54835 Results for: "2-Chloroquinoline-5-carboxylic+acid&pageNo=48"

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HBXIP (Hepatitis B virus X interacting protein) complexes with the C-terminus of hepatitis B virus X protein (HBx) and down-regulates hepatitis B virus (HBV) replication. When complexed to BIRC5, it interferes with apoptosome assembly, preventing recruitment of pro-caspase-9 to oligomerized APAF1, thereby selectively suppressing apoptosis initiated via the mitochondrial/cytochrome c pathway.

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The Hox proteins play a role in patterns of embryonic development and cellular differentiation by regulating downstream target genes. In vivo, the HoxD9 protein interacts with the autoregulatory and cross-regulatory enhancers of the murine HoxB1 and human HoxD9 genes. Specifically, the HoxD9 protein interacts with the human control region (HCR) of the HoxD9 gene, thus inducing transcription of the HoxD9 promoter. HoxD9 may be a multifunctional transcriptional regulator, as it contains different activation domains. Activation of HoxD9 depends on the structure of the target regulatory element, and results in differential cofactor interaction. The HoxD9 protein is expressed in the early stages of mouse joint development, primarily in the articular cartilage. HoxD9 transcripts are also detected in the synovial tissue of arthritic mice, but not in that of normal mice, suggesting that HoxD9 may have a role in the pathology of arthritis. Furthermore, the HoxD9 protein is highly expressed in the synoviocytes of patients with rheumatoid arthritis (RA), but not in osteoarthritis patients. The human HoxD9 protein is also differentially expressed in the human cervical cancer cell line HeLa, but is not expressed in the normal cervix and may thus play a role in tumorigenesis.

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Thin filament-associated protein that is implicated in the regulation and modulation of smooth muscle contraction. It is capable of binding to actin, calmodulin, troponin C and tropomyosin. The interaction of calponin with actin inhibits the actomyosin Mg-ATPase activity (By similarity).

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The coiled-coil domain is a structural motif found in proteins that are involved in a diverse array of biological functions such as the regulation of gene expression, cell division, membrane fusion and drug extrusion and delivery. CCDC38 (coiled-coil domain containing 38) is a 563 amino acid protein encoded by a gene that maps to human chromosome 12q23.1. Encoding over 1,100 genes, chromosome 12 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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Calcyclin, also known as Protein S100-A6, growth factor-inducible protein 2A9, S-100 calcium-binding protein A6 (S-100A6) or MLN 4, is a homodimeric member of the S-100 calcium-binding protein family whose expression is upregulated in proliferating and differentiating cells. Calcyclin is inducible by growth factors and overexpressed in acute myeloid leukemias. It is expressed in a cell-specific manner in subpopulations of neurons and astrocytes and in epithelial cells and fibroblasts. Calcyclin is a specific target of S-100B protein in vivo. The binding of Calcyclin to S-100B is stabilized by S-100B-bound calcium and zinc. Calcyclin associates with both Annexin XI and CacyBP (calcyclin-binding protein). It functions to activate several processes along the calcium signal transduction pathway including the regulation of cell growth, proliferation, secretion and exocytosis.

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Negative regulator of YAP1 in the Hippo signaling pathway that 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 LATS1 inhibits its translocation into the nucleus to regulate cellular genes important for cell proliferation, cell death, and cell migration. Acts as a tumor suppressor which plays a critical role in maintenance of ploidy through its actions in both mitotic progression and the G1 tetraploidy checkpoint. Negatively regulates G2/M transition by down-regulating CDK1 kinase activity. Involved in the control of p53 expression. Affects cytokinesis by regulating actin polymerization through negative modulation of LIMK1. May also play a role in endocrine function.

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RNF121 protein contains a RING finger, a motif present in a variety of functionally distinct proteins and known to be involved in protein-protein and protein-DNA interactions. Multiple alternatively spliced transcript variants encoding distinct isoforms have been reported. Three of them are supported by at least two independent transcripts or ESTs, the full length natures of others are not clear.

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The RING finger motif is a specialized DNA-binding zinc finger domain found in many transcriptional regulatory proteins. The ring finger protein (RNF) family includes any protein containing the signature RING finger motif. RNF8 is a ubiquitously expressed nuclear RING finger protein that acts as an E3 ubiquitin-protein ligase. It is required for the ubiquitination of some nuclear proteins and promotes their subsequent degradation. The heterodimeric ubiquitin-conjugating enzyme UBC13 interacts with RNF8, and they co-localize in the nucleus. RNF8 may regulate mediation of UBC13 polyubiquitylation by elongating the ubiquitin chains. RNF8 also binds to Retinoid X receptor alpha (RXR?, a member of the steroid hormone receptor superfamily. It increases RXR?mediated transactivation of the RXR?responsive element (RXRE) promoter in a dose-dependent manner, suggesting that RNF8 is a regulator of RXR?mediated transcriptional activity.

