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There are two forms of glutamic acid decarboxylases (GADs) that exist in brain: GAD-65 (also known as GAD2) and GAD-67 (also known as GAD1, GAD or SCP). GAD-65 and GAD-67 are members of the group II decarboxylase family of proteins and are responsible for catalyzing the rate limiting step in the production of GABA (gamma-aminobutyric acid) from L-glutamic acid. Although both GADs are found in brain, GAD-65 localizes to synaptic vesicle membranes in nerve terminals, while GAD-67 is distributed throughout the cell. GAD-67 is responsible for the basal levels of GABA synthesis. In the case of a heightened demand for GABA in neurotransmission, GAD-65 transiently activates to assist in GABA production. As a member of the group II decarboxylase family, GADL1 (Glutamate decarboxylase-like protein 1) is a 521 amino acid protein that utilizes pyridoxal phosphate as a cofactor for its carboxylase activity. There are two isoforms of GADL1 that exist as a result of alternative splicing events.

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Most upstream protease of the activation cascade of caspases responsible for the TNFRSF6/FAS mediated and TNFRSF1A induced cell death. Binding to the adapter molecule FADD recruits it to either receptor. The resulting aggregate called death-inducing signaling complex (DISC) performs CASP8 proteolytic activation. The active dimeric enzyme is then liberated from the DISC and free to activate downstream apoptotic proteases. Proteolytic fragments of the N-terminal propeptide (termed CAP3, CAP5 and CAP6) are likely retained in the DISC. Cleaves and activates CASP3, CASP4, CASP6, CASP7, CASP9 and CASP10. May participate in the GZMB apoptotic pathways. Cleaves ADPRT. Hydrolyzes the small-molecule substrate, Ac-Asp-Glu-Val-Asp-|-AMC. Likely target for the cowpox virus CRMA death inhibitory protein. Isoform 5, isoform 6, isoform 7 and isoform 8 lack the catalytic site and may interfere with the pro-apoptotic activity of the complex.

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CDC-like kinase 2 (CLK2) belongs to a family of autophosphorylating kinases termed CLK (CDC2/CDC28-like kinases), which have been shown to phosphorylate serine- and arginine-rich (SR) proteins of the spliceosomal complex, and to influence alternative splicing in overexpression systems. Recent findings demonstrated that the CLK kinases activate PTP-1B family members, and this phosphatase may be an important cellular target for CLK action. Mutations in the CLK2 proteins affect organismal features such as development, behavior, reproduction, and aging as well as cellular features such as the cell cycle, apoptosis, the DNA replication checkpoint, and telomere length.

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This gene encodes a member of the ribosomal S6 kinase family of serine/threonine kinases. The encoded protein responds to mTOR (mammalian target of rapamycin) signaling to promote protein synthesis, cell growth, and cell proliferation. Activity of this gene has been associated with human cancer. Alternatively spliced transcript variants have been observed. The use of alternative translation start sites results in isoforms with longer or shorter N-termini which may differ in their subcellular localizations. There are two pseudogenes for this gene on chromosome 17. [provided by RefSeq, Jan 2013].

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Cytoskeletal protein involved in actin-membrane attachment at sites of cell adhesion to the extracellular matrix (focal adhesion).

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Catalyses the cleavage of the pyrrol ring of tryptophan and incorporates both atoms of a molecule of oxygen.

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The Raf family of serine/threonine specific kinases is comprised of three members (aRaf, bRaf, and cRaf) that play a critical role in regulating cell growth and differentiation, and couple growth factor receptor stimulation to nuclear transcription factors via the Ras/mitogen activated protein kinase (MAPK) pathway. cRaf kinase (also known as Raf1) is a small GTPase like kinase of 73 kDa, and is a signal transducer of multiple extracellular stimuli that is regulated by several pathways, and that once activated, phosphorylates MEK which in turn phosphorylates ERK. Raf1 is involved in the transduction of mitogenic signals from the cell membrane to the nucleus. It is part of the Ras dependent signaling pathway from receptors to the nucleus.

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Zinc-finger proteins contain DNA-binding domains and have a wide variety of functions, most of which encompass some form of transcriptional activation or repression. The majority of zinc-finger proteins contain a Krüppel-type DNA binding domain and a KRAB domain, which is thought to interact with KAP1, thereby recruiting histone modifying proteins. Zinc finger and BTB domain-containing protein 43 (ZBTB43), also known as ZNF297B or ZBTB22B, is a 467 amino acid member of the Krüppel C2H2-type zinc-finger protein family. Localized to the nucleus, ZBTB43 contains a BTB domain, also known as a POZ domain, which inhibits DNA binding and mediates homotypic and heterotypic dimerization. Characteristics of the BTB domain and the interaction of ZBTB43 with BDP1 suggest that ZBTB43 functions as a transcription regulator.

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The protein encoded by this gene binds nucleosomal DNA and is associated with transcriptionally active chromatin. Along with a similar protein, HMG17, the encoded protein may help maintain an open chromatin configuration around transcribable genes. [provided by RefSeq, Aug 2011]

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Plays a central role in autophagy. Required for the abcission step in cytokinesis. May play a role in antiviral host defense. Protects against infection by a neurovirulent strain of Sindbis virus.

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NMDA receptor subtype of glutamate-gated ion channels with high calcium permeability and voltage-dependent sensitivity to magnesium. Mediated by glycine. In concert with DAPK1 at extrasynaptic sites, acts as a central mediator for stroke damage. Its phosphorylation at Ser-1303 by DAPK1 enhances synaptic NMDA receptor channel activity inducing injurious Ca2+ influx through them, resulting in an irreversible neuronal death (By similarity).

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Anti-PDI Rabbit Polyclonal Antibody

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The protein encoded by this gene is a member of the MAP kinase family. MAP kinases act as an integration point for multiple biochemical signals, and are involved in a wide variety of cellular processes such as proliferation, differentiation, transcription regulation and development. This kinase is activated by various environmental stresses and proinflammatory cytokines. The activation requires its phosphorylation by MAP kinase kinases (MKKs), or its autophosphorylation triggered by the interaction of MAP3K7IP1/TAB1 protein with this kinase. The substrates of this kinase include transcription regulator ATF2, MEF2C, and MAX, cell cycle regulator CDC25B, and tumor suppressor p53, which suggest the roles of this kinase in stress related transcription and cell cycle regulation, as well as in genotoxic stress response. Four alternatively spliced transcript variants of this gene encoding distinct isoforms have been reported. [provided by RefSeq, Jul 2008]

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Displays several functions associated with host defense: it promotes agglutination, bacterial capsular swelling, phagocytosis and complement fixation through its calcium-dependent binding to phosphorylcholine. Can interact with DNA and histones and may scavenge nuclear material released from damaged circulating cells.

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IFNW1.

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Cardiac muscle myosin is a hexamer consisting of two heavy chain subunits, two light chain subunits, and two regulatory subunits. This gene encodes the alpha heavy chain subunit of cardiac myosin. The gene is located 4 kb downstream of the gene encoding the beta heavy chain subunit of cardiac myosin. Mutations in this gene cause familial hypertrophic cardiomyopathy and atrial septal defect 3.