Ubiquitin. Medical search

A highly conserved 76-amino acid peptide universally found in eukaryotic cells that functions as a marker for intracellular PROTEIN TRANSPORT and degradation. Ubiquitin becomes activated through a series of complicated steps and forms an isopeptide bond to lysine residues of specific proteins within the cell. These "ubiquitinated" proteins can be recognized and degraded by proteosomes or be transported to specific compartments within the cell.

A diverse class of enzymes that interact with UBIQUITIN-CONJUGATING ENZYMES and ubiquitination-specific protein substrates. Each member of this enzyme group has its own distinct specificity for a substrate and ubiquitin-conjugating enzyme. Ubiquitin-protein ligases exist as both monomeric proteins multiprotein complexes.

A family of proteins that are structurally-related to Ubiquitin. Ubiquitins and ubiquitin-like proteins participate in diverse cellular functions, such as protein degradation and HEAT-SHOCK RESPONSE, by conjugation to other proteins.

A thioester hydrolase which acts on esters formed between thiols such as DITHIOTHREITOL or GLUTATHIONE and the C-terminal glycine residue of UBIQUITIN.

The act of ligating UBIQUITINS to PROTEINS to form ubiquitin-protein ligase complexes to label proteins for transport to the PROTEASOME ENDOPEPTIDASE COMPLEX where proteolysis occurs.

A class of enzymes that form a thioester bond to UBIQUITIN with the assistance of UBIQUITIN-ACTIVATING ENZYMES. They transfer ubiquitin to the LYSINE of a substrate protein with the assistance of UBIQUITIN-PROTEIN LIGASES.

A large multisubunit complex that plays an important role in the degradation of most of the cytosolic and nuclear proteins in eukaryotic cells. It contains a 700-kDa catalytic sub-complex and two 700-kDa regulatory sub-complexes. The complex digests ubiquitinated proteins and protein activated via ornithine decarboxylase antizyme.

A family of structurally related proteins that were originally discovered for their role in cell-cycle regulation in CAENORHABDITIS ELEGANS. They play important roles in regulation of the CELL CYCLE and as components of UBIQUITIN-PROTEIN LIGASES.

An oligomer formed from the repetitive linking of the C-terminal glycine of one UBIQUITIN molecule via an isopeptide bond to a lysine residue on a second ubiquitin molecule. It is structurally distinct from UBIQUITIN C, which is a single protein containing a tandemly arrayed ubiquitin peptide sequence.

A class of enzymes that catalyze the formation of a bond between two substrate molecules, coupled with the hydrolysis of a pyrophosphate bond in ATP or a similar energy donor. (Dorland, 28th ed) EC 6.

A subset of ubiquitin protein ligases that are formed by the association of a SKP DOMAIN PROTEIN, a CULLIN DOMAIN PROTEIN and a F-BOX DOMAIN PROTEIN.

Complexes of enzymes that catalyze the covalent attachment of UBIQUITIN to other proteins by forming a peptide bond between the C-terminal GLYCINE of UBIQUITIN and the alpha-amino groups of LYSINE residues in the protein. The complexes play an important role in mediating the selective-degradation of short-lived and abnormal proteins. The complex of enzymes can be broken down into three components that involve activation of ubiquitin (UBIQUITIN-ACTIVATING ENZYMES), conjugation of ubiquitin to the ligase complex (UBIQUITIN-CONJUGATING ENZYMES), and ligation of ubiquitin to the substrate protein (UBIQUITIN-PROTEIN LIGASES).

A class of enzymes that catalyzes the ATP-dependent formation of a thioester bond between itself and UBIQUITIN. It then transfers the activated ubiquitin to one of the UBIQUITIN-PROTEIN LIGASES.

A single protein comprised of tandem repeats of the UBIQUITIN 78-amino acid sequence. It is a product of the polyubiquitin gene which contains multiple copies of the ubiquitin coding sequence. Proteolytic processing of ubiquitin C results in the formation of individual ubiquitin molecules. This protein is distinct from POLYUBIQUITIN, which is a protein formed through isopeptide linkage of multiple ubiquitin species.

A set of protein subcomplexes involved in PROTEIN SORTING of UBIQUITINATED PROTEINS into intraluminal vesicles of MULTIVESICULAR BODIES and in membrane scission during formation of intraluminal vesicles, during the final step of CYTOKINESIS, and during the budding of enveloped viruses. The ESCRT machinery is comprised of the protein products of Class E vacuolar protein sorting genes.

A family of proteins that share the F-BOX MOTIF and are involved in protein-protein interactions. They play an important role in process of protein ubiquition by associating with a variety of substrates and then associating into SCF UBIQUITIN LIGASE complexes. They are held in the ubiquitin-ligase complex via binding to SKP DOMAIN PROTEINS.

A zinc-binding domain defined by the sequence Cysteine-X2-Cysteine-X(9-39)-Cysteine-X(l-3)-His-X(2-3)-Cysteine-X2-Cysteine -X(4-48)-Cysteine-X2-Cysteine, where X is any amino acid. The RING finger motif binds two atoms of zinc, with each zinc atom ligated tetrahedrally by either four cysteines or three cysteines and a histidine. The motif also forms into a unitary structure with a central cross-brace region and is found in many proteins that are involved in protein-protein interactions. The acronym RING stands for Really Interesting New Gene.

The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.

Cleavage of proteins into smaller peptides or amino acids either by PROTEASES or non-enzymatically (e.g., Hydrolysis). It does not include Protein Processing, Post-Translational.

The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.

The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.

An E3 ubiquitin ligase primarily involved in regulation of the metaphase-to-anaphase transition during MITOSIS through ubiquitination of specific CELL CYCLE PROTEINS. Enzyme activity is tightly regulated through subunits and cofactors, which modulate activation, inhibition, and substrate specificity. The anaphase-promoting complex, or APC-C, is also involved in tissue differentiation in the PLACENTA, CRYSTALLINE LENS, and SKELETAL MUSCLE, and in regulation of postmitotic NEURONAL PLASTICITY and excitability.

Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.

Proteins covalently modified with UBIQUITINS or UBIQUITIN-LIKE PROTEINS.

A family of structurally-related proteins that were originally identified by their ability to complex with cyclin proteins (CYCLINS). They share a common domain that binds specifically to F-BOX MOTIFS. They take part in SKP CULLIN F-BOX PROTEIN LIGASES, where they can bind to a variety of F-BOX PROTEINS.

ENDOPEPTIDASES which have a cysteine involved in the catalytic process. This group of enzymes is inactivated by CYSTEINE PROTEINASE INHIBITORS such as CYSTATINS and SULFHYDRYL REAGENTS.

Members of the peptidase C19 family which regulate signal transduction by removing UBIQUITIN from specific protein substrates via a process known as deubiquitination or deubiquitylation.

An essential amino acid. It is often added to animal feed.

Proto-oncogene proteins that negatively regulate RECEPTOR PROTEIN-TYROSINE KINASE signaling. It is a UBIQUITIN-PROTEIN LIGASE and the cellular homologue of ONCOGENE PROTEIN V-CBL.

Proteins obtained from the species SACCHAROMYCES CEREVISIAE. The function of specific proteins from this organism are the subject of intense scientific interest and have been used to derive basic understanding of the functioning similar proteins in higher eukaryotes.

Systems of enzymes which function sequentially by catalyzing consecutive reactions linked by common metabolic intermediates. They may involve simply a transfer of water molecules or hydrogen atoms and may be associated with large supramolecular structures such as MITOCHONDRIA or RIBOSOMES.

Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.

A cell line generated from human embryonic kidney cells that were transformed with human adenovirus type 5.

Enzymes that catalyze the cleavage of a carbon-nitrogen bond by means other than hydrolysis or oxidation. Subclasses are the AMMONIA-LYASES, the AMIDINE-LYASES, the amine-lyases, and other carbon-nitrogen lyases. EC 4.3.

Proteins that control the CELL DIVISION CYCLE. This family of proteins includes a wide variety of classes, including CYCLIN-DEPENDENT KINASES, mitogen-activated kinases, CYCLINS, and PHOSPHOPROTEIN PHOSPHATASES as well as their putative substrates such as chromatin-associated proteins, CYTOSKELETAL PROTEINS, and TRANSCRIPTION FACTORS.

A family of F-box domain proteins that contain sequences that are homologous to the beta subunit of transducin (BETA-TRANSDUCIN). They play an important role in the protein degradation pathway by becoming components of SKP CULLIN F-BOX PROTEIN LIGASES, which selectively act on a subset of proteins including beta-catenin and IkappaBbeta.

Transport proteins that carry specific substances in the blood or across cell membranes.

Established cell cultures that have the potential to propagate indefinitely.

A species of the genus SACCHAROMYCES, family Saccharomycetaceae, order Saccharomycetales, known as "baker's" or "brewer's" yeast. The dried form is used as a dietary supplement.

The first continuously cultured human malignant CELL LINE, derived from the cervical carcinoma of Henrietta Lacks. These cells are used for VIRUS CULTIVATION and antitumor drug screening assays.

Any of various enzymatically catalyzed post-translational modifications of PEPTIDES or PROTEINS in the cell of origin. These modifications include carboxylation; HYDROXYLATION; ACETYLATION; PHOSPHORYLATION; METHYLATION; GLYCOSYLATION; ubiquitination; oxidation; proteolysis; and crosslinking and result in changes in molecular weight and electrophoretic motility.

Compounds that inhibit the function or proteolytic action of the PROTEASOME.

A subclass of PEPTIDE HYDROLASES that catalyze the internal cleavage of PEPTIDES or PROTEINS.

Commonly observed structural components of proteins formed by simple combinations of adjacent secondary structures. A commonly observed structure may be composed of a CONSERVED SEQUENCE which can be represented by a CONSENSUS SEQUENCE.

A 1.5-kDa small ubiquitin-related modifier protein that can covalently bind via an isopeptide link to a number of cellular proteins. It may play a role in intracellular protein transport and a number of other cellular processes.

A group of acylated oligopeptides produced by Actinomycetes that function as protease inhibitors. They have been known to inhibit to varying degrees trypsin, plasmin, KALLIKREINS, papain and the cathepsins.

The intracellular transfer of information (biological activation/inhibition) through a signal pathway. In each signal transduction system, an activation/inhibition signal from a biologically active molecule (hormone, neurotransmitter) is mediated via the coupling of a receptor/enzyme to a second messenger system or to an ion channel. Signal transduction plays an important role in activating cellular functions, cell differentiation, and cell proliferation. Examples of signal transduction systems are the GAMMA-AMINOBUTYRIC ACID-postsynaptic receptor-calcium ion channel system, the receptor-mediated T-cell activation pathway, and the receptor-mediated activation of phospholipases. Those coupled to membrane depolarization or intracellular release of calcium include the receptor-mediated activation of cytotoxic functions in granulocytes and the synaptic potentiation of protein kinase activation. Some signal transduction pathways may be part of larger signal transduction pathways; for example, protein kinase activation is part of the platelet activation signal pathway.

Proteins found in the nucleus of a cell. Do not confuse with NUCLEOPROTEINS which are proteins conjugated with nucleic acids, that are not necessarily present in the nucleus.

The ability of a protein to retain its structural conformation or its activity when subjected to physical or chemical manipulations.

Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.

The process of moving proteins from one cellular compartment (including extracellular) to another by various sorting and transport mechanisms such as gated transport, protein translocation, and vesicular transport.

A class of structurally related proteins of 12-20 kDa in size. They covalently modify specific proteins in a manner analogous to UBIQUITIN.

Macromolecular complexes formed from the association of defined protein subunits.

Hydrolases that specifically cleave the peptide bonds found in PROTEINS and PEPTIDES. Examples of sub-subclasses for this group include EXOPEPTIDASES and ENDOPEPTIDASES.

A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.

The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.

The aggregation of soluble ANTIGENS with ANTIBODIES, alone or with antibody binding factors such as ANTI-ANTIBODIES or STAPHYLOCOCCAL PROTEIN A, into complexes large enough to fall out of solution.

Screening techniques first developed in yeast to identify genes encoding interacting proteins. Variations are used to evaluate interplay between proteins and other molecules. Two-hybrid techniques refer to analysis for protein-protein interactions, one-hybrid for DNA-protein interactions, three-hybrid interactions for RNA-protein interactions or ligand-based interactions. Reverse n-hybrid techniques refer to analysis for mutations or other small molecules that dissociate known interactions.

Recombinant proteins produced by the GENETIC TRANSLATION of fused genes formed by the combination of NUCLEIC ACID REGULATORY SEQUENCES of one or more genes with the protein coding sequences of one or more genes.

