45955 Results for: "Dibutyl+carbonate&pageNo=88"

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May play a role in mediating neutrophil activation and chemotaxis. This gene encodes an intracellular F-actin binding protein. The protein is expressed in lymphocytes, neutrophils, macrophages, and endothelium and may regulate neutrophil motility, adhesion to fibrinogen matrix proteins, and transendothelial migration. Alternative splicing results in multiple transcript variants encoding different isoforms. [provided by RefSeq, Jul 2008]

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Testis and spermatogenesis related gene 4 may play a role in the development of cryptorchidism, the failure of the testis to descend from the abdomen into the scrotum [RGD] [TISSUE SPECIFICITY] Testis.

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Importin 7 is a 1,038 amino acid protein encoded by the human gene IPO7. Importin-7 belongs to the importin b family and contains one importin N-terminal domain. Importin-7 functions in nuclear protein import, either by acting as an autonomous nuclear transport receptor or as an adapter-like protein in association with the Importin b subunit KPNB1. Acting autonomously, Importin-7 is thought to serve itself as receptor for nuclear localization signals (NLS) and to promote translocation of import substrates through the nuclear pore complex (NPC) by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to Importin-7, the Importin-7/substrate complex dissociates and Importin-7 is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran. Importin-7 is a nuclear protein that is expressed in most tissues.

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Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity.

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Could be involved in signal transduction.

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Component of some chromatin complex recruited to chromatin sites methylated 'Lys-4' of histone H3 (H3K4me).

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C22orf37 (chromosome 22 open reading frame 37), also known as FLJ40542, is a 170 amino acid protein encoded by a gene located on human chromosome 22, which contains over 500 genes and about 49 million bases. As the second smallest human chromosome, chomosome 22 contains a wide variety of genes with numerous functions. Phelan-McDermid syndrome, Neurofibromatosis type 2 and autism are associated with chromosome 22. A schizophrenia susceptibility locus has been identified on chromosome 22 and studies show that 22q11 deletion symptoms include a high incidence of schizophrenia. Translocations between chromosomes 9 and 22 may lead to the formation of the Philadelphia Chromosome and the subsequent production of the novel fusion protein, BCR-Abl, a potent cell proliferation activator found in several types of leukemia.

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Glycogen synthase kinase 3 (GSK3) is a proline directed serine threonine kinase that was initially identified as a phosphorylating and inactivating glycogen synthase. GSK3 has been implicated in fundamental cell processes such as cell fate determination, metabolism, transcriptional control and oncogenesis. Two isoforms, alpha (GSK3A; OMIM 606784) and beta, show a high degree of amino acid homology within their catalytic domains. GSK3B is involved in energy metabolism, neuronal cell development and body pattern formation.

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Beta-tectorin is a 329 amino acid secreted protein that contains one zona pellucida (ZP) domain. While it may form homomeric filaments after self-association, Beta-tectorin may also form heteromeric filaments when it associates with ?tectorin. The presence of a hydrophobic C-terminus preceded by a potential cleavage site strongly suggests that tectorins are synthesized as glycosylphosphatidylinositol-linked, membrane-bound precursors. Tectorins are targeted to the apical surface of the inner ear epithelia and proteolytically released into the extracellular compartment. Beta-tectorin is one of the major non-collagenous components of the tectorial membrane. The tectorial membrane is an extracellular matrix of the inner ear that covers the neuroepithelium of the cochlea and contacts the stereocilia bundles of specialized sensory hair cells. Sound induces movement of these hair cells relative to the tectorial membrane, deflects the stereocilia and leads to fluctuations in hair-cell membrane potential, transducing sound into electrical signals.

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MEK5 is a dual specificity protein kinase belonging to thr Ser/Thr protein kinase family, (MAP kinase kinase family). It is activated by phosphorylation on Ser/Thr by MAP kinase kinases and interacts specifically with ERK5, and not with another MAP kinase like P38. This kinase specifically interacts with and activates MAPK7/ERK5. This kinase itself can be phosphorylated and activated by MAP3K3/MEKK3, as well as by atypical protein kinase C isoforms (aPKCs). It is not phosphorylated by RAFA, RAFB or RAFC and it may interact with GTPases such as CDC42. The signal cascade mediated by this kinase is involved in growth factor stimulated cell proliferation and muscle cell differentiation. MEK5 is expressed in many adult tissues and is most abundant in heart and skeletal muscle.

