Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 3.1.3.16 - protein-serine/threonine phosphatase and Organism(s) Gallus gallus and UniProt Accession P62207

for references in articles please use BRENDA:EC3.1.3.16
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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).
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Gallus gallus
UNIPROT: P62207
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
hide
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
protein phosphatase 1
-
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 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
Mn2+
required for full activiy
Ca2+
-
calcineurin is dependent on Ca2+/calmodulin
Mn2+
-
activation
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
isozyme delta; PP1 isozyme delta
SwissProt
Manually annotated by BRENDA team
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?
PP1B_CHICK
327
0
37187
Swiss-Prot
other Location (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