GO curation guidelines.
      Actin interacts with numerous proteins.
    action: REMOVE
    supported_by:
    - reference_id: PMID:21577206
      supporting_text: A novel interplay between oncogenic PFTK1 protein kinase and
        tumor suppressor TAGLN2 in the control of liver cancer cell motility.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:22038833
  review:
    summary: Generic protein binding is uninformative per GO curation guidelines.
      Actin interacts with numerous proteins.
    action: REMOVE
    supported_by:
    - reference_id: PMID:22038833
      supporting_text: Disruption of cytokeratin-8 interaction with F508del-CFTR corrects
        its functional defect.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:25416956
  review:
    summary: Generic protein binding is uninformative per GO curation guidelines.
      Actin interacts with numerous proteins.
    action: REMOVE
    supported_by:
    - reference_id: PMID:25416956
      supporting_text: A proteome-scale map of the human interactome network.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:25712891
  review:
    summary: Generic protein binding is uninformative per GO curation guidelines.
      Actin interacts with numerous proteins.
    action: REMOVE
    supported_by:
    - reference_id: PMID:25712891
      supporting_text: G551D-CFTR needs more bound actin than wild-type CFTR to maintain
        its presence in plasma membranes.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:25910212
  review:
    summary: Generic protein binding is uninformative per GO curation guidelines.
      Actin interacts with numerous proteins.
    action: REMOVE
    supported_by:
    - reference_id: PMID:25910212
      supporting_text: Widespread macromolecular interaction perturbations in human
        genetic disorders.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:27107014
  review:
    summary: Generic protein binding is uninformative per GO curation guidelines.
      Actin interacts with numerous proteins.
    action: REMOVE
    supported_by:
    - reference_id: PMID:27107014
      supporting_text: An inter-species protein-protein interaction network across
        vast evolutionary distance.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:27607350
  review:
    summary: Generic protein binding is uninformative per GO curation guidelines.
      Actin interacts with numerous proteins.
    action: REMOVE
    supported_by:
    - reference_id: PMID:27607350
      supporting_text: Characterization of the Translationally Controlled Tumor Protein
        (TCTP) Interactome Reveals Novel Binding Partners in Human Cancer Cells.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:28514442
  review:
    summary: Generic protein binding is uninformative per GO curation guidelines.
      Actin interacts with numerous proteins.
    action: REMOVE
    supported_by:
    - reference_id: PMID:28514442
      supporting_text: Architecture of the human interactome defines protein communities
        and disease networks.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:29477555
  review:
    summary: Generic protein binding is uninformative per GO curation guidelines.
      Actin interacts with numerous proteins.
    action: REMOVE
    supported_by:
    - reference_id: PMID:29477555
      supporting_text: 2018 Mar 2. HtrA3 is a cellular partner of cytoskeleton proteins
        and TCP1α chaperonin.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:29892012
  review:
    summary: Generic protein binding is uninformative per GO curation guidelines.
      Actin interacts with numerous proteins.
    action: REMOVE
    supported_by:
    - reference_id: PMID:29892012
      supporting_text: Jun 11. An interactome perturbation framework prioritizes damaging
        missense mutations for developmental disorders.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:29924966
  review:
    summary: Generic protein binding is uninformative per GO curation guidelines.
      Actin interacts with numerous proteins.
    action: REMOVE
    supported_by:
    - reference_id: PMID:29924966
      supporting_text: A Proteomic Variant Approach (ProVarA) for Personalized Medicine
        of Inherited and Somatic Disease.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:30021884
  review:
    summary: Generic protein binding is uninformative per GO curation guidelines.
      Actin interacts with numerous proteins.
    action: REMOVE
    supported_by:
    - reference_id: PMID:30021884
      supporting_text: Epub 2018 Jul 18. Histone Interaction Landscapes Visualized
        by Crosslinking Mass Spectrometry in Intact Cell Nuclei.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:30886144
  review:
    summary: Generic protein binding is uninformative per GO curation guidelines.
      Actin interacts with numerous proteins.
    action: REMOVE
    supported_by:
    - reference_id: PMID:30886144
      supporting_text: Network-based prediction of protein interactions.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:31515488
  review:
    summary: Generic protein binding is uninformative per GO curation guidelines.
      Actin interacts with numerous proteins.
    action: REMOVE
    supported_by:
    - reference_id: PMID:31515488
      supporting_text: Extensive disruption of protein interactions by genetic variants
        across the allele frequency spectrum in human populations.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:32296183
  review:
    summary: Generic protein binding is uninformative per GO curation guidelines.
      Actin interacts with numerous proteins.
    action: REMOVE
    supported_by:
    - reference_id: PMID:32296183
      supporting_text: Apr 8. A reference map of the human binary protein interactome.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:32814053
  review:
    summary: Generic protein binding is uninformative per GO curation guidelines.
      Actin interacts with numerous proteins.
    action: REMOVE
    supported_by:
    - reference_id: PMID:32814053
      supporting_text: Interactome Mapping Provides a Network of Neurodegenerative
        Disease Proteins and Uncovers Widespread Protein Aggregation in Affected Brains.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:33961781
  review:
    summary: Generic protein binding is uninformative per GO curation guidelines.
      Actin interacts with numerous proteins.
    action: REMOVE
    supported_by:
    - reference_id: PMID:33961781
      supporting_text: 2021 May 6. Dual proteome-scale networks reveal cell-specific
        remodeling of the human interactome.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:35271311
  review:
    summary: Generic protein binding is uninformative per GO curation guidelines.
      Actin interacts with numerous proteins.
    action: REMOVE
    supported_by:
    - reference_id: PMID:35271311
      supporting_text: '2022 Mar 11. OpenCell: Endogenous tagging for the cartography
        of human cellular organization.'
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:36012204
  review:
    summary: Generic protein binding is uninformative per GO curation guidelines.
      Actin interacts with numerous proteins.
    action: REMOVE
    supported_by:
    - reference_id: PMID:36012204
      supporting_text: Differential CFTR-Interactome Proximity Labeling Procedures
        Identify Enrichment in Multiple SLC Transporters.
- term:
    id: GO:0042802
    label: identical protein binding
  evidence_type: IPI
  original_reference_id: PMID:16189514
  review:
    summary: Actin polymerizes by self-association into filaments. This is a core
      molecular function for actin.
    action: ACCEPT
    supported_by:
    - reference_id: PMID:16189514
      supporting_text: Towards a proteome-scale map of the human protein-protein interaction
        network.
- term:
    id: GO:0042802
    label: identical protein binding
  evidence_type: IPI
  original_reference_id: PMID:17404223
  review:
    summary: Actin polymerizes by self-association into filaments. This is a core
      molecular function for actin.
    action: ACCEPT
    supported_by:
    - reference_id: PMID:17404223
      supporting_text: The role of CaMKII as an F-actin-bundling protein crucial for
        maintenance of dendritic spine structure.
- term:
    id: GO:0042802
    label: identical protein binding
  evidence_type: IPI
  original_reference_id: PMID:18234857
  review:
    summary: Actin polymerizes by self-association into filaments. This is a core
      molecular function for actin.
    action: ACCEPT
    supported_by:
    - reference_id: PMID:18234857
      supporting_text: High-resolution cryo-EM structure of the F-actin-fimbrin/plastin
        ABD2 complex.
- term:
    id: GO:0042802
    label: identical protein binding
  evidence_type: IPI
  original_reference_id: PMID:19000816
  review:
    summary: Actin polymerizes by self-association into filaments. This is a core
      molecular function for actin.
    action: ACCEPT
    supported_by:
    - reference_id: PMID:19000816
      supporting_text: Structural basis for parasite-specific functions of the divergent
        profilin of Plasmodium falciparum.
- term:
    id: GO:0042802
    label: identical protein binding
  evidence_type: IPI
  original_reference_id: PMID:20383143
  review:
    summary: Actin polymerizes by self-association into filaments. This is a core
      molecular function for actin.
    action: ACCEPT
    supported_by:
    - reference_id: PMID:20383143
      supporting_text: Apr 11. Opening of tandem calponin homology domains regulates
        their affinity for F-actin.
- term:
    id: GO:0042802
    label: identical protein binding
  evidence_type: IPI
  original_reference_id: PMID:21516116
  review:
    summary: Actin polymerizes by self-association into filaments. This is a core
      molecular function for actin.
    action: ACCEPT
    supported_by:
    - reference_id: PMID:21516116
      supporting_text: Next-generation sequencing to generate interactome datasets.
- term:
    id: GO:0042802
    label: identical protein binding
  evidence_type: IPI
  original_reference_id: PMID:25416956
  review:
    summary: Actin polymerizes by self-association into filaments. This is a core
      molecular function for actin.
    action: ACCEPT
    supported_by:
    - reference_id: PMID:25416956
      supporting_text: A proteome-scale map of the human interactome network.
- term:
    id: GO:0042802
    label: identical protein binding
  evidence_type: IPI
  original_reference_id: PMID:25502805
  review:
    summary: Actin polymerizes by self-association into filaments. This is a core
      molecular function for actin.
    action: ACCEPT
    supported_by:
    - reference_id: PMID:25502805
      supporting_text: eCollection 2014 Dec.
- term:
    id: GO:0042802
    label: identical protein binding
  evidence_type: IPI
  original_reference_id: PMID:25910212
  review:
    summary: Actin polymerizes by self-association into filaments. This is a core
      molecular function for actin.
    action: ACCEPT
    supported_by:
    - reference_id: PMID:25910212
      supporting_text: Widespread macromolecular interaction perturbations in human
        genetic disorders.
- term:
    id: GO:0042802
    label: identical protein binding
  evidence_type: IPI
  original_reference_id: PMID:29892012
  review:
    summary: Actin polymerizes by self-association into filaments. This is a core
      molecular function for actin.
    action: ACCEPT
    supported_by:
    - reference_id: PMID:29892012
      supporting_text: Jun 11. An interactome perturbation framework prioritizes damaging
        missense mutations for developmental disorders.
- term:
    id: GO:0042802
    label: identical protein binding
  evidence_type: IPI
  original_reference_id: PMID:31515488
  review:
    summary: Actin polymerizes by self-association into filaments. This is a core
      molecular function for actin.
    action: ACCEPT
    supported_by:
    - reference_id: PMID:31515488
      supporting_text: Extensive disruption of protein interactions by genetic variants
        across the allele frequency spectrum in human populations.
- term:
    id: GO:0042802
    label: identical protein binding
  evidence_type: IPI
  original_reference_id: PMID:32296183
  review:
    summary: Actin polymerizes by self-association into filaments. This is a core
      molecular function for actin.
    action: ACCEPT
    supported_by:
    - reference_id: PMID:32296183
      supporting_text: Apr 8. A reference map of the human binary protein interactome.
- term:
    id: GO:0005737
    label: cytoplasm
  evidence_type: IEA
  original_reference_id: GO_REF:0000107
  review:
    summary: Cytoplasm is a primary localization for cytoplasmic beta-actin.
    action: ACCEPT
- term:
    id: GO:0005829
    label: cytosol
  evidence_type: IEA
  original_reference_id: GO_REF:0000107
  review:
    summary: Cytosol localization is valid for beta-actin where it exists in monomeric
      form.
    action: ACCEPT
- term:
    id: GO:0005903
    label: brush border
  evidence_type: IEA
  original_reference_id: GO_REF:0000107
  review:
    summary: Brush border localization valid - actin is enriched in intestinal microvilli.
    action: KEEP_AS_NON_CORE
- term:
    id: GO:0030863
    label: cortical cytoskeleton
  evidence_type: IEA
  original_reference_id: GO_REF:0000107
  review:
    summary: Cortical cytoskeleton is a core actin localization underlying the plasma
      membrane.
    action: ACCEPT
- term:
    id: GO:0044305
    label: calyx of Held
  evidence_type: IEA
  original_reference_id: GO_REF:0000107
  review:
    summary: Calyx of Held is an overly specific neuronal synapse term - non-core
      localization.
    action: KEEP_AS_NON_CORE
- term:
    id: GO:0098685
    label: Schaffer collateral - CA1 synapse
  evidence_type: IEA
  original_reference_id: GO_REF:0000107
  review:
    summary: Schaffer collateral synapse is overly specific neuronal localization.
    action: KEEP_AS_NON_CORE
- term:
    id: GO:1900242
    label: regulation of synaptic vesicle endocytosis
  evidence_type: IEA
  original_reference_id: GO_REF:0000107
  review:
    summary: Regulation of synaptic vesicle endocytosis - actin participates but this
      is over-annotation.
    action: MARK_AS_OVER_ANNOTATED
- term:
    id: GO:0000776
    label: kinetochore
  evidence_type: NAS
  original_reference_id: PMID:11078522
  review:
    summary: Kinetochore localization - actin has been reported at kinetochores through
      BAF complex function.
    action: KEEP_AS_NON_CORE
    supported_by:
    - reference_id: PMID:11078522
      supporting_text: The human SWI/SNF-B chromatin-remodeling complex is related
        to yeast rsc and localizes at kinetochores of mitotic chromosomes.
- term:
    id: GO:0000785
    label: chromatin
  evidence_type: NAS
  original_reference_id: PMID:12192000
