45955 Results for: "6-Fluoro-4-cyanoquinoline+N-oxide&pageNo=88"

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Making up nearly 6% of the human genome, chromosome 6 contains around 1200 genes within 170 million base pairs of sequence. Deletion of a portion of the q arm of chromosome 6 is associated with early onset intestinal cancer suggesting the presence of a cancer susceptibility locus. Porphyria cutanea tarda is associated with chromosome 6 through the HFE gene which, when mutated, predisposes an individual to developing this porphyria. Notably, the PARK2 gene, which is associated with Parkinson's disease, and the genes encoding the major histocompatiblity complex proteins, which are key molecular components of the immune system and determine predisposition to rheumatic diseases, are also located on chromosome 6. Stickler syndrome, 21-hydroxylase deficiency and maple syrup urine disease are also associated with genes on chromosome 6. A bipolar disorder susceptibility locus has been identified on the q arm of chromosome 6. The C6orf195 gene product has been provisionally designated C6orf195 pending further characterisation.

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SRPK2 belongs to the protein kinase superfamily. It phosphorylates RS domain-containing proteins, such as SFRS1 and SFRS2 on serine residues. It has a role in spliceosome assembly and in mediating the trafficking of splicing factors and appears to mediate HBV core protein phosphorylation which is a prerequisite for pregenomic RNA encapsidation into viral capsids. SRPK2 highly expressed in brain, moderately expressed in heart and skeletal muscle and at low levels in lung, liver, and kidney.

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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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The protein encoded by this gene is secreted and then cleaved to form the 10 aa luteinizing hormone-releasing hormone (LHRH, also known as gonadoliberin-1), and prolactin release-inhibiting factor (also known as GnRH-associated peptide 1). LHRH stimulates the release of luteinizing and follicle stimulating hormones, which are important for reproduction. Mutation in this gene are associated with hypogonadotropic hypogonadism. Alternatively spliced transcript variants have been described for this gene. [provided by RefSeq, Jul 2012].

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This protein is a minor sialoglycoprotein in human erythrocyte membranes. The blood group Gerbich antigens and receptors for Plasmodium falciparum merozoites are most likely located within the extracellular domain. Glycophorin-C plays an important role in regulating the stability of red cells.

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Has glycerophosphoinositol inositolphosphodiesterase activity and specifically hydrolyzes glycerophosphoinositol, with no activity for other substrates such as glycerophosphoinositol 4-phosphate, glycerophosphocholine, glycerophosphoethanolamine, and glycerophosphoserine. Accelerates the program of osteoblast differentiation and growth. May play a role in remodeling of the actin cytoskeleton (By similarity).

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Targets the cAMP-dependent protein kinase (PKA) to the plasma membrane, and permits functional coupling to the L-type calcium channel. The membrane-associated form reduces epithelial sodium channel (ENaC) activity, whereas the free cytoplasmic form may negatively regulate ENaC channel feedback inhibition by intracellular sodium.

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Members of the RAS subfamily of GTPases function in signal transduction as GTP/GDP-regulated switches that cycle between inactive GDP- and active GTP-bound states. Guanine nucleotide exchange factors (GEFs), such as Repac, serve as RAS activators by promoting acquisition of GTP to maintain the active GTP-bound state and are the key link between cell surface receptors and RAS activation. Repac, also known as Rap guanine nucleotide exchange factor 5 (RAPGEF5), is a 580 amino acid protein that is expressed in brain and testis, with weaker expression in heart, placenta, lung, pancreas and small intestine. Existing as two alternatively spliced isoforms, the Repac gene is conserved in cow, mouse and rat. The gene that encodes Repac maps to human chromosome 7p15.3, with high expression of this region linking to positive response to erlotinib therapy for those with non-small-cell lung cancer.

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DACH2 is a transcription factor that is involved in regulation of organogenesis. It seems to be a regulator for SIX1 and SIX6 and may act as a corepressor of SIX6 in regulating proliferation by directly repressing cyclin-dependent kinase inhibitors, including the p27Kip1 promoter. It probably binds to DNA via its DACH box-N domain.

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Receptor for the lysosphingolipid sphingosine 1-phosphate (S1P). S1P is a bioactive lysophospholipid that elicits diverse physiological effect on most types of cells and tissues. Is coupled to both the G(i/0)alpha and G(12) subclass of heteromeric G-proteins (By similarity). May play a regulatory role in the transformation of radial glial cells into astrocytes and may affect proliferative activity of these cells.

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The protein encoded by this gene is a member of the cyclin-dependent protein kinase (CDK) family. CDK family members are highly similar to the gene products of Saccharomyces cerevisiae cdc28, and Schizosaccharomyces pombe cdc2, and are known to be important regulators of cell cycle progression. This kinase is a catalytic subunit of the protein kinase complex that is important for cell cycle G1 phase progression and G1/S transition. The activity of this kinase first appears in mid-G1 phase, which is controlled by the regulatory subunits including D-type cyclins and members of INK4 family of CDK inhibitors.

