45952 Results for: "6-Fluoro-4-cyanoquinoline+N-oxide&pageNo=88"

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This gene is a member of the family of serotonin receptors, which are G protein coupled receptors that stimulate cAMP production in response to serotonin (5-hydroxytryptamine). The gene product is a glycosylated transmembrane protein that functions in both the peripheral and central nervous system to modulate the release of various neurotransmitters. Multiple transcript variants encoding proteins with distinct C-terminal sequences have been described. [provided by RefSeq, May 2010]

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The RING-type zinc finger motif is present in a number of viral and eukaryotic proteins and is made of a conserved cysteine-rich domain that is able to bind two zinc atoms. Proteins that contain this conserved domain are generally involved in the ubiquitination pathway of protein degradation. RNF130 (ring finger protein 130), also known as GP, G1RZFP (G1-related zinc finger protein) or GOLIATH, is a 419 amino acid single-pass type I membrane protein that shares similarity with a Drosophila zinc-finger protein found in mesoderm known as g1. RNF130 contains one PA (protease associated) domain and a single RING-type zinc finger. Implicated in the regulation of growth factor withdrawal-induced apoptosis of myeloid precursor cells, RNF130 is encoded by a gene located on human chromosome 5q35.3 and mouse chromosome 11 B1.3.

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The 2'- 5'- oligoadenylate synthetase (OAS) family is comprised of four members: OAS1, OAS2, OAS3 and OASL. These proteins are induced by interferons and function to convert ATP into 2'- 5'- linked oligomers of adenosine in the presence of double-stranded RNA and magnesium ions. Copper, iron and zinc ions strongly inhibit the OAS enzymatic activity, while manganese ions can replace magnesium ions as an activator. The OAS family plays a significant role in the inhibition of cellular protein synthesis, apoptosis and growth, and its members are important factors in viral infection resistance. OAS3, also referred to as p100, contains three adjacent OAS1-like domains and maps to the human chromosome 12q24.2

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TRIM36 (tripartite motif-containing 36), also known as RNF98 (RING finger protein 98), HAPRIN (haploid germ cell-specific RBCC protein) or RBCC728, is a 728 amino acid protein that belongs to the TRIM/RBCC (Ring finger, B box, coiled-coil) family. Predominantly expressed in prostate, testis and brain with weak expression in heart, kidney and lung, TRIM36 contains two B box-type zinc fingers, a SPRY domain, a coiled-coil domain, a fibronectin type-III domain and a RING-type zinc finger; a motif that has zinc-chelating activity and is involved in mediating protein-protein and protein-DNA interactions. Localizing to the cytoplasm and the acrosomal region of germ cells and mature sperm, TRIM36 is believed to play a role in the acrosome reaction and fertilization. In addition, TRIM36 is overexpressed in prostate cancer, suggesting a possible role for TRIM36 in prostate tumorigenesis.

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The cJun proto-oncogene was first identified as the cellular homolog of the avian sarcoma virus vjun oncogene. JunB and JunD have been shown to be almost identical to cJun in their C terminal regions, which are involved in dimerization and DNA binding, whereas their N terminal domains, which are involved in transcriptional activation, diverge. JunB is a transcription factor involved in regulating gene activity following the primary growth factor response. It binds to the DNA sequence 5'-TGA[CG]TCA-3'.

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HEATR4.

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May be involved in transcriptional regulation.

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Nucleotides are important extracellular signaling molecules that mediate several events, such as cell proliferation, differentiation, chemotaxis and cytokine release. The P2 receptor family is activated by the binding of nucleotides and is divided into two subfamilies, designated P2X and P2Y. The P2Y receptor family are G protein-coupled receptors that mediate the effects of extracellular nucleotides, primarily through the activation of phospholipase C (PLC). To some extent, the P2Y receptors can also activate potassium channels or, alternatively, inhibit adenylate cyclase and N-type calcium channels in response to extracellular nucleotides. P2Y10 (purinergic receptor P2Y, G-protein coupled, 10), also known as P2RY10, is a 339 amino acid multi-pass membrane protein that is thought to act as a receptor for purines coupled to G-proteins. P2Y10 is found at low levels in blood leukocytes and is upregulated during promyelocytic cell differentiation.

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Receptor for the cytotoxic ligand TRAIL. Contains a truncated death domain and hence is not capable of inducing apoptosis but protects against TRAIL-mediated apoptosis. Reports are contradictory with regards to its ability to induce the NF-kappa-B pathway. According to PubMed:9382840, it cannot but according to PubMed:9430226, it can induce the NF-kappa-B pathway.