An E3 UBIQUITIN LIGASE that interacts with and inhibits TUMOR SUPPRESSOR PROTEIN P53. Its ability to ubiquitinate p53 is regulated by TUMOR SUPPRESSOR PROTEIN P14ARF.

Proteins which bind to DNA. The family includes proteins which bind to both double- and single-stranded DNA and also includes specific DNA binding proteins in serum which can be used as markers for malignant diseases.

A type of POST-TRANSLATIONAL PROTEIN MODIFICATION by SMALL UBIQUITIN-RELATED MODIFIER PROTEINS (also known as SUMO proteins).

Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein.

Cell surface receptors for AUTOCRINE MOTILITY FACTOR, which is the secreted form of GLUCOSE-6-PHOSPHATE ISOMERASE. The receptor has an unusual composition in that it shares some structural similarities with G-PROTEIN-COUPLED RECEPTORS and functions as an ubiquitin protein ligase when internalized.

Theoretical representations that simulate the behavior or activity of biological processes or diseases. For disease models in living animals, DISEASE MODELS, ANIMAL is available. Biological models include the use of mathematical equations, computers, and other electronic equipment.

A broad category of carrier proteins that play a role in SIGNAL TRANSDUCTION. They generally contain several modular domains, each of which having its own binding activity, and act by forming complexes with other intracellular-signaling molecules. Signal-transducing adaptor proteins lack enzyme activity, however their activity can be modulated by other signal-transducing enzymes

Ligases that catalyze the joining of adjacent AMINO ACIDS by the formation of carbon-nitrogen bonds between their carboxylic acid groups and amine groups.

Protein modules with conserved ligand-binding surfaces which mediate specific interaction functions in SIGNAL TRANSDUCTION PATHWAYS and the specific BINDING SITES of their cognate protein LIGANDS.

The parts of a macromolecule that directly participate in its specific combination with another molecule.

A gene silencing phenomenon whereby specific dsRNAs (RNA, DOUBLE-STRANDED) trigger the degradation of homologous mRNA (RNA, MESSENGER). The specific dsRNAs are processed into SMALL INTERFERING RNA (siRNA) which serves as a guide for cleavage of the homologous mRNA in the RNA-INDUCED SILENCING COMPLEX. DNA METHYLATION may also be triggered during this process.

Endogenous substances, usually proteins, which are effective in the initiation, stimulation, or termination of the genetic transcription process.

Small double-stranded, non-protein coding RNAs (21-31 nucleotides) involved in GENE SILENCING functions, especially RNA INTERFERENCE (RNAi). Endogenously, siRNAs are generated from dsRNAs (RNA, DOUBLE-STRANDED) by the same ribonuclease, Dicer, that generates miRNAs (MICRORNAS). The perfect match of the siRNAs' antisense strand to their target RNAs mediates RNAi by siRNA-guided RNA cleavage. siRNAs fall into different classes including trans-acting siRNA (tasiRNA), repeat-associated RNA (rasiRNA), small-scan RNA (scnRNA), and Piwi protein-interacting RNA (piRNA) and have different specific gene silencing functions.

The uptake of naked or purified DNA by CELLS, usually meaning the process as it occurs in eukaryotic cells. It is analogous to bacterial transformation (TRANSFORMATION, BACTERIAL) and both are routinely employed in GENE TRANSFER TECHNIQUES.

Proteins which maintain the transcriptional quiescence of specific GENES or OPERONS. Classical repressor proteins are DNA-binding proteins that are normally bound to the OPERATOR REGION of an operon, or the ENHANCER SEQUENCES of a gene until a signal occurs that causes their release.

Processes involved in the formation of TERTIARY PROTEIN STRUCTURE.

A cell line derived from cultured tumor cells.

The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety.

Identification of proteins or peptides that have been electrophoretically separated by blot transferring from the electrophoresis gel to strips of nitrocellulose paper, followed by labeling with antibody probes.

Immunologic method used for detecting or quantifying immunoreactive substances. The substance is identified by first immobilizing it by blotting onto a membrane and then tagging it with labeled antibodies.

Cellular uptake of extracellular materials within membrane-limited vacuoles or microvesicles. ENDOSOMES play a central role in endocytosis.

The arrangement of two or more amino acid or base sequences from an organism or organisms in such a way as to align areas of the sequences sharing common properties. The degree of relatedness or homology between the sequences is predicted computationally or statistically based on weights assigned to the elements aligned between the sequences. This in turn can serve as a potential indicator of the genetic relatedness between the organisms.

NMR spectroscopy on small- to medium-size biological macromolecules. This is often used for structural investigation of proteins and nucleic acids, and often involves more than one isotope.

The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).

Proteins prepared by recombinant DNA technology.

The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.

Nuclear phosphoprotein encoded by the p53 gene (GENES, P53) whose normal function is to control CELL PROLIFERATION and APOPTOSIS. A mutant or absent p53 protein has been found in LEUKEMIA; OSTEOSARCOMA; LUNG CANCER; and COLORECTAL CANCER.

CELL LINES derived from the CV-1 cell line by transformation with a replication origin defective mutant of SV40 VIRUS, which codes for wild type large T antigen (ANTIGENS, POLYOMAVIRUS TRANSFORMING). They are used for transfection and cloning. (The CV-1 cell line was derived from the kidney of an adult male African green monkey (CERCOPITHECUS AETHIOPS).)

A generic term for any circumscribed mass of foreign (e.g., lead or viruses) or metabolically inactive materials (e.g., ceroid or MALLORY BODIES), within the cytoplasm or nucleus of a cell. Inclusion bodies are in cells infected with certain filtrable viruses, observed especially in nerve, epithelial, or endothelial cells. (Stedman, 25th ed)

The complex series of phenomena, occurring between the end of one CELL DIVISION and the end of the next, by which cellular material is duplicated and then divided between two daughter cells. The cell cycle includes INTERPHASE, which includes G0 PHASE; G1 PHASE; S PHASE; and G2 PHASE, and CELL DIVISION PHASE.

Proteins and peptides that are involved in SIGNAL TRANSDUCTION within the cell. Included here are peptides and proteins that regulate the activity of TRANSCRIPTION FACTORS and cellular processes in response to signals from CELL SURFACE RECEPTORS. Intracellular signaling peptide and proteins may be part of an enzymatic signaling cascade or act through binding to and modifying the action of other signaling factors.

Exogenous and endogenous compounds which inhibit CYSTEINE ENDOPEPTIDASES.

Proteins that are normally involved in holding cellular growth in check. Deficiencies or abnormalities in these proteins may lead to unregulated cell growth and tumor development.

A ubiquitin-protein ligase that mediates OXYGEN-dependent polyubiquitination of HYPOXIA-INDUCIBLE FACTOR 1, ALPHA SUBUNIT. It is inactivated in VON HIPPEL-LINDAU SYNDROME.

Injuries to DNA that introduce deviations from its normal, intact structure and which may, if left unrepaired, result in a MUTATION or a block of DNA REPLICATION. These deviations may be caused by physical or chemical agents and occur by natural or unnatural, introduced circumstances. They include the introduction of illegitimate bases during replication or by deamination or other modification of bases; the loss of a base from the DNA backbone leaving an abasic site; single-strand breaks; double strand breaks; and intrastrand (PYRIMIDINE DIMERS) or interstrand crosslinking. Damage can often be repaired (DNA REPAIR). If the damage is extensive, it can induce APOPTOSIS.

A negative regulatory effect on physiological processes at the molecular, cellular, or systemic level. At the molecular level, the major regulatory sites include membrane receptors, genes (GENE EXPRESSION REGULATION), mRNAs (RNA, MESSENGER), and proteins.

Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control (induction or repression) of gene action at the level of transcription or translation.

Proteins produced from GENES that have acquired MUTATIONS.

Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors.

The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)

A system of cisternae in the CYTOPLASM of many cells. In places the endoplasmic reticulum is continuous with the plasma membrane (CELL MEMBRANE) or outer membrane of the nuclear envelope. If the outer surfaces of the endoplasmic reticulum membranes are coated with ribosomes, the endoplasmic reticulum is said to be rough-surfaced (ENDOPLASMIC RETICULUM, ROUGH); otherwise it is said to be smooth-surfaced (ENDOPLASMIC RETICULUM, SMOOTH). (King & Stansfield, A Dictionary of Genetics, 4th ed)

Immature ERYTHROCYTES. In humans, these are ERYTHROID CELLS that have just undergone extrusion of their CELL NUCLEUS. They still contain some organelles that gradually decrease in number as the cells mature. RIBOSOMES are last to disappear. Certain staining techniques cause components of the ribosomes to precipitate into characteristic "reticulum" (not the same as the ENDOPLASMIC RETICULUM), hence the name reticulocytes.

Methods for determining interaction between PROTEINS.

Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others.

Cytoplasmic vesicles formed when COATED VESICLES shed their CLATHRIN coat. Endosomes internalize macromolecules bound by receptors on the cell surface.

Motifs in DNA- and RNA-binding proteins whose amino acids are folded into a single structural unit around a zinc atom. In the classic zinc finger, one zinc atom is bound to two cysteines and two histidines. In between the cysteines and histidines are 12 residues which form a DNA binding fingertip. By variations in the composition of the sequences in the fingertip and the number and spacing of tandem repeats of the motif, zinc fingers can form a large number of different sequence specific binding sites.

Proteins found in any species of fungus.

A species of CERCOPITHECUS containing three subspecies: C. tantalus, C. pygerythrus, and C. sabeus. They are found in the forests and savannah of Africa. The African green monkey (C. pygerythrus) is the natural host of SIMIAN IMMUNODEFICIENCY VIRUS and is used in AIDS research.

Within a eukaryotic cell, a membrane-limited body which contains chromosomes and one or more nucleoli (CELL NUCLEOLUS). The nuclear membrane consists of a double unit-type membrane which is perforated by a number of pores; the outermost membrane is continuous with the ENDOPLASMIC RETICULUM. A cell may contain more than one nucleus. (From Singleton & Sainsbury, Dictionary of Microbiology and Molecular Biology, 2d ed)

A class of morphologically heterogeneous cytoplasmic particles in animal and plant tissues characterized by their content of hydrolytic enzymes and the structure-linked latency of these enzymes. The intracellular functions of lysosomes depend on their lytic potential. The single unit membrane of the lysosome acts as a barrier between the enzymes enclosed in the lysosome and the external substrate. The activity of the enzymes contained in lysosomes is limited or nil unless the vesicle in which they are enclosed is ruptured. Such rupture is supposed to be under metabolic (hormonal) control. (From Rieger et al., Glossary of Genetics: Classical and Molecular, 5th ed)

A group of enzymes which catalyze the hydrolysis of ATP. The hydrolysis reaction is usually coupled with another function such as transporting Ca(2+) across a membrane. These enzymes may be dependent on Ca(2+), Mg(2+), anions, H+, or DNA.

Proteins that originate from plants species belonging to the genus ARABIDOPSIS. The most intensely studied species of Arabidopsis, Arabidopsis thaliana, is commonly used in laboratory experiments.

Protein structural motifs that play a role in protein-protein binding. The motifs are comprised of approximately 50 residues. Their name derives from the fact that they were found in cyclin F.

Derangement in size and number of muscle fibers occurring with aging, reduction in blood supply, or following immobilization, prolonged weightlessness, malnutrition, and particularly in denervation.

A degradation process whereby incorrectly folded proteins are selectively transported out of the ENDOPLASMIC RETICULUM and into the CYTOSOL. The misfolded proteins are subsequently ubiquitinated and degraded by the PROTEASOME.

The artificial induction of GENE SILENCING by the use of RNA INTERFERENCE to reduce the expression of a specific gene. It includes the use of DOUBLE-STRANDED RNA, such as SMALL INTERFERING RNA and RNA containing HAIRPIN LOOP SEQUENCE, and ANTI-SENSE OLIGONUCLEOTIDES.

A group of cell cycle proteins that negatively regulate the activity of CYCLIN/CYCLIN-DEPENDENT KINASE complexes. They inhibit CELL CYCLE progression and help control CELL PROLIFERATION following GENOTOXIC STRESS as well as during CELL DIFFERENTIATION.

Endosomes containing intraluminal vesicles which are formed by the inward budding of the endosome membrane. Multivesicular bodies (MVBs) may fuse with other organelles such as LYSOSOMES or fuse back with the PLASMA MEMBRANE releasing their contents by EXOCYTOSIS. The MVB intraluminal vesicles released into the extracellular environment are known as EXOSOMES.

