background:
Actin filament associated protein (AFAP-110) interacts directly with actin filaments through its SLCterminal actin-binding domain. AFAP-110 contains additional protein-binding domains as well, and serves as an adaptor protein. By linking signaling molecules to actin filaments, AFAP-110 provides a platform for the preparation of larger signaling complexes, activates Src kinases in response to cellular signals and also directly affects Actin organization as an Actin filament cross-linking protein. AFAP-1L2 (Actin filament-associated protein 1-like 2), also known as XB130, is a 818 amino acid cytoplasmic protein that contains two Pleckstrin homology (PH) domains, which are normally found in proteins involved in intracellular signaling. Like its relative AFAP110, AFAP-1L2 interacts with Src kinase and may play a role in Src-regulated transcription activation. AFAP-1L2 is expressed in thyroid and spleen and can also be detected at lower levels in lung, brain, pancreas and kidney. There are four isoforms of AFAP-1L2 that are produced as a result of alternative splicing events.
Function:
May play a role in a signaling cascade by enhancing the kinase activity of SRC. Contributes to SRSLCregulated transcription activation.
Subunit:
Interacts with SRC. Interacts with LCK when tyrosine phosphorylated.
Subcellular Location:
Cytoplasm.
Tissue Specificity:
Detected in spleen and thyroid, and at lower levels in kidney, brain, lung and pancreas.
Post-translational modifications:
Tyrosine phosphorylated (by SRC).
Similarity:
Contains 2 PH domains.
Database links:
NCBI Reference Sequence: NP_001001936 UniProtKB/Swiss-Prot: Q8N4X5
Important Note:
This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications.
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