Editing Threonine (section)

==Modifications==

The threonine residue is susceptible to numerous [[posttranslational modification]]s.<ref>{{Cite journal |last1=Walsh |first1=Christopher T. |last2=Garneau-Tsodikova |first2=Sylvie |last3=Gatto |first3=Gregory J. |date=2005-11-18 |title=Protein Posttranslational Modifications: The Chemistry of Proteome Diversifications |url=https://onlinelibrary.wiley.com/doi/10.1002/anie.200501023 |journal=Angewandte Chemie International Edition |language=en |volume=44 |issue=45 |pages=7342–7372 |doi=10.1002/anie.200501023|pmid=16267872 }}</ref><ref>{{Cite journal |last1=Millar |first1=A. Harvey |last2=Heazlewood |first2=Joshua L. |last3=Giglione |first3=Carmela |last4=Holdsworth |first4=Michael J. |last5=Bachmair |first5=Andreas |last6=Schulze |first6=Waltraud X. |date=2019-04-29 |title=The Scope, Functions, and Dynamics of Posttranslational Protein Modifications |url=https://www.annualreviews.org/content/journals/10.1146/annurev-arplant-050718-100211 |journal=Annual Review of Plant Biology |language=en |volume=70 |issue=1 |pages=119–151 |doi=10.1146/annurev-arplant-050718-100211 |pmid=30786234 |bibcode=2019AnRPB..70..119M |issn=1543-5008}}</ref> The [[hydroxyl]] [[Side chain|side-chain]] can undergo [[O-linked glycosylation|''O''-linked glycosylation]]. In addition, threonine residues undergo [[phosphorylation]] through the action of a threonine [[protein kinase|kinase]]. In its phosphorylated form, it can be referred to as phosphothreonine. Phosphothreonine has three potential coordination sites (carboxyl, amine and phosphate group) and determination of the mode of coordination between phosphorylated [[Ligand|ligands]] and [[metal]] [[Ion|ions]] occurring in an organism is important to explain the function of the phosphothreonine in biological processes.<ref>{{Cite journal | author = Jastrzab, Renata | date = 2013 | title = Studies of new phosphothreonine complexes formed in binary and ternary systems including biogenic amines and copper(II) | journal = Journal of Coordination Chemistry | volume = 66 | issue = 1 | pages = 98–113 | doi = 10.1080/00958972.2012.746678 }}</ref>