127977 Results for: "Bioss"

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CKLFSF2 isoform 1

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ATF2 is a member of the ATF/CREB family of basic region leucine zipper DNA binding proteins that regulates transcription by binding to a consensus cAMP response element (CRE) in the promoter of various viral and cellular genes. Many of these genes are important in cell growth and differentiation, and in stress and immune responses. ATF2 is a nuclear protein that binds DNA as a dimer and can form dimers with members of the ATF/CREB and Jun/Fos families. It is a stronger activator as a heterodimer with cJun than as a homodimer. Several isoforms of ATF2 arise by differential splicing. The stable native full length ATF2 is transcriptionally inactive as a result of an inhibitory direct intramolecular interaction of its carboxy terminal DNA binding domain with the amino terminal transactivation domain. Following dimerization ATF2 becomes a short lived protein that undergoes ubiquitination and proteolysis, seemingly in a protein phosphatase-dependent mechanism. Stimulation of the transcriptional activity of ATF2 occurs following cellular stress induced by several genotoxic agents, inflammatory cytokines, and UV irradiation. This activation requires phosphorylation of two threonine residues in ATF2 by both JNK/SAP kinase and p38 MAP kinase. ATF2 is abundantly expressed in brain.

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EFR3A is a plasma membrane protein that contains 821 amino acids and belongs to the EFR3 family. EFR3A is alternatively spliced creating three isoforms and is encoded by a gene that maps to human chromosome 8. Human chromosome 8 consists of nearly 146 million base pairs, encodes over 800 genes and is associated with a variety of diseases and malignancies. Schizophrenia, bipolar disorder, Trisomy 8, Pfeiffer syndrome, congenital hypothyroidism, Waardenburg syndrome and some leukaemias and lymphomas are thought to occur as a result of defects in specific genes that map to chromosome 8.

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CCDC18, also known as NY-SAR-41 or dJ717I23.1, is a 1,454 amino acid protein expressed as two isoforms and encoded by a gene mapping to human chromosome 1. Chromosome 1 is the largest human chromosome spanning about 260 million base pairs and making up 8% of the human genome. There are about 3,000 genes on chromosome 1, and considering the great number of genes there are also a large number of diseases associated with chromosome 1. Notably, the rare aging disease Hutchinson-Gilford progeria is associated with the LMNA gene which encodes lamin A. When defective, the LMNA gene product can build up in the nucleus and cause characteristic nuclear blebs. The mechanism of rapidly enhanced aging is unclear and is a topic of continuing exploration. The MUTYH gene is located on chromosome 1 and is partially responsible for familial adenomatous polyposis. Stickler syndrome, Parkinsons, Gaucher disease and Usher syndrome are also associated with chromosome 1. A breakpoint has been identified in 1q which disrupts the DISC1 gene and is linked to schizophrenia. Aberrations in chromosome 1 are found in a variety of cancers including head and neck cancer, malignant melanoma and multiple myeloma.

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Interaction with CADM1 promotes natural killer (NK) cell cytotoxicity and interferon-gamma (IFN-gamma) secretion by CD8+ cells in vitro as well as NK cell-mediated rejection of tumors expressing CADM3 in vivo.

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The homeobox protein, HESX1, which is also known as Rathke’s pouch homeobox, HANF, homeodomain transcription factor, and anterior-restricted homeobox protein is a transcription factor that belongs to the homeodomain family of DNA binding proteins. HESX1 is initially expressed in embryonic stem cells and the primitive forebrain, and is essential for normal development of the eyes and other anterior CNS structures, such as the hypothalamus, the pituitary gland and the olfactory bulbs. The homeobox gene Hesx1 is expressed in the anterior visceral endoderm (AVE), anterior axial mesendoderm (AME), and anterior neural ectoderm (ANE) during early embryogenesis. Mutations in the Hesx1 gene are associated with disorders that are comparable with septo-optic dysplasia (SOD). These disorders are characterized by hypoplasia of the optic nerve, various types of forebrain defects and pituitary hormone deficiencies, including hypothyroidism. Hesx1 also acts as a transcriptional repressor of reporter gene constructs in tissue culture assays.

