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Protein

Actin, cytoplasmic 1

Gene

ACTB

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Actin is a highly conserved protein that polymerizes to produce filaments that form cross-linked networks in the cytoplasm of cells (PubMed:29581253). Actin exists in both monomeric (G-actin) and polymeric (F-actin) forms, both forms playing key functions, such as cell motility and contraction (PubMed:29581253). In addition to their role in the cytoplasmic cytoskeleton, G- and F-actin also localize in the nucleus, and regulate gene transcription and motility and repair of damaged DNA (PubMed:29925947).2 Publications

Miscellaneous

In vertebrates 3 main groups of actin isoforms, alpha, beta and gamma have been identified. The alpha actins are found in muscle tissues and are a major constituent of the contractile apparatus. The beta and gamma actins coexist in most cell types as components of the cytoskeleton and as mediators of internal cell motility.Curated

Caution

Was originally thought to be part of the MLL5-L complex, at least composed of KMT2E, STK38, PPP1CA, PPP1CB, PPP1CC, HCFC1, ACTB and OGT (PubMed:19377461). However, the corresponding article has been retracted (PubMed:24336203).2 Publications

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-1445148 Translocation of SLC2A4 (GLUT4) to the plasma membrane
R-HSA-190873 Gap junction degradation
R-HSA-196025 Formation of annular gap junctions
R-HSA-2029482 Regulation of actin dynamics for phagocytic cup formation
R-HSA-3214847 HATs acetylate histones
R-HSA-389957 Prefoldin mediated transfer of substrate to CCT/TriC
R-HSA-390450 Folding of actin by CCT/TriC
R-HSA-3928662 EPHB-mediated forward signaling
R-HSA-3928665 EPH-ephrin mediated repulsion of cells
R-HSA-418990 Adherens junctions interactions
R-HSA-437239 Recycling pathway of L1
R-HSA-4420097 VEGFA-VEGFR2 Pathway
R-HSA-445095 Interaction between L1 and Ankyrins
R-HSA-446353 Cell-extracellular matrix interactions
R-HSA-5250924 B-WICH complex positively regulates rRNA expression
R-HSA-5626467 RHO GTPases activate IQGAPs
R-HSA-5663213 RHO GTPases Activate WASPs and WAVEs
R-HSA-5663220 RHO GTPases Activate Formins
R-HSA-5674135 MAP2K and MAPK activation
R-HSA-5689603 UCH proteinases
R-HSA-5696394 DNA Damage Recognition in GG-NER
R-HSA-6802946 Signaling by moderate kinase activity BRAF mutants
R-HSA-6802948 Signaling by high-kinase activity BRAF mutants
R-HSA-6802949 Signaling by RAS mutants
R-HSA-6802952 Signaling by BRAF and RAF fusions
R-HSA-6802955 Paradoxical activation of RAF signaling by kinase inactive BRAF
R-HSA-8856828 Clathrin-mediated endocytosis
R-HSA-983231 Factors involved in megakaryocyte development and platelet production

SignaLink: a signaling pathway resource with multi-layered regulatory networks

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SignaLinki
P60709

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Actin, cytoplasmic 1
Alternative name(s):
Beta-actin
Cleaved into the following chain:
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:ACTB
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 7

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000075624.13

Human Gene Nomenclature Database

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HGNCi
HGNC:132 ACTB

Online Mendelian Inheritance in Man (OMIM)

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MIMi
102630 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_P60709

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Dystonia, juvenile-onset (DJO)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of dystonia with juvenile onset. Dystonia is defined by the presence of sustained involuntary muscle contraction, often leading to abnormal postures. Patients with juvenile-onset dystonia manifest progressive, generalized, dopa-unresponsive dystonia, developmental malformations and sensory hearing loss.
See also OMIM:607371
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_030026183R → W in DJO; modifies cell response to latrunculin A. 1 PublicationCorresponds to variant dbSNP:rs104894003EnsemblClinVar.1
Baraitser-Winter syndrome 1 (BRWS1)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA rare developmental disorder characterized by the combination of congenital ptosis, high-arched eyebrows, hypertelorism, ocular colobomata, and a brain malformation consisting of anterior-predominant lissencephaly. Other typical features include postnatal short stature and microcephaly, intellectual disability, seizures, and hearing loss.
See also OMIM:243310
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_06781012N → D in BRWS1. 1 PublicationCorresponds to variant dbSNP:rs281875331EnsemblClinVar.1
Natural variantiVAR_06781165L → V in BRWS1. 1 PublicationCorresponds to variant dbSNP:rs281875332EnsemblClinVar.1
Natural variantiVAR_067812196R → C in BRWS1. 1 PublicationCorresponds to variant dbSNP:rs281875333EnsemblClinVar.1
Natural variantiVAR_067813196R → H in BRWS1. 1 PublicationCorresponds to variant dbSNP:rs281875334EnsemblClinVar.1

