118486 Results for: "Butelki+i+butle&pageNo=30"

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The protein encoded by this gene is a nuclear transcription factor involved in the activation of the solute carrier family 2 member 4 gene. The encoded protein interacts with another transcription factor, myocyte enhancer factor 2, to activate transcription of this gene. [provided by RefSeq, Jul 2008].

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Dab1, a homolog of the Drosophila Disabled protein, is an adaptor protein involved in neural development. This cytoplasmic protein is tyrosine-phosphorylated during rapid expansion of the developing nervous system, and it is thought to interact with other proteins via a domain similar to the PTB domains of the Shc family. Dab1 has been shown to interact with the SH2 domains of Src, Fyn and Abl (1). Mutations in Dab1 result in widespread abnormalities in the brain, similar to those seen in Reelin mutants (2). Reelin is a secreted protein thought to play a role in directing migrating neurons (3). Evidence suggests that Dab1 functions downstream of Reelin in a signaling pathway involved in positioning cells in the developing brain (4). Dab2 (also designated DOC-2) is a mitogen-responsive phosphoprotein that binds the SH3 domain of Grb2, and it is thought to be a negative regulator of growth (5).

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Essential PPIase that regulates mitosis presumably by interacting with NIMA and attenuating its mitosis-promoting activity. Displays a preference for an acidic residue N-terminal to the isomerized proline bond. Catalyzes pSer/Thr-Pro cis/trans isomerizations. Down-regulates kinase activity of BTK. Can transactivate multiple oncogenes and induce centrosome amplification, chromosome instability and cell transformation. Required for the efficient dephosphorylation and recycling of RAF1 after mitogen activation. Binds and targets PML and BCL6 for degradation in a phosphorylation-dependent manner.

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Smad3 is a 50 kDa member of a family of proteins that act as key mediators of TGF beta superfamily signaling in cell proliferation, differentiation and development. The Smad family is divided into three subclasses: receptor regulated Smads, activin/TGF beta receptor regulated (Smad2 and 3) or BMP receptor regulated (Smad 1, 5, and 8); the common partner, (Smad4) that functions via its interaction to the various Smads; and the inhibitory Smads, (Smad6 and 7). Activated Smad3 oligomerizes with Smad4 upon TGF beta stimulation and translocates as a complex into the nucleus, allowing its binding to DNA and transcription factors. Phosphorylation of the two TGF beta dependent serines 423 and 425 in the C terminus of Smad3 is critical for Smad3 transcriptional activity and TGF beta signaling.

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MPDZ is a 2,042 amino acid peripheral membrane protein that colocalizes with SR-2C on the apical membrane of epithelial choroid plexus cells. Expressed in heart, brain, placenta, liver, skeletal muscle, kidney and pancreas, MPDZ causes clustering of SR-2C, a serotonin receptor, at the cell surface. MPDZ is member of the NMDAR signaling complex that is involved in regulating AMPAR potentiation and synaptic plasticity in excitatory synapses. As a tight junction protein in epithelial cells, MPDZ interacts with SSTR3, a G-protein-coupled receptor, to regulate transepithelial permeability in a pertussis toxin sensitive manner. MPDZ, along with Kir4.2, may form a complex with other proteins in the nephron and regulate ion transport. MPDZ contains one L27 domain and thirteen PDZ domains.

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Cystatin A and cystatin B (also designated PME, CST6, STFB, CPI-B, stefin B and liver thiol proteinase inhibitor) are thiol protease inhibitors that form complexes with papain and the cathepsins B, H, and L. Cystatin A, a cytoplasmic protein, is one of the precursor proteins of the cornified cell envelope in keratinocytes and plays a role in epidermal development and maintenance. Cystatin B protects against intracellular proteases leaking out of lysosomes and is primarily expressed in heart, liver and kidney.