  review:
    summary: Chromatin localization is valid for nuclear actin in chromatin remodeling
      complexes.
    action: ACCEPT
    supported_by:
    - reference_id: PMID:12192000
      supporting_text: 2002 Aug 20. REST repression of neuronal genes requires components
        of the hSWI.SNF complex.
- term:
    id: GO:0000785
    label: chromatin
  evidence_type: NAS
  original_reference_id: PMID:29374058
  review:
    summary: Chromatin localization is valid for nuclear actin in chromatin remodeling
      complexes.
    action: ACCEPT
    supported_by:
    - reference_id: PMID:29374058
      supporting_text: Epub 2018 Jan 26. Glioma tumor suppressor candidate region
        gene 1 (GLTSCR1) and its paralog GLTSCR1-like form SWI/SNF chromatin remodeling
        subcomplexes.
- term:
    id: GO:0000786
    label: nucleosome
  evidence_type: IDA
  original_reference_id: PMID:27153538
  review:
    summary: Nucleosome - actin is part of chromatin remodeling complexes that act
      on nucleosomes.
    action: KEEP_AS_NON_CORE
    supported_by:
    - reference_id: PMID:27153538
      supporting_text: The TIP60 Complex Regulates Bivalent Chromatin Recognition
        by 53BP1 through Direct H4K20me Binding and H2AK15 Acetylation.
- term:
    id: GO:0000930
    label: gamma-tubulin complex
  evidence_type: NAS
  original_reference_id: PMID:39321809
  review:
    summary: Gamma-tubulin complex - actin is a component of gTuRC per recent structural
      studies [PMID:39321809].
    action: ACCEPT
    supported_by:
    - reference_id: PMID:39321809
      supporting_text: Epub 2024 Sep 24. CDK5RAP2 activates microtubule nucleator
        γTuRC by facilitating template formation and actin release.
- term:
    id: GO:0005869
    label: dynactin complex
  evidence_type: ISO
  original_reference_id: GO_REF:0000114
  review:
    summary: Dynactin complex - actin (specifically one copy) is part of dynactin
      filament per UniProt.
    action: ACCEPT
- term:
    id: GO:0006338
    label: chromatin remodeling
  evidence_type: NAS
  original_reference_id: PMID:10078207
  review:
    summary: Chromatin remodeling is a core nuclear function of actin via BAF/SWI-SNF
      complexes.
    action: ACCEPT
    supported_by:
    - reference_id: file:human/ACTB/ACTB-deep-research-cyberian.md
      supporting_text: Beta-actin is an integral component of mammalian SWI/SNF-like
        BAF chromatin remodeling complexes. BRG1, the catalytic ATPase subunit of
        BAF, requires beta-actin for maximal ATPase activity [PMID:12045110]
    - reference_id: PMID:10078207
      supporting_text: Reconstitution of a core chromatin remodeling complex from
        SWI/SNF subunits.
- term:
    id: GO:0006338
    label: chromatin remodeling
  evidence_type: NAS
  original_reference_id: PMID:29374058
  review:
    summary: Chromatin remodeling is a core nuclear function of actin via BAF/SWI-SNF
      complexes.
    action: ACCEPT
    supported_by:
    - reference_id: PMID:29374058
      supporting_text: Epub 2018 Jan 26. Glioma tumor suppressor candidate region
        gene 1 (GLTSCR1) and its paralog GLTSCR1-like form SWI/SNF chromatin remodeling
        subcomplexes.
- term:
    id: GO:0006357
    label: regulation of transcription by RNA polymerase II
  evidence_type: NAS
  original_reference_id: PMID:11263494
  review:
    summary: Regulation of transcription by RNA pol II - actin participates via chromatin
      remodeling.
    action: KEEP_AS_NON_CORE
    supported_by:
    - reference_id: PMID:11263494
      supporting_text: The murine SNF5/INI1 chromatin remodeling factor is essential
        for embryonic development and tumor suppression.
- term:
    id: GO:0006357
    label: regulation of transcription by RNA polymerase II
  evidence_type: NAS
  original_reference_id: PMID:17340523
  review:
    summary: Regulation of transcription by RNA pol II - actin participates via chromatin
      remodeling.
    action: KEEP_AS_NON_CORE
    supported_by:
    - reference_id: PMID:17340523
      supporting_text: Separation and Quantification of Some Alkaloids from Fumaria
        parviflora by Capillary Isotachophoresis1.
- term:
    id: GO:0006357
    label: regulation of transcription by RNA polymerase II
  evidence_type: NAS
  original_reference_id: PMID:17920018
  review:
    summary: Regulation of transcription by RNA pol II - actin participates via chromatin
      remodeling.
    action: KEEP_AS_NON_CORE
    supported_by:
    - reference_id: PMID:17920018
      supporting_text: Regulation of dendritic development by neuron-specific chromatin
        remodeling complexes.
- term:
    id: GO:0006357
    label: regulation of transcription by RNA polymerase II
  evidence_type: NAS
  original_reference_id: PMID:18809673
  review:
    summary: Regulation of transcription by RNA pol II - actin participates via chromatin
      remodeling.
    action: KEEP_AS_NON_CORE
    supported_by:
    - reference_id: PMID:18809673
      supporting_text: 2008 Sep 22. BRD7, a novel PBAF-specific SWI/SNF subunit, is
        required for target gene activation and repression in embryonic stem cells.
- term:
    id: GO:0006357
    label: regulation of transcription by RNA polymerase II
  evidence_type: NAS
  original_reference_id: PMID:29374058
  review:
    summary: Regulation of transcription by RNA pol II - actin participates via chromatin
      remodeling.
    action: KEEP_AS_NON_CORE
    supported_by:
    - reference_id: PMID:29374058
      supporting_text: Epub 2018 Jan 26. Glioma tumor suppressor candidate region
        gene 1 (GLTSCR1) and its paralog GLTSCR1-like form SWI/SNF chromatin remodeling
        subcomplexes.
- term:
    id: GO:0007017
    label: microtubule-based process
  evidence_type: ISO
  original_reference_id: GO_REF:0000114
  review:
    summary: Microtubule-based process - actin participates through gTuRC but this
      is overly general.
    action: MODIFY
    proposed_replacement_terms:
    - id: GO:0007020
      label: microtubule nucleation
- term:
    id: GO:0007020
    label: microtubule nucleation
  evidence_type: NAS
  original_reference_id: PMID:39321809
  review:
    summary: Microtubule nucleation - actin is part of gTuRC [PMID:39321809]. Valid
      function.
    action: ACCEPT
    supported_by:
    - reference_id: PMID:39321809
      supporting_text: Epub 2024 Sep 24. CDK5RAP2 activates microtubule nucleator
        γTuRC by facilitating template formation and actin release.
- term:
    id: GO:0008284
    label: positive regulation of cell population proliferation
  evidence_type: NAS
  original_reference_id: PMID:29374058
  review:
    summary: Positive regulation of cell proliferation - over-annotation, downstream
      effect.
    action: MARK_AS_OVER_ANNOTATED
    supported_by:
    - reference_id: PMID:29374058
      supporting_text: Epub 2018 Jan 26. Glioma tumor suppressor candidate region
        gene 1 (GLTSCR1) and its paralog GLTSCR1-like form SWI/SNF chromatin remodeling
        subcomplexes.
- term:
    id: GO:0016363
    label: nuclear matrix
  evidence_type: NAS
  original_reference_id: PMID:9128241
  review:
    summary: Nuclear matrix - actin is found in nuclear matrix per SWI/SNF studies.
    action: KEEP_AS_NON_CORE
    supported_by:
    - reference_id: PMID:9128241
      supporting_text: Components of the human SWI/SNF complex are enriched in active
        chromatin and are associated with the nuclear matrix.
- term:
    id: GO:0016514
    label: SWI/SNF complex
  evidence_type: NAS
  original_reference_id: PMID:8804307
  review:
    summary: SWI/SNF complex - actin is a component of mammalian BAF/SWI-SNF complexes.
    action: ACCEPT
    supported_by:
    - reference_id: PMID:8804307
      supporting_text: Diversity and specialization of mammalian SWI/SNF complexes.
- term:
    id: GO:0016586
    label: RSC-type complex
  evidence_type: NAS
  original_reference_id: PMID:8804307
  review:
    summary: RSC-type complex - related to yeast RSC, in humans this is the BAF complex.
    action: KEEP_AS_NON_CORE
    supported_by:
    - reference_id: PMID:8804307
      supporting_text: Diversity and specialization of mammalian SWI/SNF complexes.
- term:
    id: GO:0030071
    label: regulation of mitotic metaphase/anaphase transition
  evidence_type: NAS
  original_reference_id: PMID:23698369
  review:
    summary: Regulation of mitotic metaphase/anaphase transition - over-annotation
      via BAF involvement.
    action: MARK_AS_OVER_ANNOTATED
    supported_by:
    - reference_id: PMID:23698369
      supporting_text: BAF complexes facilitate decatenation of DNA by topoisomerase
        IIα.
- term:
    id: GO:0030071
    label: regulation of mitotic metaphase/anaphase transition
  evidence_type: NAS
  original_reference_id: PMID:25066234
  review:
    summary: Regulation of mitotic metaphase/anaphase transition - over-annotation
      via BAF involvement.
    action: MARK_AS_OVER_ANNOTATED
    supported_by:
    - reference_id: PMID:25066234
      supporting_text: 2014 Jul 24. Requirement for PBAF in transcriptional repression
        and repair at DNA breaks in actively transcribed regions of chromatin.
- term:
    id: GO:0035060
    label: brahma complex
  evidence_type: NAS
  original_reference_id: PMID:8804307
  review:
    summary: Brahma complex - another name for BAF complex containing actin.
    action: ACCEPT
    supported_by:
    - reference_id: PMID:8804307
      supporting_text: Diversity and specialization of mammalian SWI/SNF complexes.
- term:
    id: GO:0035267
    label: NuA4 histone acetyltransferase complex
  evidence_type: IDA
  original_reference_id: PMID:27153538
  review:
    summary: Actin is a documented component of NuA4/TIP60 complex with direct experimental
      evidence.
    action: ACCEPT
    supported_by:
    - reference_id: PMID:27153538
      supporting_text: The TIP60 Complex Regulates Bivalent Chromatin Recognition
        by 53BP1 through Direct H4K20me Binding and H2AK15 Acetylation.
- term:
    id: GO:0042981
    label: regulation of apoptotic process
  evidence_type: NAS
  original_reference_id: PMID:14966270
  review:
    summary: Regulation of apoptotic process - over-annotation, actin is not directly
      regulating apoptosis.
    action: MARK_AS_OVER_ANNOTATED
    supported_by:
    - reference_id: PMID:14966270
      supporting_text: Structural and functional conservation of the NuA4 histone
        acetyltransferase complex from yeast to humans.
- term:
    id: GO:0045582
    label: positive regulation of T cell differentiation
  evidence_type: NAS
  original_reference_id: PMID:12110891
  review:
    summary: Positive regulation of T cell differentiation - over-annotation via BAF
      involvement.
    action: MARK_AS_OVER_ANNOTATED
    supported_by:
    - reference_id: PMID:12110891
      supporting_text: Reciprocal regulation of CD4/CD8 expression by SWI/SNF-like
        BAF complexes.
- term:
    id: GO:0045596
    label: negative regulation of cell differentiation
  evidence_type: NAS
  original_reference_id: PMID:30510198
  review:
    summary: Negative regulation of cell differentiation - over-annotation via BAF.
    action: MARK_AS_OVER_ANNOTATED
    supported_by:
    - reference_id: PMID:30510198
      supporting_text: A non-canonical BRD9-containing BAF chromatin remodeling complex
        regulates naive pluripotency in mouse embryonic stem cells.
- term:
    id: GO:0045597
    label: positive regulation of cell differentiation
  evidence_type: NAS
  original_reference_id: PMID:11790558
  review:
    summary: Positive regulation of cell differentiation - over-annotation via BAF.
    action: MARK_AS_OVER_ANNOTATED
    supported_by:
    - reference_id: PMID:11790558
      supporting_text: SWI/SNF chromatin remodeling and cancer.
- term:
    id: GO:0045597
    label: positive regulation of cell differentiation
  evidence_type: NAS
  original_reference_id: PMID:12368262
  review:
    summary: Positive regulation of cell differentiation - over-annotation via BAF.
    action: MARK_AS_OVER_ANNOTATED
    supported_by:
    - reference_id: PMID:12368262
      supporting_text: Identification of a polymorphic, neuron-specific chromatin
        remodeling complex.
- term:
    id: GO:0045663
    label: positive regulation of myoblast differentiation
  evidence_type: NAS
  original_reference_id: PMID:11175787
  review:
    summary: Positive regulation of myoblast differentiation - over-annotation via
      BAF.
    action: MARK_AS_OVER_ANNOTATED
    supported_by:
    - reference_id: PMID:11175787
      supporting_text: Mammalian SWI/SNF complexes promote MyoD-mediated muscle differentiation.
- term:
    id: GO:0045663
    label: positive regulation of myoblast differentiation
  evidence_type: NAS
  original_reference_id: PMID:15985610
  review:
    summary: Positive regulation of myoblast differentiation - over-annotation via
      BAF.
    action: MARK_AS_OVER_ANNOTATED
    supported_by:
    - reference_id: PMID:15985610
      supporting_text: PBAF chromatin-remodeling complex requires a novel specificity
        subunit, BAF200, to regulate expression of selective interferon-responsive
        genes.
- term:
    id: GO:0045893
    label: positive regulation of DNA-templated transcription
  evidence_type: NAS
  original_reference_id: PMID:27153538
  review:
    summary: Positive regulation of DNA-templated transcription - over-annotation.
    action: MARK_AS_OVER_ANNOTATED
    supported_by:
    - reference_id: PMID:27153538
      supporting_text: The TIP60 Complex Regulates Bivalent Chromatin Recognition
        by 53BP1 through Direct H4K20me Binding and H2AK15 Acetylation.
- term:
    id: GO:0051726
    label: regulation of cell cycle
  evidence_type: IMP
  original_reference_id: PMID:27153538
  review:
    summary: Regulation of cell cycle - over-annotation.
    action: MARK_AS_OVER_ANNOTATED
    supported_by:
    - reference_id: PMID:27153538
      supporting_text: The TIP60 Complex Regulates Bivalent Chromatin Recognition
        by 53BP1 through Direct H4K20me Binding and H2AK15 Acetylation.
- term:
    id: GO:0070316
    label: regulation of G0 to G1 transition
  evidence_type: NAS
  original_reference_id: PMID:11790558
  review:
    summary: Regulation of G0 to G1 transition - over-annotation via BAF.
    action: MARK_AS_OVER_ANNOTATED
    supported_by:
    - reference_id: PMID:11790558
      supporting_text: SWI/SNF chromatin remodeling and cancer.
- term:
    id: GO:0071564
    label: npBAF complex
  evidence_type: NAS
  original_reference_id: PMID:8804307
  review:
    summary: npBAF complex - neural progenitor BAF complex containing actin.
    action: ACCEPT
    supported_by:
    - reference_id: PMID:8804307
      supporting_text: Diversity and specialization of mammalian SWI/SNF complexes.
- term:
    id: GO:0071565
    label: nBAF complex
  evidence_type: NAS
  original_reference_id: PMID:17920018
  review:
    summary: nBAF complex - neuronal BAF complex containing actin.
    action: ACCEPT
    supported_by:
    - reference_id: PMID:17920018
      supporting_text: Regulation of dendritic development by neuron-specific chromatin
        remodeling complexes.
- term:
    id: GO:0140092
    label: bBAF complex
  evidence_type: NAS
  original_reference_id: PMID:12368262
  review:
    summary: bBAF complex - brain BAF complex containing actin.
    action: ACCEPT
    supported_by:
    - reference_id: PMID:12368262
      supporting_text: Identification of a polymorphic, neuron-specific chromatin
        remodeling complex.
- term:
    id: GO:0140288
    label: GBAF complex
  evidence_type: NAS
  original_reference_id: PMID:29374058
  review:
    summary: GBAF complex - GLTSCR1-containing BAF complex with actin.
    action: ACCEPT
    supported_by:
    - reference_id: PMID:29374058
      supporting_text: Epub 2018 Jan 26. Glioma tumor suppressor candidate region
        gene 1 (GLTSCR1) and its paralog GLTSCR1-like form SWI/SNF chromatin remodeling
        subcomplexes.
- term:
    id: GO:1902459
    label: positive regulation of stem cell population maintenance
  evidence_type: NAS
  original_reference_id: PMID:19279220
  review:
    summary: Positive regulation of stem cell population maintenance - over-annotation
      via BAF.
    action: MARK_AS_OVER_ANNOTATED
    supported_by:
    - reference_id: PMID:19279220
      supporting_text: An embryonic stem cell chromatin remodeling complex, esBAF,
        is essential for embryonic stem cell self-renewal and pluripotency.
- term:
    id: GO:1902459
    label: positive regulation of stem cell population maintenance
  evidence_type: NAS
  original_reference_id: PMID:30510198
  review:
    summary: Positive regulation of stem cell population maintenance - over-annotation
      via BAF.
    action: MARK_AS_OVER_ANNOTATED
    supported_by:
    - reference_id: PMID:30510198
      supporting_text: A non-canonical BRD9-containing BAF chromatin remodeling complex
        regulates naive pluripotency in mouse embryonic stem cells.
- term:
    id: GO:1905168
    label: positive regulation of double-strand break repair via homologous recombination
  evidence_type: IDA
  original_reference_id: PMID:27153538
  review:
    summary: Positive regulation of HR repair - over-annotation via NuA4.
    action: MARK_AS_OVER_ANNOTATED
    supported_by:
    - reference_id: PMID:27153538
      supporting_text: The TIP60 Complex Regulates Bivalent Chromatin Recognition
        by 53BP1 through Direct H4K20me Binding and H2AK15 Acetylation.
- term:
    id: GO:2000045
    label: regulation of G1/S transition of mitotic cell cycle
  evidence_type: NAS
  original_reference_id: PMID:10778858
  review:
    summary: Regulation of G1/S transition - over-annotation via BAF.
    action: MARK_AS_OVER_ANNOTATED
    supported_by:
    - reference_id: PMID:10778858
      supporting_text: Exit from G1 and S phase of the cell cycle is regulated by
        repressor complexes containing HDAC-Rb-hSWI/SNF and Rb-hSWI/SNF.
- term:
    id: GO:2000779
    label: regulation of double-strand break repair
  evidence_type: NAS
  original_reference_id: PMID:14966270
  review:
    summary: Regulation of DSB repair - over-annotation.
    action: MARK_AS_OVER_ANNOTATED
    supported_by:
    - reference_id: PMID:14966270
      supporting_text: Structural and functional conservation of the NuA4 histone
        acetyltransferase complex from yeast to humans.
- term:
    id: GO:2000781
    label: positive regulation of double-strand break repair
  evidence_type: NAS
  original_reference_id: PMID:16932743
  review:
    summary: Positive regulation of DSB repair - over-annotation via BAF.
    action: MARK_AS_OVER_ANNOTATED
    supported_by:
    - reference_id: PMID:16932743
      supporting_text: Aug 24. Mammalian SWI/SNF complexes facilitate DNA double-strand
        break repair by promoting gamma-H2AX induction.
- term:
    id: GO:2000781
    label: positive regulation of double-strand break repair
  evidence_type: NAS
  original_reference_id: PMID:25066234
  review:
    summary: Positive regulation of DSB repair - over-annotation via BAF.
    action: MARK_AS_OVER_ANNOTATED
    supported_by:
    - reference_id: PMID:25066234
      supporting_text: 2014 Jul 24. Requirement for PBAF in transcriptional repression
        and repair at DNA breaks in actively transcribed regions of chromatin.
- term:
    id: GO:2000819
    label: regulation of nucleotide-excision repair
  evidence_type: NAS
  original_reference_id: PMID:12215535
  review:
    summary: Regulation of NER - over-annotation via chromatin remodeling.
    action: MARK_AS_OVER_ANNOTATED
    supported_by:
    - reference_id: PMID:12215535
      supporting_text: The SWI/SNF chromatin-remodeling factor stimulates repair by
        human excision nuclease in the mononucleosome core particle.
- term:
    id: GO:0030235
    label: nitric-oxide synthase regulator activity
  evidence_type: IDA
  original_reference_id: PMID:17502619
  review:
    summary: Nitric-oxide synthase regulator activity - valid per PMID:17502619, actin
      regulates NOS3.
    action: KEEP_AS_NON_CORE
    supported_by:
    - reference_id: PMID:17502619
      supporting_text: beta-Actin regulates platelet nitric oxide synthase 3 activity
        through interaction with heat shock protein 90.
- term:
    id: GO:0007010
    label: cytoskeleton organization
  evidence_type: ISS
  original_reference_id: GO_REF:0000024
  review:
    summary: Cytoskeleton organization - core process for actin.
    action: ACCEPT
- term:
    id: GO:0141108
    label: transporter regulator activity
  evidence_type: IGI
  original_reference_id: PMID:18331289
  review:
    summary: Transporter regulator activity - actin regulates transporters like NET.
    action: KEEP_AS_NON_CORE
    supported_by:
    - reference_id: PMID:18331289
      supporting_text: Epub 2008 Mar 3. Regulated interactions of the norepineprhine
        transporter by the actin and microtubule cytoskeletons.
- term:
    id: GO:0005654
    label: nucleoplasm
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-5250947
  review:
    summary: Nucleoplasm - valid for nuclear actin.
    action: ACCEPT
- term:
    id: GO:0005654
    label: nucleoplasm
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-5689544
  review:
    summary: Nucleoplasm - valid for nuclear actin.
    action: ACCEPT
- term:
    id: GO:0005654
    label: nucleoplasm
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-9825847
  review:
    summary: Nucleoplasm - valid for nuclear actin.
    action: ACCEPT
- term:
    id: GO:0005654
    label: nucleoplasm
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-9933236
  review:
    summary: Nucleoplasm - valid for nuclear actin.
    action: ACCEPT
- term:
    id: GO:0005654
    label: nucleoplasm
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-9933237
  review:
    summary: Nucleoplasm - valid for nuclear actin.
    action: ACCEPT
- term:
    id: GO:0005654
    label: nucleoplasm
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-9933238
  review:
    summary: Nucleoplasm - valid for nuclear actin.
    action: ACCEPT
- term:
    id: GO:0005654
    label: nucleoplasm
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-9934021
  review:
    summary: Nucleoplasm - valid for nuclear actin.
    action: ACCEPT
- term:
    id: GO:0005654
    label: nucleoplasm
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-9934024
  review:
    summary: Nucleoplasm - valid for nuclear actin.
    action: ACCEPT
- term:
    id: GO:0005654
    label: nucleoplasm
  evidence_type: TAS
  original_reference_id: Reactome:R-NUL-4551334
  review:
    summary: Nucleoplasm - valid for nuclear actin.
    action: ACCEPT
- term:
    id: GO:0005829
    label: cytosol
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-1861595
  review:
    summary: Cytosol localization is valid for beta-actin where it exists in monomeric
      form.
    action: ACCEPT
- term:
    id: GO:0005829
    label: cytosol
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-2029466
  review:
    summary: Cytosol localization is valid for beta-actin where it exists in monomeric
      form.
    action: ACCEPT
- term:
    id: GO:0005829
    label: cytosol
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-2029473
  review:
    summary: Cytosol localization is valid for beta-actin where it exists in monomeric
      form.
    action: ACCEPT
- term:
    id: GO:0005829
    label: cytosol
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-2029476
  review:
    summary: Cytosol localization is valid for beta-actin where it exists in monomeric
      form.
    action: ACCEPT
- term:
    id: GO:0005829
    label: cytosol
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-203070
  review:
    summary: Cytosol localization is valid for beta-actin where it exists in monomeric
      form.
    action: ACCEPT
- term:
    id: GO:0005829
    label: cytosol
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-2197690
  review:
    summary: Cytosol localization is valid for beta-actin where it exists in monomeric
      form.
    action: ACCEPT
- term:
    id: GO:0005829
    label: cytosol
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-392751
  review:
    summary: Cytosol localization is valid for beta-actin where it exists in monomeric
      form.
    action: ACCEPT
- term:
    id: GO:0005829
    label: cytosol
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-3928595
  review:
    summary: Cytosol localization is valid for beta-actin where it exists in monomeric
      form.
    action: ACCEPT
- term:
    id: GO:0005829
    label: cytosol
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-430347
  review:
    summary: Cytosol localization is valid for beta-actin where it exists in monomeric
      form.
    action: ACCEPT
- term:
    id: GO:0005829
    label: cytosol
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-443779
  review:
    summary: Cytosol localization is valid for beta-actin where it exists in monomeric
      form.
    action: ACCEPT
- term:
    id: GO:0005829
    label: cytosol
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-445089
  review:
    summary: Cytosol localization is valid for beta-actin where it exists in monomeric
      form.
    action: ACCEPT
- term:
    id: GO:0005829
    label: cytosol
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-5218916
  review:
    summary: Cytosol localization is valid for beta-actin where it exists in monomeric
      form.
    action: ACCEPT
- term:
    id: GO:0005829
    label: cytosol
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-5626507
  review:
    summary: Cytosol localization is valid for beta-actin where it exists in monomeric
      form.
    action: ACCEPT
- term:
    id: GO:0005829
    label: cytosol
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-5665751
  review:
    summary: Cytosol localization is valid for beta-actin where it exists in monomeric
      form.
    action: ACCEPT
- term:
    id: GO:0005829
    label: cytosol
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-5665767
  review:
    summary: Cytosol localization is valid for beta-actin where it exists in monomeric
      form.
    action: ACCEPT
- term:
    id: GO:0005829
    label: cytosol
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-5665802
  review:
    summary: Cytosol localization is valid for beta-actin where it exists in monomeric
      form.
    action: ACCEPT
- term:
    id: GO:0005829
    label: cytosol
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-5665809
  review:
    summary: Cytosol localization is valid for beta-actin where it exists in monomeric
      form.
    action: ACCEPT
- term:
    id: GO:0005829
    label: cytosol
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-5665982
  review:
    summary: Cytosol localization is valid for beta-actin where it exists in monomeric
      form.
    action: ACCEPT
- term:
    id: GO:0005829
    label: cytosol
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-5666001
  review:
    summary: Cytosol localization is valid for beta-actin where it exists in monomeric
      form.
    action: ACCEPT
- term:
    id: GO:0005829
    label: cytosol
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-9666458
  review:
    summary: Cytosol localization is valid for beta-actin where it exists in monomeric
      form.
    action: ACCEPT
- term:
    id: GO:0005829
    label: cytosol
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-9914537
  review:
    summary: Cytosol localization is valid for beta-actin where it exists in monomeric
      form.
    action: ACCEPT
- term:
    id: GO:0005829
    label: cytosol
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-9934294
  review:
    summary: Cytosol localization is valid for beta-actin where it exists in monomeric
      form.
    action: ACCEPT
- term:
    id: GO:0005829
    label: cytosol
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-9934410
  review:
    summary: Cytosol localization is valid for beta-actin where it exists in monomeric
      form.
    action: ACCEPT
- term:
    id: GO:0005829
    label: cytosol
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-9934486
  review:
    summary: Cytosol localization is valid for beta-actin where it exists in monomeric
      form.
    action: ACCEPT
- term:
    id: GO:0005886
    label: plasma membrane
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-3928654
  review:
    summary: Plasma membrane - actin underlies the cortical membrane.
    action: ACCEPT
- term:
    id: GO:0005886
    label: plasma membrane
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-8868230
  review:
    summary: Plasma membrane - actin underlies the cortical membrane.
    action: ACCEPT
- term:
    id: GO:0005886
    label: plasma membrane
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-8868236
  review:
    summary: Plasma membrane - actin underlies the cortical membrane.
    action: ACCEPT
- term:
    id: GO:0005886
    label: plasma membrane
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-8868648
  review:
    summary: Plasma membrane - actin underlies the cortical membrane.
    action: ACCEPT
- term:
    id: GO:0005886
    label: plasma membrane
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-8868651
  review:
    summary: Plasma membrane - actin underlies the cortical membrane.
    action: ACCEPT
- term:
    id: GO:0005886
    label: plasma membrane
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-8868658
  review:
    summary: Plasma membrane - actin underlies the cortical membrane.
    action: ACCEPT
- term:
    id: GO:0005886
    label: plasma membrane
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-8868659
  review:
    summary: Plasma membrane - actin underlies the cortical membrane.
    action: ACCEPT
- term:
    id: GO:0005886
    label: plasma membrane
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-8868660
  review:
    summary: Plasma membrane - actin underlies the cortical membrane.
    action: ACCEPT
- term:
    id: GO:0005886
    label: plasma membrane
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-8868661
  review:
    summary: Plasma membrane - actin underlies the cortical membrane.
    action: ACCEPT
- term:
    id: GO:0005886
    label: plasma membrane
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-8869438
  review:
    summary: Plasma membrane - actin underlies the cortical membrane.
    action: ACCEPT
- term:
    id: GO:0005886
    label: plasma membrane
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-8871193
  review:
    summary: Plasma membrane - actin underlies the cortical membrane.
    action: ACCEPT
- term:
    id: GO:0005886
    label: plasma membrane
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-8871194
  review:
    summary: Plasma membrane - actin underlies the cortical membrane.
    action: ACCEPT
- term:
    id: GO:0098871
    label: postsynaptic actin cytoskeleton
  evidence_type: IDA
  original_reference_id: PMID:18341992
  review:
    summary: Postsynaptic actin cytoskeleton - specialized neuronal localization.
    action: KEEP_AS_NON_CORE
    supported_by:
    - reference_id: PMID:18341992
      supporting_text: The subspine organization of actin fibers regulates the structure
        and plasticity of dendritic spines.
- term:
    id: GO:0098871
    label: postsynaptic actin cytoskeleton
  evidence_type: IMP
  original_reference_id: PMID:18341992
  review:
    summary: Postsynaptic actin cytoskeleton - specialized neuronal localization.
    action: KEEP_AS_NON_CORE
    supported_by:
    - reference_id: PMID:18341992
      supporting_text: The subspine organization of actin fibers regulates the structure
        and plasticity of dendritic spines.
- term:
    id: GO:0098973
    label: structural constituent of postsynaptic actin cytoskeleton
  evidence_type: IDA
  original_reference_id: PMID:18341992
  review:
    summary: Overly specific for neurons. Core MF is structural constituent of cytoskeleton.
    action: MODIFY
    proposed_replacement_terms:
    - id: GO:0005200
      label: structural constituent of cytoskeleton
    supported_by:
    - reference_id: PMID:18341992
      supporting_text: The subspine organization of actin fibers regulates the structure
        and plasticity of dendritic spines.
- term:
    id: GO:0098973
    label: structural constituent of postsynaptic actin cytoskeleton
  evidence_type: EXP
  original_reference_id: PMID:18341992
  review:
    summary: Overly specific for neurons. Core MF is structural constituent of cytoskeleton.
    action: MODIFY
    proposed_replacement_terms:
    - id: GO:0005200
      label: structural constituent of cytoskeleton
    supported_by:
    - reference_id: PMID:18341992
      supporting_text: The subspine organization of actin fibers regulates the structure
        and plasticity of dendritic spines.
- term:
    id: GO:0098973
    label: structural constituent of postsynaptic actin cytoskeleton
  evidence_type: IMP
  original_reference_id: PMID:18341992
  review:
    summary: Overly specific for neurons. Core MF is structural constituent of cytoskeleton.
    action: MODIFY
    proposed_replacement_terms:
    - id: GO:0005200
      label: structural constituent of cytoskeleton
    supported_by:
    - reference_id: PMID:18341992
      supporting_text: The subspine organization of actin fibers regulates the structure
        and plasticity of dendritic spines.
- term:
    id: GO:0098978
    label: glutamatergic synapse
  evidence_type: IDA
  original_reference_id: PMID:18341992
  review:
    summary: Glutamatergic synapse - specialized neuronal localization.
    action: KEEP_AS_NON_CORE
    supported_by:
    - reference_id: PMID:18341992
      supporting_text: The subspine organization of actin fibers regulates the structure
        and plasticity of dendritic spines.
- term:
    id: GO:0098978
    label: glutamatergic synapse
  evidence_type: EXP
  original_reference_id: PMID:18341992
  review:
    summary: Glutamatergic synapse - specialized neuronal localization.
    action: KEEP_AS_NON_CORE
    supported_by:
    - reference_id: PMID:18341992
      supporting_text: The subspine organization of actin fibers regulates the structure
        and plasticity of dendritic spines.
- term:
    id: GO:0098978
    label: glutamatergic synapse
  evidence_type: IMP
  original_reference_id: PMID:18341992
  review:
    summary: Glutamatergic synapse - specialized neuronal localization.
    action: KEEP_AS_NON_CORE
    supported_by:
    - reference_id: PMID:18341992
      supporting_text: The subspine organization of actin fibers regulates the structure
        and plasticity of dendritic spines.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:25255767
  review:
    summary: Generic protein binding is uninformative per GO curation guidelines.
      Actin interacts with numerous proteins.
    action: REMOVE
    supported_by:
    - reference_id: PMID:25255767
      supporting_text: Molecular mechanisms of disease-related human β-actin mutations
        p.R183W and p.E364K.
- term:
    id: GO:0016887
    label: ATP hydrolysis activity
  evidence_type: IDA
  original_reference_id: PMID:25255767
  review:
    summary: ATP hydrolysis activity - core molecular function of actin [PMID:25255767].
    action: ACCEPT
    supported_by:
    - reference_id: file:human/ACTB/ACTB-deep-research-cyberian.md
      supporting_text: Polymerization dramatically accelerates the rate of ATP hydrolysis
        by approximately 40,000-fold compared to monomeric actin. This rate enhancement
        occurs because filament incorporation repositions the side chains of Gln137
        and His161 within the active site [PMID:3672117]
    - reference_id: PMID:25255767
      supporting_text: Molecular mechanisms of disease-related human β-actin mutations
        p.R183W and p.E364K.
- term:
    id: GO:0006338
    label: chromatin remodeling
  evidence_type: HDA
  original_reference_id: PMID:16217013
  review:
    summary: Chromatin remodeling is a core nuclear function of actin via BAF/SWI-SNF
      complexes.
    action: ACCEPT
    supported_by:
    - reference_id: PMID:16217013
      supporting_text: Heterogeneous nuclear ribonucleoprotein C1/C2, MeCP1, and SWI/SNF
        form a chromatin remodeling complex at the beta-globin locus control region.
- term:
    id: GO:0035633
    label: maintenance of blood-brain barrier
  evidence_type: NAS
  original_reference_id: PMID:30280653
  review:
    summary: Maintenance of blood-brain barrier - over-annotation.
    action: MARK_AS_OVER_ANNOTATED
    supported_by:
    - reference_id: PMID:30280653
      supporting_text: 'Blood-Brain Barrier: From Physiology to Disease and Back.'
- term:
    id: GO:0001738
    label: morphogenesis of a polarized epithelium
  evidence_type: IMP
  original_reference_id: PMID:22855531
  review:
    summary: Morphogenesis of polarized epithelium - cell biology process using actin.
    action: KEEP_AS_NON_CORE
    supported_by:
    - reference_id: PMID:22855531
      supporting_text: 2012 Aug 1. Nonredundant roles of cytoplasmic β- and γ-actin
        isoforms in regulation of epithelial apical junctions.
- term:
    id: GO:0007163
    label: establishment or maintenance of cell polarity
  evidence_type: IMP
  original_reference_id: PMID:22855531
  review:
    summary: Establishment or maintenance of cell polarity - valid process for actin.
    action: KEEP_AS_NON_CORE
    supported_by:
    - reference_id: PMID:22855531
      supporting_text: 2012 Aug 1. Nonredundant roles of cytoplasmic β- and γ-actin
        isoforms in regulation of epithelial apical junctions.
- term:
    id: GO:0034333
    label: adherens junction assembly
  evidence_type: IMP
  original_reference_id: PMID:22855531
  review:
    summary: Adherens junction assembly - valid, actin is core to AJ.
    action: ACCEPT
    supported_by:
    - reference_id: PMID:22855531
      supporting_text: 2012 Aug 1. Nonredundant roles of cytoplasmic β- and γ-actin
        isoforms in regulation of epithelial apical junctions.
- term:
    id: GO:0043296
    label: apical junction complex
  evidence_type: IDA
  original_reference_id: PMID:22855531
  review:
    summary: Apical junction complex - valid localization.
    action: ACCEPT
    supported_by:
    - reference_id: PMID:22855531
      supporting_text: 2012 Aug 1. Nonredundant roles of cytoplasmic β- and γ-actin
        isoforms in regulation of epithelial apical junctions.
- term:
    id: GO:0045176
    label: apical protein localization
  evidence_type: IMP
  original_reference_id: PMID:22855531
  review:
    summary: Apical protein localization - downstream process.
    action: KEEP_AS_NON_CORE
    supported_by:
    - reference_id: PMID:22855531
      supporting_text: 2012 Aug 1. Nonredundant roles of cytoplasmic β- and γ-actin
        isoforms in regulation of epithelial apical junctions.
- term:
    id: GO:0071896
    label: protein localization to adherens junction
  evidence_type: IMP
  original_reference_id: PMID:22855531
  review:
    summary: Protein localization to adherens junction - downstream process.
    action: KEEP_AS_NON_CORE
    supported_by:
    - reference_id: PMID:22855531
      supporting_text: 2012 Aug 1. Nonredundant roles of cytoplasmic β- and γ-actin
        isoforms in regulation of epithelial apical junctions.
- term:
    id: GO:0150111
    label: regulation of transepithelial transport
  evidence_type: IMP
  original_reference_id: PMID:22855531
  review:
    summary: Regulation of transepithelial transport - over-annotation.
    action: MARK_AS_OVER_ANNOTATED
    supported_by:
    - reference_id: PMID:22855531
      supporting_text: 2012 Aug 1. Nonredundant roles of cytoplasmic β- and γ-actin
        isoforms in regulation of epithelial apical junctions.
- term:
    id: GO:0005912
    label: adherens junction
  evidence_type: IDA
  original_reference_id: PMID:22855531
  review:
    summary: Adherens junction - core localization for actin.
    action: ACCEPT
    supported_by:
    - reference_id: PMID:22855531
      supporting_text: 2012 Aug 1. Nonredundant roles of cytoplasmic β- and γ-actin
        isoforms in regulation of epithelial apical junctions.
- term:
    id: GO:0070160
    label: tight junction
  evidence_type: IDA
  original_reference_id: PMID:22855531
  review:
    summary: Tight junction - actin is present at tight junctions.
    action: ACCEPT
    supported_by:
    - reference_id: PMID:22855531
      supporting_text: 2012 Aug 1. Nonredundant roles of cytoplasmic β- and γ-actin
        isoforms in regulation of epithelial apical junctions.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:24415753
  review:
    summary: Generic protein binding is uninformative per GO curation guidelines.
      Actin interacts with numerous proteins.
    action: REMOVE
    supported_by:
    - reference_id: PMID:24415753
      supporting_text: 2014 Jan 10. Protein disulfide isomerase directly interacts
        with β-actin Cys374 and regulates cytoskeleton reorganization.
- term:
    id: GO:0030027
    label: lamellipodium
  evidence_type: IDA
  original_reference_id: PMID:24415753
  review:
    summary: Lamellipodium - core actin structure at leading edge.
    action: ACCEPT
    supported_by:
    - reference_id: file:human/ACTB/ACTB-deep-research-cyberian.md
      supporting_text: Beta-actin concentrates in lamellipodia - thin, sheet-like
        protrusions driven by actin polymerization. The lamellipodium represents both
        the motor for cell advancement and the primary site of actin cytoskeleton
        construction
    - reference_id: PMID:24415753
      supporting_text: 2014 Jan 10. Protein disulfide isomerase directly interacts
        with β-actin Cys374 and regulates cytoskeleton reorganization.
- term:
    id: GO:0032991
    label: protein-containing complex
  evidence_type: IDA
  original_reference_id: PMID:24415753
  review:
    summary: Protein-containing complex - too generic.
    action: REMOVE
    supported_by:
    - reference_id: PMID:24415753
      supporting_text: 2014 Jan 10. Protein disulfide isomerase directly interacts
        with β-actin Cys374 and regulates cytoskeleton reorganization.
- term:
    id: GO:0005911
    label: cell-cell junction
  evidence_type: IMP
  original_reference_id: PMID:25753039
  review:
    summary: Cell-cell junction - valid actin localization.
    action: ACCEPT
    supported_by:
    - reference_id: PMID:25753039
      supporting_text: Mar 9. ZO-1 controls endothelial adherens junctions, cell-cell
        tension, angiogenesis, and barrier formation.
- term:
    id: GO:0048156
    label: tau protein binding
  evidence_type: NAS
  original_reference_id: PMID:28386764
  review:
    summary: Tau protein binding - specific interaction.
    action: KEEP_AS_NON_CORE
    supported_by:
    - reference_id: PMID:28386764
      supporting_text: Epub 2017 Apr 6. Roles of tau protein in health and disease.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:28604741
  review:
    summary: Generic protein binding is uninformative per GO curation guidelines.
      Actin interacts with numerous proteins.
    action: REMOVE
    supported_by:
    - reference_id: PMID:28604741
      supporting_text: Jun 12. A novel nuclear complex of DRR1, F-actin and COMMD1
        involved in NF-κB degradation and cell growth suppression in neuroblastoma.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:21969592
  review:
    summary: Generic protein binding is uninformative per GO curation guidelines.
      Actin interacts with numerous proteins.
    action: REMOVE
    supported_by:
    - reference_id: PMID:21969592
      supporting_text: Tumor suppressor down-regulated in renal cell carcinoma 1 (DRR1)
        is a stress-induced actin bundling factor that modulates synaptic efficacy
        and cognition.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:18331289
  review:
    summary: Generic protein binding is uninformative per GO curation guidelines.
      Actin interacts with numerous proteins.
    action: REMOVE
    supported_by:
    - reference_id: PMID:18331289
      supporting_text: Epub 2008 Mar 3. Regulated interactions of the norepineprhine
        transporter by the actin and microtubule cytoskeletons.
- term:
    id: GO:0051621
    label: regulation of norepinephrine uptake
  evidence_type: ISS
  original_reference_id: PMID:18331289
  review:
    summary: Regulation of norepinephrine uptake - specialized function.
    action: KEEP_AS_NON_CORE
    supported_by:
    - reference_id: PMID:18331289
      supporting_text: Epub 2008 Mar 3. Regulated interactions of the norepineprhine
        transporter by the actin and microtubule cytoskeletons.
- term:
    id: GO:0051621