Keywords - Diseasei

Deafness, Disease mutation, Dystonia, Mental retardation

Organism-specific databases

DisGeNET

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DisGeNETi
60

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

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GeneReviewsi
ACTB

MalaCards human disease database

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MalaCardsi
ACTB
MIMi243310 phenotype
607371 phenotype

Open Targets

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OpenTargetsi
ENSG00000075624

Orphanet; a database dedicated to information on rare diseases and orphan drugs

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Orphaneti
2995 Baraitser-Winter cerebrofrontofacial syndrome
64755 Becker nevus syndrome
79107 Developmental malformations-deafness-dystonia syndrome

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA24457

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL2062353

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
ACTB

Domain mapping of disease mutations (DMDM)

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DMDMi
46397333

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00003670731 – 375Actin, cytoplasmic 1Add BLAST375
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved; alternateCombined sources2 Publications
ChainiPRO_00000007712 – 375Actin, cytoplasmic 1, N-terminally processed1 PublicationAdd BLAST374

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei1N-acetylmethionineCombined sources1
Modified residuei2N-acetylaspartate; in Actin, cytoplasmic 1, N-terminally processedCombined sources3 Publications1
Modified residuei44Methionine (R)-sulfoxideBy similarity1
Modified residuei47Methionine (R)-sulfoxideBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki50(Microbial infection) Isoglutamyl lysine isopeptide (Lys-Glu) (interchain with E-270); by Vibrio toxins RtxA and VgrG11 Publication
Modified residuei73Tele-methylhistidineBy similarity1
Modified residuei84N6-methyllysine1 Publication1
Cross-linki270(Microbial infection) Isoglutamyl lysine isopeptide (Glu-Lys) (interchain with K-50); by Vibrio toxins RtxA and VgrG11 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

ISGylated.1 Publication
Oxidation of Met-44 and Met-47 by MICALs (MICAL1, MICAL2 or MICAL3) to form methionine sulfoxide promotes actin filament depolymerization. MICAL1 and MICAL2 produce the (R)-S-oxide form. The (R)-S-oxide form is reverted by MSRB1 and MSRB2, which promote actin repolymerization.By similarity
Monomethylation at Lys-84 (K84me1) regulates actin-myosin interaction and actomyosin-dependent processes (PubMed:23673617). Demethylation by ALKBH4 is required for maintaining actomyosin dynamics supporting normal cleavage furrow ingression during cytokinesis and cell migration (PubMed:23673617).1 Publication
Actin, cytoplasmic 1, N-terminally processed: N-terminal acetylation by NAA80 affects actin filament depolymerization and elongation, including elongation driven by formins (PubMed:29581253). In contrast, filament nucleation by the Arp2/3 complex is not affected (PubMed:29581253).1 Publication
(Microbial infection) Monomeric actin is cross-linked by V.cholerae toxins RtxA and VgrG1 in case of infection: bacterial toxins mediate the cross-link between Lys-50 of one monomer and Glu-270 of another actin monomer, resulting in formation of highly toxic actin oligomers that cause cell rounding (PubMed:19015515). The toxin can be highly efficient at very low concentrations by acting on formin homology family proteins: toxic actin oligomers bind with high affinity to formins and adversely affect both nucleation and elongation abilities of formins, causing their potent inhibition in both profilin-dependent and independent manners (PubMed:26228148).2 Publications

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Oxidation, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P60709

