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In molecular biology, miR-194 microRNA precursor is a small non-coding RNA gene that regulated gene expression. Its expression has been verified in mouse (MI0000236, MI0000733) and in human (MI0000488, MI0000732). mir-194 appears to be a vertebrate-specific miRNA and has now been predicted or experimentally confirmed in a range of vertebrate species (MIPF0000055). The mature microRNA is processed from the longer hairpin precursor by the Dicer enzyme. In this case, the mature sequence is excised from the 5' arm of the hairpin. | https://en.wikipedia.org/wiki/Mir-194_microRNA_precursor_family |
In molecular biology, mir-160 is a microRNA that has been predicted or experimentally confirmed in a range of plant species including Arabidopsis thaliana (mouse-ear cress) and Oryza sativa (rice). miR-160 is predicted to bind complementary sites in the untranslated regions of auxin response factor genes to regulate their expression. The hairpin precursors (represented here) are predicted based on base pairing and cross-species conservation; their extents are not known. In this case, the mature sequence is excised from the 5' arm of the hairpin. | https://en.wikipedia.org/wiki/Mir-160_microRNA_precursor_family |
Specifically, 3 of A. thaliana's 23 auxin-response factor genes are thought to be post-transcriptionally regulated by mir-160. When one of these targets (ARF17) is manipulated to become miRNA-resistant, several developmental defects can be observed in the host plant. This experiment has been repeated with another mir-160 target, ARF10, and results highlighted a regulatory role in post-embryonic development and seed germination. | https://en.wikipedia.org/wiki/Mir-160_microRNA_precursor_family |
In molecular biology, mir-221 microRNA (and its paralogue, mir-222) is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. mir-221 is an oncogenic microRNA. | https://en.wikipedia.org/wiki/Mir-221_microRNA |
It targets CD117, which then prevents cell migration and proliferation in endothelial cells. miR-221 is known as an anti angiogenic miRNA. Recent important studies have reported that miR-221 is also involved in induction of angiogenesis. | https://en.wikipedia.org/wiki/Mir-221_microRNA |
RNA induced Silencing Complex (RISC) proteins SND1 and AEG-1 induces miR-221 expression in Liver cancer. In liver cancer miR-221 induces the tumor angiogenesis. miR-221 detection in human faeces can be a non-invasive screening marker for colorectal cancer. | https://en.wikipedia.org/wiki/Mir-221_microRNA |
In molecular biology, mir-337 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. | https://en.wikipedia.org/wiki/Mir-337_microRNA_precursor_family |
In molecular biology, mir-46 (MI0000017) and mir-47 (MI0000018) are microRNA expressed in C. elegans from related hairpin precursor sequences. The predicted hairpin precursor sequences for Drosophila mir-281 (MI0000366, MI0000370) are also related and, hence, belong to this family. The hairpin precursors (represented here) are predicted based on base pairing and cross-species conservation; their extents are not known. In this case, the mature sequences are expressed from the 3' arms of the hairpin precursors. | https://en.wikipedia.org/wiki/Mir-46/mir-47/mir-281_microRNA_precursor_family |
In molecular biology, mir-720 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. | https://en.wikipedia.org/wiki/Mir-720_microRNA_precursor_family |
In molecular biology, molecular chaperones are proteins that assist in the folding, unfolding, assembly, or disassembly of other macromolecular structures. Under typical conditions, molecular chaperones facilitate changes in shape (conformational change) of macromolecules in response to changes in environmental factors like temperature, pH, and voltage. By reducing conformational flexibility, scientists can constrain the function of certain proteins. Recent research has shown that proteins are promiscuous, or able to do jobs in addition to the ones they evolved to carry out. Additionally, protein promiscuity plays a key role in the adaptation of species to new environments. It is possible that finding a way to control conformational change in promiscuous proteins could allow scientists to induce biostasis in living organisms. | https://en.wikipedia.org/wiki/Biostasis |
In molecular biology, molecular chaperones are proteins that assist the conformational folding or unfolding of large proteins or macromolecular protein complexes. There are a number of classes of molecular chaperones, all of which function to assist large proteins in proper protein folding during or after synthesis, and after partial denaturation. Chaperones are also involved in the translocation of proteins for proteolysis. The first molecular chaperones discovered were a type of assembly chaperones which assist in the assembly of nucleosomes from folded histones and DNA. | https://en.wikipedia.org/wiki/Chaperone_proteins |
One major function of molecular chaperones is to prevent the aggregation of misfolded proteins, thus many chaperone proteins are classified as heat shock proteins, as the tendency for protein aggregation is increased by heat stress. The majority of molecular chaperones do not convey any steric information for protein folding, and instead assist in protein folding by binding to and stabilizing folding intermediates until the polypeptide chain is fully translated. The specific mode of function of chaperones differs based on their target proteins and location. | https://en.wikipedia.org/wiki/Chaperone_proteins |
Various approaches have been applied to study the structure, dynamics and functioning of chaperones. Bulk biochemical measurements have informed us on the protein folding efficiency, and prevention of aggregation when chaperones are present during protein folding. Recent advances in single-molecule analysis have brought insights into structural heterogeneity of chaperones, folding intermediates and affinity of chaperones for unstructured and structured protein chains. | https://en.wikipedia.org/wiki/Chaperone_proteins |
In molecular biology, multicopper oxidases are enzymes which oxidise their substrate by accepting electrons at a mononuclear copper centre and transferring them to a trinuclear copper centre; dioxygen binds to the trinuclear centre and, following the transfer of four electrons, is reduced to two molecules of water. There are three spectroscopically different copper centres found in multicopper oxidases: type 1 (or blue), type 2 (or normal) and type 3 (or coupled binuclear). Multicopper oxidases consist of 2, 3 or 6 of these homologous domains, which also share homology with the cupredoxins azurin and plastocyanin. Structurally, these domains consist of a cupredoxin-like fold, a beta-sandwich consisting of 7 strands in 2 beta-sheets, arranged in a Greek-key beta-barrel. | https://en.wikipedia.org/wiki/Multicopper_oxidase |