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Has a dual function in spindle-assembly checkpoint signaling and in promoting the establishment of correct kinetochore-microtubule (K-MT) attachments. Promotes the formation of stable end-on bipolar attachments. Necessary for kinetochore localization of BUB1. Regulates chromosome segregation during oocyte meiosis. The BUB1/BUB3 complex plays a role in the inhibition of anaphase-promoting complex or cyclosome (APC/C) when spindle-assembly checkpoint is activated and inhibits the ubiquitin ligase activity of APC/C by phosphorylating its activator CDC20. This complex can also phosphorylate MAD1L1.

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14-3-3 are activates tyrosine and tryptophan hydroxylases in the presence of Ca (2+)/calmodulin-dependent protein kinase II, and strongly activates protein kinase C. Is probably a multifunctional regulator of the cell signaling processes mediated by both kinases. Activates the ADP-ribosyltransferase (exoS) activity of bacterial origin. 14-3-3 proteins are localized in neurons, and are axonally transported to the nerve terminals. They may be also present, at lower levels, in various other eukaryotic tissues. It belongs to the 14-3-3 family.

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The Myc family, including c-Myc-, N-Myc- and L-Myc, are nuclear proteins with relatively short half lives that contribute an important role in cellular processes such as proliferation, differentiation, apoptosis and transformation. The c-Myc protein activates transcription as part of a heteromeric complex with a number of interacting partners, including Max and Mxi 1; however the transforming properties of the Myc proto-oncogene are believed to be associated with Myc-mediated transcriptional repression. A POZ domain Zn finger protein, designated Miz-1 for Myc-interacting Zn finger protein-1, is a specific target of Myc-induced gene repression. Miz-1 interacts with Myc, but not Max or other Myc partners, and binding of Myc to Miz-1 requires the helix-loop-helix domain of Myc and a short amphipathic helix located in the carboxy-terminus of Miz-1. Miz-1 associates with DNA elements on the adenovirus major late and cyclin D1 promoters and activates transcription of both promoters. Expression of Miz-1 induces potent growth arrest function, and this latency is reversed by the addition of Myc.

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FIGNL1 is a 674 amino acid protein belonging to the AAA ATPase family. FIGNL1 exists as a hexamer that undergoes alternative splicing to produce two isoforms. FIGNL1 utilizes magnesium as a cofactor and is phosphorylated upon DNA damage, probably by ATM or ATR. FIGNL1 is suggested to regulate osteoblast proliferation and differentiation. FIGNL1 is encoded by a gene located on human chromosome 7, which consists about 158 milllion bases, encodes over 1000 genes and makes up about 5% of the human genome. Chromosome 7 has been linked to Osteogenesis imperfecta, Pendred syndrome, Lissencephaly, Citrullinemia and Shwachman-Diamond syndrome. The deletion of a portion of the q arm of chromosome 7 is associated with Williams-Beuren syndrome, a condition characterized by mild mental retardation, an unusual comfort and friendliness with strangers and an elfin appearance. Deletions of portions of the q arm of chromosome 7 are also seen in a number of myeloid disorders including cases of acute myelogenous leukemia and myelodysplasia.

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Involved in dendrite morphogenesis and maintenance by regulating lysosomal trafficking via its interaction with MAP6. May act by inhibiting retrograde transport of lysosomes along dendrites. Required for dendrite branching.

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APPBP2 is a hydrophilic, microtubule binding protein that functions in the trafficking of Beta-Amyloid precursor protein. It is expressed in a variety of cell types and localizes to the cytoplasm. APPBP2 shares homology with kinesin light chain. It consists of a coiled-coil domain, PKC phosphorylation sites, four imperfect C-terminal tandem repeats, eight tetratricopeptide repeats and N- and C-terminal globular structures. APPBP2 recognizes and binds to the basolateral sorting sequence (BaSS) present in the cytoplasmic domain of the Beta-Amyloid precursor protein. In addition, APPBP2 interacts with the androgen receptor and suppresses androgen signaling.