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
P60709

PeptideAtlas

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PeptideAtlasi
P60709

PRoteomics IDEntifications database

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PRIDEi
P60709

ProteomicsDB human proteome resource

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ProteomicsDBi
57224

Consortium for Top Down Proteomics

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TopDownProteomicsi
P60709

2D gel databases

DOSAC-COBS 2D-PAGE database

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DOSAC-COBS-2DPAGEi
P60709

REPRODUCTION-2DPAGE

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REPRODUCTION-2DPAGEi
P60709

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

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SWISS-2DPAGEi
P60709

University College Dublin 2-DE Proteome Database

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UCD-2DPAGEi
P60709

PTM databases

CarbonylDB database of protein carbonylation sites

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CarbonylDBi
P60709

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P60709

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
P60709

SwissPalm database of S-palmitoylation events

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SwissPalmi
P60709

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000075624 Expressed in 230 organ(s), highest expression level in popliteal artery

CleanEx database of gene expression profiles

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CleanExi
HS_ACTB

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P60709 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P60709 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB002621
HPA041264
HPA041271

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Polymerization of globular actin (G-actin) leads to a structural filament (F-actin) in the form of a two-stranded helix (PubMed:28604741, PubMed:16685646). Each actin can bind to 4 others (PubMed:28604741, PubMed:16685646). Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs (PubMed:17289661). Component of the BAF complex, which includes at least actin (ACTB), ARID1A, ARID1B/BAF250, SMARCA2, SMARCA4/BRG1, ACTL6A/BAF53, ACTL6B/BAF53B, SMARCE1/BAF57 SMARCC1/BAF155, SMARCC2/BAF170, SMARCB1/SNF5/INI1, and one or more of SMARCD1/BAF60A, SMARCD2/BAF60B, or SMARCD3/BAF60C (PubMed:18765789). In muscle cells, the BAF complex also contains DPF3 (PubMed:18765789). Found in a complex with XPO6, Ran, ACTB and PFN1 (PubMed:14592989). Interacts with XPO6 and EMD (PubMed:15328537). Interacts with ERBB2 (PubMed:21555369). Interacts with GCSAM (PubMed:17823310). Interacts with TBC1D21 (By similarity). Interacts with CPNE1 (via VWFA domain) and CPNE4 (via VWFA domain) (By similarity). Interacts with DHX9 (via C-terminus); this interaction is direct and mediates the attachment to nuclear ribonucleoprotein complexes (PubMed:11687588). Interacts with FAM107A (PubMed:21969592, PubMed:28604741).By similarity10 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
106575, 319 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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ComplexPortali
CPX-1164 SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA2 variant
CPX-1194 Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA2 variant
CPX-1195 Embryonic stem cell-specific SWI/SNF ATP-dependent chromatin remodeling complex
CPX-1196 Polybromo-associated SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B variant
CPX-1199 Polybromo-associated SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A variant
CPX-1201 Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA2 variant
CPX-1202 Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA2 variant
CPX-1203 Brain-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA2 variant
CPX-1204 SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA4 variant
CPX-1205 SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA2 variant
CPX-1206 SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA4 variant
CPX-1207 SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA2 variant
CPX-1209 SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA4 variant
CPX-1210 SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA2 variant
CPX-1211 SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA4 variant
CPX-1212 Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA4 variant
CPX-1213 Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA2 variant
CPX-1215 Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA4 variant
CPX-1216 Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA4 variant
CPX-1217 Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA2 variant
CPX-1218 Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA4 variant
CPX-1219 Brain-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA4 variant
CPX-1220 Brain-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA2 variant
CPX-1221 Brain-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA4 variant
CPX-1222 Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA4 variant
CPX-1223 Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA2 variant
CPX-1224 Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA4 variant
CPX-1225 Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA2 variant
CPX-1226 Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA4 variant
CPX-1227 Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA2 variant
CPX-1228 Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA4 variant
CPX-978 NuA4 histone acetyltransferase complex

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P60709

Database of interacting proteins

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DIPi
DIP-29686N

Protein interaction database and analysis system

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IntActi
P60709, 223 interactors

Molecular INTeraction database

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MINTi
P60709

STRING: functional protein association networks

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STRINGi
9606.ENSP00000349960

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P60709

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P60709

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P60709

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the actin family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG0676 Eukaryota
COG5277 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000154122

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG003771

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P60709

KEGG Orthology (KO)

