Ubiquitin carboxyl-terminal hydrolase 17-like protein 21 (USP17L21)

Ubiquitin carboxyl-terminal hydrolase 17-like protein 21 (USP17L21) is a deubiquitinating enzyme that belongs to the cysteine protease family and specifically the USP17 subfamily. Like other USP17 subfamily members, USP17L21 contains a USP domain responsible for its catalytic activity, targeting the removal of ubiquitin from specific protein substrates to regulate their degradation, stability, and cellular signaling. It is predicted to participate in the regulation of apoptosis, protein stability, and cell proliferation. Members of the USP17 subfamily, including USP17L21, have been implicated in cell death, cancer progression, and possibly inflammation, making them relevant for therapeutic intervention. No drugs are currently approved targeting USP17L21 specifically, but its family is considered druggable due to their functional importance in malignant and proliferative processes. Expression of USP17 family members is variable, sometimes induced by cytokines and upregulated in certain tumors. Human USP17 subfamily has multiple members with distinct but related functions; USP17L21 is part of this group and shares sequence and functional homology. It is mainly localized in the nucleoli and may contain RNA and hyaluronan binding motifs crucial for its cellular localization and function. Overexpression of USP17 subfamily members can lead to cell death, indicating their tight regulation is critical for cell viability.

Other names

Ubiquitin specific peptidase 17 like family member 21USP17L21Ubiquitin carboxyl-terminal hydrolase 17-like protein 21D6R901 (UniProt)HGNC:44449

For drugs targeting this enzyme family: inhibition of deubiquitinating (DUB) activity, leading to altered ubiquitin-mediated degradation pathways