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Arginine and glutamate-rich protein 1 (ARGLU1) is an evolutionarily conserved nuclear protein of 273 amino acids, with a bipartite structure: a positively charged, arginine-rich N-terminus and a negatively charged, glutamate-rich C-terminus. It acts primarily as a dual-function protein with key roles in both the regulation of gene transcription (as a coactivator for nuclear receptors such as estrogen and glucocorticoid receptors) and in modulating alternative splicing of pre-mRNAs by associating with the spliceosome and other splicing factors. ARGLU1 is highly expressed in the central nervous system, and loss of its function leads to severe developmental defects, particularly in neural tissue. It is not an enzyme, receptor, or ion channel, but rather a highly specialized regulatory cofactor and splicing modulator. ARGLU1 has been implicated in cancer biology, DNA damage response, neural development, and the regulation of chromatin organization, but there are currently no approved drugs specifically targeting this protein.
Not drug-targeted yet; mechanistic data pertains to coactivation of nuclear receptors (e.g., estrogen receptor, glucocorticoid receptor) via enhancer function, and promotion of alternative splicing events via interaction with spliceosome machinery and pre-mRNA.
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