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UniProtKB - P60710 (ACTB_MOUSE)

Entry version 167 (16 Oct 2019)
Sequence version 1 (01 Apr 1988)
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Protein

Actin, cytoplasmic 1

Gene

Actb

Organism
Mus musculus (Mouse)
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 (By similarity). Actin exists in both monomeric (G-actin) and polymeric (F-actin) forms, both forms playing key functions, such as cell motility and contraction (By similarity). 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:23558171, PubMed:25759381).By similarity2 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

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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

More...Reactomei		R-MMU-190873 Gap junction degradation
R-MMU-196025 Formation of annular gap junctions
R-MMU-2029482 Regulation of actin dynamics for phagocytic cup formation
R-MMU-3928662 EPHB-mediated forward signaling
R-MMU-418990 Adherens junctions interactions
R-MMU-437239 Recycling pathway of L1
R-MMU-4420097 VEGFA-VEGFR2 Pathway
R-MMU-445095 Interaction between L1 and Ankyrins
R-MMU-446353 Cell-extracellular matrix interactions
R-MMU-5250924 B-WICH complex positively regulates rRNA expression
R-MMU-5626467 RHO GTPases activate IQGAPs
R-MMU-5663213 RHO GTPases Activate WASPs and WAVEs
R-MMU-5663220 RHO GTPases Activate Formins
R-MMU-5674135 MAP2K and MAPK activation
R-MMU-5689603 UCH proteinases
R-MMU-5696394 DNA Damage Recognition in GG-NER
R-MMU-8856828 Clathrin-mediated endocytosis

<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:
Actin, cytoplasmic 1, N-terminally processed
<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>OrganismiMus musculus (Mouse)
<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 identifieri10090 [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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
<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
  • UP000000589 <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 5

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...MGIi		MGI:87904 Actb

<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 & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

<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_00003670761 – 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; alternate1 Publication
ChainiPRO_00000007752 – 375Actin, cytoplasmic 1, N-terminally processedAdd 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-acetylmethionineBy similarity1
Modified residuei2N-acetylaspartate; in Actin, cytoplasmic 1, N-terminally processed1 Publication1
Modified residuei44Methionine (R)-sulfoxide1 Publication1
Modified residuei47Methionine (R)-sulfoxide1 Publication1
Modified residuei73Tele-methylhistidine2 Publications1
Modified residuei84N6-methyllysineBy similarity1

<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 (PubMed:23911929). MICAL1 and MICAL2 produce the (R)-S-oxide form. The (R)-S-oxide form is reverted by MSRB1 and MSRB2, which promote actin repolymerization (PubMed:23911929).1 Publication
Monomethylation at Lys-84 (K84me1) regulates actin-myosin interaction and actomyosin-dependent processes. Demethylation by ALKBH4 is required for maintaining actomyosin dynamics supporting normal cleavage furrow ingression during cytokinesis and cell migration.By similarity
Methylated at His-73 by SETD3 (PubMed:30626964). Methylation at His-73 is required for smooth muscle contraction of the laboring uterus during delivery (PubMed:30626964).1 Publication
Actin, cytoplasmic 1, N-terminally processed: N-terminal acetylation by NAA80 affects actin filament depolymerization and elongation, including elongation driven by formins. In contrast, filament nucleation by the Arp2/3 complex is not affected.By similarity

Keywords - PTMi

Acetylation, Methylation, Oxidation, Ubl conjugation

Proteomic databases

The CPTAC Assay portal

More...CPTACi		non-CPTAC-3542

Encyclopedia of Proteome Dynamics

More...EPDi		P60710

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P60710

MaxQB - The MaxQuant DataBase

More...MaxQBi		P60710

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

More...PaxDbi		P60710

PeptideAtlas

More...PeptideAtlasi		P60710

PRoteomics IDEntifications database

More...PRIDEi		P60710

Consortium for Top Down Proteomics

More...TopDownProteomicsi		P60710

2D gel databases

2-DE database at Universidad Complutense de Madrid

More...COMPLUYEAST-2DPAGEi		P60710

REPRODUCTION-2DPAGE

More...REPRODUCTION-2DPAGEi		P60710

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

More...SWISS-2DPAGEi		P99041

University College Dublin 2-DE Proteome Database

More...UCD-2DPAGEi		P60710

PTM databases

CarbonylDB database of protein carbonylation sites

More...CarbonylDBi		P60710

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P60710

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

More...PhosphoSitePlusi		P60710

SwissPalm database of S-palmitoylation events

More...SwissPalmi		P60710

<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

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed in the epididymis (at protein level).1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSMUSG00000029580 Expressed in 312 organ(s), highest expression level in male reproductive system

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P60710 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P60710 MM

<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:25759381). Each actin can bind to 4 others (By similarity).

Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs (By similarity).

Component of the BAF complex, which includes at least actin (ACTB), ARID1A, ARID1B/BAF250, SMARCA2, SMARCA4/BRG1, MARCB1/BAF47, 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 (By similarity). In muscle cells, the BAF complex also contains DPF3 (By similarity).

Found in a complex with XPO6, Ran, ACTB and PFN1 (By similarity).

Component of a complex composed at least of ACTB, AP2M1, AP2A1, AP2A2, MEGF10 and VIM (By similarity).

Interacts with XPO6 and EMD (By similarity).

Interacts with ERBB2 (By similarity).

Interacts with GCSAM (By similarity).

Interacts with CPNE1 (via VWFA domain) and CPNE4 (via VWFA domain) (PubMed:12522145).

Interacts with TBC1D21 (PubMed:21128978).

Interacts with DHX9 (via C-terminus); this interaction is direct and mediates the attachment to nuclear ribonucleoprotein complexes (By similarity).

Interacts with FAM107A (PubMed:21969592).

By similarity4 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

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		197944, 218 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-1232 SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA2 variant
CPX-1233 SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA4 variant
CPX-1234 SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA2 variant
CPX-1235 SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA4 variant
CPX-1236 SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA2 variant
CPX-1237 SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA4 variant
CPX-1238 SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA2 variant
CPX-1239 SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA4 variant
CPX-1240 Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA2 variant
CPX-1241 Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA4 variant
CPX-1242 Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA2 variant
CPX-1243 Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA4 variant
CPX-1244 Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA2 variant
CPX-1245 Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA4 variant
CPX-1246 Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA2 variant
CPX-1247 Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA4 variant
CPX-1248 Polybromo-associated SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A variant
CPX-1250 Polybromo-associated SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B variant
CPX-1251 Embryonic stem cell-specific SWI/SNF ATP-dependent chromatin remodeling complex
CPX-1252 Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA2 variant
CPX-1253 Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA4 variant
CPX-1254 Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA2 variant
CPX-1255 Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA4 variant
CPX-1256 Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA2 variant
CPX-1257 Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA4 variant
CPX-1258 Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA2 variant
CPX-1259 Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA4 variant
CPX-1261 Brain-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA2 variant
CPX-1262 Brain-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA4 variant
CPX-1263 Brain-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA2 variant
CPX-1264 Brain-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA4 variant
CPX-4202 GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6A-BICRA-SMARCA2 variant
CPX-4204 GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6A-BICRAL-SMARCA2 variant
CPX-4221 GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6A-BICRA-SMARCA4 variant
CPX-4222 GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6A-BICRAL-SMARCA4 variant
CPX-4227 GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6B-BICRA-SMARCA2 variant
CPX-4228 GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6B-BICRAL-SMARCA2 variant
CPX-4229 GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6B-BICRA-SMARCA4 variant
CPX-4230 GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6B-BICRAL-SMARCA4 variant
CPX-990 NuA4 histone acetyltransferase complex

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		P60710

Database of interacting proteins

More...DIPi		DIP-31574N

Protein interaction database and analysis system

More...IntActi		P60710, 227 interactors

Molecular INTeraction database

More...MINTi		P60710

STRING: functional protein association networks

More...STRINGi		10090.ENSMUSP00000098066

<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

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

More...SMRi		P60710

Database of comparative protein structure models

More...ModBasei		Search...

<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

More...eggNOGi		KOG0676 Eukaryota
COG5277 LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00950000182960

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P60710

KEGG Orthology (KO)

More...KOi		K05692

Identification of Orthologs from Complete Genome Data

More...OMAi		MIGKESE

Database of Orthologous Groups

More...OrthoDBi		649708at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P60710

TreeFam database of animal gene trees

More...TreeFami		TF354237

Family and domain databases

Integrated resource of protein families, domains and functional sites

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

The PANTHER Classification System

More...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>. The information is filed in different subsections. The current subsections and their content are listed below:<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 4 potential isoforms that are computationally mapped.Show allAlign All

P60710-1 [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 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
E9Q5F4E9Q5F4_MOUSE
Actin, cytoplasmic 1
Actb
265Annotation 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>
E9Q1F2E9Q1F2_MOUSE
Actin, cytoplasmic 1
Actb
295Annotation 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>
E9Q606E9Q606_MOUSE
Actin, cytoplasmic 1
Actb
150Annotation 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>
E9Q2D1E9Q2D1_MOUSE
Actin, cytoplasmic 1
Actb
108Annotation 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 conflicti38P → S in CAA27396 (PubMed:3084797).Curated1
Sequence conflicti38P → S in AAA37144 (PubMed:3084797).Curated1
Sequence conflicti52S → F in BAE39957 (PubMed:16141072).Curated1
Sequence conflicti80D → E in BAE35572 (PubMed:16141072).Curated1
Sequence conflicti109P → T in BAE39957 (PubMed:16141072).Curated1
Sequence conflicti156G → R in BAE39957 (PubMed:16141072).Curated1
Sequence conflicti178L → V in BAE39957 (PubMed:16141072).Curated1

