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The protein encoded by this gene is a pyruvate kinase that catalyzes the production of phosphoenolpyruvate from pyruvate and ATP. This protein has been shown to interact with thyroid hormone, and thus may mediate cellular metabolic effects induced by thyroid hormones. This protein has been found to bind Opa protein, a bacterial outer membrane protein involved in gonococcal adherence to and invasion of human cells, suggesting a role of this protein in bacterial pathogenesis. Three alternative

A20 is a Cys2/Cys2 zinc finger protein that is induced by a variety of inflammatory stimuli and regulates gene expression. Specifically, A20 is induced by tumor necrosis factor (TNF) and interleukin 1 (IL-1), and acts as a negative regulator of nuclear factor κ B (NFκB) gene expression. By inhibiting NFκB activation, A20 plays a critical role in terminating NFκB responses to various stimuli. Although the C-terminal region of A20 contains seven zinc finger domains, only four of these doma

PARK7/DJ1 is a ubiquitously expressed protein involved in various cellular processes including cell proliferation, RNA-binding, and oxidative stress. The protein has been found to colocalize within a subset of pathologic tau inclusions in a diverse group of neurodegenerative disorders known as tauopathies (Rizzu et al. 2004). Defects in PARK7/DJ1 are the cause of autosomal recessive early-onset Parkinson's disease 7 (PARK7). Parkinson's disease (PD) is a complex, multifactorial disorder that

Nuclear factor kappa B (NFkB) is a ubiquitous transcription factor and an essential mediator of gene expression during activation of immune and inflammatory responses. NFkB mediates the expression of a great variety of genes in response to extracellular stimuli including IL1, TNF alpha, and bacterial product LPS. NFkB is associated with IkB proteins in the cell cytoplasm, which inhibit NFkB activity. IKK is a serine protein kinase, and the IKK complex contains alpha and beta subunits (IKK

This gene encodes a protein that is a member of the dickkopf family. It is a secreted protein with two cysteine rich regions and is involved in embryonic development through its inhibition of the WNT signaling pathway. Elevated levels of DKK1 in bone marrow plasma and peripheral blood is associated with the presence of osteolytic bone lesions in patients with multiple myeloma. [provided by RefSeq, Jul 2008]

The ILK protein is important in different biological pathways such as cell adhesion, anchorage-dependent cell cycle progression, oncogenic transformation, and growth factor signaling. The kinase activity of ILK is low in non-activated cells; its activity is stimulated by cell-ECM interactions and by certain growth factors. 3 Negative regulation of ILK is mediated by two phosphatases: PTEN, a tumor suppressor lipid sphatase, and ILKAP, a PP2C protein phosphatase. In tumor cells that do not ex