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KOi
K05692

Identification of Orthologs from Complete Genome Data

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OMAi
YKCDLDI

Database of Orthologous Groups

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OrthoDBi
EOG091G08LD

Database for complete collections of gene phylogenies

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PhylomeDBi
P60709

TreeFam database of animal gene trees

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TreeFami
TF354237

Family and domain databases

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR004000 Actin
IPR020902 Actin/actin-like_CS
IPR004001 Actin_CS

The PANTHER Classification System

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PANTHERi
PTHR11937 PTHR11937, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00022 Actin, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00190 ACTIN

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00268 ACTIN, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00406 ACTINS_1, 1 hit
PS00432 ACTINS_2, 1 hit
PS01132 ACTINS_ACT_LIKE, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 9 potential isoforms that are computationally mapped.Show allAlign All

P60709-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MDDDIAALVV DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGVMVGMGQK
60 70 80 90 100
DSYVGDEAQS KRGILTLKYP IEHGIVTNWD DMEKIWHHTF YNELRVAPEE
110 120 130 140 150
HPVLLTEAPL NPKANREKMT QIMFETFNTP AMYVAIQAVL SLYASGRTTG
160 170 180 190 200
IVMDSGDGVT HTVPIYEGYA LPHAILRLDL AGRDLTDYLM KILTERGYSF
210 220 230 240 250
TTTAEREIVR DIKEKLCYVA LDFEQEMATA ASSSSLEKSY ELPDGQVITI
260 270 280 290 300
GNERFRCPEA LFQPSFLGME SCGIHETTFN SIMKCDVDIR KDLYANTVLS
310 320 330 340 350
GGTTMYPGIA DRMQKEITAL APSTMKIKII APPERKYSVW IGGSILASLS
360 370
TFQQMWISKQ EYDESGPSIV HRKCF
Length:375
Mass (Da):41,737
Last modified:April 1, 1988 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i6AFD05CA94E360E2
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 9 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
G5E9R0G5E9R0_HUMAN
Actin, cytoplasmic 1
ACTB hCG_15971
125Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E7EVS6E7EVS6_HUMAN
Actin, cytoplasmic 1
ACTB
163Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A2R8Y793A0A2R8Y793_HUMAN
Actin, cytoplasmic 1
ACTB
309Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A2R8YGF8A0A2R8YGF8_HUMAN
Actin, cytoplasmic 1
ACTB
165Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A2R8YEA7A0A2R8YEA7_HUMAN
Actin, cytoplasmic 1
ACTB
157Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
C9JZR7C9JZR7_HUMAN
Actin, cytoplasmic 1
ACTB
102Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
C9JTX5C9JTX5_HUMAN
Actin, cytoplasmic 1
ACTB
80Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
C9JUM1C9JUM1_HUMAN
Actin, cytoplasmic 1
ACTB
96Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A2R8YFE2A0A2R8YFE2_HUMAN
Actin, cytoplasmic 1
ACTB
79Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti97A → P in AAH16045 (PubMed:15489334).Curated1
Sequence conflicti116R → L in AAH12854 (PubMed:15489334).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_06781012N → D in BRWS1. 1 PublicationCorresponds to variant dbSNP:rs281875331EnsemblClinVar.1
Natural variantiVAR_06781165L → V in BRWS1. 1 PublicationCorresponds to variant dbSNP:rs281875332EnsemblClinVar.1
Natural variantiVAR_030026183R → W in DJO; modifies cell response to latrunculin A. 1 PublicationCorresponds to variant dbSNP:rs104894003EnsemblClinVar.1
Natural variantiVAR_067812196R → C in BRWS1. 1 PublicationCorresponds to variant dbSNP:rs281875333EnsemblClinVar.1
Natural variantiVAR_067813196R → H in BRWS1. 1 PublicationCorresponds to variant dbSNP:rs281875334EnsemblClinVar.1
Natural variantiVAR_048185243P → L. Corresponds to variant dbSNP:rs11546899Ensembl.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
X00351 mRNA Translation: CAA25099.1
M10277 Genomic DNA Translation: AAA51567.1
X63432 mRNA Translation: CAA45026.1
AY582799 Genomic DNA Translation: AAS79319.1
AC006483 Genomic DNA Translation: AAP22343.1
BC001301 mRNA Translation: AAH01301.1
BC002409 mRNA Translation: AAH02409.1
BC004251 mRNA Translation: AAH04251.1
BC008633 mRNA Translation: AAH08633.1
BC012854 mRNA Translation: AAH12854.1
BC013380 mRNA Translation: AAH13380.1
BC014861 mRNA Translation: AAH14861.1
BC016045 mRNA Translation: AAH16045.1
V00478 mRNA Translation: CAA23745.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS5341.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A25168 ATHUB

