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Chemical compound
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
Phosphoserine
The enzyme phosphoserine phosphatase (EC 3.1.3.3) catalyzes the reaction O-phospho-L(or D)-serine + H2O ⇌ {\displaystyle \rightleftharpoons } L(or D)-serine
Phosphoserine_phosphatase
Biochemical process
such as ceramide. Phosphoglycans linked through the phosphate of a phosphoserine. C-linked glycans, a rare form of glycosylation where a sugar is added
Glycosylation
IUPAC Nomenclature of a catalyst enzyme
Phosphoserine transaminase (EC 2.6.1.52, PSAT, phosphoserine aminotransferase, 3-phosphoserine aminotransferase, hydroxypyruvic phosphate-glutamic transaminase
Phosphoserine_transaminase
Amino acid
ketone by phosphoserine transaminase (EC 2.6.1.52) yields 3-phosphoserine (O-phosphoserine) which is hydrolyzed to serine by phosphoserine phosphatase
Serine
Enzyme found in humans
Phosphoserine phosphatase is an enzyme that in humans is encoded by the PSPH gene. The protein encoded by this gene belongs to a subfamily of the phosphotransferases
PSPH
Class of enzymes
O-phosphoserine sulfhydrylase (EC 2.5.1.65) is an enzyme that catalyzes the chemical reaction phosphoserine H2S Pi cysteine The two substrates
O-phosphoserine_sulfhydrylase
produces L-cysteic acid by reacting phosphoserine with sulfite (H2SO3), giving orthophosphate (Pi) as a byproduct: phosphoserine + H2SO3 Pi L-cysteic
Cysteate_synthase
Protein-coding gene in the species Homo sapiens
Phosphoserine aminotransferase (PSA) also known as phosphohydroxythreonine aminotransferase (PSAT) is an enzyme that in humans is encoded by the PSAT1
PSAT1
Class of enzymes
phosphate + phosphoserine The enzyme characterised from Propionibacterium shermanii converts L-serine to phosphoserine by transferring a phosphate
Diphosphate—serine phosphotransferase
Diphosphate—serine_phosphotransferase
KIAA0232 is a nuclear phosphoserine protein which in humans is encoded by the KIAA0232 gene. KIAA0232 is located at 4p16.1 neighboring TBC1 domain family
KIAA0232
Class of lipids
(ammonium salt) Phosphatidylglycerol DLPS-NA 1,2-Dilauroyl-sn-glycero-3-phosphoserine (sodium salt) Phosphatidylserine DMPA-NA 80724-3 1
Phospholipid
Ion of fluorine
et al. (2002). "Structural characterization of the reaction pathway in phosphoserine phosphatase: crystallographic "snapshots" of intermediate states". J
Fluoride
Protein-coding gene in the species Homo sapiens
14-3-3 protein family which mediate signal transduction by binding to phosphoserine-containing proteins. This highly conserved protein family is found in
YWHAG
Process where substrates are converted into more complex products in living organisms
the enzyme phosphoserine aminotransferase, which transfers an amino group from glutamate onto 3-phosphonooxypyruvate to yield L-phosphoserine. The final
Biosynthesis
Sulfur-containing amino acid
CysM in E. coli), but in Aeropyrum pernix and some other archaea O-phosphoserine is used. CysK and CysM are homologues, but belong to the PLP fold type
Methionine
Selenium-containing amino acid
https://3d.nih.gov/entries/3DPX-007805. Accessed 5 Dec. 2025. “NIH 3D – dl-O-Phosphoserine.” Nih.gov, 2017, https://3d.nih.gov/entries/5203. Accessed 5 Dec. 2025
Selenocysteine
Amino acid
reliable protein-protein interactions—by means of phosphotyrosine, phosphoserine and phosphothreonine. Binding sites for a signalling phosphoprotein
Tyrosine
Class of enzymes
Phosphotyrosine Serine-/threonine-specific phosphatases PP2C (PPP2CA) Phosphoserine/-threonine Dual specificity phosphatases VHR, DUSP1–DUSP28
Protein_phosphatase
Describes a new class of consumer health testing
N-Acetylaspartic acid ✓ N-Acetylaspartylglutamic acid ✓ Kynurenic acid ✓ Phosphoserine ✓ Pipecolic Acid ✓ DOPA ✓ ANTIOXIDANT LEVELS 1-Methylhistidine ✓ Anserine
Direct-to-consumer blood testing
Direct-to-consumer_blood_testing
possess a substrate ambiguity and overexpression of hisB can rescue phosphoserine phosphatase (serB) knockouts. hisB-N D-erythro-1-(imidazol-4-yl)glycerol
HisB
Family of proteins
2001). "Crystal structure of a phosphorylated Smad2. Recognition of phosphoserine by the MH2 domain and insights on Smad function in TGF-beta signaling"
SMAD_(protein)
dihydrofolate reductase, 3-phosphoglycerate dehydrogenase, 3-phosphoserine phosphatase, phosphoserine aminotransferase, the glycine cleavage system (the deficiency
International Working Group on Neurotransmitter Related Disorders
International_Working_Group_on_Neurotransmitter_Related_Disorders
