FABDF-actin binding domain (FABD)
|SMART accession number:||SM00808|
|Description:||FABD is the F-actin binding domain of Bcr-Abl and its cellular counterpart c-Abl. The Bcr-Abl tyrosine kinase causes different forms of leukemia in humans. Depending on its position within the cell, Bcr-Abl differentially affects cellular growth. The FABD forms a compact left-handed four-helix bundle in solution.|
|Interpro abstract (IPR015015):|
The F-actin binding domain forms a compact bundle of four antiparallel alpha-helices, which are arranged in a left-handed topology. Binding of F-actin to the F-actin binding domain may result in cytoplasmic retention and subcellular distribution of the protein, as well as possible inhibition of protein function [(PUBMED:16109371)]. Proteins containing this domain include tyrosine-protein kinases Abl1, which is a non-receptor tyrosine-protein kinase that plays a role in many key processes linked to cell growth and survival such as cytoskeleton remodeling in response to extracellular stimuli, cell motility and adhesion, receptor endocytosis, autophagy, DNA damage response and apoptosis [(PUBMED:9037071), (PUBMED:11971963)]. Abl1 is linked to different forms of leukemia in humans.
|GO process:||protein phosphorylation (GO:0006468)|
|GO function:||non-membrane spanning protein tyrosine kinase activity (GO:0004715), ATP binding (GO:0005524)|
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