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Binds copper, nickel, and fatty acids as well as, and bilirubin less well than, serum albumin. Only a small percentage (less than 2%) of the human AFP shows estrogen-binding properties.

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Regulatory component of the cyclin D3-CDK4 (DC) complex that phosphorylates and inhibits members of the retinoblastoma (RB) protein family including RB1 and regulates the cell-cycle during G(1)/S transition. Phosphorylation of RB1 allows dissociation of the transcription factor E2F from the RB/E2F complex and the subsequent transcription of E2F target genes which are responsible for the progression through the G(1) phase. Hypophosphorylates RB1 in early G(1) phase. Cyclin D-CDK4 complexes are major integrators of various mitogenenic and antimitogenic signals. Also substrate for SMAD3, phosphorylating SMAD3 in a cell-cycle-dependent manner and repressing its transcriptional activity. Component of the ternary complex, cyclin D3/CDK4/CDKN1B, required for nuclear translocation and activity of the cyclin D-CDK4 complex.

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Receptor for pituitary gland growth hormone involved in regulating postnatal body growth. On ligand binding, couples to the JAK2/STAT5 pathway (By similarity). The soluble form (GHBP) acts as a reservoir of growth hormone in plasma and may be a modulator/inhibitor of GH signaling. Isoform 2 up-regulates the production of GHBP and acts as a negative inhibitor of GH signaling.

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Adrenodoxin Reductase (ADX Reductase) is a mitochondrial flavoprotein that receives electrons from NADPH and thereby initiates the electron-transport chain serving mitochondrial cytochromes P450. ADX Reductase participates in cholesterol side chain cleavage in all steroidogenic tissues, steroid 11-? hydroxylation in the adrenal cortex, 25-OH-vitamin D3-24 hydroxylation in the kidney and sterol C-27 hydroxylation in the liver. Alternate splicing of ADX Reductase produces two isoforms. Human ADX Reductase maps to human chromosome 17q24-q25.

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Produced by macrophages, IFN-alpha have antiviral activities. Interferon stimulates the production of two enzymes: a protein kinase and an oligoadenylate synthetase.

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Mediates cAMP-dependent signaling triggered by receptor binding to GPCRs. PKA activation regulates diverse cellular processes such as cell proliferation, the cell cycle, and differentiation and regulation of microtubule dynamics, chromatin condensation and decondensation, nuclear envelope disassembly and reassembly, as well as regulation of intracellular transport mechanisms and ion flux. Regulates the abundance of compartmentalized pools of its regulatory subunits through phosphorylation of PJA2 which binds and ubiquitinates these subunits, leading to their subsequent proteolysis (By similarity).

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Two families of mammalian lectin-like adhesion molecules bind glycoconjugate ligands in a sialic acid-dependent manner: the selectins and the sialoadhesins. The sialic acid-binding immunoglobulin superfamily lectins, designated siglecs or sialoadhesins, are immunoglobulin superfamily members recognizing sialylated ligands. The common sialic acids of mammalian cells are N-acetyl-neuraminic acid (Neu5Ac) and N-glycolyl-neuraminic acid (Neu5Gc). Siglec-1 mediates local cell-cell interactions in lymphoid tissues and can be detected at contact points of macrophages with other macrophages, sinus-lining cells and reticulum cells. Siglec-7, highly expressed in monocytes and resident blood cells, but not in parenchymatous cells, mediates inhibition of natural killer cell cytotoxicity. Siglec-9 is closely homologous to Siglec-7; the gene encoding it maps to chromosome 19q13.41 in humans. It is highly expressed in peripheral blood leukocytes (but not eosinophils), liver, bone marrow, placenta and spleen. Siglec-8, a type I membrane protein, is selectively expressed on human eosinophils, basophils and mast cells, where it regulates their function and survival.

