USP27X
Description
The USP27X (ubiquitin specific peptidase 27 X-linked) is a protein-coding gene located on chromosome X.
USP27X is a deubiquitinating enzyme, meaning it removes ubiquitin (Ub) from proteins. Ubiquitin is a small protein that attaches to other proteins and can regulate their activity or target them for degradation. USP27X is encoded by the USP27X gene located on chromosome X. It is found in the cytosol, nucleus, nucleoplasm, and vesicles of cells. USP27X is an intracellular protein present in many human tissues.
USP27X belongs to the ubiquitin-specific protease (USP) family, a group of enzymes that play important roles in various cellular processes. USPs have a conserved catalytic domain for removing ubiquitin from proteins. Other regions of the enzyme may be involved in recognizing specific target proteins, interacting with other proteins, and directing the enzyme to its proper location in the cell.
USP27X, a deubiquitinase, plays a role in innate antiviral immunity by removing ubiquitin tags from CGAS and RIGI proteins. This process helps regulate the signaling pathways involved in immune responses to viral infections. USP27X negatively controls RIGI by removing 'Lys-63'-linked ubiquitin, which inhibits type I interferon signaling. It also regulates the ubiquitination levels of MDA5/IFIH1, another protein involved in antiviral responses. In addition to its role in antiviral immunity, USP27X is a positive regulator of the cGAS-STING pathway. It promotes the stabilization of CGAS by removing 'Lys-48'-linked ubiquitin. USP27X can also reduce the levels of BCL2L11/BIM ubiquitination and stabilize BCL2L11 in response to the RAF-MAPK-degradation signal, potentially counteracting the anti-apoptotic effects of MAPK activity.
USP27X is also known as MRX105, USP22L, USP27, XLID105.
