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Transcriptional coactivator involved in neuroepithelial stem cell differentiation and neurogenesis. Involved in particular in lens epithelial cell gene regulation and stress responses. May play an important role in lens epithelial to fiber cell terminal differentiation. May play a protective role during stress-induced apoptosis. Isoform 2 is a more general and stronger transcriptional coactivator. Isoform 2 may also act as an adapter to coordinate pre-mRNA splicing. Cellular cofactor for len

LAP3 (leucine aminopeptidase 3), also known as LAPEP or PEPS, is a 519 amino acid protein that localizes to the cytoplasm and belongs to the peptidase M17 family. Existing as a homohexamer, LAP3 uses zinc as a cofactor to catalyze the release of an N-terminal proline from a target peptide and is, therefore, involved in the processing and turnover of intracellular proteins. Multiple isoforms of LAP3 exist due to alternative splicing events. The gene encoding LAP3 maps to human chromosome 4, w

The Sec61 complex is the central component of the protein translocation apparatus of the endoplasmic reticulum (ER) membrane. The protein encoded by this gene and SEC63 protein are found to be associated with ribosome-free SEC61 complex. It is speculated that Sec61-Sec62-Sec63 may perform post-translational protein translocation into the ER. The Sec61-Sec62-Sec63 complex might also perform the backward transport of ER proteins that are subject to the ubiquitin-proteasome-dependent degradation

The 26S proteasome is a multicatalytic proteinase complex with a highly ordered structure composed of 2 complexes, a 20S core and a 19S regulator. The 20S core is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. The 19S regulator is composed of a base, which contains 6 ATPase subunits and 2 non-ATPase subunits, and a lid, which contains up to 10 non-ATPase subunits. Proteasomes are distributed throughout

Caeruloplasmin is a copper binding plasma glycoprotein consisting of a single polypeptide chain. It has a molecular weight of 132kDa and occurs in plasma at a concentration of 150-500 mg/L. Although the physiological functions of Caeruloplasmin are not fully understood it is implicated in a number of possible functions. 95% of plasma copper is bound to Caeruloplasmin, implying some involvement in copper transport. Caeruloplasmin has been described as both an oxidant and an antioxidant, its ex