Anti-OTUB1 antibody

Target data

Hydrolase that can specifically remove 'Lys-48'-linked conjugated ubiquitin from proteins and plays an important regulatory role at the level of protein turnover by preventing degradation (PubMed : 12401499, PubMed : 12704427, PubMed : 14661020, PubMed : 23827681). Regulator of T-cell anergy, a phenomenon that occurs when T-cells are rendered unresponsive to antigen rechallenge and no longer respond to their cognate antigen (PubMed : 14661020). Acts via its interaction with RNF128/GRAIL, a crucial inductor of CD4 T-cell anergy (PubMed : 14661020). Isoform 1 destabilizes RNF128, leading to prevent anergy (PubMed : 14661020). In contrast, isoform 2 stabilizes RNF128 and promotes anergy (PubMed : 14661020). Surprisingly, it regulates RNF128-mediated ubiquitination, but does not deubiquitinate polyubiquitinated RNF128 (PubMed : 14661020). Deubiquitinates estrogen receptor alpha (ESR1) (PubMed : 19383985). Mediates deubiquitination of 'Lys-48'-linked polyubiquitin chains, but not 'Lys-63'-linked polyubiquitin chains (PubMed : 18954305, PubMed : 19211026, PubMed : 23827681). Not able to cleave di-ubiquitin (PubMed : 18954305, PubMed : 23827681). Also capable of removing NEDD8 from NEDD8 conjugates, but with a much lower preference compared to 'Lys-48'-linked ubiquitin (PubMed : 18954305, PubMed : 23827681).. Plays a key non-catalytic role in DNA repair regulation by inhibiting activity of RNF168, an E3 ubiquitin-protein ligase that promotes accumulation of 'Lys-63'-linked histone H2A and H2AX at DNA damage sites (PubMed : 20725033, PubMed : 22325355). Inhibits RNF168 independently of ubiquitin thioesterase activity by binding and inhibiting UBE2N/UBC13, the E2 partner of RNF168, thereby limiting spreading of 'Lys-63'-linked histone H2A and H2AX marks (PubMed : 20725033, PubMed : 22325355). Inhibition occurs by binding to free ubiquitin : free ubiquitin acts as an allosteric regulator that increases affinity for UBE2N/UBC13 and disrupts interaction with UBE2V1 (PubMed : 20725033, PubMed : 22325355). The OTUB1-UBE2N/UBC13-free ubiquitin complex adopts a configuration that mimics a cleaved 'Lys48'-linked di-ubiquitin chain (PubMed : 20725033, PubMed : 22325355). Acts as a regulator of mTORC1 and mTORC2 complexes (PubMed : 29382726, PubMed : 35927303). When phosphorylated at Tyr-26, acts as an activator of the mTORC1 complex by mediating deubiquitination of RPTOR via a non-catalytic process : acts by binding and inhibiting the activity of the ubiquitin-conjugating enzyme E2 (UBE2D1/UBCH5A, UBE2W/UBC16 and UBE2N/UBC13), thereby preventing ubiquitination of RPTOR (PubMed : 35927303). Can also act as an inhibitor of the mTORC1 and mTORC2 complexes in response to amino acids by mediating non-catalytic deubiquitination of DEPTOR (PubMed : 29382726).