All terms in GO

Label Id Description
metal chelating activity GO_0046911 [The formation of bonds from two or more atoms within the same ligand to a metal atom in complexes in which the metal is part of a ring.]
regulation of intracellular mRNA localization GO_1904580 [Any process that modulates the frequency, rate or extent of intracellular mRNA localization.]
GO_0046913 GO_0046913
recycling of RNA polymerase GO_0140182 [The process of freeing aborted or stalled RNA polymerase (RNAP), which dissociates it from nucleic acids and allows RNAP to reinitiate another transcription cycle. The freed mRNA is not used for further transcription.]
negative regulation of oskar mRNA translation GO_0007319 [Any process that stops, prevents or reduces the rate that oskar mRNAs are effectively translated into protein.]
regulation of oskar mRNA translation GO_0046011 [Any process that modulates the frequency, rate or extent of oskar mRNA translation. To ensure the localization of Oskar protein at the posterior pole of the oocyte, translation of oskar mRNA is repressed during its transport to the posterior pole and activated upon localization of the mRNA at the posterior cortex.]
obsolete intracellular transition metal ion homeostasis GO_0046916 [OBSOLETE. A homeostatic process involved in the maintenance of a steady state level of transition metal ions within a cell. A transition metal is an element whose atom has an incomplete d-subshell of extranuclear electrons, or which gives rise to a cation or cations with an incomplete d-subshell. Transition metals often have more than one valency state. Biologically relevant transition metals include vanadium, manganese, iron, copper, cobalt, nickel, molybdenum and silver.]
host-mediated activation of viral RNA-templated transcription GO_0140181 [A process in which a host organism initiates, promotes, or enhances the normal execution of viral RNA-templated transcription, the synthesis of either RNA on a RNA template.]
pole plasm protein localization GO_0007318 [Any process in which a protein is transported to, or maintained in, the oocyte pole plasm. An example of this is found in Drosophila melanogaster.]
centriole scaffold activity GO_0140180 [The binding activity of a protein that contributes to the stable formation of a centriole by forming persistent structures, or templates, upon which other centriolar proteins assemble.]
obsolete N-terminal peptidyl-glycine N-palmitoylation GO_0046918 [OBSOLETE. The covalent attachment of a palmitoyl group to a nitrogen (N) atom in an N-terminal glycine residue to form N-palmitoyl-glycine.]
triphosphoribosyl-dephospho-CoA synthase activity GO_0046917 [Catalysis of the reaction: ATP + 3-dephospho-CoA = 2'-(5''-triphosphoribosyl)-3'-dephospho-CoA + adenine.]
pectinesterase inhibitor activity GO_0046910 [Binds to and stops, prevents or reduces the activity of pectinesterase.]
obsolete intermembrane transport GO_0046909 [OBSOLETE. The directed movement of substances between any membrane of a cell, including the plasma membrane and its regions.]
(2R)-2-hydroxycarboxylate dehydrogenase activity GO_0140174 [Catalysis of the activity: a (2R)-2-hydroxycarboxylate + FAD + H+ = a 2-oxocarboxylate + FADH2.]
obsolete negative regulation of crystal formation GO_0046908 [OBSOLETE. Any process that stops, prevents, or reduces the frequency, rate or extent of the spontaneous (nonenzymatic) formation of crystals in a solution, for example, calcium oxalate crystals in urine.]
histone H2AS139pho reader activity GO_0140173 [A histone reader that recognizes a histone H2A phosphorylated at serine 139.]
histone H2A reader activity GO_0140054 [A histone reader that specifically binds either to an unmodified histone H2A or a form modified by a post-translational modification on a specific residue. The most common PTMs on histones are methylation, acetylation and phosphorylation.]
insemination GO_0007320 [The introduction of semen or sperm into the genital tract of a female.]
histone H2AT120pho reader activity GO_0140172 [A histone reader that recognizes a histone H2A phosphorylated at threonine 120.]