Multicopper oxidases include: Ceruloplasmin EC 1.16.3.1 (ferroxidase), a 6-domain enzyme found in the serum of mammals and birds that oxidizes different inorganic and organic substances; exhibits internal sequence homology that appears to have evolved from the triplication of a Cu-binding domain similar to that of laccase and ascorbate oxidase. Laccase EC 1.10.3.2 (urishiol oxidase), a 3-domain enzyme found in fungi and plants, which oxidizes different phenols and diamines. CueO is a laccase found in Escherichia coli that is involved in copper-resistance. | https://en.wikipedia.org/wiki/Multicopper_oxidase |
Ascorbate oxidase EC 1.10.3.3, a 3-domain enzyme found in higher plants. Nitrite reductase EC 1.7.2.1, a 2-domain enzyme containing type-1 and type-2 copper centres.In addition to the above enzymes there are a number of other proteins that are similar to the multi-copper oxidases in terms of structure and sequence, some of which have lost the ability to bind copper. These include: copper resistance protein A (copA) from a plasmid in Pseudomonas syringae; domain A of (non-copper binding) blood coagulation factors V (Fa V) and VIII (Fa VIII); yeast Fet3p (FET3) required for ferrous iron uptake; yeast hypothetical protein YFL041w; and the fission yeast homologue SpAC1F7.08. == References == | https://en.wikipedia.org/wiki/Multicopper_oxidase |
In molecular biology, mutagenesis is an important laboratory technique whereby DNA mutations are deliberately engineered to produce libraries of mutant genes, proteins, strains of bacteria, or other genetically modified organisms. The various constituents of a gene, as well as its regulatory elements and its gene products, may be mutated so that the functioning of a genetic locus, process, or product can be examined in detail. The mutation may produce mutant proteins with interesting properties or enhanced or novel functions that may be of commercial use. Mutant strains may also be produced that have practical application or allow the molecular basis of a particular cell function to be investigated. | https://en.wikipedia.org/wiki/Mutagenesis_(molecular_biology_technique) |
Many methods of mutagenesis exist today. Initially, the kind of mutations artificially induced in the laboratory were entirely random using mechanisms such as UV irradiation. Random mutagenesis cannot target specific regions or sequences of the genome; however, with the development of site-directed mutagenesis, more specific changes can be made. | https://en.wikipedia.org/wiki/Mutagenesis_(molecular_biology_technique) |
Since 2013, development of the CRISPR/Cas9 technology, based on a prokaryotic viral defense system, has allowed for the editing or mutagenesis of a genome in vivo. Site-directed mutagenesis has proved useful in situations that random mutagenesis is not. Other techniques of mutagenesis include combinatorial and insertional mutagenesis. Mutagenesis that is not random can be used to clone DNA, investigate the effects of mutagens, and engineer proteins. It also has medical applications such as helping immunocompromised patients, research and treatment of diseases including HIV and cancers, and curing of diseases such as beta thalassemia. | https://en.wikipedia.org/wiki/Mutagenesis_(molecular_biology_technique) |
In molecular biology, nuclear ribonuclease P (RNase P) is a ubiquitous endoribonuclease, found in archaea, bacteria and eukarya as well as chloroplasts and mitochondria. Its best characterised enzyme activity is the generation of mature 5′-ends of tRNAs by cleaving the 5′-leader elements of precursor-tRNAs. Cellular RNase Ps are ribonucleoproteins. The RNA from bacterial RNase P retains its catalytic activity in the absence of the protein subunit, i.e. it is a ribozyme. | https://en.wikipedia.org/wiki/Nuclear_RNase_P |
Similarly, archaeal RNase P RNA has been shown to be weakly catalytically active in the absence of its respective protein cofactors. Isolated eukaryotic RNase P RNA has not been shown to retain its catalytic function, but is still essential for the catalytic activity of the holoenzyme. Although the archaeal and eukaryotic holoenzymes have a much greater protein content than the bacterial ones, the RNA cores from all three lineages are homologous—the helices corresponding to P1, P2, P3, P4, and P10/11 are common to all cellular RNase P RNAs. Yet there is considerable sequence variation, particularly among the eukaryotic RNAs. | https://en.wikipedia.org/wiki/Nuclear_RNase_P |
In molecular biology, olfactory marker protein is a protein involved in signal transduction. It is a highly expressed, cytoplasmic protein found in mature olfactory sensory receptor neurons of all vertebrates. OMP is a modulator of the olfactory signal transduction cascade. The crystal structure of OMP reveals a beta sandwich consisting of eight strands in two sheets with a jelly-roll topology. Three highly conserved regions have been identified as possible protein–protein interaction sites in OMP, indicating a possible role for OMP in modulating such interactions, thereby acting as a molecular switch. | https://en.wikipedia.org/wiki/Olfactory_marker_protein |
In molecular biology, open reading frames (ORFs) are defined as spans of DNA sequence between the start and stop codons. Usually, this is considered within a studied region of a prokaryotic DNA sequence, where only one of the six possible reading frames will be "open" (the "reading", however, refers to the RNA produced by transcription of the DNA and its subsequent interaction with the ribosome in translation). Such an ORF may contain a start codon (usually AUG in terms of RNA) and by definition cannot extend beyond a stop codon (usually UAA, UAG or UGA in RNA). That start codon (not necessarily the first) indicates where translation may start. | https://en.wikipedia.org/wiki/Open_reading_frame |
The transcription termination site is located after the ORF, beyond the translation stop codon. If transcription were to cease before the stop codon, an incomplete protein would be made during translation.In eukaryotic genes with multiple exons, introns are removed and exons are then joined together after transcription to yield the final mRNA for protein translation. In the context of gene finding, the start-stop definition of an ORF therefore only applies to spliced mRNAs, not genomic DNA, since introns may contain stop codons and/or cause shifts between reading frames. | https://en.wikipedia.org/wiki/Open_reading_frame |
