PSPH: Difference between revisions

Jump to navigation Jump to search
VisualWikitext
WikiBot (talk | contribs)
Bots, Bureaucrats, bureaucrats, interwiki, nocaptcha, Administrators
57,550 edits
m Robot: Automated text replacement (-{{reflist}} +{{reflist|2}}, -<references /> +{{reflist|2}}, -{{WikiDoc Cardiology Network Infobox}} +)
 
 
Line 1: Line 1:
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Underlinked|date=March 2014}}
{{PBB_Controls
{{Infobox_gene}}
| update_page = yes
'''Phosphoserine phosphatase''' is an [[enzyme]] that in humans is encoded by the ''PSPH'' [[gene]].<ref name="pmid6297854">{{cite journal | vauthors = Koch GA, Eddy RL, Haley LL, Byers MG, McAvoy M, Shows TB | title = Assignment of the human phosphoserine phosphatase gene (PSP) to the pter leads to q22 region of chromosome 7 | journal = Cytogenetics and Cell Genetics | volume = 35 | issue = 1 | pages = 67–9 | date = Apr 1983 | pmid = 6297854 | pmc =  | doi = 10.1159/000131839 }}</ref><ref name="pmid9188776">{{cite journal | vauthors = Collet JF, Gerin I, Rider MH, Veiga-da-Cunha M, Van Schaftingen E | title = Human L-3-phosphoserine phosphatase: sequence, expression and evidence for a phosphoenzyme intermediate | journal = FEBS Letters | volume = 408 | issue = 3 | pages = 281–4 | date = May 1997 | pmid = 9188776 | pmc =  | doi = 10.1016/S0014-5793(97)00438-9 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: PSPH phosphoserine phosphatase| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5723| accessdate = }}</ref>
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image = PBB_Protein_PSPH_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1l8l.
| PDB = {{PDB2|1l8l}}, {{PDB2|1l8o}}, {{PDB2|1nnl}}
| Name = Phosphoserine phosphatase
| HGNCid = 9577
| Symbol = PSPH
| AltSymbols =; PSP
| OMIM = 172480
| ECnumber = 
| Homologene = 31245
| MGIid = 97788
| GeneAtlas_image1 = PBB_GE_PSPH_205048_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_PSPH_205194_at_tn.png
| GeneAtlas_image3 = PBB_GE_PSPH_gnf1h09519_s_at_tn.png
| Function = {{GNF_GO|id=GO:0000287 |text = magnesium ion binding}} {{GNF_GO|id=GO:0004647 |text = phosphoserine phosphatase activity}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}}
| Component =
| Process = {{GNF_GO|id=GO:0006564 |text = L-serine biosynthetic process}} {{GNF_GO|id=GO:0008152 |text = metabolic process}} {{GNF_GO|id=GO:0008652 |text = amino acid biosynthetic process}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 5723
    | Hs_Ensembl = ENSG00000146733
    | Hs_RefseqProtein = NP_004568
    | Hs_RefseqmRNA = NM_004577
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 7
    | Hs_GenLoc_start = 56046240
    | Hs_GenLoc_end = 56086762
    | Hs_Uniprot = P78330
    | Mm_EntrezGene = 100678
    | Mm_Ensembl = ENSMUSG00000029446
    | Mm_RefseqmRNA = NM_133900
    | Mm_RefseqProtein = NP_598661
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 5
    | Mm_GenLoc_start = 130080273
    | Mm_GenLoc_end = 130101913
    | Mm_Uniprot = Q99LS3
  }}
}}
'''Phosphoserine phosphatase''', also known as '''PSPH''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PSPH phosphoserine phosphatase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5723| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
The protein encoded by this gene belongs to a subfamily of the phosphotransferases. This encoded enzyme is responsible for the third and last step in L-serine formation. It catalyzes magnesium-dependent hydrolysis of L-phosphoserine and is also involved in an exchange reaction between L-serine and L-phosphoserine. Deficiency of this protein is thought to be linked to Williams syndrome.<ref name="entrez" />
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene belongs to a subfamily of the phosphotransferases. This encoded enzyme is responsible for the third and last step in L-serine formation. It catalyzes magnesium-dependent hydrolysis of L-phosphoserine and is also involved in an exchange reaction between L-serine and L-phosphoserine. Deficiency of this protein is thought to be linked to Williams syndrome.<ref name="entrez">{{cite web | title = Entrez Gene: PSPH phosphoserine phosphatase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5723| accessdate = }}</ref>
}}


