SP140 Activators

SP140, also known as Nuclear Body Protein SP140, is a protein that is highly expressed in immune cells, particularly in lymphoid tissues. It belongs to a family of nuclear body proteins that include SP100, SP110, and SP140L, characterized by a shared domain structure that suggests roles in chromatin organization and transcriptional regulation. The SP140 protein contains several domains indicative of its involvement in chromatin-mediated gene regulation: a plant homeodomain (PHD) finger, a bromodomain, a SAND domain, and a Leucine-rich repeat (LRR).

The PHD finger and bromodomain are known to be important for binding to histones and reading epigenetic marks, which is essential for the regulation of gene expression. The SAND domain is implicated in DNA binding, whereas LRRs typically participate in protein-protein interactions. SP140 has been implicated in the pathogenesis of chronic lymphocytic leukemia and is associated with autoimmune diseases like multiple sclerosis. This association is likely due to its role in the regulation of genes involved in immune response and inflammation.Alterations in the SP140 gene can affect its expression and function, leading to dysregulation of immune-related genes and contributing to disease.