UniProtKB - P60712 (ACTB_BOVIN)
Actin, cytoplasmic 1
ACTB
Functioni
Actin is a highly conserved protein that polymerizes to produce filaments that form cross-linked networks in the cytoplasm of cells. Actin exists in both monomeric (G-actin) and polymeric (F-actin) forms, both forms playing key functions, such as cell motility and contraction. 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.
By similarityMiscellaneous
GO - Molecular functioni
- ATP binding Source: UniProtKB-KW
- identical protein binding Source: Ensembl
- kinesin binding Source: Ensembl
- nitric-oxide synthase binding Source: Ensembl
- protein kinase binding Source: GO_Central
- structural constituent of postsynaptic actin cytoskeleton Source: GO_Central
- Tat protein binding Source: Ensembl
GO - Biological processi
- adherens junction assembly Source: Ensembl
- apical protein localization Source: Ensembl
- axonogenesis Source: GO_Central
- cell motility Source: GO_Central
- cellular response to cytochalasin B Source: Ensembl
- establishment or maintenance of cell polarity Source: Ensembl
- histone H2A acetylation Source: Ensembl
- histone H4 acetylation Source: Ensembl
- morphogenesis of a polarized epithelium Source: Ensembl
- negative regulation of protein binding Source: Ensembl
- positive regulation of double-strand break repair via homologous recombination Source: Ensembl
- protein localization to adherens junction Source: Ensembl
- regulation of cell cycle Source: Ensembl
- regulation of norepinephrine uptake Source: Ensembl
- regulation of protein localization to plasma membrane Source: Ensembl
- regulation of transepithelial transport Source: Ensembl
- regulation of transmembrane transporter activity Source: Ensembl
- synaptic vesicle endocytosis Source: Ensembl
Keywordsi
Ligand | ATP-binding, Nucleotide-binding |
Names & Taxonomyi
Protein namesi | Recommended name: Actin, cytoplasmic 1Alternative name(s): Beta-actin Cleaved into the following chain: |
Gene namesi | Name:ACTB |
Organismi | Bos taurus (Bovine) |
Taxonomic identifieri | 9913 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Artiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos |
Proteomesi |
|
Organism-specific databases
VEuPathDBi | HostDB:ENSBTAG00000026199 |
VGNCi | VGNC:106628, ACTB |
Subcellular locationi
Cytoskeleton
- cytoskeleton By similarity
Nucleus
- Nucleus By similarity
Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs.By similarity
Cytoskeleton
- actin cytoskeleton Source: UniProtKB
- actin filament Source: GO_Central
- cortical cytoskeleton Source: Ensembl
- cytoskeleton Source: AgBase
- postsynaptic actin cytoskeleton Source: Ensembl
Cytosol
- cytosol Source: Reactome
Nucleus
- NuA4 histone acetyltransferase complex Source: AgBase
- nucleus Source: UniProtKB
Plasma Membrane
- plasma membrane Source: AgBase
Other locations
- adherens junction Source: Ensembl
- apical junction complex Source: Ensembl
- axon Source: GO_Central
- calyx of Held Source: Ensembl
- cytoplasm Source: GO_Central
- cytoplasmic ribonucleoprotein granule Source: Ensembl
- dense body Source: AgBase
- focal adhesion Source: AgBase
- glutamatergic synapse Source: Ensembl
- lamellipodium Source: Ensembl
- membrane Source: GO_Central
- nucleosome Source: Ensembl
- protein-containing complex Source: UniProtKB
- ribonucleoprotein complex Source: Ensembl
- Schaffer collateral - CA1 synapse Source: Ensembl
- synapse Source: GO_Central
- tight junction Source: Ensembl
Keywords - Cellular componenti
Cytoplasm, Cytoskeleton, NucleusPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000000757 | 1 – 375 | Actin, cytoplasmic 1Add BLAST | 375 | |
Initiator methioninei | Removed; alternateBy similarity | |||
ChainiPRO_0000367066 | 2 – 375 | Actin, cytoplasmic 1, N-terminally processedAdd BLAST | 374 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 1 | N-acetylmethionineBy similarity | 1 | |
Modified residuei | 2 | N-acetylaspartate; in Actin, cytoplasmic 1, N-terminally processedBy similarity | 1 | |
Modified residuei | 44 | Methionine (R)-sulfoxideBy similarity | 1 | |
Modified residuei | 47 | Methionine (R)-sulfoxideBy similarity | 1 | |
Modified residuei | 73 | Tele-methylhistidineBy similarity | 1 | |
Modified residuei | 84 | N6-methyllysineBy similarity | 1 |
Post-translational modificationi
Keywords - PTMi
Acetylation, Methylation, Oxidation, Ubl conjugationProteomic databases
PeptideAtlasi | P60712 |
PRIDEi | P60712 |
Interactioni
Subunit structurei
Polymerization of globular actin (G-actin) leads to a structural filament (F-actin) in the form of a two-stranded helix. Each actin can bind to 4 others.
Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs.
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. In muscle cells, the BAF complex also contains DPF3.
Found in a complex with XPO6, Ran, ACTB and PFN1.
Interacts with XPO6 and EMD.
Interacts with ERBB2.
Interacts with GCSAM (By similarity).
Interacts with TBC1D21.
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.
Interacts with FAM107A (By similarity).