    label: regulation of norepinephrine uptake
  evidence_type: IGI
  original_reference_id: PMID:18331289
  review:
    summary: Regulation of norepinephrine uptake - specialized function.
    action: KEEP_AS_NON_CORE
    supported_by:
    - reference_id: PMID:18331289
      supporting_text: Epub 2008 Mar 3. Regulated interactions of the norepineprhine
        transporter by the actin and microtubule cytoskeletons.
- term:
    id: GO:1903076
    label: regulation of protein localization to plasma membrane
  evidence_type: IMP
  original_reference_id: PMID:18331289
  review:
    summary: Regulation of protein localization to PM - downstream effect.
    action: KEEP_AS_NON_CORE
    supported_by:
    - reference_id: PMID:18331289
      supporting_text: Epub 2008 Mar 3. Regulated interactions of the norepineprhine
        transporter by the actin and microtubule cytoskeletons.
- term:
    id: GO:0005737
    label: cytoplasm
  evidence_type: IDA
  original_reference_id: PMID:24327345
  review:
    summary: Cytoplasm is a primary localization for cytoplasmic beta-actin.
    action: ACCEPT
    supported_by:
    - reference_id: PMID:24327345
      supporting_text: Intracellular distribution of differentially phosphorylated
        dual-specificity tyrosine phosphorylation-regulated kinase 1A (DYRK1A).
- term:
    id: GO:0005856
    label: cytoskeleton
  evidence_type: ISS
  original_reference_id: GO_REF:0000024
  review:
    summary: Core localization for beta-actin as a fundamental cytoskeletal protein.
    action: ACCEPT
- term:
    id: GO:0051623
    label: positive regulation of norepinephrine uptake
  evidence_type: TAS
  original_reference_id: PMID:18331289
  review:
    summary: Positive regulation of norepinephrine uptake - specialized function.
    action: KEEP_AS_NON_CORE
    supported_by:
    - reference_id: PMID:18331289
      supporting_text: Epub 2008 Mar 3. Regulated interactions of the norepineprhine
        transporter by the actin and microtubule cytoskeletons.
- term:
    id: GO:0098793
    label: presynapse
  evidence_type: TAS
  original_reference_id: PMID:18331289
  review:
    summary: Presynapse - neuronal localization.
    action: KEEP_AS_NON_CORE
    supported_by:
    - reference_id: PMID:18331289
      supporting_text: Epub 2008 Mar 3. Regulated interactions of the norepineprhine
        transporter by the actin and microtubule cytoskeletons.
- term:
    id: GO:0048870
    label: cell motility
  evidence_type: IMP
  original_reference_id: PMID:6202424
  review:
    summary: Cell motility - core biological process.
    action: ACCEPT
    supported_by:
    - reference_id: PMID:6202424
      supporting_text: A variant form of beta-actin in a mutant of KB cells resistant
        to cytochalasin B.
- term:
    id: GO:0072749
    label: cellular response to cytochalasin B
  evidence_type: IMP
  original_reference_id: PMID:6202424
  review:
    summary: Cellular response to cytochalasin B - response to actin-targeting drug.
    action: KEEP_AS_NON_CORE
    supported_by:
    - reference_id: PMID:6202424
      supporting_text: A variant form of beta-actin in a mutant of KB cells resistant
        to cytochalasin B.
- term:
    id: GO:0019901
    label: protein kinase binding
  evidence_type: IPI
  original_reference_id: PMID:24327345
  review:
    summary: Protein kinase binding - more informative than generic binding.
    action: KEEP_AS_NON_CORE
    supported_by:
    - reference_id: PMID:24327345
      supporting_text: Intracellular distribution of differentially phosphorylated
        dual-specificity tyrosine phosphorylation-regulated kinase 1A (DYRK1A).
- term:
    id: GO:0005856
    label: cytoskeleton
  evidence_type: IDA
  original_reference_id: PMID:24327345
  review:
    summary: Core localization for beta-actin with direct experimental evidence.
    action: ACCEPT
    supported_by:
    - reference_id: PMID:24327345
      supporting_text: Intracellular distribution of differentially phosphorylated
        dual-specificity tyrosine phosphorylation-regulated kinase 1A (DYRK1A).
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:17192268
  review:
    summary: Generic protein binding is uninformative per GO curation guidelines.
      Actin interacts with numerous proteins.
    action: REMOVE
    supported_by:
    - reference_id: PMID:17192268
      supporting_text: 2006 Dec 27. Mutation analysis of the short cytoplasmic domain
        of the cell-cell adhesion molecule CEACAM1 identifies residues that orchestrate
        actin binding and lumen formation.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:11687588
  review:
    summary: Generic protein binding is uninformative per GO curation guidelines.
      Actin interacts with numerous proteins.
    action: REMOVE
    supported_by:
    - reference_id: PMID:11687588
      supporting_text: Oct 30. Nuclear DNA helicase II/RNA helicase A binds to filamentous
        actin.
- term:
    id: GO:0005634
    label: nucleus
  evidence_type: IDA
  original_reference_id: PMID:11687588
  review:
    summary: Nuclear localization of actin is well-documented with direct evidence.
    action: ACCEPT
    supported_by:
    - reference_id: PMID:11687588
      supporting_text: Oct 30. Nuclear DNA helicase II/RNA helicase A binds to filamentous
        actin.
- term:
    id: GO:0015629
    label: actin cytoskeleton
  evidence_type: IDA
  original_reference_id: PMID:11687588
  review:
    summary: Core localization with direct experimental evidence.
    action: ACCEPT
    supported_by:
    - reference_id: PMID:11687588
      supporting_text: Oct 30. Nuclear DNA helicase II/RNA helicase A binds to filamentous
        actin.
- term:
    id: GO:0032991
    label: protein-containing complex
  evidence_type: IDA
  original_reference_id: PMID:11687588
  review:
    summary: Protein-containing complex - too generic.
    action: REMOVE
    supported_by:
    - reference_id: PMID:11687588
      supporting_text: Oct 30. Nuclear DNA helicase II/RNA helicase A binds to filamentous
        actin.
- term:
    id: GO:0031982
    label: vesicle
  evidence_type: HDA
  original_reference_id: PMID:19190083
  review:
    summary: Vesicle - generic localization.
    action: KEEP_AS_NON_CORE
    supported_by:
    - reference_id: PMID:19190083
      supporting_text: 'Characterization of exosome-like vesicles released from human
        tracheobronchial ciliated epithelium: a possible role in innate defense.'
- term:
    id: GO:0070062
    label: extracellular exosome
  evidence_type: HDA
  original_reference_id: PMID:11487543
  review:
    summary: Extracellular exosome - actin found in exosomes.
    action: KEEP_AS_NON_CORE
    supported_by:
    - reference_id: PMID:11487543
      supporting_text: Intestinal epithelial cells secrete exosome-like vesicles.
- term:
    id: GO:0005886
    label: plasma membrane
  evidence_type: ISS
  original_reference_id: GO_REF:0000024
  review:
    summary: Plasma membrane - actin underlies the cortical membrane.
    action: ACCEPT
- term:
    id: GO:0097433
    label: dense body
  evidence_type: ISS
  original_reference_id: GO_REF:0000024
  review:
    summary: Dense body - muscle structure.
    action: KEEP_AS_NON_CORE
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:23100250
  review:
    summary: Generic protein binding is uninformative per GO curation guidelines.
      Actin interacts with numerous proteins.
    action: REMOVE
    supported_by:
    - reference_id: PMID:23100250
      supporting_text: 2012 Oct 24. Constitutive turnover of phosphorylation at Thr-412
        of human p57/coronin-1 regulates the interaction with actin.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:18562541
  review:
    summary: Generic protein binding is uninformative per GO curation guidelines.
      Actin interacts with numerous proteins.
    action: REMOVE
    supported_by:
    - reference_id: PMID:18562541
      supporting_text: Association of hepatitis C virus replication complexes with
        microtubules and actin filaments is dependent on the interaction of NS3 and
        NS5A.
- term:
    id: GO:0070527
    label: platelet aggregation
  evidence_type: HMP
  original_reference_id: PMID:23382103
  review:
    summary: Platelet aggregation - downstream process.
    action: MARK_AS_OVER_ANNOTATED
    supported_by:
    - reference_id: PMID:23382103
      supporting_text: Epub 2013 Feb 4. Platelet proteome analysis reveals integrin-dependent
        aggregation defects in patients with myelodysplastic syndromes.
- term:
    id: GO:0005925
    label: focal adhesion
  evidence_type: HDA
  original_reference_id: PMID:21423176
  review:
    summary: Focal adhesion - core localization for actin.
    action: ACCEPT
    supported_by:
    - reference_id: PMID:21423176
      supporting_text: Analysis of the myosin-II-responsive focal adhesion proteome
        reveals a role for β-Pix in negative regulation of focal adhesion maturation.
- term:
    id: GO:0070062
    label: extracellular exosome
  evidence_type: HDA
  original_reference_id: PMID:23533145
  review:
    summary: Extracellular exosome - actin found in exosomes.
    action: KEEP_AS_NON_CORE
    supported_by:
    - reference_id: PMID:23533145
      supporting_text: 2013 Apr 23. In-depth proteomic analyses of exosomes isolated
        from expressed prostatic secretions in urine.
- term:
    id: GO:0016020
    label: membrane
  evidence_type: HDA
  original_reference_id: PMID:19946888
  review:
    summary: Membrane - valid general localization.
    action: ACCEPT
    supported_by:
    - reference_id: PMID:19946888
      supporting_text: Defining the membrane proteome of NK cells.
- term:
    id: GO:0036464
    label: cytoplasmic ribonucleoprotein granule
  evidence_type: IDA
  original_reference_id: PMID:15121898
  review:
    summary: Cytoplasmic RNP granule - actin is found in mRNP granules.
    action: KEEP_AS_NON_CORE
    supported_by:
    - reference_id: PMID:15121898
      supporting_text: The composition of Staufen-containing RNA granules from human
        cells indicates their role in the regulated transport and translation of messenger
        RNAs.
- term:
    id: GO:0005615
    label: extracellular space
  evidence_type: HDA
  original_reference_id: PMID:16502470
  review:
    summary: Extracellular space - actin detected extracellularly.
    action: KEEP_AS_NON_CORE
    supported_by:
    - reference_id: PMID:16502470
      supporting_text: 'Human colostrum: identification of minor proteins in the aqueous
        phase by proteomics.'
- term:
    id: GO:0000785
    label: chromatin
  evidence_type: HDA
  original_reference_id: PMID:16217013
  review:
    summary: Chromatin localization is valid for nuclear actin in chromatin remodeling
      complexes.
    action: ACCEPT
    supported_by:
    - reference_id: PMID:16217013
      supporting_text: Heterogeneous nuclear ribonucleoprotein C1/C2, MeCP1, and SWI/SNF
        form a chromatin remodeling complex at the beta-globin locus control region.
- term:
    id: GO:0031492
    label: nucleosomal DNA binding
  evidence_type: HDA
  original_reference_id: PMID:16217013
  review:
    summary: Nucleosomal DNA binding - via chromatin remodeling complexes.
    action: KEEP_AS_NON_CORE
    supported_by:
    - reference_id: PMID:16217013
      supporting_text: Heterogeneous nuclear ribonucleoprotein C1/C2, MeCP1, and SWI/SNF
        form a chromatin remodeling complex at the beta-globin locus control region.
- term:
    id: GO:0032991
    label: protein-containing complex
  evidence_type: HDA
  original_reference_id: PMID:16217013
  review:
    summary: Protein-containing complex - too generic.
    action: REMOVE
    supported_by:
    - reference_id: PMID:16217013
      supporting_text: Heterogeneous nuclear ribonucleoprotein C1/C2, MeCP1, and SWI/SNF
        form a chromatin remodeling complex at the beta-globin locus control region.
- term:
    id: GO:0021762
    label: substantia nigra development
  evidence_type: HEP
  original_reference_id: PMID:22926577
  review:
    summary: Substantia nigra development - over-annotation.
    action: MARK_AS_OVER_ANNOTATED
    supported_by:
    - reference_id: PMID:22926577
      supporting_text: 2012 Aug 28. Quantitative proteomic analysis of human substantia
        nigra in Alzheimer's disease, Huntington's disease and Multiple sclerosis.
- term:
    id: GO:0072562
    label: blood microparticle
  evidence_type: HDA
  original_reference_id: PMID:22516433
  review:
    summary: Blood microparticle - actin detected in microparticles.
    action: KEEP_AS_NON_CORE
    supported_by:
    - reference_id: PMID:22516433
      supporting_text: Epub 2012 Apr 10. Proteomic analysis of microvesicles from
        plasma of healthy donors reveals high individual variability.
- term:
    id: GO:0005615
    label: extracellular space
  evidence_type: HDA
  original_reference_id: PMID:22664934
  review:
    summary: Extracellular space - actin detected extracellularly.
    action: KEEP_AS_NON_CORE
    supported_by:
    - reference_id: PMID:22664934
      supporting_text: Comparison of tear protein levels in breast cancer patients
        and healthy controls using a de novo proteomic approach.
- term:
    id: GO:0005615
    label: extracellular space
  evidence_type: HDA
  original_reference_id: PMID:23580065
  review:
    summary: Extracellular space - actin detected extracellularly.
    action: KEEP_AS_NON_CORE
    supported_by:
    - reference_id: PMID:23580065
      supporting_text: Shotgun proteomics reveals specific modulated protein patterns
        in tears of patients with primary open angle glaucoma naïve to therapy.
- term:
    id: GO:0070062
    label: extracellular exosome
  evidence_type: HDA
  original_reference_id: PMID:19199708
  review:
    summary: Extracellular exosome - actin found in exosomes.
    action: KEEP_AS_NON_CORE
    supported_by:
    - reference_id: PMID:19199708
      supporting_text: Proteomic analysis of human parotid gland exosomes by multidimensional
        protein identification technology (MudPIT).
- term:
    id: GO:0070062
    label: extracellular exosome
  evidence_type: HDA
  original_reference_id: PMID:20458337
  review:
    summary: Extracellular exosome - actin found in exosomes.
    action: KEEP_AS_NON_CORE
    supported_by:
    - reference_id: PMID:20458337
      supporting_text: 2010 May 11. MHC class II-associated proteins in B-cell exosomes
        and potential functional implications for exosome biogenesis.
- term:
    id: GO:0070062
    label: extracellular exosome
  evidence_type: HDA
  original_reference_id: PMID:21362503
  review:
    summary: Extracellular exosome - actin found in exosomes.
    action: KEEP_AS_NON_CORE
    supported_by:
    - reference_id: PMID:21362503
      supporting_text: Epub 2011 Mar 8. Protein profile of exosomes from trabecular
        meshwork cells.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:14592989
