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Information on EC 3.1.3.16 - protein-serine/threonine phosphatase and Organism(s) Plasmodium falciparum and UniProt Accession O15920
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3.1.3.16 protein-serine/threonine phosphataseIUBMB 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).
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Word Map
- 3.1.3.16
-
cyclosporine
- phosphatases
- tacrolimus
-
rejection
-
okadaic
- mycophenolate
-
allograft
- cardiac
- steroid
-
corticosteroid
- mofetil
- rapamycin
-
nephrotoxicity
- nfat
- sirolimus
- agonist
- t-cells
- creatinine
- hypertrophy
- mapks
- glycogen
- synaptic
- mtor
-
glomerular
- pkc
- platelet
-
ca2+-dependent
- hypertension
- episode
- erk
-
atopic
- cardiomyocytes
- nephropathy
-
everolimus
- dermatitis
- myocytes
-
trough
-
hyperphosphorylation
- azathioprine
-
posttransplant
-
prophylaxis
-
allogeneic
- proteinuria
- camkii
-
post-transplantation
- graft-versus-host
- rituximab
- cyclophilins
-
biopsy-proven
- prednisone
- diagnostics
- analysis
- drug development
- medicine
The taxonomic range for the selected organisms is: Plasmodium falciparum
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
calcineurin, protein phosphatase, pac-1, dusp1, dusp6, serine/threonine phosphatase, pp2ac, ppm1d, phosphoprotein phosphatase, laforin, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3-hydroxy 3-methylglutaryl CoenzymeA reductase phosphatase
-
-
-
-
Aspergillus awamori acid protein phosphatase
-
-
-
-
BCKDH phosphatase
-
-
-
-
branched-chain alpha-keto acid dehydrogenase phosphatase
-
-
-
-
calcineurin
-
-
-
-
Calcineurin A1
-
-
-
-
Calcineurin A2
-
-
-
-
CaM-kinase phosphatase
-
-
-
-
CaMKPase
-
-
-
-
casein phosphatase
-
-
-
-
DRES10
-
-
-
-
Fibroblast growth factor inducible protein 13
-
-
-
-
FIN13
-
-
-
-
Flap wing protein
-
-
-
-
HMG-CoA reductase phosphatase
-
-
-
-
Magnesium-dependent calcium inhibitable phosphatase
-
-
-
-
MCPP
-
-
-
-
Microtubule star protein
-
-
-
-
phosphatase 2A
-
-
-
-
phosphatase 2B
-
-
-
-
phosphatase C-II
-
-
-
-
Phosphatase esp1
-
-
-
-
phosphatase H-II
-
-
-
-
phosphatase I
-
-
-
-
phosphatase IB
-
-
-
-
phosphatase II
-
-
-
-
phosphatase III
-
-
-
-
phosphatase IV
-
-
-
-
phosphatase SP
-
-
-
-
phosphoprotein phosphatase
-
-
-
-
phosphopyruvate dehydrogenase phosphatase
-
-
-
-
phosphospectrin phosphatase
-
-
-
-
PK-Pase
-
-
-
-
polycation modulated (PCM-) phosphatase
-
-
-
-
PP-1A
-
-
-
-
PP-1B
-
-
-
-
PP-1G
-
-
-
-
PP2A-alpha
-
-
-
-
PP2A-beta
-
-
-
-
PP2C
-
-
-
-
PP2C-alpha
-
-
-
-
PP2C-beta
-
-
-
-
PP2C-delta
-
-
-
-
PP2C-gamma
-
-
-
-
Pp4
-
-
-
-
PP5
PP6
-
-
-
-
PPEF
-
-
-
-
PPN
-
-
-
-
PPT
-
-
-
-
protein D phosphatase
-
-
-
-
protein phosphatase
-
-
-
-
Protein phosphatase 1A
-
-
-
-
Protein phosphatase 1B
-
-
-
-
Protein phosphatase 1C
-
-
-
-
Protein phosphatase magnesium-dependent 1 delta
-
-
-
-
Protein phosphatase magnesium-dependent 1 gamma
-
-
-
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Protein phosphatase with EF calcium-binding domain
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-
-
-
PSPase
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-
-
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Retinal degeneration C protein
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-
-
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Suppressor protein SDS21
-
-
-
-
PP5
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
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-
-
-
SYSTEMATIC NAME
IUBMB Comments
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).
CAS REGISTRY NUMBER
COMMENTARY
9025-75-6
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
phosphophosphorylase kinase + H2O
phosphorylase kinase + phosphate
specific for alpha-subunit
-
-
?
phosphorylated phosphorylase alpha + H2O
phosphorylase alpha + phosphate
-
-
-
?
[a protein]-serine/threonine phosphate + H2O
[a protein]-serine/threonine + phosphate
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
very low activity
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
very low activity
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
[a protein]-serine/threonine phosphate + H2O
[a protein]-serine/threonine + phosphate
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
-
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). O15920_PLAFA
466
0
53723
TrEMBL
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
34000
x * 34000, SDS-PAGE and calculated from nucleic acid sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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
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
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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