NAC1 is an N-terminal homodimerization domain that contains multiple copies of kelch repeats and/or C2H2-type zinc fingers. Proteins that contain BTB domains are thought to be involved in transcriptional regulation via control of chromatin structure and function. BTBD14B (BTB/POZ domain-containing protein 14B), also known as NACC1 (nucleus accumbens associated 1), BEND8 or NAC1, is a 527 amino acid protein that localizes to both the nucleus and the cytoplasm and contains one BTB (POZ) domain. Existing as a homooligomer that interacts with HDAC3 and HDAC4, BTBD14B functions as a transcriptional repressor that influences the transcriptional activity of CRIF1 and is required for proteasome recruitment to the nucleus and cytoplasm in dendritic spines. BTBD14B is overexpressed in multiple carcinomas, suggesting a role in tumor development and metastasis.