Disease relevance of USP3

• To determine whether the N termini also influence the biochemical functions of the UBP, we expressed UBP-t1, UBP-t2, and the common core domain, UBP core, in Escherichia coli [1].
• The overexpression of USP25 in Down syndrome fetal brains supports the gene-dosage effects suggested for other UBP members related to aneuploidy syndromes [2].

High impact information on USP3

• The ubiquitin binding domain ZnF UBP recognizes the C-terminal diglycine motif of unanchored ubiquitin [3].
• Thus, UBP enzymes appear to contain a catalytic core domain, the activities and specificities of which can be modulated by N-terminal extensions [1].
• UBP-core removed ubiquitin from testis ubiquitinated proteins more rapidly than UBP-t2 and UBP-t1 [1].
• We have isolated a complete USP3 cDNA clone containing both of these conserved sequence regions [4].
• The USP3 gene appears to be single copy and maps to human chromosome 15q22 [4].

Biological context of USP3

• To inhibit cytoplasmic TG hydrolysis, the lipase inhibitor, diethylumbelliferyl phosphate (UBP), was added at the time of cholesterol enrichment [5].
• All analogues showed weak inhibition toward the catalytic domain of UCH-L3 and a UBP pseudogene [6].
• These (and earlier) results suggest that UBP isozymes may exhibit significant substrate specificity, consistent with a role in the regulated catabolism of the polymeric ubiquitin, including the polyubiquitin protein degradation signal [7].
• With the tools ECOINDICATOR and UBP anaerobic digestion shows to be advantageous as compared to composting, incineration or combination of digestion and composting, mainly because of a better energy balance [8].
• RESULTS: Database homology searches at the DNA and protein levels and cDNA library screenings led to the identification of a new UBP member in the human genome, named USP28, at 11q23 [2].

Anatomical context of USP3

• Because ubiquitination can also be regulated by deubiquitinating enzymes, we used degenerate oligonucleotides derived from conserved sequences in the ubiquitin-specific protease (UBP) family of deubiquitinating enzymes in RT-PCR with skeletal muscle RNA to amplify putative deubiquitinating enzymes [9].

Associations of USP3 with chemical compounds

• The USP15 protein consists of 952 amino acids with a predicted molecular mass of 109.2 kDa and contains the highly conserved Cys and His boxes present in all members of the UBP family of deubiquitinating enzymes [10].
• Tests included treadmill run and double-pole lactate profile and VO2peak tests, and a double-pole peak power test (UBP) [11].
• The first crystal structures have been obtained for a UBP domain both alone and in complex with ubiquitin aldehyde, thus providing a framework for structural conservation throughout the UBP protease family [12].

Other interactions of USP3

• Two lines, USP-1 and USP-3, with the best in vitro characteristics of pluripotency were used in chimera-generating experiments [13].

Analytical, diagnostic and therapeutic context of USP3

• However, 47 samples positive in immunoblotting, 37 positive for UBP, seven for anti-SSA, are for anti-Jo-1, one for anti-RNP and one for anti-Sm were missed by radial immunodiffusion [14].

References