Terminology Service < Semantic Lookup Platform

All terms in GO

Label	Id	Description
peptide cross-linking via chondroitin 4-sulfate glycosaminoglycan	GO_0019800	[The formation of a cross-link between peptide chains mediated by a chondroitin 4-sulfate glycosaminoglycan that originates from a typical O-glycosidic link to serine of one chain; the other chain is esterified, via the alpha-carbon of its C-terminal Asp, to C-6 of an internal N-acetylgalactosamine of the glycosaminoglycan chain.]
peptidyl-serine modification	GO_0018209	[The modification of peptidyl-serine.]
peptide cross-linking	GO_0018149	[The formation of a covalent cross-link between or within protein chains.]
cyclization of asparagine involved in intein-mediated protein splicing	GO_0019801	[The cyclization of asparagine to yield an L-aspartimide (otherwise known as alpha-aminosuccinimide) residue at the C-terminus of an excised intein during protein splicing.]
asparagine metabolic process	GO_0006528	[The chemical reactions and pathways involving asparagine, 2-amino-3-carbamoylpropanoic acid.]
intein-mediated protein splicing	GO_0016539	[The removal of an internal amino acid sequence (an intein) from a protein during protein maturation; the excision of inteins is precise and the N- and C-terminal exteins are joined by a normal peptide bond. Protein splicing involves 4 nucleophilic displacements by the 3 conserved splice junction residues.]
cyclization of glutamine involved in intein-mediated protein splicing	GO_0019802	[The cyclization of glutamine to yield an L-glutamimide residue at the C-terminus of an excised intein during protein splicing.]
glutamine metabolic process	GO_0006541	[The chemical reactions and pathways involving glutamine, 2-amino-4-carbamoylbutanoic acid.]
peptidyl-aspartic acid carboxylation	GO_0019803	[The carboxylation of peptidyl-aspartic acid to form peptidyl-L-beta-carboxyaspartic acid.]
protein carboxylation	GO_0018214	[The addition of a carboxy group to a protein amino acid.]
peptidyl-aspartic acid modification	GO_0018197	[The modification of peptidyl-aspartic acid.]
obsolete quinolinate synthetase complex	GO_0019804	[OBSOLETE. A heterodimer which acts as a quinolinate synthetase; quinolinate synthetase B (L-aspartate oxidase) catalyzes the oxidation of L-aspartate to L-iminoaspartate; quinolinate synthetase A condenses L-imidoaspartate and dihydroxyacetone to quinolinate.]
quinolinate biosynthetic process	GO_0019805	[The chemical reactions and pathways resulting in the formation of quinolinate, the anion of quinolinic acid, also known as 2,3-pyridinedicarboxylic acid.]
quinolinate metabolic process	GO_0046874	[The chemical reactions and pathways involving quinolinate, the anion of quinolinic acid, also known as 2,3-pyridinedicarboxylic acid.]
pyridine-containing compound biosynthetic process	GO_0072525	[The chemical reactions and pathways resulting in the formation of a pyridine-containing compound, i.e. any compound that contains pyridine or a formal derivative thereof.]
bromide peroxidase activity	GO_0019806	[Catalysis of the reaction: 2 R-H + 2 bromide + hydrogen peroxide = 2 R-Br + 2 H2O. Enzymes with this activity often accept other halide ions as substrates, including chloride and iodide.]
peroxidase activity	GO_0004601	[Catalysis of the reaction: donor + hydrogen peroxide = oxidized donor + 2 H2O.]
GO_0019818	GO_0019818
P1 peroxisome	GO_0019819	[A subform of peroxisome that corresponds to an intermediate in a peroxisome assembly pathway, which operates by conversion of peroxisomal subforms in the direction P1, P2 -> P3 -> P4 -> P5 -> P6. P1 peroxisomes are distinguished from the other subforms on the bases of buoyant density and protein content; they contain fewer peroxisomal proteins than the other subforms.]
peroxisome	GO_0005777	[A small organelle enclosed by a single membrane, and found in most eukaryotic cells. Contains peroxidases and other enzymes involved in a variety of metabolic processes including free radical detoxification, lipid catabolism and biosynthesis, and hydrogen peroxide metabolism.]