Addition of multiple ubiquitin groups to a protein, forming a ubiquitin chain.

Any recombinational process that contributes to the maintenance of proper telomeric length.

The error-free repair of a double-strand break in DNA in which the broken DNA molecule is repaired using homologous sequences. A strand in the broken DNA searches for a homologous region in an intact chromosome to serve as the template for DNA synthesis. The restoration of two intact DNA molecules results in the exchange, reciprocal or nonreciprocal, of genetic material between the intact DNA molecule and the broken DNA molecule.

Repression of transcription of telomeric DNA by altering the structure of chromatin.

The cellular process that completes DNA-templated transcription; the formation of phosphodiester bonds ceases, the RNA-DNA hybrid dissociates, and RNA polymerase releases the DNA.

The synthesis of RNA from a DNA template by RNA polymerase II (RNAP II), originating at an RNA polymerase II promoter. Includes transcription of messenger RNA (mRNA) and certain small nuclear RNAs (snRNAs).

The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of a ubiquitin group, or multiple ubiquitin groups, to the protein.

The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of a ubiquitin group, or multiple ubiquitin groups, to the protein.

Addition of a single ubiquitin group to a protein.

The modification of histones by addition of a single ubiquitin group.

The series of steps necessary to target endoplasmic reticulum (ER)-resident proteins for degradation by the cytoplasmic proteasome. Begins with recognition of the ER-resident protein, includes retrotranslocation (dislocation) of the protein from the ER to the cytosol, protein ubiquitination necessary for correct substrate transfer, transport of the protein to the proteasome, and ends with degradation of the protein by the cytoplasmic proteasome.

A mitotic cell cycle checkpoint that detects and negatively regulates progression through the G1/S transition of the cell cycle in response to DNA damage.

The cell cycle process in which double-strand breaks are generated at defined hotspots throughout the genome during meiosis I. This results in the initiation of meiotic recombination.

The conversion of DNA-damage induced single-stranded gaps into large molecular weight DNA via processes such as template switching, which does not remove the replication-blocking lesions but does not increase the endogenous mutation rate.

The conversion of DNA-damage induced single-stranded gaps into large molecular weight DNA after replication by using a specialized DNA polymerase or replication complex to insert a defined nucleotide across the lesion. This process does not remove the replication-blocking lesions and causes an increase in the endogenous mutation level. For example, in E. coli, a low fidelity DNA polymerase, pol V, copies lesions that block replication fork progress. This produces mutations specifically targeted to DNA template damage sites, but it can also produce mutations at undamaged sites.

A protein ubiquitination process in which a polymer of ubiquitin, formed by linkages between lysine residues at position 63 of the ubiquitin monomers, is added to a protein. K63-linked ubiquitination does not target the substrate protein for degradation, but is involved in several pathways, notably as a signal to promote error-free DNA postreplication repair.

The conversion of DNA-damage induced single-stranded gaps into large molecular weight DNA after replication by using a specialized DNA polymerase or replication complex to insert a defined nucleotide across the lesion. This process does not remove the replication-blocking lesions but does not causes an increase in the endogenous mutation level. For S. cerevisiae, RAD30 encodes DNA polymerase eta, which incorporates two adenines. When incorporated across a thymine-thymine dimer, it does not increase the endogenous mutation level.

The chemical reactions and pathways resulting in the breakdown of a protein or peptide covalently tagged with ubiquitin, via the N-end rule pathway. In the N-end rule pathway, destabilizing N-terminal residues (N-degrons) in substrates are recognized by E3 ligases (N-recognins), whereupon the substrates are linked to ubiquitin and then delivered to the proteasome for degradation.

The chemical reactions and pathways resulting in the breakdown of misfolded proteins in the cytoplasm, which are targeted to cytoplasmic proteasomes for degradation.

Any process that modulates the rate, frequency or extent of dipeptide transport. Dipeptide transport is the directed movement of a dipeptide, a combination of two amino acids by means of a peptide (-CO-NH-) link, into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.

A stress-inducible protein catabolic pathway that promotes protein quality control by accelerating the degradation of misfolded ER membrane and cytosolic proteins, as well as native proteins. The pathway starts with the activation, by stress, of the Nma111p/Ynm3p serine protease, which cleaves the stress-induced hydrophilin Roq1p, resulting in the generation of a Roq1p cleavage product that selectively interacts with Ubr1p, an E3 ubiquitin ligase. Interaction with the Ubr1p type-1 substrate binding site reprograms the substrate specificity of this ubiquitin ligase resulting in the selective proteasome-mediated degradation of misfolded and native proteins. The pathway ends with degradation of the protein by the cytoplasmic proteasome. Currently, NMA111, ROQ1, UBR1, RAD6, and CDC48 are considered to be involved in this quality control pathway.

Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating damage to its DNA from environmental insults or errors during metabolism.

The process in which a multicellular organism, a unicellular organism or a group of unicellular organisms grow in a threadlike, filamentous shape.

Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an ultraviolet radiation (UV light) stimulus. Ultraviolet radiation is electromagnetic radiation with a wavelength in the range of 10 to 380 nanometers.

Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an ultraviolet radiation (UV light) stimulus. Ultraviolet radiation is electromagnetic radiation with a wavelength in the range of 10 to 380 nanometers.

Any process that results in the specification, formation or maintenance of the physical structure of eukaryotic chromatin.

The assembly of DNA, histone proteins, other associated proteins, and sometimes RNA, into chromatin structure, beginning with the formation of the basic unit, the nucleosome, followed by organization of the nucleosomes into higher order structures, ultimately giving rise to a complex organization of specific domains within the nucleus.

Any process that stops, prevents, or reduces the frequency, rate or extent of chromatin silencing at telomeres.

The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of ubiquitin, and mediated by the proteasome.

Any process that modulates the frequency, rate or extent of the covalent addition of a methyl group to the lysine at position 4 of histone H3.

Any process that decreases the frequency, rate, or extent of chromatin silencing at silent mating-type cassette. Chromatin silencing at silent mating-type cassette is the repression of transcription at silent mating-type loci by altering the structure of chromatin.

Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating increased oxygen tension.

A histone ubiquitination process in which a ubiquitin monomer is added to a conserved lysine residue in the C-terminus of histone H2B. The conserved lysine residue is K119 in fission yeast, K123 in budding yeast, or K120 in mammals.

A histone ubiquitination process in which a ubiquitin monomer is added to a conserved lysine residue in the C-terminus of histone H2B. The conserved lysine residue is K119 in fission yeast, K123 in budding yeast, or K120 in mammals.

Any process in which the proteasome is transported to, or maintained at the nuclear periphery.

Any process that stops, prevents or reduces the frequency, rate or extent of the SREBP signaling pathway.

A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.

All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.

A ubiquitin ligase complex found to be involved in post-replicative bypass of UV-damaged DNA and UV mutagenesis. In S. cerevisiae, the complex contains the ubiquitin conjugating enzyme Rad6 and Rad18, a protein containing a RING finger motif and a nucleotide binding motif. The yeast Rad6-Rad18 heterodimer has ubiquitin conjugating activity, binds single-stranded DNA, and possesses single-stranded DNA-dependent ATPase activity.

A ubiquitin ligase complex consisting of UBR1 and RAD6 components. It polyubiquitinates proteins containing non-acetylated N-terminal residues causing their subsequent degradation by the proteasome as part of the Ac/N-End Rule pathway. It recognizes non-acetylated N-terminal methionine if it is followed by a hydrophobic residue. Additionally, it acts in an N-end rule independent manner as a component of a novel quality control pathway for proteins synthesized on cytosolic ribosomes.

A ubiquitin ligase complex consisting of UBR1 and RAD6 components. It polyubiquitinates proteins containing non-acetylated N-terminal residues causing their subsequent degradation by the proteasome as part of the Ac/N-End Rule pathway. It recognizes non-acetylated N-terminal methionine if it is followed by a hydrophobic residue. Additionally, it acts in an N-end rule independent manner as a component of a novel quality control pathway for proteins synthesized on cytosolic ribosomes.

A ubiquitin ligase complex consisting of MUB1, RAD6 and UBR2 components. It ubiquitinates, and targets for destruction, the RPN4 transcription factor, which upregulates the proteasome genes. The binding of MUB1 may position the RPN4 ubiquitylation site proximal to the Ubiquitin-RAD6 thioester and allow the transfer of Ubiquitin from RAD6 to RPN4. One of its components, MUB1, is a short-lived protein ubiquitinated by the UBR2-RAD6 ubiquitin conjugating enzyme.

The ordered and organized complex of DNA, protein, and sometimes RNA, that forms the chromosome in the nucleus.

A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.

The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.

A ubiquitin-conjugating enzyme complex that contains two RING finger proteins, which have ubiquitin ligase activity, in addition to a protein with ubiquitin-conjugating enzyme activity; catalyzes the ubiquitination of histone H2B at lysine 119 (or the equivalent residue). In Schizosaccharomyces the subunits are Rhp1, Brl2/Rfp1 and Brl1/Rfp2.