USP17L27 Gene: Function, Location, and Disease Relevance | Biomedical SEO

USP17L27 is a protein-coding gene that belongs to the USP17 family of deubiquitinating enzymes. It is located on chromosome 4p16.1, within a cluster of highly similar USP17-like genes that arose through segmental duplication. The encoded protein contains a peptidase C19 domain characteristic of ubiquitin-specific proteases, which cleave ubiquitin from target proteins, thereby regulating protein stability and signaling pathways. USP17L27 is part of a gene family implicated in cell proliferation, apoptosis, and immune responses. However, due to its high sequence similarity to other USP17 family members, functional studies often require careful discrimination. The gene is expressed in various tissues and may be upregulated in certain cancers, suggesting a potential role in tumorigenesis, though specific disease associations are still under investigation.

Tissue Expression

Cell Line Expression

Hotspot Mutations

Mutation functional classification

• Ubiquitin-proteasome pathway

• Cytokine signaling (e.g.

• JAK-STAT)

• Cell cycle regulation

The USP17L27 protein is a deubiquitinating enzyme that removes ubiquitin from specific target proteins, thereby preventing their degradation by the proteasome. It contains a conserved peptidase C19 domain. Its precise substrates are not fully characterized, but USP17 family members are known to regulate proteins involved in cell cycle progression, apoptosis, and immune signaling. Due to its high similarity to other USP17 proteins, functional redundancy is likely.