EDD is a progestin-regulated gene that was isolated from T-47D human breast cancer cells. Based on sequence homology, EDD appears to be a human homolog of the Drosophila hyperplastic discs (hyd) gene, a tumor suppressor gene that is required for control of imaginal disc growth. EDD contains a HECT domain in the carboxy terminus. HECT domain-containing proteins function as ubiquitin-protein ligases, or E3 enzymes. EDD has been shown to bind to ubiquitin, and like other HECT family proteins, may

The onset of angiogenesis is believed to be an early event in tumorigenesis and may facilitate tumor progression and metastasis. Several growth factors with angiogenic activity have been described and include fibroblast growth factor (FGF), platelet derived growth factor (PDGF) and vascular endothelial growth factors (VEGFs). The VEGF protein family is comprised of VEGF, VEGF-B, VEGF-C and VEGF-D, all of which may exhibit angiogenic function in vivo. VEGF-B, which exists as two alternative

Glutamate receptors are the predominant excitatory neurotransmitter receptors in the mammalian brain and are activated in a variety of normal neurophysiologic processes. This gene product belongs to a family of glutamate receptors that are sensitive to alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate(AMPA), and function as ligand-activated cation channels. These channels are assembled from 4 related subunits, Gria1-4. The subunit encoded by this gene (Gria2) is subject to RNA editing(CAG

This gene encodes a syntaxin-binding protein. The encoded protein appears to play a role in release of neurotransmitters via regulation of syntaxin, a transmembrane attachment protein receptor. Mutations in this gene have been associated with infantile epileptic encephalopathy-4. Alternatively spliced transcript variants have been described. [provided by RefSeq, Feb 2010]

This gene encodes a nicotinic acetylcholine receptor, which belongs to a superfamily of ligand-gated ion channels that play a role in fast signal transmission at synapses. These pentameric receptors can bind acetylcholine, which causes an extensive change in conformation that leads to the opening of an ion-conducting channel across the plasma membrane. This protein is an integral membrane receptor subunit that can interact with either nAChR beta-2 or nAChR beta-4 to form a functional receptor.

The protein encoded by this gene belongs to the membrane-associated guanylate kinase (MAGUK) family, a class of proteins that functions as molecular scaffolds for the assembly of multiprotein complexes at specialized regions of the plasma membrane. This protein is also a member of the CARD protein family, which is defined by carrying a characteristic caspase-associated recruitment domain (CARD). This protein has a domain structure similar to that of CARD14 protein. The CARD domains of both prot