DBC-1 Core component of the DBIRD complex, a multiprotein complex that acts at the interface between core mRNP particles and RNA polymerase II (RNAPII) and integrates transcript elongation with the regulation of alternative splicing: the DBIRD complex affects local transcript elongation rates and alternative splicing of a large set of exons embedded in (A + T)-rich DNA regions. Inhibits SIRT1 deacetylase activity leading to increasing levels of p53/TP53 acetylation and p53-mediated apoptosis. Inhibits SUV39H1 methyltransferase activity. As part of a histone H3-specific methyltransferase complex may mediate ligand-dependent transcriptional activation by nuclear hormone receptors. Plays a critical role in maintaining genomic stability and cellular integrity following UV-induced genotoxic stress. Regulates the circadian expression of the core clock components NR1D1 and ARNTL/BMAL1. Enhances the transcriptional repressor activity of NR1D1 through stabilization of NR1D1 protein levels by preventing its ubiquitination and subsequent degradation. Represses the ligand-dependent transcriptional activation function of ESR2. Acts as a regulator of PCK1 expression and gluconeogenesis by a mechanism that involves, at least in part, both NR1D1 and SIRT1. Negatively regulates the deacetylase activity of HDAC3 and can alter its subcellular localization. Positively regulates the beta-catenin pathway (canonical Wnt signaling pathway) and is required for MCC-mediated repression of the beta-catenin pathway. Represses ligand-dependent transcriptional activation function of NR1H2 and NR1H3 and inhibits the interaction of SIRT1 with NR1H3. Plays an important role in tumor suppression through p53/TP53 regulation; stabilizes p53/TP53 by affecting its interaction with ubiquitin ligase MDM2. Represses the transcriptional activator activity of BRCA1. Inhibits SIRT1 in a CHEK2 and PSEM3-dependent manner and inhibits the activity of CHEK2 in vitro. Expressed in gastric carcinoma tissue and the expression gradually increases with the progression of the carcinoma (at protein level). Expressed ubiquitously in normal tissues. Expressed in 84 to 100% of neoplastic breast, lung, and colon tissues. 2 alternatively spliced human isoforms have been reported. Note: This description may include information from UniProtKB.
Protein type: Apoptosis; Mitochondrial; Nuclear receptor co-regulator; RNA-binding; Tumor suppressor
Chromosomal Location of Human Ortholog: 8p21.3
Cellular Component:  cytoplasm; DBIRD complex; mitochondrial matrix; nuclear chromatin; nucleoplasm; nucleus
Molecular Function:  enzyme binding; enzyme inhibitor activity; protein binding; RNA polymerase II complex binding
Biological Process:  cell cycle; cellular response to DNA damage stimulus; mitochondrial fragmentation involved in apoptotic process; mRNA processing; negative regulation of catalytic activity; negative regulation of cell growth; negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage; negative regulation of proteasomal ubiquitin-dependent protein catabolic process; negative regulation of transcription, DNA-templated; positive regulation of apoptotic process; positive regulation of canonical Wnt signaling pathway; positive regulation of DNA damage checkpoint; positive regulation of nucleic acid-templated transcription; regulation of cellular response to heat; regulation of circadian rhythm; regulation of DNA-templated transcription, elongation; regulation of protein deacetylation; regulation of protein stability; response to UV; rhythmic process; RNA splicing; Wnt signaling pathway
Reference #:  Q8N163 (UniProtKB)
Alt. Names/Synonyms: cell cycle and apoptosis regulator 2; Cell cycle and apoptosis regulator protein 2; DBC-1; DBC.1; DBC1; deleted in breast cancer 1; Deleted in breast cancer gene 1 protein; K1967; KIAA1967; NET35; p30 DBC; p30 DBC protein
Gene Symbols: CCAR2
Molecular weight: 102,902 Da
Basal Isoelectric point: 5.14  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
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Protein Structure Not Found.

Cross-references to other databases:  STRING  |  cBioPortal  |  Wikipedia  |  neXtProt  |  Protein Atlas  |  BioGPS  |  Pfam  |  Phospho.ELM  |  NetworKIN  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene  |  NURSA  |  InnateDB