Highly conserved proteins that specifically bind to and activate the anaphase-promoting complex-cyclosome, promoting ubiquitination and proteolysis of cell-cycle-regulatory proteins. Cdc20 is essential for anaphase-promoting complex activity, initiation of anaphase, and cyclin proteolysis during mitosis.

Together with the Apc2 subunit, forms the catalytic core of the E3 ubiquitin ligase, anaphase-promoting complex-cyclosome. It has a RING H2 domain which interacts with the cullin domain of Apc2. Apc11 also interacts with the E2 ubiquitin ligases involved in APC-C ubiquitination reactions.

The protein constituents of muscle, the major ones being ACTINS and MYOSINS. More than a dozen accessory proteins exist including TROPONIN; TROPOMYOSIN; and DYSTROPHIN.

Small chromosomal proteins (approx 12-20 kD) possessing an open, unfolded structure and attached to the DNA in cell nuclei by ionic linkages. Classification into the various types (designated histone I, histone II, etc.) is based on the relative amounts of arginine and lysine in each.

A plant genus of the family BRASSICACEAE that contains ARABIDOPSIS PROTEINS and MADS DOMAIN PROTEINS. The species A. thaliana is used for experiments in classical plant genetics as well as molecular genetic studies in plant physiology, biochemistry, and development.

RNA sequences that serve as templates for protein synthesis. Bacterial mRNAs are generally primary transcripts in that they do not require post-transcriptional processing. Eukaryotic mRNA is synthesized in the nucleus and must be exported to the cytoplasm for translation. Most eukaryotic mRNAs have a sequence of polyadenylic acid at the 3' end, referred to as the poly(A) tail. The function of this tail is not known for certain, but it may play a role in the export of mature mRNA from the nucleus as well as in helping stabilize some mRNA molecules by retarding their degradation in the cytoplasm.

The reconstruction of a continuous two-stranded DNA molecule without mismatch from a molecule which contained damaged regions. The major repair mechanisms are excision repair, in which defective regions in one strand are excised and resynthesized using the complementary base pairing information in the intact strand; photoreactivation repair, in which the lethal and mutagenic effects of ultraviolet light are eliminated; and post-replication repair, in which the primary lesions are not repaired, but the gaps in one daughter duplex are filled in by incorporation of portions of the other (undamaged) daughter duplex. Excision repair and post-replication repair are sometimes referred to as "dark repair" because they do not require light.

Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.

A sequence of amino acids in a polypeptide or of nucleotides in DNA or RNA that is similar across multiple species. A known set of conserved sequences is represented by a CONSENSUS SEQUENCE. AMINO ACID MOTIFS are often composed of conserved sequences.

Extrachromosomal, usually CIRCULAR DNA molecules that are self-replicating and transferable from one organism to another. They are found in a variety of bacterial, archaeal, fungal, algal, and plant species. They are used in GENETIC ENGINEERING as CLONING VECTORS.

The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.

The biosynthesis of RNA carried out on a template of DNA. The biosynthesis of DNA from an RNA template is called REVERSE TRANSCRIPTION.

Single chains of amino acids that are the units of multimeric PROTEINS. Multimeric proteins can be composed of identical or non-identical subunits. One or more monomeric subunits may compose a protomer which itself is a subunit structure of a larger assembly.

A signal transducing tumor necrosis factor receptor associated factor that is involved in regulation of NF-KAPPA B signalling and activation of JNK MITOGEN-ACTIVATED PROTEIN KINASES.

Strains of mice in which certain GENES of their GENOMES have been disrupted, or "knocked-out". To produce knockouts, using RECOMBINANT DNA technology, the normal DNA sequence of the gene being studied is altered to prevent synthesis of a normal gene product. Cloned cells in which this DNA alteration is successful are then injected into mouse EMBRYOS to produce chimeric mice. The chimeric mice are then bred to yield a strain in which all the cells of the mouse contain the disrupted gene. Knockout mice are used as EXPERIMENTAL ANIMAL MODELS for diseases (DISEASE MODELS, ANIMAL) and to clarify the functions of the genes.

One of the mechanisms by which CELL DEATH occurs (compare with NECROSIS and AUTOPHAGOCYTOSIS). Apoptosis is the mechanism responsible for the physiological deletion of cells and appears to be intrinsically programmed. It is characterized by distinctive morphologic changes in the nucleus and cytoplasm, chromatin cleavage at regularly spaced sites, and the endonucleolytic cleavage of genomic DNA; (DNA FRAGMENTATION); at internucleosomal sites. This mode of cell death serves as a balance to mitosis in regulating the size of animal tissues and in mediating pathologic processes associated with tumor growth.

A type of CELL NUCLEUS division by means of which the two daughter nuclei normally receive identical complements of the number of CHROMOSOMES of the somatic cells of the species.

The process of cleaving a chemical compound by the addition of a molecule of water.

Nuclear antigen with a role in DNA synthesis, DNA repair, and cell cycle progression. PCNA is required for the coordinated synthesis of both leading and lagging strands at the replication fork during DNA replication. PCNA expression correlates with the proliferation activity of several malignant and non-malignant cell types.

Proteins that originate from insect species belonging to the genus DROSOPHILA. The proteins from the most intensely studied species of Drosophila, DROSOPHILA MELANOGASTER, are the subject of much interest in the area of MORPHOGENESIS and development.

The level of protein structure in which regular hydrogen-bond interactions within contiguous stretches of polypeptide chain give rise to alpha helices, beta strands (which align to form beta sheets) or other types of coils. This is the first folding level of protein conformation.

The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.

The segregation and degradation of damaged or unwanted cytoplasmic constituents by autophagic vacuoles (cytolysosomes) composed of LYSOSOMES containing cellular components in the process of digestion; it plays an important role in BIOLOGICAL METAMORPHOSIS of amphibians, in the removal of bone by osteoclasts, and in the degradation of normal cell components in nutritional deficiency states.

An analytical method used in determining the identity of a chemical based on its mass using mass analyzers/mass spectrometers.

A cyclin-dependent kinase inhibitor that coordinates the activation of CYCLIN and CYCLIN-DEPENDENT KINASES during the CELL CYCLE. It interacts with active CYCLIN D complexed to CYCLIN-DEPENDENT KINASE 4 in proliferating cells, while in arrested cells it binds and inhibits CYCLIN E complexed to CYCLIN-DEPENDENT KINASE 2.

The rate dynamics in chemical or physical systems.

Protein analogs and derivatives of the Aequorea victoria green fluorescent protein that emit light (FLUORESCENCE) when excited with ULTRAVIOLET RAYS. They are used in REPORTER GENES in doing GENETIC TECHNIQUES. Numerous mutants have been made to emit other colors or be sensitive to pH.

A general term for single-celled rounded fungi that reproduce by budding. Brewers' and bakers' yeasts are SACCHAROMYCES CEREVISIAE; therapeutic dried yeast is YEAST, DRIED.

The phosphoprotein encoded by the BRCA1 gene (GENE, BRCA1). In normal cells the BRCA1 protein is localized in the nucleus, whereas in the majority of breast cancer cell lines and in malignant pleural effusions from breast cancer patients, it is localized mainly in the cytoplasm. (Science 1995;270(5237):713,789-91)

A syndrome characterized by multiple abnormalities, MENTAL RETARDATION, and movement disorders. Present usually are skull and other abnormalities, frequent infantile spasms (SPASMS, INFANTILE); easily provoked and prolonged paroxysms of laughter (hence "happy"); jerky puppetlike movements (hence "puppet"); continuous tongue protrusion; motor retardation; ATAXIA; MUSCLE HYPOTONIA; and a peculiar facies. It is associated with maternal deletions of chromosome 15q11-13 and other genetic abnormalities. (From Am J Med Genet 1998 Dec 4;80(4):385-90; Hum Mol Genet 1999 Jan;8(1):129-35)

Ubiquitous, inducible, nuclear transcriptional activator that binds to enhancer elements in many different cell types and is activated by pathogenic stimuli. The NF-kappa B complex is a heterodimer composed of two DNA-binding subunits: NF-kappa B1 and relA.

A subunit of the anaphase-promoting complex whose primary function is to provide structural support for the catalytic and substrate-recognition modules of the complex. Apc5, along with Apc4, tethers the tetratricopeptide-coactivator binding subcomplex to the main structural subunit, Apc1.

The outward appearance of the individual. It is the product of interactions between genes, and between the GENOTYPE and the environment.

Microscopy of specimens stained with fluorescent dye (usually fluorescein isothiocyanate) or of naturally fluorescent materials, which emit light when exposed to ultraviolet or blue light. Immunofluorescence microscopy utilizes antibodies that are labeled with fluorescent dye.

A broad category of proteins involved in the formation, transport and dissolution of TRANSPORT VESICLES. They play a role in the intracellular transport of molecules contained within membrane vesicles. Vesicular transport proteins are distinguished from MEMBRANE TRANSPORT PROTEINS, which move molecules across membranes, by the mode in which the molecules are transported.

The region of an enzyme that interacts with its substrate to cause the enzymatic reaction.

Compounds which inhibit or antagonize biosynthesis or actions of proteases (ENDOPEPTIDASES).

The assembly of the QUATERNARY PROTEIN STRUCTURE of multimeric proteins (MULTIPROTEIN COMPLEXES) from their composite PROTEIN SUBUNITS.

A protein serine-threonine kinase that catalyzes the PHOSPHORYLATION of I KAPPA B PROTEINS. This enzyme also activates the transcription factor NF-KAPPA B and is composed of alpha and beta catalytic subunits, which are protein kinases and gamma, a regulatory subunit.

Proteins that are coded by immediate-early genes, in the absence of de novo protein synthesis. The term was originally used exclusively for viral regulatory proteins that were synthesized just after viral integration into the host cell. It is also used to describe cellular proteins which are synthesized immediately after the resting cell is stimulated by extracellular signals.

The part of a cell that contains the CYTOSOL and small structures excluding the CELL NUCLEUS; MITOCHONDRIA; and large VACUOLES. (Glick, Glossary of Biochemistry and Molecular Biology, 1990)

A transferase that catalyzes the addition of aliphatic, aromatic, or heterocyclic FREE RADICALS as well as EPOXIDES and arene oxides to GLUTATHIONE. Addition takes place at the SULFUR. It also catalyzes the reduction of polyol nitrate by glutathione to polyol and nitrite.

RPN4 is a ligand, substrate, and transcriptional regulator of the 26S proteasome: a negative feedback circuit. (1/5483)

The RPN4 (SON1, UFD5) protein of the yeast Saccharomyces cerevisiae is required for normal levels of intracellular proteolysis. RPN4 is a transcriptional activator of genes encoding proteasomal subunits. Here we show that RPN4 is required for normal levels of these subunits. Further, we demonstrate that RPN4 is extremely short-lived (t(1/2) approximately 2 min), that it directly interacts with RPN2, a subunit of the 26S proteasome, and that rpn4Delta cells are perturbed in their cell cycle. The degradation signal of RPN4 was mapped to its N-terminal region, outside the transcription-activation domains of RPN4. The ability of RPN4 to augment the synthesis of proteasomal subunits while being metabolically unstable yields a negative feedback circuit in which the same protein up-regulates the proteasome production and is destroyed by the assembled active proteasome. (+info)

Raft-partitioning of the ubiquitin ligases Cbl and Nedd4 upon IgE-triggered cell signaling. (2/5483)

The high affinity receptor for IgE, FcepsilonRI on mast cells and basophils plays an essential role in immunological defense. Upon multivalent antigen binding, FcepsilonRI becomes phoshorylated by the protein-tyrosine kinase Lyn, as a result of receptor clustering in lipid rafts. FcepsilonRI has been shown to be ubiquitinated. Ubiquitination can lead to degradation by proteasomes, but it can also act as a sorting signal to internalize proteins destined to the endosomal/lysosomal pathway. We have analyzed whether FcepsilonRI ubiquitination takes place within rafts. We report biochemical and imaging evidence in rat basoleukemia cells for the presence of ubiquitinated FcepsilonRI in clustered rafts upon receptor activation. Moreover, we demonstrated that the ubiquitin ligases Cbl and Nedd4 colocalize with FcepsilonRI patches and showed that both ligases become associated with lipid rafts after activation of IgE signaling. Because Cbl is known to interact with the FcepsilonRI signaling complex, ubiquitination is likely to be an important parameter regulating IgE-triggered signaling occurring in rafts. (+info)