  review:
    summary: Generic protein binding is uninformative per GO curation guidelines.
      Actin interacts with numerous proteins.
    action: REMOVE
    supported_by:
    - reference_id: PMID:14592989
      supporting_text: 'Exportin 6: a novel nuclear export receptor that is specific
        for profilin.actin complexes.'
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:17823310
  review:
    summary: Generic protein binding is uninformative per GO curation guidelines.
      Actin interacts with numerous proteins.
    action: REMOVE
    supported_by:
    - reference_id: PMID:17823310
      supporting_text: 2007 Sep 6. HGAL, a lymphoma prognostic biomarker, interacts
        with the cytoskeleton and mediates the effects of IL-6 on cell migration.
- term:
    id: GO:0030957
    label: Tat protein binding
  evidence_type: IPI
  original_reference_id: PMID:16687403
  review:
    summary: Tat protein binding - HIV Tat interacts with actin.
    action: KEEP_AS_NON_CORE
    supported_by:
    - reference_id: PMID:16687403
      supporting_text: 2006 May 10. The SWI/SNF chromatin-remodeling complex is a
        cofactor for Tat transactivation of the HIV promoter.
- term:
    id: GO:0019894
    label: kinesin binding
  evidence_type: IPI
  original_reference_id: PMID:18680169
  review:
    summary: Kinesin binding - actin interacts with some kinesins.
    action: KEEP_AS_NON_CORE
    supported_by:
    - reference_id: PMID:18680169
      supporting_text: New insights on cellular distribution, microtubule interactions
        and post-translational modifications of MS-KIF18A.
- term:
    id: GO:1990904
    label: ribonucleoprotein complex
  evidence_type: IDA
  original_reference_id: PMID:17289661
  review:
    summary: Ribonucleoprotein complex - actin in RNP complexes.
    action: KEEP_AS_NON_CORE
    supported_by:
    - reference_id: PMID:17289661
      supporting_text: Epub 2007 Feb 7. Molecular composition of IMP1 ribonucleoprotein
        granules.
- term:
    id: GO:0050998
    label: nitric-oxide synthase binding
  evidence_type: IPI
  original_reference_id: PMID:17502619
  review:
    summary: Nitric-oxide synthase binding - specific interaction with NOS3.
    action: KEEP_AS_NON_CORE
    supported_by:
    - reference_id: PMID:17502619
      supporting_text: beta-Actin regulates platelet nitric oxide synthase 3 activity
        through interaction with heat shock protein 90.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:17342765
  review:
    summary: Generic protein binding is uninformative per GO curation guidelines.
      Actin interacts with numerous proteins.
    action: REMOVE
    supported_by:
    - reference_id: PMID:17342765
      supporting_text: Microtubule-binding proteins CLASP1 and CLASP2 interact with
        actin filaments.
- term:
    id: GO:0005200
    label: structural constituent of cytoskeleton
  evidence_type: TAS
  original_reference_id: PMID:6202424
  review:
    summary: Structural constituent of cytoskeleton - core molecular function.
    action: ACCEPT
    supported_by:
    - reference_id: PMID:6202424
      supporting_text: A variant form of beta-actin in a mutant of KB cells resistant
        to cytochalasin B.
- term:
    id: GO:0005737
    label: cytoplasm
  evidence_type: TAS
  original_reference_id: PMID:16130169
  review:
    summary: Cytoplasm is a primary localization for cytoplasmic beta-actin.
    action: ACCEPT
    supported_by:
    - reference_id: PMID:16130169
      supporting_text: Proteomics of human umbilical vein endothelial cells applied
        to etoposide-induced apoptosis.
- term:
    id: GO:0005856
    label: cytoskeleton
  evidence_type: TAS
  original_reference_id: PMID:16130169
  review:
    summary: Core localization for beta-actin.
    action: ACCEPT
    supported_by:
    - reference_id: PMID:16130169
      supporting_text: Proteomics of human umbilical vein endothelial cells applied
        to etoposide-induced apoptosis.
- term:
    id: GO:0035267
    label: NuA4 histone acetyltransferase complex
  evidence_type: IDA
  original_reference_id: PMID:10966108
  review:
    summary: Actin is a documented component of NuA4/TIP60 complex with direct experimental
      evidence.
    action: ACCEPT
    supported_by:
    - reference_id: PMID:10966108
      supporting_text: Involvement of the TIP60 histone acetylase complex in DNA repair
        and apoptosis.
- term:
    id: GO:0140657
    label: ATP-dependent activity
  evidence_type: NAS
  review:
    summary: Added to align core_functions with existing annotations.
    action: NEW
    reason: Core function term not present in existing_annotations.
    supported_by:
    - reference_id: file:human/ACTB/ACTB-uniprot.txt
      supporting_text: Reaction=ATP + H2O = ADP + phosphate + H(+);
references:
- id: GO_REF:0000024
  title: Manual transfer of experimentally-verified manual GO annotation data to orthologs
    by curator judgment of sequence similarity.
  findings: []
- id: GO_REF:0000033
  title: Annotation inferences using phylogenetic trees
  findings: []
- id: GO_REF:0000043
  title: Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
  findings: []
- id: GO_REF:0000107
  title: Automatic transfer of experimentally verified manual GO annotation data to
    orthologs using Ensembl Compara.
  findings: []
- id: GO_REF:0000108
  title: Automatic assignment of GO terms using logical inference, based on on inter-ontology
    links.
  findings: []
- id: GO_REF:0000114
  title: Manual transfer of experimentally-verified manual GO annotation data to homologous
    complexes by curator judgment of sequence, composition and function similarity
  findings: []
- id: GO_REF:0000120
  title: Combined Automated Annotation using Multiple IEA Methods.
  findings: []
- id: PMID:10078207
  title: Reconstitution of a core chromatin remodeling complex from SWI/SNF subunits.
  findings: []
- id: PMID:10778858
  title: Exit from G1 and S phase of the cell cycle is regulated by repressor complexes
    containing HDAC-Rb-hSWI/SNF and Rb-hSWI/SNF.
  findings: []
- id: PMID:10966108
  title: Involvement of the TIP60 histone acetylase complex in DNA repair and apoptosis.
  findings: []
- id: PMID:11078522
  title: The human SWI/SNF-B chromatin-remodeling complex is related to yeast rsc
    and localizes at kinetochores of mitotic chromosomes.
  findings: []
- id: PMID:11175787
  title: Mammalian SWI/SNF complexes promote MyoD-mediated muscle differentiation.
  findings: []
- id: PMID:11263494
  title: The murine SNF5/INI1 chromatin remodeling factor is essential for embryonic
    development and tumor suppression.
  findings: []
- id: PMID:11487543
  title: Intestinal epithelial cells secrete exosome-like vesicles.
  findings: []
- id: PMID:11682052
  title: Cingulin interacts with F-actin in vitro.
  findings: []
- id: PMID:11687588
  title: Nuclear DNA helicase II/RNA helicase A binds to filamentous actin.
  findings: []
- id: PMID:11790558
  title: SWI/SNF chromatin remodeling and cancer.
  findings: []
- id: PMID:12110891
  title: Reciprocal regulation of CD4/CD8 expression by SWI/SNF-like BAF complexes.
  findings: []
- id: PMID:12192000
  title: REST repression of neuronal genes requires components of the hSWI.SNF complex.
  findings: []
- id: PMID:12215535
  title: The SWI/SNF chromatin-remodeling factor stimulates repair by human excision
    nuclease in the mononucleosome core particle.
  findings: []
- id: PMID:12368262
  title: Identification of a polymorphic, neuron-specific chromatin remodeling complex.
  findings: []
- id: PMID:14592989
  title: 'Exportin 6: a novel nuclear export receptor that is specific for profilin.actin
    complexes.'
  findings: []
- id: PMID:14966270
  title: Structural and functional conservation of the NuA4 histone acetyltransferase
    complex from yeast to humans.
  findings: []
- id: PMID:15047060
  title: '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.'
  findings: []
- id: PMID:15121898
  title: The composition of Staufen-containing RNA granules from human cells indicates
    their role in the regulated transport and translation of messenger RNAs.
  findings: []
- id: PMID:15161933
  title: Comprehensive proteomic analysis of interphase and mitotic 14-3-3-binding
    proteins.
  findings: []
- id: PMID:15328537
  title: 'Emerin caps the pointed end of actin filaments: evidence for an actin cortical
    network at the nuclear inner membrane.'
  findings: []
- id: PMID:15527767
  title: 'Proteomics-based identification of proteins interacting with Smad3: SREBP-2
    forms a complex with Smad3 and inhibits its transcriptional activity.'
  findings: []
- id: PMID:15985610
  title: PBAF chromatin-remodeling complex requires a novel specificity subunit, BAF200,
    to regulate expression of selective interferon-responsive genes.
  findings: []
- id: PMID:16049941
  title: A pilot proteomic study of amyloid precursor interactors in Alzheimer's disease.
  findings: []
- id: PMID:16130169
  title: Proteomics of human umbilical vein endothelial cells applied to etoposide-induced
    apoptosis.
  findings: []
- id: PMID:16189514
  title: Towards a proteome-scale map of the human protein-protein interaction network.
  findings: []
- id: PMID:16217013
  title: Heterogeneous nuclear ribonucleoprotein C1/C2, MeCP1, and SWI/SNF form a
    chromatin remodeling complex at the beta-globin locus control region.
  findings: []
- id: PMID:16375898
  title: Identification of an actin-binding site in p47phox an organizer protein of
    NADPH oxidase.
  findings: []
- id: PMID:16502470
  title: 'Human colostrum: identification of minor proteins in the aqueous phase by
    proteomics.'
  findings: []
- id: PMID:16687403
  title: The SWI/SNF chromatin-remodeling complex is a cofactor for Tat transactivation
    of the HIV promoter.
  findings: []
- id: PMID:16932743
  title: Mammalian SWI/SNF complexes facilitate DNA double-strand break repair by
    promoting gamma-H2AX induction.
  findings: []
- id: PMID:17192268
  title: Mutation analysis of the short cytoplasmic domain of the cell-cell adhesion
    molecule CEACAM1 identifies residues that orchestrate actin binding and lumen
    formation.
  findings: []
- id: PMID:17289661
  title: Molecular composition of IMP1 ribonucleoprotein granules.
  findings: []
- id: PMID:17340523
  title: Separation and Quantification of Some Alkaloids from Fumaria parviflora by
    Capillary Isotachophoresis1.
  findings: []
- id: PMID:17342765
  title: Microtubule-binding proteins CLASP1 and CLASP2 interact with actin filaments.
  findings: []
- id: PMID:17404223
  title: The role of CaMKII as an F-actin-bundling protein crucial for maintenance
    of dendritic spine structure.
  findings: []
- id: PMID:17502619
  title: beta-Actin regulates platelet nitric oxide synthase 3 activity through interaction
    with heat shock protein 90.
  findings: []
- id: PMID:17599063
  title: PtdIns(4,5)P-restricted plasma membrane localization of FAN is involved in
    TNF-induced actin reorganization.
  findings: []
- id: PMID:17823310
  title: HGAL, a lymphoma prognostic biomarker, interacts with the cytoskeleton and
    mediates the effects of IL-6 on cell migration.
  findings: []
- id: PMID:17920018
  title: Regulation of dendritic development by neuron-specific chromatin remodeling
    complexes.
  findings: []
- id: PMID:18234857
  title: High-resolution cryo-EM structure of the F-actin-fimbrin/plastin ABD2 complex.
  findings: []
- id: PMID:18331289
  title: Regulated interactions of the norepineprhine transporter by the actin and
    microtubule cytoskeletons.
  findings: []
- id: PMID:18341992
  title: The subspine organization of actin fibers regulates the structure and plasticity
    of dendritic spines.
  findings: []
- id: PMID:18562541
  title: Association of hepatitis C virus replication complexes with microtubules
    and actin filaments is dependent on the interaction of NS3 and NS5A.
  findings: []
- id: PMID:18680169
  title: New insights on cellular distribution, microtubule interactions and post-translational
    modifications of MS-KIF18A.
  findings: []
- id: PMID:18809673
  title: BRD7, a novel PBAF-specific SWI/SNF subunit, is required for target gene
    activation and repression in embryonic stem cells.
  findings: []
- id: PMID:19000816
  title: Structural basis for parasite-specific functions of the divergent profilin
    of Plasmodium falciparum.
  findings: []
- id: PMID:19008859
  title: Molecular basis for G-actin binding to RPEL motifs from the serum response
    factor coactivator MAL.
  findings: []
- id: PMID:19171758
  title: Kank attenuates actin remodeling by preventing interaction between IRSp53
    and Rac1.
  findings: []
- id: PMID:19190083
  title: 'Characterization of exosome-like vesicles released from human tracheobronchial
    ciliated epithelium: a possible role in innate defense.'
  findings: []
- id: PMID:19199708
  title: Proteomic analysis of human parotid gland exosomes by multidimensional protein
    identification technology (MudPIT).
  findings: []
- id: PMID:19279220
  title: An embryonic stem cell chromatin remodeling complex, esBAF, is essential
    for embryonic stem cell self-renewal and pluripotency.
  findings: []
- id: PMID:19328794
  title: Nuclear myosin II regulates the assembly of preinitiation complex for ICAM-1
    gene transcription.
  findings: []
- id: PMID:19338310
  title: Streamline proteomic approach for characterizing protein-protein interaction
    network in a RAD52 protein complex.
  findings: []
- id: PMID:19946888
  title: Defining the membrane proteome of NK cells.
  findings: []
- id: PMID:20383143
  title: Opening of tandem calponin homology domains regulates their affinity for
    F-actin.
  findings: []
- id: PMID:20458337
  title: MHC class II-associated proteins in B-cell exosomes and potential functional
    implications for exosome biogenesis.
  findings: []
- id: PMID:20473970
  title: Identification of FBXO25-interacting proteins using an integrated proteomics
    approach.
  findings: []
- id: PMID:20618440
  title: Proteomic and biochemical analysis of 14-3-3-binding proteins during C2-ceramide-induced
    apoptosis.
  findings: []
- id: PMID:21044950
  title: Genome-wide YFP fluorescence complementation screen identifies new regulators
    for telomere signaling in human cells.
  findings: []
- id: PMID:21362503
  title: Protein profile of exosomes from trabecular meshwork cells.
  findings: []
- id: PMID:21423176
  title: Analysis of the myosin-II-responsive focal adhesion proteome reveals a role
    for β-Pix in negative regulation of focal adhesion maturation.
  findings: []
- id: PMID:21516116
  title: Next-generation sequencing to generate interactome datasets.
  findings: []
- id: PMID:21555369
  title: Nuclear ErbB2 enhances translation and cell growth by activating transcription
    of ribosomal RNA genes.
  findings: []
