44096 Results for: "Bioss"

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PJA2, also known as E3 ubiquitin-protein ligase praja-2, RNF131 (ring finger protein 131) or Neurodap1, is a 708 amino acid protein that contains one ring-type zinc finger and exists as two alternatively spliced isoforms. Significantly conserved in chimpanzee, dog, cow, mouse, rat, chicken and zebrafish, PJA2 shares 52% identity with PJA1, which is involved in protein ubiquitination in brain and may play a role in X-linked mental retardation. Encoded by a gene that maps to human chromosome 5q21.3, PJA2 localizes to both endoplasmic reticulum and Golgi apparatus membranes. Participating in E2-dependent, E3 ubiquitin-protein ligase activity, PJA2 binds to a variety of E2s and interacts with ubiquitin-conjugating enzymes, such as UBE2D2, in vitro.

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Proteins containing PDZ domains have been shown frequently to bind the C-termini of transmembrane receptors or ion channels. They have also been shown to bind to other PDZ domain proteins and could possibly be involved in intracellular signalling. PDZK3 contains six PDZ domains and shares sequence similarity with pro-interleukin-16 (pro-IL-16). Like pro-IL-16, the encoded protein localizes to the endoplasmic reticulum and is thought to be cleaved by a caspase to produce a secreted peptide containing two PDZ domains. In addition, the PDZK3 gene is upregulated in primary prostate tumors and may be involved in the early stages of prostate tumorigenesis.

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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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PBGD, also designated hydroxymethylbilane synthase, is a cytoplasmic enzyme found in the heme synthesis pathway. PBGD belongs to the HMBS (hydroxymethylbilane synthase) family. Deficiency of PBGD causes errors in pyrrole metabolism, which in turn leads to an inherited autosomal disorder called acute intermittent porphyria (AIP). AIP is characterized by acute attacks of neurological dysfunctions with hypertension, tachycardia, peripheral neurologic disturbances, abdominal pain and excessive amounts of aminolevulinic acid and porphobilinogen in the urine.

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GHRH-R is a seven transmembrane domain protein that localizes to the somatotroph of the pituitary. GHRH-R plays an important role in growth and acts as a high-affinity receptor for GHRH. Binding of GHRH leads to the coupling of GHRH-R to G-protein which stimulates increased adenylyl cyclase activity and the accumulation of cAMP leading to the synthesis and release of growth hormone and somatotroph proliferation. In addition, this signalling pathway may have direct action in fetal/placental development, reproduction and immune function. GHRH and GHRH-R may also play a role in the regulation of non-rapid eye movement sleep (NREMS). The expression of GHRH-R is dependent on the presence of the POU domain factor Pit-1. Mutations in the gene encoding this protein can result in isolated growth hormone deficiency (IGHD), also known as Dwarfism of Sindh, and anterior pituitary hypoplasia (APH).

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STOML2 is a 356 amino acid member of the mec-2 family of proteins. Expressed ubiquitously at low levels, STOML2 is highly expressed in heart, liver and pancreas. STOML2 is localized to the cytoplasm with some distribution on the membrane. STOML2 was first identified as an overexpressed protein in human endometrial adenocarcinoma. Changes in cell growth in samples with different levels of STOML2 indicate that STOML2 could play a role in endometrial tumorigenesis. STOML2 is also thought to play a role in regulating ion channel conductances or the organization of sphingolipid and cholesterol-rich lipid rafts.

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Involved in accumulation of zinc in synaptic vesicles.

Supplier: Bioss

Involved in accumulation of zinc in synaptic vesicles.

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Diversin, also known as ANKRD6 (ankyrin repeat domain 6), is a 727 amino acid protein that contains eight ankyrin repeats and belongs to the ankyrin repeat domain protein family. Members of the ankyrin repeat domain family facilitate protein-protein interactions and function as adaptors of signaling pathways. Expressed in a developmentally-regulated manner and at highest levels in the brain, Diversin is believed to play a role in brain development. Via its ankyrin repeats, Diversin can directly interact with Dvl (dishevelled), an interaction that is essential for the activation of noncanonical Wnt signaling. In addition, Diversin contains a C-terminal domain that binds Axin/Conductin and a casein kinase-binding domain in its central region that specifically binds casein kinase Ié. Through the action of these additional domains, Diversin may also facilitate canonical Wnt signaling. Due to alternative splicing events, three Diversin isoforms exist.