==References==
== Clinical significance ==
{{reflist|2}}
 
==Further reading==
Homozygous or compound heterozygous mutations in ''PSPH'' cause [[Neu-Laxova syndrome]]<ref>{{cite journal | vauthors = Acuna-Hidalgo R, Schanze D, Kariminejad A, Nordgren A, Kariminejad MH, Conner P, Grigelioniene G, Nilsson D, Nordenskjöld M, Wedell A, Freyer C, Wredenberg A, Wieczorek D, Gillessen-Kaesbach G, Kayserili H, Elcioglu N, Ghaderi-Sohi S, Goodarzi P, Setayesh H, van de Vorst M, Steehouwer M, Pfundt R, Krabichler B, Curry C, MacKenzie MG, Boycott KM, Gilissen C, Janecke AR, Hoischen A, Zenker M | title = Neu-Laxova syndrome is a heterogeneous metabolic disorder caused by defects in enzymes of the L-serine biosynthesis pathway | journal = American Journal of Human Genetics | volume = 95 | issue = 3 | pages = 285–93 | date = Sep 2014 | pmid = 25152457 | doi = 10.1016/j.ajhg.2014.07.012 | url = http://www.cell.com/ajhg/abstract/S0002-9297(14)00321-8 | pmc=4157144}}</ref> and Phosphoserine phosphatase deficiency.<ref>{{cite journal | vauthors = Veiga-da-Cunha M, Collet JF, Prieur B, Jaeken J, Peeraer Y, Rabbijns A, Van Schaftingen E | title = Mutations responsible for 3-phosphoserine phosphatase deficiency | journal = European Journal of Human Genetics | volume = 12 | issue = 2 | pages = 163–6 | date = Feb 2004 | pmid = 14673469 | doi = 10.1038/sj.ejhg.5201083 | url = http://www.nature.com/ejhg/journal/v12/n2/full/5201083a.html }}</ref><ref>{{cite journal | vauthors = Jaeken J, Detheux M, Fryns JP, Collet JF, Alliet P, Van Schaftingen E | title = Phosphoserine phosphatase deficiency in a patient with Williams syndrome | journal = Journal of Medical Genetics | volume = 34 | issue = 7 | pages = 594–6 | date = Jul 1997 | pmid = 9222972 | pmc = 1051004 | doi = 10.1136/jmg.34.7.594 | url = http://jmg.bmj.com/content/34/7/594.long }}</ref>
 
