Search Results
Overview
| Uniprot ID | P61158 |
|---|---|
| Protein Name | Actin-related protein 3 |
| Gene Name | ACTR3 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 240 | YVCPDLVKEFNKYDT |
| 251 | KYDTDGSKWIKQYTG |
| 254 | TDGSKWIKQYTGINA |
| 264 | TGINAISKKEFSIDV |
| 265 | GINAISKKEFSIDVG |
| 361 | SGGRLKPKPIDVQVI |
| 398 | YQVCHTKKDYEEIGP |
| 42 | IAIKESAKVGDQAQR |
Function
ATP-binding component of the Arp2/3 complex, a multiprotein complex that mediates actin polymerization upon stimulation by nucleation-promoting factor (NPF) (PubMed:9000076). The Arp2/3 complex mediates the formation of branched actin networks in the cytoplasm, providing the force for cell motility (PubMed:9000076). Seems to contact the pointed end of the daughter actin filament (PubMed:9000076). In podocytes, required for the formation of lamellipodia downstream of AVIL and PLCE1 regulation (PubMed:29058690). 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:17220302, 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). Plays a role in ciliogenesis (PubMed:20393563)
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:0005903 | brush border |
| Cellular Component | GO:0005911 | cell-cell junction |
| Cellular Component | GO:0005737 | cytoplasm |
| 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:0005524 | ATP 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:0060271 | cilium assembly |
| Biological Process | GO:0010592 | positive regulation of lamellipodium assembly |
| Biological Process | GO:0045944 | positive regulation of transcription by RNA polymerase II |
Reference
[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.
[2] 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.
[3] Yang YH, Wang QC, Kong J, Yang JT, Liu JF. Global profiling of lysine lactylation in human lungs.. Proteomics 23(15):e2200437. 2023 Aug. PMID: 37170646.
[4] Chao L, Xu Y, Yang Y, Ao X, Liang J. Identification of lactylation-related biomarkers for diagnosis, prognosis, and treatment responsiveness in triple-negative breast cancer.. World J Surg Oncol 24(1):77. 2026 Jan 22. PMID: 41566505.
[5] 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.