Search Results
Overview
| Uniprot ID | O15145 |
|---|---|
| Protein Name | Actin-related protein 2/3 complex subunit 3 |
| Gene Name | ARPC3 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 158 | PQNDKPSKWWTCFVK |
| 165 | KWWTCFVKRQFMNKS |
| 29 | LPIRSQFKGPAPRET |
| 61 | FFKNYEIKNEADRTL |
Function
Component of the Arp2/3 complex, a multiprotein complex that mediates actin polymerization upon stimulation by nucleation-promoting factor (NPF) (PubMed:9230079). The Arp2/3 complex mediates the formation of branched actin networks in the cytoplasm, providing the force for cell motility (PubMed:9230079). In addition to its role in the cytoplasmic cytoskeleton, the Arp2/3 complex also promotes actin polymerization in the nucleus, thereby regulating gene transcription and repair of damaged DNA (PubMed:29925947). The Arp2/3 complex promotes homologous recombination (HR) repair in response to DNA damage by promoting nuclear actin polymerization, leading to drive motility of double-strand breaks (DSBs) (PubMed:29925947)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0015629 | actin cytoskeleton |
| Cellular Component | GO:0005885 | Arp2/3 protein complex |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0070062 | extracellular exosome |
| Cellular Component | GO:0005925 | focal adhesion |
| Cellular Component | GO:0030027 | lamellipodium |
| Cellular Component | GO:0016020 | membrane |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0035861 | site of double-strand break |
| Molecular Function | GO:0003779 | actin binding |
| Molecular Function | GO:0005200 | structural constituent of cytoskeleton |
| Biological Process | GO:0070358 | actin polymerization-dependent cell motility |
| Biological Process | GO:0034314 | Arp2/3 complex-mediated actin nucleation |
| Biological Process | GO:0030833 | regulation of actin filament polymerization |
| Biological Process | GO:1900242 | regulation of synaptic vesicle endocytosis |
Reference
[1] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.
[2] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.