Terminology Service < Semantic Lookup Platform

All terms in GO

Label	Id	Description
replisome	GO_0030894	[A multi-component enzymatic machine at the replication fork which mediates DNA replication. Includes DNA primase, one or more DNA polymerases, DNA helicases, and other proteins.]
periciliary membrane compartment	GO_1990075	[A plasma membrane region adjacent to the base of eukaryotic cilia and flagella that is enriched in endocytosis-associated proteins and vesicles and that appears to regulate ciliary membrane homeostasis.]
cell wall polysaccharide catabolic process involved in abscission	GO_1990076	[Any cell wall polysaccharide catabolic process that is involved in abscission.]
perforation plate	GO_1990073	[A cell wall part that is the part of a wall of a vessel member and bears one or more openings (perforations).]
polyuridylation-dependent mRNA catabolic process	GO_1990074	[The chemical reactions and pathways resulting in the breakdown of a messenger RNA (mRNA) molecule, initiated by the enzymatic addition of a sequence of uridylyl residues (polyuridylation) at the 3' end of the target mRNA.]
modification-dependent macromolecule catabolic process	GO_0043632	[The chemical reactions and pathways resulting in the breakdown of a macromolecule, initiated by covalent modification of the target molecule.]
mRNA catabolic process	GO_0006402	[The chemical reactions and pathways resulting in the breakdown of mRNA, messenger RNA, which is responsible for carrying the coded genetic 'message', transcribed from DNA, to sites of protein assembly at the ribosomes.]
TRAPPII protein complex	GO_1990071	[A complex that mediates intra-Golgi traffic, Golgi exit, endosome-to-Golgi traffic, and the trafficking of autophagy proteins from Golgi to the phagophore assembly site. Binds to a component of the COPI coat. In yeast it includes the following subunits: Bet3 (as homodimer), Bet5, Tca17, Trs20, Trs23, Trs31, Trs33, Trs65, Trs120, Trs130. The whole complex is thought to dimerize with itself.]
TRAPPIII protein complex	GO_1990072	[A complex that functions in anterograde transport at the Golgi and also regulates autophagy. In yeast it includes at least the following subunits: Bet3 (as homodimer), Bet5, Trs20, Trs23, Trs31, Trs33, Trs85. TRAPPIII may include further, as yet undescribed, proteins.]
TRAPPI protein complex	GO_1990070	[A complex that tethers COPII vesicles at ER-Golgi intermediate compartment. Its role in this part of the vesicular transport may start at the ER exit sites. Binds to a component of the COPII coat. In yeast it includes the following subunits: Bet3 (as homodimer), Bet5, Trs20, Trs23, Trs31, Trs33 which are regarded as the "core subunits" of all TRAPP complexes in yeast.]
endoplasmic reticulum-Golgi intermediate compartment	GO_0005793	[A complex system of membrane-bounded compartments located between endoplasmic reticulum (ER) and the Golgi complex, with a distinctive membrane protein composition; involved in ER-to-Golgi and Golgi-to-ER transport.]
pre-primosome complex	GO_1990099	[Any of the protein-DNA complexes that contain a DNA helicase and associated protein(s) at the origin of replication, and build up to assembling the core primosome. The associated protein(s) chaperone the helicase to the DNA, and assembly of the pre-primosome is essential for the initiation or restart of replication. Pre-primosome complexes lack a primase component.]
SeqA-DNA complex	GO_1990097	[A protein-DNA complex that contains an oligomer of SeqA bound to GATC sites in methylated or newly-synthesized, hemi-methylated double-stranded DNA, with preference for the latter. Binding of SeqA to hemimethylated DNA sequesters oriC, prevents re-methylation of DNA by Dam and in turn stops premature re-initiation of replication during one replication cycle.]
core primosome complex	GO_1990098	[A protein-DNA complex containing at least one DNA helicase and one primase. Can also contain associated proteins. The helicase component continues to unwind the double-stranded DNA (dsDNA) and the primase component synthesizes a RNA primer during initiation or restart of replication.]
positive regulation of transcription from RNA polymerase II promoter in response to reactive oxygen species	GO_1990095	[Any process that increases the frequency, rate or extent of transcription from an RNA polymerase II promoter as a result of a reactive oxygen species stimulus. Reactive oxygen species include singlet oxygen, superoxide, and oxygen free radicals.]
positive regulation of transcription from RNA polymerase II promoter in response to oxidative stress	GO_0036091	[Any process that increases the frequency, rate or extent of transcription from an RNA polymerase II promoter as a result of a stimulus indicating the organism is under oxidative stress, a state often resulting from exposure to high levels of reactive oxygen species, e.g. superoxide anions, hydrogen peroxide (H2O2), and hydroxyl radicals.]
cellular response to reactive oxygen species	GO_0034614	[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 reactive oxygen species stimulus. Reactive oxygen species include singlet oxygen, superoxide, and oxygen free radicals.]
positive regulation of transcription from RNA polymerase II promoter in response to superoxide	GO_1990096	[Any process that increases the frequency, rate or extent of transcription from an RNA polymerase II promoter as a result of a superoxide stimulus. Superoxide is the anion, oxygen-, formed by addition of one electron to dioxygen (O2) or any compound containing the superoxide anion.]
obsolete negative regulation of N-methyl-D-aspartate receptor clustering	GO_1990093	[OBSOLETE. The negative regulation of the receptor clustering process in which N-methyl-D-aspartate (NMDA) receptors are localized to distinct domains in the cell membrane.]
obsolete positive regulation of N-methyl-D-aspartate receptor clustering	GO_1990094	[OBSOLETE. The positive regulation of the receptor clustering process in which N-methyl-D-aspartate (NMDA) receptors are localized to distinct domains in the cell membrane.]