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.

Identification of determinants in E2 ubiquitin-conjugating enzymes required for hect E3 ubiquitin-protein ligase interaction. (1/1387)

Members of the hect domain protein family are characterized by sequence similarity of their C-terminal regions to the C terminus of E6-AP, an E3 ubiquitin-protein ligase. An essential intermediate step in E6-AP-dependent ubiquitination is the formation of a thioester complex between E6-AP and ubiquitin in the presence of distinct E2 ubiquitin-conjugating enzymes including human UbcH5, a member of the UBC4/UBC5 subfamily of E2s. Similarly, several hect domain proteins, including Saccharomyces cerevisiae RSP5, form ubiquitin thioester complexes, indicating that hect domain proteins in general have E3 activity. We show here, by the use of chimeric E2s generated between UbcH5 and other E2s, that a region of UbcH5 encompassing the catalytic site cysteine residue is critical for its ability to interact with E6-AP and RSP5. Of particular importance is a phenylalanine residue at position 62 of UbcH5 that is conserved among the members of the UBC4/UBC5 subfamily but is not present in any of the other known E2s, whereas the N-terminal 60 amino acids do not contribute significantly to the specificity of these interactions. The conservation of this phenylalanine residue throughout evolution underlines the importance of the ability to interact with hect domain proteins for the cellular function of UBC4/UBC5 subfamily members.  (+info)

Histone ubiquitination and chromatin remodeling in mouse spermatogenesis. (2/1387)

Male infertility in HR6B knockout mice is associated with impairment of spermatogenesis. The HR6B gene is a mammalian, autosomal homolog of the Saccharomyces cerevisiae gene Rad6 encoding a ubiquitin-conjugating enzyme. In addition, X-chromosomal HR6A has been identified, in human and mouse. RAD6 in yeast is required for a variety of cellular functions, including sporulation, DNA repair, and mutagenesis. Since RAD6 and its mammalian homologs can ubiquitinate histones in vitro, we have investigated the pattern of histone ubiquitination in mouse testis. By immunoblot and immunohistochemical analysis of wild-type mouse testis, a high amount of ubiquitinated H2A (uH2A) was detected in pachytene spermatocytes. This signal became undetectable in round spermatids, but then increased again during a relatively short developmental period, in elongating spermatids. No other ubiquitinated histones were observed. In the HR6B knockout mice, we failed to detect an overt defect in the overall pattern of histone ubiquitination. For somatic cell types, it has been shown that histone ubiquitination is associated with destabilization of nucleosomes, in relation to active gene transcription. Unexpectedly, the most intense uH2A signal in pachytene spermatocytes was detected in the sex body, an inactive nuclear structure that contains the heterochromatic X and Y chromosomes. The postmeiotic uH2A immunoexpression in elongating spermatids indicates that nucleosome destabilization induced by histone ubiquitination may play a facilitating role during histone-to-protamine replacement.  (+info)

A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly. (3/1387)

Proteins modified by multiubiquitin chains are the preferred substrates of the proteasome. Ubiquitination involves a ubiquitin-activating enzyme, E1, a ubiquitin-conjugating enzyme, E2, and often a substrate-specific ubiquitin-protein ligase, E3. Here we show that efficient multiubiquitination needed for proteasomal targeting of a model substrate requires an additional conjugation factor, named E4. This protein, previously known as UFD2 in yeast, binds to the ubiquitin moieties of preformed conjugates and catalyzes ubiquitin chain assembly in conjunction with E1, E2, and E3. Intriguingly, E4 defines a novel protein family that includes two human members and the regulatory protein NOSA from Dictyostelium required for fruiting body development. In yeast, E4 activity is linked to cell survival under stress conditions, indicating that eukaryotes utilize E4-dependent proteolysis pathways for multiple cellular functions.  (+info)

Noncanonical MMS2-encoded ubiquitin-conjugating enzyme functions in assembly of novel polyubiquitin chains for DNA repair. (4/1387)

Ubiquitin-conjugating enzyme variant (UEV) proteins resemble ubiquitin-conjugating enzymes (E2s) but lack the defining E2 active-site residue. The MMS2-encoded UEV protein has been genetically implicated in error-free postreplicative DNA repair in Saccharomyces cerevisiae. We show that Mms2p forms a specific heteromeric complex with the UBC13-encoded E2 and is required for the Ubc13p-dependent assembly of polyubiquitin chains linked through lysine 63. A ubc13 yeast strain is UV sensitive, and single, double, and triple mutants of the UBC13, MMS2, and ubiquitin (ubiK63R) genes display a comparable phenotype. These findings support a model in which an Mms2p/Ubc13p complex assembles novel polyubiquitin chains for signaling in DNA repair, and they suggest that UEV proteins may act to increase diversity and selectivity in ubiquitin conjugation.  (+info)

Reconstitution of G1 cyclin ubiquitination with complexes containing SCFGrr1 and Rbx1. (5/1387)

Control of cyclin levels is critical for proper cell cycle regulation. In yeast, the stability of the G1 cyclin Cln1 is controlled by phosphorylation-dependent ubiquitination. Here it is shown that this reaction can be reconstituted in vitro with an SCF E3 ubiquitin ligase complex. Phosphorylated Cln1 was ubiquitinated by SCF (Skp1-Cdc53-F-box protein) complexes containing the F-box protein Grr1, Rbx1, and the E2 Cdc34. Rbx1 promotes association of Cdc34 with Cdc53 and stimulates Cdc34 auto-ubiquitination in the context of Cdc53 or SCF complexes. Rbx1, which is also a component of the von Hippel-Lindau tumor suppressor complex, may define a previously unrecognized class of E3-associated proteins.  (+info)

Caffeine-mediated override of checkpoint controls. A requirement for rhp6 (Schizosaccharomyces pombe). (6/1387)

Cells exposed to inhibitors of DNA synthesis or suffering DNA damage are arrested or delayed in interphase through the action of checkpoint controls. If the arrested cell is exposed to caffeine, relatively normal cell cycle progression is resumed and, as observed in checkpoint control mutants, loss of checkpoint control activity is associated with a reduction in cell viability. To address the mechanism of caffeine's action on cell progression, fission yeast mutants that take up caffeine but are not sensitized to hydroxyurea (HU) by caffeine were selected. Mutants 788 and 1176 are point mutants of rhp6, the fission yeast homolog of the budding yeast RAD6 gene. Mutant rhp6-788 is slightly HU sensitive, radiosensitive, and exhibits normal checkpoint responses to HU, radiation, or inactivation of DNA ligase. However, the addition of caffeine does not override the associated cell cycle blocks. Both point and deletion mutations show synthetic lethality at room temperature with temperature-sensitive mutations in cyclin B (cdc13-117) or the phosphatase cdc25 (cdc25-22). These observations suggest that the rhp6 gene product, a ubiquitin-conjugating enzyme required for DNA damage repair, promotes entry to mitosis in response to caffeine treatment.  (+info)

Identification of rabbit reticulocyte E217K as a UBC7 homologue and functional characterization of its core domain loop. (7/1387)

The structural basis by which ubiquitin (Ub)-conjugating enzymes (E2s) determine substrate specificity remains unclear. We cloned rabbit reticulocyte E217K because unlike the similarly sized class I E2s, E214K and UBC4, it is unable to support ubiquitin-protein ligase (E3)-dependent conjugation to endogenous proteins. RNA analysis revealed that this E2 was expressed in all tissues tested, with higher levels in the testis. Analysis of testis RNA from rats of different ages showed that E217K mRNA was induced from days 15 to 30. The predicted amino acid sequence indicates that E217K is a 19. 5-kDa class I E2 but differs from other class I enzymes in possessing an insertion of 13 amino acids distal to the active site cysteine. E217K shows 74% amino acid identity with Saccharomyces cerevisiae UBC7, and therefore, we rename it mammalian UBC7. Yeast UBC7 crystal structure indicates that this insertion forms a loop out of the otherwise conserved folding structure. Sequence analysis of E2s had previously suggested that this loop is a hypervariable region and may play a role in substrate specificity. We created mutant UBC7 lacking the loop (ubc7Deltaloop) and a mutant E214k with an inserted loop (E214k+loop) and characterized their biochemical functions. Ubc7Deltaloop had higher affinity for the E1-Ub thiol ester than native UBC7 and permitted conjugation of Ub to selected proteins in the testis but did not permit the broad spectrum E3-dependent conjugation to endogenous reticulocyte proteins. Surprisingly, E214k+loop was unable to accept Ub from ubiquitin-activating enzyme (E1) but was able to accept NEDD8 from E1. E214k+loop was able to support conjugation of NEDD8 to endogenous reticulocyte proteins but with much lower efficiency than E214k. Thus, the loop can influence interactions of the E2 with charged E1 as well as with E3s or substrates, but the exact nature of these interactions depends on divergent sequences in the remaining conserved core domain.  (+info)

Identification of the ubiquitin carrier proteins, E2s, involved in signal-induced conjugation and subsequent degradation of IkappaBalpha. (8/1387)

The last step in the activation of the transcription factor NF-kappaB is signal-induced, ubiquitin- and proteasome-mediated degradation of the inhibitor IkappaBalpha. Although most of the components involved in the activation and degradation pathways have been identified, the ubiquitin carrier proteins (E2) have remained elusive. Here we show that the two highly homologous members of the UBCH5 family, UBCH5b and UBCH5c, and CDC34/UBC3, the mammalian homolog of yeast Cdc34/Ubc3, are the E2 enzymes involved in the process. The conjugation reaction they catalyze in vitro is specific, as they do not recognize the S32A,S36A mutant species of IkappaBalpha that cannot be phosphorylated and conjugated following an extracellular signal. Furthermore, the reaction is specifically inhibited by a doubly phosphorylated peptide that spans the ubiquitin ligase recognition domain of the inhibitor. Cys-to-Ala mutant species of the enzymes that cannot bind ubiquitin inhibit tumor necrosis factor alpha-induced degradation of the inhibitor in vivo. Not surprisingly, they have a similar effect in a cell-free system as well. Although it is clear that the E2 enzymes are not entirely specific to IkappaBalpha, they are also not involved in the conjugation and degradation of the bulk of cellular proteins, thus exhibiting some degree of specificity that is mediated probably via their association with a defined subset of ubiquitin-protein ligases. The mechanisms that underlie the involvement of two different E2 species in IkappaBalpha conjugation are not clear at present. It is possible that different conjugating machineries operate under different physiological conditions or in different cells.  (+info)