== Model organisms ==
 
[[Model organism]]s have been used in the study of PSPH function. A conditional [[knockout mouse]] line called ''Psph<sup>tm1a(EUCOMM)Hmgu</sup>'' was generated at the [[Wellcome Trust Sanger Institute]].<ref name="mgp_reference">{{cite journal |title=The Sanger Mouse Genetics Programme: high throughput characterisation of knockout mice |author=Gerdin AK |year=2010 |journal=Acta Ophthalmologica|volume=88 |pages=925–7|doi=10.1111/j.1755-3768.2010.4142.x }}</ref> Male and female animals underwent a standardized [[phenotypic screen]]<ref name="IMPCsearch_ref">{{cite web |url=http://www.mousephenotype.org/data/search?q=Psph#fq=*:*&facet=gene |title=International Mouse Phenotyping Consortium}}</ref> to determine the effects of deletion.<ref name="pmid21677750">{{cite journal | vauthors = Skarnes WC, Rosen B, West AP, Koutsourakis M, Bushell W, Iyer V, Mujica AO, Thomas M, Harrow J, Cox T, Jackson D, Severin J, Biggs P, Fu J, Nefedov M, de Jong PJ, Stewart AF, Bradley A | title = A conditional knockout resource for the genome-wide study of mouse gene function | journal = Nature | volume = 474 | issue = 7351 | pages = 337–42 | date = Jun 2011 | pmid = 21677750 | pmc = 3572410 | doi = 10.1038/nature10163 }}</ref><ref name="mouse_library">{{cite journal | vauthors = Dolgin E | title = Mouse library set to be knockout | journal = Nature | volume = 474 | issue = 7351 | pages = 262–3 | date = Jun 2011 | pmid = 21677718 | doi = 10.1038/474262a }}</ref><ref name="mouse_for_all_reasons">{{cite journal | vauthors = Collins FS, Rossant J, Wurst W | title = A mouse for all reasons | journal = Cell | volume = 128 | issue = 1 | pages = 9–13 | date = Jan 2007 | pmid = 17218247 | doi = 10.1016/j.cell.2006.12.018 }}</ref><ref name="pmid23870131">{{cite journal | vauthors = White JK, Gerdin AK, Karp NA, Ryder E, Buljan M, Bussell JN, Salisbury J, Clare S, Ingham NJ, Podrini C, Houghton R, Estabel J, Bottomley JR, Melvin DG, Sunter D, Adams NC, Tannahill D, Logan DW, Macarthur DG, Flint J, Mahajan VB, Tsang SH, Smyth I, Watt FM, Skarnes WC, Dougan G, Adams DJ, Ramirez-Solis R, Bradley A, Steel KP | title = Genome-wide generation and systematic phenotyping of knockout mice reveals new roles for many genes | journal = Cell | volume = 154 | issue = 2 | pages = 452–64 | date = Jul 2013 | pmid = 23870131 | doi = 10.1016/j.cell.2013.06.022 | pmc=3717207}}</ref> Additional screens performed:  - In-depth immunological phenotyping<ref name="iii_ref">{{cite web |url= http://www.immunophenotyping.org/data/search?keys=Psph&field_gene_construct_tid=All |title=Infection and Immunity Immunophenotyping (3i) Consortium}}</ref>
{| class="wikitable sortable collapsible collapsed" border="1" cellpadding="2" style="float: left;" |
|+ ''Psph'' knockout mouse phenotype
|-
! Characteristic!! Phenotype
|-
| colspan=2; style="text-align: center;" | All data available at.<ref name="IMPCsearch_ref"/><ref name="iii_ref" />
|-
| Peripheral blood leukocytes 6 Weeks || bgcolor="#488ED3"|Normal
 