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SNX2 and SNX4 share a high degree of amino acid similarity with SNX1, as they all contain a characteristic phox homology (PX) domain (4). These proteins are all partially associated with cellular membranes, and they, likewise, associate with EGF, PDGF and insulin receptor tyrosine kinases (2). These nexins are widely expressed and yet have various tissue distribution patterns. Additionally, the sorting nexins can associate with each other and with a variety of other cellular proteins, suggesting that they exist as part of multisubunit complexes (1,5). The related protein, SNX3, comprises a distinct subgroup of nexins that share less sequence similarity outside of the PX domain and have dramatically different binding affinities for the tyrosine kinase receptors (2,6).

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Actin polymerization is required for a variety of cell functions, including chemotaxis, cell migration, cell adhesion, and platelet activation. Cells trigger actin polymerization through either the de novo nucleation of filaments from monomeric actin, the severing of existing filaments to create uncapped barbed ends, or the uncapping of existing barbed ends. The nucleation of actin is a rate-limiting and unfavorable reaction in actin polymerization and therefore requires the involvement of the Arp2/3 complex, which helps create new filaments and promotes the end-to-side cross-linking of actin filaments into the branching meshwork. The Arp2/3 complex consists of the actin-related proteins Arp2 and Arp3, and various other accessory proteins. The Arp2/3 complex promotes actin nucleation by binding the pointed end of actin filaments, or by associating with the side of an existing filament, and nucleates growth in the barbed direction. In addition, the Arp2/3 complex also mediates actin cytoskeletal outgrowths that are regulated by the Rho family of small GTPases. In response to GTP-binding Cdc42, the Arp2/3 complex binds the Cdc42 substrates, namely the WASP proteins, and initiates the formation of lamellipodia and filopodia.

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E3 ubiquitin-protein ligase that mediates polyubiquitination of CD4. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates. May play a role in ubuquitin-dependent protein sorting in developmenting spermatids.

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C22orf29

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Phospholipase C is a key enzyme in phosphatidylinositol (PIP2) metabolism and lipid signaling pathways. The Phospholipase C family consists of 13 isozymes split between six subfamilies. Phospholipase C beta is activated by G protein subunits.

Supplier: Bioss

C6orf115 is a Making up nearly 6% of the human genome, chromosome 6 contains around 1,200 genes within 170 million base pairs of sequence. Deletion of a portion of the q arm of chromosome 6 is associated with early onset intestinal cancer suggesting the presence of a cancer susceptibility locus. Porphyria cutanea tarda is associated with chromosome 6 through the HFE gene which, when mutated, predisposes an individual to developing this porphyria. Notably, the PARK2 gene, which is associated with Parkinson's disease, and the genes encoding the major histocompatiblity complex proteins, which are key molecular components of the immune system and determine predisposition to rheumatic diseases, are also located on chromosome 6. Stickler syndrome, 21-hydroxylase deficiency and maple syrup urine disease are also associated with genes on chromosome 6. A bipolar disorder susceptibility locus has been identified on the q arm of chromosome 6. The C6orf115 gene product has been provisionally designated C6orf115 pending further characterization.

Supplier: Bioss

F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments.

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The human protooncogene JUN is the putative transforming gene of avian sarcoma virus 17, and it encodes a protein which is highly homologous to the viral protein. cJun (previously known as the Fos binding protein p39) and c Fos form a complex in the nucleus. AP 1 (activating protein 1) is a collective term referring to these dimeric transcription factors composed of Jun, Fos or ATF subunits that bind to a common DNA site, the AP1 binding site. AP 1 proteins, mostly the Jun group, regulate the expression and function of cell cycle regulators such as Cyclin D1, p53, p21 (cip1/waf1), p19 (ARF) and p16. Fos and Jun proto oncogene expression is induced transiently by a variety of extracellular stimuli associated with mitogenesis, differentiation processes or depolarization of neurons. JUN has been mapped to 1p32 to p31, a chromosomal region involved in both translocations and deletions in human malignancies.

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BXDC1 is a 306 amino acid protein encoded by the human gene BXDC1. BXDC1 is a nuclear protein that contains one Brix domain. Brix domain containing proteins represent a family of proteins involved in the biogenesis of large ribosomal subunits. The Brix domain is a region with homology to the yeast protein Pitx1 (Ribosome biogenesis protein BRX1). Pitx1 is part of a complex that includes RPF1, RPF2 and SSF1 or SSF2. This complex is required for the biogenesis of the 60S ribosomal subunit.

