A heterodimeric complex comprising BRCA1 and BARD1, which possesses ubiquitin ligase activity and is involved in genome maintenance, possibly by functioning in surveillance for DNA damage.

ATPase activity, coupled to transmembrane movement of substances

Catalysis of the reaction: ATP + H2O = ADP + phosphate to directly drive the transport of a substance across a membrane.

Citrate lyase is a multienzyme complex with three constituents: the alpha subunit, citrate-ACP transferase; the beta subunit, citryl-ACP lyase; and the gamma subunit, an acyl-carrier protein which also carries the prosthetic group components. All three subunits are required for citrate lyase enzyme activity.

Interacting selectively with an amino acid, organic acids containing one or more amino substituents.

A particle composed of a central core of triglycerides surrounded by a protein-phospholipid coating. Chylomicrons are found in blood or lymph and carry lipids from the intestines into other body tissues.

The morphological and physiological alterations undergone by mitochondria during apoptosis.

The posttranslational conjugation of arginine to the N-terminal aspartate or glutamate of a protein; required for the degradation of the protein via the ubiquitin pathway.

An enzyme complex that catalyzes the transfer of a carbamoyl to ornithine, forming citrulline.

G-protein signaling, coupled to IP3 second messenger (phospholipase C activating)

G-protein signalling, coupled to IP3 second messenger (phospholipase C activating)

The series of molecular signals generated as a consequence of a G-protein coupled receptor binding to its physiological ligand, followed by the activation of phospholipase C and the subsequent release of inositol trisphosphate.

The membrane area of caveolae, the small pits, depressions, or invaginations found in the plasma membrane of cells. Caveolar membrane is characterized by the presence of caveolins, which constitute the major protein component of caveolar membrane in vivo.

Catalysis of the hydrolysis of peptide bonds. Specificity similar to chymotrypsin C.