118481 Results for: "Zamra\\u017Carki+kriogeniczne,+skrzyniowe&pageNo=30"

Supplier: Bioss

Netrin proteins are a family of laminin-related secreted proteins that provide guidance signals for axonal growth and cell migration during development. Netrin signaling is dependent on the concentration of calcium outside the cell and the level of PKA activity. In axonal cells, a reduction in PKA activity converts the responsiveness of the axons to the netrin proteins as the cells are repelled, rather than attracted, by the netrin gradient. Neogenin serves as the primary guidance receptor for netrin-3. Netrin-2 and the corresponding mouse homolog netrin-3 are expressed primarily in the lower two-thirds of the spinal cord, and, like netrin-1, they can either attract or repel commissural axons at a distance. Netrin-3 proteins are associated with the axon fibers projecting from motor neurons and from neurons within sympathetic and sensory ganglia, suggesting that netrin-3 may be involved in pathfinding and fasciculation of axon projection. Neogenin serves as the primary guidance receptor for netrin-3. During peripheral nerve development, high netrin-3 expression has been detected in mesenchymal cells, sensory ganglia and muscles. In humans, the gene encoding for the netrin-3 protein is localized to chromosome 16p13.3.

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MIP1 alpha and MIP1 beta were originally co-purified from medium conditioned by an LPS-stimulated murine macrophage cell line. Human MIP1 beta refers to the products of several independently cloned cDNAs, including Act2, PAT 744, hH400, G26, HIMAP, HC21, and MAD 5a. The predicted protein products of these cDNAs represent variants that are between 94% - 98% identical and these proteins are all approximately 75% homologous to murine MIP1 beta. MIP1 beta also shares approximately 70% amino acid identity with MIP1 alpha. MIP1 proteins are expressed primarily in T cells, B cells, and monocytes after antigen or mitogen stimulation. The MIP1 proteins have chemoattractant and adhesive effects on lymphocytes, with MIP1 alpha and MIP1 beta preferentially attracting CD8+ and CD4+ T cells, respectively. A signal transducing receptor designated the CC chemokine receptor 1 (CC CKR1) with seven transmembrane domains that binds MIP1 alpha, MIP1 beta, MCP1 and RANTES with varying affinities has been isolated.

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C5orf35 is a With 181 million base pairs encoding around 1,000 genes, chromosome 5 is about 6% of human genomic DNA. It is associated with Cockayne syndrome through the ERCC8 gene and familial adenomatous polyposis through the adenomatous polyposis coli (APC) tumor suppressor gene. Treacher Collins syndrome is also chromosome 5 associated and is caused by insertions or deletions within the TCOF1 gene. Deletion of the p arm of chromosome 5 leads to Cri du chat syndrome. Deletion of 5q or chromosome 5 altogether is common in therapy-related acute myelogenous leukemias and myelodysplastic syndrome. The C5orf35 gene product has been provisionally designated C5orf35 pending further characterization.

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HGFA Inhibitor 1 is an endogenous inhibitor of the kunitz-type serine proteinase HGF-activator (HGFA). HGF was first described as a hepatocyte-specific mitogen and survival factor, and has since been shown to exert a variety of actions on many cell types by binding to its MET receptor. HGF is activated by cleavage of the single-chain form to form a two-chain version by HGFA. HGFA Inhibitor 1 also inhibits trypsin, and MTSP-1 (Matriptase), a serine proteinase that also activates HGF. HGFB Inhibitor 1 is a splice variant of HGFA Inhibitor 1, and contains a 16 amino acid insert after the first kringle domain, relative to the HGFA Inhibitor 1 sequence.

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Extracellular matrix protein implicated in guidance of migrating neurons as well as axons during development, synaptic plasticity as well as neuronal regeneration. Promotes neurite outgrowth from cortical neurons grown on a monolayer of astrocytes. Ligand for integrins alpha-8/beta-1, alpha-9/beta-1, alpha-V/beta-3 and alpha-V/beta-6.

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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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This gene belongs to the chemokine-like factor gene superfamily, a novel family that is similar to the chemokine and the transmembrane 4 superfamilies. This gene is one of several chemokine-like factor genes located in a cluster on chromosome 3. This gene is widely expressed in many tissues, but the exact function of the encoded protein is unknown. [provided by RefSeq, Jul 2008].

