Information on EC 3.1.3.53 - [myosin-light-chain] phosphatase

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The expected taxonomic range for this enzyme is: Eukaryota

EC NUMBER
COMMENTARY
3.1.3.53
-
RECOMMENDED NAME
GeneOntology No.
[myosin-light-chain] phosphatase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
[myosin light-chain] phosphate + H2O = [myosin light-chain] + phosphate
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
hydrolysis of phosphoric ester
-
-
hydrolysis of phosphoric ester
-
-
hydrolysis of phosphoric ester
-
-
hydrolysis of phosphoric ester
-
-
hydrolysis of phosphoric ester
-
-
hydrolysis of phosphoric ester
-
-
hydrolysis of phosphoric ester
-
-
hydrolysis of phosphoric ester
-
-
hydrolysis of phosphoric ester
Canis lupus familiaris Madin Darby, Mus musculus BALB/c
-
-
-
hydrolysis of phosphoric ester
Rattus norvegicus Sprague-Dawley
-
;
-
additional information
-
MYTP1 binds the catalytic subunit of type 1 phosphatase delta, binds many proteins like myosin II, ezrin, radixin, moesin, a-adducin, tau, MAP, elongation factor-1a, ZIP kinase, RhoA-GTP, key reaction is dephosphorylation of myosin II but also in cell migration, cell division
additional information
-
cardiac derived MYPT2 and smooth muscle derived MYPT2 have similar properties
SYSTEMATIC NAME
IUBMB Comments
[myosin-light-chain]-phosphate phosphohydrolase
The enzyme is composed of three subunits. The holoenzyme dephosphorylates myosin light chains and EC 2.7.11.18, myosin-light-chain kinase, but not myosin; the catalytic subunit acts on all three substrates.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
DMBS
-
Drosophila homolog of MBS
MBS
-
myosin-binding subunit
MBS
-
myosin binding subunit of myosin light chain phosphatase
mLC phosphatase
-
-
mLC phosphatase
-
-
MLCP
-
-
-
-
MLCP
Canis lupus familiaris Madin Darby
-
-
-
MLCP
Rattus norvegicus Sprague-Dawley
-
;
-
MLCP
-
-
MLCPase
-
-
-
-
MLCPPase
-
-
-
-
MP
-
-
-
-
MP
-
-
myosin light chain kinase phosphatase
-
-
-
-
myosin light chain phosphatase
-
-
-
-
myosin light chain phosphatase
-
-
myosin light chain phosphatase
Canis lupus familiaris Madin Darby
-
-
-
myosin light chain phosphatase
-
-
myosin light chain phosphatase
-
-
myosin light chain phosphatase
-
-
myosin light chain phosphatase
-
-
myosin light chain phosphatase
Rattus norvegicus Sprague-Dawley
-
-
-
myosin light chain phosphatase
-
-
myosin phosphatase
-
-
-
-
myosin phosphatase
-
-
myosin phosphatase
Canis lupus familiaris Madin Darby
-
-
-
myosin phosphatase
O14974
-
myosin phosphatase
-
-
myosin phosphatase
-
-
myosin phosphatase
-
-
myosin phosphatase
Mus musculus BALB/c
-
-
-
myosin phosphatase
-
-
myosin phosphatase
-
-
myosin phosphatase
Rattus norvegicus Sprague-Dawley
-
-
-
myosin phosphatase
-
-
myosin-targeting protein 1
-
-
myosin-targeting protein 1
Canis lupus familiaris Madin Darby
-
-
-
myosin-targeting protein 1
-
-
MYPT1
Canis lupus familiaris Madin Darby
-
-
-
MYPT1
-
the targeting subunit of MLCP
MYPT1
-
-
MYPT1
Mus musculus BALB/c
-
-
-
MYPT1
Rattus norvegicus Sprague-Dawley
-
-
-
MYPT1
-
-
MYPT1-pT853
-
myosin light-chain phosphatase-targeting subunit at Thr853
MYTP 1
-
myosin phosphatase target subunit
phosphatase, myosin
-
-
-
-
phosphatase, myosin light-chain kinase
-
-
-
-
plasmodial phosphatase
-
-
PP-1G
-
-
-
-
PP-1M
-
-
-
-
PP-2A
-
-
-
-
PP1
Mus musculus BALB/c
-
-
-
protein phosphatase 1beta
-
-
protein phosphatase 2A
-
-
-
-
SMMP
-
-
-
-
smooth muscle myosin phosphatase
-
-
-
-
smooth muscle phosphatase I-IV
-
-
-
-
SMP-I
-
-
-
-
SMP-II
-
-
-
-
SMP-III
-
-
-
-
SMP-IV
-
-
-
-
SMPP
-
-
-
-
[myosin-light-chain] phosphatase
-
-
[myosin-light-chain] phosphatase
-
-
[myosin-light-chain] phosphatase
Rattus norvegicus Sprague-Dawley
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
108658-39-5
-
86417-96-1
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
isoenzyme PP-1M and PP-2A, not isoenzyme PP-1G
-
-
Manually annotated by BRENDA team
Madin Darby
-
-
Manually annotated by BRENDA team
Canis lupus familiaris Madin Darby
Madin Darby
-
-
Manually annotated by BRENDA team
mutant in the myosin phosphatase-targeting subunit Mbs enhances the lethality of flapwing, flw, and JNK phosphatase puckered, puc, mutants
-
-
Manually annotated by BRENDA team
wild type, DMBS null mutants and transheterozygotes with stronger and weaker alleles
-
-
Manually annotated by BRENDA team
full-length and deletion mutants
-
-
Manually annotated by BRENDA team
MP, protein phosphatase type 1
-