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CCT2 is one of eight largely unrelated subunit proteins found in a protein chaperone complex known as the chaperonin-containing TCP-1 (CCT) or TRiC complex. The CCT complex is an abundanct cytoslic component that is credited with helping newly synthesized polypeptides adopt the correct conformation (1). Proteins that fold and assemble with the help of CCT include the cytoskeletal proteins actin and tubulin as well as up to 15% of newly synthesized eukaryotic proteins (2). CCT2 is the β-subunit of the chaperone complex and is one of several CCT proteins that exhibit increased expression in response to stress. This implies that the CCT complex helps cells recover from protein damage by assisting in protein folding and assembly (3). CCT subunit levels also change throughout the cell cycle, with lower proteins levels (and reduced chaperone activity) found during induced cell cycle arrest during at M phase (4). Each CCT subunit is thought to perform a specific function during protein folding and assembly (5); CCT2 exhibits both actin and tubulin binding activities (6,3) but the exact molecular function on this subunit remains uncertain.

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This gene encodes a ubiquitous nuclear protein that stimulates both cell proliferation and differentiation. It is a member of the MADS (MCM1, Agamous, Deficiens, and SRF) box superfamily of transcription factors. This protein binds to the serum response element (SRE) in the promoter region of target genes. This protein regulates the activity of many immediate-early genes, for example c-fos, and thereby participates in cell cycle regulation, apoptosis, cell growth, and cell differentiation. This gene is the downstream target of many pathways; for example, the mitogen-activated protein kinase pathway (MAPK) that acts through the ternary complex factors (TCFs).

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Borrelia burgdorferi is a spirochete and the cause of Lyme disease, a tick transmitted illness of humans and animals. B. burgdorferi may persist in humans and animals for months or years following initial infection, despite a robust humoral immune response. B. burgdorferi resembles other spirochetes in that it is a highly specialized, motile, two-membrane, spiral shaped bacteria which lives primarily as an extracellular pathogen. B. burgdorferi has an unusual genome compared with other eubacteria which includes a linear chromosome approximately one megabase in size and numerous linear and circular plasmids.

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HIV1 performs highly complex orchestrated tasks during the assembly, budding, maturation and infection stages of the viral replication cycle. During viral assembly, the proteins form membrane associations and self-associations that ultimately result in budding of an immature virion from the infected cell. Gag precursors also function during viral assembly to selectively bind and package two plus strands of genomic RNA. HIV1 Gag p17, the HIV1 matrix protein is produced by the digestion of its precursor Gag p55 by HIV1 protease.

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Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form. Activity on G(z)-alpha is inhibited by phosphorylation of the G-protein. Activity on G(z)-alpha and G(i)-alpha-1 is inhibited by palmitoylation of the G-protein.

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Transcriptional activator that regulates the tissue specific expression of multiple genes, especially in pancreatic islet cells and in liver. Required for the expression of several liver specific genes. Binds to the inverted palindrome 5'-GTTAATNATTAAC-3'.

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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 oxygen transport in the brain. Hexacoordinate globin, displaying competitive binding of oxygen or the distal His residue to the iron atom. Not capable of penetrating cell membranes. The deoxygenated form exhibits nitrite reductase activity inhibiting cellular respiration via NO-binding to cytochrome c oxidase. Involved in neuroprotection during oxidative stress. May exert its anti-apoptotic activity by acting to reset the trigger level of mitochondrial cytochrome c release necessary to commit the cells to apoptosis.

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Best vitelliform macular dystrophy, known as Best disease, is an early-onset autosomal dominant condition in which accumulation of lipofuscin-like material within and beneath the RPE leads to progressive loss of central vision. Best disease is frequently a reflection of mutations in the Bestrophin gene, which encodes a protein containing four putative transmembrane domains and localizes to the basolateral plasma membrane of RPE cells. Human Bestrophin forms oligomeric chloride channels that are sensitive to intracellular calcium. Missense mutations at the Bestrophin locus reduces or abolishes Bestrophin protein mediated membrane current. Bestrophin Bestrophin 2,Bestrophin 3, and Bestrophin 4 are transmembrane proteins that contain a high percentage of aromatic residues, a conserved RFP (Arg-Phe-Pro) motif and they function as anion channels.