Protein-coding gene in the species Homo sapiens
There is extensive, predicted phosphorylation of C6orf222, with 42 phosphoserines and 7 phosphothreonines being conserved in orthologs of the human C6orf222
BNIP5
Protein-coding gene in the species Homo sapiens
phosphatases inactivate their target kinases by dephosphorylating both the phosphoserine/threonine and phosphotyrosine residues. They negatively regulate members
DUSP3
been proposed as biomarkers for breast cancer. Protein phosphorylation Phosphoserine Keyword - Phosphoprotein Phosphoproteins in extracellular vesicles as
Phosphoprotein
Protein with oligosaccharide modifications
hydroxyproline. In P-glycosylation, sugars are attached to phosphorus on a phosphoserine. In C-glycosylation, sugars are attached directly to carbon, such as
Glycoprotein
Human gene and protein
YWHAE is involved in signal transduction pathways due to its binding of phosphoserine-containing proteins. Zinc finger protein 839 has many phosphorylation
ZNF839
Muscle enzyme involved in glycogen breakdown
PYGM also has the following modified residues: N-acetylserine at p. 2, phosphoserine at p. 15, 2014, 227, 430, 473, 514, 747, and 748, and N6-(pyridoxal
Myophosphorylase
Protein-coding gene in the species Homo sapiens
It contains a domain of unknown function, DUF846, and a predicted phosphoserine site. It is a multipass transmembrane protein and a member of the FAM18/TVP23
TVP23B
Protein-coding gene in the species Homo sapiens
phosphatases inactivate their target kinases by dephosphorylating both the phosphoserine/threonine and phosphotyrosine residues. They negatively regulate members
DUSP10
Family of enzymes
It includes a diverse range of phosphoesterases, including protein phosphoserine phosphatases, nucleotidases, sphingomyelin phosphodiesterases and 2'-3'
Calcineurin-like phosphoesterase
Calcineurin-like_phosphoesterase
American chemist
phosphates, including the first synthesis of the CF2-phosphonate analogs of phosphoserine and phosphothreonine, among others. These "Teflon phosphates" are inert
David_B._Berkowitz
Modified genetic code
papers dealing with natural non-proteinogenic amino acids, such as phosphoserine), or non-canonical amino acids. The first element of the system is the
Expanded_genetic_code
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase EC 2.5.1.65: O-phosphoserine sulfhydrylase EC 2.5.1.66: N2-(2-carboxyethyl)arginine synthase EC 2
List_of_EC_numbers_(EC_2)
Protein-coding gene in the species Homo sapiens
phosphatases inactivate their target kinases by dephosphorylating both the phosphoserine/threonine and phosphotyrosine residues. They negatively regulate members
DUSP12
and 112. The serine in position 62 can be phosphorylated to form a phosphoserine group. The c10orf35 protein has expression over the 75th percentile
FAM241B
Protein family
enzymes can be grouped into subfamilies. This family is called class-V. Phosphoserine aminotransferase InterPro: IPR003248 Cysteine desulfurase InterPro: IPR010240
Aminotransferase,_class_V
Protein-coding gene in the species Homo sapiens
proteins, members of which mediate signal transduction by binding to phosphoserine-containing proteins. This highly conserved protein family is found in
YWHAB
British biochemist (born 1945)
muscle: effects of insulin on the state of phosphorylation of the seven phosphoserine residues in vivo Inhibition of glycogen synthase kinase-3 by insulin
Philip Cohen (British biochemist)
Philip_Cohen_(British_biochemist)
Protein domain
particular proline-motifs, [AP]-P-P-[AP]-Y, some WW domains bind to phosphoserine- and phosphothreonine-containing motifs. The WW domain is one of the
WW_domain
Protein found in humans
insulin-like growth factor I receptor and insulin receptor substrate I in a phosphoserine-dependent manner". The Journal of Biological Chemistry. 272 (17): 11663–9
Insulin_receptor_substrate_1
Branch of proteomics
purification, but fewer reports have been published using antibodies against phosphoserine- or phosphothreonine-containing proteins. IMAC enrichment is based on
Phosphoproteomics
Protein-coding gene in the species Homo sapiens
Zhou XZ, Shen M, Lu KP (February 1999). "Function of WW domains as phosphoserine- or phosphothreonine-binding modules". Science. 283 (5406). New York
PIN1
Topics referred to by the same term
dictionary. SERC, Serc, etc. may refer to: Sérc, a municipality in Austria Phosphoserine transaminase, an enzyme Serc, a brand name of the antivertigo drug betahistine