-
Manually annotated by BRENDA team
PP-1M
-
-
Manually annotated by BRENDA team
Gallus gallus MLCP
MLCP
-
-
Manually annotated by BRENDA team
Gallus gallus PP-1
PP-1
-
-
Manually annotated by BRENDA team
Gallus gallus PP-1M
PP-1M
-
-
Manually annotated by BRENDA team
heart-specific small regulatory subunit isoform hHS-M21 A of MLCP; heart-specific small regulatory subunit isoform hHS-M21 B of MLCP
SwissProt
Manually annotated by BRENDA team
isoforms of enzyme targeting subunit, MYPT 1
-
-
Manually annotated by BRENDA team
MLCPPase, member of type 1 phosphatases
-
-
Manually annotated by BRENDA team
myosin-associated PP-1M
-
-
Manually annotated by BRENDA team
PP-1 and PP-2A
-
-
Manually annotated by BRENDA team
4 different protein phosphatases are active towards isolated myosin light-chains: SMP-I, SMP-II, SMP-III, SMP-IV
-
-
Manually annotated by BRENDA team
catalytic subunit PP1c
-
-
Manually annotated by BRENDA team
KAMPPase: kinase- and myosin-associated protein phosphatase, a myofibrillar form of smooth muscle myosin light chain phosphatase forms a multienzyme complex with myosin light chain kinase
-
-
Manually annotated by BRENDA team
smooth muscle phosphatase I, i.e. SMP-I
-
-
Manually annotated by BRENDA team
Meleagris gallopavo MLCP
MLCP
-
-
Manually annotated by BRENDA team
BALB/c
-
-
Manually annotated by BRENDA team
Mus musculus BALB/c
BALB/c
-
-
Manually annotated by BRENDA team
Japanese male white
-
-
Manually annotated by BRENDA team
male albino rabbits, MLCP, i.e. protein phosphatase type 1
-
-
Manually annotated by BRENDA team
myosin-bound form PP-1M, glycogen-bound form PP-1G and PP-2A
-
-
Manually annotated by BRENDA team
New Zealand White rabbits, MLCP
-
-
Manually annotated by BRENDA team
normal and pulmonary hypertensive fetal sheep, MLCP, protein phosphatase type 1
-
-
Manually annotated by BRENDA team
72.5 kDa N-terminal fragment of the 110 kDa subunit
-
-
Manually annotated by BRENDA team
isoforms of enzyme targeting subunit 1, MYPT 1
-
-
Manually annotated by BRENDA team
myosin-binding subunit of MLCP
-
-
Manually annotated by BRENDA team
recombinant protein
-
-
Manually annotated by BRENDA team
Sprague-Dawley
-
-
Manually annotated by BRENDA team
Sprague-Dawley, virgin rat, pregnant rat, in pregnant rats with hypertension
-
-
Manually annotated by BRENDA team
Rattus norvegicus Sprague-Dawley
Sprague-Dawley
-
-
Manually annotated by BRENDA team
89.6 kDa fragment of MYPT1, an isoform of the 130 kDa regulatory subunit of myosin phosphatase
SwissProt
Manually annotated by BRENDA team
MLCP, i.e. protein phosphatase type 1
-
-
Manually annotated by BRENDA team
SMPP-1M
-
-
Manually annotated by BRENDA team
Sus scrofa SMPP-1M
SMPP-1M
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
-
enzyme domain MYPT mutation, MEL-11, causes cytokinesis failure
malfunction
-
a loss-of-function mutation of flapwing, which encodes the catalytic subunit of protein phosphatase 1beta, disrupts oocyte polarization. Proliferation and differentiation of the posterior follicle cells are affected by FP41, also FP41 mutation disrupts cell differentiation and Notch signaling of the cells. Excessive myosin activity in the posterior follicle cells causes oocyte mispolarization and defective Notch signaling and endocytosis in the posterior follicle cells, phenotype, detailed overview. The Notch intracellular domain can rescue the Notch signaling phenotype, but not the oocyte polarity phenotype of flwFP41 mutant cells
physiological function
-
physiological roles of myosin light chain kinase, MLCK, activation and myosin light chain phosphatase, MLCP, inhibition in the myogenic response, MLCP inhibition may also be required to slow the rate of LC20 dephosphorylation, mechanism, overview
physiological function
-
myosin phosphatase is required for contractile ring disassembly at the end of cytokinesis, it is involved in the assembly of ring canals derived from incomplete cytokinesis and function as intracellular bridges between nurse cells, thereby allowing cytoplasmic flow from nurse cells to oocytes. Myosin phosphatase must be temporally controlled during cytokinesis: it is first inactivated for the activation of a contractile ring at the initial stage of cytokinesis and then inactivated for the disassembly of the contractile ring
physiological function
-
PP1beta, by regulating myosin activity, controls the generation of the oocyte polarizing signal, it is essential for dephosphorylation and inactivation of the non-muscle myosin II light chain encoded by spaghetti squash. PP1beta regulates the membrane levels of apical complexes in the posterior follicle cells
