| Post Translational Modifications | Oxidation of Met-46 and Met-49 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 promotes actin repolymerization. Monomethylation at Lys-86 (K86me1) 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, alpha cardiac muscle 1, intermediate form: N-terminal cleavage of acetylated cysteine of intermediate muscle actin by ACTMAP. Methylated at His-75 by SETD3. (Microbial infection) Monomeric actin is cross-linked by V.cholerae toxins RtxA and VgrG1 in case of infection: bacterial toxins mediate the cross-link between Lys-52 of one monomer and Glu-272 of another actin monomer, resulting in formation of highly toxic actin oligomers that cause cell rounding. The toxin can be highly efficient at very low concentrations by acting on formin homology family proteins: toxic actin oligomers bind with high affinity to formins and adversely affect both nucleation and elongation abilities of formins, causing their potent inhibition in both profilin-dependent and independent manners. |
| Function | Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. |
| Protein Name | Actin - Alpha Cardiac Muscle 1Alpha-Cardiac Actin Cleaved Into - Actin - Alpha Cardiac Muscle 1 - Intermediate Form |
| Database Links | Reactome: R-HSA-390522Reactome: R-HSA-8980692Reactome: R-HSA-9013026Reactome: R-HSA-9913351 |
| Cellular Localisation | CytoplasmCytoskeleton |
| Alternative Antibody Names | Anti-Actin - Alpha Cardiac Muscle 1 antibodyAnti-Alpha-Cardiac Actin Cleaved Into - Actin - Alpha Cardiac Muscle 1 - Intermediate Form antibodyAnti-ACTC1 antibodyAnti-ACTC antibody |
Information sourced from Uniprot.org
