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The palmitoylation of peptidyl-threonine to form peptidyl-O-palmitoyl-L-threonine. The posttranslational decanoylation of peptidyl-threonine to form peptidyl-O3-decanoyl-L-threonine, typical of the protein ghrelin. The posttranslational octanoylation of peptidyl-threonine to form peptidyl-O3-octanoyl-L-threonine, typical of the protein ghrelin. The racemization of peptidyl-L-threo-threonine at the alpha-carbon to form D-allo-threonine. This is coupled with the formation of the cross-link 2-(S-L-cysteinyl)-D-allo-threonine. Keratan sulfate components are covalently linked to a core glycoprotein via O-glycosidic linkages between xylose and threonine residues. The post-translational cross-linking of a cysteine residue to an L-threonine residue to form 2-(S-L-cysteinyl)-D-allo-threonine. The formation of a C-terminal peptidyl-threonine amide by hydrolysis and oxidation of an interior Thr-Gly peptide in a secreted protein. The modification of peptidyl-threonine. The formation of (Z)-dehydrobutyrine by the posttranslational dehydration of peptidyl-threonine. The process of linking a protein to peptidoglycan via a carboxy terminal threonine carboxyl group through a pentaglycyl peptide to the lysine or diaminopimelic acid of the peptidoglycan. The formation of a protein-protein cross-link between peptidyl-threonine and peptidyl-cysteine by the synthesis of (2S,3S,4Xi,6R)-3-methyl-lanthionine sulfoxide (3-methyl-L-lanthionine sulfoxide), as found in the antibiotic actagardine. The formation of a covalent cross-link between DNA and a peptidyl-threonine residue by the formation of O-(phospho-5'-DNA)-L-threonine. The formation of a protein-protein cross-link between peptidyl-threonine and peptidyl-cysteine by the synthesis of (2S,3S,6R)-3-methyl-lanthionine (3-methyl-L-lanthionine). The posttranslational phosphorylation of peptidyl-threonine to form peptidyl-O-phospho-L-threonine. The formation of a cross-link between peptidyl-cysteine and peptidyl-threonine via the formation of S-(2-aminovinyl)-3-methyl-D-cysteine. The alteration of an amino acid residue in a peptide. The adenylylation of peptidyl-threonine to form peptidyl-O-(phospho-5'-adenosine)-L-threonine. The chemical reactions and pathways resulting in the formation of a C-terminal peptidyl-threonyl ethanolamide-linked glycosylphosphatidylinositol (GPI) anchor following hydrolysis of a threonyl-peptide bond in the carboxy-terminal region of a membrane-associated protein. The posttranslational glycosylation of protein via the O3 atom of peptidyl-threonine, forming O3-glycosyl-L-threonine; the most common forms are N-acetylgalactosaminyl, mannosyl, and galactosyl threonine. The posttranslational sulfation of peptidyl-threonine to form peptidyl-O-sulfo-L-threonine. The acetylation of the N-terminal threonine of proteins to form the derivative N-acetyl-L-threonine; catalyzed by peptide alpha-N-acetyltransferase. The deamination of N-terminal peptidyl-threonine to form peptidyl-2-oxobutanoic acid. 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


Name: peptidyl-threonine modification
Acc: GO:0018210
Aspect: Biological Process
Desc: The modification of peptidyl-threonine.
Proteins in PDR annotated with:
   This term: 0
   Term or descendants: 69 [Search]


GO:0018210 - peptidyl-threonine modification (interactive image map)

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