54116 Results for: "2,3-Dichlorobenzenesulphonyl+chloride&pageNo=48"

Supplier: Bioss

Get4 is a 327 amino acid cytoplasmic protein that exists as two alternatively spliced isoforms. Get4 forms a multiprotein complex, known as the BAT3 complex, with UBL4A, BAT3 and ARSA. The BAT3 complex plays a role in transporting tail-anchored membrane proteins to the endoplasmic reticulum membrane. The gene encoding Get4 maps to human chromosome 7p22.3. Human chromosome 7 houses over 1,000 genes, comprises nearly 5% of the human genome and has been linked to Osteogenesis imperfecta, Pendred syndrome, Lissencephaly, Citrullinemia and Shwachman-Diamond syndrome.

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Required for zonula adherens biogenesis and maintenance. Acts via its interaction with KIAA1543/Nezha, which anchors microtubules at their minus-ends to zonula adherens, leading to the recruitment of KIFC3 kinesin to the junctional site.

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C8orf58 (chromosome 8 open reading frame 58) is a 365 amino acid protein that exists as two alternatively spliced isoforms, which are encoded by a gene that maps to human chromosome 8p21. Consisting of nearly 146 million bases, chromosome 8 encodes about 800 genes. Translocation of portions of chromosome 8 with amplifications of the c-Myc gene are found in some leukemias and lymphomas, and are typically associated with a poor prognosis. Portions of chromosome 8 have been linked to schizophrenia and bipolar disorder. Trisomy 8, also known as Warkany syndrome 2, most often results in early miscarriage but is occasionally seen in a mosaic form in surviving patients who suffer to a varying degree from a number of symptoms including retarded mental and motor development, and certain facial and developmental defects. WRN is a DNA helicase encoded by chromosome 8 and shown defective in those with the early aging disorder Werner syndrome. Chromosome 8 is also associated with Pfeiffer syndrome, congenital hypothyroidism and Waardenburg syndrome.

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In complex with TSC1, inhibits the nutrient-mediated or growth factor-stimulated phosphorylation of S6K1 and EIF4EBP1 by negatively regulating mTORC1 signaling. Acts as a GTPase-activating protein (GAP) for the small GTPase RHEB, a direct activator of the protein kinase activity of mTORC1. Implicated as a tumor suppressor. Involved in microtubule-mediated protein transport, but this seems to be due to unregulated mTOR signaling. Stimulates weakly the intrinsic GTPase activity of the Ras-related proteins RAP1A and RAB5 in vitro. Mutations in TSC2 lead to constitutive activation of RAP1A in tumors.

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The Beta-Amyloid precursor protein (Beta-APP) is a major constituent of the amyloid deposits in patients with Alzheimer’s disease. The Beta-Amyloid precursor is known to interact with several proteins, including X11 and the G heterotrimetric protein APP-BP1. The neuronal, transmembrane protein X11 is known to bind to the ∫-Amyloid precursor protein via a phosphotyrosine binding (PTB) domain, reducing the secretion of cellular Beta-APP and slowing Beta-APP processing pathways. X11 binds specifically to the YENPTY motif, which is involved in the internalization of Beta-APP. Multiple splice varitents of X11 have been identified, including X11å (also designated Mint 1), X11Beta (Mint 2) and X11(Mint 3).

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Degradation in endoplasmic reticulum proteins, also designated Derlins or DERtrins, are crucial for the degradation of misfolded endoplasmic reticulum (ER) luminal proteins. Derlin proteins are multi-pass membrane proteins localizing to the ER. Derlins are involved in transferring misfolded proteins from the ER to the cytosol, where the misfolded proteins are destroyed in an ubiquitin-dependent manner by the proteasome. In the case of cytomegalovirus infection, Derlin-1, as opposed to Derlins-2 and -3, is involved in the export of MHC class I heavy chains from the ER via its interaction with the viral protein US11. Derlins may also be important for cell proliferation.

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The genus Salmonella is a member of the family Enterobacteriaceae. The genus is composed of Gram-negative bacilli that are facultative and flagellated (motile). Salmonellae possess 3 major antigens; the "H" or flagellar antigen (phase 1 & 2), the "O" or somatic antigen (part of the LPS moiety) and the "Vi" or capsular antigen (referred to as "K" in other Enterobacteriaceae). Salmonellae also possess the LPS endotoxin characteristic of Gram-negative bacteria. This LPS is composed of an "O" polysaccharide ("O" antigen) an "R" core and the endotoxic inner "Lipid A". Endotoxins evoke fever and can activate complement, kinin and clotting factors. Until recently the most common cause of food poisoning by Salmonella species was due to S. Typhimurium. As its name suggests, it causes a typhoid-like disease in mice. In humans S. Typhimurium does not cause as severe disease as S. Typhi, and is not normally fatal. The disease is characterized by diarrhea, abdominal cramps, vomiting and nausea, and generally lasts up to 7 days.