By similarityGO - Molecular functioni
- identical protein binding Source: Ensembl
- kinesin binding Source: Ensembl
- nitric-oxide synthase binding Source: Ensembl
- protein kinase binding Source: GO_Central
- Tat protein binding Source: Ensembl
Protein-protein interaction databases
CORUMi | P60712 |
DIPi | DIP-57682N |
IntActi | P60712, 5 interactors |
MINTi | P60712 |
STRINGi | 9913.ENSBTAP00000036739 |
Structurei
Secondary structure
3D structure databases
SMRi | P60712 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P60712 |
Family & Domainsi
Sequence similaritiesi
Phylogenomic databases
GeneTreei | ENSGT00950000182960 |
InParanoidi | P60712 |
OMAi | FHTTAER |
OrthoDBi | 649708at2759 |
Family and domain databases
InterProi | View protein in InterPro IPR004000, Actin IPR020902, Actin/actin-like_CS IPR004001, Actin_CS IPR043129, ATPase_NBD |
PANTHERi | PTHR11937, PTHR11937, 1 hit |
Pfami | View protein in Pfam PF00022, Actin, 1 hit |
PRINTSi | PR00190, ACTIN |
SMARTi | View protein in SMART SM00268, ACTIN, 1 hit |
SUPFAMi | SSF53067, SSF53067, 2 hits |
PROSITEi | View protein in PROSITE PS00406, ACTINS_1, 1 hit PS00432, ACTINS_2, 1 hit PS01132, ACTINS_ACT_LIKE, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
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
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 126 | T → A in AAI42414 (Ref. 3) Curated | 1 | |
Sequence conflicti | 204 – 206 | AER → GRA in AAM98378 (PubMed:14559974).Curated | 3 | |
Sequence conflicti | 281 | S → F in AAM98378 (PubMed:14559974).Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AY141970 mRNA Translation: AAM98378.1 BT030480 mRNA Translation: ABQ12920.1 BC102948 mRNA Translation: AAI02949.1 BC142413 mRNA Translation: AAI42414.1 K00622 mRNA Translation: AAA30352.1 K00623 mRNA Translation: AAA30353.1 |
PIRi | E14185, ATBOB |
RefSeqi | NP_776404.2, NM_173979.3 |
Genome annotation databases
Ensembli | ENSBTAT00000036888; ENSBTAP00000036739; ENSBTAG00000026199 |
GeneIDi | 280979 |
KEGGi | bta:280979 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AY141970 mRNA Translation: AAM98378.1 BT030480 mRNA Translation: ABQ12920.1 BC102948 mRNA Translation: AAI02949.1 BC142413 mRNA Translation: AAI42414.1 K00622 mRNA Translation: AAA30352.1 K00623 mRNA Translation: AAA30353.1 |
PIRi | E14185, ATBOB |
RefSeqi | NP_776404.2, NM_173979.3 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1HLU | X-ray | 2.65 | A | 2-375 | [»] | |
2BTF | X-ray | 2.55 | A | 2-375 | [»] | |
2OAN | X-ray | 2.61 | A/B/C/D | 1-375 | [»] | |
3U4L | X-ray | 2.40 | A | 1-375 | [»] | |
3UB5 | X-ray | 2.20 | A | 2-375 | [»] | |
7PDZ | electron microscopy | 3.80 | I/J/K/L/N/O | 1-375 | [»] | |
SMRi | P60712 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
CORUMi | P60712 |
DIPi | DIP-57682N |
IntActi | P60712, 5 interactors |
MINTi | P60712 |
STRINGi | 9913.ENSBTAP00000036739 |
Proteomic databases
PeptideAtlasi | P60712 |
PRIDEi | P60712 |
Genome annotation databases
Ensembli | ENSBTAT00000036888; ENSBTAP00000036739; ENSBTAG00000026199 |
GeneIDi | 280979 |
KEGGi | bta:280979 |
Organism-specific databases
CTDi | 60 |
VEuPathDBi | HostDB:ENSBTAG00000026199 |
VGNCi | VGNC:106628, ACTB |
Phylogenomic databases
GeneTreei | ENSGT00950000182960 |
InParanoidi | P60712 |
OMAi | FHTTAER |
OrthoDBi | 649708at2759 |
Miscellaneous databases
EvolutionaryTracei | P60712 |
Gene expression databases
ExpressionAtlasi | P60712, baseline and differential |
Family and domain databases
InterProi | View protein in InterPro IPR004000, Actin IPR020902, Actin/actin-like_CS IPR004001, Actin_CS IPR043129, ATPase_NBD |
PANTHERi | PTHR11937, PTHR11937, 1 hit |
Pfami | View protein in Pfam PF00022, Actin, 1 hit |
PRINTSi | PR00190, ACTIN |
SMARTi | View protein in SMART SM00268, ACTIN, 1 hit |
SUPFAMi | SSF53067, SSF53067, 2 hits |
PROSITEi | View protein in PROSITE PS00406, ACTINS_1, 1 hit PS00432, ACTINS_2, 1 hit PS01132, ACTINS_ACT_LIKE, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | ACTB_BOVIN | |
Accessioni | P60712Primary (citable) accession number: P60712 Secondary accession number(s): A5D961 Q8MIJ0 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 21, 1986 |
Last sequence update: | April 1, 1988 | |
Last modified: | February 23, 2022 | |
This is version 148 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families