127977 Ergebnisse für: "Bioss"

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GTP-binding protein that functions as an allosteric activator of the cholera toxin catalytic subunit, an ADP-ribosyltransferase. Involved in protein trafficking among different compartments. Modulates vesicle budding and uncoating within the Golgi complex. Deactivation induces the redistribution of the entire Golgi complex to the endoplasmic reticulum, suggesting a crucial role in protein trafficking. In its GTP-bound form, its triggers the association with coat proteins with the Golgi membrane. The hydrolysis of ARF1-bound GTP, which is mediated by ARFGAPs proteins, is required for dissociation of coat proteins from Golgi membranes and vesicles.

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GTP-binding protein that functions as an allosteric activator of the cholera toxin catalytic subunit, an ADP-ribosyltransferase. Involved in protein trafficking among different compartments. Modulates vesicle budding and uncoating within the Golgi complex. Deactivation induces the redistribution of the entire Golgi complex to the endoplasmic reticulum, suggesting a crucial role in protein trafficking. In its GTP-bound form, its triggers the association with coat proteins with the Golgi membrane. The hydrolysis of ARF1-bound GTP, which is mediated by ARFGAPs proteins, is required for dissociation of coat proteins from Golgi membranes and vesicles.

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Bcl-11a genes play crucial roles in lymphopoiesis and influence the progression of hematopoietic malignancies. Disruption of the Bcl-11b locus is linked to T cell acute lymphoblastic leukemia, and the loss of heterozygosity in mice results in T cell lymphoma. Bcl-11 proteins are related C2H2 zinc-finger transcription factors that act as transcriptional repressors. Bcl-11b can interact with the metastasis-associated proteins MTA1 and MTA2 through the amino-terminal region. Bcl-11a is essential for postnatal development and normal lymphopoiesis. The Bcl-11a mouse gene is a common site of retroviral integration in myeloid leukemia, and may function as a leukemia disease gene, in part, through its interaction with Bcl-6.

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MAX is a basic helix-loop-helix, leucine zipper protein that forms heterodimers with MYC and MAD. It is involved in regulating gene expression.

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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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Bcl-11a genes play crucial roles in lymphopoiesis and influence the progression of hematopoietic malignancies. Disruption of the Bcl-11b locus is linked to T cell acute lymphoblastic leukemia, and the loss of heterozygosity in mice results in T cell lymphoma. Bcl-11 proteins are related C2H2 zinc-finger transcription factors that act as transcriptional repressors. Bcl-11b can interact with the metastasis-associated proteins MTA1 and MTA2 through the amino-terminal region. Bcl-11a is essential for postnatal development and normal lymphopoiesis. The Bcl-11a mouse gene is a common site of retroviral integration in myeloid leukemia, and may function as a leukemia disease gene, in part, through its interaction with Bcl-6.

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MAX is a basic helix-loop-helix, leucine zipper protein that forms heterodimers with MYC and MAD. It is involved in regulating gene expression.

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Ig delta chain C region is an allelic product of the human IGHD gene. The two known IGHD alleles, IGHD*01 and IGHD*02, respectively produce isoforms 1, a secreted protein, and 2, a single-pass type I membrane protein. A member of the adaptive immune system, IgD are monomers expressed by activated B cells. Containing 3 Ig-like (immunoglobulin-like) domains, IgD chain C is located on chromosome 14 within the human heavy chain locus, lying on the 3? side of the IgM chain C region from the V-D-J cassette. Polyadenylation at certain sites along the heavy chain locus likely effects the mechanism that determines the alternative splicing event which results in the expression of either IgD chain C or IgM chain C. Some studies have suggested that antigenic coactivation of IgD+ B cells can have a negative influence on bone resorption during infectious events.

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Together with dynein may be involved in spindle assembly and cytokinesis.Tissue specificity:Ubiquitously expressed. Highly expressed in muscle and pancreas and detected at lower levels in brain.

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IGIP.

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Suppresses apoptosis in a variety of cell systems including factor-dependent lymphohematopoietic and neural cells. Regulates cell death by controlling the mitochondrial membrane permeability. Appears to function in a feedback loop system with caspases. Inhibits caspase activity either by preventing the release of cytochrome c from the mitochondria and/or by binding to the apoptosis-activating factor (APAF-1).

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Teneurin-3, also known as Ten-3, TNM3 or ODZ3, is a 2,699 amino acid single-pass type II membrane protein that contains 25 YD repeats, 8 EGF-like domains, 5 NHL repeats and one teneurin N-terminal domain. Localised to the membrane and expressed in brain, testis and ovary, Teneurin-3 exists as a disulfide-liked homodimer that is thought to function as a cellular signal transducer. Additionally, Teneurin-3 may participate in eye-specific patterning in the visual pathway and is required for aligned binocular vision. The gene encoding Teneurin-3 maps to chromosome 4. Representing approximately 6% of the human genome, chromosome 4 contains nearly 900 genes, one of which is the Huntingtin gene, which is found to encode an expanded glutamine tract in cases of Huntington's disease. FGFR-3 is also encoded on chromosome 4 and has been associated with thanatophoric dwarfism, achondroplasia, Muenke syndrome and bladder cancer. Chromosome 4 is also tied to Ellis-van Creveld syndrome, methylmalonic acidemia and polycystic kidney disease.

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Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.

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Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.

