P60710 · ACTB_MOUSE
- ProteinActin, cytoplasmic 1
- GeneActb
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids375 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
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).
Part of the ACTR1A/ACTB filament around which the dynactin complex is built. The dynactin multiprotein complex activates the molecular motor dynein for ultra-processive transport along microtubules (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).
Part of the ACTR1A/ACTB filament around which the dynactin complex is built. The dynactin multiprotein complex activates the molecular motor dynein for ultra-processive transport along microtubules (By similarity).
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.
Catalytic activity
- ATP + H2O = ADP + H+ + phosphate
GO annotations
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameActin, cytoplasmic 1
- Alternative names
- Cleaved into 1 chains
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionP60710
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs.
Keywords
- Cellular component
Phenotypes & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 41 variants from UniProt as well as other sources including ClinVar and dbSNP.
Chemistry
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed; alternate | ||||
Sequence: M | ||||||
Modified residue | 1 | N-acetylmethionine | ||||
Sequence: M | ||||||
Chain | PRO_0000367076 | 1-375 | Actin, cytoplasmic 1 | |||
Sequence: MDDDIAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVTHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSYELPDGQVITIGNERFRCPEALFQPSFLGMESCGIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF | ||||||
Modified residue | 2 | N-acetylaspartate; in Actin, cytoplasmic 1, N-terminally processed | ||||
Sequence: D | ||||||
Chain | PRO_0000000775 | 2-375 | Actin, cytoplasmic 1, N-terminally processed | |||
Sequence: DDDIAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVTHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSYELPDGQVITIGNERFRCPEALFQPSFLGMESCGIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF | ||||||
Modified residue | 44 | Methionine (R)-sulfoxide | ||||
Sequence: M | ||||||
Modified residue | 47 | Methionine (R)-sulfoxide | ||||
Sequence: M | ||||||
Modified residue | 73 | Tele-methylhistidine | ||||
Sequence: H | ||||||
Modified residue | 84 | N6-methyllysine | ||||
Sequence: K |
Post-translational modification
ISGylated.
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).
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).
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.
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).
Methylation at His-73 is required for smooth muscle contraction of the laboring uterus during delivery (PubMed:30626964).
Actin, cytoplasmic 1
N-terminal cleavage of acetylated methionine of immature cytoplasmic actin by ACTMAP.
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.
Keywords
- PTM
Proteomic databases
2D gel databases
PTM databases
Interaction
Subunit
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).
Interacts with 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).
Part of the ACTR1A/ACTB filament around which the dynactin complex is built. The filament contains 8 copies of ACTR1A and 1 ACTB (By similarity).
Interacts with TPRN which forms ring-like structures in the stereocilium taper region; the interaction may stabilize stereocilia in inner ear hair cells (PubMed:37952086).
Interacts with AMOTL2, the interaction facilitates binding of cell junction complexes to actin fibers in endothelial cells (PubMed:24806444).
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).
Interacts with 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).
Part of the ACTR1A/ACTB filament around which the dynactin complex is built. The filament contains 8 copies of ACTR1A and 1 ACTB (By similarity).
Interacts with TPRN which forms ring-like structures in the stereocilium taper region; the interaction may stabilize stereocilia in inner ear hair cells (PubMed:37952086).