An alternative definition says that an ORF is a sequence that has a length divisible by three and is bounded by stop codons. This more general definition can be useful in the context of transcriptomics and metagenomics, where a start or stop codon may not be present in the obtained sequences. Such an ORF corresponds to parts of a gene rather than the complete gene. | https://en.wikipedia.org/wiki/Open_reading_frame |
In molecular biology, origin recognition complex (ORC) is a multi-subunit DNA binding complex (6 subunits) that binds in all eukaryotes and archaea in an ATP-dependent manner to origins of replication. The subunits of this complex are encoded by the ORC1, ORC2, ORC3, ORC4, ORC5 and ORC6 genes. ORC is a central component for eukaryotic DNA replication, and remains bound to chromatin at replication origins throughout the cell cycle.ORC directs DNA replication throughout the genome and is required for its initiation. ORC and Noc3p bound at replication origins serve as the foundation for assembly of the pre-replication complex (pre-RC), which includes Cdc6, Tah11 (a.k.a. | https://en.wikipedia.org/wiki/Origin_Recognition_Complex |
Cdt1), and the Mcm2-Mcm7 complex. Pre-RC assembly during G1 is required for replication licensing of chromosomes prior to DNA synthesis during S phase. Cell cycle-regulated phosphorylation of Orc2, Orc6, Cdc6, and MCM by the cyclin-dependent protein kinase Cdc28 regulates initiation of DNA replication, including blocking reinitiation in G2/M phase.The ORC is present throughout the cell cycle bound to replication origins, but is only active in late mitosis and early G1. | https://en.wikipedia.org/wiki/Origin_Recognition_Complex |
In yeast, ORC also plays a role in the establishment of silencing at the mating-type loci Hidden MAT Left (HML) and Hidden MAT Right (HMR). ORC participates in the assembly of transcriptionally silent chromatin at HML and HMR by recruiting the Sir1 silencing protein to the HML and HMR silencers.Both Orc1 and Orc5 bind ATP, though only Orc1 has ATPase activity. The binding of ATP by Orc1 is required for ORC binding to DNA and is essential for cell viability. | https://en.wikipedia.org/wiki/Origin_Recognition_Complex |
The ATPase activity of Orc1 is involved in formation of the pre-RC. ATP binding by Orc5 is crucial for the stability of ORC as a whole. | https://en.wikipedia.org/wiki/Origin_Recognition_Complex |
Only the Orc1-5 subunits are required for origin binding; Orc6 is essential for maintenance of pre-RCs once formed. Interactions within ORC suggest that Orc2-3-6 may form a core complex. A 2020 report suggests that budding yeast ORC dimerizes in a cell cycle dependent manner to control licensing. | https://en.wikipedia.org/wiki/Origin_Recognition_Complex |
In molecular biology, ornatin is a potent glycoprotein IIb-IIIa (GP IIb-IIIa) antagonist and platelet aggregation inhibitor isolated from Placobdella ornata (Turtle leech). The protein is 41-52 amino acids in length and contains the RGD recognition motif common in adhesion proteins, and 6 conserved cysteine residues. These form three disulphide bonds, which are required for activity. | https://en.wikipedia.org/wiki/Ornatin |
The sequences of ornatin B, C, D and E are highly similar, while A2 and A3 are less similar, lacking the N-terminal 9 residues. Ornatins share ~40% identity with decorsin, a GP IIb-IIIa antagonist isolated from the leech (Macrobdella decora). == References == | https://en.wikipedia.org/wiki/Ornatin |
In molecular biology, pertactin (PRN) is a highly immunogenic virulence factor of Bordetella pertussis, the bacterium that causes pertussis. Specifically, it is an outer membrane protein that promotes adhesion to tracheal epithelial cells. PRN is purified from Bordetella pertussis and is used for the vaccine production as one of the important components of acellular pertussis vaccine.A large part of the N-terminus of the pertactin protein is composed of beta helix repeats. This region of the pertactin protein is secreted through the C-terminal autotransporter. | https://en.wikipedia.org/wiki/Pertactin |
The N-terminal signal sequences promotes the secretion of PRN into the periplasm through the bacterial secretion system (Sec) and consequently, the translocation into the outer membrane where it is proteolytically cleaved. The loops in the right handed β-helix of the N-terminus that protrudes out of cell surface (region R1) contains sequence repeats Gly-Gly-Xaa-Xaa-Pro and the RGD domain Arg-Gly-Asp. This RGD domain allows PRN to function as an adhesin and invasin, binding to integrins on the outer membrane of the cell. | https://en.wikipedia.org/wiki/Pertactin |
Another loop of the extending β-helix is region 2 (R2) which contains Pro-Gln-Pro (PQP) repeats towards the C-terminus. This protein’s contribution to immunity is still premature. Reports suggest that R1 and R2 are immunogenic regions, however, recent studies regarding genetic variation of those regions prove otherwise. | https://en.wikipedia.org/wiki/Pertactin |
In molecular biology, protein aggregation is a phenomenon in which intrinsically-disordered or mis-folded proteins aggregate (i.e., accumulate and clump together) either intra- or extracellularly. Protein aggregates have been implicated in a wide variety of diseases known as amyloidoses, including ALS, Alzheimer's, Parkinson's and prion disease.After synthesis, proteins typically fold into a particular three-dimensional conformation that is the most thermodynamically favorable: their native state. This folding process is driven by the hydrophobic effect: a tendency for hydrophobic (water-fearing) portions of the protein to shield themselves from the hydrophilic (water-loving) environment of the cell by burying into the interior of the protein. Thus, the exterior of a protein is typically hydrophilic, whereas the interior is typically hydrophobic. | https://en.wikipedia.org/wiki/Protein_aggregates |
Protein structures are stabilized by non-covalent interactions and disulfide bonds between two cysteine residues. The non-covalent interactions include ionic interactions and weak van der Waals interactions. Ionic interactions form between an anion and a cation and form salt bridges that help stabilize the protein. | https://en.wikipedia.org/wiki/Protein_aggregates |
Van der Waals interactions include nonpolar interactions (i.e. London dispersion force) and polar interactions (i.e. hydrogen bonds, dipole-dipole bond). These play an important role in a protein's secondary structure, such as forming an alpha helix or a beta sheet, and tertiary structure. Interactions between amino acid residues in a specific protein are very important in that protein's final structure. | https://en.wikipedia.org/wiki/Protein_aggregates |