SERC
Medical condition
defects in two known enzymes: 3-phosphogycerate dehydrogenase and 3-phosphoserine phosphatase, leading to severe neurological abnormalities Like familial
Achalasia_microcephaly
Protein-coding gene in humans
constituitively phosphorylated on CR2 S445. This allows the negatively charged phosphoserine to immediately repel CR1 through steric and electrostatic interactions
BRAF_(gene)
Protein-coding gene in the species Homo sapiens
S2CID 7200157. Gburcik V, Bot N, Maggiolini M, Picard D (May 2005). "SPBP is a phosphoserine-specific repressor of estrogen receptor alpha". Molecular and Cellular
TCF20
Protein-coding gene in the species Homo sapiens
phosphatases inactivate their target kinases by dephosphorylating both the phosphoserine/threonine and phosphotyrosine residues. They negatively regulate members
DUSP5
Class of enzymes
PMID 7822274. Korn ED, Brzeska H (1998). "Effect of mutating the regulatory phosphoserine and conserved threonine on the activity of the expressed catalytic domain
Myosin-heavy-chain_kinase
Protein-coding gene in the species Homo sapiens
In addition, there is an N6-acetyllysine site at leucine 747 and a phosphoserine site at serine 23. C1orf112 has been found experimentally to interact
FIRRM
Structural material present in almost all organic life
mineral matrix ultimately interacts with the synthetic fibril via a phosphoserine residue which results in mineral nucleation and growth. Fibre Microfibril
Fibril
Medical condition
James R.; Jaeken, Jaak; Matthijs, Gert; Van Schaftingen, Emile (2007). "Phosphoserine Aminotransferase Deficiency: A Novel Disorder of the Serine Biosynthesis
Neu–Laxova_syndrome
Human chromosome
subunit p20 PPP1R17: protein phosphatase 1 regulatory subunit 17 PSPH: phosphoserine phosphatase PURB: purine-rich element binding protein B PVRIG: encoding
Chromosome_7
Fungal protein found in Saccharomyces cerevisiae S288c
protein amino acid modifications can be found at residue 156 being a phosphoserine and at residue 157 being a phosphothreonine. Cdh1 also contains a C-terminal
APC/C_activator_protein_CDH1
Standard and alternative genetic codes
Whitman, WB; Söll, D (12 December 2006). "RNA-dependent conversion of phosphoserine forms selenocysteine in eukaryotes and archaea". Proceedings of the
List_of_genetic_codes
Chemical changes in proteins following their translation from mRNA
conversion to an alkene by beta-elimination of phosphothreonine and phosphoserine, or dehydration of threonine and serine disulfide bridges, the covalent
Post-translational modification
Post-translational_modification
Protein-coding gene in the species Homo sapiens
There is extensive, predicted phosphorylation of C5orf34, with 32 phosphoserines and 7 phosphothreonines being conserved in orthologs of the human C5orf34
C5orf34
Protein-coding gene in the species Homo sapiens
single-stranded DNA binding DNA binding RNA polymerase II C-terminal domain phosphoserine binding RNA binding molecular function Cellular component nucleolus
RTFDC1
Chemical compound
PMC 528146. PMID 16589713. Hanford, J.; Davies, D.D. (1958). "Formation of Phosphoserine from 3-Phosphoglycerate in Higher Plants". Nature. 182 (4634): 532–533
3-Phosphoglyceric_acid
Type of biochemical process
3-phosphohydroxypyruvate (3-phosphoglycerate dehydrogenase) → 3-phosphoserine (aminotransferase) → Serine (phosphoserine phosphatase) Threonine§ CH3−CH(OH)− Aspartate →
Protein_metabolism
Protein-coding gene in the species Homo sapiens
family of proteins which mediate signal transduction by binding to phosphoserine-containing proteins. This highly conserved protein family is found in
YWHAE
Mammalian protein found in humans
lipid-binding site 17 17 Phosphoserine site 35 35 Phosphoserine site 69 69 Phosphoserine site 74 74 Phosphothreonine site 75 75 Phosphoserine; by CDK5 region 87
Proto-oncogene tyrosine-protein kinase Src
Proto-oncogene_tyrosine-protein_kinase_Src
Set of biochemical processes
following pathway: 3-phosphoglycerate → phosphohydroxyl-pyruvate → phosphoserine → serine The conversion from 3-phosphoglycerate to phosphohydroxyl-pyruvate
Amino_acid_synthesis
In organisms like Archaeoglobus fulgidus, this enzyme ligates O-phosphoserine to tRNACys. Fukunaga R, Yokoyama S (April 2007). "Structural insights
O-phospho-L-serine—tRNA ligase
O-phospho-L-serine—tRNA_ligase
Egg yolk phosphoprotein
As the most phosphorylated natural protein, phosvitin contains 123 phosphoserine residues accounting for 56.7% of its total 217 amino acid residues.
