Search Results
Overview
| Uniprot ID | P42768 |
|---|---|
| Protein Name | Actin nucleation-promoting factor WAS |
| Gene Name | WAS |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 235 | SGKKKISKADIGAPS |
Function
Effector protein for Rho-type GTPases that regulates actin filament reorganization via its interaction with the Arp2/3 complex (PubMed:12235133, PubMed:12769847, PubMed:16275905). Important for efficient actin polymerization (PubMed:12235133, PubMed:16275905, PubMed:8625410). Possible regulator of lymphocyte and platelet function (PubMed:9405671). Mediates actin filament reorganization and the formation of actin pedestals upon infection by pathogenic bacteria (PubMed:18650809). In addition to its role in the cytoplasmic cytoskeleton, also promotes actin polymerization in the nucleus, thereby regulating gene transcription and repair of damaged DNA (PubMed:20574068). 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:0005884 | actin filament |
| Cellular Component | GO:0005911 | cell-cell junction |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0070062 | extracellular exosome |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0045335 | phagocytic vesicle |
| Cellular Component | GO:0035861 | site of double-strand break |
| Cellular Component | GO:0012506 | vesicle membrane |
| Molecular Function | GO:0003779 | actin binding |
| Molecular Function | GO:0030695 | GTPase regulator activity |
| Molecular Function | GO:0042802 | identical protein binding |
| Molecular Function | GO:0043274 | phospholipase binding |
| Molecular Function | GO:0019901 | protein kinase binding |
| Molecular Function | GO:0017124 | SH3 domain binding |
| Molecular Function | GO:0031267 | small GTPase binding |
| Biological Process | GO:0030041 | actin filament polymerization |
| Biological Process | GO:0008154 | actin polymerization or depolymerization |
| Biological Process | GO:0007596 | blood coagulation |
| Biological Process | GO:0032488 | Cdc42 protein signal transduction |
| Biological Process | GO:0006952 | defense response |
| Biological Process | GO:0008544 | epidermis development |
| Biological Process | GO:0006955 | immune response |
| Biological Process | GO:2000146 | negative regulation of cell motility |
| Biological Process | GO:0051497 | negative regulation of stress fiber assembly |
| Biological Process | GO:1905168 | positive regulation of double-strand break repair via homologous recombination |
| Biological Process | GO:0045944 | positive regulation of transcription by RNA polymerase II |
| Biological Process | GO:0065003 | protein-containing complex assembly |
| Biological Process | GO:0008064 | regulation of actin polymerization or depolymerization |
| Biological Process | GO:0010591 | regulation of lamellipodium assembly |
| Biological Process | GO:0051492 | regulation of stress fiber assembly |
| Biological Process | GO:0002625 | regulation of T cell antigen processing and presentation |
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] Guo X, Ren X, Yan C, Huang H. Quantitative Proteomics Reveals the Role of Lysine Lactylation in Lenalidomide-Resistance in Multiple Myeloma Cells.. ACS Chem Biol 20(7):1728-1738. 2025 Jul 18. PMID: 40590393.