Ubiquitin-conjugating enzyme E2 that specifically acts with HECT-type and RBR family E3 ubiquitin-protein ligases. Does not function with most RING-containing E3 ubiquitin-protein ligases because it lacks intrinsic E3-independent reactivity with lysine: in contrast, it has activity with the RBR family E3 enzymes, such as PRKN and ARIH1, that function like function like RING-HECT hybrids. Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes Lys-11-linked polyubiquitination. Involved in the selective degradation of short-lived and abnormal proteins. Down-regulated during the S-phase it is involved in progression through the cell cycle. Regulates nuclear hormone receptors transcriptional activity. May play a role in myelopoiesis.
Reagents for the antigen UBE2I / ubiquitin-conjugating enzyme E2I / UBC9 stained with APC-Cy7™ in the Antibody Database
TY - JOUR. T1 - The ubiquitin-conjugating enzyme UBCH7 acts as a coactivator for steroid hormone receptors. AU - Verma, Seema. AU - Ismail, Ayesha. AU - Gao, Xiuhua. AU - Fu, Guilian. AU - Li, Xiaotao. AU - OMalley, Bert W.. AU - Nawaz, Zafar. PY - 2004/10/1. Y1 - 2004/10/1. N2 - We investigated the role of the ubiquitin-conjugating enzyme UBCH7 in nuclear receptor transactivation. Using transient transfection assays, we demonstrated that UBCH7 modulates the transcriptional activity of progesterone receptor (PR) and glucocorticoid, androgen, and retinoic acid receptors in a hormone-dependent manner and that the ubiquitin conjugation activity of UBCH7 is required for its ability to potentiate transactivation by steroid hormone receptors (SHR). However, UBCH7 showed no significant effect on the transactivation functions of p53 and VP-16 activation domain. Depletion of endogenous UBCH7 protein by small interfering RNAs suggests that UBCH7 is required for the proper function of SHR. Furthermore, a ...
Mouse non-canonical ubiquitin-conjugating enzyme 2 ELISA Kit;Mouse NCUBE-2 ELISA Kit;Mouse Ncube2 ELISA Kit;Mouse 1200007B18Rik ELISA Kit;Mouse 2400008G19Rik ELISA Kit;Mouse 5730472G04Rik ELISA Kit;Mouse AL022923 ELISA Kit;Mouse Ubc6 ELISA Kit;Mouse Ubc6p ELISA Kit;Mouse ubiquitin-conjugating enzyme E2J 2 ELISA Kit;Mouse ubiquitin-conjugating enzyme E2 J2 ELISA Kit;Mouse Ubc6p homolog ELISA Kit;Mouse ubiquitin conjugating enzyme 6 ELISA Kit;Mouse ubiquitin-conjugating enzyme E2, J2 homolog ELISA Kit ...
Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. Specifically monoubiquitinates the N-terminus of various substrates, including ATXN3, MAPT/TAU, POLR2H/RPB8 and STUB1/CHIP, by recognizing backbone atoms of disordered N-termini. Involved in degradation of misfolded chaperone substrates by mediating monoubiquitination of STUB1/CHIP, leading to recruitment of ATXN3 to monoubiquitinated STUB1/CHIP, and restriction of the length of ubiquitin chain attached to STUB1/CHIP substrates by ATXN3. After UV irradiation, but not after mitomycin-C (MMC) treatment, acts as a specific E2 ubiquitin-conjugating enzyme for the Fanconi anemia complex by associating with E3 ubiquitin-protein ligase FANCL and catalyzing monoubiquitination of FANCD2, a key step in the DNA damage pathway. In vitro catalyzes Lys-11-linked polyubiquitination. UBE2W-catalyzed ubiquitination occurs also in the presence of inactive RING/U-box type E3s, i.e. lacking the active site cysteine residues to
C25-140 Featured C25-140 is a specific, first-in-class small molecule inhibitor of the TRAF6-Ubc13 interaction, binds TRAF6, inhibits TRAF6-Ubc13 interaction and TRAF6 activity.. ...
Reaktivität: Fledermaus, Huhn, Rind (Kuh) and more. verschiedene UBE2D1 Antikörper vergleichen. Alle direkt auf antikörper-online bestellbar!
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Réactivité: Roussette (Chauve-souris), Poulet, Boeuf (Vache) and more. Comparez 113 UBE2K Anticorps. Commandez directement chez anticorps-enligne.fr.
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The RAD6 gene of Saccharomyces cerevisiae is required for DNA repair, DNA damage-induced mutagenesis, and sporulation. RAD6 protein is a ubiquitin-conjugating enzyme (E2) that has been shown to attach multiple molecules of ubiquitin to histones H2A and H2B. We have now examined whether the E2 activity of RAD6 is involved in its various biological functions. Since the formation of a thioester adduct between E2 and ubiquitin is necessary for E2 activity, the single cysteine residue (Cys-88) present in RAD6 was changed to alanine or valine. The mutant proteins were overproduced in yeast cells and purified to near homogeneity. We show that the rad6 Ala-88 and rad6 Val-88 mutant proteins lack the capacity for thioester formation with ubiquitin and, as a consequence, are totally devoid of any E2 activity. The rad6 Ala-88 and rad6 Val-88 mutations confer a defect in DNA repair, mutagenesis, and sporulation equivalent to that in the rad6 null allele. We suggest that the biological functions of RAD6 ...
ER-resident proteins destined for degradation are dislocated into the cytosol by components of the ER quality control machinery for proteasomal degradation. Dislocation substrates are ubiquitylated in the cytosol by E2 ubiquitin-conjugating/E3 ligase complexes. UBE2J1 is one of the well-characterized E2 enzymes that participate in this process. However, the physiological function of Ube2j1 is poorly defined. We find that Ube2j1−/− mice have reduced viability and fail to thrive early after birth. Male Ube2j1−/− mice are sterile due to a defect in late spermatogenesis. Ultrastructural analysis shows that removal of the cytoplasm is incomplete in Ube2j1−/− elongating spermatids, compromising the release of mature elongate spermatids into the lumen of the seminiferous tubule. Our findings identify an essential function for the ubiquitin-proteasome-system in spermiogenesis and define a novel, non-redundant physiological function for the dislocation step of ER quality control ...
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TY - JOUR. T1 - Structural insights into K48-linked ubiquitin chain formation by the Pex4p-Pex22p complex. AU - Groves, Matthew R. AU - Schroer, Carsten F E. AU - Middleton, Adam J. AU - Lunev, Sergey. AU - Danda, Natasha. AU - Ali, Ameena M. AU - Marrink, Siewert J. AU - Williams, Chris. N1 - Copyright © 2017. Published by Elsevier Inc.. PY - 2018/2/5. Y1 - 2018/2/5. N2 - Pex4p is a peroxisomal E2 involved in ubiquitinating the conserved cysteine residue of the cycling receptor protein Pex5p. Previously, we demonstrated that Pex4p from the yeast Saccharomyces cerevisiae binds directly to the peroxisomal membrane protein Pex22p and that this interaction is vital for receptor ubiquitination. In addition, Pex22p binding allows Pex4p to specifically produce lysine 48 linked ubiquitin chains in vitro through an unknown mechanism. This activity is likely to play a role in targeting peroxisomal proteins for proteasomal degradation. Here we present the crystal structures of Pex4p alone and in complex ...
Author: Liwocha, Joanna et al.; Genre: Journal Article; Published in Print: 2020; Keywords: Enzyme mechanisms; Enzymes; Protein design|br/|; Title: Linkage-specific ubiquitin chain formation depends on a lysine hydrocarbon ruler
TY - JOUR. T1 - Characterization of novel yeast Rad6 (UBC2) ubiquitin-conjugating enzyme mutants constructed by charge-to-alanine scanning mutagenesis. AU - McDonough, Michele M. AU - Sagan, P. AU - Gonda, D. PY - 1995. Y1 - 1995. N2 - Ubiquitination of intracellular proteins by the yeast RAD6 (UBC2) ubiquitin-conjugating (E2) enzyme is required for cellular processes as diverse as DNA repair, selective proteolysis, and normal growth. For most RAD6-dependent functions, the relevant in vivo targets, as well as the mechanisms and cofactors that govern RAD6 substrate selectivity, are unknown. We have explored the utility of charge-to-alanine scanning mutagenesis to generate novel RAD6 mutants that are enzymatically competent with respect to unfacilitated (E3-independent) ubiquitination but that are nevertheless severely handicapped with respect to several in vivo functions. Five of the nine mutants we generated show defects in their in vivo functions, but almost all of the most severely affected ...
Ubiquitination, also known as ubiquitylation, regulates degradation of cellular proteins by the ubiquitinproteasome system, controlling a proteins half-life and expression levels. This process involves the sequential action of ubiquitin-activating enzymes (E1), ubiquitin-conjugating enzymes (E2), and ubiquitin ligases (E3). The reaction catalyzed by each enzyme transfers a covalent bond with ubiquitin from one enzyme to the next and finally to a target protein. Formation of polyubiquitin chains occurs when the target protein is another ubiquitin molecule already covalently linked to another protein. Mammalian genomes encode approximately 12 E1 enzymes, 30-40 E2 enzymes, and hundreds of E3 enzymes. The diversity of these enzymes also suggests a wide variety of protein targets or functions with different regulatory mechanisms for each one. For example, monoubiquitination of cell surface transmembrane receptors marks them for endocytosis, and polyubiquitin chains act as scaffolds for ...
We approached the problem of E2 specificity with the simple assumption that the unique determinants of specificity for each E2 catalytic domain could be identified by searching for amino acids whose transposition from one E2 to another resulted in a corresponding transposition of function. Such an approach has previously been used to make a single amino acid substitution in NEDD8, making it a substrate for the ubiquitin pathway (56). The ubiquitin-conjugating enzymes UBC4 and RAD6 (UBC2) from S. cerevisiae were employed, as each carries out a distinct, nonoverlapping function and their respective biological properties can be easily measured by determining cell viability in simple plating experiments.. Initially, comparisons of the sequence similarities and differences both within and among the six members of the RAD6 and UBC4 families from S. cerevisiae, Schizosaccharomyces pombe,Drosophila melanogaster, Caenorhabditis elegans,Arabidopsis thaliana, and H. sapiens were carried out (6, 9, 24, 25, ...
Proteins degraded by the ubiquitin-mediated proteolysis must be covalently linked to the small protein ubiquitin. Ubiquitin serves as a molecular tag that marks proteins for degradation by the 26S proteasome. The selection of substrates for ubiquitination is prescribed by a specific class of enzymes called ubiquitin-protein ligases (also known as E3s). Most E3 ligases comprise a large superfamily of protein-protein complexes. They bind the substrate protein and a cognate ubiquitin-conjugating enzyme (E2), and catalyze the transfer of ubiquitin from the E2 to specific lysine residues within the substrate. Thus E3s are responsible for both ubiquitin transfer and specific recognition of each of the target proteins. However, the molecular details underlying these two processes remain poorly understood. ...
Ubiquitin-conjugating enzymes, also known as E2 enzymes and more rarely as ubiquitin-carrier enzymes, perform the second step in the ubiquitination reaction that targets a protein for degradation via the proteasome. The ubiquitination process covalently attaches ubiquitin, a short protein of 76 amino acids, to a lysine residue on the target protein. Once a protein has been tagged with one ubiquitin molecule, additional rounds of ubiquitination form a polyubiquitin chain that is recognized by the proteasomes 19S regulatory particle, triggering the ATP-dependent unfolding of the target protein that allows passage into the proteasomes 20S core particle, where proteases degrade the target into short peptide fragments for recycling by the cell. ...
Epithelial ovarian cancer (EOC) is one of the leading causes of cancer deaths in women worldwide. Ubiquitin-conjugating enzyme 9 (Ubc9), the sole conjugating enzyme for sumoylation, regulates protein function and plays an important role in sumoylation-mediated cellular pathways. Although sumoylation plays a key role in DNA repair and tumorgenesis, whether Ubc9 is involved in EOC progression remains unknown. In the present study, we constructed Ubc-9 expressed recombined plasmid pEGFP-N1-Ubc9. The mRNA levels of Ubc9 were confirmed in human ovarian cell lines before and after transfection with pEGFP-N1-Ubc9 or small interfering RNA (siRNA) targeted Ubc9 by real-time polymerase chain reaction (PCR). The MTT (3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide) assay was used to observe the effect of Ubc9 on cell proliferation. The protein levels of Ubc9, and proliferation-related signals Akt and physphorylated Akt were determined by Western blot. Our results showed that proliferation of EOC
The majority of eukaryotic proteins are degraded by the ubiquitin-proteasome system. In this pathway, cytosolic substrates are first earmarked for degradation by modification with ubiquitin (ubiquitylation) and subsequently degraded by the 26S pro-teasome, a large protease residing in both the cytosol and the nucleus. ER-resident proteins are similarly degraded but take the route of a specialized pathway coined ER-associated degradation (ERAD). In order to reach the cytosolic ubiquitin/proteasome system, these substrates must first relocate from the ER to the cytosol, possibly with the help of protein conducting membrane channels. Previous work has shown that specific ubiquitin-conjugating enzymes (e.g. Ubc6, Ubc7) and ubiquitin ligases (e.g. Hrd1) con-tribute to ERAD, but how the substrates reach the proteasome remained to be clarified. Besides its function as a quality control system in recognizing and eliminating aberrant proteins, ERAD appears also to play a part in regulatory pathways. ...
The eukaryotic ubiquitin-conjugation system sets the turnover rate of many proteins and includes activating enzymes (E1s), conjugating enzymes (UBCs/E2s), and ubiquitin-protein ligases (E3s), which are responsible for activation, covalent attachment and substrate recognition, respectively. There are also ubiquitin-like proteins with distinct functions, which require their own E1s and E2s for attachment. We describe the results of RNA interference (RNAi) experiments on the E1s, UBC/E2s and ubiquitin-like proteins in Caenorhabditis elegans. We also present a phylogenetic analysis of UBCs. The C. elegans genome encodes 20 UBCs and three ubiquitin E2 variant proteins. RNAi shows that only four UBCs are essential for embryogenesis: LET-70 (UBC-2), a functional homolog of yeast Ubc4/5p, UBC-9, an ortholog of yeast Ubc9p, which transfers the ubiquitin-like modifier SUMO, UBC-12, an ortholog of yeast Ubc12p, which transfers the ubiquitin-like modifier Rub1/Nedd8, and UBC-14, an ortholog of Drosophila Courtless.
Read Over-expression of tobacco UBC1 encoding a ubiquitin-conjugating enzyme increases cadmium tolerance by activating the 20S/26S proteasome and by decreasing Cd accumulation and oxidative stress in tobacco (Nicotiana tabacum), Plant Molecular Biology on DeepDyve, the largest online rental service for scholarly research with thousands of academic publications available at your fingertips.
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UBE2D3 overexpression lysate, 0.1 mg. Transient overexpression lysate of ubiquitin-conjugating enzyme E2D 3 (UBC4/5 homolog, yeast) (UBE2D3), transcript variant 1
Ube2j1 - Ube2j1 (GFP-tagged) - Mouse ubiquitin-conjugating enzyme E2, J1 (Ube2j1) available for purchase from OriGene - Your Gene Company.
UBE2D1 antibody (ubiquitin-conjugating enzyme E2D 1 (UBC4/5 homolog, yeast)) for ICC/IF, IHC-P, WB. Anti-UBE2D1 pAb (GTX109257) is tested in Human, Mouse samples. 100% Ab-Assurance.
The protein encoded by this gene contains a RING zinc finger, a motif known to be involved in protein-protein interactions. This protein interacts with androgen receptor (AR) and may function as a coactivator that induces AR target gene expression in prostate. A dominant negative mutant of this gene has been demonstrated to inhibit the AR-mediated growth of prostate cancer. This protein also interacts with class III ubiquitin-conjugating enzymes (E2s) and may act as a ubiquitin-ligase (E3) in the ubiquitination of certain nuclear proteins. Five alternatively spliced transcript variants encoding two distinct isoforms have been reported.[7] ...
