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Information on EC 3.1.3.16 - protein-serine/threonine phosphatase and Organism(s) Gallus gallus

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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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Gallus gallus
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The taxonomic range for the selected organisms is: Gallus gallus
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
-
-
-
-
Ca-calmodulin-dependent protein 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 1
-
Protein phosphatase 1A
-
-
-
-
Protein phosphatase 1B
-
-
-
-
Protein phosphatase 1C
-
-
-
-
Protein phosphatase magnesium-dependent 1 delta
-
-
-
-
Protein phosphatase magnesium-dependent 1 gamma
-
-
-
-
Protein phosphatase with EF calcium-binding domain
-
-
-
-
PSPase
-
-
-
-
Retinal degeneration C protein
-
-
-
-
Suppressor protein SDS21
-
-
-
-
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
phosphophosphorylase kinase + H2O
phosphorylase kinase + phosphate
show the reaction diagram
-
specific for alpha-subunit
-
-
?
phosphoproteins + H2O
proteins + phosphate
show the reaction diagram
-
-
-
-
?
phosphorylated protein phosphatase inhibitor-1 + H2O
protein phosphatase inhibitor-1 + phosphate
show the reaction diagram
-
-
-
-
?
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 enzyme is involved in regulation of many biological processes, e.g. glycogen metabolism, cell-cycle progression, and muscle relaxation, regulatory mechanism involving myosin phosphatase targeting subunit MYPT1 in smooth muscle relaxation, overview
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
calcineurin is dependent on Ca2+/calmodulin
additional information
one of the two metal ions in the metal center of the enzyme might as well be Fe2+ instead of Mn2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
A23187
-
reduces the Ca2+ level and thereby inhibits Ca2+-dependent calcineurin
cyclosporin A
-
in vivo inhibition in cell culture, 40% inhibition at 0.002 mM in vitro
EGTA
-
reduces the Ca2+ level and thereby inhibits Ca2+-dependent calcineurin
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Calmodulin
-
calcineurin is dependent on Ca2+/calmodulin
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.5 - 6.5
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
smooth muscle
Manually annotated by BRENDA team
-
from distal parts of the limb buds of 4-day-old Ross hybrid chicken embryos
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
calcineurin is one of the target molecules regulated by the changes of intracellular Ca2+ level, it has a regulatory role in Ca2+ cytosolic concentration and signaling in chondrogenic cells, Ca2+ plays an important role in chondrogenesis, cartilage formation and cartilage differentiation, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
DUS29_CHICK
214
0
24322
Swiss-Prot
other Location (Reliability: 2)
PP1B_CHICK
327
0
37187
Swiss-Prot
other Location (Reliability: 2)
SSU72_CHICK
194
0
22574
Swiss-Prot
Mitochondrion (Reliability: 4)
CTDSL_CHICK
275
0
31244
Swiss-Prot
other Location (Reliability: 1)
UBCP1_CHICK
318
0
36800
Swiss-Prot
other Location (Reliability: 2)
DUS4_CHICK
375
0
41052
Swiss-Prot
other Location (Reliability: 3)
EYA1_CHICK
119
0
13549
Swiss-Prot
other Location (Reliability: 5)
PP2AA_CHICK
309
0
35563
Swiss-Prot
other Location (Reliability: 1)
F1NT98_CHICK
423
0
49394
TrEMBL
other Location (Reliability: 2)
A0A3Q2U767_CHICK
1047
0
116165
TrEMBL
other Location (Reliability: 2)
A0A3Q2U2T9_CHICK
780
0
83823
TrEMBL
Mitochondrion (Reliability: 4)
F1NIB9_CHICK
207
0
23131
TrEMBL
other Location (Reliability: 2)
Q5ZIM8_CHICK
510
0
57590
TrEMBL
other Location (Reliability: 4)
E1BQP0_CHICK
249
0
27130
TrEMBL
other Location (Reliability: 1)
Q5F335_CHICK
382
0
42387
TrEMBL
other Location (Reliability: 4)
F1NBW9_CHICK
603
0
67658
TrEMBL
other Location (Reliability: 3)
A0A3Q2UBQ4_CHICK
178
0
20113
TrEMBL
other Location (Reliability: 2)
A0A3Q2UIX5_CHICK
511
0
57385
TrEMBL
other Location (Reliability: 5)
Q7T1F5_CHICK
504
0
56914
TrEMBL
other Location (Reliability: 3)
Q9PSQ6_CHICK
64
0
7083
TrEMBL
other Location (Reliability: 2)
A0A3Q3AAE8_CHICK
688
0
74555
TrEMBL
