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Information on EC 3.1.3.16 - protein-serine/threonine phosphatase and Organism(s) Solanum lycopersicum and UniProt Accession Q84K11
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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: Solanum lycopersicum
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
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-
-
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Aspergillus awamori acid protein phosphatase
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-
-
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BCKDH phosphatase
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-
-
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branched-chain alpha-keto acid dehydrogenase phosphatase
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-
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calcineurin
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-
-
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Calcineurin A1
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-
-
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Calcineurin A2
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-
-
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CaM-kinase phosphatase
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-
-
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CaMKPase
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-
-
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casein phosphatase
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-
-
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DRES10
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-
-
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Fibroblast growth factor inducible protein 13
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-
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FIN13
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-
-
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Flap wing protein
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-
-
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HMG-CoA reductase phosphatase
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-
-
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Magnesium-dependent calcium inhibitable phosphatase
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-
-
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MCPP
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-
-
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Microtubule star protein
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-
-
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phosphatase 2A
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-
-
-
phosphatase 2B
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-
-
-
phosphatase C-II
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-
-
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Phosphatase esp1
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-
-
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phosphatase H-II
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-
-
-
phosphatase I
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-
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-
phosphatase IB
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-
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-
phosphatase II
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-
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phosphatase III
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-
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-
phosphatase IV
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-
-
-
phosphatase SP
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-
-
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phosphoprotein phosphatase
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-
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phosphopyruvate dehydrogenase phosphatase
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-
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phosphospectrin phosphatase
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-
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PK-Pase
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-
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polycation modulated (PCM-) phosphatase
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-
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PP-1A
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-
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PP-1B
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-
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PP-1G
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-
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PP2A-alpha
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PP2A-beta
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-
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PP2C
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-
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PP2C-alpha
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-
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PP2C-beta
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-
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PP2C-delta
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-
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PP2C-gamma
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-
-
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Pp4
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-
-
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PP5
-
-
-
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PP6
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-
-
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PPEF
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-
-
-
PPN
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-
-
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PPT
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-
-
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protein D phosphatase
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-
-
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protein phosphatase
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-
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Protein phosphatase 1A
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-
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Protein phosphatase 1B
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-
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Protein phosphatase 1C
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-
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Protein phosphatase magnesium-dependent 1 delta
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-
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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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-
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PS2;1 protein
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plays an important role in phosphate starvation-induced processes in tomato
PSPase
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-
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Retinal degeneration C protein
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Suppressor protein SDS21
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
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-
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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
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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
RRApTVA + H2O
RRATVA + phosphate
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a protein concentration at 15 ng per reaction was found to be optimal for dephosphorylation of the synthetic peptide RRApTVA, maximum enzyme activity can be achieved in the presence of 100 ng of substrate
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-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
addition of Mg2+ and Ca2+ does not affect the enzyme activity
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
addition of EGTA and vanadate to the assay does not affect the enzyme activity
-
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
0.245
DELTATPR at pH 7.5 with p-nitrophenyl phosphate as substrate
pH 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
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). PPP5_SOLLC
556
2
61860
Swiss-Prot
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
removal of the TPR domain leads to a higher specific activity than wild-type enzyme at pH 7.5 but not at pH 5
additional information
-
removal of the TPR domain leads to a higher specific activity than wild-type enzyme at pH 7.5 but not at pH 5
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
de la Fuente van Bentem, S.; Vossen, J.H.; Vermeer, J.E.; de Vroomen, M.J.; Gadella, T.W., Jr.; Haring, M.A.; Cornelissen, B.J.
The subcellular localization of plant protein phosphatase 5 isoforms is determined by alternative splicing
Plant Physiol.
133
702-712
2003
Rattus norvegicus (P53042), Solanum lycopersicum (Q84K11), Solanum lycopersicum
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Release 2023.1 (January 2023)
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