The PDB archive contains information about experimentally-determined structures of proteins, nucleic acids, and complex assemblies. As a member of the wwPDB, the RCSB PDB curates and annotates PDB data according to agreed upon standards. The RCSB PDB also provides a variety of tools and resources. Users can perform simple and advanced searches based on annotations relating to sequence, structure and function. These molecules are visualized, downloaded, and analyzed by users who range from students to specialized scientists.
The PDB archive contains information about experimentally-determined structures of proteins, nucleic acids, and complex assemblies. As a member of the wwPDB, the RCSB PDB curates and annotates PDB data according to agreed upon standards. The RCSB PDB also provides a variety of tools and resources. Users can perform simple and advanced searches based on annotations relating to sequence, structure and function. These molecules are visualized, downloaded, and analyzed by users who range from students to specialized scientists.
ARIH1 antibody (ariadne homolog, ubiquitin-conjugating enzyme E2 binding protein, 1 (Drosophila)) for WB. Anti-ARIH1 pAb (GTX23891) is tested in Human, Mouse samples. 100% Ab-Assurance.
ubiquitin carrier protein kinase: a 300 kDa kinase consisting of 3 subunits of MWs 70, 105 & 120; requires Mg2+ but inhibited by high concentration; from HeLa cells
Using an integrative genomics approach called amplification breakpoint ranking and assembly analysis, we nominated KRAS as a gene fusion with the ubiquitin-conjugating enzyme UBE2L3 in the DU145 cell line, originally derived from prostate cancer metastasis to the brain. Interestingly, analysis of tissues revealed that 2 of 62 metastatic prostate cancers harbored aberrations at the KRAS locus. In DU145 cells, UBE2L3-KRAS produces a fusion protein, a specific knockdown of which attenuates cell invasion and xenograft growth. Ectopic expression of the UBE2L3-KRAS fusion protein exhibits transforming activity in NIH 3T3 fibroblasts and RWPE prostate epithelial cells in vitro and in vivo. In NIH 3T3 cells, UBE2L3-KRAS attenuates MEK/ERK signaling, commonly engaged by oncogenic mutant KRAS, and instead signals via AKT and p38 mitogen-activated protein kinase (MAPK) pathways. This is the first report of a gene fusion involving the Ras family, suggesting that this aberration may drive metastatic ...
We identified a protein degradation pathway at the INM in yeast mediated by the Asi complex. The Asi complex functions together with the ubiquitin-conjugating enzymes Ubc6 and Ubc7 to degrade soluble and integral membrane proteins. Genetic evidence suggests that the Asi ubiquitin ligase defines a pathway distinct from, but complementary to, ERAD. Using unbiased screening with a novel genome-wide yeast library based on a tandem fluorescent protein timer, we identify more than 50 substrates of the Asi, Hrd1 and Doa10 E3 ubiquitin ligases. We show that the Asi ubiquitin ligase is involved in degradation of mislocalized integral membrane proteins, thus acting to maintain and safeguard the identity of the INM.. ​. Khmelinskii A, Blaszczak E, Pantazopoulou M, Fischer B, Omnus DJ, Le Dez G, Brossard A, Gunnarsson A, Barry JD, Meurer M, Kirrmaier D, Boone C, Huber W, Rabut G, Ljungdahl PO & Knop M (2014) Protein quality control at the inner nuclear membrane. Nature 516: 410-413 ...
Breast cancer is a common and aggressive cancer among women. Mortality is often caused by metastatic disease, but therapeutic options for treating metastases are limited. Signaling mediated by the transforming growth factor-β (TGF-β) and mitogen-activated protein kinase (MAPK) pathways are commonly associated with metastatic progression, and the abundance of the ubiquitin-conjugating enzyme Ubc13 is increased in metastatic breast cancer. Wu et al. explored the role of Ubc13 and its links with the TGF-β and MAPK pathways in breast cancer. In multiple xenograft or allograft models, knocking down Ubc13 before injection of the cells into the mammary fat pads of mice did not affect primary tumor growth but prevented or reduced the size and number of lung metastases. Bioluminescent imaging of breast cancer cells transfected with an inducible, fluorescent-labeled shRNA lentivirus against Ubc13 mRNA showed that Ubc13 was required for metastatic growth in the lung but not for extravasation or ...
En ubiquitin-conjugating enzym som regulerer cellesyklus fremmer kromosom missegregation og tumordannelse, ifølge van Ree et al. i januar 11 Utgave av Journal of Cell Biology (www.jcb.org)
p53 is a tumor suppressor that is widely mutated or deleted in cancer cells. Mdm2, an E3 ubiquitin ligase, is the master regulator of p53. It targets p53 for proteasomal degradation, restraining the potent activity of p53 and enabling cell survival and proliferation. There are complex regulatory mechanisms balancing the activity and stability of Mdm2 in a cell. Mdm2 has an extremely short half-life in the unstressed cell and its regulation is not well understood. Like most E3 ligases, Mdm2 can autoubiquitinate. Previously, the sole function of autoubiquitination was thought to be to signal Mdm2 degradation. Here I show that autoubiquitination of Mdm2 is an activating event. Mdm2 that has been conjugated with polyubiquitin chains exhibits substantially enhanced activity to polyubiquitinate p53. Mechanistically, autoubiquitination of Mdm2 facilitates the recruitment of the E2 ubiquitin-conjugating enzymes through non-covalent interactions between the ubiquitin chains on Mdm2 and the ubiquitin-binding
634 The ubiquitin-proteasome pathway plays a major role in cancer development and is a bona fide target for cancer therapy. The covalent attachment of ubiquitin to a target protein proceeds through a multi-enzyme cascade. Initially, E1 activates ubiquitin and is then transferred to a cysteine residue of an E2 ubiquitin-conjugating enzyme (ubc). Finally, the E2 itself, or more commonly in concert with an E3 ubiquitin ligase, ligates the ubiquitin via its carboxy terminus to lysine residues of a protein substrate. This enzymatic cascade, responsible for ubiquitylating target proteins is complex, and its regulation is only beginning to be understood. The complexity stems from the large number of E2 and E3 enzymes; in humans, more than 30 E2s and hundreds of putative E3 ligases have been identified. The enzymatic nature, multitude of E2 and E3s and their specific substrate recognition predestines them as therapeutic targets in major diseases.. Targeting components of ubiquitination pathway for drug ...
Ubiquitin carrier proteins (E2s) are involved in the covalent attachment of ubiquitin to a variety of cellular target proteins in eukaryotes. Here, we report the cloning of genes from wheat and Arabidopsis thaliana that encode 16-kDa E2s and a domain analysis of E2s by in vitro mutagenesis. The genes for E216kDa, which we have designated wheat and At UBC1, encode proteins that are only 33% identical (58% similar) with a 23-kDa E2 from wheat (encoded by the gene now designated wheat UBC4), but are 63% identical (82% similar) with the E2 encoded by the Saccharomyces cerevisiae DNA repair gene, RAD6. Unlike the proteins encoded by RAD6 and wheat UBC4, the UBC1 gene products lack acidic C-terminal domains extending beyond the conserved core of the proteins and are incapable of efficient in vitro ligation of ubiquitin to histones. From enzymatic analysis of the UBC1 and UBC4 gene products mutagenized in vitro, we have identified several domains important for E2 function, including the active site ...
One effective way to study the biological function of a protein in vivo is to inactivate it and see what happens to the cell. For proteins that are dispensable for cell viability, the corresponding gene can simply be deleted from its chromosomal locus. The study of essential proteins is more challenging, however, because the function of the protein must be inactivated conditionally. Here, we describe a method that allows the target protein to be depleted rapidly and conditionally, so that the immediate effects on the cell can be examined. The chromosomal locus of a budding yeast gene is modified so that a heat-inducible degron cassette is added to the N terminus of the encoded protein, causing it to be degraded by a specific ubiquitin-mediated pathway when cells are shifted from 24° to 37°C. Degradation requires recognition of the degron cassette by the evolutionarily conserved Ubr1 protein, which is associated with a ubiquitin-conjugating enzyme. To promote rapid and conditional depletion ...
A systematic computational analysis of protein sequences containing known nuclear domains led to the identification of 28 novel domain families. This represents a 26% increase in the starting set of 107 known nuclear domain families used for the analysis. Most of the novel domains are present in all major eukaryotic lineages, but 3 are species specific. For about 500 of the 1200 proteins that contain these new domains, nuclear localization could be inferred, and for 700, additional features could be predicted. For example, we identified a new domain, likely to have a role downstream of the unfolded protein response; a nematode-specific signalling domain; and a widespread domain, likely to be a noncatalytic homolog of ubiquitin-conjugating enzymes. ...
What I dont understand is the syslinux/isolinux/grub4dos setup. Being that my original intentions was to understand the bootloader concept with ISO/CDs, it really bugs me. I could just drop in custom configurations as per the manual and never think of /what/ Im actually doing (ok, yeah I get that too, dropping the iso and modifying the bootloader(s) cfg..) but what Im confused about is WHY is there two bootloaders, that are actually select-able from the first bootloader (which I believe is the sys/isolinux bootloader ...
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Ubiquitin-editing enzyme that contains both ubiquitin ligase and deubiquitinase activities. Involved in immune and inflammatory responses signaled by cytokines, such as TNF-alpha and IL-1 beta, or pathogens via Toll-like receptors (TLRs) through terminating NF-kappa-B activity. Essential component of a ubiquitin-editing protein complex, comprising also RNF11, ITCH and TAX1BP1, that ensures the transient nature of inflammatory signaling pathways. In cooperation with TAX1BP1 promotes disassembly of E2-E3 ubiquitin protein ligase complexes in IL-1R and TNFR-1 pathways; affected are at least E3 ligases TRAF6, TRAF2 and BIRC2, and E2 ubiquitin-conjugating enzymes UBE2N and UBE2D3. In cooperation with TAX1BP1 promotes ubiquitination of UBE2N and proteasomal degradation of UBE2N and UBE2D3. Upon TNF stimulation, deubiquitinates Lys-63-polyubiquitin chains on RIPK1 and catalyzes the formation of Lys-48-polyubiquitin chains. This leads to RIPK1 proteasomal degradation and consequently termination of ...
Lentiviral Nef increases T cell signaling activity, but the molecular nature of the stimulus involved is incompletely described. We explored CD4 T cell lipid raft composition in the presence and absence of Nef. Here, the E2 ubiquitin-conjugating enzyme UbcH7, which acts in conjunction with c-Cbl, is absent from lipid rafts. This Nef-mediated exclusion is associated with failure of ubiquitination of activated Vav. In the presence of Nef, lipid raft Cdc42 is activated and forms a ternary complex between the c-Cbl-interacting protein p85Cool-1/betaPix and c-Cbl, displacing UbcH7 from rafts. Suppression of p85Cool-1/betaPix expression restores UbcH7 raft localization and Vav ubiquitination and diminishes Cdc42 activity. Moreover, p85Cool-1/betaPix knockdown attenuates HIV replication. Thresholds for activation of signaling involve the intricate balance of positive and negative regulators. Here we provide evidence for Nef disruption of a negative regulator of T cell signaling in promoting HIV replication.
UBE2J1 Full-Length MS Protein Standard (NP_057105), Labeled with [U- 13C6, 15N4]-L-Arginine and [U- 13C6, 15N2]-L-Lysine, was produced in human 293 cells (HEK293) with fully chemically defined cell culture medium to obtain incorporation efficiency at Creative-Proteomics. The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes, or E1s, ubiquitin-conjugating enzymes, or E2s, and ubiquitin-protein ligases, or E3s. This gene encodes a member of the E2 ubiquitin-conjugating enzyme family. This enzyme is located in the membrane of the endoplasmic reticulum (ER) and may contribute to quality control ER-associated degradation by the ubiquitin-proteasome system.
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Gentaur molecular products has all kinds of products like :search , Cell Sciences \ Recombinant Human UBC9 \ CSI12725 for more molecular products just contact us
Lenalidomide promotes p53 degradation by inhibiting MDM2 auto-ubiquitination in myelodysplastic syndrome with chromosome 5q deletion. Oncogene. 2013 Feb 28; 32(9):1110-20 ...
The S73/S97/loop motif is a hallmark of the Cdc34 family of E2 ubiquitin-conjugating enzymes that together with the SCF E3 ubiquitin ligases promote degradation of proteins involved in cell cycle and growth regulation. The inability of the loop-less Δ12Cdc34 mutant to support growth was linked to its inability to catalyze polyubiquitination. However, the loop-less t riple m utant (tm) Cdc34, which not only lacks the loop but also contains the S73K and S97D substitutions typical of the K73/D97/no loop motif present in other E2s, supports growth. Whether tmCdc34 supports growth despite defective polyubiquitination, or the S73K and S97D substitutions, directly or indirectly, correct the defect caused by the loop absence, are unknown. tmCdc34 supports yeast viability with normal cell size and cell cycle profile despite producing fewer polyubiquitin conjugates in vivo and in vitro. The in vitro defect in Sic1 substrate polyubiquitination is similar to the defect observed in reactions with Δ12Cdc34 that
TY - JOUR. T1 - Regulation of WASH-dependent actin polymerization and protein trafficking by ubiquitination. AU - Hao, Yi Heng. AU - Doyle, Jennifer M.. AU - Ramanathan, Saumya. AU - Gomez, Timothy S.. AU - Jia, Da. AU - Xu, Ming. AU - Chen, Zhijian J.. AU - Billadeau, Daniel D.. AU - Rosen, Michael K.. AU - Potts, Patrick Ryan. PY - 2013/2/28. Y1 - 2013/2/28. N2 - Endosomal protein trafficking is an essential cellular process that is deregulated in several diseases and targeted by pathogens. Here, we describe a role for ubiquitination in this process. We find that the E3 RING ubiquitin ligase, MAGE-L2-TRIM27, localizes to endosomes through interactions with the retromer complex. Knockdown of MAGE-L2-TRIM27 or the Ube2O E2 ubiquitin-conjugating enzyme significantly impaired retromer-mediated transport. We further demonstrate that MAGE-L2-TRIM27 ubiquitin ligase activity is required for nucleation of endosomal F-actin by the WASH regulatory complex, a known regulator of retromer-mediated ...
The enzymes of the ubiquitylation pathway play a pivotal role in a number of cellular processes including regulated and targeted proteasomal degradation of substrate proteins. Three classes of enzymes are involved in the process of ubiquitylation; activating enzymes (E1s), conjugating enzymes (E2s) and protein ligases (E3s). UBE2V2 is a member of the E2 conjugating enzyme family and cloning of the human gene was first described by Fritsche et al. (1997). UBE2V2 shares 90% sequence identity with UBE2V1 in its C-terminal domain (Sancho et al., 1998). The UEV protein Mms2 (yeast homologue of human UBE2V2) forms a heterodimer with yeast Ubc13 (UBE2N) which is recruited to chromatin by the RING finger proteins RAD5 and RAD18 in the RAD6 dependent post-replicative DNA repair pathway (Hofmann and Pickart 1999). These proteins also play a central role in the assembly of K63-linked polyubiquitin chains (Ulrich and Jentsch 2000; Xiao et al., 1998). UEV/Ubc complexes have been implicated in the assembly of ...