Supplier: Bioss

Diversin, also known as ANKRD6 (ankyrin repeat domain 6), is a 727 amino acid protein that contains eight ankyrin repeats and belongs to the ankyrin repeat domain protein family. Members of the ankyrin repeat domain family facilitate protein-protein interactions and function as adaptors of signaling pathways. Expressed in a developmentally-regulated manner and at highest levels in the brain, Diversin is believed to play a role in brain development. Via its ankyrin repeats, Diversin can directly interact with Dvl (dishevelled), an interaction that is essential for the activation of noncanonical Wnt signaling. In addition, Diversin contains a C-terminal domain that binds Axin/Conductin and a casein kinase-binding domain in its central region that specifically binds casein kinase Ié. Through the action of these additional domains, Diversin may also facilitate canonical Wnt signaling. Due to alternative splicing events, three Diversin isoforms exist.

Supplier: Bioss

Diversin, also known as ANKRD6 (ankyrin repeat domain 6), is a 727 amino acid protein that contains eight ankyrin repeats and belongs to the ankyrin repeat domain protein family. Members of the ankyrin repeat domain family facilitate protein-protein interactions and function as adaptors of signaling pathways. Expressed in a developmentally-regulated manner and at highest levels in the brain, Diversin is believed to play a role in brain development. Via its ankyrin repeats, Diversin can directly interact with Dvl (dishevelled), an interaction that is essential for the activation of noncanonical Wnt signaling. In addition, Diversin contains a C-terminal domain that binds Axin/Conductin and a casein kinase-binding domain in its central region that specifically binds casein kinase Ié. Through the action of these additional domains, Diversin may also facilitate canonical Wnt signaling. Due to alternative splicing events, three Diversin isoforms exist.

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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. RNF215 (ring finger protein 215), is a 377 amino acid multi-pass membrane protein containing one RING-type zinc finger. The gene encoding RNF215 maps to human chromosome 22, which houses over 500 genes and is the second smallest human chromosome. Mutations in several of the genes that map to chromosome 22 are involved in the development of Phelan-McDermid syndrome, Neurofibromatosis type 2, autism and schizophrenia.

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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. RNF186 (RING finger protein 186) is a 227 amino acid multi-pass membrane protein containing one RING-type zinc finger. The gene encoding RNF186 maps to human chromosome 1p36.13. 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. 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.

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IGSF1 is a highly glycolylated immunoglobulin domain-containing protein. IGSF1 has been shown to act as a coreceptor in inhibin signaling, however, it does not appear to be a high-affinity inhibin receptor by itself. May reduce or inhibit activin A signaling and is believed to be necessary in the mediation of specific effects of inhibin B on activin-stimulated transcription. IGSF1 has been found to interact with several members of the ACVR family and possibly some members of the BMPR group. There are 3 known isoforms of IGSF1, with 1 and 2 likely being multi-pass membrane proteins. Isoform 3 is believed to be expressed as a secreted form. Expression is high in pancreas, testis and fetal liver, while heart, prostate and small intestine show only moderate expression. IGSF1 may be found at very low levels in brain, muscle, thymus, ovary, colon, fetal lung and fetal kidney. Isoform 3 has been detected in pituitary gland.

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IGSF3, also known as V8 or EWI-3, is a 1,214 amino acid protein. Widely expressed with predominant expression in kidney, placenta and lung, IGSF3 localizes to the membrane and contains an N-terminal signal peptide, eight immunoglobulin (Ig) domains and a transmembrane segment. IGSF3 exhibits strong sequence and structural similarity to CD101 (32% identity), a leukocyte surface protein with seven Ig domains that is believed to play a role in T-cell activation. Despite the structural similarities between IGSF3 and CD101, IGSF3 is not expressed in peripheral blood lymphocytes and does not appear to participate in an immune function. Based on its subcellular localization and the presence of the eight Ig domains, IGSF3 is hypothesized to function as a surface receptor or as a cell adhesion molecule.

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IGSF3, also known as V8 or EWI-3, is a 1,214 amino acid protein. Widely expressed with predominant expression in kidney, placenta and lung, IGSF3 localizes to the membrane and contains an N-terminal signal peptide, eight immunoglobulin (Ig) domains and a transmembrane segment. IGSF3 exhibits strong sequence and structural similarity to CD101 (32% identity), a leukocyte surface protein with seven Ig domains that is believed to play a role in T-cell activation. Despite the structural similarities between IGSF3 and CD101, IGSF3 is not expressed in peripheral blood lymphocytes and does not appear to participate in an immune function. Based on its subcellular localization and the presence of the eight Ig domains, IGSF3 is hypothesized to function as a surface receptor or as a cell adhesion molecule.