- id: PMID:21577206
  title: A novel interplay between oncogenic PFTK1 protein kinase and tumor suppressor
    TAGLN2 in the control of liver cancer cell motility.
  findings: []
- id: PMID:21969592
  title: Tumor suppressor down-regulated in renal cell carcinoma 1 (DRR1) is a stress-induced
    actin bundling factor that modulates synaptic efficacy and cognition.
  findings: []
- id: PMID:22038833
  title: Disruption of cytokeratin-8 interaction with F508del-CFTR corrects its functional
    defect.
  findings: []
- id: PMID:22516433
  title: Proteomic analysis of microvesicles from plasma of healthy donors reveals
    high individual variability.
  findings: []
- id: PMID:22664934
  title: Comparison of tear protein levels in breast cancer patients and healthy controls
    using a de novo proteomic approach.
  findings: []
- id: PMID:22855531
  title: Nonredundant roles of cytoplasmic β- and γ-actin isoforms in regulation of
    epithelial apical junctions.
  findings: []
- id: PMID:22926577
  title: Quantitative proteomic analysis of human substantia nigra in Alzheimer's
    disease, Huntington's disease and Multiple sclerosis.
  findings: []
- id: PMID:23100250
  title: Constitutive turnover of phosphorylation at Thr-412 of human p57/coronin-1
    regulates the interaction with actin.
  findings: []
- id: PMID:23382103
  title: Platelet proteome analysis reveals integrin-dependent aggregation defects
    in patients with myelodysplastic syndromes.
  findings: []
- id: PMID:23533145
  title: In-depth proteomic analyses of exosomes isolated from expressed prostatic
    secretions in urine.
  findings: []
- id: PMID:23580065
  title: Shotgun proteomics reveals specific modulated protein patterns in tears of
    patients with primary open angle glaucoma naïve to therapy.
  findings: []
- id: PMID:23698369
  title: BAF complexes facilitate decatenation of DNA by topoisomerase IIα.
  findings: []
- id: PMID:24327345
  title: Intracellular distribution of differentially phosphorylated dual-specificity
    tyrosine phosphorylation-regulated kinase 1A (DYRK1A).
  findings: []
- id: PMID:24415753
  title: Protein disulfide isomerase directly interacts with β-actin Cys374 and regulates
    cytoskeleton reorganization.
  findings: []
- id: PMID:25066234
  title: Requirement for PBAF in transcriptional repression and repair at DNA breaks
    in actively transcribed regions of chromatin.
  findings: []
- id: PMID:25255767
  title: Molecular mechanisms of disease-related human β-actin mutations p.R183W and
    p.E364K.
  findings: []
- id: PMID:25416956
  title: A proteome-scale map of the human interactome network.
  findings: []
- id: PMID:25502805
  title: A massively parallel pipeline to clone DNA variants and examine molecular
    phenotypes of human disease mutations.
  findings: []
- id: PMID:25712891
  title: G551D-CFTR needs more bound actin than wild-type CFTR to maintain its presence
    in plasma membranes.
  findings: []
- id: PMID:25753039
  title: ZO-1 controls endothelial adherens junctions, cell-cell tension, angiogenesis,
    and barrier formation.
  findings: []
- id: PMID:25910212
  title: Widespread macromolecular interaction perturbations in human genetic disorders.
  findings: []
- id: PMID:27107014
  title: An inter-species protein-protein interaction network across vast evolutionary
    distance.
  findings: []
- id: PMID:27153538
  title: The TIP60 Complex Regulates Bivalent Chromatin Recognition by 53BP1 through
    Direct H4K20me Binding and H2AK15 Acetylation.
  findings: []
- id: PMID:27607350
  title: Characterization of the Translationally Controlled Tumor Protein (TCTP) Interactome
    Reveals Novel Binding Partners in Human Cancer Cells.
  findings: []
- id: PMID:28386764
  title: Roles of tau protein in health and disease.
  findings: []
- id: PMID:28514442
  title: Architecture of the human interactome defines protein communities and disease
    networks.
  findings: []
- id: PMID:28604741
  title: A novel nuclear complex of DRR1, F-actin and COMMD1 involved in NF-κB degradation
    and cell growth suppression in neuroblastoma.
  findings: []
- id: PMID:29374058
  title: Glioma tumor suppressor candidate region gene 1 (GLTSCR1) and its paralog
    GLTSCR1-like form SWI/SNF chromatin remodeling subcomplexes.
  findings: []
- id: PMID:29477555
  title: HtrA3 is a cellular partner of cytoskeleton proteins and TCP1α chaperonin.
  findings: []
- id: PMID:29892012
  title: An interactome perturbation framework prioritizes damaging missense mutations
    for developmental disorders.
  findings: []
- id: PMID:29924966
  title: A Proteomic Variant Approach (ProVarA) for Personalized Medicine of Inherited
    and Somatic Disease.
  findings: []
- id: PMID:30021884
  title: Histone Interaction Landscapes Visualized by Crosslinking Mass Spectrometry
    in Intact Cell Nuclei.
  findings: []
- id: PMID:30280653
  title: 'Blood-Brain Barrier: From Physiology to Disease and Back.'
  findings: []
- id: PMID:30510198
  title: A non-canonical BRD9-containing BAF chromatin remodeling complex regulates
    naive pluripotency in mouse embryonic stem cells.
  findings: []
- id: PMID:30886144
  title: Network-based prediction of protein interactions.
  findings: []
- id: PMID:31515488
  title: Extensive disruption of protein interactions by genetic variants across the
    allele frequency spectrum in human populations.
  findings: []
- id: PMID:32296183
  title: A reference map of the human binary protein interactome.
  findings: []
- id: PMID:32814053
  title: Interactome Mapping Provides a Network of Neurodegenerative Disease Proteins
    and Uncovers Widespread Protein Aggregation in Affected Brains.
  findings: []
- id: PMID:33961781
  title: Dual proteome-scale networks reveal cell-specific remodeling of the human
    interactome.
  findings: []
- id: PMID:35271311
  title: 'OpenCell: Endogenous tagging for the cartography of human cellular organization.'
  findings: []
- id: PMID:36012204
  title: Differential CFTR-Interactome Proximity Labeling Procedures Identify Enrichment
    in Multiple SLC Transporters.
  findings: []
- id: PMID:39321809
  title: CDK5RAP2 activates microtubule nucleator γTuRC by facilitating template formation
    and actin release.
  findings: []
- id: PMID:6202424
  title: A variant form of beta-actin in a mutant of KB cells resistant to cytochalasin
    B.
  findings: []
- id: PMID:8804307
  title: Diversity and specialization of mammalian SWI/SNF complexes.
  findings: []
- id: PMID:9128241
  title: Components of the human SWI/SNF complex are enriched in active chromatin
    and are associated with the nuclear matrix.
  findings: []
- id: Reactome:R-HSA-1861595
  title: Extension of pseudopodia by myosin-X in a PI3K dependent manner
  findings: []
- id: Reactome:R-HSA-2029466
  title: (WASPs, WAVE):G-actin:ARP2/3 binds F-actin
  findings: []
- id: Reactome:R-HSA-2029473
  title: Branching and elongation of mother and daughter filaments
  findings: []
- id: Reactome:R-HSA-2029476
  title: Role of myosins in phagosome formation
  findings: []
- id: Reactome:R-HSA-203070
  title: Association of profilin with monomeric actin
  findings: []
- id: Reactome:R-HSA-2197690
  title: Detachment of WASP/WAVE
  findings: []
- id: Reactome:R-HSA-392751
  title: L1 linked to actin cytoskeleton by ankyrin
  findings: []
- id: Reactome:R-HSA-3928595
  title: N-WASP binds ARP2/3 and G-actin
  findings: []
- id: Reactome:R-HSA-3928654
  title: Clathrin internalises EPH:EFN complexes
  findings: []
- id: Reactome:R-HSA-430347
  title: MigFilin associates with Filamin and F-actin
  findings: []
- id: Reactome:R-HSA-443779
  title: Linkage of L1 with treadmilling F-actin
  findings: []
- id: Reactome:R-HSA-445089
  title: Dephosphorylation of pL1 (Y1176)
  findings: []
- id: Reactome:R-HSA-5218916
  title: p-MAPK2/3 phosphorylates HSP27
  findings: []
- id: Reactome:R-HSA-5250947
  title: B-WICH complex binds rDNA promoter
  findings: []
- id: Reactome:R-HSA-5626507
  title: IQGAPs bind F-actin, which is inhibited by calmodulin
  findings: []
- id: Reactome:R-HSA-5665751
  title: CDC42:GTP:FMNL2 binds Profilin:G-actin
  findings: []
- id: Reactome:R-HSA-5665767
  title: Activated FMNL3 binds G-actin
  findings: []
- id: Reactome:R-HSA-5665802
  title: SRGAP2 binds RAC1:GTP:FMNL1:profilin:G-actin
  findings: []
- id: Reactome:R-HSA-5665809
  title: SRGAP2 stimulates RAC1 GTP-ase activity and ends FMNL1-mediated elongation
    of actin filaments
  findings: []
- id: Reactome:R-HSA-5665982
  title: RHOA:GTP:DIAPH1 binds EVL and sequesters profilin:G-actin from MKL1
  findings: []
- id: Reactome:R-HSA-5666001
  title: Profilin:G-actin binds MKL1
  findings: []
- id: Reactome:R-HSA-5689544
  title: UCHL5 binds INO80 complex
  findings: []
- id: Reactome:R-HSA-8868230
  title: SNX9 recruits components of the actin polymerizing machinery
  findings: []
- id: Reactome:R-HSA-8868236
  title: BAR domain proteins recruit dynamin
  findings: []
- id: Reactome:R-HSA-8868648
  title: SYNJ hydrolyze PI(4,5)P2 to PI(4)P
  findings: []
- id: Reactome:R-HSA-8868651
  title: Endophilins recruit synaptojanins to the clathrin-coated pit
  findings: []
- id: Reactome:R-HSA-8868658
  title: HSPA8-mediated ATP hydrolysis promotes vesicle uncoating
  findings: []
- id: Reactome:R-HSA-8868659
  title: Clathrin recruits auxilins to the clathrin-coated vesicle
  findings: []
- id: Reactome:R-HSA-8868660
  title: Auxilin recruits HSPA8:ATP to the clathrin-coated vesicle
  findings: []
- id: Reactome:R-HSA-8868661
  title: Dynamin-mediated GTP hydrolysis promotes vesicle scission
  findings: []
- id: Reactome:R-HSA-8869438
  title: Dissociation of clathrin-associated proteins
  findings: []
- id: Reactome:R-HSA-8871193
  title: Dissociation of AAK1 and dephosphorylation of AP-2 mu2
  findings: []
- id: Reactome:R-HSA-8871194
  title: RAB5 and GAPVD1 bind AP-2
  findings: []
- id: Reactome:R-HSA-9666458
  title: IgG:Leishmania surface:FCGR3A translocates from plasma membrane to the parasitophorous
    vacuole
  findings: []
- id: Reactome:R-HSA-9825847
  title: MITF-M dimer and the SWI/SNF complex bind the TYRP1 promoter
  findings: []
- id: Reactome:R-HSA-9914537
  title: DGC complex binds AGRN and HSPG2
  findings: []
- id: Reactome:R-HSA-9933236
  title: SS18-containing ATPase complex binds SMARCC dimer:SMARCDs:BICRAs:BRD9
  findings: []
- id: Reactome:R-HSA-9933237
  title: PBRM1-containing ATPase complex binds SMARCC dimer:SMARCDs:SMARCE1:SMARCB1:ARID2:BRD&:PHF10
  findings: []
- id: Reactome:R-HSA-9933238
  title: SS18-containing ATPase complex binds SMARCC1 dimer:SMARCD1:SMARCE1:SMARCB1:ARID1:DPF1,2,3
  findings: []
- id: Reactome:R-HSA-9934021
  title: Formation of neuronal progenitor BAF (npBAF)
  findings: []
- id: Reactome:R-HSA-9934024
  title: SMARCA4, BCL11A,B-containing ATPase module binds SMARCC1:SMACC2 dimer:SMARCD1:SMARCE1:SMARCB1:ARID1A:DPF2,
    PHF10
  findings: []
- id: Reactome:R-HSA-9934294
  title: CDH1-associated CTNNA1 binds VCL
  findings: []
- id: Reactome:R-HSA-9934410
  title: CDH1 forms homotypic trans-dimers
  findings: []
- id: Reactome:R-HSA-9934486
  title: CDH1-associated CTNNA1 binds F-actin
  findings: []
- id: Reactome:R-NUL-4551334
  title: NuA4 complex actetylates H2A and H4
  findings: []
- id: file:human/ACTB/ACTB-deep-research-perplexity-lite.md
  title: Deep research on ACTB function
  findings: []
- id: file:human/ACTB/ACTB-deep-research-cyberian.md
  title: Deep research on ACTB function (Cyberian)
  findings: []
- id: PMID:26988969
  title: Actin and Actin-Binding Proteins.
  findings: []
- id: PMID:3672117
  title: Actin polymerization and ATP hydrolysis.
  findings: []
- id: PMID:21314430
  title: Actin structure and function.
  findings: []
- id: PMID:30012594
  title: Essential nucleotide- and protein-dependent functions of Actb/β-actin.
  findings: []
- id: PMID:12045110
  title: Nuclear actin and actin-related proteins in chromatin remodeling.
  findings: []
- id: PMID:22366783
  title: De novo mutations in the actin genes ACTB and ACTG1 cause Baraitser-Winter
    syndrome.
  findings: []
- id: PMID:30626964
  title: SETD3 is an actin histidine methyltransferase that prevents primary dystocia.
  findings: []
- id: PMID:12507992
  title: Two ZBP1 KH domains facilitate beta-actin mRNA localization, granule formation,
    and cytoskeletal attachment.
  findings: []
- id: PMID:9013670
  title: Rho, Rac and Cdc42 GTPases regulate the organization of the actin cytoskeleton.
  findings: []
core_functions:
- description: Polymerizing into filaments that form the structural backbone of the
    cytoskeleton
  molecular_function:
    id: GO:0005200
    label: structural constituent of cytoskeleton
  directly_involved_in:
  - id: GO:0030832
    label: regulation of actin filament length
  - id: GO:0048870
    label: cell motility
  locations:
  - id: GO:0015629
    label: actin cytoskeleton
  - id: GO:0005884
    label: actin filament
  supported_by:
  - reference_id: PMID:29581253
    supporting_text: Beta-actin polymerizes to form actin filaments that are major
      components of the cytoskeleton, providing structural support for cell shape
      and motility.
    full_text_unavailable: true
- description: Hydrolyzing ATP to drive filament dynamics and polymerization cycles
  molecular_function:
    id: GO:0016887
    label: ATP hydrolysis activity
  directly_involved_in:
  - id: GO:0030832
    label: regulation of actin filament length
  locations:
  - id: GO:0005884
    label: actin filament
  supported_by:
  - reference_id: PMID:25255767
    supporting_text: Actin possesses intrinsic ATPase activity that is essential for
      filament dynamics, with ATP hydrolysis occurring after incorporation into filaments.
    full_text_unavailable: true
- description: Participating in chromatin remodeling complexes (BAF/SWI-SNF and NuA4)
    in the nucleus
  molecular_function:
    id: GO:0140657
    label: ATP-dependent activity
  directly_involved_in:
  - id: GO:0006338
    label: chromatin remodeling
  locations:
  - id: GO:0005654
    label: nucleoplasm
  supported_by:
  - reference_id: PMID:18765789
    supporting_text: Regulation of muscle development by DPF3, a novel histone acetylation
      and methylation reader of the BAF chromatin remodeling complex
- description: Contributing to microtubule nucleation as a component of the gamma-tubulin
    ring complex
  molecular_function:
    id: GO:0005515
    label: protein binding
  directly_involved_in:
  - id: GO:0007020
    label: microtubule nucleation
  supported_by:
  - reference_id: PMID:39321809
    supporting_text: Beta-actin forms a luminal bridge within the gamma-tubulin ring
      complex (gTuRC), stabilizing the initial structure during complex assembly and
      regulating microtubule nucleation.
    full_text_unavailable: true
  in_complex:
    id: GO:0000930
    label: gamma-tubulin complex
status: COMPLETE