Phosvitin
Chemical compound
after, the country's Supreme Court suspended the law. Phosphocholine Phosphoserine Lipid A phosphoethanolamine transferase MCR-1 Myller, AT; et al. (2010)
Phosphorylethanolamine
Genus of archaea
in studies this far. Additional studies have been coordinated on the phosphoserine phosphatase (PSP) enzyme of T. onnurineus, which provided an essential
Thermococcus
Physical interactions and constructions between multiple proteins
binding pocket with high affinity for phosphotyrosine, but not for phosphoserine or phosphothreonine, is essential for the recognition of tyrosine phosphorylated
Protein–protein_interaction
Protein-coding gene in the species Homo sapiens
protein binding RNA polymerase binding proline-rich region binding phosphoserine residue binding phosphothreonine residue binding ionotropic glutamate
NEDD4
Species of bacterium
It should also be noted that H. thermophilus lacks the typical PSP (phosphoserine phosphatase) genes involved in amino acid metabolism. In addition, it
Hydrogenobacter_thermophilus
Topics referred to by the same term
may refer to: PSAT/NMSQT, a standardized test in the United States Phosphoserine transaminase, an enzyme Palm Springs Aerial Tramway Pop-up satellite
PSAT
Protein-coding gene in the species Homo sapiens
Dümmler BA, Jensen CJ, Deak M, Gammeltoft S, et al. (October 2002). "A phosphoserine/threonine-binding pocket in AGC kinases and PDK1 mediates activation
Phosphoinositide-dependent kinase-1
Phosphoinositide-dependent_kinase-1
Class of protein kinase enzymes
phosphoserine
Serine/threonine-specific protein kinase
Serine/threonine-specific_protein_kinase
Family of conserved regulatory molecules
Cdc25C by CDS1 and CHEK1 creates a binding site for the 14-3-3 family of phosphoserine binding proteins. Binding of 14-3-3 has little effect on Cdc25C activity
14-3-3_protein
AM, Whitman WB, Söll D (December 2006). "RNA-dependent conversion of phosphoserine forms selenocysteine in eukaryotes and archaea". Proceedings of the
O-phospho-L-seryl-tRNA:Cys-tRNA synthase
O-phospho-L-seryl-tRNA:Cys-tRNA_synthase
Cell receptor protein found in humans
insulin-like growth factor I receptor and insulin receptor substrate I in a phosphoserine-dependent manner". The Journal of Biological Chemistry. 272 (17): 11663–9
Insulin-like growth factor 1 receptor
Insulin-like_growth_factor_1_receptor
DNA strand exchange
transesterification reaction, in which a phosphodiester bond is replaced by a phosphoserine bond between a 5' phosphate at the cleavage site and the hydroxyl group
Site-specific_recombination
Chromosome 19 open reading frame 47
3-Monooxygenase/Tryptophan 5-Monooxygenase Activation Protein, Theta Polypeptide Mediates signal transduction by binding to phosphoserine-containing proteins.
C19orf47
Mammalian protein found in Homo sapiens
Zhou XZ, Shen M, Lu KP (February 1999). "Function of WW domains as phosphoserine- or phosphothreonine-binding modules". Science. 283 (5406): 1325–8.