When there are changes in the non-covalent interactions, as may happen with a change in the amino acid sequence, the protein is susceptible to misfolding or unfolding. In these cases, if the cell does not assist the protein in re-folding, or degrade the unfolded protein, the unfolded/misfolded protein may aggregate, in which the exposed hydrophobic portions of the protein may interact with the exposed hydrophobic patches of other proteins. There are three main types of protein aggregates that may form: amorphous aggregates, oligomers, and amyloid fibrils. | https://en.wikipedia.org/wiki/Protein_aggregates |
In molecular biology, protein catabolism is the breakdown of proteins into smaller peptides and ultimately into amino acids. Protein catabolism is a key function of digestion process. Protein catabolism often begins with pepsin, which converts proteins into polypeptides. | https://en.wikipedia.org/wiki/Protein_breakdown |
These polypeptides are then further degraded. In humans, the pancreatic proteases include trypsin, chymotrypsin, and other enzymes. In the intestine, the small peptides are broken down into amino acids that can be absorbed into the bloodstream. These absorbed amino acids can then undergo amino acid catabolism, where they are utilized as an energy source or as precursors to new proteins.The amino acids produced by catabolism may be directly recycled to form new proteins, converted into different amino acids, or can undergo amino acid catabolism to be converted to other compounds via the Krebs cycle. | https://en.wikipedia.org/wiki/Protein_breakdown |
In molecular biology, protein fold classes are broad categories of protein tertiary structure topology. They describe groups of proteins that share similar amino acid and secondary structure proportions. Each class contains multiple, independent protein superfamilies (i.e. are not necessarily evolutionarily related to one another). | https://en.wikipedia.org/wiki/Protein_fold_class |
In molecular biology, protein threading, also known as fold recognition, is a method of protein modeling which is used to model those proteins which have the same fold as proteins of known structures, but do not have homologous proteins with known structure. It differs from the homology modeling method of structure prediction as it (protein threading) is used for proteins which do not have their homologous protein structures deposited in the Protein Data Bank (PDB), whereas homology modeling is used for those proteins which do. Threading works by using statistical knowledge of the relationship between the structures deposited in the PDB and the sequence of the protein which one wishes to model. The prediction is made by "threading" (i.e. placing, aligning) each amino acid in the target sequence to a position in the template structure, and evaluating how well the target fits the template. After the best-fit template is selected, the structural model of the sequence is built based on the alignment with the chosen template. Protein threading is based on two basic observations: that the number of different folds in nature is fairly small (approximately 1300); and that 90% of the new structures submitted to the PDB in the past three years have similar structural folds to ones already in the PDB. | https://en.wikipedia.org/wiki/Fold_recognition |
In molecular biology, proteins containing the carboxyl transferase domain include biotin-dependent carboxylases. This domain carries out the following reaction: transcarboxylation from biotin to an acceptor molecule. There are two recognised types of carboxyl transferase. | https://en.wikipedia.org/wiki/Carboxyl_transferase_domain |
One of them uses acyl-CoA and the other uses 2-oxo acid as the acceptor molecule of carbon dioxide. All of the members in this family use acyl-CoA as the acceptor molecule. == References == | https://en.wikipedia.org/wiki/Carboxyl_transferase_domain |
In molecular biology, quantitation of nucleic acids is commonly performed to determine the average concentrations of DNA or RNA present in a mixture, as well as their purity. Reactions that use nucleic acids often require particular amounts and purity for optimum performance. To date, there are two main approaches used by scientists to quantitate, or establish the concentration, of nucleic acids (such as DNA or RNA) in a solution. These are spectrophotometric quantification and UV fluorescence tagging in presence of a DNA dye. | https://en.wikipedia.org/wiki/Quantification_of_nucleic_acids |
In molecular biology, repeat-induced point mutation or RIP is a process by which DNA accumulates G:C to A:T transition mutations. Genomic evidence indicates that RIP occurs or has occurred in a variety of fungi while experimental evidence indicates that RIP is active in Neurospora crassa, Podospora anserina, Magnaporthe grisea, Leptosphaeria maculans, Gibberella zeae and Nectria haematococca. In Neurospora crassa, sequences mutated by RIP are often methylated de novo.RIP occurs during the sexual stage in haploid nuclei after fertilization but prior to meiotic DNA replication. In Neurospora crassa, repeat sequences of at least 400 base pairs in length are vulnerable to RIP. | https://en.wikipedia.org/wiki/Point_mutation |
Repeats with as low as 80% nucleotide identity may also be subject to RIP. Though the exact mechanism of repeat recognition and mutagenesis are poorly understood, RIP results in repeated sequences undergoing multiple transition mutations. | https://en.wikipedia.org/wiki/Point_mutation |
The RIP mutations do not seem to be limited to repeated sequences. Indeed, for example, in the phytopathogenic fungus L. maculans, RIP mutations are found in single copy regions, adjacent to the repeated elements. These regions are either non-coding regions or genes encoding small secreted proteins including avirulence genes. | https://en.wikipedia.org/wiki/Point_mutation |
The degree of RIP within these single copy regions was proportional to their proximity to repetitive elements.Rep and Kistler have speculated that the presence of highly repetitive regions containing transposons, may promote mutation of resident effector genes. So the presence of effector genes within such regions is suggested to promote their adaptation and diversification when exposed to strong selection pressure.As RIP mutation is traditionally observed to be restricted to repetitive regions and not single copy regions, Fudal et al. suggested that leakage of RIP mutation might occur within a relatively short distance of a RIP-affected repeat. Indeed, this has been reported in N. crassa whereby leakage of RIP was detected in single copy sequences at least 930 bp from the boundary of neighbouring duplicated sequences. To elucidate the mechanism of detection of repeated sequences leading to RIP may allow to understand how the flanking sequences may also be affected. | https://en.wikipedia.org/wiki/Point_mutation |