Our early work defined structures initiating UBL conjugation, including how E1s recognize specific UBLs and promote conjugation to a cognate E2 (Walden et al. Nature 2003, Walden et al. Molecular Cell 2003, Huang et al. Nature SMB 2004, Huang et al. Molecular Cell 2005, Huang et al. Nature 2007, Huang et al. Molecular Cell 2009, Taherbhoy et al. Molecular Cell 2011, Kaiser et al. Nature SMB 2012). However, despite great importance, our knowledge of substrate modification and polyubiquitylation by E3 enzymes remains rudimentary. Thus, one focus of the department is to visualize E3 ligases trapped as if in the act of handing UB off to its recipient (Kamadurai et al. Molecular Cell 2009, Kamadurai et al. eLife 2013, Scott et al. Cell 2014, Brown et al. PNAS 2015, Brown et al. Cell 2016).. We are also studying how ubiquitylation is controlled in space and in time. We have already uncovered numerous mechanisms by which different E3 ligases are restrained until they are needed, as well as how these ...
Standard Operating Procedures (SOPs) provide a detailed description of commonly used procedures. SOPs offer investigators an alternative to writing detailed procedures in their animal use protocol (AUP). Any deviation from the approved procedures must be clearly described and justified in the AUP. Approval of the AUP indicates approval of the deviation from the SOP for that AUP only.. These SOPs were created and/or revised by the SOP committee and approved by the University Animal Care Committee (UACC). There is no need to attach SOPs to your AUP in Topaz - you may simply refer to the appropriate SOP number and title in the relevant procedural description within the AUP.. Rat and Mouse SOPs are listed below. Please follow the link to the Queens UACC approved SOPs for additional species. Access requires registration through the Training Coordinator.. SOP development and revision is an ongoing process. Please ensure that you read all SOPs thoroughly prior to referencing them in any of your ...
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Plasmid EF.hICN1.Ubc.GFP from Dr. Linzhao Chengs lab contains the insert ICN1 and is published in Stem Cells. 2006 Apr . 24(4):876-88. This plasmid is available through Addgene.
Ube2L6 overexpression裂解液裂解液datasheet (ab94307).Abcam抗体、ELISA、激动剂拮抗剂、表观遗传试剂、蛋白多肽,使用效果保证,中国70%以上现货。
Ubiquitin-conjugating enzyme E2 O is a protein that in humans is encoded by the UBE2O gene. UBE2O functions during terminal ... "Entrez Gene: UBE2O ubiquitin-conjugating enzyme E2O". Nguyen AT, Prado MA, et al. (2017). "UBE2O remodels the proteome during ... and chromosomal position of a novel gene encoding human ubiquitin-conjugating enzyme E2-230k". Gene. 267 (1): 95-100. doi: ...
Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes, or E1s, ubiquitin-conjugating enzymes ... This gene encodes a member of the E2 ubiquitin-conjugating enzyme family and catalyzes the covalent attachment of ubiquitin to ... Ubiquitin-conjugating enzyme E2 G1 is a protein that in humans is encoded by the UBE2G1 gene. The modification of proteins with ... "Entrez Gene: UBE2G1 ubiquitin-conjugating enzyme E2G 1 (UBC7 homolog, yeast)". Chen P, Johnson P, Sommer T, et al. (1993). " ...
Ubiquitin-conjugating enzyme E2 R2 is a protein that in humans is encoded by the UBE2R2 gene. Protein kinase CK2 is a ... "Entrez Gene: UBE2R2 ubiquitin-conjugating enzyme E2R 2". Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to ... This gene encodes a protein similar to the E2 ubiquitin conjugating enzyme UBC3/CDC34. Studies suggest that CK2-dependent ... Semplici F, Meggio F, Pinna LA, Oliviero S (May 2002). "CK2-dependent phosphorylation of the E2 ubiquitin conjugating enzyme ...
1999). "RING fingers mediate ubiquitin-conjugating enzyme (E2)-dependent ubiquitination". Proc. Natl. Acad. Sci. U.S.A. 96 (20 ... This protein is located in the endoplasmic reticulum, and has been shown to possess ubiquitin ligase activity. This gene was ...
"An altered-specificity ubiquitin-conjugating enzyme/ubiquitin-protein ligase pair". Journal of Molecular Biology. 337 (1): 157- ... The encoded protein interacts with CNOT1 and has ubiquitin ligase activity. Several transcript variants encoding different ... "Identification of a ubiquitin-protein ligase subunit within the CCR4-NOT transcription repressor complex". The EMBO Journal. 21 ...
UBC9 is a ubiquitin conjugating enzyme whose proteins associates with MITF. Although hUBC9 is known to act preferentially with ... of microphthalmia-associated transcription factor MITF protein levels by association with the ubiquitin-conjugating enzyme ... The enzyme is 17 kDa large and can freely diffuse between the nucleus and cytosol explaining its presence in the nucleus. It ... The regulatory mechanism relies on the enzyme diadenosine tetraphosphate hydrolase, a member of the Nudix type 2 enzymatic ...
Ubiquitin-conjugating enzymes and ubiquitin ligases regulate the ubiquitination of histone H2B. These enzymes use co- ... All ubiquitin moieties are removed from histone H2B during metaphase and re-conjugated during anaphase. Histone H2B's amino ... transcription to conjugate ubiquitin to histone H2B. Histone H2B's level of ubiquitination varies throughout the cell cycle. ... Ubiquitin residues are usually added to the lysine at position 120 on histone H2B. Ubiquitinating this lysine residue activates ...
"Characterization of functionally independent domains in the human ubiquitin conjugating enzyme UbcH2". FEBS Letters. 377 (2): ...
Block, K; Boyer T G; Yew P R (November 2001). "Phosphorylation of the human ubiquitin-conjugating enzyme, CDC34, by casein ... The enzyme is a tetramer of 2 alpha- and 2 beta-subunits. However, some species (e.g., mammals) possess 2 related forms of the ... The enzyme localizes to the endoplasmic reticulum and the Golgi apparatus. Casein kinase, a ubiquitous, well-conserved protein ... Enzyme Regul. 34: 225-46. doi:10.1016/0065-2571(94)90018-3. PMID 7942276. el Benna J, Faust LP, Babior BM (1994). "The ...
Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes, or E1s, ubiquitin-conjugating enzymes ... This gene encodes a member of the E2 ubiquitin-conjugating enzyme family. This enzyme is required for post-replicative DNA ... Ubiquitin-conjugating enzyme E2 A is a protein that in humans is encoded by the UBE2A gene. The modification of proteins with ... "Entrez Gene: UBE2A ubiquitin-conjugating enzyme E2A (RAD6 homolog)". Xin, H; Lin W; Sumanasekera W; Zhang Y; Wu X; Wang Z (July ...
Ubiquitin-conjugating enzyme E2 variant 1 is a protein that in humans is encoded by the UBE2V1 gene. Ubiquitin-conjugating E2 ... "Substrate modification with lysine 63-linked ubiquitin chains through the UBC13-UEV1A ubiquitin-conjugating enzyme". J. Biol. ... "Entrez Gene: UBE2V1 ubiquitin-conjugating enzyme E2 variant 1". Deng L, Wang C, Spencer E, Yang L, Braun A, You J, Slaughter C ... They have sequence similarity to other ubiquitin-conjugating enzymes but lack the conserved cysteine residue that is critical ...
The mouse protein also binds ubiquitin-conjugating enzymes (E2s) and is a substrate for E2-dependent ubiquitination. RNF25 has ... Lorick KL, Jensen JP, Fang S, Ong AM, Hatakeyama S, Weissman AM (1999). "RING fingers mediate ubiquitin-conjugating enzyme (E2 ... E3 ubiquitin-protein ligase RNF25 is an enzyme that in humans is encoded by the RNF25 gene. The protein encoded by this gene ...
Lorick KL, Jensen JP, Fang S, Ong AM, Hatakeyama S, Weissman AM (1999). "RING fingers mediate ubiquitin-conjugating enzyme (E2 ... Joazeiro CA, Weissman AM (2000). "RING finger proteins: mediators of ubiquitin ligase activity". Cell. 102 (5): 549-52. doi: ... Many RING finger domains simultaneously bind ubiquitination enzymes and their substrates and hence function as ligases. ...
Cdc4 protein interacts with Cdc34, an ubiquitin-conjugating enzyme, and Cdc53 in vivo. (There is a Cdc4p/Cdc53p-binding region ... ubiquitin ligase ubiquitin proteasome system cell cycle Simchen G, Hirschberg J (May 1977). "Effects of the mitotic cell-cycle ... which acts as a mediator of ubiquitin transfer to target proteins, leading to their subsequent degradation via the ubiquitin- ... Cdc4 (cell division control protein 4) is a substrate recognition component of the SCF (SKP1-CUL1-F-box protein) ubiquitin ...
"Modulation of TEL transcription activity by interaction with the ubiquitin-conjugating enzyme UBC9". Proceedings of the ... enzyme genes TTL (adds and removes tyrosine residues on α-tubulin), GOT1 (an Aspartate transaminase), and ACSL6 (a Long-chain- ...
Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes, or E1s, ubiquitin-conjugating enzymes ... Plafker SM, Plafker KS, Weissman AM, Macara IG (2005). "Ubiquitin charging of human class III ubiquitin-conjugating enzymes ... or E2s, and ubiquitin-protein ligases, or E3s. This gene encodes a member of the E2 ubiquitin-conjugating enzyme family. The ... Ubiquitin-conjugating enzyme E2 E3 is a protein that in humans is encoded by the UBE2E3 gene. The modification of proteins with ...
... with the ubiquitin-conjugating enzyme hUBC9. Implication of the ubiquitin/proteasome pathway in regulation of ATF2 in T cells ...
Plafker SM, Plafker KS, Weissman AM, Macara IG (2005). "Ubiquitin charging of human class III ubiquitin-conjugating enzymes ... Ubiquitin-conjugating enzyme E2 E2 is a protein that in humans is encoded by the UBE2E2 gene. GRCh38: Ensembl release 89: ... "Entrez Gene: UBE2E2 ubiquitin-conjugating enzyme E2E 2 (UBC4/5 homolog, yeast)". Auffray C, Behar G, Bois F, et al. (1995). "[ ... 1999). "The ubiquitin-conjugating enzymes UbcH7 and UbcH8 interact with RING finger/IBR motif-containing domains of HHARI and ...
The enzyme specifically cleaves ubiquitin from ubiquitin-conjugated protein substrates. The protein is found in the nucleus and ... Ubiquitin specific peptidase 10, also known as USP10, is an enzyme which in humans is encoded by the USP10 gene. Ubiquitin is a ... "Entrez Gene: USP10 ubiquitin specific peptidase 10". Soncini C, Berdo I, Draetta G (June 2001). "Ras-GAP SH3 domain binding ... Faus H, Meyer HA, Huber M, Bahr I, Haendler B (2006). "The ubiquitin-specific protease USP10 modulates androgen receptor ...
Ubiquitin-conjugating enzyme E2 variant 1, also known as Kua-UEV, is a human gene. The Kua-UEV mRNA is an infrequent but ... Ubiquitin-conjugating E2 enzyme variant proteins constitute a distinct subfamily within the E2 protein family. They have ... "Entrez Gene: Kua-UEV ubiquitin-conjugating enzyme E2 variant 1". Thomson TM, Lozano JJ, Loukili N, Carrió R, Serras F, Cormand ... January 1998). "Role of UEV-1, an inactive variant of the E2 ubiquitin-conjugating enzymes, in in vitro differentiation and ...
Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes, or E1s, ubiquitin-conjugating enzymes ... or E2s, and ubiquitin-protein ligases, or E3s. This gene encodes a member of the E2 ubiquitin-conjugating enzyme family. ... Ubiquitin-conjugating enzyme E2 N is a protein that in humans is encoded by the UBE2N gene. The modification of proteins with ... "Entrez Gene: UBE2N ubiquitin-conjugating enzyme E2N (UBC13 homolog, yeast)". Ewart-Toland A, Briassouli P, de Koning JP, Mao JH ...
Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes, or E1s, ubiquitin-conjugating enzymes ... This gene encodes a member of the E2 ubiquitin-conjugating enzyme family. The encoded protein is linked with a ubiquitin-like ... "Entrez Gene: UBE2M ubiquitin-conjugating enzyme E2M (UBC12 homolog, yeast)". Gong L, Yeh ET (Apr 1999). "Identification of the ... NEDD8-conjugating enzyme Ubc12 is a protein that in humans is encoded by the UBE2M gene. The modification of proteins with ...
1999). "RING fingers mediate ubiquitin-conjugating enzyme (E2)-dependent ubiquitination". Proc. Natl. Acad. Sci. U.S.A. 96 (20 ...
Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes, or E1s, ubiquitin-conjugating enzymes ... This gene encodes a member of the E2 ubiquitin-conjugating enzyme family. This enzyme is located in the membrane of the ... Ubiquitin-conjugating enzyme E2 J1 is a protein that in humans is encoded by the UBE2J1 gene. The modification of proteins with ... "Entrez Gene: UBE2J1 ubiquitin-conjugating enzyme E2, J1 (UBC6 homolog, yeast)". Maruyama K, Sugano S (1994). "Oligo-capping: a ...
May contribute to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. This protein is a part ... 1998). "Association of human CUL-1 and ubiquitin-conjugating enzyme CDC34 with the F-box protein p45(SKP2): evidence for ... 1999). "Recruitment of a ROC1-CUL1 ubiquitin ligase by Skp1 and HOS to catalyze the ubiquitination of I kappa B alpha". Mol. ... This is an essential component of the SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complex, which mediates the ...
"Huntingtin is ubiquitinated and interacts with a specific ubiquitin-conjugating enzyme". The Journal of Biological Chemistry. ... Enzymes in the cell often cut this elongated protein into fragments. The protein fragments form abnormal clumps, known as ...
Ubiquitin-conjugating enzyme E2 K is a protein that in humans is encoded by the UBE2K gene. The protein encoded by this gene ... de Pril R, Fischer DF, Roos RA, van Leeuwen FW (2007). "Ubiquitin-conjugating enzyme E2-25K increases aggregate formation and ... "Induction of ubiquitin-conjugating enzyme by aggregated low density lipoprotein in human macrophages and its implications for ... a human ubiquitin-conjugating enzyme". FEBS Lett. 503 (1): 61-4. doi:10.1016/S0014-5793(01)02689-8. PMID 11513855. S2CID ...
This protein is a member of the ubiquitin-conjugating enzyme family, which catalyzes the covalent attachment of ubiquitin to ... Pati D, Meistrich ML, Plon SE (July 1999). "Human Cdc34 and Rad6B ubiquitin-conjugating enzymes target repressors of cyclic AMP ... Block K, Boyer TG, Yew PR (November 2001). "Phosphorylation of the human ubiquitin-conjugating enzyme, CDC34, by casein kinase ... Semplici F, Meggio F, Pinna LA, Oliviero S (June 2002). "CK2-dependent phosphorylation of the E2 ubiquitin conjugating enzyme ...
Sarcevic B, Mawson A, Baker RT, Sutherland RL (April 2002). "Regulation of the ubiquitin-conjugating enzyme hHR6A by CDK- ... The same enzyme that phosphorylates the CTD also phosphorylates the Rad6 complex, which in turn adds a ubiquitin mark to H2B ... Enzymes called peptidylarginine deiminases (PADs) hydrolyze the imine group of arginines and attach a keto group, so that there ... Histones are subject to post translational modification by enzymes primarily on their N-terminal tails, but also in their ...
The RING protein appears to function as a docking site for ubiquitin-conjugating enzymes (E2s). Other proteins contain a cullin ... Nedd8/Rub1 is a small ubiquitin-like protein, which was originally found to be conjugated to Cdc53, a cullin component of the ... Cullin-RING ubiquitin ligases (CRLs), such as Cul1 (SCF) play an essential role in targeting proteins for ubiquitin-mediated ... They combine with RING proteins to form Cullin-RING ubiquitin ligases (CRLs) that are highly diverse and play a role in myriad ...
"Mammalian ubiquitin-conjugating enzyme Ubc9 interacts with Rad51 recombination protein and localizes in synaptonemal complexes" ... The enzyme encoded by this gene is a member of the RAD51 protein family which assists in repair of DNA double strand breaks. ...
"Regulation of the ubiquitin-conjugating enzyme hHR6A by CDK-mediated phosphorylation". The EMBO Journal. 21 (8): 2009-18. doi: ... The same enzyme that phosphorylates the CTD also phosphorylates the Rad6 complex,[58][59] which in turn adds a ubiquitin mark ... Enzymes called peptidylarginine deiminases (PADs) hydrolyze the imine group of arginines and attach a keto group, so that there ... Histones are subject to post translational modification by enzymes primarily on their N-terminal tails, but also in their ...
