USP38
Description
The USP38 (ubiquitin specific peptidase 38) is a protein-coding gene located on chromosome 4.
USP38 is a deubiquitinating enzyme that plays a role in various cellular processes, including DNA repair, cell cycle regulation, and immune response. It inhibits type I interferon signaling by mediating the 'Lys-33' to 'Lys-48' ubiquitination transition of TBK1, leading to its degradation. USP38 also cleaves the ubiquitin chain from the histone demethylase LSD1/KDM1A, preventing its degradation and maintaining LSD1 protein levels in cells. In response to DNA damage, USP38 removes the 'Lys-63'-linked ubiquitin chain, promoting the deacetylase activity of HDAC1. USP38 also acts as a specific deubiquitinase of histone deacetylase 3/HDAC3, cleaving its 'Lys-63'-linked ubiquitin chains to lower its histone deacetylase activity. USP38 regulates MYC levels and cell proliferation by antagonizing ubiquitin E3 ligase FBXW7, preventing MYC 'Lys-48'-linked ubiquitination and degradation. USP38 participates in antiviral response by removing both 'Lys-48'-linked and 'Lys-63'-linked polyubiquitination of Zika virus envelope protein E. Finally, USP38 is constitutively associated with IL-33R/IL1RL1, deconjugating its 'Lys-27'-linked polyubiquitination, leading to its autophagic degradation.
USP38 is also known as HP43.8KD.
