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Ubiquitin specific peptidase 39 (USP39)
- Target
- USP39
- Molecular classification
- Enzyme (deubiquitinating enzyme), Spliceosome complex protein, Other (RNA splicing factor)
01
Overview
Ubiquitin specific peptidase 39 (USP39) is a nuclear protein involved in the assembly and function of the U4/U6–U5 tri-small nuclear ribonucleoprotein (tri-snRNP) complex, an essential component of the spliceosome responsible for pre-mRNA splicing[1][2][5]. Although classified in the ubiquitin-specific peptidase family, USP39 lacks intrinsic deubiquitinase (DUB) activity, but it is crucial for mRNA processing and the regulation of cell cycle, DNA repair, and apoptosis[5][7]. USP39 is highly expressed in multiple cancer types, where it promotes tumor proliferation, migration, invasion, cell cycle progression, and resistance to therapy by affecting RNA maturation and modulating oncogenic signaling pathways[2][4][7]. This makes USP39 a promising but challenging cancer therapeutic target, with potential biomarker utility for cancer prognosis[2][7].
- Other names
- 65KHSPC332SAD1SNRNP65CGI-21U4/U6.U5 tri-snRNP-associated protein 2ubiquitin specific protease 39Sad1p
02
Mechanism of action
Inhibitors would be expected to interfere with spliceosome assembly or mRNA maturation, and/or to block pro-tumorigenic functions (hypothetical, not clinically validated)
03
Biological functions
Pre-mRNA splicing (part of the U4/U6-U5 tri-snRNP of the spliceosome)Regulation of mRNA maturationRegulation of mitotic spindle checkpoint and cytokinesisRegulation of apoptosis and cell cycle checkpointDNA repair (non-homologous end joining)Regulation of immune signaling (e.g., type I IFN signaling)Negative regulation of NF-κB activationRegulation of non-canonical Wnt signaling
04
Disease associations
Cancer (oncogenic/pro-tumorigenic: promotes proliferation, migration, invasion, therapy resistance; involved in glioma, breast, hepatocellular, renal, prostate, thyroid, bladder cancer, and melanoma)Ciliary dyskinesia, primary, 18Nephronophthisis 1
05
Safety considerations
Targeting USP39 could disrupt essential pre-mRNA splicing in normal proliferating cells, possibly causing toxicity
06
Interacting drugs
None currently listed in major databases; small-molecule inhibitors are proposed as an area of future research for cancer therapy
07
Biomarkers
High USP39 expression is associated with poor prognosis in several cancers, including glioma and hepatocellular carcinoma
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