Lesche R, Peetz A, van der Hoeven F, Rüther U (1998). "Ft1, a novel gene related to ubiquitin-conjugating enzymes, is deleted ... ubiquitin-like protein transferase activity. • ‏GO:0001948 ربط بروتيني. • ubiquitin protein ligase binding. • ‏GO:1904264، ‏GO: ...
... ubiquitin-conjugating enzyme (E2). In the last step, a member of a highly diverse class of enzymes known as ubiquitin ligases ( ... In the first step, a ubiquitin-activating enzyme (known as E1) hydrolyzes ATP and adenylylates a ubiquitin molecule. This is ... The tagging reaction is catalyzed by enzymes called ubiquitin ligases. Once a protein is tagged with a single ubiquitin ... Haas AL, Warms JV, Hershko A, Rose IA (March 1982). "Ubiquitin-activating enzyme. Mechanism and role in protein-ubiquitin ...
The resulting conjugate protein then binds Atg16L1 to form an E3-like complex which functions as part of the second ubiquitin- ... There are four pathways of autophagy and these are mediated by the autophagy-related genes and their associated enzymes.[6][7][ ... The first of the two ubiquitin-like conjugation systems involved in autophagy covalently binds the ubiquitin-like protein Atg12 ... T. Hanada, N. N. Noda, Y. Satomi, Y. Ichimura, Y. Fujioka, T. Takao, F. Inagaki, and Y. Ohsumi, 'The Atg12-Atg5 Conjugate Has a ...
The resulting conjugate protein then binds Atg16L1 to form an E3-like complex which functions as part of the second ubiquitin- ... The degradation of betaine homo-cysteine methyltransferase (BHMT), a metabolic enzyme, could be used to assess autophagy flux ... The first of the two ubiquitin-like conjugation systems involved in autophagy covalently binds the ubiquitin-like protein Atg12 ... T. Hanada, N. N. Noda, Y. Satomi, Y. Ichimura, Y. Fujioka, T. Takao, F. Inagaki, and Y. Ohsumi, 'The Atg12-Atg5 Conjugate Has a ...
Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes, or E1s, ubiquitin-conjugating enzymes ... This enzyme contains an E2 binding domain, which resembles ubiquitin, and recruits the catalytic core of the E2 enzyme UBE2M ( ... NEDD8 activating enzyme activity. • ubiquitin-like modifier activating enzyme activity. • ATP binding. • identical protein ... This gene encodes a member of the E1 ubiquitin-activating enzyme family. The encoded enzyme associates with AppBp1, an amyloid ...
Ubiquitin-conjugating enzymes, also known as E2 enzymes and more rarely as ubiquitin-carrier enzymes, perform the second step ... Ubiquitin-Conjugating+Enzymes at the US National Library of Medicine Medical Subject Headings (MeSH) ... A ubiquitin-activating enzyme, or E1, first activates the ubiquitin by covalently attaching the molecule to its active site ... Once conjugated to ubiquitin, the E2 molecule binds one of several ubiquitin ligases or E3s via a structurally conserved ...
ATG12 is conjugated to ATG5 in a ubiquitin-like reaction that requires ATG7 and ATG10. The Atg12-Atg5 conjugate then interacts ... See also related articles in The Plant Cell Online Ito J, Fukuda H (2002). "ZEN1 Is a Key Enzyme in the Degradation of Nuclear ... LC3/ATG8 is cleaved at its C terminus by ATG4 protease to generate the cytosolic LC3-I. LC3-I is conjugated to ... phosphatidylethanolamine (PE) also in a ubiquitin-like reaction that requires Atg7 and Atg3. The lipidated form of LC3, known ...
E2 Ubiquitin-conjugating enzyme *A. *B. *C. *D1. *D2. *D3. *E1. *E2 ... Interaction with CHIP (Carboxyl-terminus of Hsp70 Interacting Protein)-an E3 ubiquitin ligase-allows Hsp70 to pass proteins to ... Lüders J, Demand J, Höhfeld J (February 2000). "The ubiquitin-related BAG-1 provides a link between the molecular chaperones ...
The nucleophilic sulfhydryl group allows cysteine to conjugate to other groups, e.g., in prenylation. Ubiquitin ligases ... The enzyme cystathionine gamma-lyase converts the cystathionine into cysteine and alpha-ketobutyrate. In plants and bacteria, ... The enzyme O-acetylserine (thiol)-lyase, using sulfide sources, converts this ester into cysteine, releasing acetate.[12] ... Beyond the iron-sulfur proteins, many other metal cofactors in enzymes are bound to the thiolate substituent of cysteinyl ...
Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes, or E1s, ubiquitin-conjugating enzymes ... ubiquitin conjugating enzyme activity. Cellular component. • cytosol. • ubiquitin ligase complex. • nucleoplasm. • protein ... This gene encodes a member of the E2 ubiquitin-conjugating enzyme family. This enzyme functions in the ubiquitination of the ... Ubiquitin-conjugating enzyme E2 D2 is a protein that in humans is encoded by the UBE2D2 gene.[5][6] ...
The resulting activated ubiquitin is then passed to E2, which is a ubiquitin-conjugating enzyme. Another group of enzymes, more ... The first of these reactions takes place when the ubiquitin-activating enzyme E1 hydrolyses ATP and forms a high-energy ... Ubiquitin is cleaved before terminal digestion by deubiquitinating enzymes. This third step is very closely associated with the ... anchored membrane protein Ubc6 as well as Ubc1 and the Cue1 dependent membrane bound Ubc7 are the ubiquitin conjugating enzymes ...
The active site is usually a groove or pocket of the enzyme which can be located in a deep tunnel within the enzyme,[3] or ... Amino acids at the binding site of ubiquitin generally follow the induced fit model, whereas the rest of the protein generally ... It contains a distinct conjugated isoalloxazine ring system. Flavin has multiple redox states and can be used in processes that ... Examples of enzyme catalysis mechanismsEdit. In reality, most enzyme mechanisms involve a combination of several different ...
Ubiquitin. *E1: X-linked spinal muscular atrophy 2. *E3: Johanson-Blizzard syndrome ... Deubiquitinating enzyme: Machado-Joseph disease. *Aneurysmal bone cyst. *Multiple familial trichoepithelioma 1 ... Conjugate gaze palsy. *Convergence insufficiency. *Internuclear ophthalmoplegia. *One and a half syndrome ...
ubiquitin conjugating enzyme binding. • transferase activity. Cellular component. • cytoplasm. • ubiquitin ligase complex. • ... This protein also interacts with class III ubiquitin-conjugating enzymes (E2s) and may act as a ubiquitin-ligase (E3) in the ... E3 ubiquitin-protein ligase RNF14 is an enzyme that in humans is encoded by the RNF14 gene.[5][6][7] ... "N-Terminally extended human ubiquitin-conjugating enzymes (E2s) mediate the ubiquitination of RING-finger proteins, ARA54 and ...
Hershko, A., Leshinsky, E., Ganoth, D. and Heller, H. (1984) ATP-dependent degradation of ubiquitin-protein conjugates. Proc. ... Ciechanover, A., Elias, S., Heller, H. and Hershko, A. (1982) Covalent affinity purification of ubiquitin-activating enzyme. J ... A multicomponent system that degrades proteins conjugated to ubiquitin. Resolution of components and evidence for ATP-dependent ... Hershko, A., Heller, H., Eytan, E. and Reiss, Y. (1986) The protein substrate binding site of the ubiquitin-protein ligase ...
enzyme binding. • metal ion binding. • identical protein binding. • ubiquitin protein ligase binding. • p53 binding. • SUMO ... ubiquitin binding. Cellular component. • cytosol. • endocytic vesicle membrane. • plasma membrane. • synapse. • nuclear body. • ... Mouse double minute 2 homolog (MDM2) also known as E3 ubiquitin-protein ligase Mdm2 is a protein that in humans is encoded by ... ubiquitin-protein transferase activity. • transferase activity. • ligase activity. • 5S rRNA binding. • zinc ion binding. • ...
E2 Ubiquitin-conjugating enzyme *A. *B. *C. *D1. *D2. *D3. *E1. *E2 ... Raboy B, Sharon G, Parag HA, Shochat Y, Kulka RG (1991). "Effect of stress on protein degradation: role of the ubiquitin system ... The small 8-kilodalton protein ubiquitin, which marks proteins for degradation, also has features of a heat shock protein.[8] A ...
UBC9 is a ubiquitin conjugating enzyme whose proteins associates with MITF. Although hUBC9 is known to act preferentially with ... of microphthalmia-associated transcription factor MITF protein levels by association with the ubiquitin-conjugating enzyme ...
Deshaies discovered a biochemical function for the ubiquitin-conjugated enzyme CDC34, which he showed mediates conjugation of ... Petroski, M.D. and Deshaies, R.J. (2005). Mechanism of lysine 48-linked ubiquitin-chain synthesis by the cullin-RING ubiquitin- ... 250 enzymes known as cullin-RING ubiquitin ligases (CRLs) that are conserved throughout eukaryotes and exert a major impact on ... CSN plays a key role in regulating SCF and other CRL enzymes by removing the ubiquitin-like protein NEDD8 from their cullin ...
"Structures of the cIAP2 RING domain reveal conformational changes associated with ubiquitin-conjugating enzyme (E2) recruitment ... 2000). "The inhibitor of apoptosis, cIAP2, functions as a ubiquitin-protein ligase and promotes in vitro monoubiquitination of ...
ubiquitin conjugating enzyme binding. • zinc ion binding. Cydrannau o'r gell. • cytoplasm. • ubiquitin ligase complex. • ... Cul2-RING ubiquitin ligase complex. • Cul3-RING ubiquitin ligase complex. • Cul4A-RING E3 ubiquitin ligase complex. • Lewy body ... ubiquitin protein ligase activity. • ubiquitin protein ligase binding. • ubiquitin-protein transferase activity. • transferase ... positive regulation of proteasomal ubiquitin-dependent protein catabolic process. • protein ubiquitination. • ubiquitin- ...
E2 Ubiquitin-conjugating enzyme *A. *B. *C. *D1. *D2. *D3. *E1. *E2 ... Mitochondrial import inner membrane translocase subunit TIM14 is an enzyme that in humans is encoded by the DNAJC19 gene on ...
Succinate is generated from succinyl-CoA by the enzyme succinyl-CoA synthetase in a GTP/ATP-producing step:[22]:Section 17.1 ... succinic acid readily ionizes to form its conjugate base, succinate (/ˈsʌksɪneɪt/). As a diprotic acid, succinic acid undergoes ... thus marking it for proteolytic destruction by the ubiquitin/proteasome pathway. Since PDHs have an absolute requirement for ... Catalyzed by the enzyme succinate dehydrogenase (SDH), succinate is subsequently oxidized to fumarate:[22]:Section 17.1 ...
"The ubiquitin-conjugating enzymes UbcH7 and UbcH8 interact with RING finger/IBR motif-containing domains of HHARI and H7-AP1". ...
... a cable television company in Thailand Ubiquitin C, a human gene Ubiquitin-conjugating enzyme Ultra Bright Colour, a mobile ...
... performed by ubiquitin-activating enzymes (E1); conjugation, performed by ubiquitin-conjugating enzymes (E2); and ligation, ... Schulman BA, Harper JW (May 2009). "Ubiquitin-like protein activation by E1 enzymes: the apex for downstream signalling ... 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-conjugating enzymes, also known as E2 enzymes and more rarely as ubiquitin-carrier enzymes, perform the second step ... Ubiquitin-Conjugating+Enzymes at the US National Library of Medicine Medical Subject Headings (MeSH) ... A ubiquitin-activating enzyme, or E1, first activates the ubiquitin by covalently attaching the molecule to its active site ... Once conjugated to ubiquitin, the E2 molecule binds one of several ubiquitin ligases or E3s via a structurally conserved ...
InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool.
Ubiquitin conjugating enzyme E2 Q2 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 ...
A ubiquitin-conjugating enzyme that regulates the cell cycle promotes chromosome missegregation and tumor formation, according ... Enzyme, Genes, Microscopy, Mitosis, Research, T-Cell, Tumor, Tumorigenesis, Ubiquitin, Ubiquitin-Conjugating Enzyme, X ... Ubiquitin-conjugating enzyme promotes chromosome missegregation and tumor formation. *Download PDF Copy ... A ubiquitin-conjugating enzyme that regulates the cell cycle promotes chromosome missegregation and tumor formation, according ...
UBIQUITIN-CONJUGATING ENZYME E9. A. 160. Mus musculus. Mutation(s): 0 Gene Names: Ube2i, Ubc9, Ubce2i, Ubce9. EC: 6.3.2.19 (PDB ... Murine/human ubiquitin-conjugating enzyme Ubc9 is a functional homolog of Saccharomyces cerevisiae Ubc9 that is essential for ... Murine/human ubiquitin-conjugating enzyme Ubc9 is a functional homolog of Saccharomyces cerevisiae Ubc9 that is essential for ... Crystal structure of murine/human Ubc9 provides insight into the variability of the ubiquitin-conjugating system.. Tong, H., ...
Meiosis and small ubiquitin-related modifier (SUMO)-conjugating enzyme, Ubc9.. Sakaguchi K1, Koshiyama A1, Iwabata K1. ... In this review, we describe the role of a small ubiquitin-like protein modifier (SUMO)-conjugating protein, Ubc9, in ... CcUbc9 works with factors including CcLim15 and CcTopII as an inhibitor of ubiquitin-mediated degradation and as a metabolic ... Small Ubiquitin-Related Modifier Proteins/metabolism*. *Ubiquitin-Conjugating Enzymes/metabolism*. Substances. *Cell Cycle ...
Ubiquitin-conjugating enzyme E2 AImported. ,p>Information which has been imported from another database using automatic ... Belongs to the ubiquitin-conjugating enzyme family.UniRule annotation. Automatic assertion according to rulesi ... tr,A0A146NRI0,A0A146NRI0_FUNHE Ubiquitin-conjugating enzyme E2 A OS=Fundulus heteroclitus OX=8078 PE=3 SV=1 ... PS00183 UBIQUITIN_CONJUGAT_1, 1 hit. PS50127 UBIQUITIN_CONJUGAT_2, 1 hit. ...
Ubiquitin-conjugating enzymes (E2s) collaborate with the ubiquitin-activating enzyme (E1) and ubiquitin ligases (E3s) to attach ... Ubiquitin-conjugating enzymes (E2s) collaborate with the ubiquitin-activating enzyme (E1) and ubiquitin ligases (E3s) to attach ... Mechanistic insight into the allosteric activation of a ubiquitin-conjugating enzyme by RING-type ubiquitin ligases. Ozkan, E. ... Ubiquitin-conjugating enzyme E2 D2. A. 149. Homo sapiens. Mutation(s): 1 Gene Names: UBE2D2, UBC4, UBCH5B, PUBC1, UBC5B, UBCH4 ...
ubiquitin conjugating enzyme E2R 2. ubiquitin-conjugating enzyme E2-CDC34B. ubiquitin-conjugating enzyme UBC3B. ubiquitin- ... ubiquitin-conjugating enzyme E2 R2. Names. E2 ubiquitin-conjugating enzyme R2. ubiquitin carrier protein R2. ... UBE2R2 ubiquitin conjugating enzyme E2 R2 [Homo sapiens] UBE2R2 ubiquitin conjugating enzyme E2 R2 [Homo sapiens]. Gene ID: ... UBCc; Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain. This is part of the ubiquitin-mediated protein degradation ...
IPR023313 Ubiquitin-conjugating enzyme, active site. IPR000608 Ubiquitin-conjugating enzyme E2. IPR016135 Ubiquitin-conjugating ...
Abbreviations: E1, ubiquitin-activating enzyme; E2, ubiquitin-conjugating enzyme; E3, ubiquitin-ligating enzyme; TTS, type III ... a limited number of ubiquitin-conjugating enzymes (E2s; also known as Ubc in enzyme designations), and a large number of ... ubiquitin, biotinylated ubiquitin, and ubiquitin-activating enzyme were from Affiniti Research (Mamhead, U.K.); anti-c-myc ... The Shigella flexneri effector OspG interferes with innate immune responses by targeting ubiquitin-conjugating enzymes. Dong ...
Ubiquitin-conjugating enzyme E2 E3. Ubiquitin-conjugating enzyme E2 E3, EC 2.3.2.23 (E2 ubiquitin-conjugating enzyme E3) (UbcM2 ... Ubiquitin carrier protein E3) (Ubiquitin-conjugating enzyme E2-23 kDa) (Ubiquitin-protein ligase E3) ... Ubiquitin-conjugating enzyme E2 E3Imported. ,p>Information which has been imported from another database using automatic ... tr,B2FDH0,B2FDH0_MOUSE Ubiquitin-conjugating enzyme E2 E3 (Fragment) OS=Mus musculus OX=10090 GN=Ube2e3 PE=1 SV=8 ...
... Author(s). Koenig, Paul-Albert; Hagiwara, ... "The E2 Ubiquitin-Conjugating Enzyme UBE2J1 Is Required for Spermiogenesis in Mice." Journal of Biological Chemistry 289, no. 50 ... Dislocation substrates are ubiquitylated in the cytosol by E2 ubiquitin-conjugating/E3 ligase complexes. UBE2J1 is one of the ... Our findings identify an essential function for the ubiquitin-proteasome-system in spermiogenesis and define a novel, non- ...
The worlds first wiki where authorship really matters. Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts.
