118487 Results for: "Butelki+i+butle&pageNo=30"

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IFI16 is a member of the HIN-200 (hematopoietic interferon-inducible nuclear antigens with 200 amino acid repeats) family of cytokines. The encoded protein contains domains involved in DNA binding, transcriptional regulation, and protein-protein interactions. The protein localises to the nucleoplasm and nucleoli, and interacts with p53 and retinoblastoma-1. It modulates p53 function, and inhibits cell growth in the Ras/Raf signaling pathway. Alternatively spliced transcript variants encoding different isoforms have been found for this gene.

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Converts transient diacylglycerol (DAG) signals into prolonged physiological effects, downstream of PKC. Involved in resistance to oxidative stress (By similarity).

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Members of the transforming growth factor b superfamily bind to a pair of transmembrane proteins, known as receptor types I and II, which contain serine/threonine kinases and associate to form a signaling complex (1). Activin has been shown to bind a heteromeric noncovalent complex, which consists of a type I receptor, ACTR-IA (also designated ACVRI and ALK-2) or ACTR-IB (also designated ALK-4 and SKR2), and a type II receptor, ACTR-IIA (also designated ACVR2A) or ACTR-IIB (also designated ACVR2B) (1-6). Both receptor types are highly expressed in brain (5). The activin receptor family members are thought to mediate distinct effects on gene expression, cell differentiation, and morpho- genesis in a dose dependent fashion (5,6).

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The cystatin superfamily encompasses proteins that contain multiple cystatin-like sequences. Some of the members are active cysteine protease inhibitors, while others have lost or perhaps never acquired this inhibitory activity. There are three inhibitory families in the superfamily, including the type 1 cystatins(stefins), type 2 cystatins and the kininogens. The type 2 cystatin proteins are a class of cysteine proteinase inhibitors found in a variety of human fluids and secretions. The cystatin locus on chromosome 20 contains the majority of the type 2 cystatin genes and pseudogenes. This gene is located in the cystatin locus and encodes a type 2 salivary cysteine peptidase inhibitor. The protein is an S-type cystatin, based on its high level of expression in saliva, tears and seminal plasma. The specific role in these fluids is unclear but antibacterial and antiviral activity is present, consistent with a protective function. [provided by RefSeq, Jul2008].

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The cerebral and vascular plaques associated with Alzheimer's disease are mainly composed of Amyloid beta peptides. beta Amyloid is derived from cleavage of the Amyloid precursor protein and varies in length from 39 to 43 amino acids. beta Amyloid [1-40], beta Amyloid [1-42], and beta Amyloid [1-43] peptides result from cleavage of Amyloid precursor protein after residues 40, 42, and 43, respectively. The cleavage takes place by gamma-secretase during the last Amyloid precursor protein processing step. beta Amyloid [1-40], beta Amyloid [1-42], and beta Amyloid [1-43] peptides are major constituents of the plaques and tangles that occur in Alzheimer's disease. beta Amyloid and peptides have been developed as tools for elucidating the biology of Alzheimer's disease.

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KIF2B belongs to the kinesin-like protein family. It is a plus end-directed microtubule-dependent motor required for spindle assembly and chromosome movement. It also has microtubule depolymerization activity.