Supplier: Bioss

The leucine-rich repeat-containing protein 6 (LRRC6), also designated Leucine-rich testis-specific protein (LRTP), is a 466 amino acid protein that contains 3 LRR repeats and plays a role in spermatogenesis. The gene encoding LRRC6 maps to chromosome 8, which encodes approximately 800 genes. Translocation of portions of chromosome 8 with amplifications of the c-Myc gene are found in some leukemias and lymphomas, and typically associated with a poor prognosis. Chromosome 8 is also associated with Trisomy 8, Pfeiffer syndrome, congenital hypothyroidism and Waardenburg syndrome.

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DQX1 (DEAQ box RNA-dependent ATPase 1), also known as FLJ23757, is a 71 amino acid protein that contains one helicase ATP-binding domain and one helicase C-terminal domain. Localized to the nucleus, DQX1 catalyzes the conversion of ATP to ADP and a phosphate. Expressed as three isoforms produced by alternative splicing events, DQX1 is encoded by a gene that maps to human chomosome 2. As the second largest human chromosome, chromosome 2 makes up approximately 8% of the human genome and contains 237 million bases encoding over 1,400 genes. A number of genetic diseases are linked to genes on chromosome 2, including Harlequin icthyosis, sitosterolemia and Alstré°‰ syndrome.

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Probable transcription factor. Could be involved in thyroid gland organogenesis.

Supplier: Bioss

Adapter protein which mediates the IRAK1 and TRAF6 interaction following IL-1 stimulation, resulting in the downstream activation of NF-kappa-B and AP-1 pathways. Induces the oligomerization and polyubiquitination of TRAF6, which leads to the activation of TAK1 and IKK through a proteasome-independent mechanism.

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Troponin I is the inhibitory subunit of troponin, the thin filament regulatory complex which confers calcium-sensitivity to striated muscle actomyosin ATPase activity.

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Chromosome 16 encodes over 900 genes in approximately 90 million base pairs, makes up nearly 3% of human cellular DNA and is associated with a variety of genetic disorders. The GAN gene is located on chromosome 16 and, with mutation, may lead to giant axonal neuropathy, a nervous system disorder characterized by increasing malfunction with growth. The rare disorder Rubinstein-Taybi syndrome is also associated with chromosome 16, though through the CREBBP gene which encodes a critical CREB binding protein. Signs of Rubinstein-Taybi include mental retardation and predisposition to tumor growth and white blood cell neoplasias. Crohn's disease is a gastrointestinal inflammatory condition associated with chromosome 16 through the NOD2 gene. An association with systemic lupus erythematosis and a number of other autoimmune disorders with the pericentromeric region of chromosome 16 has led to the identification of SLC5A11 as a potential autoimmune modifier. The KIAA1576 gene product has been provisionally designated KIAA1576 pending further characterization.

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Sodium permeable non-voltage-sensitive ion channel inhibited by the diuretic amiloride. Mediates the electrodiffusion of the luminal sodium (and water, which follows osmotically) through the apical membrane of epithelial cells. Plays an essential role in electrolyte and blood pressure homeostasis, but also in airway surface liquid homeostasis, which is important for proper clearance of mucus. Controls the reabsorption of sodium in kidney, colon, lung and sweat glands. Also plays a role in taste perception.

Supplier: Bioss

CCRK contains a kinase domain most closely related to the cyclin-dependent protein kinases. The encoded kinase activates CDK2 and is involved in cell growth.

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ADAM13 was first described as a protein expressed in somatic mesoderm and neural crest cells, in developing Xenopus embryos. ADAM13 was also found in liver, heart, and intestines from adult Xenopus. ADAM13 may regulate cellular signaling via Src and Src tyrosine kinase. ADAM13 may also act as a cell attachment molecule, by binding integrins through the cysteine rich domain amoung many other roles. A member of the metalloproteinase family containing disintegrin like domains (ADAMs) the functions of ADAM13 are still poorly understood. ADAM13 contains the canonical HExxHxxxxxH zinc metalloproteinase motif, as well as disintegrin, cysteine rich, EFG like, transmembrane and Cytoplasmic domains. ADAM13 has been shown to be proteolytically active, cleaving fibronectin after binding it to the EGF like domain. ADAM13 is also shed from cells in culture, cleaved aminoterminal from the transmembrane domain, and is released into the culture media. Shed ADAM13 is a 52 kD protein, and can form complexes with a2 macroglobulin, suggesting it is a competent protease. Xenopus ADAM13 has greatest homology with human ADAM 33 (51% identical), and is 46% identical with human or mouse ADAM12 or ADAM19. It is still unclear if any of these ADAMs are species orthologs of Xenopus ADAM13, but there are significant differences between the related sequences, suggesting that ADAM13 may be a unique protein. The full length Xenopus ADAM13 sequence codes for a 914 amino acid protein. Predicted mass is 99.749 kD, but glycosylation and cyteine rich regions give Xenopus ADAM13 an apparent MW of 120 kD unprocessed, and 97 kD processed forms, on reduced SDS PAGE gels. ADAM13 contains a putative furin cleavage site, suggesting that a prohormone convertase cleaves the propeptide domain away from the catalytic domain