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Signaling adapter that couples activated growth factor receptors to signaling pathways. Participates in a signaling cascade initiated by activated KIT and KITLG/SCF. Isoform p46Shc and isoform p52Shc, once phosphorylated, couple activated receptor tyrosine kinases to Ras via the recruitment of the GRB2/SOS complex and are implicated in the cytoplasmic propagation of mitogenic signals. Isoform p46Shc and isoform p52Shc may thus function as initiators of the Ras signaling cascade in various non-neuronal systems. Isoform p66Shc does not mediate Ras activation, but is involved in signal transduction pathways that regulate the cellular response to oxidative stress and life span. Isoform p66Shc acts as a downstream target of the tumor suppressor p53 and is indispensable for the ability of stress-activated p53 to induce elevation of intracellular oxidants, cytochrome c release and apoptosis. The expression of isoform p66Shc has been correlated with life span (By similarity). Participates in signaling downstream of the angiopoietin receptor TEK/TIE2, and plays a role in the regulation of endothelial cell migration and sprouting angiogenesis.

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Summary: This gene encodes a member of the p34Cdc2 protein kinase family. p34Cdc2 kinase family members are known to be essential for eukaryotic cell cycle control. This gene is in close proximity to CDC2L2, a nearly identical gene in the same chromosomal region. The gene loci including this gene, CDC2L2, as well as metalloprotease MMP21/22, consist of two identical, tandemly linked genomic regions which are thought to be a part of the larger region that has been duplicated. This gene and CDC2L2 were shown to be deleted or altered frequently in neuroblastoma with amplified MYCN genes. The protein kinase encoded by this gene could be cleaved by caspases and was demonstrated to play roles in cell apoptosis. Several alternatively spliced variants of this gene have been reported. [provided by RefSeq, Jul 2008].

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IER2.

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ATP citrate lyase is the primary enzyme responsible for the synthesis of cytosolic acetyl-CoA in many tissues. The enzyme is a tetramer (relative molecular weight approximately 440,000) of apparently identical subunits. It catalyzes the formation of acetyl-CoA and oxaloacetate from citrate and CoA with a concomitant hydrolysis of ATP to ADP and phosphate. The product, acetyl-CoA, serves several important biosynthetic pathways, including lipogenesis and cholesterogenesis. In nervous tissue, ATP citrate-lyase may be involved in the biosynthesis of acetylcholine. Two transcript variants encoding distinct isoforms have been identified for this gene. [provided by RefSeq]

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The Annexins constitute a family of structurally-related, relatively abundant proteins that exhibit Ca2+-dependent binding to phospholipids. Annexins function in multiple aspects of cell biology including regulation of membrane trafficking, transmembrane channel activity, inhibition of phospholipase A2, inhibition of coagulation and mediation of cell-matrix interactions. Annexin A13 is considered the original progenitor of the 12 members of vertebrate Annexins. The expression of Annexin A13 is highly tissue-specific, being expressed only in intestinal and kidney epithelial cells. This expression is associated with a highly differentiated intracellular transport function. Two alternative splicing isoforms of Annexin A13 exist, both of which bind to rafts.

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The ADP-ribosylation factor (ARF) protein family are structurally and functionally conserved members of the Ras superfamily of regulatory GTP-binding proteins (1–3). ARFs influence vesicle trafficking and signal transduction in eukaryotic cells (1–3). ARF-dependent regulatory mechanisms include the coordination of spectrin interactions with golgi membranes and the association of actin to the golgi via rho family-dependent G-protein localization (Rac, CDC42) and WASP/Arp2/3 complexes (3–7). Additionally, ARFs play a central role in maintenance of organelle integrity, assembly of coat proteins, and activation of phospholipase D (5–7). The ARF proteins are categorized as class I (ARF1, ARF2,and ARF3), class II (ARF4 and ARF5) and class III (ARF6); members of each class share a common gene organization (8,9). The human ARF6 gene maps to chromosome 7q22.1, contains five exons and four introns, and encodes a 175 amino acid protein (8,9).

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Involved in transcriptional regulation. Transcriptional activity differed among the various isoforms. All isoforms except isoform 3 seem to suppresses the transcriptional activities of AP-1 and p53/TP53.Tissue specificity:Expressed in all tissues examined. Isoforms are differentially expressed. Isoform 3 and isoform 5 were highly expressed, isoform 4 moderately expressed, isoform 2 lower expression, the lowest expression level was seem with isoform 1.

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E3 ubiquitin-protein ligase that plays a role in the control of mitochondrial morphology. Promotes mitochondrial fragmentation and influences mitochondrial localization. Inhibits cell growth. When overexpressed, activates JNK through MAP3K7/TAK1 and induces caspase-dependent apoptosis. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugatin.