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The product of this gene is a member of the nuclearfactors of activated T cells DNA-binding transcription complex.This complex consists of at least two components: a preexistingcytosolic component that translocates to the nucleus upon T cellreceptor (TCR) stimulation and an inducible nuclear component.Other members of this family of nuclear factors of activated Tcells also participate in the formation of this complex. Theproduct of this gene plays a role in the inducible expression ofcytokine genes in T cells, especially in the induction of the IL-2and IL-4. Alternatively spliced transcript variants encodingdifferent isoforms have been noted for this gene.

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Location-regulated scaffolding protein connecting MEK to RAF. Promotes MEK and RAF phosphorylation and activity through assembly of an activated signaling complex. By itself, it has no demonstrated kinase activity.

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NCF4 is a cytosolic oxidase associated protein. It is a component of the nicotinamide adenine dinucleotide phosphate oxidase, which mediates down regulation of NADPH oxidase through interactions with its SH3 domain. NCF4 is associated with p67 phox but is absent in patients with chronic granulomatous disease who lack p67 phox.

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Photoreceptor-specific nuclear receptor, also known as NR2E3 or PNR, belongs to a large family of nuclear hormone receptor transcription factors. The proteins belonging to this family are characterized by discrete domains functioning in DNA and ligand binding. NR2E3 has a role in regulating the signaling pathway elemental to the photoreceptor cell function and in regulating pathways involved in embryonic development. NR2E3 is an eye specific nuclear protein found in the outer nuclear layer of the adult retina (where the nuclei of cone and rod photoreceptors are located). Defects in this gene encoding for the protein, which localizes to chromosome 15q22.32, cause enhanced S cone syndrome.

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Hsp22 (HSPB8) is a 196-amino acid protein that contains a central portion homologous to a highly conserved HSP-alpha crystallin domain common to all the small heat shock protein (HSP20) family members. Hsp22 is a monomeric protein which interacts with HSPB1. It displays temperature-dependent chaperone activity. The highest abundance of Hsp22 is in skeletal muscle, heart, and placenta. Mutations in the HSPB8 gene are associated with the inherited peripheral neuropathies, autosomal dominant distal hereditary motor neuropathy type IIA (dSMA) and axonal Charcot-Marie-Tooth disease type 2L (CMT2L).

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p44/42 MAP Kinase(Thr202); ERK (extracellular signal regulated kinase), also known as MAPK (mitogen activated protein kinase) has two closely related isoforms of 44 kDa and 42 kDa, respectively. These kinases belong to a family of serine/threonine kinases that are activated upon treatment of cells with a large variety of stimuli including mitogens, hormones, growth factors, cytokines, and bioactive peptides. Cell stimulation induces the activation of a signaling cascade, the downstream effects of which have been linked to the regulation of cell growth and differentiation as well as the cytoskeleton. ERK1 and ERK2 are phosphorylated within the activation loop on both a Threonine and a Tyrosine residue (within a Thr-Glu-Tyr motif) by MEKs (MAPK/ERK kinases), thereby greatly elevating the activity of ERK1&2.

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Hox, Pbx and Meis families of transcription factors form heteromeric complexes and bind DNA through specific homeobox domains. Hox proteins are involved in regulating tissue patterning during development, and are also expressed in lineage- and stage-specific patterns during adult hematopoietic differentiation and in leukemias. The Hox proteins, which include paralog groups 1-10, have a low intrinsic binding affinity for DNA and are instead associated into cooperative DNA binding complexes with Pbx or the Pbx- related Meis proteins, which result in an enhanced Hox-DNA binding affinity and an increased selectivity for the binding site. Both Meis1 and Meis2 (also known as Meis-related gene 1 or Mrg1) are members of the TALE (“three amino acid loop extension”) family of homeodomain-containing proteins. In addition to binding with Hox proteins, Meis1 also forms heterodimers with the ubiquitously expressed Pbx proteins, including Pbx1, Pbx2 and Pbx3, and these complexes contain distinct DNA-binding specificities. Like Hox and Pbx proteins, Meis1 is implicated in oncogenesis, as it is overexpressed as a result of adjacent retroviral insertion in BHX-2 myeloid leukemias. Two Meis-related proteins, Meis2 and Meis3 (also designated Mrg1 and Mrg2, respectively), possess largely similar sequence identity with Meis1 and are expressed in normal tissues and myeloid leukemias. In the pancreas, Meis2 preferentially associates with Pbx1, and together they associate with the pancreas-specific homeodomain factor, Pdx1, to repress Pdx1-induced transcriptional activation.