NCBI Reference Sequences

More...
RefSeqi
NP_001092.1, NM_001101.3

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.520640

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000331789; ENSP00000349960; ENSG00000075624
ENST00000493945; ENSP00000494269; ENSG00000075624
ENST00000646664; ENSP00000494750; ENSG00000075624

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
60

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:60

Keywords - Coding sequence diversityi

Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology
NIEHS-SNPs
Mendelian genes actin, beta (ACTB)

Leiden Open Variation Database (LOVD)

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X00351 mRNA Translation: CAA25099.1
M10277 Genomic DNA Translation: AAA51567.1
X63432 mRNA Translation: CAA45026.1
AY582799 Genomic DNA Translation: AAS79319.1
AC006483 Genomic DNA Translation: AAP22343.1
BC001301 mRNA Translation: AAH01301.1
BC002409 mRNA Translation: AAH02409.1
BC004251 mRNA Translation: AAH04251.1
BC008633 mRNA Translation: AAH08633.1
BC012854 mRNA Translation: AAH12854.1
BC013380 mRNA Translation: AAH13380.1
BC014861 mRNA Translation: AAH14861.1
BC016045 mRNA Translation: AAH16045.1
V00478 mRNA Translation: CAA23745.1
CCDSiCCDS5341.1
PIRiA25168 ATHUB
RefSeqiNP_001092.1, NM_001101.3
UniGeneiHs.520640

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3BYHelectron microscopy12.00A2-375[»]
3D2UX-ray2.21C/G170-178[»]
3J82electron microscopy7.70B/C/D2-375[»]
3LUEelectron microscopy-A/B/C/D/E/F/G/H/I/J2-375[»]
6ANUelectron microscopy7.00A/B/C/D/E/F1-375[»]
ProteinModelPortaliP60709
SMRiP60709
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106575, 319 interactors
ComplexPortaliCPX-1164 SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA2 variant
CPX-1194 Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA2 variant
CPX-1195 Embryonic stem cell-specific SWI/SNF ATP-dependent chromatin remodeling complex
CPX-1196 Polybromo-associated SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B variant
CPX-1199 Polybromo-associated SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A variant
CPX-1201 Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA2 variant
CPX-1202 Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA2 variant
CPX-1203 Brain-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA2 variant
CPX-1204 SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA4 variant
CPX-1205 SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA2 variant
CPX-1206 SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA4 variant
CPX-1207 SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA2 variant
CPX-1209 SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA4 variant
CPX-1210 SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA2 variant
CPX-1211 SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA4 variant
CPX-1212 Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA4 variant
CPX-1213 Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA2 variant
CPX-1215 Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA4 variant
CPX-1216 Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA4 variant
CPX-1217 Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA2 variant
CPX-1218 Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA4 variant
CPX-1219 Brain-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA4 variant
CPX-1220 Brain-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA2 variant
CPX-1221 Brain-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA4 variant
CPX-1222 Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA4 variant
CPX-1223 Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA2 variant
CPX-1224 Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA4 variant
CPX-1225 Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA2 variant
CPX-1226 Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA4 variant
CPX-1227 Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA2 variant
CPX-1228 Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA4 variant
CPX-978 NuA4 histone acetyltransferase complex
CORUMiP60709
DIPiDIP-29686N
IntActiP60709, 223 interactors
MINTiP60709
STRINGi9606.ENSP00000349960

Chemistry databases

ChEMBLiCHEMBL2062353

PTM databases

CarbonylDBiP60709
iPTMnetiP60709
PhosphoSitePlusiP60709
SwissPalmiP60709

Polymorphism and mutation databases

BioMutaiACTB
DMDMi46397333

2D gel databases

DOSAC-COBS-2DPAGEiP60709
REPRODUCTION-2DPAGEiP60709
SWISS-2DPAGEiP60709
UCD-2DPAGEiP60709

Proteomic databases

EPDiP60709
PaxDbiP60709
PeptideAtlasiP60709
PRIDEiP60709
ProteomicsDBi57224
TopDownProteomicsiP60709