The Mdm-2 amino terminus is required for Mdm2 binding and SUMO-1 conjugation by the E2 SUMO-1 conjugating enzyme Ubc9. (3/5483)

Covalent attachment of SUMO-1 to Mdm2 requires the activation of a heterodimeric Aos1-Uba2 enzyme (ubiquitin-activating enzyme (E1)) followed by the conjugation of Sumo-1 to Mdm2 by Ubc9, a protein with a strong sequence similarity to ubiquitin carrier proteins (E2s). Upon Sumo-1 conjugation, Mdm2 is protected from self-ubiquitination and elicits greater ubiquitin-protein isopeptide ligase (E3) activity toward p53, thereby increasing its oncogenic potential. Because of the biological implication of Mdm2 sumoylation, we mapped Ubc9 binding on Mdm2. Here we demonstrate that Ubc9 can associate with Mdm2 only if amino acids 40-59 within the N terminus of Mdm2 are present. Mdm2 from which amino acids 40-59 have been deleted can no longer be sumoylated. Furthermore, addition of a peptide that corresponds to amino acids 40-59 on Mdm2 to a sumoylation reaction efficiently inhibits Mdm2 sumoylation in vitro and in vivo. In UV-treated cells Mdm2 exhibits reduced association with Ubc9, which coincides with decreased Mdm2 sumoylation. Our findings regarding the association of Ubc9 with Mdm2, and the effect of UV-irradiation on Ubc9 binding, point to an additional level in the regulation of Mdm2 sumoylation under normal growth conditions as well as in response to stress conditions. (+info)

Heat capacity changes upon burial of polar and nonpolar groups in proteins. (4/5483)

In this paper we address the question of whether the burial of polar and nonpolar groups in the protein locale is indeed accompanied by the heat capacity changes, DeltaC(p), that have an opposite sign, negative for nonpolar groups and positive for polar groups. To accomplish this, we introduced amino acid substitutions at four fully buried positions of the ubiquitin molecule (Val5, Val17, Leu67, and Gln41). We substituted Val at positions 5 and 17 and Leu at position 67 with a polar residue, Asn. As a control, Ala was introduced at the same three positions. We also replaced the buried polar Gln41 with Val and Leu, nonpolar residues that have similar size and shape as Gln. As a control, Asn was introduced at Gln41 as well. The effects of these amino acid substitutions on the stability, and in particular, on the heat capacity change upon unfolding were measured using differential scanning calorimetry. The effect of the amino acid substitutions on the structure was also evaluated by comparing the (1)H-(15)N HSQC spectra of the ubiquitin variants. It was found that the Ala substitutions did not have a considerable effect on the heat capacity change upon unfolding. However, the substitutions of aliphatic side chains (Val or Leu) with a polar residue (Asn) lead to a significant (> 30%) decrease in the heat capacity change upon unfolding. The decrease in heat capacity changes does not appear to be the result of significant structural perturbations as seen from the HSQC spectra of the variants. The substitution of a buried polar residue (Gln41) to a nonpolar residue (Leu or Val) leads to a significant (> 25%) increase in heat capacity change upon unfolding. These results indicate that indeed the heat capacity change of burial of polar and nonpolar groups has an opposite sign. However, the observed changes in DeltaC(p) are several times larger than those predicted, based on the changes in water accessible surface area upon substitution. (+info)

Proteasomes are involved in the constitutive degradation of growth hormone receptors. (5/5483)

In the mouse Ba/F3-hGHR cell line, which stably expresses human growth hormone receptors (hGHRs), the hGHRs were rapidly degraded in the absence of the ligand. Human growth hormone-binding protein (hGH-BP), a soluble form of hGHR, was released from Ba/F3-hGHR cells, but the hGH-BP release was less than 1% of total hGHRs in the cells. Therefore, the hGH-BP release does not markedly contribute to hGHR degradation in Ba/F3-hGHR cells. The constitutive degradation of hGHRs was inhibited by the proteasome inhibitors MG-132 and clasto-lactacystin beta-lactone, or the vacuolar H+-ATPase inhibitor, bafilomycin A1. hGH-enhanced degradation of hGHRs was also inhibited by MG-132. Moreover, MG-132 inhibited the internalization of hGHRs as assessed by 125I-hGH binding to the cell surfaces. Ubiquitinated hGHRs were detected in the cell lysate and increased by hGH-treatment. Furthermore, MG-132 accumulated the ubiquitinated hGHRs induced by hGH. However, the ratio of ubiquitinated hGHRs to unubiquitinated hGHRs was very small, even with treatment involving both hGH and MG-132. In the hGH-untreated cells, the ubiquitinated hGHRs were weakly detected. However, the ubiquitination of hGHR was not enhanced by MG-132 as a result of immunoblotting. Thus, the ubiquitination of hGHR is unlikely to be involved, at least in the constitutive degradation. Taken together, both the proteasome pathway and endosome/lysosome pathway are involved in the constitutive degradation of hGHRs. Our results also suggest that ubiquitination of the hGHR itself is unlikely to be the trigger of the proteasome-dependent degradation. (+info)

High and sustained transgene expression in vivo from plasmid vectors containing a hybrid ubiquitin promoter. (6/5483)

Sustained transgene expression will be required for the successful treatment of most genetic diseases being considered for gene therapy. The initially high levels of expression attained with plasmid DNA (pDNA) vectors containing viral promoters, such as that from cytomegalovirus (CMV), decline precipitously to near-background levels within two to three weeks. Here we constructed pDNA vectors containing the human cellular UBB (encoding ubiquitin B; Ub) promoter and evaluated their expression in the mouse lung. Cationic lipid-pDNA complexes were instilled intranasally (IN) or injected intravenously (IV) into immunodeficient BALB/c mice. Chloramphenicol acetyltransferase (CAT) reporter gene expression from the UBB promoter was initially very low at day 2 post-administration, but by day 35 exceeded the level of expression attained from a CMV promoter vector by four- to ninefold. Appending a portion of the CMV enhancer 5' of the UBB promoter (CMV-Ub) increased CAT expression to nearly that of the CMV promoter and expression persisted in the lung for at least 3 months, with 50% of day 2 levels remaining at day 84. In the liver, expression from the CMV-Ub hybrid promoter was sustained for 42 days. As previous studies have shown that eliminating immunostimulatory CpG motifs in pDNA vectors reduces their toxicity, we constructed a CpG-deficient version of the CMV-Ub vector expressing alpha-galactosidase A, the enzyme deficient in Fabry disease, a lysosomal storage disorder. After IN or IV administration, levels of alpha-galactosidase A from this vector were not only undiminished but increased 500% to 1500% by day 35. Our results indicate that CpG-reduced plasmid vectors containing a CMV-Ub hybrid promoter may provide the long-term expression required for a practical gene therapeutic. (+info)

Effects of arachidonic and docosahexaenoic acids on secretion and degradation of bile salt-dependent lipase in AR4-2J cells. (7/5483)

In this study we demonstrated that two polyunsaturated fatty acids, arachidonic acid (AA, n-6) and docosahexaenoic acid (DHA, n-3), modulate the secretion of bile salt-dependent lipase (BSDL) by pancreatic AR4-2J cells. The effects of AA and DHA were also compared with that of the monounsaturated fatty acid, oleic acid (OA). Our results showed that the chronic treatment of cells with AA or DHA, that did not affect the biosynthesis rate of BSDL, similarly decreased the amount of secreted BSDL and perturbed the intracellular partitioning of the enzyme, whereas OA had no effect. Particularly, AA and DHA induced the retention of the enzyme in microsomes and lowered its content in the cell cytosol. We have further shown that AA treatment decreased the ubiquitination of the protein, and consequently diminished its export toward the cytosol, a result that might explain the retention of BSDL in microsomes and correlated with membrane phospholipids alteration. The retained protein was further degraded by a nonproteasomal pathway that likely involves ATP-dependent endoplasmic reticulum proteases. These findings concerning the regulation of the pancreatic BSDL secretion by two polyunsaturated acids, AA and DHA, might be of physiological importance in the plasmatic and cellular cholesterol homeostasis. (+info)

Toxoplasma gondii tachyzoites inhibit proinflammatory cytokine induction in infected macrophages by preventing nuclear translocation of the transcription factor NF-kappa B. (8/5483)

Control of microbial infection requires regulated induction of NF-kappaB-dependent proinflammatory cytokines such as IL-12 and TNF-alpha. Activation of this important transcription factor is driven by phosphorylation-dependent degradation of the inhibitory IkappaB molecule, an event which enables NF-kappaB translocation from the cytoplasm to the nucleus. In this study, we show that intracellular infection of macrophages with the protozoan parasite Toxoplasma gondii induces rapid IkappaB phosphorylation and degradation. Nevertheless, NF-kappaB failed to translocate to the nucleus, enabling the parasite to invade cells without triggering proinflammatory cytokine induction. Infected cells subsequently subjected to LPS triggering were severely crippled in IL-12 and TNF-alpha production, a result of tachyzoite-induced blockade of NF-kappaB nuclear translocation. Our results are the first to demonstrate the ability of an intracellular protozoan to actively interfere with the NF-kappaB activation pathway in macrophages, an activity that may enable parasite survival within the host. (+info)

Proteins can specifically bind to ubiquitin via ubiquitin-binding domains (UBDs). The distances between individual ubiquitin ... Ubiquitination requires three types of enzyme: ubiquitin-activating enzymes, ubiquitin-conjugating enzymes, and ubiquitin ... ubiquitin fold-modifier-1 (UFM1) and ubiquitin-like protein-5 (UBL5, which is but known as homologous to ubiquitin-1 [Hub1] in ... Multi-ubiquitin chains at least four ubiquitin molecules long must be attached to a lysine residue on the condemned protein in ...

https://en.wikipedia.org/wiki/Ubiquitin

Ubiquitin is a protein that in humans is encoded by the UBB gene. Ubiquitin is one of the most conserved proteins known in ... Ubiquitin is covalently bound to proteins to be degraded, and presumably labels these proteins for degradation. Ubiquitin also ... "Entrez Gene: UBB ubiquitin B". Conaway RC, Brower CS, Conaway JW (2002). "Emerging roles of ubiquitin in transcription ... 1985). "The human ubiquitin multigene family: some genes contain multiple directly repeated ubiquitin coding sequences". EMBO J ...

https://en.wikipedia.org/wiki/Ubiquitin_B

"Entrez Gene: UBC ubiquitin C". Kimura Y, Tanaka K (June 2010). "Regulatory mechanisms involved in the control of ubiquitin ... Polyubiquitin-C is one of the sources of ubiquitin, along with UBB, UBA52, and RPS27A. UBC gene is one of the two stress- ... Different linking of ubiquitin chains results in distinct conformations. There are 8 linkage types of polyubiquitin-C, and each ... Kim NS, Yamaguchi T, Sekine S, Saeki M, Iwamuro S, Kato S (July 1998). "Cloning of human polyubiquitin cDNAs and a ubiquitin- ...

https://en.wikipedia.org/wiki/Ubiquitin_C

A ubiquitin ligase (also called an E3 ubiquitin ligase) is a protein that recruits an E2 ubiquitin-conjugating enzyme that has ... WWP2 Parkin MKRN1 ERAD Ubiquitin Ubiquitin-activating enzyme Ubiquitin-conjugating enzyme Dou H, Buetow L, Hock A, Sibbet GJ, ... The ubiquitin ligase is referred to as an E3, and operates in conjunction with an E1 ubiquitin-activating enzyme and an E2 ... Ubiquitin signaling relies on the diversity of ubiquitin tags for the specificity of its message. A protein can be tagged with ...

https://en.wikipedia.org/wiki/Ubiquitin_ligase

... is a protein that in humans is encoded by the UBD gene, also known as FAT10. UBD acts like ubiquitin, by covalently ... "Entrez Gene: UBD ubiquitin D". Hipp MS, Raasi S, Groettrup M, Schmidtke G (Apr 2004). "NEDD8 ultimate buster-1L interacts with ... Liu YC, Pan J, Zhang C, Fan W, Collinge M, Bender JR, Weissman SM (Apr 1999). "A MHC-encoded ubiquitin-like protein (FAT10) ... Liu YC, Pan J, Zhang C, Fan W, Collinge M, Bender JR, Weissman SM (Apr 1999). "A MHC-encoded ubiquitin-like protein (FAT10) ...