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Ubiquitin is an abundant, highly conserved protein found in all eukaryotic cells either free or covalently attached to cellular proteins. The primary function of ubiquitin in mammalian systems is to clear abnormal, foreign, and improperly folded proteins by targeting them for proteosome degradation. UBE2D proteins, including UBE2D1 (ubiquitin-conjugating enzyme E2D1 or UBC5A), UBE2D2 (ubiquitin-conjugating enzyme E2D2 or UBC5B) and UBE2D3 (ubiquitin-conjugating enzyme E2D3 or UBC5C), are E2 ubiquitin-conjugating enzymes that catalyze the ubiquitination of I˚Bå in a phosphorylation and SCFB-TRCP-dependent manner. Specifically, E1 first transfers a ubiquitin residue to the E2 component (a UBE2D protein), and the UBE2D protein then associates with an E3 ubiquitin-protein ligase, which immediately transfers that residue to a protein that is targeted for degradation.

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CCDC146

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Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).

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The protein encoded by this gene is a transforming protein that is related to Rho-specific exchange factors and yeast cell cycle regulators. The expression of this gene is elevated with the onset of DNA synthesis and remains elevated during G2 and M phases. In situ hybridization analysis showed that expression is at a high level in cells undergoing mitosis in regenerating liver. Thus, this protein is expressed in a cell cycle-dependent manner during liver regeneration, and is thought to have an important role in the regulation of cytokinesis. [provided by RefSeq].

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Sequence-specific, AT-rich binding transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis.

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C20orf186

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Autophagy receptor that interacts directly with both the cargo to become degraded and an autophagy modifier of the MAP1 LC3 family. Required both for the formation and autophagic degradation of polyubiquitin-containing bodies, called ALIS (aggresome-like induced structures) and links ALIS to the autophagic machinery. Involved in midbody ring degradation. May regulate the activation of NFKB1 by TNF-alpha, nerve growth factor (NGF) and interleukin-1. May play a role in titin/TTN downstream signaling in muscle cells. May regulate signaling cascades through ubiquitination. Adapter that mediates the interaction between TRAF6 and CYLD (By similarity). May be involved in cell differentiation, apoptosis, immune response and regulation of K(+) channels.

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Involved in both the initiation and regulation of meiosis, mitosis, and postmitotic functions in differentiated cells by phosphorylating a number of transcription factors such as ELK-1. Phosphorylates EIF4EBP1; required for initiation of translation. Phosphorylates microtubule-associated protein 2 (MAP2). Phosphorylates SPZ1. Phosphorylates heat shock factor protein 4(HSF4) (By similarity). Highest levels within the nervous system, expressed in different tissues, mostly in intestine, placenta and lung. Increased expression during development. Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MAP kinase subfamily. Contains 1 protein kinase domain.

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May supply copper to copper-requiring proteins within the secretory pathway, when localised in the trans-Golgi network. Under conditions of elevated extracellular copper, it relocalised to the plasma membrane where it functions in the efflux of copper from cells.

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The Oxysterol-binding protein (OSBP) family of proteins consist of OSBP (OSBP1) and OSBP2 (ORP-4), which share a high overall similarity. OSBPs are involved in lipid metabolism and signal transduction, as well as vesicle transport, and can translocate to the periphery of Golgi membranes when they are bound to oxysterols. The OSBP protein transports sterols from lysosomes to the nucleus, where sterols downregulate the genes for HMG synthetase, HMG-CoA reductase and the low density lipoprotein receptor (LDLR). OSBP localizes to the cytosol and is widely expressed, while OSBP2 is mainly detected in testis, retina and fetal liver. The extracellular signal-regulated kinase (ERK) signaling pathway is controlled by OSBP via its cholesterol-binding properties. OSBP binds with a high affinity to 25-hydroxy-cholesterol (25-HC), a suppressor of cholesterol synthesis gene transcription in cultured cells.

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ZBTB8A

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CNTD

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Phocein is a 225 amino acid protein encoded by the human gene MOBKL3. Phocein belongs to the MOB1/phocein family and is phosphorylated on serine residues. Phocein is a widely expressed, highly conserved intracellular protein. The sequence of Phocein has limited homology to the sigma subunits from Clathrin adaptor complexes and contains an additional stretch bearing a putative SH3-binding domain. Phocein is usually associated with membranes but can be present in the cytosol, where it behaves as a protein complex. Phocein is the major partner of the striatin family members, which are scaffolding proteins involved in signaling and trafficking. Due to its association with Dynamin via direct interactions with nucleotide diphosphate kinase (NDPK) and Eps15, Phocein has been implicated in vesicular trafficking, acting in particular in the endocytic process.

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Seems to have a role in retrograde membrane traffic at the level of the Golgi complex. May function in retrograde transport in neuronal cells.