In molecular biology, restriction fragment length polymorphism (RFLP) is a technique that exploits variations in homologous DNA sequences, known as polymorphisms, populations, or species or to pinpoint the locations of genes within a sequence. The term may refer to a polymorphism itself, as detected through the differing locations of restriction enzyme sites, or to a related laboratory technique by which such differences can be illustrated. In RFLP analysis, a DNA sample is digested into fragments by one or more restriction enzymes, and the resulting restriction fragments are then separated by gel electrophoresis according to their size. RFLP analysis is now largely obsolete due to the emergence of inexpensive DNA sequencing technologies, but it was the first DNA profiling technique inexpensive enough to see widespread application. RFLP analysis was an important early tool in genome mapping, localization of genes for genetic disorders, determination of risk for disease, and paternity testing. | https://en.wikipedia.org/wiki/Restriction_Fragment_Length_Polymorphism |
In molecular biology, ribosomal s6 kinase (rsk) is a family of protein kinases involved in signal transduction. There are two subfamilies of rsk, p90rsk, also known as MAPK-activated protein kinase-1 (MAPKAP-K1), and p70rsk, also known as S6-H1 Kinase or simply S6 Kinase. There are three variants of p90rsk in humans, rsk 1-3. Rsks are serine/threonine kinases and are activated by the MAPK/ERK pathway. There are two known mammalian homologues of S6 Kinase: S6K1 and S6K2. | https://en.wikipedia.org/wiki/Ribosomal_s6_kinase |
In molecular biology, sirohaem synthase (or siroheme synthase) (CysG) is a multi-functional enzyme with S-adenosyl-L-methionine (SAM)-dependent bismethyltransferase, dehydrogenase and ferrochelatase activities. Bacterial sulphur metabolism depends on the iron-containing porphinoid sirohaem. CysG synthesizes sirohaem from uroporphyrinogen III via reactions which encompass two branchpoint intermediates in tetrapyrrole biosynthesis, diverting flux first from protoporphyrin IX biosynthesis and then from cobalamin (vitamin B12) biosynthesis. CysG is a dimer. Its dimerisation region is 74 amino acids long, and acts to hold the two structurally similar protomers held together asymmetrically through a number of salt-bridges across complementary residues within the dimerisation region. CysG dimerisation produces a series of active sites, accounting for CysG's multi-functionality, catalysing four diverse reactions: Two SAM-dependent methylations NAD+-dependent tetrapyrrole dehydrogenation Metal chelation == References == | https://en.wikipedia.org/wiki/Sirohaem_synthase |
In molecular biology, small Cajal body specific RNA 4 (also known as ACA26) is believed to be a guide RNA of the H/ACA box class, since it has the predicted hairpin-hinge-hairpin-tail structure, conserved H/ACA-box motifs, and is found associated with GAR1. In particular, ACA26 is predicted to guide the pseudouridylation of residues U39 and U41 in U2 snRNA. Such scaRNAs are a specific class of small nuclear RNAs that localise to the Cajal bodies and guide the modification of RNA polymerase II transcribed spliceosomal RNAs U1, U2, U4, U5 and U12. | https://en.wikipedia.org/wiki/Small_Cajal_body_specific_RNA_4 |
In molecular biology, small nucleolar RNA R71 (also known as snoRNA R71) is a non-coding RNA (ncRNA) molecule which functions in the modification of other small nuclear RNAs (snRNAs). This type of modifying RNA is usually located in the nucleolus of the eukaryotic cell which is a major site of snRNA biogenesis. It is known as a small nucleolar RNA (snoRNA) and also often referred to as a guide RNA. R71 belongs to the C/D box class of snoRNAs which contain the conserved sequence motifs known as the C box (UGAUGA) and the D box (CUGA). Most of the members of the box C/D family function in directing site-specific 2'-O-methylation of substrate RNAs.Multiple, nearly identical copies of this snoRNA have been identified in the Arabidopsis thaliana genome and it is thought to function as a 2'-O-ribose methylation guide for 18S ribosomal RNA (rRNA). | https://en.wikipedia.org/wiki/Plant_small_nucleolar_RNA_R71 |
In molecular biology, small nucleolar RNA SNORA10 and small nuclear RNA SNORA64 are homologous members of the H/ACA class of small nucleolar RNA (snoRNA). This family of ncRNAs involved in the maturation of ribosomal RNA. snoRNA in this family act as guides in the modification of uridines to pseudouridines. This family includes the human snoRNAs U64 and ACA10 and mouse MBI-29. | https://en.wikipedia.org/wiki/Small_nucleolar_RNA_SNORA64/SNORA10_family |
In molecular biology, small nucleolar RNA SNORA11 (also known as U107) is a non-coding RNA (ncRNA) molecule which functions in the biogenesis (modification) of other small nuclear RNAs (snRNAs). This type of modifying RNA is located in the nucleolus of the eukaryotic cell which is a major site of snRNA biogenesis. It is known as a small nucleolar RNA (snoRNA). | https://en.wikipedia.org/wiki/Small_nucleolar_RNA_SNORA11 |
U107 has a predicted hairpin-hinge-hairpin-tail structure and is predicted to be a member of the H/ACA box class of snoRNAs that guide the sites of modification of uridines to pseudouridines. This snoRNA was identified by RT-PCR from blood cells and its expression confirmed by Northern blot analysis. There is no predicted RNA target for this guide snRNA. | https://en.wikipedia.org/wiki/Small_nucleolar_RNA_SNORA11 |
In molecular biology, small nucleolar RNA SNORA72 (also known as U72) is a non-coding RNA (ncRNA) molecule which functions in the biogenesis (modification) of other small nuclear RNAs (snRNAs). This type of modifying RNA is located in the nucleolus of the eukaryotic cell which is a major site of snRNA biogenesis. It is known as a small nucleolar RNA (snoRNA) and also often referred to as a "guide RNA". | https://en.wikipedia.org/wiki/Small_nucleolar_RNA_SNORA72 |
ACA30 was originally cloned from HeLa cells and belongs to the H/ACA box class of snoRNAs as it has the predicted hairpin-hinge-hairpin-tail structure, has the conserved H/ACA-box motifs and is found associated with GAR1 protein. snoRNA ACA72 is predicted to guide the pseudouridylation of U55 of 5.8S ribosomal RNA (rRNA). Pseudouridylation is the (isomerisation of the nucleoside uridine) to the different isomeric form pseudouridine. | https://en.wikipedia.org/wiki/Small_nucleolar_RNA_SNORA72 |
In molecular biology, small nucleolar RNA derived microRNAs are microRNAs (miRNA) derived from small nucleolar RNA (snoRNA). MicroRNAs are usually derived from precursors known as pre-miRNAs, these pre-miRNAs are recognised and cleaved from a pri-miRNA precursor by the Pasha and Drosha proteins. However some microRNAs, mirtrons, are known to be derived from introns via a different pathway which bypasses Pasha and Drosha. Some microRNAs are also known to be derived from small nucleolar RNA. | https://en.wikipedia.org/wiki/Small_nucleolar_RNA-derived_microRNA |