https://en.wikipedia.org/wiki/Ubiquitin_D

Collectively, ubiquitin and ubiquitin-like proteins are sometimes referred to as "ubiquitons". UBLs can be divided into two ... Prokaryotic ubiquitin-like protein (Pup) occurs in some actinobacteria and has functions closely analogous to ubiquitin in ... Ubiquitin is capable of forming polymeric chains, with additional ubiquitin molecules covalently attached to the first, which ... A systematic survey has since identified over 10,000 distinct genes for ubiquitin or ubiquitin-like proteins represented in ...

https://en.wikipedia.org/wiki/Ubiquitin-like_protein

... or known to interact with ubiquitin-like modifiers. Among the UIM proteins are two different subgroups of the UBP (ubiquitin ... Some proteins known to contain an UIM are listed below: Eukaryotic PSD4/RPN-10/S5, a multi-ubiquitin binding subunit of the 26S ... Thus, UIMs may have several functions in ubiquitin metabolism each of which may require different numbers of UIMs. The UIM is ... In molecular biology, the Ubiquitin-Interacting Motif (UIM), or 'LALAL-motif', is a sequence motif of about 20 amino acid ...

https://en.wikipedia.org/wiki/Ubiquitin-interacting_motif

UBE2Z ATG3 BIRC6 UFC1 Ubiquitin Ubiquitin-activating enzyme Ubiquitin ligase Nandi D, Tahiliani P, Kumar A, Chandu D (March ... The activated ubiquitin is then transferred to an E2 cysteine. Once conjugated to ubiquitin, the E2 molecule binds one of ... Ubiquitin-conjugating enzymes, also known as E2 enzymes and more rarely as ubiquitin-carrier enzymes, perform the second step ... A ubiquitin-activating enzyme, or E1, first activates the ubiquitin by covalently attaching the molecule to its active site ...

https://en.wikipedia.org/wiki/Ubiquitin-conjugating_enzyme

... s (UBDs) are protein domains that recognise and bind non-covalently to ubiquitin through protein- ... 2006). "The ubiquitin binding domain ZnF UBP recognizes the C-terminal diglycine motif of unanchored ubiquitin". Cell. 124 (6 ... Proteins containing UBDs are known as ubiquitin-binding proteins or sometimes as "ubiquitin receptors". Most UBDs are of small ... 2005). "Structure of the UBA Domain of Dsk2p in Complex with Ubiquitin: Molecular Determinants for Ubiquitin Recognition". ...

https://en.wikipedia.org/wiki/Ubiquitin-binding_domain

... binds to the ubiquitin protein. The E1 enzyme then passes the ubiquitin protein to a second protein, called ubiquitin carrier ... Finally, the E1-ubiquitin complex transfers ubiquitin to an E2 enzyme through a transthioesterification reaction, in which an ... It also shows how two ubiquitin substrates can be bound at one time. Figure 2. E1 protein binds a molecule of ubiquitin in each ... At the start of the ubiquitination cascade, the E1 enzyme (Figure 2) binds ATP-Mg2+ and ubiquitin and catalyses ubiquitin C- ...

https://en.wikipedia.org/wiki/Ubiquitin-activating_enzyme

... and ubiquitin, whereas its 3 products are AMP, diphosphate, and (ubiquitin)n-calmodulin. This enzyme belongs to the family of ... n ubiquitin ⇌ {\displaystyle \rightleftharpoons } n AMP + n diphosphate + (ubiquitin)n-calmodulin The 3 substrates of this ... ubiquitin ligase (AMP-forming). Other names in common use include ubiquityl-calmodulin synthase, ubiquitin-calmodulin ... In enzymology, an ubiquitin-calmodulin ligase (EC 6.3.2.21) is an enzyme that catalyzes the chemical reaction n ATP + ...

https://en.wikipedia.org/wiki/Ubiquitin—calmodulin_ligase

... is a protein that in humans is encoded by the USP54 gene. GRCh38: Ensembl release 89: ... "Entrez Gene: Ubiquitin specific peptidase 54". Retrieved 2017-10-16. v t e (Articles with short description, Short description ...

https://en.wikipedia.org/wiki/Ubiquitin_specific_peptidase_54

... is a protein that in humans is encoded by the USP38 gene. GRCh38: Ensembl release 89: ... "Entrez Gene: Ubiquitin specific peptidase 38". Retrieved 2016-08-22. v t e (Articles with short description, Short description ...

https://en.wikipedia.org/wiki/Ubiquitin_specific_peptidase_38

The terms 'Ubiquitin Bacterial' and 'Prokaryotic ubiquitin-like protein' suggest a molecular similarity between ubiquitin and ... Ubiquitin was named for its ubiquitous presence among eukaryotes, while UBact ('Ubiquitin bacterial') is very limited in ... Prokaryotic ubiquitin-like protein (Pup) is a functional analog of ubiquitin found in the prokaryote Mycobacterium tuberculosis ... "Ubiquitin-like protein Pup [Leptospirillum ferriphilum] - Protein - NCBI". "Ubiquitin-like protein UBact [Leptospirillum ...

https://en.wikipedia.org/wiki/Prokaryotic_ubiquitin-like_protein

... may refer to: Ubiquitin carboxy-terminal hydrolase L1, an enzyme Ubiquitinyl hydrolase 1, an ...

https://en.wikipedia.org/wiki/Ubiquitin_C-terminal_hydrolase

... (UBE3B) is an enzyme encoded by UBE3B gene in humans. UBE3B has an N-terminal IQ motif, which ... "Deficiency for the ubiquitin ligase UBE3B in a blepharophimosis-ptosis-intellectual-disability syndrome". American Journal of ... "The ubiquitin ligase UBE3B, disrupted in intellectual disability and absent speech, regulates metabolic pathways by targeting ... Mitochondrion-associated E3 Ubiquitin Ligase". The Journal of Biological Chemistry. 292 (6): 2470-2484. doi:10.1074/jbc. ...

https://en.wikipedia.org/wiki/Ubiquitin-Protein_Ligase_E3B

... is a protein that in humans is encoded by the DTX4 gene. GRCm38: Ensembl release 89: ... "Entrez Gene: Deltex E3 ubiquitin ligase 4". Retrieved 2018-07-05. Cui J, Li Y, Zhu L, Liu D, Songyang Z, Wang HY, Wang RF ( ... "NLRP4 negatively regulates type I interferon signaling by targeting the kinase TBK1 for degradation via the ubiquitin ligase ...

https://en.wikipedia.org/wiki/Deltex_e3_ubiquitin_ligase_4

... (EC 3.1.2.15, ubiquitin C-terminal hydrolase, UCH-L1) is a deubiquitinating enzyme. UCH ... "Entrez Gene: UCHL1 ubiquitin carboxyl-terminal esterase L1 (ubiquitin thiolesterase)". Das C, Hoang QQ, Kreinbring CA, ... an important component of the ubiquitin proteasome system. It is thought that by stabilizing the monomers of ubiquitin and ... Ubiquitin+Carboxy-Terminal+Hydrolase at the US National Library of Medicine Medical Subject Headings (MeSH) Overview of all the ...

https://en.wikipedia.org/wiki/Ubiquitin_carboxy-terminal_hydrolase_L1

... is a protein that in humans is encoded by the UBE2Q2 gene. GRCh38: Ensembl release 89: ... "Entrez Gene: Ubiquitin conjugating enzyme E2 Q2". Retrieved 2018-01-18. Seghatoleslam A, Zambrano A, Millon R, Ganguli G, ... Maeda H, Miyajima N, Kano S, Tsukiyama T, Okumura F, Fukuda S, Hatakeyama S (2009). "Ubiquitin-conjugating enzyme UBE2Q2 ... Banerjee S, Brooks WS, Crawford DF (2007). "Inactivation of the ubiquitin conjugating enzyme UBE2Q2 causes a prophase arrest ...

https://en.wikipedia.org/wiki/Ubiquitin_conjugating_enzyme_e2_q2

... is a protein that in humans is encoded by the DTX3 gene. DTX3 functions as an E3 ubiquitin ligase ... "Entrez Gene: Deltex E3 ubiquitin ligase 3". Retrieved 2016-09-26. Takeyama K, Aguiar RC, Gu L, He C, Freeman GJ, Kutok JL, ... Aster JC, Shipp MA (2003). "The BAL-binding protein BBAP and related Deltex family members exhibit ubiquitin-protein isopeptide ...

https://en.wikipedia.org/wiki/Deltex_e3_ubiquitin_ligase_3

Ubiquitin carboxyl-terminal hydrolase isozyme L5 is an enzyme that in humans is encoded by the UCHL5 gene. GRCh38: Ensembl ... "Entrez Gene: UCHL5 ubiquitin carboxyl-terminal hydrolase L5". Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to ...

https://en.wikipedia.org/wiki/Ubiquitin_carboxyl-terminal_hydrolase_L5

... is a protein that in humans is encoded by the ZUP1 gene. GRCh38: Ensembl release ... "Entrez Gene: Zinc finger containing ubiquitin peptidase 1". Retrieved 2018-03-03. v t e (Articles with short description, Short ...

https://en.wikipedia.org/wiki/Zinc_finger_containing_ubiquitin_peptidase_1

... is a protein that in humans is encoded by the UBE2F gene. GRCh38: Ensembl release ... "Entrez Gene: Ubiquitin conjugating enzyme E2 F (putative)". Retrieved 2017-08-17. PDBe-KB provides an overview of all the ...

https://en.wikipedia.org/wiki/Ubiquitin_conjugating_enzyme_E2_F_(putative)

... is a protein that in humans is encoded by the NEURL3 gene. GRCh38: Ensembl release 89 ... "Entrez Gene: Neuralized E3 ubiquitin protein ligase 3". Retrieved 2016-02-18. v t e (Genes on human chromosome 2, All stub ...

https://en.wikipedia.org/wiki/Neuralized_e3_ubiquitin_protein_ligase_3

... is a protein that in humans is encoded by the UFC1 gene. UFC1 is an E2-like ... "Entrez Gene: Ubiquitin-fold modifier conjugating enzyme 1". Retrieved 2020-04-15. Komatsu M, Chiba T, Tatsumi K, Iemura S, ... Tellermann A, Witte T, Lansche C, Stoll M, Schmidt RE, Baerlecken NT (February 2015). "Autoantibodies binding to ubiquitin-fold ... a ubiquitin-fold modifier". EMBO J. 23 (9): 1977-86. doi:10.1038/sj.emboj.7600205. PMC 404325. PMID 15071506. Liu G, Forouhar F ...

https://en.wikipedia.org/wiki/Ubiquitin-fold_modifier_conjugating_enzyme_1

Ubiquitin is synthesized as a precursor protein consisting of either polyubiquitin chains or a single ubiquitin moiety fused to ... 1985). "Nucleotide sequence analysis of a cDNA encoding human ubiquitin reveals that ubiquitin is synthesized as a precursor". ... "Mammalian class E vps proteins recognize ubiquitin and act in the removal of endosomal protein-ubiquitin conjugates". J. Cell ... Ubiquitin is a highly conserved nuclear and cytoplasmic protein that has a major role in targeting cellular proteins for ...

https://en.wikipedia.org/wiki/Ubiquitin_A-52_residue_ribosomal_protein_fusion_product_1

"Ubiquitin Signalling". WEHI. 17 April 2019. "ACRF Centre for Therapeutic Target Discovery". Australian Cancer Research ... Ubiquitin Signalling (Professor David Komander) The institute is one of five research centres to establish the ACRF Centre for ...

https://en.wikipedia.org/wiki/WEHI

The ubiquitin-proteasome pathway has a critical role in maintaining the homeostasis of cells and is believed to be involved in ... In 2004, he was awarded the Nobel Prize in Chemistry for his discovery with Avram Hershko and Irwin Rose, of ubiquitin-mediated ... Hershko, A. and Ciechanover, A. (1998). THE UBIQUITIN SYSTEM. Biochem. 1998 67:1, 425-479 Ciechanover was an invited guest ... From a Vague Idea thru the Lysosome and the Ubiquitin-Proteasome System and onto Human Diseases and Drug Targeting Website at ...

https://en.wikipedia.org/wiki/Aaron_Ciechanover

The Arg-Arg-Leu amino acid segment (abbreviated RRL) takes part in ubiquitin interactions while Trp-Trp-Tyr (abbreviated WWY) ... MYO6 has been shown to interact with GIPC1, DAB2., ubiquitin, and clathrin. Myosin VI, being a motor protein, focuses its ... Myosin-VI long struggles to interact with ubiquitin chains and GIPC1 due to this structural formation, however, increases ... March 2016). "Myosin VI Contains a Compact Structural Motif that Binds to Ubiquitin Chains". Cell Reports. 14 (11): 2683-2694. ...

https://en.wikipedia.org/wiki/Unconventional_myosin-VI

The MID1 E3 ubiquitin ligase activity is catalysed by the RING domain, a hallmark of one of the main classes of E3 ubiquitin ... Several MID1 E3 ubiquitin ligase targets have been reported: Alpha4 (α4) and its associated phosphatase, PP2A, Fu, Pax6 and ... MID1 is a microtubular protein that acts as an ubiquitin E3 ligase in vitro and in cells. Ubiquitination is a type of post- ... Napolitano LM, Jaffray EG, Hay RT, Meroni G (March 2011). "Functional interactions between ubiquitin E2 enzymes and TRIM ...

https://en.wikipedia.org/wiki/MID1

Ubiquitin News and Research. RSS Ubiquitin is a small regulatory protein that has been found in almost all cells ( ... Insight into ubiquitin system A faulty gene linked to a rare blood vessel disorder has led investigators to discover a ... announce the publication of a research article entitled "A Small Molecule Inhibitor of Ubiquitin-Specific Protease-7 Induces ...