|-
| Insulin || bgcolor="#488ED3"|Normal
 
|-
| ''[[Haematology]]'' 6 Weeks || bgcolor="#488ED3"|Normal
 
|-
| Homozygous viability at P14 || bgcolor="#C40000"|Abnormal
 
|-
| [[Recessive]] lethal study || bgcolor="#C40000"|Abnormal
 
|-
| Body weight || bgcolor="#488ED3"|Normal
 
|-
| Neurological assessment || bgcolor="#488ED3"|Normal
 
|-
| Grip strength || bgcolor="#488ED3"|Normal
 
|-
| [[Dysmorphology]] || bgcolor="#488ED3"|Normal
 
|-
| [[Indirect calorimetry]] || bgcolor="#488ED3"|Normal
 
|-
| [[Glucose tolerance test]] || bgcolor="#488ED3"|Normal
 
|-
| [[Dual-energy X-ray absorptiometry|DEXA]] || bgcolor="#488ED3"|Normal
 
|-
| [[Radiography]] || bgcolor="#488ED3"|Normal
 
|-
| Eye morphology || bgcolor="#488ED3"|Normal
 
|-
| [[Clinical chemistry]] || bgcolor="#488ED3"|Normal
 
|-
| ''[[Haematology]]'' 16 Weeks || bgcolor="#488ED3"|Normal
 
|-
| Peripheral blood leukocytes 16 Weeks || bgcolor="#488ED3"|Normal
 
|-
| Heart weight || bgcolor="#488ED3"|Normal
 
|-
| ''[[Salmonella]]'' infection || bgcolor="#488ED3"|Normal
 
|-
| Cytotoxic T Cell Function || bgcolor="#488ED3"|Normal
 
|-
| Spleen Immunophenotyping || bgcolor="#488ED3"|Normal
 
|-
| Mesenteric Lymph Node Immunophenotyping || bgcolor="#488ED3"|Normal
 
|-
| Bone Marrow Immunophenotyping || bgcolor="#488ED3"|Normal
 
|-
| Epidermal Immune Composition || bgcolor="#488ED3"|Normal
 
|-
| Influenza Challenge || bgcolor="#488ED3"|Normal
 
|-
|}
{{clear|left}}
 
== References ==
{{reflist}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Minelli A, Piantanida M, Maserati E, Campagnoli E, Pasquali F, Danesino C | title = Gene dosage effect in acquired monosomy 7: distinct behaviour of beta-glucuronidase and phosphoserine phosphatase | journal = Genes, Chromosomes & Cancer | volume = 1 | issue = 3 | pages = 216–20 | date = Jan 1990 | pmid = 1964582 | doi = 10.1002/gcc.2870010305 }}
| citations =
* {{cite journal | vauthors = Shetty KT | title = Phosphoserine phosphatase of human brain: partial purification, characterization, regional distribution, and effect of certain modulators including psychoactive drugs | journal = Neurochemical Research | volume = 15 | issue = 12 | pages = 1203–10 | date = Dec 1990 | pmid = 1965857 | doi = 10.1007/BF01208581 }}
*{{cite journal | author=Minelli A, Piantanida M, Maserati E, ''et al.'' |title=Gene dosage effect in acquired monosomy 7: distinct behaviour of beta-glucuronidase and phosphoserine phosphatase. |journal=Genes Chromosomes Cancer |volume=1 |issue= 3 |pages= 216-20 |year= 1991 |pmid= 1964582 |doi= }}
* {{cite journal | vauthors = Novelli G, Dallapiccola B | title = Gene dosage studies regionally assign the phosphoserine phosphatase gene to 7p15.1 or 2 | journal = Annales de Génétique | volume = 31 | issue = 3 | pages = 195–6 | year = 1989 | pmid = 2851960 | doi =  }}
*{{cite journal | author=Veeranna , Shetty KT |title=Phosphoserine phosphatase of human brain: partial purification, characterization, regional distribution, and effect of certain modulators including psychoactive drugs. |journal=Neurochem. Res. |volume=15 |issue= 12 |pages= 1203-10 |year= 1991 |pmid= 1965857 |doi= }}
* {{cite journal | vauthors = Moro-Furlani AM, Turner VS, Hopkinson DA | title = Genetical and biochemical studies on human phosphoserine phosphatase | journal = Annals of Human Genetics | volume = 43 | issue = 4 | pages = 323–33 | date = May 1980 | pmid = 6249179 | doi = 10.1111/j.1469-1809.1980.tb01566.x }}
*{{cite journal | author=Novelli G, Dallapiccola B |title=Gene dosage studies regionally assign the phosphoserine phosphatase gene to 7p15.1 or 2. |journal=Ann. Genet. |volume=31 |issue= 3 |pages= 195-6 |year= 1989 |pmid= 2851960 |doi=  }}
