<unk>  is composed of a multidomain structure that is able to bind to chromatin and act as a<unk>  of gene transcription. The specific makeup of<unk>  includes a caspase activation and recruitment domain (CARD), nuclear localization signal (NLS), SAND domain, and two plant-homeodomain (PHD) fingers. The SAND domain is located in the middle of the amino-acid chain (aa 180-280) and mediates the binding of<unk>  to phosphate groups of DNA. Another potential role for this domain is to anchor<unk>  to heterologous proteins. The two cysteine-rich PHD finger domains at the C-terminus of<unk>  are PHD1 (aa 299-340) and PHD2 (aa 434-475) which are separated by a proline-rich region of amino acids. These finger domains serve to read chromatin marks through the degree of methylation at the tail of histone H3. More specifically, PHD1 is able to recognize unmethylation at the H3 tail as an epigenetic mark. An integral characteristic of<unk>  is its ability to homomerize into dimers and trimers which allows it to bind to specific oligonucleotide motifs. This property comes from the homogeneously staining region (HSR) located at the N-terminus. Because of the α-helical four-helix bundle structure, HSR’s are sensitive to conformational changes of the gene. Variants and deletions involving this domain cause an inability to activate gene transcription by preventing oligomer formation and can result in APS-1.
Autoimmune regulator
Inflammatory cytokine
Lymphokine
Tumor antigen
Cytokine
Bacterial adhesin
Autoantibody
Microantibody