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ubiquitin specific protease 45. ubiquitin thioesterase 45. ubiquitin thiolesterase 45. ubiquitin-specific-processing protease ... ubiquitin specific peptidase 45provided by HGNC. Primary source. HGNC:HGNC:20080 See related. Ensembl:ENSG00000123552 MIM: ... involved_in ubiquitin-dependent protein catabolic process IEA Inferred from Electronic Annotation. more info ... USP45 ubiquitin specific peptidase 45 [ Homo sapiens (human) ] Gene ID: 85015, updated on 5-Aug-2022 ...

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Significant mentions of ubiquitin protein ligase e3a: Help Advanced Feedback iPhone/iPad Android API @RhymeZoneCom Blog Privacy ...

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The process of creating free ubiquitin chains, compounds composed of a large number of ubiquitin monomers. These chains are not ... Gene Ontology Term: free ubiquitin chain polymerization. GO ID. GO:0010994 Aspect. Biological Process. Description. ...

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... and ubiquitin-like proteins (Ubls) are conjugated to their targets by specific cascades involving three classes of enzymes, E1 ... Ubiquitin (Ub) and ubiquitin-like proteins (Ubls) are conjugated to their targets by specific cascades involving three classes ... Structural insights into E1-catalyzed ubiquitin activation and transfer to conjugating enzymes Cell. 2008 Jul 25;134(2):268-78. ... The negatively charged C-terminal ubiquitin-fold domain (UFD) is primed for binding of E2s and recognizes their positively ...

https://pubmed.ncbi.nlm.nih.gov/18662542/?dopt=Abstract

Furthermore, analyses of AhA degradation in cells bearing a temperature-sensitive mutation in the ubiquitin-activating enzyme ( ... Collectively, these studies demonstrate that TCDD induces degradation of AhA via a ubiquitin-proteasome pathway. Lastly, we ...

https://www.cdc.gov/niosh/nioshtic-2/20020997.html

All ubiquitin articles in Chemistry World

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Proton-Detected 4D DREAM Solid-State NMR Structure of Ubiquitin ... Ubiquitin. A. 76. Homo sapiens. Mutation(s): 0 Gene Names: UBC ... Proton-Detected 4D DREAM Solid-State NMR Structure of Ubiquitin. *PDB DOI: 10.2210/pdb2L3Z/pdb ...

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Our data are consistent with AnkUBD functioning as an enzymatic S1′ ubiquitin-binding site, which orients a ubiquitin chain so ... NMR analysis identifies the ankyrin domain as a new ubiquitin-binding fold, which we have termed AnkUBD, and DUB assays in ... Structural analysis of TRABID reveals an unpredicted ankyrin-repeat domain that binds ubiquitin and is crucial for TRABID ... Eight different types of ubiquitin linkages are present in eukaryotic cells that regulate diverse biological processes. ...

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J:303991 Bedekovics T, et al., USP24 Is a Cancer-Associated Ubiquitin Hydrolase, Novel Tumor Suppressor, and Chromosome ...

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Ubiquitin and Ubiquitin-Like Protein Resources. Page View: CST signaling pathway diagrams allow you to click on individual ... forms a thio-ester bond with ubiquitin. This reaction allows subsequent binding of ubiquitin to a "ubiquitin conjugating enzyme ... Small ubiquitin-related modifier 1, 2, and 3 (SUMO-1, -2, and -3) and NEDD8 are members of the ubiquitin-like protein family. ... DUB activity maintains ubiquitin recycling and ensures the cellular pool of ubiquitin molecules remains steady. DUBs are ...

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More info for Family d.15.1.1: Ubiquitin-related. Timeline for Family d.15.1.1: Ubiquitin-related: *Family d.15.1.1: Ubiquitin- ... Superfamily d.15.1: Ubiquitin-like [54236] (8 families) *. Family d.15.1.1: Ubiquitin-related [54237] (38 proteins). Pfam ... Family d.15.1.1: Ubiquitin-related appears in SCOP 1.73. *Family d.15.1.1: Ubiquitin-related appears in SCOPe 2.01. *Family d. ... Ubiquitin-like protein 7 [142942] (1 species). *. Species Mouse (Mus musculus) [TaxId:10090] [142943] (1 PDB entry). Uniprot ...

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Lysine63-linked ubiquitin chains earmark GPCRs for BBSome-mediated removal from cilia. Swapnil Rohidas Shinde, Andrew R. Nager ... Removal of ubiquitin acceptor residues from the somatostatin receptor 3 (SSTR3) and from the orphan GPCR GPR161 demonstrates ... Here we find that, upon activation, ciliary GPCRs become tagged with K63-linked ubiquitin (K63Ub) chains in a β-arrestin- ... Lysine63-linked ubiquitin chains earmark GPCRs for BBSome-mediated removal from cilia ...

https://www.biorxiv.org/content/10.1101/2020.03.04.977090v2

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The N-terminal domain of the Aurora-A Phe-31 variant encodes an E3 ubiquitin ligase and mediates ubiquitination of I{kappa}B{ ... Noncanonical MMS2-encoded ubiquitin-conjugating enzyme functions in assembly of novel polyubiquitin chains for DNA repair. ...

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Like all ubiquitin ligases, the peroxisomal ubiquitin ligase complex needs to cooperate with ubiquitin-conjugating (E2) enzymes ... The peroxisomal ubiquitin ligase complex. The components of the peroxisomal ubiquitin ligase complex were discovered ... In step 4, the N terminus of PEX5 inserts into the pore of the ubiquitin ligase complex and a ubiquitin (Ub) molecule is ... In step 4, the N terminus of PEX5 inserts into the pore of the ubiquitin ligase complex and a ubiquitin (Ub) molecule is ...

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... Apr 1, 2009 , Magazine: Neurobiology of ... We identified association of ubiquitin associated protein 1 (UBAP1; OR 1.42 95% CI 1.08-1.88, P=0.013) with FTLD in this cohort ...

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... Smrt RD, Szulwach KE, Pfeiffer RL, Li ... MicroRNA miR-137 regulates neuronal maturation by targeting ubiquitin ligase mind bomb-1. Zhao, PhD, X. MicroRNA MiR-137 ... MicroRNA miR-137 regulates neuronal maturation by targeting ubiquitin ligase mind bomb-1 ... MicroRNA miR-137 regulates neuronal maturation by targeting ubiquitin ligase mind bomb-1. Stem Cells. Jun;28(6):1060-70 PMCID: ...

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Occasional auto-modification of ubiquitin ligases typically leads to their proteasomal destruction, but new findings published ... Occasional auto-modification of ubiquitin ligases typically leads to their proteasomal destruction, but new findings published ... Hill, S., Kleiger, G. (2017). Self-regulating Ubiquitin Ligases. EMBO Journal http://dx.doi.org/10.15252/embj.201696154. ...

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... 2003-06-01 Affiliation ... NIRF is a ubiquitin ligase that is capable of ubiquitinating PCNP, a PEST-containing nuclear protein.. 21. ... NIRF is a ubiquitin ligase that is capable of ubiquitinating PCNP, a PEST-containing nuclear protein.. 21. ... Intranuclear degradation of polyglutamine aggregates by the ubiquitin-proteasome system.. 37. 21598301. 2011. Cooperative DNA ...

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Ubiquitin can itself be phosphorylated and cross-talk between ubiquitin and the kinase pathway and ubiquitin and SUMO has been ... The team also suggest that the study of exosomal proteins may provide a non-invasive approach to the study of ubiquitin ... It seems that far from acting as a mere marker for protein degradation ubiquitin is applying new regulatory roles within the ... ESCRT is a protein located on the outer membrane of the multi-vesicular body that contains multiple ubiquitin binding domains. ...

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The ubiquitin-proteasome system mediates a cellular stress response capable of eliminating misfolded proteins. Here we identify ... Cuz1/Ynl155w functions as a zinc-dependent ubiquitin-binding protein. Thus, Cuz1/Ynl155w is proposed to protect cells from ... Results: Ynl155w is a zinc-dependent ubiquitin-binding protein, interacts with proteasome and Cdc48, and is essential for ... "Cuz1/Ynl155w, a Zinc-Dependent Ubiquitin-Binding Protein, Protects Cells from Metalloid-Induced Proteotoxicity." Journal of ...

https://dash.harvard.edu/handle/1/41483193

Another is the ubiquitin-proteasome system. Broken or excess proteins are tagged with a ubiquitin molecule, which ensures they ... Most studies of proteolysis by the ubiquitin-proteasome pathway have focused on the regulation by ubiquitination. However, we ... Upregulation of the Ubiquitin-Proteasome System as a Potential Mode of Therapy. Permalink Read 2 Comments Add a Comment Posted ... The best-studied biochemical system used by cells to remove junk proteins is the ubiquitin-proteasome pathway. It involves ...

https://www.fightaging.org/archives/2019/02/upregulation-of-the-ubiquitin-proteasome-system-as-a-potential-mode-of-therapy/

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The latter reaction requires a "ubiquitin ligase" (E3). (cellsignal.com)
Recycling requires receptor monoubiquitination by a membrane-embedded ubiquitin ligase complex composed of three RING finger (RF) domain-containing proteins: PEX2, PEX10, and PEX12. (portlandpress.com)
Zhao, PhD, X. MicroRNA MiR-137 Regulates Neuronal Maturation by Targeting Ubiquitin Ligase Mind Bomb-1 . (wisc.edu)
NIRF is a ubiquitin ligase that is capable of ubiquitinating PCNP, a PEST-containing nuclear protein. (atlasgeneticsoncology.org)
Our preliminary results showed that introducing a point mutation within RING finger domain of E3 ubiquitin ligase Cbl-b into lpr mice (carrying a mutation in Fas gene) on a C57BL/6 background (B6-lpr.CblbC373A), exacerbates the disease. (lupusresearch.org)
Although the SCFSkp2 ubiquitin ligase has been reported to mediate p27Kip1 degradation, the nature of the human ubiquitin-conjugating enzyme involved in this process has not yet been determined at the cellular level. (novartis.com)
Furthermore, downregulation of Cdc34 is found to specifically increase the abundance of the SCFSkp2) ubiquitin ligase substrate p27Kip1, but has no concomitant effect on the level of IkBalpha and beta-catenin, which are known substrates of a closely related SCF ligase. (novartis.com)
The E3 ubiquitin ligase Itch restricts antigen-driven B cell responses. (upenn.edu)
The ubiquitin ligase Stub1 negatively modulates regulatory T cell suppressive activity by promoting degradation of the transcription factor Foxp3. (bvsalud.org)
Here, we demonstrate that stress signals elicited by proinflammatory cytokines and lipopolysaccharides lead to the degradation of Foxp3 through the action of the E3 ubiquitin ligase Stub1. (bvsalud.org)
So there clearly is an important function for the ubiquitin ligase, at least during spermatogenesis," Ludwig added. (the-scientist.com)
Site-Specific Protein Labeling with N-Hydroxysuccinimide-Esters and the Analysis of Ubiquitin Ligase Mechanisms. (harvard.edu)
Viral E3 Ubiquitin Ligase-Mediated Degradation of a Cellular E3: Viral Mimicry of a Cellular Phosphorylation Mark Targets the RNF8 FHA Domain,' Molecular Cell, published online March 8, 2012, to appear in print, April 13, 2012. (infectioncontroltoday.com)
Activities and binding partners of E3 ubiquitin ligase DTX3L and its roles in cancer. (oulu.fi)
DTX3L is a multi-domain E3 ubiquitin ligase in which the N-terminus mediates protein oligomerisation, a middle D3 domain mediates the interaction with PARP9, a RING domain responsible for recognising E2 ∼ Ub and a DTC domain has the dual activity of ADP-ribosylating ubiquitin and mediating ubiquitination. (oulu.fi)
Pirh2 E3 ubiquitin ligase targets DNA. (neb.com)
Mdm2 protein functions both as an E3 ubiquitin ligase that recognizes the N-terminal trans-activation domain (TAD) of the p53 tumor suppressor. (mdm2signaling.com)