other Location (Reliability: 4)
A0A1D5PEM7_CHICK
994
0
110213
TrEMBL
other Location (Reliability: 2)
F1P3I1_CHICK
1395
0
153739
TrEMBL
other Location (Reliability: 3)
F1P225_CHICK
202
0
22256
TrEMBL
other Location (Reliability: 3)
A0A452J821_CHICK
282
0
32244
TrEMBL
other Location (Reliability: 1)
E1C2T7_CHICK
520
0
58632
TrEMBL
other Location (Reliability: 4)
E1BSB5_CHICK
207
0
23135
TrEMBL
Mitochondrion (Reliability: 3)
A0A1D5PZA0_CHICK
192
0
21253
TrEMBL
other Location (Reliability: 2)
A0A3Q2U6R6_CHICK
593
0
66221
TrEMBL
other Location (Reliability: 3)
A0A1D5P5S2_CHICK
385
0
42315
TrEMBL
Mitochondrion (Reliability: 5)
E1BTX9_CHICK
632
0
73496
TrEMBL
other Location (Reliability: 2)
A0A1D5P3Y2_CHICK
469
0
53094
TrEMBL
other Location (Reliability: 2)
A0A3Q2TVT2_CHICK
592
0
66298
TrEMBL
other Location (Reliability: 3)
Q5ZM47_CHICK
309
0
35564
TrEMBL
other Location (Reliability: 1)
Q5ZL39_CHICK
323
0
37000
TrEMBL
other Location (Reliability: 2)
E1BY90_CHICK
195
0
22127
TrEMBL
Mitochondrion (Reliability: 2)
A0A1D5P2F6_CHICK
527
0
59514
TrEMBL
other Location (Reliability: 5)
A0A3S5ZPJ0_CHICK
563
0
62242
TrEMBL
Mitochondrion (Reliability: 5)
A0A1D5P888_CHICK
347
0
39101
TrEMBL
other Location (Reliability: 3)
A0A1D5P463_CHICK
369
0
39975
TrEMBL
other Location (Reliability: 3)
Q7T1F6_CHICK
266
0
30836
TrEMBL
other Location (Reliability: 4)
A0A3Q2U159_CHICK
510
0
57598
TrEMBL
other Location (Reliability: 3)
A0A3Q2U428_CHICK
388
0
42926
TrEMBL
other Location (Reliability: 2)
A0A1L1RMC6_CHICK
347
0
39846
TrEMBL
Mitochondrion (Reliability: 3)
Q7T2L9_CHICK
382
0
42528
TrEMBL
other Location (Reliability: 2)
E1BR80_CHICK
738
0
86262
TrEMBL
Mitochondrion (Reliability: 5)
A0A1D5PI23_CHICK
184
0
20695
TrEMBL
other Location (Reliability: 1)
F1NCC5_CHICK
375
0
41053
TrEMBL
other Location (Reliability: 3)
A0A3Q2TTA5_CHICK
615
0
68955
TrEMBL
other Location (Reliability: 3)
Q5ZIV0_CHICK
305
0
35158
TrEMBL
other Location (Reliability: 1)
A0A1D5PJC6_CHICK
315
0
35895
TrEMBL
Mitochondrion (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
103000 - 109000
-
gel filtration
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme bound to the regulatory 34 kDa myosin phosphatase targeting subunit MYPT1 residues 1-299, 8 mg/ml protein in 10 mM Tris, pH 7.5, 20 mM NaCl, 4 mM DTT, and 1 mM MnCl2, 20°C, hanging drop vapour diffusion method, mixed with an equal volume of reservoir solution containing 9.2% w/v PEG 5000 monomethylether, 35% v/v glycerol, and 200 mM NH4Cl, X-ray diffraction structure determination and analysis at 2.7 A resolution
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant intein-enzyme fusion protein from Escherichia coli strain BL21(DE3) by chitin affinity chromatography, DTT-induced self-cleavage of the intein tag, followed by ion exchange chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
co-expression of the intein-enzyme fusion protein and the regulatory 34 kDa myosin phosphatase targeting subunit MYPT1 residues 1-299 in Escherichia coli strain BL21(DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Di Salvo, J.; Gifford, D.; Kokkinakis, A.
Properties and function of a bovine aortic polycation-modulated protein phosphatase
Adv. Protein Phosphatases
1
327-345
1985
Gallus gallus
-
Manually annotated by BRENDA team
Kanayama, K.; Wada, K.; Negami, A.; Yamamura, H.; Tanabe, T.
Purification of protein phosphatase from hen oviduct
FEBS Lett.
184
78-81
1985
Gallus gallus
Manually annotated by BRENDA team
Begum, N.; Sussman, E.; Draznin, B.
Differential effects of diabetes on adipocyte and liver phosphotyrosine and phosphosereine phosphatase activities
Diabetes
40
1620-1629
1991
Gallus gallus, Rattus norvegicus, Sus scrofa
Manually annotated by BRENDA team
Terrak, M.; Kerff, F.; Langsetmo, K.; Tao, T.; Dominguez, R.
Structural basis of protein phosphatase 1 regulation
Nature
429
780-784
2004
Gallus gallus (P62207)
Manually annotated by BRENDA team
Matta, C.; Fodor, J.; Szijgyarto, Z.; Juhasz, T.; Gergely, P.; Csernoch, L.; Zakany, R.
Cytosolic free Ca2+ concentration exhibits a characteristic temporal pattern during in vitro cartilage differentiation: a possible regulatory role of calcineurin in Ca-signalling of chondrogenic cells
Cell Calcium
44
310-323
2008
Gallus gallus
Manually annotated by BRENDA team