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Calcium-activated, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase involved in various cellular processes such as regulation of the B-cell receptor (BCR) signalosome, oxidative stress-induced apoptosis, androgen receptor-dependent transcription regulation, insulin signaling and endothelial cells proliferation. Plays a key role in B-cell activation by regulating BCR-induced NF-kappa-B activation. Mediates the activation of the canonical NF-kappa-B pathway (NFKB1) by direct phosphorylation of CARD11/CARMA1 at 'Ser-559', 'Ser-644' and 'Ser-652'. Phosphorylation induces CARD11/CARMA1 association with lipid rafts and recruitment of the BCL10-MALT1 complex as well as MAP3K7/TAK1, which then activates IKK complex, resulting in nuclear translocation and activation of NFKB1. Plays a direct role in the negative feedback regulation of the BCR signaling, by down-modulating BTK function via direct phosphorylation of BTK at 'Ser-180', which results in the alteration of BTK plasma membrane localization and in turn inhibition of BTK activity. Involved in apoptosis following oxidative damage: in case of oxidative conditions, specifically phosphorylates 'Ser-36' of isoform p66Shc of SHC1, leading to mitochondrial accumulation of p66Shc, where p66Shc acts as a reactive oxygen species producer. Acts as a coactivator of androgen receptor (ANDR)-dependent transcription, by being recruited to ANDR target genes and specifically mediating phosphorylation of 'Thr-6' of histone H3 (H3T6ph), a specific tag for epigenetic transcriptional activation that prevents demethylation of histone H3 'Lys-4' (H3K4me) by LSD1/KDM1A. In insulin signaling, may function downstream of IRS1 in muscle cells and mediate insulin-dependent DNA synthesis through the RAF1-MAPK/ERK signaling cascade. May participate in the regulation of glucose transport in adipocytes by negatively modulating the insulin-stimulated translocation of the glucose transporter SLC2A4/GLUT4.

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Members of the protein-tyrosine phosphatase superfamilycooperate with protein kinases to regulate cell proliferation anddifferentiation. This superfamily is separated into two familiesbased on the substrate that is dephosphorylated. One family, thedual specificity phosphatases (DSPs) acts on both phosphotyrosineand phosphoserine/threonine residues. This gene encodes differentbut related DSP proteins through the use of non-overlapping openreading frames, alternate splicing, and presumed differenttranscription promoters. Expression of the distinct proteins fromthis gene has been found to be tissue specific and the proteins maybe involved in postnatal development of specific tissues. A proteinencoded by the upstream ORF was found in skeletal muscle, whereasthe encoded protein from the downstream ORF was found only intestis. In mouse, a similar pattern of expression was found.Multiple alternatively spliced transcript variants were described,but the full-length sequence of only some were determined.[provided by RefSeq, Jul 2008].

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Probable transcription factor which may play a role in the regulation of specific gene expression within a subset of neuronal lineages. May play a role in determining or maintaining the identities of a small subset of visual system neurons.

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RNF169 contains 1 RING type zinc finger. The exact functions of RNF169 remain unknown.

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Endocytic receptor involved in endocytosis and in phagocytosis of apoptotic cells. Required for early embryonic development. Involved in cellular lipid homeostasis. Involved in the plasma clearance of chylomicron remnants and activated LRPAP1 (alpha 2-macroglobulin), as well as the local metabolism of complexes between plasminogen activators and their endogenous inhibitors. May modulate cellular events, such as APP metabolism, kinase-dependent intracellular signaling, neuronal calcium signaling as well as neurotransmission. Functions as a receptor for Pseudomonas aeruginosa exotoxin A.

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Sequence-specific RNA-binding protein that regulates mRNA cytoplasmic polyadenylation and translation initiation during oocyte maturation, early development and at postsynapse sites of neurons. Binds to the cytoplasmic polyadenylation element (CPE), an uridine-rich sequence element (consensus sequence 5'-UUUUUAU-3') within the mRNA 3'-UTR. In absence of phosphorylation and in association with TACC3 is also involved as a repressor of translation of CPE-containing mRNA; a repression that is relieved by phosphorylation or degradation (By similarity). Involved in the transport of CPE-containing mRNA to dendrites; those mRNAs may be transported to dendrites in a translationally dormant form and translationally activated at synapses (By similarity). Its interaction with APLP1 promotes local CPE-containing mRNA polyadenylation and translation activation (By similarity). Induces the assembly of stress granules in the absence of stress.

