All terms in GO

Label Id Description
ribonuclease IX activity GO_0033896 [Catalysis of the endonucleolytic cleavage of poly(U) or poly(C) to fragments terminated by 3'-hydroxy and 5'-phosphate groups.]
daunorubicin transport GO_0043215 [The directed movement of daunorubicin, an anthracycline antibiotic produced by Streptomyces coeruleorubidus or S. peucetius and used as an antineoplastic into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.]
protein N-linked glycosylation via asparagine GO_0018279 [The glycosylation of protein via the N4 atom of peptidyl-asparagine forming N4-glycosyl-L-asparagine; the most common form is N-acetylglucosaminyl asparagine; N-acetylgalactosaminyl asparagine and N4 glucosyl asparagine also occur. This modification typically occurs in extracellular peptides with an N-X-(ST) motif. Partial modification has been observed to occur with cysteine, rather than serine or threonine, in the third position; secondary structure features are important, and proline in the second or fourth positions inhibits modification.]
obsolete N-terminal peptidyl-threonine deamination GO_0018278 [OBSOLETE. The deamination of N-terminal peptidyl-threonine to form peptidyl-2-oxobutanoic acid.]
protein deamination GO_0018277 [The removal of an amino group from a protein amino acid.]
obsolete homotaurine:2-oxoglutarate aminotransferase activity GO_0102081 [OBSOLETE. Catalysis of the reaction: homotaurine + 2-oxoglutarate(2-) = 3-sulfopropanal + L-glutamate(1-).]
obsolete isopeptide cross-linking via N6-glycyl-L-lysine GO_0018276 [OBSOLETE. The formation of an isopeptide cross-link between peptidyl-lysine and peptidyl-glycine to produce N6-glycyl-L-lysine. This is distinct from the formation of the thiolester intermediate, which occurs during ubiquitination.]
phenylacetyl-coenzyme A:glycine N-acyltransferase activity GO_0102080 [Catalysis of the reaction: phenylacetyl-CoA + glycine = H+ + phenylacetylglycine + coenzyme A.]
obsolete N-terminal peptidyl-cysteine acetylation GO_0018275 [OBSOLETE. The acetylation of the N-terminal cysteine of proteins to form the derivative N-acetyl-L-cysteine.]
obsolete peptide cross-linking via L-lysinoalanine GO_0018274 [OBSOLETE. The modification of peptidyl-lysine and peptidyl-serine to form a (2Xi,9S)-L-lysinoalanine cross-link.]
obsolete protein-chromophore linkage via peptidyl-N6-retinal-L-lysine GO_0018273 [OBSOLETE. The modification of peptidyl-lysine to form N6-retinal-L-lysine.]
obsolete OPC6-trans-2-enoyl-CoA hydratase activity GO_0102074 [OBSOLETE. Catalysis of the reaction: OPC6-3-hydroxyacyl-CoA = OPC6-trans-2-enoyl-CoA + H2O.]
iron incorporation into metallo-sulfur cluster GO_0018283 [The incorporation of iron into a metallo-sulfur cluster.]
obsolete OPC8-trans-2-enoyl-CoA hydratase activity GO_0102073 [OBSOLETE. Catalysis of the reaction: OPC8-3-hydroxyacyl-CoA = OPC8-trans-2-enoyl-CoA + H2O.]
obsolete 3-oxo-cis-Delta9-hexadecenoyl-[acp] reductase activity GO_0102072 [OBSOLETE. Catalysis of the reaction: NADP + a 3R-hydroxy cis Delta9-hexadecenoyl-[acp] = NADPH + H+ + a 3-oxo-cis-Delta9-hexadecenoyl-[acp].]
obsolete GSI anchor biosynthetic process via N-seryl-glycosylsphingolipidinositolethanolamine GO_0018281 [OBSOLETE. The formation of a C-terminal peptidyl-serine ethanolamide-linked glycosylsphingolipidinositol (GSI) anchor following hydrolysis of a seryl-peptide bond in the carboxy-terminal region of a membrane-associated protein.]
obsolete 9,10-epoxy-18-hydroxystearate hydrolase activity GO_0102071 [OBSOLETE. Catalysis of the reaction: 9,10-epoxy-18-hydroxystearate + H2O = 9,10,18-trihydroxystearate.]
protein S-linked glycosylation GO_0018280 [A protein glycosylation process in which a carbohydrate or carbohydrate derivative unit is added to a protein via a sulfur atom of a peptidyl-amino-acid such as cysteine or methionine.]
tuft GO_0151001 [A dense cluster of elongated, thick microvilli on the apical surface of tuft cells in epithelial tissues, such as the intestine and respiratory tract. The apical tuft extends further into the lumen than typical microvilli, featuring larger, more compact projections with unique actin cores that penetrate deep into the cytoplasm, often reaching the perinuclear region. This distinctive structure, rich in microfilaments and microtubules, supports the chemosensory functions of the cell.]
GO_0102078 GO_0102078