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Revision as of 12:58, 5 December 2011 editBeetstra (talk | contribs)Edit filter managers, Administrators172,031 edits Saving copy of the {{chembox}} taken from revid 455926560 of page Phosphoserine for the Chem/Drugbox validation project (updated: '').  Latest revision as of 08:29, 26 June 2024 edit 0dorkmann (talk | contribs)259 editsm img 
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{{ambox | text = This page contains a copy of the infobox ({{tl|chembox}}) taken from revid of page ] with values updated to verified values.}}
{{Chembox {{Chembox
| Verifiedfields = changed | Watchedfields = changed
| verifiedrevid = 417926134 | verifiedrevid = 464205670
| Name = <small>L</small>-Phosphoserine | Name = {{sm|l}}-Phosphoserine
| ImageFile = L-Phosphoserine.png | ImageFile = L-Phosphoserine.svg
| ImageSize = 180 | ImageSize = 180
| ImageName = Skeletal formula | ImageName = Skeletal formula
| ImageFile1 = Phosphoserine-3D-balls.png | ImageFile1 = Phosphoserine-3D-balls.png
| ImageSize1 = 120px | ImageSize1 = 120px
| ImageName1 = Ball-and-stick model | ImageName1 = Ball-and-stick model
| IUPACName = (''S'')-2-Amino-3-(phosphonooxy)propionic acid | IUPACName = (''S'')-2-Amino-3-(phosphonooxy)propionic acid
| OtherNames = | OtherNames =
| Section1 = {{Chembox Identifiers |Section1={{Chembox Identifiers
| UNII_Ref = {{fdacite|correct|FDA}} | IUPHAR_ligand = 1411
| UNII_Ref = {{fdacite|correct|FDA}}
| UNII = VI4F0K069V | UNII = VI4F0K069V
| InChI = 1/C3H8NO6P/c4-2(3(5)6)1-10-11(7,8)9/h2H,1,4H2,(H,5,6)(H2,7,​8,9)/t2-/m0/s1 | InChI = 1/C3H8NO6P/c4-2(3(5)6)1-10-11(7,8)9/h2H,1,4H2,(H,5,6)(H2,7,8,9)/t2-/m0/s1
| ChEMBL_Ref = {{ebicite|correct|EBI}} | ChEMBL_Ref = {{ebicite|correct|EBI}}
| ChEMBL = 284377 | ChEMBL = 284377
| StdInChI_Ref = {{stdinchicite|correct|chemspider}} | StdInChI_Ref = {{stdinchicite|correct|chemspider}}
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| StdInChIKey = BZQFBWGGLXLEPQ-REOHCLBHSA-N | StdInChIKey = BZQFBWGGLXLEPQ-REOHCLBHSA-N
| CASNo = 407-41-0 | CASNo = 407-41-0
| CASNo_Ref = {{cascite|correct|CAS}} | CASNo_Ref = {{cascite|correct|CAS}}
| EC-number = 206-986-0 | EC_number = 206-986-0
| ChemSpiderID_Ref = {{chemspidercite|correct|chemspider}} | ChemSpiderID_Ref = {{chemspidercite|correct|chemspider}}
| ChemSpiderID = 62074 | ChemSpiderID = 62074
| PubChem = 106 | PubChem = 106
| DrugBank_Ref = {{drugbankcite|changed|drugbank}} | DrugBank_Ref = {{drugbankcite|correct|drugbank}}
| DrugBank = DB04522 | DrugBank = DB04522
| ChEBI_Ref = {{ebicite|changed|EBI}} | ChEBI_Ref = {{ebicite|correct|EBI}}
| ChEBI = 15811 | ChEBI = 15811
| KEGG = C01005
| SMILES = O=P(O)(O)OC(C(=O)O)N | SMILES = O=P(O)(O)OC(C(=O)O)N
| MeSHName = Phosphoserine | MeSHName = Phosphoserine
}} }}
| Section2 = {{Chembox Properties |Section2={{Chembox Properties
| Formula = C<sub>3</sub>H<sub>8</sub>NO<sub>6</sub>P | Formula = C<sub>3</sub>H<sub>8</sub>NO<sub>6</sub>P
| MolarMass = 185.07 g/mol | MolarMass = 185.073 g/mol
| Appearance = | Appearance =
| Density = | Density =
| MeltingPtC = 228
| MeltingPt =
| BoilingPt = | BoilingPt =
}} }}
}} }}

