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Information on EC 3.1.3.16 - protein-serine/threonine phosphatase and Organism(s) Caenorhabditis elegans

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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.3 Phosphoric-monoester hydrolases
                3.1.3.16 protein-serine/threonine phosphatase
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).
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This record set is specific for:
Caenorhabditis elegans
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Word Map
The taxonomic range for the selected organisms is: Caenorhabditis elegans
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, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
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
-
-
-
-
phosphoglycerate mutase 5
-
PGAM5 lacks PGAM activity and instead associates with signal-regulating kinase 1 and acts as a specific protein Ser/Thr phosphatase that activates apoptosis signal-regulating kinase 1, PGAM5 is a protein Ser/Thr phosphatase unrelated to the other known families of Ser/Thr phosphatases
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
-
-
-
-
PP5
-
-
-
-
PP6
-
-
-
-
PPEF
-
-
-
-
PPN
-
-
-
-
PPT
-
-
-
-
protein D phosphatase
-
-
-
-
protein phosphatase
-
-
-
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Protein phosphatase 1A
-
-
-
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Protein phosphatase 1B
-
-
-
-
Protein phosphatase 1C
-
-
-
-
protein phosphatase 4
-
-
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
-
-
-
-
PSPase
-
-
-
-
Retinal degeneration C protein
-
-
-
-
SCPL-1a
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isozyme
SCPL-1b
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isozyme
serine/threonine phosphatase
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-
small CTD phosphatase-like-1
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the protein contains a C-terminal domain phosphatase type domain
Suppressor protein SDS21
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
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 hide
9025-75-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
-
-
-
-
?
p38 + H2O
?
show the reaction diagram
-
-
-
-
?
phosphorylated apoptosis signal-regulating kinase 1 + H2O
apoptosis signal-regulating kinase 1 + phosphate
show the reaction diagram
-
PGAM5 acts as a specific protein Ser/Thr phosphatase that activates apoptosis signal-regulating kinase 1 by dephosphorylation of inhibitory sites (phosphorylation of Thr-838), PGAM5 serves as a specialized activator of apoptosis signal-regulating kinase 1
-
-
?
RRApSVA + H2O
?
show the reaction diagram
-
-
-
-
?
RRApTVA + H2O
?
show the reaction diagram
-
-
-
-
?
UNC-89 + H2O
?
show the reaction diagram
-
the protein kinase 2 region of UNC-89 specifically interacts with SCPL-1
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
the holoenzyme plays a role in organelle assembly and is essential for maturation of the centrosome, overview, PP4 depletion results in disrupted centrosome maturation and a decreased number of chiasmata between homologous chromosomes during meiosis in oocytes
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
SCPL-1 is dependent on Mg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
SCPL-1 is not inhibited by the typical phosphatase inhibitors NaF, BeCl2, AlCl3, and Na3VO4
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Calmodulin
-
calcineurin is a Ca2+/calmodulin-activated Ser/Thr phosphatase
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
-
around pH 5.0
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
membrane-associated, N-terminus is neccessary for membrane association
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
FEM2_CAEEL
449
0
50898
Swiss-Prot
other Location (Reliability: 1)
PTEN_CAEEL
962
0
110329
Swiss-Prot
other Location (Reliability: 2)
PP2A_CAEEL
318
0
36302
Swiss-Prot
other Location (Reliability: 1)
SSU72_CAEEL
197
0
22775
Swiss-Prot
other Location (Reliability: 5)
YT91_CAEEL
364
0
41208
Swiss-Prot
other Location (Reliability: 1)
GLC7A_CAEEL
329
0
37205
Swiss-Prot
other Location (Reliability: 2)
GLC7B_CAEEL
333
0
37792
Swiss-Prot
other Location (Reliability: 2)
GLC7C_CAEEL
305
0
34596
Swiss-Prot
other Location (Reliability: 3)
GLC7D_CAEEL
305
0
34584
Swiss-Prot
other Location (Reliability: 3)
PHLPP_CAEEL
1126
0
128125
Swiss-Prot
other Location (Reliability: 3)
PPM1A_CAEEL
468
0
51899
Swiss-Prot
other Location (Reliability: 3)
PPP5_CAEEL
496
0
56462
Swiss-Prot
other Location (Reliability: 2)
PP2B_CAEEL
542
0
61505
Swiss-Prot
other Location (Reliability: 2)
PP2C2_CAEEL
356
0
39064
Swiss-Prot
other Location (Reliability: 1)
PP4C1_CAEEL
333
0
37359
Swiss-Prot
other Location (Reliability: 2)
PP4C2_CAEEL
321
0
36306
Swiss-Prot
other Location (Reliability: 1)
PPM1G_CAEEL
491
0
53142
Swiss-Prot
other Location (Reliability: 1)
DUSL_CAEEL
381
0
42174
Swiss-Prot
