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This gene encodes a member of the mammalian activation transcription factor/cAMP responsive element-binding (CREB) protein family of transcription factors. This gene is induced by a variety of signals, including many of those encountered by cancer cells, and is involved in the complex process of cellular stress response. Multiple transcript variants encoding different isoforms have been found for this gene. It is possible that alternative splicing of this gene may be physiologically important

Ferrochelatase catalyzes the insertion of the ferrous form of iron into protoporphyrin IX in the heme synthesis pathway, and is localised in the mitochondrion. Defects in ferrochelatase are associated with protoporphyria. Two transcript variants encoding different isoforms have been found for this gene. Porphyrias are a group of inherited or acquired disorders of certain enzymes in the heme biosynthetic pathway (also called porphyrin pathway). They are broadly classified as hepatic porphyrias

The protein encoded by this gene belongs to the EGR family of C2H2-type zinc-finger proteins. It is a nuclear protein and functions as a transcriptional regulator. The products of target genes it activates are required for differentitation and mitogenesis. Studies suggest this is a cancer suppresor gene. [provided by RefSeq].

Plexin A2 is a coreceptor for SEMA3A and is necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton. This coreceptor plays a role in axon guidance, invasive growth and cell migration. Class 3 semaphorins bind to a complex composed of a neuropilin and a plexin in which the plexin modulates the affinity of the complex for specific semaphorins, and its cytoplasmic domain is required for the activation of down-stream signaling events in the cytoplasm.

This gene encodes human lysozyme, whose natural substrate is the bacterial cell wall peptidoglycan (cleaving the beta[1-4]glycosidic linkages between N-acetylmuramic acid and N-acetylglucosamine). Lysozyme is one of the antimicrobial agents found in human milk, and is also present in spleen, lung, kidney, white blood cells, plasma, saliva, and tears. The protein has antibacterial activity against a number of bacterial species. Missense mutations in this gene have been identified in heritable

Mox1 and the glycoprotein gp91-phox are largely related proteins that are essential components of the NADPH oxidase. The superoxide-generating NADPH oxidase is present in phagocytes, neuroepithelial bodies, vascular smooth muscle cells and endothelial cells. It includes a membrane-bound flavocytochrome containing two subunits, gp91-phox and p22-phox, and the cytosolic proteins p47-phox and p67-phox. During activation of the NADPH oxidase, p47-phox and p67-phox migrate to the plasma membra