PLK1
Protein-coding gene in the species Homo sapiens
phosphatases inactivate their target kinases by dephosphorylating both the phosphoserine/threonine and phosphotyrosine residues. They negatively regulate members
DUSP2
Protein-coding gene in the species Homo sapiens
Bioinformatics. Retrieved 1 May 2018. Yaffe MB, Smerdon SJ (March 2001). "PhosphoSerine/threonine binding domains: you can't pSERious?". Structure. 9 (3): R33-8
TASOR2
3.1: alkaline phosphatase EC 3.1.3.2: acid phosphatase EC 3.1.3.3: phosphoserine phosphatase EC 3.1.3.4: phosphatidate phosphatase EC 3.1.3.5: 5′-nucleotidase
List_of_EC_numbers_(EC_3)
Protein-coding gene in the species Homo sapiens
phosphatases inactivate their target kinases by dephosphorylating both the phosphoserine/threonine and phosphotyrosine residues. They negatively regulate members
Dual specificity phosphatase 8
Dual_specificity_phosphatase_8
Protein-coding gene in the species Homo sapiens
Cardoso AM, Whitman WB, Söll D (Dec 2006). "RNA-dependent conversion of phosphoserine forms selenocysteine in eukaryotes and archaea". Proc. Natl. Acad. Sci
SEPSECS
Mammalian protein found in Homo sapiens
sites for post-translational phosphorylation of Ser residues to form phosphoserine, providing additional negative charge. Contiguous stretches of high
Osteopontin
kinase deficiency of liver and muscle, autosomal recessive; 261750; PHKB Phosphoserine aminotransferase deficiency; 610992; PSAT1 Pick disease; 172700; MAPT
List_of_OMIM_disorder_codes
Protein-coding gene in the species Homo sapiens
dual specificity phosphatases (DSPs) acts on both phosphotyrosine and phosphoserine/threonine residues. This gene encodes different but related DSP proteins
DUSP13B
Protein-coding gene in the species Homo sapiens
GDP. Mature RAB2B contains three post-translational modifications, a phosphoserine is found in the location 202 instead of a normal serine, and two lipidations
RAB2B
Protein-coding gene in humans
sites have been experimentally found, including a phosphotyrosine, phosphoserine, and glycyl-lysine isopeptide. A portion of the 3' UTR of C1orf123 has
CZIB
Human protein
modified residues) such as N-acetylalanine, omega-N-methylarginine, and phosphoserine). This gene has 5 transcripts (splice variants), 62 orthologues and
UPF0488
Human biochemical pathway
insulin-like growth factor I receptor and insulin receptor substrate I in a phosphoserine-dependent manner". The Journal of Biological Chemistry. 272 (17): 11663–9
Insulin signal transduction pathway
Insulin_signal_transduction_pathway
Protein-coding gene in the species Homo sapiens
number of binding partners, mostly by recognizing phosphothreonine or phosphoserine motifs. FHAD1 showed differential expression in patients diagnosed with
FHAD1
Protein-coding gene in the species Homo sapiens
residues that functions to cleave single-stranded RNA. SMG6 also shares a phosphoserine-binding domain resembling the one in 14–3–3 proteins with its other
SMG6
Genome engineering tools
serine responsible for attacking the scissile phosphate to form a 5'-phosphoserine linkage. These undisputed facts, however, were compromised by a good
Site-specific recombinase technology
Site-specific_recombinase_technology
Partial list of the "D" codes for Medical Subject Headings
MeSH D12.125.740.675 – phosphocreatine MeSH D12.125.740.700 – phosphoserine MeSH D12.125.740.725 – phosphothreonine MeSH D12.125.740.740 – phosphotyrosine
List_of_MeSH_codes_(D12.125)
Protein-coding gene in the species Homo sapiens
and has 8 exons. POLG2, the protein encoded by this gene, contains a phosphoserine modified residue at p. 38 and a transit peptide. Its structure consists
POLG2
AM, Whitman WB, Söll D (December 2006). "RNA-dependent conversion of phosphoserine forms selenocysteine in eukaryotes and archaea". Proceedings of the
O-phospho-L-seryl-tRNASec:L-selenocysteinyl-tRNA synthase
O-phospho-L-seryl-tRNASec:L-selenocysteinyl-tRNA_synthase
Protein-coding gene in the species Homo sapiens
contribute to catalysis and substrate binding. These regions are: the phosphoserine residue that participates in phosphoryl transfer; the metal- binding
PGM1
Protein-coding gene in the species Homo sapiens
14-3-3 family of proteins that mediate signal transduction by binding to phosphoserine-containing proteins. This highly conserved protein family is found in
YWHAQ
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