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The addition of biotin (vitamin B7 / vitamin H) to a protein amino acid. The removal of a ubiquitin-like protein of the NEDD8 type from a protein. The formation of a cluster of several metal atoms, including manganese or calcium, with one or more bridging (mu-bond) oxygen atoms; amino acids residues in proteins that may ligate the metal oxygen cluster are histidine, aspartate, and glutamate. The removal of one or more ubiquitin moieties from a protein. The addition of a halogen to a protein amino acid. Covalent attachment of the ubiquitin-like protein UFM1 to another protein. The addition of a carbamoyl group to a protein amino acid. A carbamoyl group is the acyl group -CO-NH2. The addition of a nucleotide to a protein amino acid. The addition of a flavin group to a protein amino acid. The addition of a nitrosyl group to a protein amino acid. Chemical reaction, between proteins and reactive oxygen species, that occurs in dividing cells as they age and leads to a variety of changes in the affected proteins, including increases in protein carbonyl content, oxidized methionine, protein hydrophobicity, and cross-linking. Covalent attachment of the ubiquitin-like protein NEDD8 (RUB1) to another protein. The process by which a SUMO protein (small ubiquitin-related modifier) is cleaved from its target protein. The covalent addition to a protein of ISG15, a ubiquitin-like protein. The process by which a SUMO protein (small ubiquitin-related modifier) is conjugated to a target protein via an isopeptide bond between the carboxyl terminus of SUMO with an epsilon-amino group of a lysine residue of the target protein. A transamidation reaction that results in the cleavage of the polypeptide chain and the concomitant transfer of the GPI anchor to the newly formed carboxy-terminal amino acid of the anchored protein. The cleaved C-terminal contains the C-terminal GPI signal sequence of the newly synthesized polypeptide chain. The covalent linking of a cofactor to a protein. The modification of a protein amino acid by phosphopantetheinylation. The breakage of covalent or non-covalent bonds to detach lipid moieties from a protein. The addition of a carboxy group to a protein amino acid. The addition of an ester group to a protein amino acid. The modification of part of an enzyme to form the active site. The addition of a hydroxy group to a protein amino acid. The covalent addition to a protein of Smt3, a ubiquitin-like protein. The posttranslational conjugation of arginine to the N-terminal aspartate or glutamate of a protein; required for the degradation of the protein via the ubiquitin pathway. The chemical reactions and pathways involving a specific protein, rather than of proteins in general, occurring at the level of an individual cell. Includes protein modification. The covalent alteration of one or more amino acids occurring in a protein after the protein has been completely translated and released from the ribosome. The modification of a protein by cis-trans isomerization of a proline residue. The process by which one or more ubiquitin moieties are added to a protein. The covalent alteration of one or more amino acid residues within the CAAX box region of CAAX box proteins. The addition of a tyrosine molecule to a protein amino acid. The posttranslational addition of glycyl units covalently bound to the gamma carboxyl group peptidyl-glutamic acid. The transfer, from NAD, of ADP-ribose to protein amino acids. The covalent or noncovalent linking of a chromophore to a protein. The modification of a protein by amino acid glucuronidation. The process of removing one or more phosphoric residues from a protein. null The process by which a Pup protein is conjugated to a target protein via an isopeptide bond between the carboxyl terminus of Pup and the epsilon-amino group of a lysine residue of the target protein. The modification of a protein amino acid by oxidation. The process of removing one or more ADP-ribose residues from a protein. The addition of a sulfate group as an ester to a protein amino acid. The removal of an acetyl group from a protein amino acid. An acetyl group is CH3CO-, derived from acetic [ethanoic] acid. Covalent modification of an actin molecule. The modification of a protein amino acid by succinylation. The covalent alteration of one or more amino acid residues within a histone protein. Covalent attachment of the ubiquitin-like protein URM1 to another protein. The incorporation of a metal into a metallo-molybdopterin complex. The incorporation of exogenous sulfur into a metallo-sulfur cluster. The modification of a protein amino acid by polyamination. The formation of a covalent cross-link between or within protein chains. The removal of a sulfur group from a protein amino acid. The covalent linking of a tetrapyrrole to a protein. The formation of a cluster of several metal atoms, including iron, nickel, molybdenum, vanadium, or copper, with one or more bridging (mu-bond) sulfur atoms; amino acids residues in proteins that may ligate the metal sulfur cluster are cysteine, histidine, aspartate, glutamate, serine and cysteine persulfide. Oxidation of two organic sulfhydryl groups (thiols) by a disulfide compound to form a disulfide bond. The formation of a covalent cross-link between a nucleic acid and a protein. The process of introducing a phosphate group on to a protein. The covalent alteration of one or more monomeric units in a polypeptide, polynucleotide, polysaccharide, or other biological macromolecule, resulting in a change in its properties. 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. The removal of a water group from a protein amino acid. The removal of an alkyl group from a protein amino acid. An alkyl group is any group derived from an alkane by removal of one hydrogen atom. The covalent alteration of one or more amino acids occurring in proteins, peptides and nascent polypeptides (co-translational, post-translational modifications). Includes the modification of charged tRNAs that are destined to occur in a protein (pre-translation modification).

View Gene Ontology (GO) Term

GO TERM SUMMARY

Name: post-translational protein modification
Acc: GO:0043687
Aspect: Biological Process
Desc: The covalent alteration of one or more amino acids occurring in a protein after the protein has been completely translated and released from the ribosome.
Synonyms:
  • posttranslational amino acid modification
  • posttranslational modification
  • posttranslational protein modification
  • PTM
  • post-translational modification
  • post-translational amino acid modification
Proteins in PDR annotated with:
   This term: 151 [Search]
   Term or descendants: 7755 [Refine Search]


[geneontology.org]
INTERACTIVE GO GRAPH

GO:0043687 - post-translational protein modification (interactive image map)

YRC Informatics Platform - Version 3.0
Created and Maintained by: Michael Riffle