* {{cite journal | vauthors = Sparkes RS, Mohandas T, Sparkes MC | title = The human phosphoserine phosphatase gene (PSP) is mapped to chromosome 7 by somatic cell genetic analysis | journal = Cytogenetics and Cell Genetics | volume = 35 | issue = 1 | pages = 70–1 | year = 1983 | pmid = 6297855 | doi = 10.1159/000131840 }}
*{{cite journal | author=Moro-Furlani AM, Turner VS, Hopkinson DA |title=Genetical and biochemical studies on human phosphoserine phosphatase. |journal=Ann. Hum. Genet. |volume=43 |issue= 4 |pages= 323-33 |year= 1980 |pmid= 6249179 |doi= }}
* {{cite journal | vauthors = Maruyama K, Sugano S | title = Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides | journal = Gene | volume = 138 | issue = 1-2 | pages = 171–4 | date = Jan 1994 | pmid = 8125298 | doi = 10.1016/0378-1119(94)90802-8 }}
*{{cite journal  | author=Koch GA, Eddy RL, Haley LL, ''et al.'' |title=Assignment of the human phosphoserine phosphatase gene (PSP) to the pter leads to q22 region of chromosome 7. |journal=Cytogenet. Cell Genet. |volume=35 |issue= 1 |pages= 67-9 |year= 1983 |pmid= 6297854 |doi=  }}
* {{cite journal | vauthors = Jaeken J, Detheux M, Fryns JP, Collet JF, Alliet P, Van Schaftingen E | title = Phosphoserine phosphatase deficiency in a patient with Williams syndrome | journal = Journal of Medical Genetics | volume = 34 | issue = 7 | pages = 594–6 | date = Jul 1997 | pmid = 9222972 | pmc = 1051004 | doi = 10.1136/jmg.34.7.594 }}
*{{cite journal | author=Sparkes RS, Mohandas T, Sparkes MC |title=The human phosphoserine phosphatase gene (PSP) is mapped to chromosome 7 by somatic cell genetic analysis. |journal=Cytogenet. Cell Genet. |volume=35 |issue= 1 |pages= 70-1 |year= 1983 |pmid= 6297855 |doi= }}
* {{cite journal | vauthors = Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S | title = Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library | journal = Gene | volume = 200 | issue = 1-2 | pages = 149–56 | date = Oct 1997 | pmid = 9373149 | doi = 10.1016/S0378-1119(97)00411-3 }}
*{{cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi= }}
* {{cite journal | vauthors = Collet JF, Stroobant V, Pirard M, Delpierre G, Van Schaftingen E | title = A new class of phosphotransferases phosphorylated on an aspartate residue in an amino-terminal DXDX(T/V) motif | journal = The Journal of Biological Chemistry | volume = 273 | issue = 23 | pages = 14107–12 | date = Jun 1998 | pmid = 9603909 | doi = 10.1074/jbc.273.23.14107 }}
*{{cite journal  | author=Collet JF, Gerin I, Rider MH, ''et al.'' |title=Human L-3-phosphoserine phosphatase: sequence, expression and evidence for a phosphoenzyme intermediate. |journal=FEBS Lett. |volume=408 |issue= 3 |pages= 281-4 |year= 1997 |pmid= 9188776 |doi=  }}
* {{cite journal | vauthors = Collet JF, Stroobant V, Van Schaftingen E | title = Mechanistic studies of phosphoserine phosphatase, an enzyme related to P-type ATPases | journal = The Journal of Biological Chemistry | volume = 274 | issue = 48 | pages = 33985–90 | date = Nov 1999 | pmid = 10567362 | doi = 10.1074/jbc.274.48.33985 }}
*{{cite journal | author=Jaeken J, Detheux M, Fryns JP, ''et al.'' |title=Phosphoserine phosphatase deficiency in a patient with Williams syndrome. |journal=J. Med. Genet. |volume=34 |issue= 7 |pages= 594-6 |year= 1997 |pmid= 9222972 |doi= }}
* {{cite journal | vauthors = Peeraer Y, Rabijns A, Verboven C, Collet JF, Van Schaftingen E, De Ranter C | title = Purification, crystallization and preliminary X-ray diffraction analysis of human phosphoserine phosphatase | journal = Acta Crystallographica Section D | volume = 58 | issue = Pt 1 | pages = 133–4 | date = Jan 2002 | pmid = 11752790 | doi = 10.1107/S0907444901017310 }}
