Nuclear factor related to kappa-B-binding protein, also known as INO80 complex subunit G, is a component of the metazoan INO80 complex involved in chromatin remodelling, transcription regulation, DNA replication and DNA repair [, ].
This winged helix-like domain is found in nuclear factor related to kappa-B-binding (NFRKB) protein. NFRKB is a component of the metazoan INO80 complex involved in chromatin remodelling, transcription regulation, DNA replication and DNA repair. This winged helix-like domain is however not involved in DNA binding but is instead thought to be involved in protein-protein interactions [].
This winged helix-like domain is found in nuclear factor related to kappa-B-binding (NFRKB) protein. NFRKB is a component of the metazoan INO80 complex involved in chromatin remodelling, transcription regulation, DNA replication and DNA repair. This winged helix-like domain is however not involved in DNA binding but is instead thought to be involved in protein-protein interactions [].
This is the C-terminal domain found in eukaryotic UCH37 proteins (also known as Ubiquitin carboxyl-terminal hydrolase isozyme L5, UCHL5). UCH37 is a subunit of two complexes: INO80, which performs ATP-dependent sliding of nucleosomes for transcriptional regulation and DNA repair, and the 26S proteasome, which performs ATP-dependent proteolysis of polyubiquitylated proteins in the cytosol and nucleus. Recruitment to the proteasome is mediated by the C-terminal domain of RPN13 (also known as ADRM1). Recruitment to INO80 is mediated by the N-terminal domain of NFRKB. Structural and biochemical analysis reveal that RPN13 and NFRKB make similar interactions with the UCH37 C-terminal domain but have very different interactions with the catalytic UCH domain that are activating in the case of RPN13 and highly inhibitory in the case of NFRKB [].