Ubiquitin (Ub) and ubiquitin-like proteins (Ubls) are conjugated to their targets by specific cascades involving three classes of enzymes, E1, E2, and E3. (nih.gov)
The ubiquitin-proteasome system (UPS) is the primary means by which cellular proteins are degraded and is a highly regulated system for elimination of misfolded or damaged proteins as well as proteins whose activity is acutely regulated by signaling pathways. (cellsignal.com)
Ubiquitin is a highly conserved 76-amino acid protein that can be covalently linked to many cellular proteins by the ubiquitination process. (cellsignal.com)
With over 20 years' experience providing high quality recombinant proteins, small molecules, and substrates to the ubiquitin research community, R&D Systems has built the widest available selection of ubiquitin and ubiquitin-related products. (rndsystems.com)
If you need help with Targeted Protein Degradation (TPD or PROTACS ® ) assays, we provide a rapidly expanding portfolio of highly active E3 Ubiquitin Ligases including VHL and Cereblon (CRBN) proteins. (rndsystems.com)
We specialize in providing the highest quality ubiquitin and ubiquitin-like (Ubl) proteins, E1, E2 and E3 Ubiquitin ligases, proteasomes and other UPS-related reagents. (rndsystems.com)
With the sheer number of proteins encompassing the ubiquitin field, we must prioritize which proteins to produce. (rndsystems.com)
In particular, we focus our current efforts on the ubiquitin-binding proteins (UBDs), which interact with ubiquitylated substrates and mediate their cellular fates and downstream signaling. (igbmc.fr)
Attachment of ubiquitin to substrate proteins regulates proteolytic and non-proteolytic pathways during mitosis. (igbmc.fr)
The ubiquitin-binding proteins determine the fate of the ubiquitylated substrates and serve as intracellular "receptors" for the specific ubiquitin signals. (igbmc.fr)
Whole cell extracts (15 µg protein) from HeLa cells untreated (-) or treated with 10 µM MG-132 for 10 hours (+) were resolved by 4-12% Bis-Tris gel electrophoresis, transferred to a PVDF membrane, and probed with 0.25 µg/mL (1:4000 dilution) biotin anti-Ubiquitin antibody (clone P4D1) overnight at 4°C. Proteins were visualized by chemiluminescence detection using HRP streptavidin (Cat. (biolegend.com)
It is involved in a post-translation modification of proteins called ubiquitination of proteins by the covalent attachment (via an isopeptide bond) of one or more than one ubiquitin monomers. (biolegend.com)
This antibody recognizes ubiquitin, polyubiquitin, and ubiquitin-conjugated proteins. (biolegend.com)
This gene encodes ubiquitin, one of the most conserved proteins known. (origene.com)
Ubiquitin has a major role in targeting cellular proteins for degradation by the 26S proteosome. (origene.com)
In fact, the presence of ubiquitinated proteins within urinary exosomes was so high, that analysis by mass spectrometry showed ubiquitin itself was the third most abundant protein in the exosomal fraction of urine samples. (avacta.com)
While it raises a lot of questions about the function of ubiquitin signalling in exosomes, this new study reveals that ubiquitinated proteins can be packaged into exosomes for secretion and offers the cell biology community a resource of numerous new ubiquitination sites for study. (avacta.com)
The team also suggest that the study of exosomal proteins may provide a non-invasive approach to the study of ubiquitin modifications in health and disease. (avacta.com)
The ubiquitin-proteasome system mediates a cellular stress response capable of eliminating misfolded proteins. (harvard.edu)
Broken or excess proteins are tagged with a ubiquitin molecule, which ensures they are broken up for raw materials by a proteasome. (fightaging.org)
The best-studied biochemical system used by cells to remove junk proteins is the ubiquitin-proteasome pathway. (fightaging.org)
It involves tagging defective or unneeded proteins with ubiquitin molecules marking them for destruction by the cell's protein-disposal unit, known as 26S proteasome . (fightaging.org)
Recognizes mono- and poly ubiquitinylated proteins, but not free ubiquitin. (merckmillipore.com)
The ubiquitin-proteasome system (UPS) is the main pathway responsible for the degradation of misfolded proteins, and its dysregulation has been implicated in several neurodegenerative diseases, including Alzheimer's disease (AD). (chalmers.se)
Tagging' a protein with ubiquitin is a post-translational modification that can improve interactions between proteins to promote signaling, or initiate protein degradation. (upenn.edu)
Parkin plays a role in the cell machinery that breaks down (degrades) unneeded proteins by tagging damaged and excess proteins with molecules called ubiquitin. (medlineplus.gov)
Ubiquitin serves as a signal to move unneeded proteins into specialized cell structures known as proteasomes, where the proteins are degraded. (medlineplus.gov)
The ubiquitin-proteasome system acts as the cell's quality control system by disposing of damaged, misshapen, and excess proteins. (medlineplus.gov)
Because of its activity in the ubiquitin-proteasome system, parkin belongs to a group of proteins called E3 ubiquitin ligases. (medlineplus.gov)
The loss of parkin activity probably disturbs the ubiquitin-proteasome system, which allows unneeded proteins to accumulate. (medlineplus.gov)
However, of the eight possible types of ubiquitin linkages, most have been assigned non-degradative roles and instead serve scaffolding functions for recruitment and activation of proteins. (bl.uk)
The latter is known to bind to the protein BARD1 (BRCA1-associated RING domain protein 1) and form a complex that helps attach ubiquitin to proteins. (the-scientist.com)
Adenovirus encodes two proteins, E1B55K and E4orf6, that work together to co-opt the host's ubiquitin machinery for the virus's own gain. (chop.edu)
E3 ubiquitin ligases regulate the final step of the ubiquitination reaction by recognising target proteins and mediating the ubiquitin transfer from an E2 enzyme. (oulu.fi)
Ubiquitin becomes activated through a series of complicated steps and forms an isopeptide bond to lysine residues of specific proteins within the cell. (bvsalud.org)

Ubiquitination is required for certain histone methylation events and involves ubiquitin-activating enzymes (E1s), ubiquitin-conjugating enzymes (E2s), and ubiquitin-protein ligases (E3s). (merckmillipore.com)
Major UPS components are ubiquitin (Ub), Ub ligases, Ub hydrolases (deubiquitinases [DUBs]), and the proteasome. (cytoskeleton.com)
Activation of the UPS begins with attachment of an 8 kDa ubiquitin protein to a target protein by a three step cascade carried out by Ub ligases. (cytoskeleton.com)
Ubiquitylation is regulated by enzymes that add (E3 ubiquitin ligases) or subtract (deubiquitylating enzymes) ubiquitin from substrates. (upenn.edu)
We use systems biology approaches to define changes in ubiquitylation as activation states change, and to identify ubiquitin ligases that regulate immune cell fate. (upenn.edu)
One area of focus in the lab has centered on catalytic HECT-type E3 ubiquitin ligases of the Nedd4-family. (upenn.edu)
Our recent work has employed systems biology approaches in which we intrgrated transcriptome, proteome and ubiquitome information to identify Cullin E3 ubiquitin ligases that are particularly active as T cells transition from resting to activated states. (upenn.edu)
We are now poised to define how cullin ligases form distinct ubiquitin complexes in T cells or other immune cells, and the unique set of substrates targeted by these complexes. (upenn.edu)

Furthermore, analyses of AhA degradation in cells bearing a temperature-sensitive mutation in the ubiquitin-activating enzyme (E1) reveal that degradation of AhA in both untreated and TCDD-treated cells requires functional E1. (cdc.gov)
A "ubiquitin activating enzyme" (E1) forms a thio-ester bond with ubiquitin. (cellsignal.com)
This reaction allows subsequent binding of ubiquitin to a "ubiquitin conjugating enzyme" (E2), followed by the formation of an isopeptide bond between the carboxy-terminus of ubiquitin and the ε-amino group of a lysine residue on the substrate protein. (cellsignal.com)
UbcH10 is a ubiquitin-conjugating enzyme with high expression in various types of cancers. (spandidos-publications.com)
Okamoto Y, Ozaki T, Miyazaki K, Aoyama M, Miyazaki M and Nakagawara A: UbcH10 is the cancer-related E2 ubiquitin-conjugating enzyme. (spandidos-publications.com)
van Ree JH, Jeganathan KB, Malureanu L and van Deursen JM: Overexpression of the E2 ubiquitin-conjugating enzyme UbcH10 causes chromosome missegregation and tumor formation. (spandidos-publications.com)
Perrotta I, Bruno L, Maltese L, Russo E, Donato A and Donato G: Immunohistochemical analysis of the ubiquitin-conjugating enzyme UbcH10 in lung cancer: A useful tool for diagnosis and therapy. (spandidos-publications.com)
The ubiquitin-conjugating yeast enzyme RAD6 and its human homologs hHR6A and hHR6B are implicated in postreplication repair and damage-induced mutagenesis. (eurekamag.com)
The ubiquitin-modifying enzyme A20 restricts ubiquitination of the kinase RIPK3 and protects cells from necroptosis. (escholarship.org)
OTUB1 is a Lys48-specific deubiquitinating enzyme that forms a complex in vivo with E2 ubiquitin (Ub)-conjugating enzymes including UBC13 and UBCH5. (elsevier.com)
Structural and biochemical studies of human and worm OTUB1 and UBCH5B show that the E2 enzyme stimulates binding of the Lys48 polyubiquitin substrate by stabilizing folding of the OTUB1 N-terminal ubiquitin-binding helix. (elsevier.com)
The human ubiquitin-conjugating enzyme Cdc34 controls cellular proliferation through regulation of p27Kip1 protein levels. (novartis.com)
Here, we show that antisense oligonucleotides targeting the human ubiquitin-conjugating enzyme Cdc34 downregulate its expression, inhibit the degradation of p27Kip1, and prevent cellular proliferation. (novartis.com)
lacks catalytic cysteine residue found in ubiquitin-conjugating enzyme E2. (or.jp)

TCDD-induced degradation of Ah receptor by the ubiquitin-proteasome pathway. (cdc.gov)
Collectively, these studies demonstrate that TCDD induces degradation of AhA via a ubiquitin-proteasome pathway. (cdc.gov)
The 26S proteasome is a highly abundant ~2 MDa complex that serves as the proteolytic arm of the ubiquitin-proteasome system. (cellsignal.com)
R&D Systems is your best source for Ubiquitin Proteasome System (UPS) related research products. (rndsystems.com)
R&D Systems Ubiquitin-Proteasome Group, formerly known as Boston Biochem, is the leading global producer of ubiquitin-related research products. (rndsystems.com)
Since 1997, it has been our mission to provide ubiquitin proteasome system (UPS) researchers with innovative tools that facilitate and accelerate drug discovery efforts. (rndsystems.com)
Intranuclear degradation of polyglutamine aggregates by the ubiquitin-proteasome system. (atlasgeneticsoncology.org)
Background: Protein misfolding, a universal threat to cells, is dealt with by the ubiquitin-proteasome system. (harvard.edu)
Results: Ynl155w is a zinc-dependent ubiquitin-binding protein, interacts with proteasome and Cdc48, and is essential for surviving metalloids. (harvard.edu)
Here we identify Cuz1/Ynl155w as a component of the ubiquitin system, capable of interacting with both the proteasome and Cdc48. (harvard.edu)
Another is the ubiquitin-proteasome system . (fightaging.org)
Like other forms of cellular maintenance, the pace at which the ubiquitin-proteasome system operates is regulated and responds to environmental cues such as lack of nutrients resulting from calorie restriction or the oxidative stress that results from mitochondrial activity during exercise . (fightaging.org)
Research programs tend to start by using exercise or calorie restriction to help understand how exactly the ubiquitin-proteasome system functions, and how proteasomal activity is regulated, and then proceed to find ways to intervene at the point of regulation. (fightaging.org)
Combined, these data verify the p53-independence of cell death caused by inhibitors of the proteasome pathway and support the proposition that the ubiquitin-dependent proteasome pathway may contain molecular targets suitable for antineoplastic drug discovery. (aspetjournals.org)
A protein marked for degradation is covalently attached to multiple molecules of ubiquitin, a highly conserved 76 aa (8.6 kda) protein, which escorts it for rapid hydrolysis to the 26S proteasome. (merckmillipore.com)
The ubiquitin-proteasome pathway has been implicated in several forms of malignancy, in the pathogenesis of several genetic diseases, and in the pathology of muscle wasting. (merckmillipore.com)
Merck 's tools for studying ubiquitin signaling have helped immensely in understanding the biological role and importance of the ubiquitin-proteasome pathway. (merckmillipore.com)
Ubiquitin-Proteasome System As A Therapeutic Target: Does Tubulin Care? (cytoskeleton.com)
The ubiquitin-proteasome system (UPS) is a well-characterized protein degradation system in cells whose dysfunction is implicated in many diseases, including neurodegeneration and cancer 1,2 . (cytoskeleton.com)
Researchers believe that the ubiquitin-proteasome system may play a role in controlling infection. (medlineplus.gov)
Polymorphisms in the PRKN gene may subtly alter parkin's function, making the ubiquitin-proteasome system less efficient. (medlineplus.gov)

