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IKK beta (I-Kappa-B kinase-beta) is a member of the IKK complex which is composed of IKK alpha, IKK beta, IKK gamma and IKAP. Phosphorylation of I-Kappa-B on a serine residue by the IKK complex frees NF-kB from I-Kappa-B and marks it for degradation via ubiquination. IKK beta has been shown to activate NF-kB and phosphorylate IKB alpha and beta. Phosphorylation of 2 sites at the activation loop of IKK beta is essential for activation of IKK by TNF and IL1. Once activated, IKK beta autophos

IKK beta (I-Kappa-B kinase-beta) is a member of the IKK complex which is composed of IKK alpha, IKK beta, IKK gamma and IKAP. Phosphorylation of I-Kappa-B on a serine residue by the IKK complex frees NF-kB from I-Kappa-B and marks it for degradation via ubiquination. IKK beta has been shown to activate NF-kB and phosphorylate IKB alpha and beta. Phosphorylation of 2 sites at the activation loop of IKK beta is essential for activation of IKK by TNF and IL1. Once activated, IKK beta autophos

C-jun (Oncoprotein C-jun) is a component of the transcription factor AP-1 that binds and activates transcription at TRE/AP-1 elements and appears to be a major downstream target of the SAPK/JNK signaling pathway. The transcriptional activity of c-Jun is regulated by phosphorylation at Ser63 and Ser73. Extracellular signals including growth factors, transforming oncoproteins and UV irradiation stimulate phosphorylation of c-Jun at Ser63/73 and activate c-Jun dependent transcription. Mutatio

Adipsin is the mouse homolog of the previously described human complement Factor D, a serine protease, which is now designated human Adipsin. Human Adipsin is highly expressed in and secreted by adipose tissue, and it has also been found in monocytes and macrophages. Rodent Adipsin has only been detected in high levels in adipose tissue. It has been shown that complement factor B, when complexed with activated complement component C3, is cleaved by Adipsin. While low expression of Adipsin ha

The protein encoded by this gene appears to be multifunctional. Along with PCBP-1 and hnRNPK, it is one of the major cellular poly(rC)-binding proteins. The encoded protein contains three K-homologous (KH) domains which may be involved in RNA binding. Together with PCBP-1, this protein also functions as a translational coactivator of poliovirus RNA via a sequence-specific interaction with stem-loop IV of the IRES, promoting poliovirus RNA replication by binding to its 5'-terminal cloverleaf s

The protein encoded by this gene is a member of the RAS superfamily which are small GTP/GDP-binding proteins with an average size of 200 amino acids. The RAS-related proteins of the RAB/YPT family may play a role in the transport of proteins from the endoplasmic reticulum to the Golgi and the plasma membrane. This protein shares 97%, 96%, and 51% similarity with the dog RAB8, mouse MEL, and mouse YPT1 proteins, respectively and contains the 4 GTP/GDP-binding sites that are present in all th