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Zinc-finger proteins contain DNA-binding domains and have a wide variety of functions, most of which encompass some form of transcriptional activation or repression. The majority of zinc-finger proteins contain a Krüppel-type DNA binding domain and a KRAB domain, which is thought to interact with KAP1, thereby recruiting histone modifying proteins. Zinc finger and BTB domain-containing protein 5 (ZBTB5) is a 677 amino acid member of the Krüppel C2H2-type zinc-finger protein family. Localized to the nucleus, ZBTB5 contains a BTB domain, also known as a POZ domain, which inhibits DNA binding and mediates homotypic and heterotypic dimerization. Characteristics of the BTB domain suggest that ZBTB5 functions as a transcription regulator.

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This gene product is highly similar to Schizosaccharomyces pombe rad9, a cell cycle checkpoint protein required for cell cycle arrest and DNA damage repair in response to DNA damage. This protein is found to possess 3' to 5' exonuclease activity, which may contribute to its role in sensing and repairing DNA damage. It forms a checkpoint protein complex with RAD1 and HUS1. This complex is recruited by checkpoint protein RAD17 to the sites of DNA damage, which is thought to be important for triggering the checkpoint-signaling cascade. Use of alternative polyA sites has been noted for this gene. [provided by RefSeq].

Supplier: Bioss

Filamins are Actin-binding proteins which contain an N-terminal Actin-binding domain, a membrane glycoprotein domain and a C-terminal self-association domain. Filamins help reshape the cytoskeleton by forming flexible cross-links between two Actin filaments, which maintain membrane integrity during force application. Filamins also participate in signal transduction pathways associated with cell motility, adhesion, differentiation and survival, and force transduction. The filamin family is comprised of Filamin 1, Filamin 2 and Filamin 3. Filamin 2, also designated Filamin C, is a skeletal- and cardiac-muscle specific form of Filamin, which binds ©-sarcoglycan and ∂-sarcoglycan, but not å-sarcoglycan or ∫-sarcoglycan. Muscular dystrophy, an inherited group of disorders resulting in progressive weakness of muscles in the body, is associated with irregular subcellular localization of Filamin 2 caused by a deficiency in KY, a protein that interacts with Filamin 2.

Supplier: Bioss

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.

Supplier: Bioss

p53 binding protein 1 (53BP1) plays a critical role in tumor suppression and is a putative substrate of ATM kinase. Upon DNA damage, it is phosphorylated and relocalizes to the presumptive sites of damage, p53 binding protein 1 (53BP1) plays a critical role in tumor suppression and is a putative substrate of ATM kinase. Upon DNA damage, it is phosphorylated and relocalizes to the presumptive sites of damage, specifically, double strand breaks. This also suggests a role in DNA repair, maintaining genomic stability.

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Esophagin, also known as small proline-rich protein 3 (SPR3) or Cornifin ∫, belongs to the cornifin family of cornified-envelope structural proteins. It is expressed in mucosal epithelia such as esophagus and tongue and is strongly induced during epidermal keratinocyte differentiation. Due to its highly inducible nature, Esophagin is considered a marker of squamous differentiation. Esophagin serves as a cross-linking protein within the cornified cell envelope and may play a role in the maintenance of normal esophageal epithelial homeostasis. It shares significant homology with the related proteins, SPRR1 and SPRR2. Esophagin is typically not expressed in healthy human epithelium, but its expression is upregulated in numerous hyperproliferative disorders of the skin. Contrastly, its expression is dramatically downregulated in esophageal squamous cell carcinoma.

Supplier: Bioss

Prostaglandin inactivation. Contributes to the regulation of events that are under the control of prostaglandin levels. Catalyzes the NAD-dependent dehydrogenation of lipoxin A4 to form 15-oxo-lipoxin A4. Inhibits in vivo proliferation of colon cancer cells.