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G protein-coupled receptors (GPRs or GPCRs), also known as seven transmembrane receptors, heptahelical receptors, or 7TM receptors, are members of the largest protein family and play a role in many different stimulus-response pathways. G-protein coupled receptors mediate extracellular signals into intracellular signals (G-protein activation). They respond to a great variety of signaling molecules, including hormones, neurotransmitters and other proteins and peptides. GPR proteins are integral seven-pass membrane proteins with some conserved amino acid regions. GPR19, an orphan receptor, shows elevated expression during embyronic development of the nervous sytem as well as in specific regions of adult mouse brain, including the olfactory bulb, the hippocampus, hypothalamic nuclei and the cerebellum. The GPR19 gene maps to a location on chromosome 12, which is a frequent target for rearrangement in cancer cells and involved in childhood acute lymphoblastic leukemia (ALL).

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Human homolog binds ADP-ribosylation factor (ARF) and inhibits ARF dependent phorbol ester induced secretion of matrix metalloproteinase 9 [RGD].

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Inhibitor of protein-phosphatase 1.

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The Crk-I and Crk-II forms differ in their biological activities. Crk-II has less transforming activity than Crk-I. Crk-II mediates attachment-induced MAPK8 activation, membrane ruffling and cell motility in a Rac-dependent manner. Involved in phagocytosis of apoptotic cells and cell motility via its interaction with DOCK1 and DOCK4. May regulate the EFNA5-EPHA3 signaling.

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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. RNF10 (ring finger protein 10), also known as RIE2, is an 811 amino acid protein that localizes to the cytoplasm and contains one RING-type zinc finger. Existing as multiple alternatively spliced isoforms, RNF10 interacts with MOX-2 and is thought to regulate its transcription in schwann cells, possibly playing a role in myelin formation. The gene encoding RNF10 maps to human chromosome 12, which encodes over 1,100 genes and comprises approximately 4.5% of the human genome. Chromosome 12 is associated with a variety of diseases and afflictions, including hypochondrogenesis, achondrogenesis, Kniest dysplasia, Noonan syndrome and Trisomy 12p, which causes facial developmental defects and seizure disorders.

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Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and the neuron-specific chromatin remodeling complex (nBAF complex). During neural development a switch from a stem/progenitor to a post-mitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to post-mitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth (By similarity). Binds DNA non-specifically.

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Organizes filamentous actin into bundles with a minimum of 4.1:1 actin/fascin ratio. Plays a role in the organization of actin filament bundles and the formation of microspikes, membrane ruffles, and stress fibers. Important for the formation of a diverse set of cell protrusions, such as filopodia, and for cell motility and migration.

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Tau proteins are important Promotes microtubule assembly and stability, and might be involved in the establishment and maintenance of neuronal polarity. The C-terminus binds axonal microtubules while the N-terminus binds neural plasma membrane components, suggesting that tau functions as a linker protein between both. Axonal polarity is predetermined by tau localization (in the neuronal cell) in the domain of the cell body defined by the centrosome. The short isoforms allow plasticity of the cytoskeleton whereas the longer isoforms may preferentially play a role in its stabilization. Tau proteins subcellular located in the axons of neurons, in the cytoso l and in association with plasma membrane components. It expressed in neurons. PNS-tau is expressed in the peripheral nervous system while the others are expressed in the central nervous system.

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IL20 is a cytokine structurally related to interleukin 10 (IL10). This cytokine has been shown to transduce its signal through signal transducer and activator of transcription 3 (STAT3) in keratinocytes. A specific receptor for this cytokine is expressed in skin and upregulated dramatically in psoriatic skin, suggesting a role for this protein in epidermal function and psoriasis.

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Fe65L2 is a 486 amino acid protein that contains one WW domain and two PID domains. Binding to the intracellular domain of the ∫-Amyloid precursor protein, Fe65L2 is thought to modulate the internalization and, therefore, the accessibility and function of ∫-Amyloid. Via its ability to control the intracellular accumulation of ∫-Amyloid, Fe65L2 is thought to play a role in the pathogenesis of Alzheimer's disease. Fe65L2 exists as four alternatively spliced isoforms designated isoform I, isoform II, isoform III and isoform IV. Fe65L2 interacts with Amyloid-like protein and is encoded by a gene located on human chromosome 5, which contains 181 million base pairs and comprises nearly 6% of the human genome. Deletion of the p arm of chromosome 5 leads to Cri du chat syndrome, while deletion of the q arm or of chromosome 5 altogether is common in therapy-related acute myelogenous leukemias and myelodysplastic syndrome.