*{{cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi= }}
* {{cite journal | vauthors = Kim HY, Heo YS, Kim JH, Park MH, Moon J, Kim E, Kwon D, Yoon J, Shin D, Jeong EJ, Park SY, Lee TG, Jeon YH, Ro S, Cho JM, Hwang KY | title = Molecular basis for the local conformational rearrangement of human phosphoserine phosphatase | journal = The Journal of Biological Chemistry | volume = 277 | issue = 48 | pages = 46651–8 | date = Nov 2002 | pmid = 12213811 | doi = 10.1074/jbc.M204866200 }}
*{{cite journal | author=Collet JF, Stroobant V, Pirard M, ''et al.'' |title=A new class of phosphotransferases phosphorylated on an aspartate residue in an amino-terminal DXDX(T/V) motif. |journal=J. Biol. Chem. |volume=273 |issue= 23 |pages= 14107-12 |year= 1998 |pmid= 9603909 |doi= }}
* {{cite journal | vauthors = Veiga-da-Cunha M, Collet JF, Prieur B, Jaeken J, Peeraer Y, Rabbijns A, Van Schaftingen E | title = Mutations responsible for 3-phosphoserine phosphatase deficiency | journal = European Journal of Human Genetics | volume = 12 | issue = 2 | pages = 163–6 | date = Feb 2004 | pmid = 14673469 | doi = 10.1038/sj.ejhg.5201083 }}
*{{cite journal | author=Collet JF, Stroobant V, Van Schaftingen E |title=Mechanistic studies of phosphoserine phosphatase, an enzyme related to P-type ATPases. |journal=J. Biol. Chem. |volume=274 |issue= 48 |pages= 33985-90 |year= 1999 |pmid= 10567362 |doi= }}
* {{cite journal | vauthors = Peeraer Y, Rabijns A, Collet JF, Van Schaftingen E, De Ranter C | title = How calcium inhibits the magnesium-dependent enzyme human phosphoserine phosphatase | journal = European Journal of Biochemistry / FEBS | volume = 271 | issue = 16 | pages = 3421–7 | date = Aug 2004 | pmid = 15291819 | doi = 10.1111/j.0014-2956.2004.04277.x }}
*{{cite journal | author=Peeraer Y, Rabijns A, Verboven C, ''et al.'' |title=Purification, crystallization and preliminary X-ray diffraction analysis of human phosphoserine phosphatase. |journal=Acta Crystallogr. D Biol. Crystallogr. |volume=58 |issue= Pt 1 |pages= 133-4 |year= 2002 |pmid= 11752790 |doi= }}
* {{cite journal | vauthors = Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D | title = Large-scale mapping of human protein-protein interactions by mass spectrometry | journal = Molecular Systems Biology | volume = 3 | issue = 1 | pages = 89 | year = 2007 | pmid = 17353931 | pmc = 1847948 | doi = 10.1038/msb4100134 }}
*{{cite journal | author=Kim HY, Heo YS, Kim JH, ''et al.'' |title=Molecular basis for the local conformational rearrangement of human phosphoserine phosphatase. |journal=J. Biol. Chem. |volume=277 |issue= 48 |pages= 46651-8 |year= 2003 |pmid= 12213811 |doi= 10.1074/jbc.M204866200 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal  | author=Veiga-da-Cunha M, Collet JF, Prieur B, ''et al.'' |title=Mutations responsible for 3-phosphoserine phosphatase deficiency. |journal=Eur. J. Hum. Genet. |volume=12 |issue= 2 |pages= 163-6 |year= 2004 |pmid= 14673469 |doi= 10.1038/sj.ejhg.5201083 }}
*{{cite journal | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal  | author=Peeraer Y, Rabijns A, Collet JF, ''et al.'' |title=How calcium inhibits the magnesium-dependent enzyme human phosphoserine phosphatase. |journal=Eur. J. Biochem. |volume=271 |issue= 16 |pages= 3421-7 |year= 2004 |pmid= 15291819 |doi= 10.1111/j.0014-2956.2004.04277.x }}
*{{cite journal | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal  | author=Ewing RM, Chu P, Elisma F, ''et al.'' |title=Large-scale mapping of human protein-protein interactions by mass spectrometry. |journal=Mol. Syst. Biol. |volume=3 |issue= |pages= 89 |year= 2007 |pmid= 17353931 |doi= 10.1038/msb4100134 }}
}}
{{refend}}
{{refend}}