Quantitative proteomics reveals the function of unconventional ubiquitin chains in proteasomal degradation. (nature.com)
It seems that far from acting as a mere marker for protein degradation ubiquitin is applying new regulatory roles within the cell. (avacta.com)
In these processes, ubiquitin functions as both a signal for protein degradation and as a chaperone promoting the formation of organelles. (merckmillipore.com)
Our results suggest that OTUB1-E2 complexes in the cell are poised to regulate polyubiquitin chain elongation or degradation in response to changing levels of E2 charging and available free ubiquitin. (elsevier.com)
Ubiquitin-mediated degradation of the cyclin-dependent kinase inhibitor p27Kip1 was shown to be required for the activation of key cyclin-dependent kinases, thereby triggering the onset of DNA replication and cell cycle progression. (novartis.com)
Ubiquitin acts as a sort of marker, either targeting the protein for degradation or affecting the protein's activity in other ways, such as promoting or preventing protein interactions. (chop.edu)

Deubiquitinating enzymes (DUBs) reverse the process of ubiquitination by removing ubiquitin from its substrate protein. (cellsignal.com)
Removal of ubiquitin acceptor residues from the somatostatin receptor 3 (SSTR3) and from the orphan GPCR GPR161 demonstrates that ubiquitination of ciliary GPCRs is required for their regulated exit from cilia. (biorxiv.org)
One of the molecular mechanisms driving fidelity of cell division is ubiquitylation (or ubiquitination), which is a covalent, posttranslational modification of substrates by a small protein ubiquitin. (igbmc.fr)
Merck is also the first provider of lead discovery services to target the ubiquitination pathway: visit our Lead Discovery Ubiquitin page . (merckmillipore.com)
Our wide range of products for measuring ubiquitination, includes unique antibodies for specific ubiquitin linkages and modified histone residues. (merckmillipore.com)
One way viruses promote infection is through ubiquitination, an enzymatic post-translational modification in which a ubiquitin protein is attached to a substrate protein. (chop.edu)

Ubiquitin can itself be phosphorylated and cross-talk between ubiquitin and the kinase pathway and ubiquitin and SUMO has been revealed. (avacta.com)
We report the phenotype of the first animal mutant in the ubiquitin pathway: inactivation of the hHR6B-homologous gene in mice causes male infertility. (eurekamag.com)

The process of creating free ubiquitin chains, compounds composed of a large number of ubiquitin monomers. (yeastgenome.org)
This stimulation is regulated by the ratio of charged to uncharged E2 and by the concentration of Lys48-linked polyubiquitin and free ubiquitin. (elsevier.com)

Eight different types of ubiquitin linkages are present in eukaryotic cells that regulate diverse biological processes. (nature.com)

Ubiquitin is a highly-conserved small protein expressed in all eukaryotes. (biolegend.com)
Ubiquitin is a polypeptide of 76 amino acid residues, being a very highly conserved and widely distributed protein in all eukaryotic cells. (merckmillipore.com)

Figure 6: Role of the NZF domains in cleaving longer ubiquitin chains. (nature.com)
Ikeda, F. & Dikic, I. Atypical ubiquitin chains: new molecular signals. (nature.com)
Here we find that, upon activation, ciliary GPCRs become tagged with K63-linked ubiquitin (K63Ub) chains in a β-arrestin-dependent manner prior to BBSome-mediated exit. (biorxiv.org)
Ubiquitin is synthesized as a precursor protein consisting of either polyubiquitin chains or a single ubiquitin moiety fused to an unrelated protein. (origene.com)
Linear ubiquitin chain assembly complex (LUBAC) is the only E3 known to generate M1-chains and is essential for productive signalling. (bl.uk)

DUB activity maintains ubiquitin recycling and ensures the cellular pool of ubiquitin molecules remains steady. (cellsignal.com)
The ubiquitin receptors (Ub-receptors) represent a novel and attractive class of druggable targets but to date no inhibitory small molecules exist that could be used in cancer therapies. (igbmc.fr)

Our group described the role of non-proteolytic ubiquitin signaling in the regulation of essential kinases during mitosis of human cells. (igbmc.fr)

Our data are consistent with AnkUBD functioning as an enzymatic S1′ ubiquitin-binding site, which orients a ubiquitin chain so that Lys29 and Lys33 linkages are cleaved preferentially. (nature.com)

Ubiquitin can be linked to a substrate as a single unit, monoubiquitination, or as a branched chain, polyubquitination. (cellsignal.com)

We combine this information with genetic, cellular and biochemical approaches to define how ubiquitin enzymes regulate immune cell biology. (upenn.edu)

In collaboration with the High Throughput Cell-based Screening facility at the IGBMC, we have performed a visual, high-throughput siRNA screen using customized, human 'Ubiquitin Decoders' library and developed multi-parametric control-based gene selection protocols. (igbmc.fr)
This gene consists of three direct repeats of the ubiquitin coding sequence with no spacer sequence. (origene.com)
Tal1 was found to bind in the vicinity of 31 genes including the E2-ubiquitin conjugase UBE2H gene. (mdc-berlin.de)
The first intron from Ubiquitin-1 enhances exogenous gene expression. (cbd.int)

NMR analysis identifies the ankyrin domain as a new ubiquitin-binding fold, which we have termed AnkUBD, and DUB assays in vitro and in vivo show that this domain is crucial for TRABID efficiency and linkage specificity. (nature.com)
Figure 2: TRABID contains two ankyrin repeats with roles in ubiquitin binding. (nature.com)

A) Model for regulation of localization and function of Aurora B by the ubiquitin receptor UBASH3B. (igbmc.fr)

Small ubiquitin-related modifier 1, 2, and 3 (SUMO-1, -2, and -3) and NEDD8 are members of the ubiquitin-like protein family. (cellsignal.com)

Formation of a polyubiquitin chain occurs when a lysine residue of ubiquitin is linked to the carboxy-terminal glycine of another ubiquitin. (cellsignal.com)

We offer a large range of full-length recombinant deubiquitinases (deubiquitylases, or DUBs) such as USP7 for enzymatic assays and high throughput screening campaigns, and provide the best quality DUB substrates such as Ubiquitin-AMC , Ubiquitin-rhodamine and ISG15-AMC . (rndsystems.com)

Cloning and enzymatic analysis of 22 novel human ubiquitin-specific proteases. (nih.gov)

Our recent investigations with electrophilic prostaglandins enabled us to devise a pharmacophore and mechanism of action hypothesis relevant to this problem: a cross-conjugated α,β-unsaturated dienone with two sterically accessible electrophilic β-carbons is a molecular determinant that confers activity among this class of ubiquitin isopeptidases inhibitors, and that inhibitors of ubiquitin isopeptidases cause cell death in vitro independently of p53. (aspetjournals.org)

Ubiquitin is a small regulatory protein that has been found in almost all cells (''ubiquitously'') with nuclei (eukaryotes). (news-medical.net)
We wish to understand both ubiquitin-dependent and ubiquitin-independent regulatory mechanisms ensuring localization of essential factors involved in these processes. (igbmc.fr)

The negatively charged C-terminal ubiquitin-fold domain (UFD) is primed for binding of E2s and recognizes their positively charged first alpha helix via electrostatic interactions. (nih.gov)

Tal1 expression activated UBE2H expression whereas Tal1 knock-down reduced UBE2H expression and ubiquitin transfer activity. (mdc-berlin.de)

Figure 3: A conserved hydrophobic surface on AnkUBD binds ubiquitin. (nature.com)
Figure 4: AnkUBD binds the ubiquitin hydrophobic patch. (nature.com)
OTUB1 binds E2∼Ub thioester intermediates and prevents ubiquitin transfer, thereby noncatalytically inhibiting accumulation of polyubiquitin. (elsevier.com)

UBB+1, a mutant variant of ubiquitin B, was found to accumulate in neurons of AD patients and it has been linked to UPS dysfunction and neuronal death. (chalmers.se)

Anatomy14

Organisms5

Diseases2

Chemicals and Drugs79

Analytical, Diagnostic and Therapeutic Techniques and Equipment16

Phenomena and Processes45

Information Science3

RPN4 is a ligand, substrate, and transcriptional regulator of the 26S proteasome: a negative feedback circuit. (1/5483)

Raft-partitioning of the ubiquitin ligases Cbl and Nedd4 upon IgE-triggered cell signaling. (2/5483)

The Mdm-2 amino terminus is required for Mdm2 binding and SUMO-1 conjugation by the E2 SUMO-1 conjugating enzyme Ubc9. (3/5483)

Heat capacity changes upon burial of polar and nonpolar groups in proteins. (4/5483)

Proteasomes are involved in the constitutive degradation of growth hormone receptors. (5/5483)

High and sustained transgene expression in vivo from plasmid vectors containing a hybrid ubiquitin promoter. (6/5483)

Effects of arachidonic and docosahexaenoic acids on secretion and degradation of bile salt-dependent lipase in AR4-2J cells. (7/5483)

Toxoplasma gondii tachyzoites inhibit proinflammatory cytokine induction in infected macrophages by preventing nuclear translocation of the transcription factor NF-kappa B. (8/5483)

Ubiquitin

Ubiquitin-Protein Ligases

Ubiquitins

Ubiquitin Thiolesterase

Ubiquitination

Ubiquitin-Conjugating Enzymes

Proteasome Endopeptidase Complex

Cullin Proteins

Polyubiquitin

Ligases

SKP Cullin F-Box Protein Ligases

Ubiquitin-Protein Ligase Complexes

Ubiquitin-Activating Enzymes

Ubiquitin C

Endosomal Sorting Complexes Required for Transport

F-Box Proteins

RING Finger Domains

Protein Binding

Proteolysis

Protein Structure, Tertiary

Amino Acid Sequence

Anaphase-Promoting Complex-Cyclosome

Molecular Sequence Data

Ubiquitinated Proteins

S-Phase Kinase-Associated Proteins

Cysteine Endopeptidases

Ubiquitin-Specific Proteases

Lysine

Proto-Oncogene Proteins c-cbl

Saccharomyces cerevisiae Proteins

Multienzyme Complexes

Mutation

HEK293 Cells

Carbon-Nitrogen Lyases

Cell Cycle Proteins

beta-Transducin Repeat-Containing Proteins

Carrier Proteins

Cell Line

Saccharomyces cerevisiae

HeLa Cells

Protein Processing, Post-Translational

Proteasome Inhibitors

Endopeptidases

Amino Acid Motifs

SUMO-1 Protein

Leupeptins

Signal Transduction

Nuclear Proteins

Protein Stability

Models, Molecular

Protein Transport

Small Ubiquitin-Related Modifier Proteins

Multiprotein Complexes

Peptide Hydrolases

Substrate Specificity

Sequence Homology, Amino Acid

Immunoprecipitation

Two-Hybrid System Techniques

Recombinant Fusion Proteins

Proto-Oncogene Proteins c-mdm2

DNA-Binding Proteins

Thiolester Hydrolases

Sumoylation

Proteins

Receptors, Autocrine Motility Factor

Models, Biological

Adaptor Proteins, Signal Transducing

Peptide Synthases

Protein Interaction Domains and Motifs

Binding Sites

RNA Interference

Transcription Factors

RNA, Small Interfering

Transfection

Repressor Proteins

Protein Folding

Cell Line, Tumor

Phosphorylation

Blotting, Western

Immunoblotting