'''Phosphoserine''' (abbreviated as '''SEP''' or '''J''') is an ] of ] and ]. Phosphoserine is a component of many proteins as the result of ]s.<ref>{{Cite journal|title = Global, In Vivo, and Site-Specific Phosphorylation Dynamics in Signaling Networks|journal = Cell|date = 2006-03-11|pmid = 17081983|pages = 635–648|volume = 127|issue = 3|doi = 10.1016/j.cell.2006.09.026|first1 = Jesper V.|last1 = Olsen|first2 = Blagoy|last2 = Blagoev|first3 = Florian|last3 = Gnad|first4 = Boris|last4 = Macek|first5 = Chanchal|last5 = Kumar|first6 = Peter|last6 = Mortensen|first7 = Matthias|last7 = Mann|s2cid = 7827573|doi-access = free}}</ref> The ] of the ] ] in ] to produce phosphoserine is catalyzed by various types of ]s.<ref>{{Cite journal|title = The phosphorylation of proteins: a major mechanism for biological regulation|journal = Biochemical Society Transactions|date = 1985-10-01|pmid = 2998902|pages = 813–820|volume = 13|issue = 5|doi = 10.1042/bst0130813|first = Edwin G.|last = Krebs}}</ref><ref>{{Cite journal|title = The Protein Kinase Complement of the Human Genome|journal = Science|date = 2002-12-06|pmid = 12471243|pages = 1912–1934|volume = 298|issue = 5600|doi = 10.1126/science.1075762|first1 = G.|last1 = Manning|first2 = D. B.|last2 = Whyte|first3 = R.|last3 = Martinez|first4 = T.|last4 = Hunter|first5 = S.|last5 = Sudarsanam|bibcode = 2002Sci...298.1912M|s2cid = 26554314}}</ref> Through the use of technologies that utilize an ], phosphoserine can also be incorporated into proteins during translation.<ref>{{Cite journal|title = Expanding the Genetic Code of Escherichia coli with Phosphoserine|journal = Science|date = 2011-08-26|pmid = 21868676|pages = 1151–1154|volume = 333|issue = 6046|doi = 10.1126/science.1207203|first1 = Hee-Sung|last1 = Park|first2 = Michael J.|last2 = Hohn|first3 = Takuya|last3 = Umehara|first4 = Li-Tao|last4 = Guo|first5 = Edith M.|last5 = Osborne|first6 = Jack|last6 = Benner|first7 = Christopher J.|last7 = Noren|first8 = Jesse|last8 = Rinehart|first9 = Dieter|last9 = Söll|pmc = 5547737|bibcode = 2011Sci...333.1151P}}</ref><ref>{{Cite journal|title = Efficient genetic encoding of phosphoserine and its nonhydrolyzable analog|journal = Nature Chemical Biology|date = 2015-01-01|volume = 11|issue = 7|pages = 496–503|doi = 10.1038/nchembio.1823|pmid = 26030730|first1 = Daniel T|last1 = Rogerson|first2 = Amit|last2 = Sachdeva|first3 = Kaihang|last3 = Wang|first4 = Tamanna|last4 = Haq|first5 = Agne|last5 = Kazlauskaite|first6 = Susan M|last6 = Hancock|first7 = Nicolas|last7 = Huguenin-Dezot|first8 = Miratul M K|last8 = Muqit|first9 = Andrew M|last9 = Fry|pmc=4830402}}</ref><ref>{{Cite journal|title = Robust production of recombinant phosphoproteins using cell-free protein synthesis|journal = Nature Communications|date = 2015-09-09|pmc = 4566161|pmid = 26350765|volume = 6|pages = 8168|doi = 10.1038/ncomms9168|first1 = Javin P.|last1 = Oza|first2 = Hans R.|last2 = Aerni|first3 = Natasha L.|last3 = Pirman|first4 = Karl W.|last4 = Barber|first5 = Charlotte M.|last5 = ter Haar|first6 = Svetlana|last6 = Rogulina|first7 = Matthew B.|last7 = Amrofell|first8 = Farren J.|last8 = Isaacs|first9 = Jesse|last9 = Rinehart|bibcode = 2015NatCo...6.8168O}}</ref>

It is a normal ] found in human biofluids.<ref>{{cite journal|pmid=7693088 |title=Analysis of free and bound O-phosphoamino acids in urine by gas chromatography with flame photometric detection|journal=Biomedical Chromatography|volume=7|issue=4|pages=184–8|year=1993|last1=Kataoka|first1=H|last2=Nakai|first2=K|last3=Katagiri|first3=Y|last4=Makita|first4=M|doi=10.1002/bmc.1130070403}}</ref>

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.<ref>{{Cite journal|title = Coordination mode in the binary systems of copper(II)/O-phospho-L-serine|journal = Journal of Coordination Chemistry|date = 2009-03-10|pages = 710–720|volume = 62|issue = 5|doi = 10.1080/00958970802317855|first1 = Renata|last1 = Jastrzab|first2 = Lechoslaw|last2 = Lomozik|s2cid = 95207026}}</ref><ref>{{Cite journal|title = Phosphoserine and specific types of its coordination in copper(II) and adenosine nucleotides systems – Potentiometric and spectroscopic studies|journal = Journal of Inorganic Biochemistry|date = 2009-05-01|pages = 766–773|volume = 103|issue = 5|doi = 10.1016/j.jinorgbio.2009.01.012|pmid = 19230980|first = Renata|last = Jastrzab}}</ref>

==References==
{{reflist}}

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