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Spindly/CCDC99

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EDD is a progestin-regulated gene that was isolated from T-47D human breast cancer cells. Based on sequence homology, EDD appears to be a human homolog of the Drosophila hyperplastic discs (hyd) gene, a tumor suppressor gene that is required for control of imaginal disc growth. EDD contains a HECT domain in the carboxy terminus. HECT domain-containing proteins function as ubiquitin-protein ligases, or E3 enzymes. EDD has been shown to bind to ubiquitin, and like other HECT family proteins, may function as an E3 ubiquitin-protein ligase.

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The protein encoded by this gene is part of a complex that is involved in membrane trafficking. The encoded protein is a molecular chaperone that aids in protein folding upon ATP hydrolysis. This protein also plays a role in adipocyte differentiation. Defects in this gene are a cause of Bardet-Biedl syndrome type 12. Two transcript variants encoding the same protein have been found for this gene.

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NAP125, also known as NCKAP1 (NCK-associated protein 1), p125Nap1 or membrane-associated protein HEM-2, is a 1,128 amino acid single pass membrane protein that exists as two alternatively spliced isoforms and belongs to the HEM-1/HEM-2 family. While widely expressed, NAP125 is found at highest levels in heart, brain and skeletal muscle where it regulates Rac-dependent actin remodeling as part of a lamellipodial complex with WAVE2, Abi-1 and CYFIP1. NAP125 localizes to the cytoplasmic side of lamellipodium membrane and is encoded by a gene that maps to human chromosome 2q32.1 and mouse chromosome 2 C3. NAP125 expression is markedly reduced in Alzheimer disease (AD)-affected brains, suggesting a possible role in the disease.

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The protein encoded by this gene is a dual specificity protein kinase that belongs to the MAP kinase kinase family. This kinase specifically activates MAPK8/JNK1 and MAPK9/JNK2, and this kinase itself is phosphorylated and activated by MAP kinase kinase kinases including MAP3K1/MEKK1, MAP3K2/MEKK2,MAP3K3/MEKK5, and MAP4K2/GCK. This kinase is involved in the signal transduction mediating the cell responses to proinflammatory cytokines, and environmental stresses. Multiple alternatively spliced transcript variants encoding distinct isoforms have been found, but only one transcript variant has been supported and defined. [provided by RefSeq].Hsp27, also referred to as the Estrogen regulated 24K protein and HSP28, is one of several small heat shock proteins (HSP) produced by all organisms studied. Hsp27 synthesis is induced by elevated temperature, as well as estrogen in hormone responsive cells. This protein is involved in stress resistance and actin organization. Interestingly, human HSP27 also shares greater than 50% homology with low molecular weight Drosophila HSP's and mammalian a-crystalline lens protein. Because of the estrogen responsive nature of Hsp27, this protein has been studied extensively in human estrogen responsive tissues such as cervix, endometrium and breast tissue. This work has led to the suggestion that Hsp27 may be a useful marker in classifying various hormone sensitive tumors.

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E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Interacts with SMAD1 and SMAD7 in order to trigger their ubiquitination and proteasome-dependent degradation. In addition, interaction with SMAD7 activates autocatalytic degradation, which is prevented by interaction with SCYE1. Forms a stable complex with the TGF-beta receptor-mediated phosphorylated SMAD2 and SMAD3. In this way, SMAD2 may recruit substrates, such as SNON, for ubiquitin-mediated degradation. Enhances the inhibitory activity of SMAD7 and reduces the transcriptional activity of SMAD2. Coexpression of SMURF2 with SMAD1 results in considerable decrease in steady-state level of SMAD1 protein and a smaller decrease of SMAD2 level.

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TLX3 (HOX11L2, RNX) belongs to a family of orphan homeobox genes that encode DNA binding nuclear transcription factors. Members of the HOX11 gene family are characterized by a threonine 47 replacing cytosine in the highly conserved homeodomain. This transcription factor is required for hematopoiesis. It is overexpressed in childhood acute lumphoblastic leukemia.

