TWF2

The protein encoded by this gene was identified by its interaction with the catalytic domain of protein kinase C-zeta. The encoded protein contains an actin-binding site and an ATP-binding site. It is most closely related to twinfilin (PTK9), a conserved actin monomer-binding protein. [provided by RefSeq, Jul 2008]

TWF2 Gene(Protein Coding) Twinfilin Actin Binding Protein 2

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).

Biological Process actin filament depolymerization Source:GO_Central1 Publication
Biological Process barbed-end actin filament capping Source:BHF-UCLBy Similarity
Biological Process cell projection organization Source:UniProtKB-KW
Biological Process cellular response to growth factor stimulus Source:BHF-UCL1 Publication
Biological Process cellular response to retinoic acid Source:BHF-UCL1 Publication
Biological Process negative regulation of actin filament polymerization Source:BHF-UCLBy Similarity
Biological Process positive regulation of axon extension Source:BHF-UCL1 Publication
Biological Process positive regulation of lamellipodium assembly Source:BHF-UCL1 Publication
Biological Process positive regulation of neuron projection development Source:BHF-UCL1 Publication
Biological Process regulation of actin cytoskeleton organization Source:BHF-UCL1 Publication
Biological Process regulation of lamellipodium assembly Source:GO_Central1 Publication
Biological Process regulation of microvillus length Source:BHF-UCL1 Publication
Biological Process sequestering of actin monomers Source:BHF-UCLBy Similarity

Cytoplasm, cytoskeleton
Cytoplasm, perinuclear region
Cell projection, stereocilium
Perinuclear and G-actin-rich cortical actin structure sublocalization.

In vitro, phosphorylated by PRKCZ, CK2 and SRC.