Hemopexin (HPX) is the plasma protein responsible for scavenging heme, thus preventing heme-mediated oxidative stress and heme-bound iron loss. In addition, hemopexin blocks heme activation of immune receptors and vascular inflammatory processes. It is mainly expressed in liver, the synthesis of which is induced after inflammation. Alterations of plasma hemopexin level have been linked to disorders like atherosclerosis and inflammatory diseases.
Hemopexin is a plasma glycoprotein that binds heme with high affinity. The encoded protein is an acute phase protein that transports heme from the plasma to the liver and may be involved in protecting cells from oxidative stress.
Mediates both influx and efflux of nucleosides across the membrane (equilibrative transporter). It is sensitive (ES) to low concentrations of the inhibitor nitrobenzylmercaptopurine riboside (NBMPR) and is sodium-independent. It has a higher affinity for adenosine. Inhibited by dipyridamole and dilazep (anticancer chemotherapeutics drugs).
The protein encoded by this gene is a membrane receptor for both human hepatitis A virus (HHAV) and TIMD4. The encoded protein may be involved in the moderation of asthma and allergic diseases. The reference genome represents an allele that retains a MTTVP amino acid segment that confers protection against atopy in HHAV seropositive individuals. Three transcript variants encoding the same protein have been found for this gene.
Hepatitis B virus (HBV) capsid assembly is a critical step in the propagation of the virus and is mediated by the core protein. The first cytoplasmic step in the formation of an infectious HBV virion is the formation of a capsid containing pregenomic RNA (pgRNA) and the viral polymerase (Pol). HBV capsid assembly is an attractive target for new antiviral therapies.
ErbB2, also called Neu and Her2, is a transmembrane glycoprotein in the ErbB family of tyrosine kinase receptors for EGF superfamily growth factors. ErbB2 is widely expressed in epithelial cells and over-expressed in a large number of breast carcinomas. ErbB2 has no identified ligands but heterodimerizes with ErbB1/EGF R, ErbB3, or ErbB4 to form higher affinity signaling complexes. The protease ADAM10 releases a 110 kDa soluble fragment of ErbB2 from the cell surface. ErbB2 plays roles in development, cancer, communication at the neuromuscular junction, and regulation of cell growth and differentiation. The ErbB2/ErbB3 heterodimer is expressed in the majority of breast, skin, ovary and gastrointestinal tumors and transduces a highly mitogenic signal in response to neuregulin 1 (NRG1; heuregulin 1) or NRG2. ErbB3, ErbB2 and neuregulin are all required for formation of the sympathetic nervous system.
This gene encodes a member of the epidermal growth factor (EGF) receptor family of receptor tyrosine kinases. This protein has no ligand binding domain of its own and therefore cannot bind growth factors. However, it does bind tightly to other ligand-bound EGF receptor family members to form a heterodimer, stabilizing ligand binding and enhancing kinase-mediated activation of downstream signalling pathways, such as those involving mitogen-activated protein kinase and phosphatidylinositol-3 kinase. Allelic variations at amino acid positions 654 and 655 of isoform a (positions 624 and 625 of isoform b) have been reported, with the most common allele, Ile654/Ile655, shown here. Amplification and/or overexpression of this gene has been reported in numerous cancers, including breast and ovarian tumors.
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