All terms in GO
| Label | Id | Description |
|---|---|---|
| dephosphorylation | GO_0016311 | [The process of removing one or more phosphoric (ester or anhydride) residues from a molecule.] |
| GO_0006472 | GO_0006472 | |
| N-terminal protein amino acid modification | GO_0031365 | [The alteration of the N-terminal amino acid residue in a protein.] |
| internal protein amino acid acetylation | GO_0006475 | [The addition of an acetyl group to a non-terminal amino acid in a protein.] |
| protein sulfation | GO_0006477 | [The addition of a sulfate group as an ester to a protein amino acid.] |
| sulfation | GO_0051923 | [The addition of a sulfate group to a molecule.] |
| gas vesicle | GO_0031411 | [An intracellular non-membrane-bounded organelle; a hollow structure made of protein, which usually has the form of a cylindrical tube closed by conical end caps. By regulating their relative gas vesicle content, aquatic microbes are able to perform vertical migrations.] |
| peptidyl-tyrosine sulfation | GO_0006478 | [The sulfation of peptidyl-tyrosine residues to form peptidyl-O4'-sulfo-L-tyrosine.] |
| protein methylation | GO_0006479 | [The addition of a methyl group to a protein amino acid. A methyl group is derived from methane by the removal of a hydrogen atom.] |
| protein alkylation | GO_0008213 | [The addition of an alkyl group to a protein amino acid. An alkyl group is any group derived from an alkane by removal of one hydrogen atom.] |
| macromolecule methylation | GO_0043414 | [The covalent attachment of a methyl residue to one or more monomeric units in a polypeptide, polynucleotide, polysaccharide, or other biological macromolecule.] |
| gas vesicle organization | GO_0031412 | [A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a gas vesicle. A gas vesicle is a hollow structure made of protein, which usually has the form of a cylindrical tube closed by conical end caps.] |
| regulation of buoyancy | GO_0031413 | [Any process that modulates an organism's tendency or ability to rise or float in a fluid medium such as water or air, often through the use of stored gases.] |
| N-terminal protein acetyltransferase complex | GO_0031414 | [A complex that catalyzes the transfer of an acetyl group to the N-terminal residue of a protein acceptor molecule.] |
| NatA complex | GO_0031415 | [A conserved complex that catalyzes the transfer of an acetyl group to an N-terminal Ser, Ala, Gly, or Thr residue of a protein acceptor molecule. In Saccharomyces the complex includes Nat1p and Ard1p, and may contain additional proteins.] |
| NatB complex | GO_0031416 | [A conserved complex that catalyzes the transfer of an acetyl group to the N-terminal residue of a protein acceptor molecule that has a Met-Glu, Met-Asp, Met-Asn, or Met-Met N-terminus. In Saccharomyces the complex includes Nat3p and Mdm20p.] |
| NatC complex | GO_0031417 | [A conserved complex that catalyzes the transfer of an acetyl group to the N-terminal residue of a protein acceptor molecule that has a Met-Ile, Met-Leu, Met-Trp, or Met-Phe N-terminus. In Saccharomyces the complex includes Mak3p, Mak10p, and Mak31p.] |
| L-ascorbic acid binding | GO_0031418 | [Interacting selectively and non-covalently with L-ascorbic acid, (2R)-2-[(1S)-1,2-dihydroxyethyl]-4-hydroxy-5-oxo-2,5-dihydrofuran-3-olate; L-ascorbic acid is vitamin C and has co-factor and anti-oxidant activities in many species.] |
| cobalamin binding | GO_0031419 | [Interacting selectively and non-covalently with cobalamin (vitamin B12), a water-soluble vitamin characterized by possession of a corrin nucleus containing a cobalt atom.] |
| N-terminal protein amino acid methylation | GO_0006480 | [The methylation of the N-terminal amino acid of a protein.] |