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ZPI, also known as SERPINA10 (serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 10) or PZI, is a 444 amino acid secreted protein that functions as a Protein Z-dependent protease inhibitor. Expressed by the liver, ZPI is secreted into the plasma where, in the presence of calcium, Protein Z and phospholipids, it inhibits the activated pro-coagulation factors X and XI (Factor X and Factor XI). This inhibition helps properly regulate intravenous blood clotting. ZPI, a member of the serpin protein family, contains five potential N-linked glycosylation sites and a tyrosine at position 387 which, when disrupted, renders ZPI inactive. Defects in the gene encoding ZPI may increase susceptibility to venous thrombosis, the formation of blood clots within a vein.

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Centrosomes are dynamic organelles involved in many aspects of cell function and growth. Centrosomes act as microtubule organizing centers, and provide a site for concerted regulation of cell cycle progression. Duplication of centrosomes occurs once during each cell cycle and requires proper mitotic spindle formation and chromosome segregation. Defects in centrosome duplication or function are linked to many human diseases, including various forms of cancer. The centrosome and spindle pole-associated protein 1 (CSPP1) interacts with centrosomes and microtubules and may play a role in the regulation of G(1)/S-phase progression and spindle assembly. Two isoforms of CSPP1 exist as a result of alternative splicing events. Isoform 1 expression increases throughout the cell cycle and peaks in G2/M phase, whereas isoform 2 expression is highest in G1 phase and decreases thereafter.

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The U-box domain is a modified RING finger motif that has been implicated in the ubiquitin/proteasome system. The ubiquitin-conjugating enzyme 7-interacting protein 5 (UIP5), also designated U-box domain-containing protein 5 or RING finger protein 37, contains 1 RING-type zinc finger and 1 U-box domain. UIP5 has been shown to interact with UBCH7, an enzyme that mediates selective degradation of abnormal proteins. The gene encoding UIP5 maps to chromosome 20, which houses over 600 genes, some of which are associated with Creutzfeldt-Jakob disease, amyotrophic lateral sclerosis, spinal muscular atrophy, ring chromosome 20 epilepsy syndrome and Alagille syndrome. Additionally, chromosome 20 contains a region with numerous genes which are thought important for seminal production and may be potential targets for male contraception.

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Ubiquitination is an important mechanism through which three classes of enzymes act in concert to target short-lived or abnormal proteins for destruction. The three classes of enzymes involved in ubiquitination are the ubiquitin-activating enzymes (E1s), the ubiquitin-conjugating enzymes (E2s) and the ubiquitin-protein ligases (E3s). Ubr2 (Ubiquitin-protein ligase E3-alpha-2), also known as N-recognin-2, is a 1755 amino acid protein that contains one UBR-type zinc finger and one RING-type zinc finger. Participating in protein modification events within the N-end rule pathway, Ubr2 functions as an E3 ubiquitin-protein ligase that recognizes and binds proteins that contain destabilizing N-terminal residues, thereby leading to their ubiquitination and subsequent degradation. Mice lacking Ubr2 are infertile due to defects in male meiosis.

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TTC33 contains 3 TPR repeats. The function of the TTC33 protein remains unknown.

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TTC33 contains 3 TPR repeats. The function of the TTC33 protein remains unknown.

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GPR120, a member of the rhodopsin family of G protein-coupled receptors (GPCRs), is a 377 amino acid protein which is expressed in the intestine. GPR120 is a receptor for unsaturated long-chain FFAs (free fatty acids). FFAs act as signaling molecules and are an important energy source. They also employ various physiological responses through their GPCRs. One such response occurs when dietary FFAs stimulate GPR120. This stimulation promotes the secretion of glucagon-like peptide 1 (GLP-1) in vivo and in vitro. GLP-1 belongs to the class of molecules known as the incretins, which are associated with insulin secreted from the pancreas as a result of food intake. GLP-1 also inhibits glucagon and gastric acid secretion and gastric emptying. Consequently, the role of GPR120 in the secretion of GLP-1 is critical in the treatment of diabetes.

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Rad and Gem related GTP binding protein (REM) is a member of the RGK subfamily of Ras-like GTPases that also includes Rad, REM2 and Gem/Kir. REM is a phosphorylated protein that is highly expressed in cardiac muscle and moderately expressed in lung, kidney and skeletal muscle. REM associates with several 14-3-3 isoforms as well as with calmodulin in a calcium-dependent manner. REM mediates two distinct signal transduction pathways that regulate both cytoskeletal reorganization and voltage-gated calcium channel activity. REM decreases the current that passes through cardiac voltage-gated L-type Ca channels (Ca(V)). Overexpression of REM may result in the development of cytoplasmic processes, reorganization of the Actin cytoskeleton, reduction in focal adhesion size and an elongated or dendritic-like cell morphology.

