Q0PGG4 · ACTB_BOSMU

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

GO annotations

AspectTerm
Cellular Componentactin cytoskeleton
Cellular Componentcytoskeleton
Cellular Componentdense body
Cellular Componentfocal adhesion
Cellular Componentnucleus
Cellular Componentplasma membrane
Cellular Componentprotein-containing complex
Molecular FunctionATP binding
Molecular Functionhydrolase activity

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

Gene names

    • Name
      ACTB

Organism names

Accessions

  • Primary accession
    Q0PGG4

Proteomes

Subcellular Location

Nucleus
Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs.

Keywords

PTM/Processing

Features

Showing features for initiator methionine, modified residue, chain.

TypeIDPosition(s)Description
Initiator methionine1Removed; alternate
Modified residue1N-acetylmethionine
ChainPRO_00002534871-375Actin, cytoplasmic 1
Modified residue2N-acetylaspartate; in Actin, cytoplasmic 1, N-terminally processed
ChainPRO_00003670652-375Actin, cytoplasmic 1, N-terminally processed
Modified residue44Methionine (R)-sulfoxide
Modified residue47Methionine (R)-sulfoxide
Modified residue73Tele-methylhistidine
Modified residue84N6-methyllysine

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).

Keywords

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).

Structure

Family & Domains

Sequence similarities

Belongs to the actin family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    375
  • Mass (Da)
    41,749
  • Last updated
    2006-09-05 v1
  • Checksum
    96C2267932D952C2
MDDDIAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPEANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVTHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMAIAASSSSLEKSYELPDGQVITIGNERFRCPEALFQPSFLGMESCGIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIANRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
DQ838049
EMBL· GenBank· DDBJ
ABH06561.1
EMBL· GenBank· DDBJ
mRNA

Similar Proteins

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