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Skeletal formula
Ball-and-stick model
IUPAC name
(S)-2-Amino-3-(phosphonooxy)propionic acid
407-41-0 YesY
ChEBI CHEBI:15811 YesY
ChEMBL ChEMBL284377 YesY
ChemSpider 62074 YesY
DrugBank DB04522 YesY
EC Number 206-986-0
Jmol interactive 3D Image
MeSH Phosphoserine
PubChem 106
Molar mass 185.073 g/mol
Melting point 228 °C (442 °F; 501 K)
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).
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Infobox references

Phosphoserine (abbreviated as SEP or J) is an ester of serine and phosphoric acid. Phosphoserine is a component of many proteins as the result of posttranslational modifications.[1] The phosphorylation of the alcohol functional group in serine to produce phosphoserine is catalyzed by various types of kinases.[2][3] Through the use of technologies that utilize an expanded genetic code, phosphoserine can also be incorporated into proteins during translation.[4][5][6]

It is a normal metabolite found in human biofluids.[7]

Phosphoserine has three potential coordination sites (carboxyl, amine and phosphate group) Determination of the mode of coordination between phosphorylated ligands and metal ions occurring in an organism is a first step to explain the function of the phosphoserine in bioinorganic processes.[8][9]


  1. ^ Olsen, Jesper V.; Blagoev, Blagoy; Gnad, Florian; Macek, Boris; Kumar, Chanchal; Mortensen, Peter; Mann, Matthias (2006-03-11). "Global, In Vivo, and Site-Specific Phosphorylation Dynamics in Signaling Networks". Cell 127 (3): 635–648. doi:10.1016/j.cell.2006.09.026. ISSN 0092-8674. PMID 17081983. 
  2. ^ Krebs, Edwin G. (1985-10-01). "The phosphorylation of proteins: a major mechanism for biological regulation". Biochemical Society Transactions 13 (5): 813–820. doi:10.1042/bst0130813. ISSN 0300-5127. PMID 2998902. 
  3. ^ Manning, G.; Whyte, D. B.; Martinez, R.; Hunter, T.; Sudarsanam, S. (2002-12-06). "The Protein Kinase Complement of the Human Genome". Science 298 (5600): 1912–1934. doi:10.1126/science.1075762. ISSN 0036-8075. PMID 12471243. 
  4. ^ Park, Hee-Sung; Hohn, Michael J.; Umehara, Takuya; Guo, Li-Tao; Osborne, Edith M.; Benner, Jack; Noren, Christopher J.; Rinehart, Jesse; Söll, Dieter (2011-08-26). "Expanding the Genetic Code of Escherichia coli with Phosphoserine". Science 333 (6046): 1151–1154. doi:10.1126/science.1207203. ISSN 0036-8075. PMID 21868676. 
  5. ^ Rogerson, Daniel T; Sachdeva, Amit; Wang, Kaihang; Haq, Tamanna; Kazlauskaite, Agne; Hancock, Susan M; Huguenin-Dezot, Nicolas; Muqit, Miratul M K; Fry, Andrew M (2015-01-01). "Efficient genetic encoding of phosphoserine and its nonhydrolyzable analog". Nature Chemical Biology 11 (7). doi:10.1038/nchembio.1823. 
  6. ^ Oza, Javin P.; Aerni, Hans R.; Pirman, Natasha L.; Barber, Karl W.; ter Haar, Charlotte M.; Rogulina, Svetlana; Amrofell, Matthew B.; Isaacs, Farren J.; Rinehart, Jesse (2015-09-09). "Robust production of recombinant phosphoproteins using cell-free protein synthesis". Nature Communications 6. doi:10.1038/ncomms9168. PMC 4566161. PMID 26350765. 
  7. ^ Analysis of free and bound O-phosphoamino acids in urine by gas chromatography with flame photometric detection
  8. ^ Jastrzab, Renata; Lomozik, Lechoslaw (2009-03-10). "Coordination mode in the binary systems of copper(II)/O-phospho-L-serine". Journal of Coordination Chemistry 62 (5): 710–720. doi:10.1080/00958970802317855. ISSN 0095-8972. 
  9. ^ Jastrzab, Renata (2009-05-01). "Phosphoserine and specific types of its coordination in copper(II) and adenosine nucleotides systems – Potentiometric and spectroscopic studies". Journal of Inorganic Biochemistry 103 (5): 766–773. doi:10.1016/j.jinorgbio.2009.01.012.