In molecular biology, small nucleolar RNAs (snoRNAs) are a class of small RNA molecules that primarily guide chemical modifications of other RNAs, mainly ribosomal RNAs, transfer RNAs and small nuclear RNAs. There are two main classes of snoRNA, the C/D box snoRNAs, which are associated with methylation, and the H/ACA box snoRNAs, which are associated with pseudouridylation. SnoRNAs are commonly referred to as guide RNAs but should not be confused with the guide RNAs that direct RNA editing in trypanosomes or the guide RNAs (gRNAs) used by Cas9 for CRISPR gene editing. | https://en.wikipedia.org/wiki/Small_nucleolar_RNA |
In molecular biology, snR54 is a non-coding RNA that is a member of the C/D class of snoRNA which contain the C box motif (UGAUGA) and D box motif (CUGA). Most of the members of the box C/D family function in directing site-specific 2'-O-methylation of substrate RNAs. This snoRNA was first identified by a computational screen followed by experimental verification. This RNA guides the 2'-O-methylation of 18S rRNA. In yeast this snoRNA is found to reside in an intron of the IMD4 gene. | https://en.wikipedia.org/wiki/Small_nucleolar_RNA_snR54 |
In molecular biology, snR64 is an RNA molecule belonging to the C/D class of small nucleolar RNA (snoRNA), which contain the C (UGAUGA) and D (CUGA) box motifs. Similar to most members of the box C/D family, snR64 is conjectured to help direct site-specific 2'-O-methylation of substrate RNAs. | https://en.wikipedia.org/wiki/Small_nucleolar_RNA_snR64 |
In molecular biology, snoR9 is a non-coding RNA (ncRNA) which functions in the biogenesis (modification) of other small nuclear RNAs (snRNAs). It is known as a small nucleolar RNA (snoRNA) and also often referred to as a 'guide RNA'. R9 is a member of the C/D box class of snoRNAs which contain the conserved sequence motifs known as the C box (UGAUGA) and the D box (CUGA). Most of the members of the box C/D family function in directing site-specific 2'-O-methylation of substrate RNAs.This plant snoRNA was identified in Arabidopsis thaliana by computational screening and experimentally verified by primer extension analysis. This snoRNA is not related to the snoRNA identified in hyperthermophiles also called snoR9. | https://en.wikipedia.org/wiki/Small_nucleolar_RNA_snoR9_plant |
In molecular biology, snoRNA HBII-210 belongs to the C/D family of snoRNAs. It is the human orthologue of the mouse MBII-210 and is predicted to guide the 2'O-ribose methylation of large 28S rRNA on residue G4464. | https://en.wikipedia.org/wiki/Small_nucleolar_RNA_SNORD69 |
In molecular biology, snoRNA HBII-239 belongs to the family of C/D snoRNAs. It is the human orthologue of the mouse MBII-239 described and is predicted to guide 2'O-ribose methylation of 5.8S rRNA on residue U14. | https://en.wikipedia.org/wiki/Small_nucleolar_RNA_SNORD71 |
In molecular biology, snoRNA HBII-289 belongs to the family of C/D snoRNAs. It is the human orthologue of the mouse MBII-289 and has no identified RNA target. | https://en.wikipedia.org/wiki/Small_nucleolar_RNA_SNORD89 |
In molecular biology, snoRNA SNORD70 (HBII-234) is a non-coding RNA that belongs to the C/D family of snoRNAs. It is the human orthologue of the mouse MBII-234 and is predicted to guide 2'O-ribose methylation of the small 18S rRNA on position A512. It is hosted, together with HBII-95, by the core C/D box snoRNA protein encoding gene NOP5/NOP58. | https://en.wikipedia.org/wiki/Small_nucleolar_RNA_SNORD70 |
In molecular biology, snoRNA SNORD90 (HBII-295) is a non-coding RNA that belongs to the family of C/D snoRNAs. Initially described as HBII-295 this RNA has now been called SNORD70 by the HUGO Gene Nomenclature Committee. It is the human orthologue of the mouse MBII-295 and has no identified RNA target. | https://en.wikipedia.org/wiki/Small_nucleolar_RNA_SNORD90 |
This RNA is expressed from an intron of the MNAB/OR1K1 gene. There is evidence that SNORD90 is involved in guiding N6-methyladenosine (m6A) modifications onto target RNA transcripts. Specifically, SNORD90 has been shown to increase m6A levels on neuregulin 3 (NRG3) leading to its down-regulation through recognition by YTHDF2. | https://en.wikipedia.org/wiki/Small_nucleolar_RNA_SNORD90 |
In molecular biology, snoRNA U101 (also known as SNORD101) is a non-coding RNA (ncRNA) molecule which functions in the modification of other small nuclear RNAs (snRNAs). This type of modifying RNA is usually located in the nucleolus of the eukaryotic cell which is a major site of snRNA biogenesis. It is known as a small nucleolar RNA (snoRNA) and also often referred to as a guide RNA. | https://en.wikipedia.org/wiki/Small_nucleolar_RNA_SNORD101 |
snoRNA U101 belongs to the C/D box class of snoRNAs which contain the conserved sequence motifs known as the C box (UGAUGA) and the D box (CUGA). Most of the members of the box C/D family function in directing site-specific 2'-O-methylation of substrate RNAs.U101 was identified by computational screening of the introns of ribosomal protein genes for conserved C/D box sequence motifs and expression experimentally verified by northern blotting. snoRNA U101 resides in intron 3 of the ribosomal protein S12. U101 shares the same host gene with C/D box snoRNA HBII-429, and the H/ACA box snoRNA ACA33.There is currently no predicted methylation target for U101. | https://en.wikipedia.org/wiki/Small_nucleolar_RNA_SNORD101 |
In molecular biology, snoRNA U102 (also known as SNORD102) is a non-coding RNA (ncRNA) molecule which functions in the modification of other small nuclear RNAs (snRNAs). This type of modifying RNA is usually located in the nucleolus of the eukaryotic cell which is a major site of snRNA biogenesis. It is known as a small nucleolar RNA (snoRNA) and also often referred to as a guide RNA. | https://en.wikipedia.org/wiki/Small_nucleolar_RNA_SNORD102 |
snoRNA U102 belongs to the C/D box class of snoRNAs which contain the conserved sequence motifs known as the C box (UGAUGA) and the D box (CUGA). Most of the members of the box C/D family function in directing site-specific 2'-O-methylation of substrate RNAs.U102 was identified by computational screening of the introns of ribosomal protein genes for conserved C/D box sequence motifs and expression experimentally verified by northern blotting. It is found within intron 2 of the L21 ribosomal protein gene. The H/ACA box snoRNA ACA27 is found in the same host gene within a different intron.U102 is predicted to guide the 2'O-ribose methylation of 28S ribosomal RNA (rRNA) residue G4020. | https://en.wikipedia.org/wiki/Small_nucleolar_RNA_SNORD102 |