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
60
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000331789; ENSP00000349960; ENSG00000075624
ENST00000493945; ENSP00000494269; ENSG00000075624
ENST00000646664; ENSP00000494750; ENSG00000075624
GeneIDi60
KEGGihsa:60

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
60
DisGeNETi60
EuPathDBiHostDB:ENSG00000075624.13

GeneCards: human genes, protein and diseases

More...
GeneCardsi
ACTB
GeneReviewsiACTB
HGNCiHGNC:132 ACTB
HPAiCAB002621
HPA041264
HPA041271
MalaCardsiACTB
MIMi102630 gene
243310 phenotype
607371 phenotype
neXtProtiNX_P60709
OpenTargetsiENSG00000075624
Orphaneti2995 Baraitser-Winter cerebrofrontofacial syndrome
64755 Becker nevus syndrome
79107 Developmental malformations-deafness-dystonia syndrome
PharmGKBiPA24457

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0676 Eukaryota
COG5277 LUCA
GeneTreeiENSGT00940000154122
HOVERGENiHBG003771
InParanoidiP60709
KOiK05692
OMAiYKCDLDI
OrthoDBiEOG091G08LD
PhylomeDBiP60709
TreeFamiTF354237

Enzyme and pathway databases

ReactomeiR-HSA-1445148 Translocation of SLC2A4 (GLUT4) to the plasma membrane
R-HSA-190873 Gap junction degradation
R-HSA-196025 Formation of annular gap junctions
R-HSA-2029482 Regulation of actin dynamics for phagocytic cup formation
R-HSA-3214847 HATs acetylate histones
R-HSA-389957 Prefoldin mediated transfer of substrate to CCT/TriC
R-HSA-390450 Folding of actin by CCT/TriC
R-HSA-3928662 EPHB-mediated forward signaling
R-HSA-3928665 EPH-ephrin mediated repulsion of cells
R-HSA-418990 Adherens junctions interactions
R-HSA-437239 Recycling pathway of L1
R-HSA-4420097 VEGFA-VEGFR2 Pathway
R-HSA-445095 Interaction between L1 and Ankyrins
R-HSA-446353 Cell-extracellular matrix interactions
R-HSA-5250924 B-WICH complex positively regulates rRNA expression
R-HSA-5626467 RHO GTPases activate IQGAPs
R-HSA-5663213 RHO GTPases Activate WASPs and WAVEs
R-HSA-5663220 RHO GTPases Activate Formins
R-HSA-5674135 MAP2K and MAPK activation
R-HSA-5689603 UCH proteinases
R-HSA-5696394 DNA Damage Recognition in GG-NER
R-HSA-6802946 Signaling by moderate kinase activity BRAF mutants
R-HSA-6802948 Signaling by high-kinase activity BRAF mutants
R-HSA-6802949 Signaling by RAS mutants
R-HSA-6802952 Signaling by BRAF and RAF fusions
R-HSA-6802955 Paradoxical activation of RAF signaling by kinase inactive BRAF
R-HSA-8856828 Clathrin-mediated endocytosis
R-HSA-983231 Factors involved in megakaryocyte development and platelet production
SignaLinkiP60709

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
ACTB human
EvolutionaryTraceiP60709

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
Beta-actin

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
60

Protein Ontology

More...
PROi
PR:P60709

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000075624 Expressed in 230 organ(s), highest expression level in popliteal artery
CleanExiHS_ACTB
ExpressionAtlasiP60709 baseline and differential
GenevisibleiP60709 HS

Family and domain databases

InterProiView protein in InterPro
IPR004000 Actin
IPR020902 Actin/actin-like_CS
IPR004001 Actin_CS
PANTHERiPTHR11937 PTHR11937, 1 hit
PfamiView protein in Pfam
PF00022 Actin, 1 hit
PRINTSiPR00190 ACTIN
SMARTiView protein in SMART
SM00268 ACTIN, 1 hit
PROSITEiView protein in PROSITE
PS00406 ACTINS_1, 1 hit
PS00432 ACTINS_2, 1 hit
PS01132 ACTINS_ACT_LIKE, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiACTB_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P60709
Secondary accession number(s): P02570
, P70514, P99021, Q11211, Q64316, Q75MN2, Q96B34, Q96HG5
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: April 1, 1988
Last modified: December 5, 2018
This is version 177 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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