{{protein-stub}}
{{PDB Gallery|geneid=5723}}
{{WikiDoc Sources}}

Latest revision as of 18:53, 7 September 2017

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

n/a

n/a

Ensembl

n/a

n/a

UniProt

n/a

n/a

RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Phosphoserine phosphatase is an enzyme that in humans is encoded by the PSPH gene.[1][2][3]

Function

The protein encoded by this gene belongs to a subfamily of the phosphotransferases. This encoded enzyme is responsible for the third and last step in L-serine formation. It catalyzes magnesium-dependent hydrolysis of L-phosphoserine and is also involved in an exchange reaction between L-serine and L-phosphoserine. Deficiency of this protein is thought to be linked to Williams syndrome.[3]

Clinical significance

Homozygous or compound heterozygous mutations in PSPH cause Neu-Laxova syndrome[4] and Phosphoserine phosphatase deficiency.[5][6]

Model organisms

Model organisms have been used in the study of PSPH function. A conditional knockout mouse line called Psphtm1a(EUCOMM)Hmgu was generated at the Wellcome Trust Sanger Institute.[7] Male and female animals underwent a standardized phenotypic screen[8] to determine the effects of deletion.[9][10][11][12] Additional screens performed: - In-depth immunological phenotyping[13]

References

  1. ↑ Koch GA, Eddy RL, Haley LL, Byers MG, McAvoy M, Shows TB (Apr 1983). "Assignment of the human phosphoserine phosphatase gene (PSP) to the pter leads to q22 region of chromosome 7". Cytogenetics and Cell Genetics. 35 (1): 67–9. doi:10.1159/000131839. PMID 6297854.
  2. ↑ Collet JF, Gerin I, Rider MH, Veiga-da-Cunha M, Van Schaftingen E (May 1997). "Human L-3-phosphoserine phosphatase: sequence, expression and evidence for a phosphoenzyme intermediate". FEBS Letters. 408 (3): 281–4. doi:10.1016/S0014-5793(97)00438-9. PMID 9188776.
  3. ↑ 3.0 3.1 "Entrez Gene: PSPH phosphoserine phosphatase".
  4. ↑ Acuna-Hidalgo R, Schanze D, Kariminejad A, Nordgren A, Kariminejad MH, Conner P, Grigelioniene G, Nilsson D, Nordenskjöld M, Wedell A, Freyer C, Wredenberg A, Wieczorek D, Gillessen-Kaesbach G, Kayserili H, Elcioglu N, Ghaderi-Sohi S, Goodarzi P, Setayesh H, van de Vorst M, Steehouwer M, Pfundt R, Krabichler B, Curry C, MacKenzie MG, Boycott KM, Gilissen C, Janecke AR, Hoischen A, Zenker M (Sep 2014). "Neu-Laxova syndrome is a heterogeneous metabolic disorder caused by defects in enzymes of the L-serine biosynthesis pathway". American Journal of Human Genetics. 95 (3): 285–93. doi:10.1016/j.ajhg.2014.07.012. PMC 4157144. PMID 25152457.
  5. ↑ Veiga-da-Cunha M, Collet JF, Prieur B, Jaeken J, Peeraer Y, Rabbijns A, Van Schaftingen E (Feb 2004). "Mutations responsible for 3-phosphoserine phosphatase deficiency". European Journal of Human Genetics. 12 (2): 163–6. doi:10.1038/sj.ejhg.5201083. PMID 14673469.
  6. ↑ Jaeken J, Detheux M, Fryns JP, Collet JF, Alliet P, Van Schaftingen E (Jul 1997). "Phosphoserine phosphatase deficiency in a patient with Williams syndrome". Journal of Medical Genetics. 34 (7): 594–6. doi:10.1136/jmg.34.7.594. PMC 1051004. PMID 9222972.
  7. ↑ Gerdin AK (2010). "The Sanger Mouse Genetics Programme: high throughput characterisation of knockout mice". Acta Ophthalmologica. 88: 925–7. doi:10.1111/j.1755-3768.2010.4142.x.
  8. ↑ 8.0 8.1 "International Mouse Phenotyping Consortium".
  9. ↑ Skarnes WC, Rosen B, West AP, Koutsourakis M, Bushell W, Iyer V, Mujica AO, Thomas M, Harrow J, Cox T, Jackson D, Severin J, Biggs P, Fu J, Nefedov M, de Jong PJ, Stewart AF, Bradley A (Jun 2011). "A conditional knockout resource for the genome-wide study of mouse gene function". Nature. 474 (7351): 337–42. doi:10.1038/nature10163. PMC 3572410. PMID 21677750.
  10. ↑ Dolgin E (Jun 2011). "Mouse library set to be knockout". Nature. 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718.
  11. ↑ Collins FS, Rossant J, Wurst W (Jan 2007). "A mouse for all reasons". Cell. 128 (1): 9–13. doi:10.1016/j.cell.2006.12.018. PMID 17218247.
  12. ↑ White JK, Gerdin AK, Karp NA, Ryder E, Buljan M, Bussell JN, Salisbury J, Clare S, Ingham NJ, Podrini C, Houghton R, Estabel J, Bottomley JR, Melvin DG, Sunter D, Adams NC, Tannahill D, Logan DW, Macarthur DG, Flint J, Mahajan VB, Tsang SH, Smyth I, Watt FM, Skarnes WC, Dougan G, Adams DJ, Ramirez-Solis R, Bradley A, Steel KP (Jul 2013). "Genome-wide generation and systematic phenotyping of knockout mice reveals new roles for many genes". Cell. 154 (2): 452–64. doi:10.1016/j.cell.2013.06.022. PMC 3717207. PMID 23870131.
  13. ↑ 13.0 13.1 "Infection and Immunity Immunophenotyping (3i) Consortium".