In molecular biology, snoRNA U103 (also known as SNORD103) is a non-coding RNA (ncRNA) molecule which functions in the modification of other small nuclear RNAs (snRNAs). This type of modifying RNA is usually located in the nucleolus of the eukaryotic cell which is a major site of snRNA biogenesis. It is known as a small nucleolar RNA (snoRNA) and also often referred to as a guide RNA. | https://en.wikipedia.org/wiki/Small_nucleolar_RNA_SNORD103 |
snoRNA U103 belongs to the C/D box class of snoRNAs which contain the conserved sequence motifs known as the C box (UGAUGA) and the D box (CUGA). Most of the members of the box C/D family function in directing site-specific 2'-O-methylation of substrate RNAs.U103 was identified by computational screening of the introns of ribosomal protein genes for conserved C/D box sequence motifs and expression experimentally verified by northern blotting.U103 is predicted to guide the 2'O-ribose methylation of 18S ribosomal RNA (rRNA) residue G601. In both the human and mouse genome there are two U103 gene copies (called U103A or SNORD103A and U103B or SNORD103B) located within introns 17 and 21 of the PUM1 gene. | https://en.wikipedia.org/wiki/Small_nucleolar_RNA_SNORD103 |
In molecular biology, snoRNA U16 (also known as SNORD16) is a non-coding RNA (ncRNA) molecule which functions in the modification of other small nuclear RNAs (snRNAs). This type of modifying RNA is usually located in the nucleolus of the eukaryotic cell which is a major site of snRNA biogenesis. It is known as a small nucleolar RNA (snoRNA) and also often referred to as a guide RNA. | https://en.wikipedia.org/wiki/Small_nucleolar_RNA_SNORD16 |
snoRNA U16 belongs to the C/D box class of snoRNAs which contain the conserved sequence motifs known as the C box (UGAUGA) and the D box (CUGA). Most of the members of the box C/D family function in directing site-specific 2'-O-methylation of substrate RNAs.U16 is predicted to guide the 2'O-ribose methylation of 18S ribosomal RNA (rRNA) residue A484 and is encoded within an intron of the gene for ribosomal proteins L1 in animals. This snoRNA was independently named MBII-98 in mouse. | https://en.wikipedia.org/wiki/Small_nucleolar_RNA_SNORD16 |
In molecular biology, snoRNA U20 (also known as SNORD20) is a non-coding RNA (ncRNA) molecule which functions in the modification of other small nuclear RNAs (snRNAs). This type of modifying RNA is usually located in the nucleolus of the eukaryotic cell which is a major site of snRNA biogenesis. It is known as a small nucleolar RNA (snoRNA) and also often referred to as a guide RNA. | https://en.wikipedia.org/wiki/Small_nucleolar_RNA_SNORD20 |
snoRNA U20 belongs to the C/D box class of snoRNAs which contain the conserved sequence motifs known as the C box (UGAUGA) and the D box (CUGA). Most of the members of the box C/D family function in directing site-specific 2'-O-methylation of substrate RNAs.U20 is encoded in intron 11 of the nucleolin gene in human, mouse and rat. It is predicted to guide the 2'O-ribose methylation of 18S ribosomal RNA (rRNA) residue U1804. | https://en.wikipedia.org/wiki/Small_nucleolar_RNA_SNORD20 |
In molecular biology, snoRNA U22 (also known as SNORD22) is a non-coding RNA (ncRNA) molecule which functions in the modification of other small nuclear RNAs (snRNAs). This type of modifying RNA is usually located in the nucleolus of the eukaryotic cell which is a major site of snRNA biogenesis. It is known as a small nucleolar RNA (snoRNA) and also often referred to as a guide RNA. | https://en.wikipedia.org/wiki/Small_nucleolar_RNA_SNORD22 |
U22 belongs to the C/D box class of snoRNAs which contain the conserved sequence motifs known as the C box (UGAUGA) and the D box (CUGA). Most of the members of the box C/D family function in directing site-specific 2'-O-methylation of substrate RNAs.In the human genome snoRNA U22 is encoded along with seven other snoRNAs within the introns of the same gene (called UHG for U22 host gene) in mammals. U22 has also been identified in the amphibian Xenopus laevis U22 is predicted to guide the 2'-O-ribose methylation guide for ribosomal RNA. | https://en.wikipedia.org/wiki/Small_nucleolar_RNA_SNORD22 |
In molecular biology, snoRNA U25 (also known as SNORD25) is a non-coding RNA (ncRNA) molecule which functions in the biogenesis (modification) of other small nuclear RNAs (snRNAs). This type of modifying RNA is located in the nucleolus of the eukaryotic cell which is a major site of snRNA biogenesis. It is known as a small nucleolar RNA (snoRNA) and also often referred to as a guide RNA. U25 is a member of the C/D box class of snoRNAs which contain the conserved sequence motifs known as the C box (UGAUGA) and the D box (CUGA). | https://en.wikipedia.org/wiki/Small_nucleolar_RNA_SNORD25 |
Most of the members of the box C/D family function in directing site-specific 2'-O-methylation of substrate RNAs.U25 is found in gene clusters in plants and within the U22 snoRNA host gene (UHG) in mammals. U25 is thought to as a 2'-O-ribose methylation guide for ribosomal RNA. This RNA has also been named snoRNA R73 in some plants. | https://en.wikipedia.org/wiki/Small_nucleolar_RNA_SNORD25 |
In molecular biology, snoRNA U32 (also known as SNORD32) is a non-coding RNA (ncRNA) molecule which functions in the modification of other small nuclear RNAs (snRNAs). This type of modifying RNA is usually located in the nucleolus of the eukaryotic cell which is a major site of snRNA biogenesis. It is known as a small nucleolar RNA (snoRNA) and also often referred to as a guide RNA. | https://en.wikipedia.org/wiki/Small_nucleolar_RNA_SNORD32 |
snoRNA U32 belongs to the C/D box class of snoRNAs which contain the conserved sequence motifs known as the C box (UGAUGA) and the D box (CUGA). Most of the members of the box C/D family function in directing site-specific 2'-O-methylation of substrate RNAs.U32 is encoded within intron 2 of the ribosomal protein L13 gene in human and mouse and is predicted to guide the 2'O-ribose methylation of both 18S ribosomal RNA (rRNA) residue G1328 and 28S rRNA residue A1511. U32A share the same host gene with the C/D box snoRNAs U33, U34 and U35A (RPL13A). | https://en.wikipedia.org/wiki/Small_nucleolar_RNA_SNORD32 |
In molecular biology, snoRNA U34 (also known as SNORD34) is a non-coding RNA (ncRNA) molecule which functions in the modification of other small nuclear RNAs (snRNAs). This type of modifying RNA is usually located in the nucleolus of the eukaryotic cell which is a major site of snRNA biogenesis. It is known as a small nucleolar RNA (snoRNA) and also often referred to as a guide RNA. | https://en.wikipedia.org/wiki/Small_nucleolar_RNA_SNORD34 |
