Human Esterase D is a cytoplasmic serine hydrolase that belongs to the esterase D family. Esterase D is involved in the detoxification of formaldehyde. Esterase D plays a part in a variety of substrates, including O-acetylated sialic acids, which may involves in the recycling of sialic acids. Esterase D is used as a genetic marker for retinoblastoma and Wilson’s disease.
Estrogen Receptor is a major ligand-activated transcription factor belonging to the nuclear hormone receptor superfamily. Estrogen Receptor is composed of several domains important for hormone binding, DNA binding, and activation of transcription. The protein localizes to the nucleus where it may form a homodimer or a heterodimer with estrogen receptor 2. Estrogen and its receptors are essential for sexual development and reproductive function, but they also play a role in other tissues such as bone. Estrogen receptors are also involved in pathological processes including breast cancer, endometrial cancer, and osteoporosis. Alternative splicing results in several transcript variants, which differ in their 5' UTRs and use different promoters.
ETS1 Protein (ETS1) is a nuclear protein that belongs to the ETS family. Members of this family recognize the core consensus DNA sequence GGAA/T in target genes. Proteins function either as transcriptional activators or repressors of numerous genes. They are involved in stem cell development, cell senescence and death, and tumorigenesis. ETS1 is a transcription factor, containing one ETS DNA-binding domain and one PNT (pointed) domain. it has been shown to interact with TTRAP, UBE2I and Death Associated Protein 6.
Ezrin is expressed in cerebral cortex, basal ganglia, hippocampus, hypophysis, and optic nerve. The N-terminus of ezrin contains a FERM domain which is further subdivided into three subdomains. The C-terminus contain a ERM domain. As a member of the ERM protein family, Ezrin serves as an intermediate between the plasma membrane and the actin cytoskeleton. It plays a key role in cell surface structure adhesion, migration, and organization. Ezrin probably involved in connections of major cytoskeletal structures to the plasma membrane. The N-terminal FERM domain strongly binds sodium-hydrogen exchanger regulatory factor (NHERF) proteins (involving long-range allostery). The C-terminal binds to actin, phosphatidylinositol bis-phosphate (PIP2) and membrane proteins like CD44 and ICAM-2. In epithelial cells, Ezrin is required for the formation of microvilli and membrane ruffles on the apical pole. Along with PLEKHG6, Ezrin is required for normal macropinocytosis.
Coagulation factor XIII is the last zymogen to become activated in the blood coagulation cascade. Plasma factor XIII is a heterotetramer composed of 2 A subunits and 2 B subunits. The A subunits have catalytic function, and the B subunits do not have enzymatic activity and may serve as plasma carrier molecules. Platelet factor XIII is composed of just 2 A subunits, which are identical to those of plasma origin. Upon cleavage of the activation peptide by thrombin and in the presence of calcium ion, the plasma factor XIII dissociates its B subunits and yields the same active enzyme, factor XIIIa, as platelet factor XIII. This enzyme acts as a transglutaminase to catalyze the formation of gamma-glutamyl-epsilon-lysine crosslinking between fibrin molecules, thus stabilizing the fibrin clot. Factor XIII deficiency is classified into two categories: type I deficiency, characterized by the lack of both the A and B subunits; and type II deficiency, characterized by the lack of the A subunit alone. These defects can result in a lifelong bleeding tendency, defective wound healing, and habitual abortion.
This gene encodes vitamin K-dependent coagulation factor IX that circulates in the blood as an inactive zymogen. This factor is converted to an active form by factor XIa, which excises the activation peptide and thus generates a heavy chain and a light chain held together by one or more disulfide bonds. The role of this activated factor IX in the blood coagulation cascade is to activate factor X to its active form through interactions with an Ca+2 ions, membrane phospholipids, and factor VIII. Alterations of this gene, including point mutations, insertions and deletions, cause factor IX deficiency, which is a recessive X-linked disorder, also called hemophilia B or Christmas disease. Alternative splicing results in multiple transcript variants encoding different isoforms that may undergo similar proteolytic processing.
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