Ubiquitin-protein hydrolase involved both in the processing of ubiquitin precursors and of ubiquitinated proteins. This enzyme is a thiol protease that recognizes and hydrolyzes a peptide bond at the C-terminal glycine of ubiquitin (By similarity). Also binds to free monoubiquitin and may prevent its degradation in lysosomes (By similarity). The homodimer may have ATP-independent ubiquitin ligase activity (By similarity).
Subcellular locations: Cytoplasm, Endoplasmic reticulum membrane, Nucleus
Found both cytoplasmic and nuclear in cytotrophoblasts and decidual cells.
Expressed in the placenta at all stages of pregnancy. Expression increases as pregnancy progresses.