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Mitochondrial ATP synthase is composed of two multi-subunit complexes that utilize an inner membrane electrochemical gradient to catalyze the synthesis of ATP during oxidative phosphorylation. The two multi-subunit complexes are designated F1 and F0, the former of which comprises the soluble catalytic core and the latter of which comprises the membrane-spanning proton channel of ATP synthase. F1 consists of five distinct subunits, designated ATP5A, ATP5B, ATP5C1, ATP5D and ATP5E, while F0 consists of ten subunits, designated ATP5H, ATP5G1, ATP5I, ATP5G2, ATP5J2, ATP5J, ATP5G3, ATP5S, ATP5F1 and ATP5L. ATP5B, also designated ATPMB, ATPSB or mitochondrial ATP synthetase, beta subunit, is a 529 amino acid protein that localizes to the mitochondrial membrane and exists as a subunit of the F0 complex. ATP5B is encoded by a nuclear gene and assembled with the other subunits encoded by both mitochondrial and nuclear genes. The ATP5B gene is activated by members of the Ets family of transcription factors, suggesting that Ets transcription factors are involved in the enhanced expression of the ATP5B gene in highly proliferating cells and in the coordinate transcription of nuclear genes for mitochondrial proteins. ATP5B mRNA levels vary among species through transcriptional control with high expression levels in heart, lower levels in skeletal muscle and the lowest levels in liver and kidney.

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Component of a probable SCF-like E3 ubiquitin-protein ligase complex, which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Probably plays a role in the degradation of proteins involved in endothelial proliferation and/or differentiation (By similarity). Seems not to promote polyubiquitination and proteasomal degradation of TP53. In vitro, complexes of CUL7 with either CUL9 or FBXW8 or TP53 contain E3 ubiquitin-protein ligase activity.Involvement in disease: Defects in CUL7 are the cause of 3M syndrome type 1 (3M1). An autosomal recessive disorder characterized by severe pre- and postnatal growth retardation, facial dysmorphism, large head circumference, and normal intelligence and endocrine function. Skeletal changes include long slender tubular bones and tall vertebral bodies.

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Essential component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2. The complex is also involved in phosphorylation of p53/TP53, c-jun/JUN, IkappaBalpha/NFKBIA, ITPK1 and IRF8/ICSBP, possibly via its association with CK2 and PKD kinases. CSN-dependent phosphorylation of TP53 and JUN promotes and protects degradation by the Ubl system, respectively. Suppresses G-protein- and mitogen-activated protein kinase-mediated signal transduction.

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heatstable enterotoxin 1 [Escherichia coli]

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Diversin, also known as ANKRD6 (ankyrin repeat domain 6), is a 727 amino acid protein that contains eight ankyrin repeats and belongs to the ankyrin repeat domain protein family. Members of the ankyrin repeat domain family facilitate protein-protein interactions and function as adaptors of signaling pathways. Expressed in a developmentally-regulated manner and at highest levels in the brain, Diversin is believed to play a role in brain development. Via its ankyrin repeats, Diversin can directly interact with Dvl (dishevelled), an interaction that is essential for the activation of noncanonical Wnt signaling. In addition, Diversin contains a C-terminal domain that binds Axin/Conductin and a casein kinase-binding domain in its central region that specifically binds casein kinase Ié. Through the action of these additional domains, Diversin may also facilitate canonical Wnt signaling. Due to alternative splicing events, three Diversin isoforms exist.

Supplier: Bioss

NOB1P is a 412 amino acid nuclear protein that is involved in proteosome biogenesis and is required for the final step in 18S rRNA maturation. NOB1P contains a PIN domain, which functions as a nuclease in nonsense-mediated mRNA decay and is required for pre-rRNA cleavage. NOB1P interacts with Rent2, which is involved in nonsense-mediated decay of mRNAs containing premature stop codons. Expressed in placenta, spleen, endothelial cells, liver and lung, NOB1P is essential for the synthesis of 40S ribosome subunits. Supression of the gene encoding NOB1P inhibits the processing of the 20S pre-rRNA to the mature 18S rRNA, therefore leading to accumulation of high levels of 20S pre-rRNA with degradation intermediates.