PSPH

Phosphoserine phosphatase is an enzyme that in humans is encoded by the PSPH gene.[5][6][7]

PSPH
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesPSPH, PSP, PSPHD, phosphoserine phosphatase
External IDsOMIM: 172480 MGI: 97788 HomoloGene: 31245 GeneCards: PSPH
Gene location (Human)
Chr.Chromosome 7 (human)[1]
Band7p11.2Start56,011,051 bp[1]
End56,051,604 bp[1]
RNA expression pattern




More reference expression data
Orthologs
SpeciesHumanMouse
Entrez

5723

100678

Ensembl

ENSG00000146733

ENSMUSG00000029446

UniProt

P78330

Q99LS3

RefSeq (mRNA)

NM_004577

NM_133900

RefSeq (protein)

NP_598661

Location (UCSC)Chr 7: 56.01 – 56.05 MbChr 5: 129.77 – 129.79 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

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.[7]

Clinical significance

Homozygous or compound heterozygous mutations in PSPH cause Neu-Laxova syndrome[8] and Phosphoserine phosphatase deficiency.[9][10]

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.[11] Male and female animals underwent a standardized phenotypic screen[12] to determine the effects of deletion.[13][14][15][16] Additional screens performed: - In-depth immunological phenotyping[17]

References
  1. GRCh38: Ensembl release 89: ENSG00000146733 - Ensembl, May 2017
  2. GRCm38: Ensembl release 89: ENSMUSG00000029446 - Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. 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.
  6. 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. S2CID 6952728.
  7. "Entrez Gene: PSPH phosphoserine phosphatase".
  8. 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.
  9. 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.
  10. 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.
  11. 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. S2CID 85911512.
  12. "International Mouse Phenotyping Consortium".
  13. 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.
  14. Dolgin E (Jun 2011). "Mouse library set to be knockout". Nature. 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718.
  15. 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. S2CID 18872015.
  16. 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.
  17. "Infection and Immunity Immunophenotyping (3i) Consortium".

Further reading
  • Overview of all the structural information available in the PDB for UniProt: P78330 (Phosphoserine phosphatase) at the PDBe-KB.
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