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Stress-activated, pro-apoptotic kinase which, following caspase-cleavage, enters the nucleus and induces chromatin condensation followed by internucleosomal DNA fragmentation. Key component of the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein STK3/MST2 and STK4/MST1, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Phosphorylation of YAP1 by LATS2 inhibits its translocation into the nucleus to regulate cellular genes important for cell proliferation, cell death, and cell migration. STK3/MST2 and STK4/MST1 are required to repress proliferation of mature hepatocytes, to prevent activation of facultative adult liver stem cells (oval cells), and to inhibit tumor formation (By similarity). Phosphorylates 'Ser-14' of histone H2B (H2BS14ph) during apoptosis. Phosphorylates FOXO3 upon oxidative stress, which results in its nuclear translocation and cell death initiation. Phosphorylates MOBKL1A, MOBKL1B and RASSF2. Phosphorylates TNNI3 (cardiac Tn-I) and alters its binding affinity to TNNC1 (cardiac Tn-C) and TNNT2 (cardiac Tn-T). Phosphorylates FOXO1 on 'Ser-212' and regulates its activation and stimulates transcription of PMAIP1 in a FOXO1-dependent manner. Phosphorylates SIRT1 and inhibits SIRT1-mediated p53/TP53 deacetylation, thereby promoting p53/TP53 dependent transcription and apoptosis upon DNA damage. Acts as an inhibitor of PKB/AKT1. Phosphorylates AR on 'Ser-650' and suppresses its activity by intersecting with PKB/AKT1 signaling and antagonizing formation of AR-chromatin complexes.

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Pbx 1, 2, 3 and 4 are members of the TALE (three amino acid loop extension) family of homeodomain-containing proteins. Human pre-B cell acute leukemias are frequently associated with a t(1;19)(q23;p13.3) chromosomal rearrangement, which creates a chimeric gene encoding a fusion between the E2A and Pbx 1 gene products. Pbx 2 and Pbx 3 share 92% and 94% respective identities with Pbx 1 over a 266 amino acid region flanking their homeobox domains, while all three proteins are quite divergent at their amino- and carboxy-termini. Two forms of Pbx 1 and Pbx 3 each differ primarily in their carboxy-termini and result from alternative mRNA splicing. Unlike other homeotic selector genes which are expressed transiently during development and differentiation, Pbx gene transcripts are ubiquitously expressed in both fetal and adult tissues and cell lines. Additionally, Pbx 2 and Pbx 3 transcripts are detected in lymphoid cells, which do not express Pbx 1. Pbx 4 expression is confined to the testis, especially to spermatocytes in the pachytene stage of the first meiotic prophase.

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This protein functions in trans to edit the amino acid moiety from incorrectly charged tRNA(Ala) (by similariy). There are 2 isoforms produced by alternative splicing.

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Involved in the negative regulation of lymphocyte motility. It mediates the migration-inhibitory effects of IL6. Serves as a positive regulator of the RhoA signaling pathway. Enhancement of RhoA activation results in inhibition of lymphocyte and lymphoma cell motility by activation of its downstream effector ROCK. Is a regulator of B-cell receptor signaling, that acts through SYK kinase activation.

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This gene encodes a calmodulin- and actin-binding protein that plays an essential role in the regulation of smooth muscle and nonmuscle contraction. The conserved domain of this protein possesses the binding activities to Ca(2+)-calmodulin, actin, tropomyosin, myosin, and phospholipids. This protein is a potent inhibitor of the actin-tropomyosin activated myosin MgATPase, and serves as a mediating factor for Ca(2+)-dependent inhibition of smooth muscle contraction. Alternative splicing of this gene results in multiple transcript variants encoding distinct isoforms.

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May play a role in fertility and microtubule formation through interaction with RANBP9.