snoRNA U34 belongs to the C/D box class of snoRNAs which contain the conserved sequence motifs known as the C box (UGAUGA) and the D box (CUGA). Most of the members of the box C/D family function in directing site-specific 2'-O-methylation of substrate RNAs.snoRNA U34 was initially characterised by a computational screen and in the human genome is encoded within intron 5 of the gene for ribosomal protein L13a. U34 is predicted to guide site-specific 2'-O-methylation of 25S rRNAs. Unusually for a snoRNA although the selection of the target nucleotide requires the antisense element and the conserved box D or D' of the snoRNA, in the case of U34 snoRNP the methyltransferase activity is thought to reside in one of the protein components. U34 snoRNA has homologues in mouse, Arabidopsis (annotated as snoR4) and in several copies in rice (alternatively named snoZ181). | https://en.wikipedia.org/wiki/Small_nucleolar_RNA_SNORD34 |
In molecular biology, snoRNA U35 (also known as SNORD35) is a non-coding RNA (ncRNA) molecule which functions in the modification of other small nuclear RNAs (snRNAs). This type of modifying RNA is usually located in the nucleolus of the eukaryotic cell which is a major site of snRNA biogenesis. It is known as a small nucleolar RNA (snoRNA) and also often referred to as a guide RNA. | https://en.wikipedia.org/wiki/Small_nucleolar_RNA_SNORD35 |
snoRNA U35 belongs to the C/D box class of snoRNAs which contain the conserved sequence motifs known as the C box (UGAUGA) and the D box (CUGA). Most of the members of the box C/D family function in directing site-specific 2'-O-methylation of substrate RNAs.U35 is encoded in intron 6 of ribosomal protein L13A and intron 3 of ribosomal protein S11 in humans and at homologous positions in mouse and chicken ribosomal protein genes. U35 is predicted to guide the 2'O-ribose methylation of 28S ribosomal RNA (rRNA) residue C4506. | https://en.wikipedia.org/wiki/Small_nucleolar_RNA_SNORD35 |
In molecular biology, snoRNA U36 (also known as SNORD36) is a non-coding RNA (ncRNA) molecule which functions in the biogenesis (modification) of other small nuclear RNAs (snRNAs). This type of modifying RNA is located in the nucleolus of the eukaryotic cell which is a major site of snRNA biogenesis. It is known as a small nucleolar RNA (snoRNA) and also often referred to as a guide RNA. snoRNA U36 is a member of the C/D box class of snoRNAs which contain the conserved sequence motifs known as the C box (UGAUGA) and the D box (CUGA). | https://en.wikipedia.org/wiki/Small_nucleolar_RNA_SNORD36 |
Most of the members of the box C/D family function in directing site-specific 2'-O-methylation of substrate RNAs.U36 is encoded within the intron of ribosomal protein rpL7a, and has two regions of complementarity to 18S and 28S ribosomal RNA. This complementarity suggests that U36 acts as a 2'-O-ribose methylation guide. This snoRNA is also related to other snoRNAs (snoR47 and Z100) identified in the rice plant Oryza sativa. | https://en.wikipedia.org/wiki/Small_nucleolar_RNA_SNORD36 |
In molecular biology, snoRNA U38 (also known as SNORD38) is a non-coding RNA (ncRNA) molecule which functions in the modification of other small nuclear RNAs (snRNAs). This type of modifying RNA is usually located in the nucleolus of the eukaryotic cell which is a major site of snRNA biogenesis. It is known as a small nucleolar RNA (snoRNA) and also often referred to as a guide RNA. snoRNA U38 belongs to the C/D box class of snoRNAs which contain the conserved sequence motifs known as the C box (UGAUGA) and the D box (CUGA). | https://en.wikipedia.org/wiki/Small_nucleolar_RNA_SNORD38 |
Most of the members of the box C/D family function in directing site-specific 2'-O-methylation of substrate RNAs.U38 is located in introns 4 and 5 of ribosomal protein S8 in human and in the homologous genes in mouse and cow. U38 is predicted to guides the methylation of 2'-O-ribose residues in 28S ribosomal RNA (rRNA). The mouse homologue of U38 (MBII-329) has also been identified. | https://en.wikipedia.org/wiki/Small_nucleolar_RNA_SNORD38 |
In molecular biology, snoRNA U39 (also known as SNORD39) is a non-coding RNA (ncRNA) molecule which functions in the modification of other small nuclear RNAs (snRNAs). This type of modifying RNA is usually located in the nucleolus of the eukaryotic cell which is a major site of snRNA biogenesis. It is known as a small nucleolar RNA (snoRNA) and also often referred to as a guide RNA. snoRNA U39 belongs to the C/D box class of snoRNAs which contain the conserved sequence motifs known as the C box (UGAUGA) and the D box (CUGA). Most of the members of the box C/D family function in directing site-specific 2'-O-methylation of substrate RNAs.snoRNA U39 was cloned from HeLa cells and also independently characterised by bioinformatics prediction (and called U55 also known as SNORD55).U39/U55 is predicted to guide the 2'O-ribose methylation of 28S ribosomal RNA (rRNA) C2791. | https://en.wikipedia.org/wiki/Small_nucleolar_RNA_SNORD39 |
In molecular biology, snoRNA U41 (also known as SNORD41) belongs to the C/D box class of snoRNAs. It is predicted to guide 2'O-ribose methylation of the large 28S rRNA on residue U4276. | https://en.wikipedia.org/wiki/Small_nucleolar_RNA_SNORD41 |
In molecular biology, snoRNA U42 (also known as SNORD42) is a non-coding RNA (ncRNA) molecule which functions in the modification of other small nuclear RNAs (snRNAs). This type of modifying RNA is usually located in the nucleolus of the eukaryotic cell which is a major site of snRNA biogenesis. It is known as a small nucleolar RNA (snoRNA) and also often referred to as a guide RNA. snoRNA U42 belongs to the C/D box class of snoRNAs which contain the conserved sequence motifs known as the C box (UGAUGA) and the D box (CUGA). | https://en.wikipedia.org/wiki/Small_nucleolar_RNA_SNORD42 |
Most of the members of the box C/D family function in directing site-specific 2'-O-methylation of substrate RNAs.In the human genome there are two closely related copies of U42 (called U42A and U42B) both located within the introns of the ribosomal protein L23a (RPL23a) gene. Both snoRNAs are predicted to guide the site specific 2'O-ribose methylation of 18S ribosomal RNA (rRNA) residue U116. The mouse orthologue (MBII-287) has also been identified. | https://en.wikipedia.org/wiki/Small_nucleolar_RNA_SNORD42 |
In molecular biology, snoRNA U43 (also known as SNORD43) is a non-coding RNA (ncRNA) molecule which functions in the modification of other small nuclear RNAs (snRNAs). This type of modifying RNA is usually located in the nucleolus of the eukaryotic cell which is a major site of snRNA biogenesis. It is known as a small nucleolar RNA (snoRNA) and also often referred to as a guide RNA. snoRNA U43 belongs to the C/D box class of snoRNAs which contain the conserved sequence motifs known as the C box (UGAUGA) and the D box (CUGA). | https://en.wikipedia.org/wiki/Small_nucleolar_RNA_SNORD43 |
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