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The formation of the fluorescent protein FP583 chromophore cross-link from the alpha-carboxyl carbon of residue n, a glutamine, to the alpha-amino nitrogen of residue n+2, a glycine, and a dehydration to form a double bond to the alpha-amino nitrogen of residue n+1. This cross-linking is coupled with a dehydrogenation of residue n+1 to form a double bond between the alpha and beta carbons. The formation of a 2-keto-5-iminopiperazine protein chromophore cross-link from the alpha-amino nitrogen of residue n, a methionine, to the alpha-carboxyl carbon of residue n+1, a tyrosine, and a dehydration to form a double bond to the alpha-amino nitrogen of residue n+2. This cross-linking is coupled with a dehydrogenation of residue n+1 to form a double bond between the alpha and beta carbons. The formation of the non-fluorescent protein chromophore cross-link from the alpha-carboxyl carbon of residue n, a glutamic acid, to the alpha-amino nitrogen of residue n+2, a glycine, and a dehydration to form a double bond to the alpha-amino nitrogen of residue n+1. This cross-linking is coupled with a dehydrogenation of residue n+1 to form a double bond between the alpha and beta carbons. This modification is found in the GFP-like non-fluorescent red chromoprotein from the sea anemone Radianthus macrodactylus. The formation of the fluorescent protein FP611 chromophore cross-link from the alpha-carboxyl carbon of residue n, a methionine, to the alpha-amino nitrogen of residue n+2, a glycine, and a dehydration to form a double bond to the alpha-amino nitrogen of residue n+1. This cross-linking is coupled with a dehydrogenation of residue n+1 to form a double bond between the alpha and beta carbons. This modification is found in the GFP-like fluorescent chromoprotein from the sea anemone Entacmaea quadricolor. The formation of a 2-tetrahydropyridinyl-5-imidazolinone protein chromophore cross-link from the alpha-carboxyl carbon of residue n, a lysine, to the alpha-amino nitrogen of residue n+2, a glycine, and a dehydration to form a double bond to the alpha-amino nitrogen of residue n+1. This cross-linking is coupled with a dehydrogenation of residue n+1 to form a double bond between the alpha and beta carbons. In addition, the residue N lysine undergoes cyclization. The alpha-amino nitrogen is replaced by the epsilon-amino nitrogen, the peptide chain is broken, residue N-1 is released as an amide, and a double bond is formed between the alpha-carbon and the nitrogen so that a tetrahydropyridine ring results. This modification is found in the GFP-like fluorescent chromoprotein FP538 from the sea anemone Zoanthus species. The formation of a fluorescent protein chromophore cross-link from the alpha-carboxyl carbon of residue n, a lysine, to the alpha-amino nitrogen of residue n+2, a glycine, and a dehydration to form a double bond to the alpha-amino nitrogen of residue n+1. This cross-linking is coupled with a dehydrogenation of residue n+1 to form a double bond between the alpha and beta carbons. The covalent or noncovalent linking of a chromophore to a protein. The posttranslation modification of peptidyl-lysine to form N6-retinal-L-lysine. The posttranslation modification of peptidyl-lysine to form N6-3,4-didehydroretinylidene-L-lysine. The formation of the green fluorescent protein chromophore cross-link from the alpha-carboxyl carbon of residue n, a serine, to the alpha-amino nitrogen of residue n+2, a glycine, and a dehydration to form a double bond to the alpha-amino nitrogen of residue n+1. This cross-linking is coupled with a dehydrogenation of residue n+1 to form a double bond between the alpha and beta carbons. The synthesis of the chromophore S-4-hydroxycinnamyl-L-cysteine. The covalent linking of a chromophore to a protein via peptidyl-cysteines. 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). The formation of the fluorescent protein FP506 chromophore cross-link from the alpha-carboxyl carbon of residue n, an asparagine, to the alpha-amino nitrogen of residue n+2, a glycine, and a dehydration to form a double bond to the alpha-amino nitrogen of residue n+1. This cross-linking is coupled with a dehydrogenation of residue n+1 to form a double bond between the alpha and beta carbons. 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.

View Gene Ontology (GO) Term

GO TERM SUMMARY
Name: protein-chromophore linkage
Acc: GO:0018298
Aspect: Biological Process
Desc: The covalent or noncovalent linking of a chromophore to a protein.
Proteins in PDR annotated with:
   This term: 48 [Search]
   Term or descendants: 48 [Search]


[geneontology.org]
INTERACTIVE GO GRAPH

GO:0018298 - protein-chromophore linkage (interactive image map)
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