physiological function
-
the heart-specific small subunit, hHS-M21, is a heart-specific effector of Rho-associated kinase and plays a regulatory role in the MYPT1 phosphorylation at Thr-696 by Rho-associated kinase, molecular mechanism, overview
physiological function
-
MLCP is directly and critically involved in endothelial cell barrier regulation, enhancement, and protection, with involvement of catalytic enzyme subunit CS1beta in the endothelial cell barrier enhancement induced by extracellular purines
metabolism
-
phosphorylation of MYPT1 is a major mechanism of MLCP regulation, but protein-protein interactions may also be important. Ca2+-dependent and Rho-associated kinase-mediated regulation of myosin light chain kinase and myosin light chain phosphatase, respectively, in the arterial myogenic response, molecular mechanisms, overview
additional information
-
smooth muscle myosin light chain phosphatase, MLCP, consists of three proteins, the catalytic PP1c-delta phosphatase, the MYPT1 targeting subunit, and M20 protein. Binding of PP1c-delta to MYPT1 occurs via a RVXF motif immediately adjacent to a series of ankyrin repeats that are implicated in protein-protein interactions. Myosin binding may occur over a region at the C-terminus that contains one of the two major ROK phosphorylation sites, T697 and T855. MYPT1 is a substrate for phosphorylation by several serine/threonine kinases that modulate MLCP activity and/or alter myosin binding. MYPT1 has three essential functions: (i) to confer myosin substrate specificity to the complex, (ii) to enhance the specific activity of PP1c-delta in dephosphorylating phospho-LC20, and (iii) to provide a means by which MLCP activity can be regulated by a variety of stimuli
additional information
-
myosin light chain phosphatase is regulated by phosphorylation of the catalytic subunit, the heart-specific small subunit, hHS-M21, plays a role in the regulation by phosphorylation, molecular mechanism, overview. Two isoforms of hHSM21, hHS-M21Aand hHS-M21B, preferentially bound the C-terminal one-third region of MYPT1 and MYPT2, respectively. Amino acid substitutions at a phosphorylation site of MYPT1, Ser852, impaired the binding of MYPT1 and hHS-M21. The hHS-M21 increases the phosphorylation level of MYPT1 at Thr696, which is attenuated by Rho-associated kinase, ROCK, inhibitors and small interfering RNAs for Rho-associated kinase
additional information
-
myosin II association with actin, which triggers contraction, is regulated by orchestrated waves of phosphorylation/dephosphorylation of the myosin regulatory light chain. Dephosphorylation is mediated by myosin phosphatase
additional information
-
regulation of the enzyme involving ERM proteins ezrin, radixin, moesin, and isozymes of myosin PPase targeting subunit 1, MYPT1, overview
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
show the reaction diagram
-
-
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
show the reaction diagram
-
-
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
show the reaction diagram
-
-
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
show the reaction diagram
-
-
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
show the reaction diagram
-
-
-
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
show the reaction diagram
-
-
-
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
show the reaction diagram
-
-
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
show the reaction diagram
-
-
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
show the reaction diagram
-
-
-
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
show the reaction diagram
-
-
-
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
show the reaction diagram
-
-
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
show the reaction diagram
-
-
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
show the reaction diagram
-
-
-
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
show the reaction diagram
-
holoenzyme and isolated catalytic subunit are active
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
show the reaction diagram
-
SMP-I, -II, -III and -IV are active
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
show the reaction diagram
-
isozyme PP-1M is more active towards native myosin than isolated myosin P-light-chains or phosphorylase A