ubiquitin-conjugating enzyme E2D 3 (UBC4/5 homolog, yeast) , ubiquitin-conjugating enzyme E2D 3 , ubiquitin-conjugating enzyme ... ubiquitin-conjugating enzyme E2 D3 , ubiquitin-conjugating enzyme E2(17)KB 3 , ubiquitin-conjugating enzyme E2-17 kDa 3 , ... ubiquitin carrier protein D2 , ubiquitin conjugating enzyme E2 , ubiquitin-conjugating enzyme E2 D2 , ubiquitin-protein ligase ... ubiquitin-conjugating enzyme E2D 3 (homologous to yeast UBC4/5) , ubiquitin-protein ligase D3 , ubiquitin-conjugating enzyme ...
... ubiquitin-conjugating enzyme E2(17)KB 1 , ubiquitin-conjugating enzyme E2-17 kDa 1 , ubiquitin-conjugating enzyme E2D 1 (UBC4/5 ... ubiquitin-conjugating enzyme E2D 1, UBC4/5 homolog , ubiquitin-conjugating enzyme E2D 1 , ubiquitin-conjugating enzyme E2D 1 ( ... Target Ubiquitin-Conjugating Enzyme E2D 1 (UBE2D1) * Ubiquitin-Conjugating Enzyme E2D 1 (UBE2D1) ... anti-Ubiquitin-Conjugating Enzyme E2Q Family Member 1 Antikörper * anti-Ubiquitin-Conjugating Enzyme E2Q Family Member 2 ...
Ub is bound to the ubiquitin-activating enzyme (E1), which activates Ub and enables it to bind to the ubiquitin-conjugating ... MMS2, encoding a ubiquitin-conjugating-enzyme-like protein, is a member of the yeast error-free postreplication repair pathway ... MMS2, encoding a ubiquitin-conjugating-enzyme-like protein, is a member of the yeast error-free postreplication repair pathway ... MMS2, encoding a ubiquitin-conjugating-enzyme-like protein, is a member of the yeast error-free postreplication repair pathway ...
Ubiquitin-conjugating enzymes (E2s) comprise a class of eukaryotic enzymes that function at an intermediate step in the ... The tail of ubiquitin-conjugating enzyme redirects multi-ubiquitin chain synthesis from the lysine 48-linked configuration to a ... making it a substrate for the ubiquitin pathway (56). The ubiquitin-conjugating enzymes UBC4 and RAD6 (UBC2) from S. cerevisiae ... Creation of a Pluripotent Ubiquitin-Conjugating Enzyme. Christopher Ptak, Chantelle Gwozd, J. Torin Huzil, Todd J. Gwozd, Grace ...
Creation of a Pluripotent Ubiquitin-Conjugating Enzyme. Christopher Ptak, Chantelle Gwozd, J. Torin Huzil, Todd J. Gwozd, Grace ... Creation of a Pluripotent Ubiquitin-Conjugating Enzyme. Christopher Ptak, Chantelle Gwozd, J. Torin Huzil, Todd J. Gwozd, Grace ... Creation of a Pluripotent Ubiquitin-Conjugating Enzyme. Christopher Ptak, Chantelle Gwozd, J. Torin Huzil, Todd J. Gwozd, Grace ... Creation of a Pluripotent Ubiquitin-Conjugating Enzyme Message Subject (Your Name) has forwarded a page to you from Molecular ...
This thesis examines the structural and biochemical features of two E2 ubiquitin-conjugating enzymes, Ube2w and Ube2h. First, ... much of the diversity in Ub signaling can be attributed to the structural characteristics of the enzymes in the ubiquitin ... These enzymes (E1, E2, and E3) work in succession to identify and modify substrates with varying Ub signals. The manner in ... In fact, as the study of ubiquitin (Ub) expands, it is becoming clear that this small post-translational modification is far ...
Here, we report a critical role of ubiquitin-conjugating enzyme E2T (UBE2T), an E2 ubiquitin-conjugating enzyme, in mammary ... which consists of ubiquitin-activating enzyme (E1), ubiquitin-conjugating enzyme (E2), ubiquitin-ligase (E3), and the 26S ... EWS/FLI1 up regulates mE2-C, a cyclin-selective ubiquitin conjugating enzyme involved in cyclin B destruction. Oncogene 1998;17 ... To further understand the biological function of UBE2T as an E2-ubiquitin conjugating enzyme, we attempted to find a potential ...
Ubiquitination and Downregulation of BRCA1 by Ubiquitin-Conjugating Enzyme E2T Overexpression in Human Breast Cancer Cells. ... Ubiquitination and Downregulation of BRCA1 by Ubiquitin-Conjugating Enzyme E2T Overexpression in Human Breast Cancer Cells ... Ubiquitination and Downregulation of BRCA1 by Ubiquitin-Conjugating Enzyme E2T Overexpression in Human Breast Cancer Cells ... Ubiquitination and Downregulation of BRCA1 by Ubiquitin-Conjugating Enzyme E2T Overexpression in Human Breast Cancer Cells ...
Showing Protein Ubiquitin-conjugating enzyme E2 E1 (HMDBP00620). IdentificationBiological propertiesGene propertiesProtein ... Nuber U, Schwarz S, Kaiser P, Schneider R, Scheffner M: Cloning of human ubiquitin-conjugating enzymes UbcH6 and UbcH7 (E2-F1) ... David Y, Ziv T, Admon A, Navon A: The E2 ubiquitin-conjugating enzymes direct polyubiquitination to preferred lysines. J Biol ... ISG15 conjugation to the UbcH6 ubiquitin E2 enzyme. J Biochem. 2005 Dec;138(6):711-9. [PubMed:16428300 ] ...
Here we identify the ubiquitin-conjugating enzyme variant UEV-1 as a regulator of AMPAR trafficking in vivo. We identified ... UEV-1 homologs in other species bind to the ubiquitin-conjugating enzyme Ubc13 to create K63-linked polyubiquitin chains on ...
The protein interacts with its cognate ubiquitin-conjugating enzyme (E2), Ube2g2, via its RING domain and a unique region ... The RING finger-dependent ubiquitin ligase (E3) gp78, known as the tumor autocrine motility factor receptor, contributes to ... The protein interacts with its cognate ubiquitin-conjugating enzyme (E2), Ube2g2, via its RING domain and a unique region ... Design, synthesis, and anticancer activity evaluation of irreversible allosteric inhibitors of the ubiquitin-conjugating enzyme ...
This Process Is Dependent Upon The Sequential Action Of An E1-activating Enzyme, An E2-conjugating Enzyme, And An E3 ... In Eukaryotic Cells The Stability And Function Of Many Proteins Are Regulated By The Addition Of Ubiquitin Or Ubiquitin-like ... Ubiquitin-Conjugating Enzymes, Ubiquitin-Protein Ligases, Ubiquitination. Genome Res. Oct. 01, 2009; 19(10);1905-11 [PUBMED: ... Analysis of the human E2 ubiquitin conjugating enzyme protein interaction network.. Markson G, Kiel C, Hyde R, Brown S, ...
Recombinant Human Ubiquitin Conjugating Enzyme 9 produced in E.coli is a 19.5 kDa protein containing 171 amino acids. The Ubc9 ... ubiquitin carrier protein; ubiquitin conjugating enzyme 9; ubiquitin-conjugating enzyme E2I; ubiquitin-conjugating enzyme E2I ( ... ubiquitin-conjugating enzyme E2I (homologous to yeast UBC9); ubiquitin-conjugating enzyme UbcE2A; ubiquitin-like protein SUMO-1 ... SUMO-conjugating enzyme UBC9; EC 6.3.2.-; SUMO-protein ligase; Ubiquitin-conjugating enzyme E2 I; Ubiquitin-protein ligase I; ...
Restriction EnzymeModified Enzyme. RT PCR KitsReal Time PCR KitsLPS Extraction KitmiRNA cDNA Synthesis KitsDirect PCR KitsDNA ... Transporter Screening & Profiling ServicesEpigenetic Screening & Profiling ServicesUbiquitin Screening & Profiling Services ... Creative Biogene Updates Its Collection of Enzymes Creative Biogene Launched A Large-scale Outdoor Development Training for Its ... Creative Biogene Announced Advanced Modified Enzyme in the Field Creative Biogene Released Novel Genomic DNA Purification ...
Characterization of the Ubiquitin-Conjugating Enzyme Gene Family in Rice and Evaluation of Expression Profiles under Abiotic ... Arabidopsis ubiquitin-conjugating enzyme UBC22 is required for female gametophyte development and likely involved in Lys11- ... Molecular Characterization of Plant Ubiquitin-Conjugating Enzymes Belonging to the UbcP4/E2-C/UBCx/UbcH10 Gene Family. Marie ... Molecular Characterization of Plant Ubiquitin-Conjugating Enzymes Belonging to the UbcP4/E2-C/UBCx/UbcH10 Gene Family ...
  • Once conjugated to ubiquitin, the E2 molecule binds one of several ubiquitin ligases or E3s via a structurally conserved binding region. (wikipedia.org)
  • Ubiquitin-conjugating enzymes (E2s) collaborate with the ubiquitin-activating enzyme (E1) and ubiquitin ligases (E3s) to attach ubiquitin to target proteins. (rcsb.org)
  • One of these patches corresponds to a binding site for both HECT and RING domain proteins, suggesting that a single substitution in the catalytic domain of RAD6 confers upon it the ability to interact with multiple ubiquitin protein ligases (E3s). (asm.org)
  • Ubiquitin ligases, critical mediators of endoplasmic reticulum-associated degradation. (semanticscholar.org)
  • Cytoplasmic protein quality control degradation mediated by parallel actions of the E3 ubiquitin ligases Ubr1 and San1. (semanticscholar.org)
  • The eukaryotic ubiquitin-conjugation system sets the turnover rate of many proteins and includes activating enzymes (E1s), conjugating enzymes (UBCs/E2s), and ubiquitin-protein ligases (E3s), which are responsible for activation, covalent attachment and substrate recognition, respectively. (biomedcentral.com)
  • As well as ubiquitin itself, the central components of this system include ubiquitin-activating enzymes (E1s), ubiquitin-conjugating enzymes (UBCs or E2s), and ubiquitin-protein ligases (E3s). (biomedcentral.com)
  • Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes, or E1s, ubiquitin-conjugating enzymes, or E2s, and ubiquitin-protein ligases, or E3s. (nih.gov)
  • Ubiquitination of proteins is mediated by a cascade of enzymes which includes E1 (ubiquitin activating), E2 (ubiquitin conjugating), and E3 (ubiquitin ligases) enzymes. (nih.gov)
  • ubiquitin ligases which have been shown to connect to UBC13 allowed UBC13-mediated FK2 and 53BP1 concentrate development at DNA breaks. (healthweeks.com)
  • We suggest that this region interacts with substrates of CDC34 or with trans-acting factors (such as CDC34-specific ubiquitin protein ligases) that govern the substrate selectivity of CDC34. (nih.gov)
  • E3 ubiquitin ligases form part of a protein complex that tags damaged or excess proteins with molecules called ubiquitin. (medlineplus.gov)
  • Ubiquitin-conjugating enzymes , also known as E2 enzymes and more rarely as ubiquitin-carrier enzymes , perform the second step in the ubiquitination reaction that targets a protein for degradation via the proteasome . (wikipedia.org)
  • We speculate that CcLim15 and CcTopII work in cohesion between homologous chromatins initially and then, in the process of the zygotene events, CcUbc9 works with factors including CcLim15 and CcTopII as an inhibitor of ubiquitin-mediated degradation and as a metabolic switch in the meiotic prophase cell cycle. (nih.gov)
  • Studies suggest that CK2-dependent phosphorylation of this ubiquitin-conjugating enzyme functions by regulating beta-TrCP substrate recognition and induces its interaction with beta-TrCP, enhancing beta-catenin degradation. (nih.gov)
  • CK2-dependent phosphorylation of the E2 ubiquitin conjugating enzyme UBC3B induces its interaction with beta-TrCP and enhances beta-catenin degradation. (nih.gov)
  • The Rad6 N terminus is also required for physical interaction with an E3 enzyme Ubr1, and for N-end rule protein degradation ( 14 - 16 ). (pnas.org)
  • The correct progress through the cell cycle is thus under the control of successive events where protein activation alternates with protein degradation mediated by the ubiquitin-dependent proteolytic pathway. (plantphysiol.org)
  • Ubiquitin-mediated degradation is a primary mechanism by which p27 Kip1 levels are regulated. (arvojournals.org)
  • The ubiquitin (Ub)/proteasome pathway facilitates the degradation of damaged proteins and regulators of growth and stress response. (semanticscholar.org)
  • Ubiquitin-conjugating enzymes UBC4 and UBC5 mediate selective degradation of short-lived and abnormal proteins. (semanticscholar.org)
  • The post translational modification of proteins by ubiquitin controls many essential cellular processes by targeting substrates for degradation, facilitating interactions with other proteins, or directing relocalization within the cell. (arvojournals.org)
  • UbcH7 is able to catalyze several different types of ubiquitin chains on p27.Some of these ubiquitin chains target substrates for degradation, but others are not proteasome targets. (arvojournals.org)
  • Ubiquitination by UbcH7 catalyzes formation of degradation incompetent p27-ubiquitin conjugates, thereby protecting it from degradation. (arvojournals.org)
  • The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. (nih.gov)
  • E2s are a family of ubiquitin carrier proteins that transfer ubiquitin to the ε-lysine of proteins designated for degradation. (emdmillipore.com)
  • Regulated degradation of misfolded, damaged or short-lived proteins in eukaryotes occurs via the ubiquitin (Ub)-proteasome system (UPS). (nih.gov)
  • It has been suggested that such motifs be called "degrons", degrons being any motif that targets proteins for degradation (by the ubiquitin-dependent or and other systems). (nottingham.ac.uk)
  • Misfolded endoplasmic reticulum (ER) proteins are dislocated towards the cytosol and degraded by the ubiquitin-proteasome system in a process called ER-associated protein degradation (ERAD). (uu.nl)
  • US2-mediated degradation of HLA-I serves as a paradigm of ERAD and has facilitated the identification of TRC8 (also known as RNF139) as an E3 ubiquitin ligase. (uu.nl)
  • We identified multiple E2 enzymes involved in this process, of which UBE2G2 was crucial for the degradation of various immunoreceptors. (uu.nl)
  • This enzyme is located in the membrane of the endoplasmic reticulum (ER) and may contribute to quality control ER-associated degradation by the ubiquitin-proteasome system. (genecards.org)
  • Ulrich, H. D. Degradation or maintenance: actions of the ubiquitin system on eukaryotic chromatin. (nature.com)
  • A major route for protein degradation occurs via the ubiquitin-proteasome pathway. (ubc.ca)
  • UBC-2, an essential E2 in the nematode C. elegans, is a functional homolog of Saccharomyces cerevisiae UBC4, a member of a branch of ubiquitin-conjugating enzymes required for the degradation of short-lived and abnormal proteins. (ubc.ca)
  • Department of Biochemistry and Molecular Biology The University of British Columbia 2146 Health Sciences Mall Vancouver, B.C. V6T 1Z3 Date: May 15,2002 ABSTRACT A major route for protein degradation occurs via the ubiquitin-proteasome pathway. (ubc.ca)
  • Muscle mass is mainly controlled by the ubiquitin-proteasome system (UPS), involving hundreds of ubiquitinating enzymes (E2s and E3s) that target their dedicated substrates for subsequent degradation. (mdpi.com)
  • We recently demonstrated that MuRF1, an E3 ubiquitin ligase known to bind to sarcomeric proteins (telethonin, α-actin, myosins) during catabolic situations, interacts with 5 different E2 enzymes and that these E2-MuRF1 couples are able to target telethonin, a small sarcomeric protein, for degradation. (mdpi.com)
  • However, it remains unclear whether nitrosative stress affects ER-associated degradation (ERAD), a separate ER stress regulatory system responsible for the degradation of substrates via the ubiquitin-proteasomal pathway. (elsevier.com)
  • For example, one member of this family called SUMO can bind to a protein "tagged" by ubiquitin for degradation, stabilizing it and preventing it from being sent to the proteasome. (news-medical.net)
  • In contrast to the well known role of ubiquitin in protein degradation by the proteasome, SUMO conjugation does not directly target proteins for destruction ( 4 - 6 ). (mcponline.org)
  • Structurally different ubiquitin chains can also play other roles in cells that are unrelated to protein degradation ( 18 , 21 ). (mcponline.org)
  • Ubiquitin-conjugating enzymes (E2s) comprise a class of eukaryotic enzymes that function at an intermediate step in the reaction pathway leading to protein ubiquitination. (asm.org)
  • This requires that downstream of E2-ubiquitin thiol ester formation, an E2 must interact with proteins that are specific to that pathway, such as an E3 or a target, through unique points of contact other than those employed with ubiquitin and E1. (asm.org)
  • The entire complement of ubiquitin pathway components that mediate this process in retinal pigment epithelial (RPE) cells remains to be identified. (arvojournals.org)
  • Inhibitory effect of ubiquitin-proteasome pathway on proliferation of esophageal carcinoma cells. (semanticscholar.org)
  • Targeting the ubiquitin-proteasome pathway in breast cancer. (semanticscholar.org)
  • The dependency of p45 SKP2 -p19 SKP1 complex formation on cyclin A-CDK2 may ensure tight coordination of the activities of the cell cycle clock with those of a potential ubiquitin conjugation pathway. (embopress.org)