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This proteoglycan is a major component of extracellular matrix of cartilagenous tissues. A major function of this protein is to resist compression in cartilage. It binds avidly to hyaluronic acid via an N-terminal globular region.

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This proteoglycan is a major component of extracellular matrix of cartilagenous tissues. A major function of this protein is to resist compression in cartilage. It binds avidly to hyaluronic acid via an N-terminal globular region.

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May be involved in transcriptional regulation of both viral and cellular genes by interacting with the host DNA-binding protein RBPJ.

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FAM59B

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Receptor for TNFSF18. Seems to be involved in interactions between activated T-lymphocytes and endothelial cells and in the regulation of T-cell receptor-mediated cell death. Mediated NF-kappa-B activation via the TRAF2/NIK pathway (By similarity).

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Multifunctional protein that controls proliferation, differentiation and other functions in many cell types. Many cells synthesize TGFB1 and have specific receptors for it. It positively and negatively regulates many other growth factors. It plays an important role in bone remodeling as it is a potent stimulator of osteoblastic bone formation, causing chemotaxis, proliferation and differentiation in committed osteoblasts. Can promote either T-helper 17 cells (Th17) or regulatory T-cells (Treg) lineage differentiation in a concentration-dependent manner. At high concentrations, leads to FOXP3-mediated suppression of RORC and down-regulation of IL-17 expression, favoring Treg cell development. At low concentrations in concert with IL-6 and IL-21, leads to expression of the IL-17 and IL-23 receptors, favoring differentiation to Th17 cells.

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FAM59B

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Receptor for TNFSF18. Seems to be involved in interactions between activated T-lymphocytes and endothelial cells and in the regulation of T-cell receptor-mediated cell death. Mediated NF-kappa-B activation via the TRAF2/NIK pathway (By similarity).

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Isoform 1 and isoform 3 are widely expressed with highest levels in retina and testis, with isoform 1 being the mot abundant in all tissues tested.Involvement in disease:Defects in FAM161A are the cause of retinitis pigmentosa type 28 (RP28) . A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well.

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The cytotoxic action of BPI is limited to many species of Gram-negative bacteria; this specificity may be explained by a strong affinity of the very basic N-terminal half for the negatively charged lipopolysaccharides that are unique to the Gram-negative bacterial outer envelope. Has antibacterial activity against the Gram-nagative bacterium P.aeruginosa, this activity is inhibited by LPS from P.aeruginosa.

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Glycosyltransferases that mediate the regio- and stereoselective transfer of sugars, such as the fucosyltransferases, determine cell surface-carbohydrate profiles, which are essential interfaces for biological recognition processes. Fucosyltransferases (FucTs) catalyze the covalent association of fucose to different positional linkages on sugar acceptor molecules. The carbohydrate moieties that are generated are covalently attached to cell surfaces and are necessary to ensure a surface contour that satisfies a variety of physiological roles. FucT-XI is a 492 amino acid single-pass type II membrane protein that belongs to the glycosyltransferase 10 family. Localizing to Golgi apparatus, FucT-XI may act as a fucosyltransferase and exists as two alternatively spliced isoforms. The gene encoding FucT-XI maps to mouse chromosome 14 A3.

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Catalytic subunit of the KPC complex that acts as E3 ubiquitin-protein ligase. Required for poly-ubiquitination and proteasome-mediated degradation of CDKN1B during G1 phase of the cell cycle.

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Members of the bactericidal/permeability-increasing protein family have antimicrobial properties and bind lipophilic substances, therefore targeting gram-negative bacteria. The bactericidal permeability increasing protein (BPI) is an antibacterial and endotoxin-neutralizing molecule that is abundant in the granules of polymorphonuclear leukocytes (neutrophil granules). Sharing structural and sequence homologies with BPI, BPIL3 (Bactericidal/permeability-increasing protein-like 3) is a 453 amino acid secreted protein that contains the family’s common conserved feature of two cysteine residues that are critical for protein function. While BPIL3 is primarily expressed at low levels in tonsils, it has been found to be upregulated in hypertrophic tonsil tissue, suggesting that it may play a role in the pathogenesis of inflamed disease tissue.

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NPTX1 is a member of the neuronal pentraxin gene family. Neuronal pentraxin 1 is similar to the rat NP1 gene which encodes a binding protein for the snake venom toxin taipoxin. Human NPTX1 mRNA is exclusively localized to the nervous system.

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Rad and Gem related GTP binding protein (REM) is a member of the RGK subfamily of Ras-like GTPases that also includes Rad, REM2 and Gem/Kir. REM is a phosphorylated protein that is highly expressed in cardiac muscle and moderately expressed in lung, kidney and skeletal muscle. REM associates with several 14-3-3 isoforms as well as with calmodulin in a calcium-dependent manner. REM mediates two distinct signal transduction pathways that regulate both cytoskeletal reorganization and voltage-gated calcium channel activity. REM decreases the current that passes through cardiac voltage-gated L-type Ca channels (Ca(V)). Overexpression of REM may result in the development of cytoplasmic processes, reorganization of the Actin cytoskeleton, reduction in focal adhesion size and an elongated or dendritic-like cell morphology.

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NTF97 is involved in nuclear protein import, either by associating itself with an adapter protein (for example, importin-alpha subunit which binds to nuclear localization signals (NLS) in cargo substrates), or by acting autonomously as a nuclear transport receptor (serves as NLS receptor, docking of the importin/substrate complex to the nuclear pore complex).