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Osteocalcin belongs to the osteocalcin/matrix Gla protein family and constitutes 1 to 2% of the total bone protein. It is a 49 amino acid single chain vitamin K dependent protein, made by osteoblasts, and is a major component of the noncollagenous bone matrix. Post translational modification by a vitamin K dependent carboxylase produces three gamma carboxyglutamic acid residues at positions 17, 21 and 24, giving it a high affinity for calcium. It also binds strongly to apatite.

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RILPL2 is a 211 amino acid protein that belongs to the RILPL family. RILPL2 does not regulate lysosomal morphology or distribution. RILPL2 shares 32% and 18% amino acid identity with RILPL1 and RILP, respectively. RILPL2 as a novel interacting partner for the actin-based molecular motor MyoVa, and has a novel role for RILPL2 in controlling neuronal morphogenesis. It has been suggested that there is also a novel role for RILPL2 in the regulation of cellular shape and dendritic-spine morphogenesis, probably via the Rac1-Pak pathway. PCR analysis of human tissues detects highest RILPL2 expression in lung, followed by placenta. Lower expression is detected in liver, kidney, pancreas, heart and brain, but no expression is detected in skeletal muscle. The RILPL2 gene is conserved in chimpanzee, dog, cow, mouse, rat, chicken and zebrafish, and maps to human chromosome 12q24.31.

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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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Filament-forming cytoskeletal GTPase. Required for normal organization of the actin cytoskeleton. Required for normal progress through mitosis. Involved in cytokinesis. Required for normal association of CENPE with the kinetochore. Plays a role in ciliogenesis and collective cell movements.

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HHLA1.

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Isoform A binds to IL-18 and inhibits its activity. Functions as an inhibitor of the early TH1 cytokine response.

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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. MARCH8 (membrane-associated ring finger (C3HC4) 8), also known as MIR or RNF178 (RING finger protein 178), is a 291 amino acid multi-pass membrane protein that localizes to vesicle membranes and contains one RING-CH-type zinc finger. Expressed in a variety of tissues, including immature dendritic cells, MARCH8 functions as an E3 ubiquitin ligase that is thought to regulate immune responses by promoting the ubiquitination and subsequent degradation of target proteins, such as B7-2 and CD71.

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Monothiol glutaredoxin involved in the biogenesis of iron-sulfur clusters. Required for normal iron homeostasis. Required for normal regulation of hemoglobin synthesis by the iron-sulfur protein ACO1.

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Protective protein appears to be essential for both the activity of beta-galactosidase and neuraminidase, it associates with these enzymes and exerts a protective function necessary for their stability and activity. This protein is also a carboxypeptidase and can deamidate tachykinins.

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The cadherins are a family of Ca2+-dependent adhesion molecules that function to mediate cell-cell binding events that are critical to the maintenance of cell structure and morphogenesis. EY-cadherin, also known as CDH18 (cadherin 18), CDH14 (cadherin 14), CDH24 or CDH14L, is a 790 amino acid single-pass type I membrane protein that contains five cadherin domains. One of several members of the cadherin superfamily, EY-cadherin functions as a type II classical cadherin that is expressed specifically in the central nervous system (CNS), where it plays a role in cell-cell binding events. Specifically, EY-cadherin is thought to be involved in axon guidance and outgrowth, as well as synaptic adhesion within the CNS. EY-cadherin contains a highly conserved C-terminal domain characteristic of all cadherins, but lacks the HAV cell adhesion sequence that is specific to type I cadherins. The gene encoding EY-cadherin is located within a region on chromosome five that is commonly deleted in carcinomas, implicating EY-cadherin as a potential tumor suppressor.

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Glycerol 3 Phosphate Dehydrogenase is a homodimer and belongs to the NAD dependent Glycerol 3 Phosphate Dehydrogenase family.

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Controls the flux of glucose into the hexosamine pathway. Most likely involved in regulating the availability of precursors for N- and O-linked glycosylation of proteins. Regulates the circadian expression of clock genes ARNTL/BMAL1 and CRY1.

