Ubiquitinating enzymes (UBEs) catalyze protein ubiquitination, a reversible process countered by deubiquitinating enzyme (DUB) action. Five DUB subfamilies are recognized, including the USP, UCH, OTU, MJD, and JAMM enzymes. Ubiquitin carboxyl-terminal hydrolase 13 (USP13; isopeptidase T-3) contains four ubiquitin-associated/translation elongation factor EF1B, amino terminal (UBA) domains and one ubiquitin-specific processing protease (UBP) domain. The UBP domain of USP13 contains a catalytic site, a zinc finger domain, and two UBA domains. Similar to other USP family members, USP13 contains cysteines and histidines that are likely involved in its catalytic mechanism. Studies show that USP13 plays a critical role in autophagy through the deubiquitination of target proteins such as BECN1 and USP10. Research also suggests that USP13 is implicated in the pathogenesis of melanoma through its ability to regulate the ubiquitination status of MITF.
ELISA, IHC, WB
Human 1, Mouse
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