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Neuropeptides are regulators of synaptic transmission and their effects are mediated by G-protein coupled receptors. NPS (Neuropeptide S) is a 20 amino acid peptide cleaved from a larger precursor that contains a hydrophobic signal peptide and proteolytic cleavage processing sites. The N-terminal residue of NPS is always a serine regardless of the species. NPS is predominantly found in the central nervous system and plays an important role regulating sleep/wake functions, locomotion, arousal/anxiety responses and food intake. NPS functions by binding and activating its receptor, NPSR, and increasing intracellular calcium levels thereby acting as an excitatory transmitter. In addition, NPS stimulates the hypothalamo-pituitary adrenal (HPA) axis via the release of corticotropin-releasing factor (CRF) and arginine vasopressin (AVP). NPS and its receptor NPSR may also play a role in asthma pathogenesis.

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Transcriptional repressor which may play a role in development of the central nervous system (CNS).

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Inhibitory receptor for the CD200/OX2 cell surface glycoprotein. Limits inflammation by inhibiting the expression of proinflammatory molecules including TNF-alpha, interferons, and inducible nitric oxide synthase (iNOS) in response to selected stimuli. Also binds to HHV-8 K14 viral CD200 homolog with identical affinity and kinetics as the host CD200.

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Receptor for the cytotoxic ligand TRAIL. Lacks a cytoplasmic death domain and hence is not capable of inducing apoptosis. May protect cells against TRAIL mediated apoptosis by competing with TRAIL-R1 and R2 for binding to the ligand.

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Synapsin I is a member of the synapsin family. Synapsins are neuronal phosphoproteins which associate with the cytoplasmic surface of synaptic vesicles. Family members are characterized by common protein domains, and they are implicated in synaptogenesis and the modulation of neurotransmitter release, suggesting a potential role in several neuropsychiatric diseases. This member of the synapsin family plays a role in regulation of axonogenesis and synaptogenesis. The protein serves as a substrate for several different protein kinases and phosphorylation may function in the regulation of this protein in the nerve terminal. Mutations of the Synapsin I gene may be associated with X linked disorders with primary neuronal degeneration such as Rett syndrome.

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Nuclear hormone receptor. The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Ligand-dependent nuclear transactivation involves either direct homodimer binding to a palindromic estrogen response element (ERE) sequence or association with other DNA-binding transcription factors, such as AP-1/c-Jun, c-Fos, ATF-2, Sp1 and Sp3, to mediate ERE-independent signaling. Ligand binding induces a conformational change allowing subsequent or combinatorial association with multiprotein coactivator complexes through LXXLL motifs of their respective components. Mutual transrepression occurs between the estrogen receptor (ER) and NF-kappa-B in a cell-type specific manner. Decreases NF-kappa-B DNA-binding activity and inhibits NF-kappa-B-mediated transcription from the IL6 promoter and displace RELA/p65 and associated coregulators from the promoter. Recruited to the NF-kappa-B response element of the CCL2 and IL8 promoters and can displace CREBBP. Present with NF-kappa-B components RELA/p65 and NFKB1/p50 on ERE sequences. Can also act synergistically with NF-kappa-B to activate transcription involving respective recruitment adjacent response elements; the function involves CREBBP. Can activate the transcriptional activity of TFF1. Also mediates membrane-initiated estrogen signaling involving various kinase cascades. Isoform 3 is involved in activation of NOS3 and endothelial nitric oxide production. Isoforms lacking one or several functional domains are thought to modulate transcriptional activity by competitive ligand or DNA binding and/or heterodimerization with the full length receptor. Essential for MTA1-mediated transcriptional regulation of BRCA1 and BCAS3. Isoform 3 can bind to ERE and inhibit isoform 1.

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RUNX3 binds to the core site of murine Leukemia virus, the core sequences in the enhancer of the polyomavirus, and also to the enhancers of the T-cell receptor genes. May be involved in the control of cellular proliferation and/or differentiation (By similarity). Heterodimer of an alpha and a beta subunit. The alpha subunit binds DNA as a monomer and through the Runt domain.DNA-binding is increased by heterodimerization. Interacts with TLE1 and SUV39H1, Subcellular location in Nucleus.

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Endonuclease which cleaves flap structures at the junction between single-stranded DNA and double-stranded DNA. Specific for 5'-overhanging flap structures in which the 5'-upstream of the flap is completely double-stranded. Prefers the blocked-flap structures similar to those occurring at replication forks, in which the 5' single-strand overhang of the flap is double-stranded.