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Leucine-rich protein (LRP130) is a cytoplasmic mRNA-binding protein likely to be involved in the processing of mitochondrial DNA transcripts. Defects in the LRPPRC gene that encodes LRP130 result in the French-Canadian type of Leigh syndrome, a severe neurological disorder characterized by lesions in the subcortical region of the brain. LRP130 also interacts with the low-affinity receptor for leukemia inhibitory factor to produce an intracelluar signal cascade.

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Uridine diphosphatase (UDPase) that promotes protein N-glycosylation and ATP level regulation. UDP hydrolysis promotes protein N-glycosylation and folding in the endoplasmic reticulum, as well as elevated ATP consumption in the cytosol via an ATP hydrolysis cycle. Together with CMPK1 and AK1, constitutes an ATP hydrolysis cycle that converts ATP to AMP and results in a compensatory increase in aerobic glycolysis. The nucleotide hydrolyzing preference is GDP >IDP >UDP, but not any other nucleoside di-, mono- or triphosphates, nor thiamine pyrophosphate. Plays a key role in the AKT1-PTEN signaling pathway by promoting glycolysis in proliferating cells in response to phosphoinositide 3-kinase (PI3K) signaling.

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The protein encoded by this gene is a regulatory subunit of the AMP-activated protein kinase (AMPK). AMPK is a heterotrimer consisting of an alpha catalytic subunit, and non-catalytic beta and gamma subunits. AMPK is an important energy-sensing enzyme that monitors cellular energy status. In response to cellular metabolic stresses, AMPK is activated, and thus phosphorylates and inactivates acetyl-CoA carboxylase (ACC) and beta-hydroxy beta-methylglutaryl-CoA reductase (HMGCR), key enzymes involved in regulating de novo biosynthesis of fatty acid and cholesterol. This subunit may be a positive regulator of AMPK activity. The myristoylation and phosphorylation of this subunit have been shown to affect the enzyme activity and cellular localization of AMPK. This subunit may also serve as an adaptor molecule mediating the association of the AMPK complex. [provided by RefSeq, Jul 2008].

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D-DIMER is A fibrin degradation fragment or product that is produced by the action of plasmin on fibrin in the clot dissolution process.

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Orphan nuclear receptor. May act concomitantly with NURR1 in regulating the expression of delayed-early genes during liver regeneration. Binds the NGFI-B response element (NBRE) 5'-AAAAGGTCA-3' (By similarity). May inhibit NF-kappa-B transactivation of IL2. Participates in energy homeostasis by sequestrating the kinase STK11 in the nucleus, thereby attenuating cytoplasmic AMPK activation.

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This gene encodes a member of the Polycomb-group (PcG) family. PcG family members form multimeric protein complexes, which are involved in maintaining the transcriptional repressive state of genes over successive cell generations. This protein associates with the embryonic ectoderm development protein, the VAV1 oncoprotein, and the X-linked nuclear protein. This protein may play a role in the hematopoietic and central nervous systems. Multiple alternatively splcied transcript variants encoding distinct isoforms have been identified for this gene. [provided by RefSeq, Feb 2011].

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Calpain, and m calpain, also known as Calpain 2, are intracellular, calcium dependent cysteine proteases. Mu calpain has a micromolar sensitivity (thus the mu) as compared to the millimolar calcium sensitivity of m calpain. Both Calpains 1 and 2 are composed of an 80 kD subunit and a 30 kD subunit. Whereas the 30 kDa subunit is shared by both enzymes, the larger catalytic subunits are different and exhibit the distinct Ca++ requirements that are suggested by their names. The calpains have papain like activity, thus the pain nomenclature. Both Calpain 1 and Calpain 2 are ubiquitously expressed, and are countered by the endogenous calpain inhibitor, calpastatin. Other calpain family members (calpain 94, ncl2, ncl3, etc) have more limited tissue distribution, and perhaps different functions. The calpain family members consist of a common small subunit (Calpain 4), and a large variable subunit. It is not clear that all calpains contain a small subunit. Domains in the large subunit include the amino terminal domain I, the proteinase domain II, domain III, and the EF hand domain IV. The calpains appear to serve multiple physiological roles, and ideas concerning the functions of these enzymes are in a state of rapid flux.