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BRCA1 Associated RING Domain gene 1 (BARD1) interacts with the N terminal region of BRCA1. In addition to its ability to bind BRCA1 in vivo and in vitro, BARD1 shares homology with the 2 most conserved regions of BRCA1: the N terminal RING motif and the C terminal BRCT domain. The RING motif is a cysteine rich sequence found in a variety of proteins that regulate cell growth, including the products of tumor suppressor genes and dominant protooncogenes. The BARD1 protein also contains 3 tande

JMJD1B (jumonji domain containing 1B), also known as KDM3B, 5qNCA (5q Nuclear Co-Activator) or C5orf7, is a member of the JHDM2 histone demethylase family of proteins. Expressed in a wide variety of tissues, JMJD1B localizes to the nucleus and contains one JMJC domain and a C-terminal zinc finger motif. JMJD1B functions as a histone demethylase and, using iron as a cofactor, demethylates lysine-9 of Histone H3. This suggests that JMJD1B plays a central role in the histone code. The gene encod

The pocket protein family consists of three structurally and functionally related proteins, Rb (retinoblastoma), p107, and p130. This family of tumor suppressors function to regulate important cellular transcription factors, such as the E2F family. The E2F proteins regulate the expression of genes whose products are important for cell cycle progression. The inactivation Rb is catalyzed by CDK phosphorylation thereby releasing E2F during the G1-S phase cellular progression. Unchecked inactivat

Enables protein serine/threonine kinase activity. Involved in peptidyl-serine phosphorylation. Located in membrane. [provided by Alliance of Genome Resources, Apr 2022]

The Peroxiredoxin (Prdx, Prx, or Trx-Px) family of enzymes is a recently identified family of peroxidases found in free-living organisms. The six known isoforms (Prx1-6) play an important role in protecting lipids, enzymes and DNA against peroxides, such as hydrogen peroxide. The ubiquitously expressed peroxiredoxins have also been shown to play a role in apoptosis and cell differentiation. This is acomplished by the active cysteine of Prx reducing peroxides, which is then converted into a tr

Several proteins mediate the biosynthesis of cholesterol. The first specific step in the cholesterol biosynthetic pathway is the conversion of transfarnesyl-diphosphate to Squalene, which is catalyzed by the endoplasmic reticulum membrane-associated enzyme Squalene synthetase, also designated Squalene synthase and Farnesyl-diphosphate farnesyltransferase. Squalene synthetase is located at a branch point in the mevalonate pathway and is also involved in isoprenoid biosynthesis. Squalene epoxid