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
X03672 mRNA Translation: CAA27307.1
AK088691 mRNA Translation: BAC40507.1
AK145191 mRNA Translation: BAE26283.1
AK145196 mRNA Translation: BAE26288.1
AK145308 mRNA Translation: BAE26359.1
AK150711 mRNA Translation: BAE29789.1
AK150879 mRNA Translation: BAE29928.1
AK151010 mRNA Translation: BAE30031.1
AK151136 mRNA Translation: BAE30144.1
AK151145 mRNA Translation: BAE30152.1
AK151159 mRNA Translation: BAE30164.1
AK151166 mRNA Translation: BAE30169.1
AK151190 mRNA Translation: BAE30187.1
AK151202 mRNA Translation: BAE30199.1
AK151226 mRNA Translation: BAE30218.1
AK151277 mRNA Translation: BAE30264.1
AK151350 mRNA Translation: BAE30326.1
AK151398 mRNA Translation: BAE30366.1
AK151995 mRNA Translation: BAE30859.1
AK151999 mRNA Translation: BAE30863.1
AK152615 mRNA Translation: BAE31359.1
AK152651 mRNA Translation: BAE31388.1
AK152844 mRNA Translation: BAE31537.1
AK159759 mRNA Translation: BAE35350.1
AK159834 mRNA Translation: BAE35412.1
AK160029 mRNA Translation: BAE35572.1
AK166349 mRNA Translation: BAE38723.1
AK166498 mRNA Translation: BAE38810.1
AK167117 mRNA Translation: BAE39265.1
AK167960 mRNA Translation: BAE39957.1
X03765 mRNA Translation: CAA27396.1
M12481 mRNA Translation: AAA37144.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS19833.1

Protein sequence database of the Protein Information Resource

More...PIRi		A39104 ATMSB

NCBI Reference Sequences

More...RefSeqi		NP_031419.1, NM_007393.5

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSMUST00000100497; ENSMUSP00000098066; ENSMUSG00000029580

Database of genes from NCBI RefSeq genomes

More...GeneIDi		11461

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		mmu:11461

UCSC genome browser

More...UCSCi		uc009ajk.1 mouse

<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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03672 mRNA Translation: CAA27307.1
AK088691 mRNA Translation: BAC40507.1
AK145191 mRNA Translation: BAE26283.1
AK145196 mRNA Translation: BAE26288.1
AK145308 mRNA Translation: BAE26359.1
AK150711 mRNA Translation: BAE29789.1
AK150879 mRNA Translation: BAE29928.1
AK151010 mRNA Translation: BAE30031.1
AK151136 mRNA Translation: BAE30144.1
AK151145 mRNA Translation: BAE30152.1
AK151159 mRNA Translation: BAE30164.1
AK151166 mRNA Translation: BAE30169.1
AK151190 mRNA Translation: BAE30187.1
AK151202 mRNA Translation: BAE30199.1
AK151226 mRNA Translation: BAE30218.1
AK151277 mRNA Translation: BAE30264.1
AK151350 mRNA Translation: BAE30326.1
AK151398 mRNA Translation: BAE30366.1
AK151995 mRNA Translation: BAE30859.1
AK151999 mRNA Translation: BAE30863.1
AK152615 mRNA Translation: BAE31359.1
AK152651 mRNA Translation: BAE31388.1
AK152844 mRNA Translation: BAE31537.1
AK159759 mRNA Translation: BAE35350.1
AK159834 mRNA Translation: BAE35412.1
AK160029 mRNA Translation: BAE35572.1
AK166349 mRNA Translation: BAE38723.1
AK166498 mRNA Translation: BAE38810.1
AK167117 mRNA Translation: BAE39265.1
AK167960 mRNA Translation: BAE39957.1
X03765 mRNA Translation: CAA27396.1
M12481 mRNA Translation: AAA37144.1
CCDSiCCDS19833.1
PIRiA39104 ATMSB
RefSeqiNP_031419.1, NM_007393.5

3D structure databases

SMRiP60710
ModBaseiSearch...

