Hydrolase that can remove conjugated ubiquitin from proteins and participates in endoplasmic reticulum-associated degradation (ERAD) for misfolded lumenal proteins. May act by triming the ubiquitin chain on the associated substrate to facilitate their threading through the VCP/p97 pore. Ubiquitin moieties on substrates may present a steric impediment to the threading process when the substrate is transferred to the VCP pore and threaded through VCP's axial channel. Mediates deubiquitination of both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. Able to cleave both polyubiquitin and di-ubiquitin.
Contains 1 C2H2-type zinc finger. Contains 1 OTU domain.
The UBAX-like region mediates the interaction with VCP. According to PubMed:19818707, it corresponds to a UBX domain, which is a hallmark for VCP-associated proteins. However, no canonical UBX is detected by prediction tools such as Pfam or PROSITE.
Confocal immunofluorescent analysis of WiDr cells labeling YOD1 with ab170179 at 1/10 dilution, followed by Alexa Fluor 488-conjugated goat anti-rabbit lgG (green). DAPI was used to stain the cell nuclei (blue).
Immunohistochemical analysis of formalin-fixed, paraffin-embedded Human bladder carcinoma tissue labeling YOD1 with ab170179 at 1/50 dilution, followed by a peroxidase conjugated secondary antibody and DAB staining.
Western blot - Anti-YOD1 antibody - C-terminal (ab170179)
Anti-YOD1 antibody - C-terminal (ab170179) at 1/100 dilution + K562 cell lysate at 35 µg