  • Among its related pathways are Proteolysis Role of Parkin in the Ubiquitin-Proteasomal Pathway and Innate Immune System . (genecards.org)
  • Two principal elements of this pathway are the ubiquitin-conjugating enzymes RAD6 and the MMS2-UBC13 heterodimer, which are recruited to chromatin by the RING-finger proteins RAD18 and RAD5, respectively. (nature.com)
  • Here we show that UBC9, a small ubiquitin-related modifier (SUMO)-conjugating enzyme, is also affiliated with this pathway and that proliferating cell nuclear antigen (PCNA)-a DNA-polymerase sliding clamp involved in DNA synthesis and repair-is a substrate. (nature.com)
  • To identify the ubiquitination pathway that is linked to Nedd4, we demonstrated that specific E2 enzymes, including human Ubc4, UbcH5B, UbcH5C, UbcH6 and UbcH7, could transfer ubiquitin molecules to Nedd4 at the active cysteine residue, whereas E6AP accepted ubiquitins from Ubc4, UbcH5B, UbcH5C and UbcH7. (elsevier.com)
  • Background: The destruction of cyclin B is required for exit from mitosis, and is mediated by the ubiquitin pathway. (elsevier.com)
  • The ubiquitination process covalently attaches ubiquitin , a short protein of 76 amino acids , to a lysine residue on the target protein. (wikipedia.org)
  • Once a protein has been tagged with one ubiquitin molecule, additional rounds of ubiquitination form a polyubiquitin chain that is recognized by the proteasome's 19S regulatory particle, triggering the ATP -dependent unfolding of the target protein that allows passage into the proteasome's 20S core particle, where proteases degrade the target into short peptide fragments for recycling by the cell . (wikipedia.org)
  • We present evidence that the effector OspG is a protein kinase that binds various ubiquitinylated ubiquitin-conjugating enzymes, including UbcH5, which belongs to the stem cell factor SCF β-TrCP complex promoting ubiquitination of phosphorylated inhibitor of NF-κB type α (phospho-IκBα). (pnas.org)
  • Although E2s have a function in common in ubiquitin thiol ester formation, they have also been shown to function within a wide range of cellular pathways resulting in the ubiquitination of protein substrates particular to those pathways. (asm.org)
  • In Saccharomyces cerevisiae , a complex of similar molecular composition (an F‐box protein, a member of the cullin family and a homolog of p19 SKP1 ) forms a functional E3 ubiquitin protein ligase complex, designated SCF CDC4 , that facilitates ubiquitination of a CDK inhibitor by CDC34. (embopress.org)
  • PCNA is mono-ubiquitinated through RAD6 and RAD18, modified by lysine-63-linked multi-ubiquitination-which additionally requires MMS2, UBC13 and RAD5-and is conjugated to SUMO by UBC9. (nature.com)
  • The ubiquitin-conjugating enzyme Pex4p together with its binding partner, the peroxisomal membrane protein Pex22p, co-ordinates cysteine-dependent ubiquitination of the cycling receptor protein Pex5p. (rug.nl)
  • In addition, a ubiquitin-conjugating enzyme (E2), UBC4, was shown to be involved in cyclin ubiquitination in Xenopus egg extracts. (elsevier.com)
  • Conclusions: UBCx is a novel ubiquitin-conjugating enzyme involved in cyclin ubiquitination in Xenopus. (elsevier.com)
  • Ubiquitination of intracellular proteins by the yeast RAD6 (UBC2) ubiquitin-conjugating (E2) enzyme is required for cellular processes as diverse as DNA repair, selective proteolysis, and normal growth. (northwestern.edu)
  • Through a process known as ubiquitination or ubiquitylation, an ubiquitin molecule can bind to a substrate protein, changing the way it functions. (news-medical.net)
  • Ubiquitination occurs when an ubiquitin molecule bonds to a substrate protein and is a type of post-translational modification. (news-medical.net)
  • The E1 enzyme is a dimer that consists of SAE1 and SAE2, and in contrast to the large set of E2 enzymes involved in ubiquitination, a single E2 enzyme, Ubc9, is responsible for sumoylation. (mcponline.org)
  • Takeuchi T, Iwahara S, Saeki Y, Sasajima H, Yokosawa H: Link between the ubiquitin conjugation system and the ISG15 conjugation system: ISG15 conjugation to the UbcH6 ubiquitin E2 enzyme. (hmdb.ca)
  • Human Ubquitin Conjugating Enzyme 9 (Ubc9) is a member of the E2 family and is specific for the conjugation of SUMO to a variety of target proteins. (creativebiomart.net)
  • Conjugation of ubiquitin to the protein involves a cascade of three enzymes: E1, E2, and E3. (plantphysiol.org)
  • Structural determinants of ubiquitin conjugation in Entamoeba histolytica. (semanticscholar.org)
  • Acts as an E2-like enzyme that catalyzes the conjugation of ATG12 to ATG5. (mybiosource.com)
  • Also acts as an autocatalytic E2-like enzyme, catalyzing the conjugation of atg12 to itself, atg12 conjugation to atg3 playing a role in mitochondrial homeostasis but not in autophagy. (mybiosource.com)
  • NEDD8 conjugation is known to occur only on cullins, components of Skip-Cullin-F-Box (SCF) complexes (reviewed in [ 10 ]) which degrade cyclins and other regulatory proteins via the ubiquitin system. (biomedcentral.com)
  • The ability of this expressed protein to form a thiolester bond with ubiquitin showed that it was functionally active, The ability of this protein to catalyze the conjugation of ubiquitin to histone H2A and H2B was also examined. (nus.edu.sg)
  • We propose that all eukaryotic cells may use a common ubiquitin conjugation apparatus to promote S phase. (embopress.org)
  • Using transient transfection assays, we demonstrated that UBCH7 modulates the transcriptional activity of progesterone receptor (PR) and glucocorticoid, androgen, and retinoic acid receptors in a hormone-dependent manner and that the ubiquitin conjugation activity of UBCH7 is required for its ability to potentiate transactivation by steroid hormone receptors (SHR). (elsevier.com)
  • It also acts in conjugation with SCF ubiquitin ligase complexes. (sigmaaldrich.com)
  • These proteases are also responsible for the maturation of SUMO precursors, a process that exposes the carboxyl-terminal diglycine motif that is characteristic for ubiquitin-like proteins and required for conjugation to target proteins. (mcponline.org)
  • Ubiquitin conjugating enzyme E2 Q2 is a protein that in humans is encoded by the UBE2Q2 gene. (wikipedia.org)
  • Ubiquitin-fold modifier conjugating enzyme 1 is a protein that in humans is encoded by the UFC1 gene. (wikipedia.org)
  • This gene encodes a protein similar to the E2 ubiquitin conjugating enzyme UBC3/CDC34. (nih.gov)
  • The RAD6 gene in Saccharomyces cerevisiae encodes a 172-amino acid, 20-kDa E2 enzyme, Ubc2 ( 4 , 8 ). (pnas.org)
  • We cloned the complete c DNA sequence of Ubiquitin-conjugating enzyme gene from black tiger shrimps( Penaeus monodon)( Pm Ubc) by rapid amplification of c DNA ends( RACE) methods based on the partial sequence of Pm Ubc obtained from the hepatopancreas transcriptome database. (cnki.com.cn)
  • This gene encodes a member of the E2 ubiquitin-conjugating enzyme family. (nih.gov)
  • Wu Z, Shen S, Zhang Z, Zhang W, Xiao W. Ubiquitin-conjugating enzyme complex Uev1A-Ubc13 promotes breast cancer metastasis through nuclear factor-small ka, CyrillicB mediated matrix metalloproteinase-1 gene regulation. (biomedcentral.com)
  • The protein encoded by this gene belongs to the ubiquitin-conjugating enzyme family. (genecards.org)
  • UBE2K (Ubiquitin Conjugating Enzyme E2 K) is a Protein Coding gene. (genecards.org)
  • GO annotations related to this gene include ligase activity and ubiquitin protein ligase binding . (genecards.org)
  • Recombinant Human Ubiquitin-Conjugating Enzyme E2 A is produced by our E.coli expression system and the target gene encoding Met1-Cys152 is expressed with a GST, 6His tag at the N-terminus. (bonopusbio.com)
  • Jentsch, S., McGrath, J. P. & Varshavsky, A. The yeast DNA repair gene RAD6 encodes a ubiquitin-conjugating enzyme. (nature.com)
  • Previous functional annotation cluster analyses of cold-induced gene expression profiles have shown that the ubiquitin-conjugating enzyme E2 (UBE2), rather than the cyclin-like F-box domain alone, forms the functional cluster. (nebraska.edu)
  • The RNF216 gene provides instructions for making a protein that plays a role in the ubiquitin-proteasome system, which is the cell machinery that breaks down (degrades) unwanted proteins. (medlineplus.gov)
  • Murine/human ubiquitin-conjugating enzyme Ubc9 is a functional homolog of Saccharomyces cerevisiae Ubc9 that is essential for the viability of yeast cells with a specific role in the G2-M transition of the cell cycle. (rcsb.org)
  • For example, the 11 E2s and two ubiquitin-like conjugating enzymes (UBC9 and UBC12) from the yeast Saccharomyces cerevisiae exhibit between 20 and 92% identity. (asm.org)
  • To isolate the genes involved in Cd tolerance, we transformed WT (wild-type) yeast Y800 with a tobacco cDNA expression library and isolated a tobacco cDNA, NtUBC1 (Ub-conjugating enzyme), that enhances cadmium tolerance. (deepdyve.com)
  • RNAi shows that only four UBCs are essential for embryogenesis: LET-70 (UBC-2), a functional homolog of yeast Ubc4/5p, UBC-9, an ortholog of yeast Ubc9p, which transfers the ubiquitin-like modifier SUMO, UBC-12, an ortholog of yeast Ubc12p, which transfers the ubiquitin-like modifier Rub1/Nedd8, and UBC-14, an ortholog of Drosophila Courtless. (biomedcentral.com)
  • McDonough, MM , Sagan, P & Gonda, D 1995, ' Characterization of novel yeast Rad6 (UBC2) ubiquitin-conjugating enzyme mutants constructed by charge-to-alanine scanning mutagenesis ', Journal of Bacteriology , vol. 177, pp. 580-585. (northwestern.edu)
  • Putative TJBC-2 interacting proteins identified include: a ubiquitin-like budding yeast DSK2 ortholog referred to as DSK-2, two RING finger proteins, a protein containing a FYVE domain, a calcium ATPase called MCA-1, and ubiquitin. (ubc.ca)
  • The NH(2)-terminal end of a protein, named SMCp, which contains an ARID (A/T rich interaction domain) DNA binding domain and is similar to the mammalian SMCY/SMCX proteins and retinoblastoma binding protein 2, was shown to bind the African swine fever virus encoded ubiquitin conjugating enzyme (UBCv1) using the yeast two hybrid system and in in vitro binding assays. (ac.ke)
  • Yeast cells that express a K63R mutant of ubiquitin are compromised in DNA repair, but proteolysis is not affected in these cells ( 23 ). (mcponline.org)
  • Meiosis and small ubiquitin-related modifier (SUMO)-conjugating enzyme, Ubc9. (nih.gov)
  • In this review, we describe the role of a small ubiquitin-like protein modifier (SUMO)-conjugating protein, Ubc9, in synaptonemal complex formation during meiosis in a basidiomycete, Coprinus cinereus. (nih.gov)
  • Ubiquitin-conjugating enzyme 9 (Ubc9), the sole conjugating enzyme for sumoylation, regulates protein function and plays an important role in sumoylation-mediated cellular pathways. (mdpi.com)
  • SUMO-conjugating enzyme UBC9, EC 6.3.2. (angioproteomie.com)
  • E2 conjugating enzyme 9 (Ubc9) is the only reported ubiquitin-conjugating enzyme that links the SUMO molecule with a target protein. (bvsalud.org)
  • The E3 molecule is responsible for binding the target protein substrate and transferring the ubiquitin from the E2 cysteine to a lysine residue on the target protein. (wikipedia.org)
  • We show herein that, although the E3-binding site on the human E2 UbcH5b is distant from its active site, two RING-type minimal E3 modules lacking substrate-binding functions greatly stimulate the rate of ubiquitin release from the UbcH5b-ubiquitin thioester. (rcsb.org)
  • E2s may transfer ubiquitin directly to a lysine side chain found either on a protein substrate or on a ubiquitin moiety in a growing multiubiquitin chain through the formation of an isopeptide bond. (asm.org)
  • In the former case, an E3 functions to assist the E2 in the recognition of a protein substrate, while in the latter case, it is believed that the E3 directly links ubiquitin to either the protein substrate or a growing multiubiquitin chain. (asm.org)
  • The transfer of ubiquitin to the target protein substrate usually requires ubiquitin-ligase activity (E3). (plantphysiol.org)
  • The E2s or UBCs accept activated ubiquitin from an E1, also forming a thioester, and mediate the covalent attachment of the activated ubiquityl moiety to an amino group of a lysyl residue on the substrate protein. (biomedcentral.com)
  • Until recently the proximal donor of ubiquitin to target proteins was thought to a ubiquitin charged E2 (UBC), and E3s were not thought to be directly involved in the transfer of ubiquitin to the substrate protein. (nottingham.ac.uk)
  • Does not transfer ubiquitin directly to but elongates monoubiquitinated substrate protein. (genecards.org)
  • At saturating enzyme concentrations, UBCx converts twice as much substrate into ubiquitin conjugates, but generates conjugates of lower molecular mass than UBC4. (elsevier.com)
  • We suggest that E2 mutants obtained by this approach are likely to be defective with respect to interaction with other, trans-acting factors required for their intracellular activity or substrate selectivity and therefore will be useful for further genetic and biochemical studies of ubiquitin-conjugating enzyme function. (northwestern.edu)
  • The interaction and co-localisation of UBCv1 with SMCp suggest that SMCp may be a substrate in vivo for the enzyme. (ac.ke)
  • Through these steps, the ubiquitin molecule forms an isopeptide bond with the residue of lysine on the protein substrate respectively. (news-medical.net)
  • The cDNA contains an open reading frame coding for 238 amino acids which shows an overall identity of 81% to human CDC34, the cell cycle-related ubiquitin-conjugating enzyme. (nus.edu.sg)
  • Here we identify human CUL‐1, a member of the cullin family, and the ubiquitin‐conjugating enzyme CDC34 as additional partners of p45 SKP2 in vivo . (embopress.org)
  • The ubiquitin conjugating (E2) enzyme encoded by CDC34 (UBC3) in Saccharomyces cerevisiae is required for the G1 to S transition of the cell cycle. (nih.gov)
  • We found that a construct encoding a chimeric RAD6-CDC34 ubiquitin conjugating enzyme, in which the 21 residue acidic carboxyl-terminal domain of RAD6 has been replaced with the 125 residue carboxyl-terminal domain of CDC34, performed the essential functions of CDC34 in vivo. (nih.gov)
  • CDC34 (cell division cycle 34), a ubiquitin carrier protein, belongs to the ubiquitin-conjugating enzyme family. (sigmaaldrich.com)
  • Dislocation substrates are ubiquitylated in the cytosol by E2 ubiquitin-conjugating/E3 ligase complexes. (mit.edu)
  • This small (8.5kDa) modification achieves its diverse signaling capabilities partly through the enzymes that catalyze its attachment to cellular substrates. (washington.edu)
  • These enzymes (E1, E2, and E3) work in succession to identify and modify substrates with varying Ub signals. (washington.edu)
  • Substrates of this enzyme include the tumor suppressor protein p53 and peroxisomal biogenesis factor 5 (PEX5). (nih.gov)
  • Ubiquitin chains were initially discovered by studying the role of ubiquitin in targeting protein substrates for proteolysis. (mcponline.org)
  • The activating enzymes and the ubiquitin-like proteins NED-8 and SUMO are required for embryogenesis. (biomedcentral.com)
  • The UbL proteins, which, like ubiquitin, are known to be conjugated to other proteins, include SUMO-1 (also known as sentrin, SMT3, PIC1, UBL1 or GMP1) and NEDD8 (also known as RUB-1). (biomedcentral.com)
  • In recent years, the covalent attachment of Ubiquitin or Small Ubiquitin-like Modifiers (SUMO) to amino acid residues of target proteins has been recognized as another crucial PTM, re-directing protein fate and protein-protein interactions. (frontiersin.org)
  • We conclude offering a perspective on Ubiquitin and SUMO pathways as targets in cancer therapy. (frontiersin.org)