Supplier: Bioss

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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Na+/H+ exchangers (NHEs) catalyze the transport of Na+ in exchange for H+ across membranes in organisms and are required for numerous physiological processes. NHEDC2 (Na+/H+ exchanger-like domain-containing protein 2), also known as NHA2, is a 537 amino acid mitochondrial protein. NHEDC2 is involved in organelle volume homeostasis by catalyzing the exchange of protons for Na+ and Li+ across the inner mitochondrial membrane. Found in red blood cells, NHEDC2 is required for bone resorption activity and osteoclast differentiation. As a multi-pass membrane protein, NHEDC2 is expressed as two isoforms produced by alternative splicing events.

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Phosphatidylinositol (PtdIns) phosphatase that specifically hydrolyzes the 5-phosphate of phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3) to produce PtdIns(3,4)P2, thereby negatively regulating the PI3K (phosphoinositide 3-kinase) pathways. Plays a central role in regulation of PI3K-dependent insulin signaling, although the precise molecular mechanisms and signaling pathways remain unclear. While overexpression reduces both insulin-stimulated MAP kinase and Akt activation, its absence does not affect insulin signaling or GLUT4 trafficking. Confers resistance to dietary obesity. May act by regulating AKT2, but not AKT1, phosphorylation at the plasma membrane. Part of a signaling pathway that regulates actin cytoskeleton remodeling. Required for the maintenance and dynamic remodeling of actin structures as well as in endocytosis, having a major impact on ligand-induced EGFR internalization and degradation. Participates in regulation of cortical and submembraneous actin by hydrolyzing PtdIns(3,4,5)P3 thereby regulating membrane ruffling. Regulates cell adhesion and cell spreading. Required for HGF-mediated lamellipodium formation, cell scattering and spreading. Acts as a negative regulator of EPHA2 receptor endocytosis by inhibiting via PI3K-dependent Rac1 activation. Acts as a regulator of neuritogenesis by regulating PtdIns(3,4,5)P3 level and is required to form an initial protrusive pattern, and later, maintain proper neurite outgrowth. Acts as a negative regulator of the FC-gamma-RIIA receptor (FCGR2A). Mediates signaling from the FC-gamma-RIIB receptor (FCGR2B), playing a central role in terminating signal transduction from activating immune/hematopoietic cell receptor systems. Involved in EGF signaling pathway. Upon stimulation by EGF, it is recruited by EGFR and dephosphorylates PtdIns(3,4,5)P3. Plays a negative role in regulating the PI3K-PKB pathway, possibly by inhibiting PKB activity.

Supplier: Bioss

Regulator of UV-induced DNA damage response: acts as a 'reader' of ubiquitinated PCNA that enhances RAD18-mediated PCNA ubiquitination and translesion DNA synthesis (TLS). Recruited to sites of UV damage and interacts with ubiquitinated PCNA and RAD18, the E3 ubiquitin ligase that monoubiquitinates PCNA. Facilitates chromatin association of RAD18 and is required for efficient PCNA monoubiquitination, promoting a feed-forward loop to enhance PCNA ubiquitination and translesion DNA synthesis. Acts as a regulator of TLS by recruiting VCP/p97 to sites of DNA damage, possibly leading to extraction of DNA polymerase eta (POLH) by VCP/p97 to prevent excessive translesion DNA synthesis and limit the incidence of mutations induced by DNA damage.

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HLA-A belongs to the HLA class I heavy chain paralogues. This class I molecule is a heterodimer consisting of a heavy chain and a light chain (beta-2 microglobulin). The heavy chain is anchored in the membrane. Class I molecules play a central role in the immune system by presenting peptides derived from the endoplasmic reticulum lumen. They are expressed in nearly all cells. The heavy chain is approximately 45 kDa and its gene contains 8 exons. Exon 1 encodes the leader peptide, exons 2 and 3 encode the alpha1 and alpha2 domains, which both bind the peptide, exon 4 encodes the alpha3 domain, exon 5 encodes the transmembrane region, and exons 6 and 7 encode the cytoplasmic tail. Polymorphisms within exon 2 and exon 3 are responsible for the peptide binding specificity of each class one molecule. Typing for these polymorphisms is routinely done for bone marrow and kidney transplantation. Hundreds of HLA-A alleles have been described. [provided by RefSeq, Jul 2008]

Supplier: Bioss

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.

Supplier: Bioss

The protein encoded by this gene can polymerize and depolymerize F-actin and G-actin in a pH-dependent manner. Increased phosphorylation of this protein by LIM kinase aids in Rho-induced reorganization of the actin cytoskeleton. Cofilin is a widely distributed intracellular actin-modulating protein that binds and depolymerizes filamentous F-actin and inhibits the polymerization of monomeric G-actin in a pH-dependent manner. It is involved in the translocation of actin-cofilin complex from cytoplasm to nucleus.