other Location (Reliability: 2)
PPE_CAEEL
707
0
80330
Swiss-Prot
other Location (Reliability: 5)
FCP1_CAEEL
659
0
74412
Swiss-Prot
other Location (Reliability: 1)
YSD1_CAEEL
454
0
51755
Swiss-Prot
other Location (Reliability: 1)
PGAM5_CAEEL
284
0
32490
Swiss-Prot
Secretory Pathway (Reliability: 3)
YY06_CAEEL
454
0
51597
Swiss-Prot
other Location (Reliability: 2)
CNEP1_CAEEL
246
1
28414
Swiss-Prot
Secretory Pathway (Reliability: 3)
PPP6_CAEEL
331
0
37388
Swiss-Prot
other Location (Reliability: 1)
RPAP2_CAEEL
455
0
52438
Swiss-Prot
other Location (Reliability: 1)
SCPL1_CAEEL
491
0
54372
Swiss-Prot
other Location (Reliability: 2)
Q27501_CAEEL
329
0
37221
TrEMBL
other Location (Reliability: 2)
Q4R171_CAEEL
300
0
33964
TrEMBL
other Location (Reliability: 2)
O45001_CAEEL
364
0
41570
TrEMBL
other Location (Reliability: 1)
O16334_CAEEL
333
0
38032
TrEMBL
Secretory Pathway (Reliability: 3)
Q27500_CAEEL
384
0
43316
TrEMBL
other Location (Reliability: 2)
Q9XW33_CAEEL
375
0
43031
TrEMBL
other Location (Reliability: 2)
P91273_CAEEL
383
0
43552
TrEMBL
other Location (Reliability: 2)
G5EC18_CAEEL
349
0
39746
TrEMBL
other Location (Reliability: 4)
Q9U3L7_CAEEL
316
0
35803
TrEMBL
other Location (Reliability: 3)
O18183_CAEEL
330
0
35292
TrEMBL
Mitochondrion (Reliability: 3)
O44507_CAEEL
383
0
42677
TrEMBL
other Location (Reliability: 2)
K8FE09_CAEEL
319
0
35554
TrEMBL
other Location (Reliability: 2)
Q21840_CAEEL
362
0
41318
TrEMBL
other Location (Reliability: 2)
Q9XVD6_CAEEL
384
0
43267
TrEMBL
other Location (Reliability: 2)
A0A0K3AU53_CAEEL
459
0
52056
TrEMBL
other Location (Reliability: 4)
W6RTP7_CAEEL
253
0
28390
TrEMBL
other Location (Reliability: 3)
Q27528_CAEEL
343
0
39142
TrEMBL
other Location (Reliability: 3)
P91569_CAEEL
296
0
34310
TrEMBL
Mitochondrion (Reliability: 1)
W6SBL5_CAEEL
204
0
22584
TrEMBL
Mitochondrion (Reliability: 5)
Q95020_CAEEL
105
0
12158
TrEMBL
other Location (Reliability: 4)
O62272_CAEEL
364
0
41162
TrEMBL
other Location (Reliability: 1)
Q4W5Q9_CAEEL
333
0
37546
TrEMBL
other Location (Reliability: 2)
Q7JK71_CAEEL
169
0
19397
TrEMBL
other Location (Reliability: 1)
Q27475_CAEEL
329
0
37336
TrEMBL
other Location (Reliability: 2)
G4SR74_CAEEL
306
0
34969
TrEMBL
other Location (Reliability: 3)
Q27494_CAEEL
368
0
42652
TrEMBL
other Location (Reliability: 1)
Q27495_CAEEL
329
0
37928
TrEMBL
other Location (Reliability: 2)
Q9U395_CAEEL
371
0
42243
TrEMBL
other Location (Reliability: 1)
Q9U3P4_CAEEL
384
0
43257
TrEMBL
other Location (Reliability: 3)
G5ECL6_CAEEL
327
0
36879
TrEMBL
other Location (Reliability: 2)
Q27496_CAEEL
363
0
41896
TrEMBL
other Location (Reliability: 1)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterodimer
-
-
additional information
-
several catalytic subunit and regulatory subunit forms, properties and interactions, overview
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C3S
-
reduced membrane association
G2A
-
reduced membrane association
additional information
-
PP4 knockdown by PPP4c catalytic subunit-RNAi interference leads to a semi-lethal phenotype with abberations in formation of spindles in mitosis and also in sperm meiosis
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
co-expression of cacineurin with HLH-11 and interaction analysis using the yeast two-hybrid system
-
expressed in Saccharomyces cerevisiae and Escherichia coli
-
expression in 293 cells and transgenic Caenorhabditis elegans
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ramulu, P.; Nathans, J.
Cellular and subcellular localization, N-terminal acylation, and calcium binding of Caenorhabditis elegans protein phosphatase with EF-hands
J. Biol. Chem.
276
25127-25135
2001
Caenorhabditis elegans
Manually annotated by BRENDA team
Cohen, P.T.; Philp, A.; Vazquez-Martin, C.
Protein phosphatase 4 - from obscurity to vital functions
FEBS Lett.
579
3278-3286
2005
Arabidopsis thaliana, Saccharomyces cerevisiae, Caenorhabditis elegans, Drosophila melanogaster, Homo sapiens
Manually annotated by BRENDA team
Qadota, H.; McGaha, L.A.; Mercer, K.B.; Stark, T.J.; Ferrara, T.M.; Benian, G.M.
A novel protein phosphatase is a binding partner for the protein kinase domains of UNC-89 (obscurin) in Caenorhabditis elegans
Mol. Biol. Cell
19
2424-2432
2008
Caenorhabditis elegans
Manually annotated by BRENDA team
Takeda, K.; Komuro, Y.; Hayakawa, T.; Oguchi, H.; Ishida, Y.; Murakami, S.; Noguchi, T.; Kinoshita, H.; Sekine, Y.; Iemura, S.; Natsume, T.; Ichijo, H.
Mitochondrial phosphoglycerate mutase 5 uses alternate catalytic activity as a protein serine/threonine phosphatase to activate ASK1
Proc. Natl. Acad. Sci. USA
106
12301-12305
2009
Caenorhabditis elegans, Drosophila melanogaster
Manually annotated by BRENDA team
Lee, S.U.; Song, H.O.; Lee, W.; Singaravelu, G.; Yu, J.R.; Park, W.Y.
Identification and characterization of a putative basic helix-loop-helix (bHLH) transcription factor interacting with calcineurin in C. elegans
Mol. Cells
28
455-461
2009
Caenorhabditis elegans
Manually annotated by BRENDA team