  • Modification of small ubiquitin-related modifier (SUMO) occurs in many cellular activities. (bvsalud.org)
  • Melchior, F. SUMO-nonclassical ubiquitin. (nature.com)
  • Vertebrates express three small ubiquitin-like modifiers, SUMO-1, SUMO-2, and SUMO-3. (mcponline.org)
  • Unusually for an ubiquitin-conjugating enzyme, Saccharomyces cerevisiae Pex4p can form a disulphide bond between the cysteine residues at positions 105 and 146. (rug.nl)
  • abstract = "We investigated the role of the ubiquitin-conjugating enzyme UBCH7 in nuclear receptor transactivation. (elsevier.com)
  • Ubiquitin-conjugating enzyme UBE2D3 is an important member of the ubiquitin-proteasome pathways. (jcancer.org)
  • Some reports have shown that the ubiquitin/proteasome system (UPS) participates in the regulation of these pathways [ 7 ]. (jcancer.org)
  • UBE2Z encodes an enzyme which ubiquitinates proteins which participate in signaling pathways and apoptosis. (antibodies-online.com)
  • Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. (hmdb.ca)
  • Catalyzes the covalent attachment of ubiquitin to other proteins. (genecards.org)
  • Overexpression of UBC4 and of UBC7, two other genes for ubiquitin-conjugating enzymes, also conferred resistance to methylmercury. (elsevier.com)
  • Furthermore, nuclear localization of N-terminal deletion mutant Nedd4 enabled us to investigate the interaction between Nedd4 and E2 enzyme (Ubc4 or UbcH7) in the cell. (elsevier.com)
  • We describe the creation of a pluripotent ubiquitin-conjugating enzyme (E2) generated through a single amino acid substitution within the catalytic domain of RAD6 (UBC2). (asm.org)
  • A putative Ariadne-like ubiquitin ligase is required for Dictyostelium discoideum development. (semanticscholar.org)
  • Since DSK-2 represented 60% of the putative interactors isolated from the screen, this project focused on the interaction of UBC-2 and DSK-2, and demonstrated a novel interaction between an E2 and an ubiquitin-domain protein (UDP) in vitro. (ubc.ca)
  • In eukaryotic cells the stability and function of many proteins are regulated by the addition of ubiquitin or ubiquitin-like peptides. (thebiogrid.org)
  • Its protein sequence is 100% identical to the mouse, rat, and rabbit homologs, which indicates that this enzyme is highly conserved in eukaryotic evolution. (nih.gov)
  • Ubiquitin is a small protein that is found in almost all cellular tissues in humans and other eukaryotic organisms, which helps to regulate the processes of other proteins in the body. (news-medical.net)
  • Dong M, Pang X, Xu Y, Wen F, Zhang Y. Ubiquitin-Conjugating Enzyme 9 Promotes Epithelial Ovarian Cancer Cell Proliferation in Vitro . (mdpi.com)
  • This study was undertaken to determine whether the human ubiquitin-conjugating enzyme, UBE2E3, is essential for RPE cell proliferation. (arvojournals.org)
  • These findings indicate that UBE2E3 is a major enzyme in modulating the balance between RPE cell proliferation and differentiation. (arvojournals.org)
  • Knockdown of ubiquitin -conjugating enzyme E2C/UbcH10 expression by RNA interference inhibits glioma cell proliferation and enhances cell apoptosis in vitro. (koreascience.or.kr)
  • From T47D cells, the endogenous UBE2T proteins were immunoprecipitated ( IP ) and immunoblotted ( IB ) by anti-ubiquitin ( Ub ) monoclonal antibody ( right ). (aacrjournals.org)
  • Anti-ubiquitin staining confirms the formation of polyubiquitin chains. (biomedcentral.com)
  • Data show that ubiquitin E2 enzymes UBE2D1 (zeige UBE2D1 Antikörper )/2/3 and E3 ligase RNF138 (zeige RNF138 Antikörper ) accumulate at DNA-damage sites and act at early resection stages by promoting CtIP (zeige RBBP8 Antikörper ) protein ubiquitylation and accrual. (antikoerper-online.de)
  • 55 Ubiquitin-Conjugating Enzyme E2D 1 (UBE2D1) Antikörper von 12 Herstellern verfügbar auf www.antikoerper-online.de. (antikoerper-online.de)
  • C-terminus of Hsc70-interacting protein (CHIP) together with ubiquitin-conjugating enzyme E2 D1 (UBE2D1) are involved in this modification. (elsevier.com)
  • We detected that UBE2D1 is S-nitrosylated at its active site, Cys85 by liquid chromatography-tandem mass spectrometry (LC-MS/MS). Furthermore, in vitro and cell-based experiments revealed that S-nitrosylated UBE2D1 has decreased ubiquitin-conjugating activity. (elsevier.com)
  • Recombinant Human Ubiquitin Conjugating Enzyme 9 produced in E.coli is a 19.5 kDa protein containing 171 amino acids. (creativebiomart.net)
  • Recombinant, human ubiquitin conjugating enzyme 5a fused to GST and expressed in E. coli . (emdmillipore.com)
  • Ubiquitin Conjµgating Enzyme E2B Human Recombinant produced in E.coli is a 19 kDa protein containing 166 amino acids.The UE2B protein contains 6xHis tag and is purified by proprietary chromatographic techniques. (neobiolab.com)
  • Ubiquitin-Conjµgating Enzyme E2I Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 154 amino acids & having a molecular mass of 17.9 kDa. (neobiolab.com)
  • Here, we report a critical role of ubiquitin-conjugating enzyme E2T (UBE2T), an E2 ubiquitin-conjugating enzyme, in mammary carcinogenesis. (aacrjournals.org)
  • We here describe identification of ubiquitin-conjugating enzyme E2T (UBE2T) as a novel therapeutic target for breast cancer. (aacrjournals.org)
  • In HEK293T cells, exogenous proteins of Flag-BRAC1, Myc-BARD1, HA-UBE2T, and HA-ubiquitin ( Ub ) were expressed in condition with MG132. (aacrjournals.org)
  • B, generation of an enzyme-dead mutant (C86A) of UBE2T. (aacrjournals.org)
  • Ubiquitin is a highly conserved, 76-amino-acid polypeptide that is posttranslationally attached to target proteins by the coordinated actions of a ubiquitin-activating enzyme (E1), a ubiquitin-conjugating enzyme (E2), and a ubiquitin protein ligase (E3). (arvojournals.org)
  • Hwang, Seongbin 2017-05-15 00:00:00 Ubiquitin (Ub)-conjugating enzyme (UBC, E2) receives Ub from Ub-activating enzyme (E1) and transfers it to target proteins, thereby playing a key role in Ub/26S proteasome-dependent proteolysis. (deepdyve.com)
  • In addition, E3 enzymes, including protein inhibitor of activated signal transducer and activator of transcription family members and RanBP2, can enhance the sumoylation of target proteins but are not strictly required in vitro ( 14 - 17 ). (mcponline.org)
  • Ubiquitin is able to form chains on target proteins via all seven internal lysines ( 18 , 19 ). (mcponline.org)
  • A ubiquitin-activating enzyme , or E1, first activates the ubiquitin by covalently attaching the molecule to its active site cysteine residue. (wikipedia.org)
  • Ubiquitin is a versatile cellular signaling molecule that can form polymers of eight different linkages, and individual linkage types have been associated with distinct cellular functions. (nature.com)
  • Five of the nine mutants we generated show defects in their in vivo functions, but almost all of the most severely affected mutants displayed unfacilitated ubiquitin-conjugating activity in vitro. (northwestern.edu)
  • Study shows that Ube2R1/2 forms a salt bridge interaction between a conserved Asp residue on Ube2R1/2 and acceptor ubiquitin residue Arg 54 and that perturbation of this interaction leads to the severe loss of UbeR2 activity. (nih.gov)
  • Ubiquitin (Ub) is a highly conserved 76-residue protein, often found covalently joined to other proteins. (pnas.org)
  • The number of UBC genes appears to increase with developmental complexity, and our results suggest functional overlap in many of these enzymes. (biomedcentral.com)
  • While there may be two or even three species of E1 in cells S. cerevisiae is currently known to contain at least 10 genes coding for ubiquitin-conjugating enzymes (E2). (nottingham.ac.uk)
  • To our knowledge, this is the first demonstration that overexpression of genes for ubiquitin-conjugating enzymes confers resistance to xenobiotics. (elsevier.com)
  • There are also ubiquitin-like proteins with distinct functions, which require their own E1s and E2s for attachment. (biomedcentral.com)
  • Proteins are targeted for destruction by the proteasome through covalent ubiquitin attachment. (ubc.ca)
  • This can occur with the attachment of a single ubiquitin protein, which is known as monoubiquitination, or several ubiquitin proteins forming a chain, known as polyubiquitination. (news-medical.net)
  • Analysis of the human E2 ubiquitin conjugating enzyme protein interaction network. (thebiogrid.org)
  • The data presented here imply that the p45 SKP2 -CUL‐1-p19 SKP1 complex may be a human representative of an SCF‐type E3 ubiquitin protein ligase. (embopress.org)
  • Mouse Anti Human Ubiquitin Conjugating Enzyme E2L 6 UBE2L6 antibody storage GENTAUR recommends for long therm storage to freeze at -24 C. For short time storage up to 30 days we suggest fridge storage at 1 to 10 C. Prevent multiple freeze taw cycles of Mouse Anti Human Ubiquitin Conjugating Enzyme E2L 6 UBE2L6. (antibody-antibodies.com)
  • Mouse Anti Human Ubiquitin Conjugating Enzyme E2L 6 UBE2L6 Human samples 80 % of the research is conducted on human samples. (antibody-antibodies.com)
  • GENTAUR suppliers human normal cells, cell lines, RNA extracts and lots of antibodies and ELISA kits to Human proteins as well as Mouse Anti Human Ubiquitin Conjugating Enzyme E2L 6 UBE2L6. (antibody-antibodies.com)
  • In this study, we used a lentiviral CRISPR/Cas9 library targeting all known human E2 enzymes to assess their involvement in US2-mediated HLA-I downregulation. (uu.nl)
  • Crystal structure of the human ubiquitin conjugating enzyme complex, hMms2-hUbc13. (nature.com)
  • Here we describe a systematic structure-function analysis of the human ubiquitin (Ub) E2 conjugating proteins, consisting of the determination of 15 new high-resolution three-dimensional structures of E2 catalytic domains, and autoubiquitylation assays for 26 Ub-loading E2s screened against a panel of nine different HECT (homologous to E6-AP carboxyl terminus) E3 ligase domains. (proteopedia.org)
  • A human ubiquitin conjugating enzyme (E2)-HECT E3 ligase structure-function screen. (proteopedia.org)
  • Several UbcH5b mutants are defective in their stimulation by E3s despite their abilities to bind to these E3s, to form ubiquitin thioesters, and to release ubiquitin at a basal rate. (rcsb.org)
  • Auf www.antikoerper-online.de finden Sie aktuell 54 Ubiquitin-Conjugating Enzyme E2D 3 (UBE2D3) Antikörper von 13 unterschiedlichen Herstellern. (antikoerper-online.de)
  • Our previous study showed that the ubiquitin conjugating enzyme UBE2D3 was negatively related to radioresistance in breast cancer cells [ 8 ]. (jcancer.org)
  • In vitro these enzymes are very poor at transferring ubiquitin to proteins on their own, and probably require an E3 to aid this in vivo . (nottingham.ac.uk)
  • Some E2s appear to require no other protein factor, at least in vitro, to transfer ubiquitin to a suitable target. (nottingham.ac.uk)
  • Here we report the generation of Lys11-linked polyubiquitin in vitro , for which the Lys11-specific E2 enzyme UBE2S was fused to a ubiquitin binding domain. (nature.com)
  • In vitro, in the presence or in the absence of BRCA1-BARD1 E3 ubiquitin-protein ligase complex, catalyzes the synthesis of Lys-48-linked polyubiquitin chains. (genecards.org)
  • The specificity in targeting a protein for ubiquitylation resides primarily in cognate pairs of E2 and E3 enzymes. (plantphysiol.org)
  • Our findings identify an essential function for the ubiquitin-proteasome-system in spermiogenesis and define a novel, non-redundant physiological function for the dislocation step of ER quality control. (mit.edu)
  • No specific E2 enzymes had previously been described for cooperation with TRC8. (uu.nl)
  • This protection involves formation of non-degradable ubiquitin conjugates on p27. (arvojournals.org)
  • The first step in ubiquitinylation involves activation of ubiquitin , followed by transfer to a ubiquitin conjugating enzyme. (nottingham.ac.uk)
  • This tagging system involves the concerted action of an ubiquitin-activating enzyme (El), an ubiquitin-conjugating enzyme (E2), and an ubiquitin ligase (E3), with the latter two being involved in achieving target specificity. (ubc.ca)
  • Covalent modification of proteins by ubiquitin (Ub) and ubiquitin-like modifiers (Ubls) regulates many cellular functions in eukaryotes. (semanticscholar.org)
  • There is an entirely family of proteins that interact with proteins in a similar way, which is referred to as ubiquitin-like modifiers. (news-medical.net)
  • Ubiquitin-like modifiers may produce similar results to ubiquitin although in some cases they can be distinctly different. (news-medical.net)
  • E1 is also found to form complexes with ubiquitin conjugating enzymes and E3s [ 17 ]. (nottingham.ac.uk)
  • The protein interacts with its cognate ubiquitin-conjugating enzyme (E2), Ube2g2, via its RING domain and a unique region called G2BR that strongly binds to E2. (rsc.org)
  • New E2 enzymes from a growing variety of species are being discovered all the time. (nottingham.ac.uk)
  • To aid in your search, use the filters on the left to focus search results based on target family, species reactivity, and antibody conjugates for detection. (biocompare.com)
  • Though little is currently known about Lys11-linked ubiquitin chains, recent data indicate that they may be as abundant as Lys48 linkages and may be involved in vital cellular processes. (nature.com)
  • Our data highlight the intrinsic specificity of the ubiquitin system that extends to Lys11-linked chains and emphasize that differentially linked polyubiquitin chains must be regarded as independent post-translational modifications. (nature.com)
  • Pickart, C. M. Ubiquitin in chains. (nature.com)
  • Although other ubiquitin-like proteins have the potential to form polymeric chains their identification in vivo is challenging and their functional role is unclear. (mcponline.org)
  • RNF8 E3 Ubiquitin Ligase Stimulates Ubc13 E2 Conjugating Activity That Is Essential for DNA Double Strand Break Signaling and BRCA1 Tumor Suppressor Recruitment. (expasy.org)
  • Notably, ERAdP interacts with ubiquitin-conjugating enzyme 13 (Ubc13) to potentiate its charging activity. (jimmunol.org)
  • The mitotic E2 enzyme UbcH10 partners with the anaphase-promoting complex/cyclosome (APC/C) to ubiquitinate cell cycle regulators, targeting them for proteasomal destruction, and ensuring progression through mitosis. (news-medical.net)
  • Initially, E2s accept ubiquitin from the active-site cysteine of a ubiquitin-activating enzyme (E1) to their own active-site cysteine via a transthiolation reaction. (asm.org)
  • This modification of the active site microenvironment is likely to restrict access of ubiquitin to the active site cysteine, modulating Pex4p activity. (rug.nl)
  • A ubiquitin-conjugating enzyme that regulates the cell cycle promotes chromosome missegregation and tumor formation, according to van Ree et al. (news-medical.net)
  • A mouse strain harboring a disrupted allele of UbcM2 (the mouse counterpart of UBE2E3) with the coding sequence for β-galactosidase was used to track the developmental expression of the enzyme in murine RPE cells. (arvojournals.org)
  • We found that the cyclin selective ubiquitin conjugase murine E2-C, was up regulated in NIH3T3 cells transformed by EWS/FLI1 but not in a nontransformed NIH3T3 clone expressing EWS/FLI1. (elsevier.com)
  • Our studies on the ubiquitin conjugating enzyme, UbcH7, elucidated an atypical regulation of the cyclin dependent kinase inhibitor p27. (arvojournals.org)
  • Recently, a 20S complex, termed the anaphase-promoting complex (APC) or the cyclosome, has been genetically and biochemically identified as the cyclin-specific ubiquitin ligase (E3). (elsevier.com)
  • However, as the patterns of conjugates generated by these E2s are distinct, these enzymes may play different roles in promoting cyclin proteolysis in mitosis. (elsevier.com)
  • Ulrich, H. D. & Jentsch, S. Two RING finger proteins mediate cooperation between ubiquitin-conjugating enzymes in DNA repair. (nature.com)