Q5R6G0 · ACTB_PONAB
- ProteinActin, cytoplasmic 1
- GeneACTB
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids375 (go to sequence)
- Protein existenceEvidence at transcript 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. 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. 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
- EC number
- Alternative names
- Cleaved into 1 chains
Gene names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Pongo
Accessions
- Primary accessionQ5R6G0
- Secondary accessions
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs.
Keywords
- Cellular component
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_0000291871 | 1-375 | Actin, cytoplasmic 1 | |||
Sequence: MDDDIAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVTHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSYELPDGQVITIGNERFRCPEALFQPSFLGMESCGIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF | ||||||
Modified residue | 2 | N-acetylaspartate; in Actin, cytoplasmic 1, N-terminally processed | ||||
Sequence: D | ||||||
Chain | PRO_0000367079 | 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
Actin, cytoplasmic 1
N-terminal cleavage of acetylated methionine of immature cytoplasmic actin by ACTMAP.
ISGylated.
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.
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.
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.
Methylated at His-73 by SETD3 (By similarity).
Methylation at His-73 is required for smooth muscle contraction of the laboring uterus during delivery (By similarity).
Methylation at His-73 is required for smooth muscle contraction of the laboring uterus during delivery (By similarity).
Keywords
- PTM
Interaction
Subunit
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 PFN1. Interacts with XPO6 and EMD. Interacts with ERBB2. Interacts with GCSAM (By similarity).
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. Interacts with FAM107A (By similarity).
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 (By similarity).
Interacts with AMOTL2 (via N-terminus), the interaction facilitates binding of cell junction complexes to actin fibers in endothelial cells (By similarity).
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. Interacts with FAM107A (By similarity).
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 (By similarity).
Interacts with AMOTL2 (via N-terminus), the interaction facilitates binding of cell junction complexes to actin fibers in endothelial cells (By similarity).
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length375
- Mass (Da)41,737
- Last updated2004-12-21 v1
- Checksum6AFD05CA94E360E2
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 288 | in Ref. 1; CAH93084 | ||||
Sequence: D → N |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CR860530 EMBL· GenBank· DDBJ | CAH92656.1 EMBL· GenBank· DDBJ | mRNA | ||
CR860982 EMBL· GenBank· DDBJ | CAH93084.1 EMBL· GenBank· DDBJ | mRNA |