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Probable molecular chaperone. Assists the folding of proteins upon ATP hydrolysis. As part of the BBS/CCT complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. May play a role in protein processing in limb, cardiac and reproductive system development. May play a role in cytokinesis.

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Bardet-Biedl syndrome (BBS) is a pleiotropic genetic disorder characterized by obesity, photoreceptor degeneration, polydactyly, hypogenitalism, renal abnormalities, and developmental delay. BBS patients also have an increased risk of developing diabetes, hypertension, and congenital heart defects. BBS is a heterogeneous disorder mapping to eight genetic loci and encoding eight proteins, BBS1-BBS8. Five BBS proteins encode basal body or cilia proteins, suggesting that BBS is a ciliary dysfunction disorder. BBS2 contains two overlapping genes: BBS2L1 and BBS2L2. BBSL1 was re-named BBS7, whereas BBS2L2 independently funcitons as BBS1. BBS7 contains 672 amino acids and is expressed at low to moderate levels in most human tissues.

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GHRH-R is a seven transmembrane domain protein that localizes to the somatotroph of the pituitary. GHRH-R plays an important role in growth and acts as a high-affinity receptor for GHRH. Binding of GHRH leads to the coupling of GHRH-R to G-protein which stimulates increased adenylyl cyclase activity and the accumulation of cAMP leading to the synthesis and release of growth hormone and somatotroph proliferation. In addition, this signalling pathway may have direct action in fetal/placental development, reproduction and immune function. GHRH and GHRH-R may also play a role in the regulation of non-rapid eye movement sleep (NREMS). The expression of GHRH-R is dependent on the presence of the POU domain factor Pit-1. Mutations in the gene encoding this protein can result in isolated growth hormone deficiency (IGHD), also known as Dwarfism of Sindh, and anterior pituitary hypoplasia (APH).

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GEFT is a 580 amino acid cytoplasmic protein that is highly expressed in excitable tissues such as brain, heart and muscle, and weakly expressed in small intestine, colon, liver, placenta and lung. GEFT may play a role in actin cytoskeleton reorganization in different tissues since its activation induces formation of actin stress fibers. GEFT works as a guanine nucleotide exchange factor for the Rho family of small GTPases and links specifically to G alpha q/11-coupled receptors in Rho A activation. GEFT is an important regulator of processes involved in axon and dendrite formation. Involved in skeletal myogenesis, GEFT seems to be an exchange factor primarily for Rac 1 in neurons. Existing as two alternatively spliced variants, GEFT contains a DH (DBL-homology) domain and a PH domain.

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This gene encodes a member of the glycogenin family. Glycogenin is a glycosyltransferase that catalyzes the formation of a short glucose polymer from uridine diphosphate glucose in an autoglucosylation reaction. This reaction is followed by elongation and branching of the polymer, catalyzed by glycogen synthase and branching enzyme, to form glycogen. This gene is expressed in muscle and other tissues. Mutations in this gene result in glycogen storage disease XV. This gene has pseudogenes on chromosomes 1, 8 and 13 respectively. Alternatively spliced transcript variants encoding different isoforms have been identified.[provided by RefSeq, Sep 2010].

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FBXO36 is a 188 amino acid protein that contains one forty amino acid F-box region, making it a member of the F-box family. F-box proteins are critical components of the SCF (Skp1-CUL-1-F-box protein) type E3 ubiquitin ligase complex and are involved in substrate recognition and recruitment for ubiquitination. F-box proteins are members of a large family that regulates cell cycle, immune response, signaling cascades and developmental programs by targeting proteins, such as cyclins, cyclin-dependent kinase inhibitors, IkB-å and ∫-catenin, for degradation by the proteasome after ubiquitination. Functioning as a component of the SCF complex, FBXO36 is thought to recognize and bind to select phosphorylated proteins, thereby promoting their ubiquitination and subsequent degradation.

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Component of triglyceride-rich very low density lipoproteins (VLDL) and high density lipoproteins (HDL) in plasma. Plays a multifaceted role in triglyceride homeostasis. Intracellularly, promotes hepatic very low density lipoprotein 1 (VLDL1) assembly and secretion; extracellularly, attenuates hydrolysis and clearance of triglyceride-rich lipoproteins (TRLs). Impairs the lipolysis of TRLs by inhibiting lipoprotein lipase and the hepatic uptake of TRLs by remnant receptors.