Search Results
Overview
| Uniprot ID | Q6IBS0 |
|---|---|
| Protein Name | Twinfilin-2 |
| Gene Name | TWF2 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 171 | TEISVESKHQTLQGL |
| 194 | QRALQQLKQKMVNYI |
| 320 | HPKQHAFKQAFAKPK |
| 325 | AFKQAFAKPKGPGGK |
| 327 | KQAFAKPKGPGGKRG |
Function
Actin-binding protein involved in motile and morphological processes. Inhibits actin polymerization, likely by sequestering G-actin. By capping the barbed ends of filaments, it also regulates motility. Seems to play an important role in clathrin-mediated endocytosis and distribution of endocytic organelles. May play a role in regulating the mature length of the middle and short rows of stereocilia (By similarity)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005884 | actin filament |
| Cellular Component | GO:0070062 | extracellular exosome |
| Cellular Component | GO:0030175 | filopodium |
| Cellular Component | GO:0030426 | growth cone |
| Cellular Component | GO:0030027 | lamellipodium |
| Cellular Component | GO:0030016 | myofibril |
| Cellular Component | GO:0048471 | perinuclear region of cytoplasm |
| Cellular Component | GO:0032420 | stereocilium |
| Molecular Function | GO:0051015 | actin filament binding |
| Molecular Function | GO:0003785 | actin monomer binding |
| Molecular Function | GO:0005524 | ATP binding |
| Molecular Function | GO:0045296 | cadherin binding |
| Molecular Function | GO:0005546 | phosphatidylinositol-4,5-bisphosphate binding |
| Molecular Function | GO:0005080 | protein kinase C binding |
| Molecular Function | GO:0003723 | RNA binding |
| Biological Process | GO:0030042 | actin filament depolymerization |
| Biological Process | GO:0051016 | barbed-end actin filament capping |
| Biological Process | GO:0030030 | cell projection organization |
| Biological Process | GO:0071363 | cellular response to growth factor stimulus |
| Biological Process | GO:0071300 | cellular response to retinoic acid |
| Biological Process | GO:0030837 | negative regulation of actin filament polymerization |
| Biological Process | GO:0045773 | positive regulation of axon extension |
| Biological Process | GO:0010592 | positive regulation of lamellipodium assembly |
| Biological Process | GO:0010976 | positive regulation of neuron projection development |
| Biological Process | GO:0032956 | regulation of actin cytoskeleton organization |
| Biological Process | GO:0010591 | regulation of lamellipodium assembly |
| Biological Process | GO:0032532 | regulation of microvillus length |
| Cellular Component | GO:0005737 | cytoplasm |
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] 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.