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Protein kinase C (PKC) is a family of serine- and threonine-specific protein kinases that can be activated by calcium and the second messenger diacylglycerol. PKC family members phosphorylate a wide variety of protein targets and are known to be involved in diverse cellular signaling pathways. PKC family members also serve as major receptors for phorbol esters, a class of tumor promoters. Each member of the PKC family has a specific expression profile and is believed to play a distinct role in cells. The protein encoded by this gene is one of the PKC family members. This kinase has been shown to be involved in many different cellular functions, such as neuron channel activation, apoptosis, cardioprotection from ischemia, heat shock response, as well as insulin exocytosis. Knockout studies in mice suggest that this kinase is important for lipopolysaccharide (LPS)-mediated signaling in activated macrophages and may also play a role in controlling anxiety-like behavior. [provided by RefSeq, Jul 2008]

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CCDC37 is a 611 amino acid protein that exists as two alternatively spliced isoforms. The gene encoding CCDC37 maps to human chromosome 3, which is made up of about 214 million bases encoding over 1,100 genes. Notably, there is a chemokine receptor gene cluster and a variety of human cancer related loci on chromosome 3. Particular regions of the chromosome 3 short arm are deleted in many types of cancer cells. Key tumor suppressing genes on chromosome 3 encode apoptosis mediator RASSF1, cell migration regulator HYAL1 and angiogenesis suppressor SEMA3B. Marfan Syndrome, porphyria, von Hippel-Lindau syndrome, osteogenesis imperfecta and Charcot-Marie-Tooth Disease are a few of the numerous genetic diseases associated with chromosome 3.

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Gemin4 is a component of the SMN core complex which, while in the cytoplasm, plays an essential role in ribonucleoprotein (snRNP) assembly, including the biogenesis, delivery and recycling of snRNPs to the spliceosome. In the nucleus, where SMN is required for pre-mRNA splicing, Gemin4 concentrates next to coiled bodies in subnuclear structures called gems, that are highly enriched in splicosomal snRNPs, and in the nucleolus. Deletion or loss-of-function mutations in the SMN lead to the neurodegenerative disease spinal muscular atrophy (SMA). The human Gemin4 maps to chromosome 17p13.

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S adenosylmethionine synthetase catalyzes the formation of S adenosylmethionine from methionine and ATP. In mammalian tissues, there are three distinct forms of AdoMet synthases designated as alpha, beta, and gamma. Alpha and beta are expressed only in adult liver, while gamma is widely distributed in extrahepatic tissues.

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Retinol dehydrogenase with a clear preference for NADP. Converts all-trans-retinol to all-trans-retinal. Has no detectable activity towards 11-cis-retinol, 9-cis-retinol and 13-cis-retinol.

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The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment.

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Participates in Wnt signaling by binding to the cytoplasmic C-terminus of frizzled family members and transducing the Wnt signal to down-stream effectors. Promotes internalization and degradation of frizzled proteins upon Wnt signaling. Plays a role both in canonical and non-canonical Wnt signaling. Plays a role in the signal transduction pathways mediated by multiple Wnt genes (By similarity).

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PLM (FXYD1)is a member of a family of small membrane proteins that share a 35-amino acid signature sequence domain, beginning with the sequence PFXYD and containing 7 invariant and 6 highly conserved amino acids. FXYD2, also known as the gamma subunit of the Na,K-ATPase, regulates the properties of that enzyme. FXYD1 (phospholemman), FXYD2 (gamma), FXYD3 (MAT-8), FXYD4 (CHIF), and FXYD5 (RIC) have been shown to induce channel activity in experimental expression systems. PLM may be phosphorylated by several kinases, including protein kinase A, protein kinase C, NIMA kinase, and myotonic dystrophy kinase. It is thought to form an ion channel or regulate ion channel activity.