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EC Tree
IUBMB Comments A group of enzymes removing the serine- or threonine-bound phosphate group from a wide range of phosphoproteins, including a number of enzymes that have been phosphorylated under the action of a kinase (cf. EC 3.1.3.48 protein-tyrosine-phosphatase). The spleen enzyme also acts on phenolic phosphates and phosphamides (cf. EC 3.9.1.1, phosphoamidase).
The taxonomic range for the selected organisms is: Plasmodium falciparum The enzyme appears in selected viruses and cellular organisms
Synonyms
calcineurin, protein phosphatase, pac-1, dusp1, dusp6, serine/threonine phosphatase, pp2ac, ppm1d, phosphoprotein phosphatase, laforin,
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3-hydroxy 3-methylglutaryl CoenzymeA reductase phosphatase
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Aspergillus awamori acid protein phosphatase
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BCKDH phosphatase
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branched-chain alpha-keto acid dehydrogenase phosphatase
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CaM-kinase phosphatase
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casein phosphatase
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Fibroblast growth factor inducible protein 13
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Flap wing protein
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HMG-CoA reductase phosphatase
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Magnesium-dependent calcium inhibitable phosphatase
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Microtubule star protein
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phosphoprotein phosphatase
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phosphopyruvate dehydrogenase phosphatase
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phosphospectrin phosphatase
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polycation modulated (PCM-) phosphatase
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protein D phosphatase
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protein phosphatase
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Protein phosphatase 1A
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Protein phosphatase 1B
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Protein phosphatase 1C
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Protein phosphatase magnesium-dependent 1 delta
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Protein phosphatase magnesium-dependent 1 gamma
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Protein phosphatase with EF calcium-binding domain
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Retinal degeneration C protein
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Ser/Thr protein phosphatase type 1
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Suppressor protein SDS21
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PP5
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hydrolysis of phosphoric ester
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protein-serine/threonine-phosphate phosphohydrolase
A group of enzymes removing the serine- or threonine-bound phosphate group from a wide range of phosphoproteins, including a number of enzymes that have been phosphorylated under the action of a kinase (cf. EC 3.1.3.48 protein-tyrosine-phosphatase). The spleen enzyme also acts on phenolic phosphates and phosphamides (cf. EC 3.9.1.1, phosphoamidase).
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p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
phosphophosphorylase kinase + H2O
phosphorylase kinase + phosphate
specific for alpha-subunit
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phosphoproteins + H2O
proteins + phosphate
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phosphorylated phosphorylase alpha + H2O
phosphorylase alpha + phosphate
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[a protein]-serine/threonine phosphate + H2O
[a protein]-serine/threonine + phosphate
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p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
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p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
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very low activity
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p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
very low activity
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[a protein]-serine/threonine phosphate + H2O
[a protein]-serine/threonine + phosphate
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?
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Calmodulin
stimulation of phosphatase PfPP2B
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Ni2+
phosphatase PfPP2A, Ni2+ can replace Mn2+ in activation
Ca2+
phosphatase PfPP2B, activated by Ca2+ plus calmodulin
Ca2+
phosphatase PfPP2A, Ca2+ can replace Mn2+ in activation
Mn2+
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Mn2+
required by phosphatase PfPP2A
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cyclosporin A
inhibition of phosphatase PfPP2B
Trifluoperazine
inhibition of phosphatase PfPP2B
okadaic acid
no inhibition
okadaic acid
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IC50: 4 nM
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0.000004
okadaic acid
Plasmodium falciparum
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IC50: 4 nM
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Uniprot
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Uniprot
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UniProt
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at lower concentrations than in the nucleus
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low levels
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predominantly
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physiological function
protein phosphatase 1 (PP1) is an enzyme essential to cell viability in the malaria parasite Plasmodium falciparum. The activity of PP1 is regulated by the binding of regulatory subunits, of which there are 3 reported for the parasite to date
additional information
detection of the PfPP1 interactome and PP1 interacting proteins (Pips) by mass spectrometry, yeast two-hybrid screening, and in silico analysis of the Plasmodium falciparum predicted proteome. The Pips include a large range of proteins, overview
additional information
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detection of the PfPP1 interactome and PP1 interacting proteins (Pips) by mass spectrometry, yeast two-hybrid screening, and in silico analysis of the Plasmodium falciparum predicted proteome. The Pips include a large range of proteins, overview
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Q9U493_PLAFA
294
0
33792
TrEMBL
other Location (Reliability: 3 )
Q8WQR3_PLAFA
594
0
69196
TrEMBL
other Location (Reliability: 1 )
Q962N7_PLAFA
594
0
69249
TrEMBL
other Location (Reliability: 1 )
O15920_PLAFA
466
0
53723
TrEMBL
other Location (Reliability: 2 )
Q8MX29_PLAFA
304
0
34904
TrEMBL
other Location (Reliability: 2 )
O96914_PLAFA
875
0
99191
TrEMBL
other Location (Reliability: 2 )
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34000
x * 34000, SDS-PAGE and calculated from nucleic acid sequence
80000
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x * 80000, SDS-PAGE
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?
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x * 80000, SDS-PAGE
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x * 34000, SDS-PAGE and calculated from nucleic acid sequence
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expression in Escherichia coli
expression in Escherichia coli M15
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Dobson, S.; May, T.; Berriman, M.; Del Vecchio, C.; Fairlamb, A.H.; Chakrabarti, D.; Barik, S.
Characterization of protein Ser/Thr phosphatases of the malaria parasite, Plasmodium falciparum: inhibition of the parasitic calcineurin by cyclophilin-cyclosporin complex
Mol. Biochem. Parasitol.
99
167-181
1999
Plasmodium falciparum (O15920), Plasmodium falciparum
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Dobson, S.; Bracchi, V.; Chakrabarti, D.; Barik, S.
Characterization of a novel serine/threonine protein phosphatase (PfPPJ) from the malaria parasite, Plasmodium falciparum
Mol. Biochem. Parasitol.
115
29-39
2001
Plasmodium falciparum (Q9U493), Plasmodium falciparum
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Lindenthal, C.; Klinkert, M.Q.
Identification and biochemical characterisation of a protein phosphatase 5 homologue from Plasmodium falciparum
Mol. Biochem. Parasitol.
120
257-268
2002
Plasmodium falciparum
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Chinkers, M.
PP5: the TPR phosphatase
Topics in Current Genetics (Arino, J. , Alexander, D. R. Eds. ) Springer
5
107-130
2004
Drosophila melanogaster, Neurospora crassa, Plasmodium falciparum, Rattus norvegicus, Trypanosoma brucei
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Hollin, T.; De Witte, C.; Lenne, A.; Pierrot, C.; Khalife, J.
Analysis of the interactome of the Ser/Thr protein phosphatase type 1 in Plasmodium falciparum
BMC Genomics
17
246
2016
Plasmodium falciparum (Q8ILV1), Plasmodium falciparum
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