All terms in GO
| Label | Id | Description |
|---|---|---|
| obsolete solute:solute exchange | GO_0030180 |
OBSOLETE. Exchange diffusion of two solutes between the inside and outside of a cell or subcellular compartment, in which movement of one solute down a concentration gradient drives movement of the other solute in the opposite direction.
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| obsolete sodium:calcium exchange | GO_0030181 |
OBSOLETE. Exchange diffusion sodium and calcium ions in which influx of sodium ions to the cytosol drives the efflux of calcium ions from the cell.
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| neuron differentiation | GO_0030182 |
The process in which a relatively unspecialized cell acquires specialized features of a neuron.
|
| peptidyl-glycine cholesteryl ester biosynthesis from peptidyl-glycine | GO_0019708 |
The synthesis of peptidyl-glycine cholest-5-en-3-beta-ol ester at the carboxy-terminus of autolytically cleaved proteins.
|
| cholesterol metabolic process | GO_0008203 |
The chemical reactions and pathways involving cholesterol, cholest-5-en-3 beta-ol, the principal sterol of vertebrates and the precursor of many steroids, including bile acids and steroid hormones. It is a component of the plasma membrane lipid bilayer and of plasma lipoproteins and can be found in all animal tissues.
|
| C-terminal protein lipidation | GO_0006501 |
The covalent attachment of a lipid group to the carboxy-terminus of a protein.
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| peptidyl-glycine modification | GO_0018201 |
The modification of peptidyl-glycine.
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| cellular modified amino acid biosynthetic process | GO_0042398 |
The chemical reactions and pathways resulting in the formation of compounds derived from amino acids, organic acids containing one or more amino substituents.
|
| iron incorporation into iron-sulfur cluster via pentakis-L-cysteinyl L-histidino nickel tetrairon pentasulfide | GO_0019709 |
The incorporation of iron into a nickel-iron-sulfur cluster via pentakis-L-cysteinyl L-histidino nickel tetrairon pentasulfide, found in carbon monoxide dehydrogenase.
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| iron incorporation into metallo-sulfur cluster | GO_0018283 |
The incorporation of iron into a metallo-sulfur cluster.
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| peptidyl-histidine modification | GO_0018202 |
The modification of peptidyl-histidine.
|
| peptidyl-cysteine modification | GO_0018198 |
The modification of peptidyl-cysteine.
|
| organic phosphonate catabolic process | GO_0019700 |
The chemical reactions and pathways resulting in the breakdown of phosphonates, any organic compound containing one or more C-PO(OH)2 or C-PO(OR)2 (with R=alkyl, aryl) groups. Catabolism of phosphonic acid itself, an inorganic compound without the biochemically relevant C-P bond, is not included.
|
| organophosphate catabolic process | GO_0046434 |
The chemical reactions and pathways resulting in the breakdown of organophosphates, any phosphate-containing organic compound.
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| organic phosphonate metabolic process | GO_0019634 |
The chemical reactions and pathways involving phosphonates, any organic compounds containing one or more C-PO(OH)2 or C-PO(OR)2 (with R=alkyl, aryl) groups. Metabolism of phosphonic acid itself, an inorganic compound without the biochemically relevant C-P bond, is not included.
|
| peptidyl-arginine N5-methylation | GO_0019701 |
The methylation of peptidyl-arginine on the internal nitrogen-5 (N5) atom (also called delta-nitrogen) to form peptidyl-N5-methyl-L-arginine.
|
| peptidyl-arginine N-methylation | GO_0035246 |
The addition of a methyl group onto a nitrogen atom of an arginine residue in a protein.
|
| protein-arginine N5-methyltransferase activity | GO_0019702 |
Catalysis of the transfer of a methyl group from S-adenosyl-L-methionine to the delta-nitrogen atom of peptidyl-arginine residues. The reaction is S-adenosyl-L-methionine + [protein]-L-arginine = S-adenosyl-L-homocysteine + [protein]-N5-methyl-L-arginine.
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| protein-arginine N-methyltransferase activity | GO_0016274 |
Catalysis of the reaction: S-adenosyl-L-methionine + (protein)-arginine = S-adenosyl-L-homocysteine + (protein)-N-methyl-arginine.
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| coenzyme A-peptidyl-cysteine covalent linking | GO_0019703 |
The covalent linkage of coenzyme A and peptidyl-cysteine to form L-cysteine coenzyme A disulfide.
|