PSPH

Enzyme found in humans
PSPH
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

1L8L, 1L8O, 1NNL

Identifiers
AliasesPSPH, PSP, PSPHD, phosphoserine phosphatase
External IDsOMIM: 172480; MGI: 97788; HomoloGene: 31245; GeneCards: PSPH; OMA:PSPH - orthologs
Gene location (Human)
Chromosome 7 (human)
Chr.Chromosome 7 (human)[1]
Chromosome 7 (human)
Genomic location for PSPH
Genomic location for PSPH
Band7p11.2Start56,011,051 bp[1]
End56,051,604 bp[1]
Gene location (Mouse)
Chromosome 5 (mouse)
Chr.Chromosome 5 (mouse)[2]
Chromosome 5 (mouse)
Genomic location for PSPH
Genomic location for PSPH
Band5|5 G1.3Start129,842,622 bp[2]
End129,864,513 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • right uterine tube

  • stromal cell of endometrium

  • C1 segment

  • ventricular zone

  • right adrenal cortex

  • gonad

  • muscle of thigh

  • nucleus accumbens

  • prefrontal cortex

  • caudate nucleus
Top expressed in
  • seminal vesicula

  • yolk sac

  • lip

  • skin of external ear

  • calvaria

  • ventricular zone

  • endothelial cell of lymphatic vessel

  • medial ganglionic eminence

  • vestibular sensory epithelium

  • epidermis
More reference expression data
BioGPS




More reference expression data
Gene ontology
Molecular function
  • calcium ion binding
  • protein homodimerization activity
  • metal ion binding
  • hydrolase activity
  • magnesium ion binding
  • phosphatase activity
Cellular component
  • cytosol
  • neuron projection
  • cytoplasm
Biological process
  • response to testosterone
  • response to mechanical stimulus
  • response to nutrient levels
  • L-serine metabolic process
  • cellular amino acid biosynthetic process
  • dephosphorylation
  • L-serine biosynthetic process
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

5723

100678

Ensembl

ENSG00000146733

ENSMUSG00000029446

UniProt

P78330

Q99LS3

RefSeq (mRNA)

NM_004577

NM_133900

RefSeq (protein)
NP_004568
NP_001357432
NP_001357433
NP_001357434
NP_001357435

NP_001357436
NP_001357437
NP_001357438
NP_001357439
NP_001357440
NP_001357441
NP_001357442
NP_001357443
NP_001357444
NP_001357445
NP_001357446
NP_001357447
NP_001357448
NP_001357449
NP_001357450
NP_001357451

NP_598661

Location (UCSC)Chr 7: 56.01 – 56.05 MbChr 5: 129.84 – 129.86 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

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

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]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000146733 – Ensembl, May 2017
  2. ^ a b c 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. ^ a b "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.

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. S2CID 31576324.
  • 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. S2CID 24831337.
  • 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. S2CID 13270060.
  • 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. Bibcode:2002AcCrD..58..133P. 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. 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.

External links

  • Overview of all the structural information available in the PDB for UniProt: P78330 (Phosphoserine phosphatase) at the PDBe-KB.
  • v
  • t
  • e
  • 1l8l: Molecular basis for the local confomational rearrangement of human phosphoserine phosphatase
    1l8l: Molecular basis for the local confomational rearrangement of human phosphoserine phosphatase
  • 1l8o: Molecular basis for the local conformational rearrangement of human phosphoserine phosphatase
    1l8o: Molecular basis for the local conformational rearrangement of human phosphoserine phosphatase
  • 1nnl: Crystal structure of Human Phosphoserine Phosphatase
    1nnl: Crystal structure of Human Phosphoserine Phosphatase