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Accelerates programmed cell death by binding to, and antagonizing the apoptosis repressor BCL2 or its adenovirus homolog E1B 19k protein. Under stress conditions, undergoes a conformation change that causes translocation to the mitochondrion membrane, leading to the release of cytochrome c that then triggers apoptosis. Promotes activation of CASP3, and thereby apoptosis.

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CRP2BP is a 782 amino acid protein encoded by the human gene CSRP2BP. CRP2BP specifically interacts with the double LIM domain protein CRP2. The LIM domain is a conserved cysteine and histidine-containing structural module of two tandemly arranged zinc fingers. It has been identified in single or multiple copies in a variety of regulatory proteins, either in combination with defined functional domains, like homeodomains, or alone, like in the CRP family of LIM proteins. Members of the cysteine- and glycine-rich protein family (CRP1, CRP2 and CRP3) contain two zinc-binding LIM domains, LIM1 (amino-terminal) and LIM2 (carboxyl-terminal), and are implicated in diverse cellular processes linked to differentiation, growth control and pathogenesis. Although present in cytoplasm, CRP2BP is mainly a ubiquitously expressed nuclear protein, with highest expression in skeletal muscle and heart.

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C3orf62 (chromosome 3 open reading frame 62) is a 267 amino acid protein encoded by a gene that maps to human chromosome 3p21.31. Chromosome 3 is made up of approximately 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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LZIC is a 190 amino acid protein that belongs to the CTNNBIP1 family. Ubiquitously expressed, LZIC is found at highest levels in kidney and is upregulated in a few gastric carcinomas. The gene encoding LZIC maps to human chromosome 1, which spans 260 million base pairs, contains over 3,000 genes and comprises nearly 8% of the human genome. Chromosome 1 houses a large number of disease-associated genes, including those that are involved in familial adenomatous polyposis, Stickler syndrome, Parkinson’s disease, Gaucher disease, schizophrenia and Usher syndrome. 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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LRRC62 contains 1 fibronectin type III domain and 5 LRR (leucine rich) repeats. The exact function of LRRC62 remains unknown.

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No data available.

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The Golgi complex plays a key role in the sorting and modification of proteins exported from the endoplasmic reticulum. GOLPH3L (golgi phosphoprotein 3-like), also known as GPP34R, is a 285 amino acid cytoplasmic protein that localizes to the Golgi apparatus. Belonging to the GOLPH3/VPS74 family, GOLPH3L may have a regulatory role in Golgi trafficking. GOLPH3L is encoded by a gene located on human chromosome 1, which spans 260 million base pairs, contains over 3,000 genes and comprises nearly 8% of the human genome. Chromosome 1 houses a large number of disease-associated genes, including those that are involved in familial adenomatous polyposis, Stickler syndrome, Parkinson’s disease, Gaucher disease, schizophrenia and Usher syndrome. 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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Component of a heterodimeric G-protein coupled receptor for GABA, formed by GABBR1 and GABBR2. Within the heterodimeric GABA receptor, only GABBR1 seems to bind agonists, while GABBR2 mediates coupling to G proteins. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling inhibits adenylate cyclase, stimulates phospholipase A2, activates potassium channels, inactivates voltage-dependent calcium-channels and modulates inositol phospholipid hydrolysis. Plays a critical role in the fine-tuning of inhibitory synaptic transmission. Pre-synaptic GABA receptor inhibits neurotransmitter release by down-regulating high-voltage activated calcium channels, whereas postsynaptic GABA receptor decreases neuronal excitability by activating a prominent inwardly rectifying potassium (Kir) conductance that underlies the late inhibitory postsynaptic potentials. Not only implicated in synaptic inhibition but also in hippocampal long-term potentiation, slow wave sleep, muscle relaxation and antinociception.

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GOLGA7 is a multi-pass membrane protein belonging to the Erf4 family of proteins. It is the functional ortholog of the yeast Erf4 protein. Localizing to the Golgi apparatus, GOLGA7 is a widely expressed protein but its expression is absent from colon and thymus tissues. GOLGA7 is palmitoylated on two cysteine residues, and this palmitoylation is required for its interaction with golgin 160 and its Golgi-localization. GOLGA7 also forms a complex with ZDHHC9 and, together, these proteins function as a Ras palmitoyltransferase (Ras PAT) which is required for palmitoylation of H-Ras and N-Ras proteins. The palmitoylation of Ras proteins is essential for the trafficking of Ras proteins from the Golgi to the plasma membrane, thus implicating GOLGA7 in protein transport from the Golgi to the cell surface.

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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).