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Cysteine string proteins (CSPs) are synaptic vesicle-associated, secretory vesicle proteins that are involved in Ca2+-regulated exocytosis of synaptic vesicles and modulation of presynaptic transmembrane calcium fluxes in neuroendocrine and endocrine cell types. CSP contains a J-domain that binds HSP 70/HSC 70 chaperone ATPases and a membrane-targeting, palmitoylated cysteine-rich string region. CSPs may act as molecular chaperones in synapses, and mediate conformational folding of components of the vesicular exocytotic machinery. CSP is involved in the fine tuning of neurotransmission through its interaction with receptor-coupled trimeric GTP binding proteins (G proteins) and N-type Ca2+ channels. Two variants of CSP have been described: CSP1; and the 31 amino acid, C-terminally truncated isoform, CSP2. Subcellular fractionation of insulinoma cells shows CSP1 in granular fractions, while the membrane and cytosol fractions contain predominantly CSP2. The fractions also contain additional proteins, presumably CSP dimers. Furthermore, in various mammalian cell lines (including rat brain) CSP1 expression predominates CSP2 expression.

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TNFRSF14 is a type I membrane protein belonging to the TNF receptor superfamily. This receptor mediates herpes virus entry into cells during infection. TNFRSF14 is able to inhibit the proliferation, activation, and cytokine production of T cells. It has an extracellular domain containing several cysteine-rich repeats and a short cytoplasmic region containing a TRAF (TNF receptor-associated factor) interaction domain. The extracellular domain of TNFRSF14 interacts with the herpes simplex virus envelope glycoprotein D. TNFRSF14 binds two cellular ligands: lymphotoxin alpha and LIGHT. LIGHT is a transmembrane protein expressed and shed from the surface of activated T cells, exhibits inducible expression, and competes with HSV glycoprotein D for HVEM, a receptor expressed by T lymphocytes. The LIGHT:TNFRSF14 interaction controls immune response functions by cell death induction as well as cell activation. TNFRSF14 is expressed by peripheral blood T cells, B cells, monocytes and in various tissues enriched in lymphoid cells.

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Acts as a transcriptional activator: mediates transcriptional activation by binding to E box-containing promoter consensus core sequences 5'-CANNTG-3'. Associates with the p300/CBP transcription coactivator complex to stimulate transcription of the secretin gene as well as the gene encoding the cyclin-dependent kinase inhibitor CDKN1A. Contributes to the regulation of several cell differentiation pathways, like those that promote the formation of early retinal ganglion cells, inner ear sensory neurons, granule cells forming either the cerebellum or the dentate gyrus cell layer of the hippocampus, endocrine islet cells of the pancreas and enteroendocrine cells of the small intestine. Together with PAX6 or SIX3, is required for the regulation of amacrine cell fate specification. Also required for dendrite morphogenesis and maintenance in the cerebellar cortex. Associates with chromatin to enhancer regulatory elements in genes encoding key transcriptional regulators of neurogenesis (By similarity).

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The members of the G-protein-coupled receptor family are distinguished by their slow transmitting response to ligand binding. These seven transmembrane proteins include the adrenergic, serotonin and dopamine receptors. The effect of the signaling molecule can be excitatory or inhibitory depending on the type of receptor to which it binds. b-adrenergic bound to adrenaline activates adenylyl cyclase, while a2-adrenergic receptor bound to adrenaline inhibits adenylyl cyclase. Like the a2-adrenergic receptor, serotonin receptor functions are also mediated by G proteins that inhibit the activity of adenylyl cyclase. The serotonin receptors have been classified into several categories, designated SR-1–7 (5HT1–7). Subtypes within the SR-1 group include SR-1A, -1B, -1D, -1E and -1F.

