OTUB2

Otubain 2 (OTUB2) is a member of DUBs that belong to the ovarian tumour (OTU) superfamily of proteins which consists of a five-stranded β-sheet sandwiched in between a small helical amino-terminal region consisting of α1 and α2, and a large helical region comprised of α3-α10. Like other DUBs, otubain 2 (OTUB2) cleaves proteins precisely at the ubiquitin-protein bond so that ubiquitylation process can be reversed and regulated. Otubain 2 (OTUB2)s active-site cleft is sterically occluded by a novel loop conformation resulting in an oxyanion hole, which consists uniquely of backbone amides. Furthermore, the residues that orient and stabilize the active-site histidine of otubain 2 (OTUB2) are different from other cysteine proteases. This reorganization of the active-site topology provides a possible explanation for the low turnover and substrate specificity of the otubains.

OTUB2

Hydrolase that can remove conjugated ubiquitin from proteins in vitro and may therefore play an important regulatory role at the level of protein turnover by preventing degradation. Mediates deubiquitination of 'Lys-11'-,'Lys-48'- and 'Lys-63'-linked polyubiquitin chains, with a preference for 'Lys-63'-linked polyubiquitin chains.

Negative regulation of double-strand break repairManual Assertion Based On ExperimentIBA:GO_Central
Negative regulation of histone H2A K63-linked ubiquitinationManual Assertion Based On ExperimentIBA:GO_Central
Protein deubiquitinationManual Assertion Based On ExperimentIMP:UniProtKB
Protein K11-linked deubiquitinationManual Assertion Based On ExperimentIDA:UniProtKB
Protein K48-linked deubiquitinationManual Assertion Based On ExperimentIDA:UniProtKB
Protein K63-linked deubiquitinationManual Assertion Based On ExperimentIDA:UniProtKB

Nucleus