Apoptosis is mediated by death domain containing adapter molecules and a caspase family of proteases. Certain serine/threonine protein kinases, such as ASK1 and RIP, are mediators of apoptosis. Two novel serine/threonine kinases that induce apoptosis were recently identified and designated DRAK1 and DRAK2 (for DAP kinase related apoptosis inducing protein kinases). DRAKs contain an N terminal kinase domain and a C terminal regulation domain. Overexpression of DRAK2 induces apoptosis. DRAKs

Semaphorin 7a is required for central and peripheral axon growth and is required for proper axon tract formation during embryonic development. Semaphorin 7a is also involved in modulating immune function. Semaphorin 7a expression is highest in the brain and increases in late embryonic and postnatal stages. The Semaphorins constitute a large family of secreted and membrane-tethered cell signaling molecules. They have functions in neural development, immunology, cardiac growth, vascular deve

NR1D1, a NR1 Thyroid Hormone-Like Receptor, is encoded by the same genomic locus as, but transcribed from the opposite strand of, Thyroid Hormone Receptor Alpha (TR Alpha). NR1D1 is a target of Nuclear Receptor ROR Alpha and a transcription regulator that has been shown to affect myocyte differentiation, adipogenesis, and lipoprotein metabolism. Mice lacking NR1D1 show abnormal postnatal cerebellar development. NR1D1 expression has been documented in human skeletal muscle and a variety of mo

BPGM (2,3-bisphosphoglycerate mutase) is a 259 amino acid protein that belongs to the phosphoglycerate mutase family and exists as a homodimer that plays a crucial role in the regulation of hemoglobin oxygen. Specifically, BPGM catalyzes the conversion of 3-phospho-D-glyceroyl phosphate to 2,3-bisphospho-D-glycerate (2,3-BPG), a reaction that is essential for controlling the concentration of 2,3-BPG within the cell. The gene encoding BPGM maps to human chromosome 7, which houses over 1,000 gen

This protein encoded is a cytoplasmic nonreceptor protein kinase which may function as an intracellular signal transducer in epithelial tissues. Overexpression of this gene in mammary epithelial cells leads to sensitization of the cells to epidermal growth factor and results in a partially transformed phenotype. Expression of this gene has been detected at low levels in some breast tumors but not in normal breast tissue. Its presence in the nucleus appears to be linked to suppression of tumor

The protein encoded by this gene is a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. The protein localizes to cytoplasmic bodies and its function has not been determined. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Mar 2010]