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C3orf62 (chromosome 3 open reading frame 62) is a 267 amino acid protein encoded by a gene that maps to human chromosome 3p21.31. Chromosome 3 is made up of approximately 214 million bases encoding over 1,100 genes. Notably, there is a chemokine receptor gene cluster and a variety of human cancer related loci on chromosome 3. Particular regions of the chromosome 3 short arm are deleted in many types of cancer cells. Key tumor suppressing genes on chromosome 3 encode apoptosis mediator RASSF1, cell migration regulator HYAL1 and angiogenesis suppressor SEMA3B. Marfan Syndrome, porphyria, von Hippel-Lindau syndrome, osteogenesis imperfecta and Charcot-Marie-Tooth disease are a few of the numerous genetic diseases associated with chromosome 3.

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Exendin 4 is a 39 amino acid peptide found in venom from the Gila monster Helicoderma suspectum. It is a member of the glucagon secretin family of peptide hormones and neuropeptides. Exendin 4 is a potent agonist of the GLP1 receptor and hence a potent stimulator of insulin secretion.

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EGR3 is a member of the early growth response transcription factor family of C2H2 zinc finger proteins (other members EGR1, EGR2 and EGR4). EGR proteins are immediate early proteins, expression of which is swiftly upregulated in response to a wide range of extracellular stimuli. EGR3 is also thought to be involved in development of muscle spindles, and is upregulated in several regions of the brain in response to stress or injury.

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Esterifies acyl-group from acyl-ACP to the sn-1 position of glycerol-3-phosphate, an essential step in glycerolipid biosynthesis.

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HEATR5B.

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Detected at the highest levels in peripheral blood leukocytes and breast cancer cell lines. Found in leukocytes of the myeloid lineage, with the strongest expression observed in granulocytes and no detectable expression in lymphocytes. Expressed in thymic epithelial cells and fibroblasts.Belongs to the SECTM family.

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Receptor for ATP and UTP coupled to G-proteins that activate a phosphatidylinositol-calcium second messenger system. The affinity range is UTP = ATP >ATP-gamma-S >2-methylthio-ATP = ADP.

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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 autophosphorylates which in turn decreases IKK activity and prevents prolonged activation of the inflammatory response. Additionally, IKK beta activity can also be regulated by MEKK1.

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Odorant receptor (Potential). May be involved in taste perception.

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TMPRSS4 is a member of the peptidase S1 family and contains 1 LDL receptor class A domain, 1 peptidase S1 domain and 1 SRCR domain. It is a probable membrane protease capable of activating ENaC and may process sodium channels in endothelial cells. TMPRSS4 is overexpressed in thyroid neoplasms, and splice variants in TMPRSS4 are thought to be linked with different cancers. Three named isoforms are produced by alternative splicing.

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Adapter protein that plays a role in the assembling of signaling complexes, being a link between ABL kinases and actin cytoskeleton. Can form complex with ABL1 and CBL, thus promoting ubiquitination and degradation of ABL1 or with AKT1 and PAK1, thus mediating AKT1-mediated activation of PAK1. Isoform 6 increases water and sodium absorption in the intestine and gall-bladder.

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OGFOD1 antibody is predicted to not cross-react with other TPA1 protein family members. At least two isoforms are known to exist; this antibody will only detect the larger isform.

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ARFGAP1 (ADP-ribosylation factor GTPase-activating protein 1), ARFGAP2 (ADP-ribosylation factor GTPase-activating protein 2) and ARFGAP3 (ADP-ribosylation factor GTPase-activating protein 3) are GTPase-activating proteins (GAP) that are associated with the Golgi apparatus and interact with ADP-ribosylation factor 1 (ARF). These proteins promote hydrolysis of ARF-bound GTP and are required for the dissociation of coat proteins from Golgi-derived membranes and vesicles. Dissociation of the coat proteins is required for the fusion of these vesicles with target compartments. The activity of ARFGAP1, ARFGAP2 and ARFGAP3 is stimulated by phosphoinosides and inhibited by phosphatidylcholine. The genes encoding ARFGAP1, ARFGAP2 and ARFGAP3 map to human chromosomes 20q13.33, 11p11.2 and 22q13.2, respectively.