UBTD2 (ubiquitin domain containing 2), also known as DCUBP (dendritic cell-derived ubiquitin-like protein), DC-UbP or SB72, is a 234 amino acid cytoplasmic and mitochondrial ubiquitin-like (UbL) protein that contains one C-terminal UbL domain. UbL proteins are involved in a variety of cellular processes, including DNA repair, protein sorting, apoptosis, protein degradation, cell division and autophagy. Predominantly expressed in dendritic cells and detected at high levels in tumor cell lines, UBTD2 has been implicated in apoptosis, cellular differentiation and tumorigenesis. The UbL domain of UBTD2 is 55% similar and 28.6% identical to the amino acid sequence of ubiquitin, but it lacks the Gly-Gly motif that is essential for ubiquitination. As its UbL domain does not actively ubiquitinate proteins, UBTD2 is believed to function as a shuttle factor involved in the ubiquitin system.
A synthesized peptide derived from human UBXD5, corresponding to a region within the internal amino acids.
Ubiquitin-binding protein that interacts with the BRCA1-BARD1 heterodimer, and regulates its activity. Specifically binds 'Lys-6'-linked polyubiquitin chains. Interaction with autoubiquitinated BRCA1, leads to inhibit the E3 ubiquitin-protein ligase activity of the BRCA1-BARD1 heterodimer. Component of a complex required to couple deglycosylation and proteasome-mediated degradation of misfolded proteins in the endoplasmic reticulum that are retrotranslocated in the cytosol.
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