USP10
USP10 (ubiquitin specific peptidase 10, also known as UBPO and KIAA0190) is a cysteine protease that removes conjugated ubiquitin from substrate proteins. It stabilises p53, supports autophagy and ribosome recycling, and restrains stress granule formation. Browse Assay Genie's current range of USP10 research reagents below, or read on for the biology behind the target.
USP10 is a hydrolase that removes conjugated ubiquitin from target proteins, including p53/TP53, the ribosomal proteins RPS2, RPS3 and RPS10, BECN1, SNX3 and CFTR. It is an essential regulator of p53 stability. In unstressed cells it deubiquitinates p53 in the cytoplasm, counteracting MDM2 and stabilising p53. After DNA damage it translocates to the nucleus and deubiquitinates p53 there, regulating the p53-dependent DNA damage response. It does not deubiquitinate MDM2.
The enzyme also sits within a regulatory loop controlling autophagy and p53 levels. USP10 deubiquitinates BECN1, stabilising PIK3C3/VPS34-containing complexes, and these complexes in turn regulate USP10 stability, suggesting a system in which they influence p53 levels through USP10 and USP13. During translational stress, USP10 promotes 40S ribosome subunit recycling by deubiquitinating RPS2, RPS3 and RPS10, which prevents their proteasomal degradation. It acts in ribosome quality control at translation initiation, and it lowers G3BP1 and G3BP2 valence, limiting their liquid-liquid phase separation and so negatively regulating stress granule assembly.
Further roles include deubiquitinating CFTR in early endosomes to enhance its endocytic recycling, and stabilising TBX21. USP10 attenuates NF-kappa-B activation in a TANK-dependent feedback response by deubiquitinating IKBKG or TRAF6, and it acts negatively in RLR signalling by removing unanchored Lys-63-linked polyubiquitin chains from MAVS. NCBI also describes it as a co-factor of the DNA-bound androgen receptor complex. The USP10 gene belongs to the ubiquitin specific peptidase group and the peptidase C19 family, USP10 subfamily; the protein is found in the nucleus and cytoplasm, and several transcript variants exist. Mouse and rat both have a Usp10 ortholog.
USP10 deubiquitinates p53, counteracting MDM2 and shaping the p53-dependent DNA damage response.
By deubiquitinating BECN1, USP10 stabilises PIK3C3/VPS34-containing complexes within a loop that links autophagy to p53 levels.
USP10 promotes 40S ribosome recycling and limits G3BP1 and G3BP2 phase separation, making it central to ribosome quality control and stress granule studies.
USP10 deubiquitinates IKBKG, TRAF6 and MAVS, attenuating NF-kappa-B and RLR signalling during stimulation or RNA virus infection.
USP10 is a deubiquitinating enzyme that cleaves ubiquitin from substrates. It stabilises p53 by counteracting MDM2, deubiquitinates BECN1 to support autophagy, recycles 40S ribosomal subunits after stalling, and negatively regulates stress granule formation by acting on G3BP1 and G3BP2.
The USP10 gene is also known as UBPO and KIAA0190, and was previously named ubiquitin specific protease 10. UniProt lists the protein as ubiquitin carboxyl-terminal hydrolase 10, EC 3.4.19.12. NCBI notes several transcript variants, some protein-coding and others not, plus several similar pseudogenes in the human genome.
Yes. Mouse and rat each have a Usp10 ortholog, so the protein can be studied in common rodent models. Check the datasheet of any product for its validated reactivity. USP10 belongs to the peptidase C19 family, USP10 subfamily, alongside other ubiquitin specific peptidases.
Other ubiquitin specific peptidases, including USP13, which acts alongside USP10 in p53 regulation, with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt Q14694; product specifications from Assay Genie datasheets.