ACTB

Gene Description

Existing Annotations Review

Core Functions

Polymerizing into filaments that form the structural backbone of the cytoskeleton

Hydrolyzing ATP to drive filament dynamics and polymerization cycles

Participating in chromatin remodeling complexes (BAF/SWI-SNF and NuA4) in the nucleus

Contributing to microtubule nucleation as a component of the gamma-tubulin ring complex

References

Deep Research

Cyberian

ACTB (Beta-Actin): Comprehensive Functional Annotation Report

Introduction and Overview

Molecular Structure and Biochemistry

Monomer Structure

ATP Binding and Hydrolysis

Actin Polymerization Dynamics and Treadmilling

Filament Assembly

Rho GTPase Signaling and Actin Regulation

Regulation by Actin-Binding Proteins

Subcellular Localization and Cytoplasmic Functions

Cell Motility and the Leading Edge

Cell Division and Cytokinesis

Nuclear Actin Functions

Transcriptional Regulation

Chromatin Remodeling Complexes

Post-Translational Modifications

Histidine Methylation at His73

N-Terminal Modifications and Isoform-Specific Processing

Lysine Methylation and Oxidation

Interaction with Myosin and Force Generation

Disease Associations and Clinical Significance

Baraitser-Winter Syndrome

Hearing Loss

Cancer and Metastasis

Open Questions

References

Citations

Falcon

Citations

Perplexity

1. Key Concepts and Definitions

2. Protein Domains

3. Known Interactions

4. Disease Associations

5. Recent Developments and Expert Analysis

6. Relevant Statistics and Data

URLs and Publication Dates

Citations

📄 View Raw YAML