Interacts with AMOTL2, the interaction facilitates binding of cell junction complexes to actin fibers in endothelial cells (PubMed:24806444).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P60710 | Cxadr P97792 | 6 | EBI-353957, EBI-7429264 | |
BINARY | P60710 | Trpm7 Q923J1 | 2 | EBI-353957, EBI-8010314 |
Protein-protein interaction databases
Miscellaneous
Structure
Sequence
- Sequence statusComplete
- Length375
- Mass (Da)41,737
- Last updated1988-04-01 v1
- Checksum6AFD05CA94E360E2
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 38 | in Ref. 5; CAA27396/AAA37144 | ||||
Sequence: P → S | ||||||
Sequence conflict | 52 | in Ref. 2; BAE39957 | ||||
Sequence: S → F | ||||||
Sequence conflict | 80 | in Ref. 2; BAE35572 | ||||
Sequence: D → E | ||||||
Sequence conflict | 109 | in Ref. 2; BAE39957 | ||||
Sequence: P → T | ||||||
Sequence conflict | 156 | in Ref. 2; BAE39957 | ||||
Sequence: G → R | ||||||
Sequence conflict | 178 | in Ref. 2; BAE39957 | ||||
Sequence: L → V |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X03672 EMBL· GenBank· DDBJ | CAA27307.1 EMBL· GenBank· DDBJ | mRNA | ||
AK088691 EMBL· GenBank· DDBJ | BAC40507.1 EMBL· GenBank· DDBJ | mRNA | ||
AK145191 EMBL· GenBank· DDBJ | BAE26283.1 EMBL· GenBank· DDBJ | mRNA | ||
AK145196 EMBL· GenBank· DDBJ | BAE26288.1 EMBL· GenBank· DDBJ | mRNA | ||
AK145308 EMBL· GenBank· DDBJ | BAE26359.1 EMBL· GenBank· DDBJ | mRNA | ||
AK150711 EMBL· GenBank· DDBJ | BAE29789.1 EMBL· GenBank· DDBJ | mRNA | ||
AK150879 EMBL· GenBank· DDBJ | BAE29928.1 EMBL· GenBank· DDBJ | mRNA | ||
AK151010 EMBL· GenBank· DDBJ | BAE30031.1 EMBL· GenBank· DDBJ | mRNA | ||
AK151136 EMBL· GenBank· DDBJ | BAE30144.1 EMBL· GenBank· DDBJ | mRNA | ||
AK151145 EMBL· GenBank· DDBJ | BAE30152.1 EMBL· GenBank· DDBJ | mRNA | ||
AK151159 EMBL· GenBank· DDBJ | BAE30164.1 EMBL· GenBank· DDBJ | mRNA | ||
AK151166 EMBL· GenBank· DDBJ | BAE30169.1 EMBL· GenBank· DDBJ | mRNA | ||
AK151190 EMBL· GenBank· DDBJ | BAE30187.1 EMBL· GenBank· DDBJ | mRNA | ||
AK151202 EMBL· GenBank· DDBJ | BAE30199.1 EMBL· GenBank· DDBJ | mRNA | ||
AK151226 EMBL· GenBank· DDBJ | BAE30218.1 EMBL· GenBank· DDBJ | mRNA | ||
AK151277 EMBL· GenBank· DDBJ | BAE30264.1 EMBL· GenBank· DDBJ | mRNA | ||
AK151350 EMBL· GenBank· DDBJ | BAE30326.1 EMBL· GenBank· DDBJ | mRNA | ||
AK151398 EMBL· GenBank· DDBJ | BAE30366.1 EMBL· GenBank· DDBJ | mRNA | ||
AK151995 EMBL· GenBank· DDBJ | BAE30859.1 EMBL· GenBank· DDBJ | mRNA | ||
AK151999 EMBL· GenBank· DDBJ | BAE30863.1 EMBL· GenBank· DDBJ | mRNA | ||
AK152615 EMBL· GenBank· DDBJ | BAE31359.1 EMBL· GenBank· DDBJ | mRNA | ||
AK152651 EMBL· GenBank· DDBJ | BAE31388.1 EMBL· GenBank· DDBJ | mRNA | ||
AK152844 EMBL· GenBank· DDBJ | BAE31537.1 EMBL· GenBank· DDBJ | mRNA | ||
AK159759 EMBL· GenBank· DDBJ | BAE35350.1 EMBL· GenBank· DDBJ | mRNA | ||
AK159834 EMBL· GenBank· DDBJ | BAE35412.1 EMBL· GenBank· DDBJ | mRNA | ||
AK160029 EMBL· GenBank· DDBJ | BAE35572.1 EMBL· GenBank· DDBJ | mRNA | ||
AK166349 EMBL· GenBank· DDBJ | BAE38723.1 EMBL· GenBank· DDBJ | mRNA | ||
AK166498 EMBL· GenBank· DDBJ | BAE38810.1 EMBL· GenBank· DDBJ | mRNA | ||
AK167117 EMBL· GenBank· DDBJ | BAE39265.1 EMBL· GenBank· DDBJ | mRNA | ||
AK167960 EMBL· GenBank· DDBJ | BAE39957.1 EMBL· GenBank· DDBJ | mRNA | ||
X03765 EMBL· GenBank· DDBJ | CAA27396.1 EMBL· GenBank· DDBJ | mRNA | ||
M12481 EMBL· GenBank· DDBJ | AAA37144.1 EMBL· GenBank· DDBJ | mRNA |