Interferon-inducible protein AIM2 (Absent in melanoma 2) is a 343 amino acid protein belonging to the HIN-200 family. Induced by IFN-, AIM2 is thought to act as a tumor suppressor by repressing NFB transcriptional activity. Localized to the nucleus, AIM2 contains one DAPIN domain and one HIN-200 domain. The DAPIN domain is composed mostly of -helixes and is a protein-protein interaction domain capable of binding other DAPIN domains. The HIN-200 domain has been shown to bind directly to DNA, which, along with the binding of another protein ASC, results in the activation of Caspase-1.
A synthetic peptide from human AIM2
A synthesized peptide derived from human AIMP1, corresponding to a region within the internal amino acids.
The protein encoded by this gene is a cytokine that is specifically induced by apoptosis, and it is involved in the control of angiogenesis, inflammation, and wound healing. The release of this cytokine renders the tumor-associated vasculature sensitive to tumor necrosis factor. The precursor protein is identical to the p43 subunit, which is associated with the multi-tRNA synthetase complex, and it modulates aminoacylation activity of tRNA synthetase in normal cells. This protein is also involved in the stimulation of inflammatory responses after proteolytic cleavage in tumor cells. Multiple transcript variants encoding different isoforms have been found for this gene. A pseudogene has been identified on chromosome 20.
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