Overview:

JosD2 (Josephin domain-containing 2) is a member of the MJD family of deubiquitinating enzymes (DUBs) that is localized to the cytoplasm and catalyzes the hydrolysis of the bond between the C-terminal glycine of the ubiquitin peptide and protein substrates. In vitro, JosD2 can cleave ubiquitin chains (1). Although JosD2 has been shown to have deubiquitinating activities, details of its substrate specificity are still mainly unknown (2).

Gene Aliases:

SBBI54

Genbank Number:

NM_138334

References:

1. Seki, T. et al: JosD1, a membrane-targeted deubiquitinating enzyme, is activated by ubiquitination and regulates membrane dynamics, cell motility, and endocytosis. Journal of biological chemistry 288(24): 17145-55, 2013.

2. Tzvetkov, N. & Breuer, P: Josephin domain-containing proteins from a variety of species are active de-ubiquitination enzymes. Biol Chem 388(9):973-8, 2007.