This gene can be found on chromosome 8 at location 22462539-22477984.

The DNA sequence contains 21 exons and the transcript length is 4012 bps translated to a 923 residues protein.

Human KIAA1967/p30 DBC encodes a 923 amino acids protein with a leucine zipper motif, a Nudix domain, an EF hand motif and a coiled coil domain.

KIAA1967/p30 DBC is widely expressed in multiple tissues.

p30 DBC has a nuclear localization motif and localizes in the nucleus.

p30 DBC is an endogenous inhibitor of the class III protein deacetylase SIRT1. p30 DBC directly interacts with the catalytic domain of SIRT1 and inhibits the deacetylase activity of SIRT1. In doing so, p30 DBC promotes the acetylation of SIRT1 substrates such as p53 and FOXO3 following cellular stress in several cancer cell lines and inhibits SIRT1-dependent cell survival.
p30 DBC inhibits the activity of SUV39H1 methyltransferase and regulate heterochromatin formation via its inhibitory effect toward both SIRT1 and SUV39H1.
p30 DBC contains the Nudix hydrolase (MutT) domain, which is predicted to bind nucleoside diphosphate sugars and nicotinamide adenine dinucleotide (NAD), a co-substrate for SIRT1 enzyme. However, the Nudix domain of p30 DBC is predicted to be catalytically inactive.
In response to apoptosis-inducing signals, such as exposure to TNFalpha, etoposide or staurosporine, p30 DBC is cleaved into C-terminal p120 and p66 fragments in a caspase-dependent manner. The C-terminal fragment then relocalizes from nucleus to cytosol and mitochondria, and sensitizes cells to apoptotic stimuli. These findings suggest that p30 DBC promotes apoptosis through a positive feedback mechanism, which might suppress tumorigenesis by facilitating cell death in response to cellular stresses.
p30 DBC was found to act as a transcriptional coactivator of retinoic acid receptor alpha (RARalpha). The induction of RARalpha target genes such as Sox9 and HoxA1 gene in response to retinoic acid requires p30 DBC in MCF-7 breast cancer cells. This transcriptional activity of p30 DBC is not affected by SIRT1 inhibitor nicotinamide, suggesting that at least this transcriptional regulation function of p30 DBC is independent of SIRT1.
The first 150 amino acids of p30 DBC has been shown to interact with ERalpha through its hormone-binding domain in an estrogen-independent manner. The interaction between p30 DBC and ERalpha could stabilize ERalpha and promote breast cancer cell survival.
In addition to regulating ERalpha activity, p30 DBC could also act as an androgen receptor (AR) coactivator. The ligand binding domain (LBD) of AR interacts with the N-terminus of p30 DBC (residues 1~265) in the presence of AR ligand. This interaction enhances AR-DNA binding and facilitates ARs transcriptional activity. Knocking-down of p30 DBC decreases the induction of AR target genes including prostate specific antigen (PSA) in LNCaP prostate cancer cells.

Homologs were found in mammals. No p30 DBC homologs was identified in lower organism so far.