Further reading

  • Minelli A, Piantanida M, Maserati E, Campagnoli E, Pasquali F, Danesino C (Jan 1990). "Gene dosage effect in acquired monosomy 7: distinct behaviour of beta-glucuronidase and phosphoserine phosphatase". Genes, Chromosomes & Cancer. 1 (3): 216–20. doi:10.1002/gcc.2870010305. PMID 1964582.
  • Shetty KT (Dec 1990). "Phosphoserine phosphatase of human brain: partial purification, characterization, regional distribution, and effect of certain modulators including psychoactive drugs". Neurochemical Research. 15 (12): 1203–10. doi:10.1007/BF01208581. PMID 1965857.
  • Novelli G, Dallapiccola B (1989). "Gene dosage studies regionally assign the phosphoserine phosphatase gene to 7p15.1 or 2". Annales de Génétique. 31 (3): 195–6. PMID 2851960.
  • Moro-Furlani AM, Turner VS, Hopkinson DA (May 1980). "Genetical and biochemical studies on human phosphoserine phosphatase". Annals of Human Genetics. 43 (4): 323–33. doi:10.1111/j.1469-1809.1980.tb01566.x. PMID 6249179.
  • Sparkes RS, Mohandas T, Sparkes MC (1983). "The human phosphoserine phosphatase gene (PSP) is mapped to chromosome 7 by somatic cell genetic analysis". Cytogenetics and Cell Genetics. 35 (1): 70–1. doi:10.1159/000131840. PMID 6297855.
  • Maruyama K, Sugano S (Jan 1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
  • Jaeken J, Detheux M, Fryns JP, Collet JF, Alliet P, Van Schaftingen E (Jul 1997). "Phosphoserine phosphatase deficiency in a patient with Williams syndrome". Journal of Medical Genetics. 34 (7): 594–6. doi:10.1136/jmg.34.7.594. PMC 1051004. PMID 9222972.
  • Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (Oct 1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
  • Collet JF, Stroobant V, Pirard M, Delpierre G, Van Schaftingen E (Jun 1998). "A new class of phosphotransferases phosphorylated on an aspartate residue in an amino-terminal DXDX(T/V) motif". The Journal of Biological Chemistry. 273 (23): 14107–12. doi:10.1074/jbc.273.23.14107. PMID 9603909.
  • Collet JF, Stroobant V, Van Schaftingen E (Nov 1999). "Mechanistic studies of phosphoserine phosphatase, an enzyme related to P-type ATPases". The Journal of Biological Chemistry. 274 (48): 33985–90. doi:10.1074/jbc.274.48.33985. PMID 10567362.
  • Peeraer Y, Rabijns A, Verboven C, Collet JF, Van Schaftingen E, De Ranter C (Jan 2002). "Purification, crystallization and preliminary X-ray diffraction analysis of human phosphoserine phosphatase". Acta Crystallographica Section D. 58 (Pt 1): 133–4. doi:10.1107/S0907444901017310. PMID 11752790.
  • Kim HY, Heo YS, Kim JH, Park MH, Moon J, Kim E, Kwon D, Yoon J, Shin D, Jeong EJ, Park SY, Lee TG, Jeon YH, Ro S, Cho JM, Hwang KY (Nov 2002). "Molecular basis for the local conformational rearrangement of human phosphoserine phosphatase". The Journal of Biological Chemistry. 277 (48): 46651–8. doi:10.1074/jbc.M204866200. PMID 12213811.
  • Veiga-da-Cunha M, Collet JF, Prieur B, Jaeken J, Peeraer Y, Rabbijns A, Van Schaftingen E (Feb 2004). "Mutations responsible for 3-phosphoserine phosphatase deficiency". European Journal of Human Genetics. 12 (2): 163–6. doi:10.1038/sj.ejhg.5201083. PMID 14673469.
  • Peeraer Y, Rabijns A, Collet JF, Van Schaftingen E, De Ranter C (Aug 2004). "How calcium inhibits the magnesium-dependent enzyme human phosphoserine phosphatase". European Journal of Biochemistry / FEBS. 271 (16): 3421–7. doi:10.1111/j.0014-2956.2004.04277.x. PMID 15291819.
  • Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Molecular Systems Biology. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.
Retrieved from "https://www.wikidoc.org/index.php?title=PSPH&oldid=1421674"