Sites of phosphorylation on the CTD serve as a recognition or anchor point for other proteins to dock with the polymerase. The capping enzyme (guanylyl transferase), which adds the G residue to the 5' end of newly synthesized mRNA, binds to CTD phosphorylated at serine 5, the first phosphorylation event catalyzed by TFIIH. 

P-TEFb leads to recruitment of a set of proteins called SCAFs to the CTD, and they in turn bind to splicing factors. This may be a means of coordinating transcription and splicing.

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#Unit 1. Molecules and their Interaction Relevant to Biology

Glu–Cys–Gly peptide in which the γ-carboxylate group of the glutamate side chain forms an isopeptide bond.

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#Unit 1. Molecules and their Interaction Relevant to Biology

Cysteine, tryptophan, and methionine are not common amino acids: together, they constitute approximately 5 percent of the amino acids in a typical protein. Four amino acids—leucine, serine, lysine, and glutamic acid—are the most abundant amino acids, constituting 32 percent of all the residues in a typical protein.

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#Unit 1. Molecules and their Interaction Relevant to Biology

Aspartate: P type ATPase and two component signalling.

Asparagine: N linked Glycosylation.

Cysteine- Fd-Trx system, PDI, G3PD, Hh, 

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#Unit 1. Molecules and their Interaction Relevant to Biology

Glycine: Most conserved, G12 Ras, RGD, FG, 

Glutamine: NPQ, CAG repeat

GlutamatE: Neurotransmitter, VGLUT, Calmodulin, Nitrogen Assimilation

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#Id: 8060

#Unit 1. Molecules and their Interaction Relevant to Biology

Histidine: Two component signalling, C2H2 zinc finger, Hemoglobin, His6-NiNTA column.

Isoleucine: AATS proofreading, RTK

Leucine: Toll like receptors, LRR, 

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#Id: 8061

#Unit 1. Molecules and their Interaction Relevant to Biology

Lysine: Histones modification, Ubiquitin, Rubisco, pyrrolysine -UAG

Methionine: N-formylmethionine, S-adenosylmethionine, ethylene, Succinyl-CoA

Phenylalanine- F506, Chymotrypsin, phenylalanine hydroxylase