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Protein kinases are enzymes that transfer a phosphate group from a phosphate donor onto an acceptor amino acid in a substrate protein. By this basic mechanism, protein kinases mediate most of the signal transduction in eukaryotic cells, regulating cellular metabolism, transcription, cell cycle progression, cytoskeletal rearrangement and cell movement, apoptosis, and differentiation. The protein kinase family is one of the largest families of proteins in eukaryotes, classified in 8 major groups based on sequence comparison of their tyrosine (PTK) or serine/threonine (STK) kinase catalytic domains. Epidermal Growth factor receptor (EGFR) is the prototype member of the type 1 receptor tyrosine kinases. EGFR overexpression in tumors indicates poor prognosis and is observed in tumors of the head and neck, brain, bladder, stomach, breast, lung, endometrium, cervix, vulva, ovary, esophagus, stomach and in squamous cell carcinoma.

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Phosphatidate phosphatases are a family of integral membrane glycoproteins that dephosphorylate a variety of lipid phosphates and play a role in signal transduction via the phospholipase D pathway. PAP-2 proteins function independently of Mg2+ and are insensitive to NEM (N-ethylmaleimide) inhibition. The lipid phosphates degraded by this family include ceramide 1-phosphate (C1P), sphingosine 1-phosphate (S1P), phosphatidic acid (PA) and lysophosphatidic acid (LPA). LPPR4 (lipid phosphate phosphatase-related protein type 4), also known as LPR4, PHP1, PRG1 or PRG-1, is a 763 amino acid multi-pass membrane protein that belongs to the PA-phosphatase related phosphoesterase family. Exclusively expressed in neurons, LPPR4 hydrolyzes lysophosphatidic acid (LPA) and facilitates axonal outgrowth during development and regenerative sprouting. LPPR4 exists as two alternatively spliced isoforms and is encoded by a gene located on human chromosome 1p21.2.

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The Src homology 3 (SH3) domain is a highly conserved 60 amino acid protein domain that is organized into a beta-barrel fold consisting of five or six beta strands arranged as two tightly packed anti-parallel beta sheets. This domain is found in proteins that mediate assembly of specific protein complexes and interact with other proteins, specifically recognizing proline-rich regions. BAIAP2L2 (Brain-specific angiogenesis inhibitor 1-associated protein 2-like protein 2) is a 529 amino acid protein containing an SH3 domain, suggesting that it may function as an adaptor protein. BAIAP2L2 also contains an IMD (IRSp53/MIM) domain, which enables the protein to bind to and bundle Actin filaments, as well as bind to membranes and interact with Rac GTPase. There are two named isoforms of BAIAP2L2 which are produced as a result of alternative splicing events.

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Several proteins involved in regulating and executing programmed cell death have been identified in C. elegans. CED-3, a member of the ICE protease/caspase family, and CED-4, a homolog of the mammalian Apaf-1, promote apoptosis. CED-9, a homolog of the mammalian Bcl-2 protein, inhibits cell death. EGL-1 and CED-6 both function as death-promoting proteins, with CED-6 playing a role in the engulfment of apoptotic cells. CED-5 and CED-7 are C. elegans orthologs of the mammalian DOCK180 and ABC transporter proteins, respectively, and also play a role in the engulfment of dying cells.

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Regulator of procaspase-1/CASP1 activation implicated in the regulation of the proteolytic maturation of pro-IL-1beta/IL1B and its release during inflammation. Inhibits the release of IL1B in response to LPS in monocytes. However, unlike CASP1, do not induce NF-kappa-B activation.

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Very active and specific thyroid hormone transporter. Stimulates cellular uptake of thyroxine (T4), triiodothyronine (T3), reverse triiodothyronine (rT3) and diidothyronine. Does not transport Leu, Phe, Trp or Tyr (By similarity).

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Actin-binding protein that enhances membrane ruffling and RAC activation. Enhances the actin-bundling activity of LCP1. Binds calcium. Plays a role in RAC signaling and in phagocytosis. May play a role in macrophage activation and function. Promotes the proliferation of vascular smooth muscle cells and of T-lymphocytes. Enhances lymphocyte migration. Plays a role in vascular inflammation.

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The protein encoded by this gene is constitutively tyrosine phosphorylated in hematopoietic progenitors isolated from chronic myelogenous leukemia (CML) patients in the chronic phase. It may be a critical substrate for p210(bcr/abl), a chimeric protein whose presence is associated with CML. This encoded protein binds p120 (RasGAP) from CML cells. [provided by RefSeq, Jul 2008]

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G-protein coupled receptor for glucagon that plays a central role in the regulation of blood glucose levels and glucose homeostasis. Regulates the rate of hepatic glucose production by promoting glycogen hydrolysis and gluconeogenesis. Plays an important role in mediating the responses to fasting. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Promotes activation of adenylate cyclase. Besides, plays a role in signaling via a phosphatidylinositol-calcium second messenger system.