Protein-protein interaction databases

BioGridi197944, 218 interactors
ComplexPortaliCPX-1232 SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA2 variant
CPX-1233 SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA4 variant
CPX-1234 SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA2 variant
CPX-1235 SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA4 variant
CPX-1236 SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA2 variant
CPX-1237 SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA4 variant
CPX-1238 SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA2 variant
CPX-1239 SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA4 variant
CPX-1240 Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA2 variant
CPX-1241 Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA4 variant
CPX-1242 Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA2 variant
CPX-1243 Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA4 variant
CPX-1244 Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA2 variant
CPX-1245 Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA4 variant
CPX-1246 Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA2 variant
CPX-1247 Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA4 variant
CPX-1248 Polybromo-associated SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A variant
CPX-1250 Polybromo-associated SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B variant
CPX-1251 Embryonic stem cell-specific SWI/SNF ATP-dependent chromatin remodeling complex
CPX-1252 Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA2 variant
CPX-1253 Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA4 variant
CPX-1254 Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA2 variant
CPX-1255 Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA4 variant
CPX-1256 Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA2 variant
CPX-1257 Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA4 variant
CPX-1258 Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA2 variant
CPX-1259 Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA4 variant
CPX-1261 Brain-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA2 variant
CPX-1262 Brain-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA4 variant
CPX-1263 Brain-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA2 variant
CPX-1264 Brain-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA4 variant
CPX-4202 GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6A-BICRA-SMARCA2 variant
CPX-4204 GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6A-BICRAL-SMARCA2 variant
CPX-4221 GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6A-BICRA-SMARCA4 variant
CPX-4222 GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6A-BICRAL-SMARCA4 variant
CPX-4227 GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6B-BICRA-SMARCA2 variant
CPX-4228 GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6B-BICRAL-SMARCA2 variant
CPX-4229 GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6B-BICRA-SMARCA4 variant
CPX-4230 GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6B-BICRAL-SMARCA4 variant
CPX-990 NuA4 histone acetyltransferase complex
CORUMiP60710
DIPiDIP-31574N
IntActiP60710, 227 interactors
MINTiP60710
STRINGi10090.ENSMUSP00000098066

PTM databases

CarbonylDBiP60710
iPTMnetiP60710
PhosphoSitePlusiP60710
SwissPalmiP60710

2D gel databases

COMPLUYEAST-2DPAGEiP60710
REPRODUCTION-2DPAGEiP60710
SWISS-2DPAGEiP99041
UCD-2DPAGEiP60710

Proteomic databases

CPTACinon-CPTAC-3542
EPDiP60710
jPOSTiP60710
MaxQBiP60710
PaxDbiP60710
PeptideAtlasiP60710
PRIDEiP60710
TopDownProteomicsiP60710

Genome annotation databases

EnsembliENSMUST00000100497; ENSMUSP00000098066; ENSMUSG00000029580
GeneIDi11461
KEGGimmu:11461
UCSCiuc009ajk.1 mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		60
MGIiMGI:87904 Actb

Phylogenomic databases

eggNOGiKOG0676 Eukaryota
COG5277 LUCA
GeneTreeiENSGT00950000182960
InParanoidiP60710
KOiK05692
OMAiMIGKESE
OrthoDBi649708at2759
PhylomeDBiP60710
TreeFamiTF354237

Enzyme and pathway databases

ReactomeiR-MMU-190873 Gap junction degradation
R-MMU-196025 Formation of annular gap junctions
R-MMU-2029482 Regulation of actin dynamics for phagocytic cup formation
R-MMU-3928662 EPHB-mediated forward signaling
R-MMU-418990 Adherens junctions interactions
R-MMU-437239 Recycling pathway of L1
R-MMU-4420097 VEGFA-VEGFR2 Pathway
R-MMU-445095 Interaction between L1 and Ankyrins
R-MMU-446353 Cell-extracellular matrix interactions
R-MMU-5250924 B-WICH complex positively regulates rRNA expression
R-MMU-5626467 RHO GTPases activate IQGAPs
R-MMU-5663213 RHO GTPases Activate WASPs and WAVEs
R-MMU-5663220 RHO GTPases Activate Formins
R-MMU-5674135 MAP2K and MAPK activation
R-MMU-5689603 UCH proteinases
R-MMU-5696394 DNA Damage Recognition in GG-NER
R-MMU-8856828 Clathrin-mediated endocytosis

Miscellaneous databases

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

More...ChiTaRSi		Actb mouse

Protein Ontology

More...PROi		PR:P60710

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSMUSG00000029580 Expressed in 312 organ(s), highest expression level in male reproductive system
ExpressionAtlasiP60710 baseline and differential
GenevisibleiP60710 MM

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...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		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_MOUSE
<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: P60710
Secondary accession number(s): P02570
, P70514, P99021, Q11211, Q3TI89, Q3TVP6, Q64316, Q6ZWM3
<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: October 16, 2019
This is version 167 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

<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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
UniProt is an ELIXIR core data resource
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