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Auxiliary subunit of GABA-B receptors that determine the pharmacology and kinetics of the receptor response. Increases agonist potency and markedly alter the G-protein signaling of the receptors by accelerating onset and promoting desensitization.

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This gene encodes a member of the transforming growth factor beta (TGFB) family of cytokines, which are multifunctional peptides that regulate proliferation, differentiation, adhesion, migration, and other functions in many cell types. Many cells have TGFB receptors, and the protein positively and negatively regulates many other growth factors. The secreted protein is cleaved into a latency-associated peptide (LAP) and a mature TGFB1 peptide, and is found in either a latent form composed of a TGFB1 homodimer, a LAP homodimer, and a latent TGFB1-binding protein, or in an active form composed of a TGFB1 homodimer. The mature peptide may also form heterodimers with other TGFB family members. This gene is frequently upregulated in tumor cells, and mutations in this gene result in Camurati-Engelmann disease.

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Poly(ADP-ribosylation) is a method of DNA damage-dependent posttranslational modification that helps to rescue injured proliferating cells from cell death. The PARP (poly(ADP-ribose) polymerase) proteins comprise a superfamily of enzymes that functionally modify histones and other nuclear proteins, thereby preventing cell death. PARPs use NAD+ as a substrate to catalytically transfer ADP-ribose residues onto protein acceptors; a process that, when repeated multiple times, leads to the formation of poly(ADPribose) chains on the protein. The presence of these chains alters the function of the target protein and promotes cell survival. PARP proteins are implicated in a variety of diseases, including cancer, neurodegenerative and inflammatory disorders. PARP-16 is a 322 amino acid poly (ADP-ribose) polymerase protein localized to the membrane. Expressed as three isoforms produced by alternative splicing, PARP-16 contains one PARP catalytic domain.

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C22orf23

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Expressed in brain, kidney, pancreas, placenta, liver, thymus and prostate.

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GALR3 a 368 and 370 amino acid protein in human and rat, respectively, belongs to a family of G protein-coupled receptors that bind the neuropeptide galanin, which is distributed throughout the central and peripheral nervous system, the pituitary gland, the gastrointestinal tract and in the endocrine and exocrine pancreas. GALR3 mRNA is widely distributed, but expressed at low abundance. In human, GALR3 mRNA is highly expressed in the hypothalamus, pituitary and testis, and is expressed to a lesser extent in adrenal gland and pancreas. Rat and human GALR3 co-express with potassium channel subunits GIRK1 and GIRK4. Like GALR1, GALR3 signaling pathways lead to the inhibition of adenylate cyclase and to the activation of potassium channels, which are linked to the regulation of neurotransmitter release. Binding of galanin to galanin receptors results in increased feeding, impaired learning, enhanced opiate analgesia and decreased opiate place preference.

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Docking protein 1 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. Docking protein 1 contains a putative pleckstrin homology domain at the amino terminus and ten PXXP SH3 recognition motifs. Docking protein 2 binds p120 (RasGAP) from CML cells. It has been postulated to play a role in mitogenic signaling.

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The protein encoded by this gene is a member of the PP2C family of Ser/Thr protein phosphatases. PP2C family members are known to be negative regulators of cell stress response pathways. This phosphatase dephosphorylates, and negatively regulates the activities of, MAP kinases and MAP kinase kinases. It has been shown to inhibit the activation of p38 and JNK kinase cascades induced by environmental stresses. This phosphatase can also dephosphorylate cyclin-dependent kinases, and thus may be involved in cell cycle control. Overexpression of this phosphatase is reported to activate the expression of the tumor suppressor gene TP53/p53, which leads to G2/M cell cycle arrest and apoptosis. Three alternatively spliced transcript variants encoding distinct isoforms have been described. [provided by RefSeq, Jul 2008].

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No Data Available.

Supplier: Bioss

Frequent loss of heterozygosity (LOH) at human chromosome 8p22-p21 is associated with various tumors including prostate and breast cancer. The 8p22-p21 region contains the FEZ1 gene, which is altered in tumors of the esophagus, prostate and breast. The FEZ1 protein (also known as leucine zipper putative tumor suppressor or LZTS1) contains a DNA-binding leucine zipper motif. FEZ1 is expressed in normal breast and prostate, but alterations in FEZ1 expression result in abnormal cell growth. The absence of FEZ1 expression is characteristic of breast and prostate cancer cell lines as well as primary breast and pro-state tumors. This absence of FEZ1 may be due to several factors, including mutations in the FEZ1 gene or hypermethylation of the CpG island flanking the FEZ1 promoter region. FEZ1 acts as a negative regulator of cell growth. During cell-cycle progression, FEZ1 localizes to microtubule components and is hyperphosphorylated by cAMP-dependent kinase.