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
show the reaction diagram
-
isozyme PP-1G dephosphorylates myosin, myosin P-light-chain and phosphorylase A at comparable rates
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
show the reaction diagram
-
from smooth muscle
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
show the reaction diagram
-
38 kDa catalytic subunit PP1c and holoenzyme are active, the 130 kDa subunit M130 activates PP1c activity, effect of truncation mutants of M130 on PP1c activity
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
show the reaction diagram
-
myosin regulatory light chain RLC from chicken gizzard, specificity of MLCP toward various phosphorylation sites of RCL, N-terminal region of RLC plays an important role in substrate recognition
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
show the reaction diagram
-
PP-2A: 30fold more effective in dephosphorylating myosin P-light-chains than native myosin, 10fold more active towards myosin P-light-chains than phosphorylase A
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
show the reaction diagram
-
from bovine stomach
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
show the reaction diagram
-
from turkey gizzard
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
show the reaction diagram
-
20 kDa myosin light chain
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
show the reaction diagram
-
20 kDa myosin light chain
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
show the reaction diagram
-
20 kDa myosin light chain
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
show the reaction diagram
-
20 kDa myosin light chain
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
show the reaction diagram
-
20 kDa myosin light chain
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
show the reaction diagram
-
20 kDa myosin light chain
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
show the reaction diagram
-
20 kDa myosin light chain
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
show the reaction diagram
-
20 kDa myosin light chain
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
show the reaction diagram
-
20 kDa myosin light chain
-
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
show the reaction diagram
-
20 kDa myosin light chain
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
show the reaction diagram
-
20 kDa myosin light chain
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
show the reaction diagram
-
20 kDa myosin light chain
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
show the reaction diagram
-
110 kDa/21 kDa complex accelerates dephosphorylation induced by the catalytic subunit PP1C by 1.6fold, the N-terminal sequence 1-309 of the 110 kDa subunit is sufficient to enhance the PP1C activity in muscle
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
show the reaction diagram
-
the 130 kDa subunit and the 20 kDa subunit enhance activity of the catalytic subunit towards heavy meromyosin or the isolated P-light-chain from smooth muscle
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
show the reaction diagram
-
important role in regulating myofibroblast contraction, Rho/Rho kinase-mediated inhibition of MLCPPase is necessary for lysophosphatidic acid-promoted myofibroblast contraction, in contrast to smooth muscle cells, in which MLCPPase activity only regulates the sensitivity of the contractile response to Ca2+
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
show the reaction diagram
-
role in the variable coupling between force and myosin light chain phosphorylation
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
show the reaction diagram
-
reaction is a prerequisite for the actin activation of the myosin Mg2+-ATPase
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
show the reaction diagram
-
key smooth muscle regulatory protein, MLCP is required for muscle relaxation
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
show the reaction diagram
-
dephosphorylation of the myosin regulatory light chain of myosin, which is phosphorylated at various sites at its N-terminal region
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
show the reaction diagram
-
plays a critical regulatory role in the Ca2+ sensitivity of myosin phosphorylation and smooth muscle contraction
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
show the reaction diagram
-
muscle
-
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
show the reaction diagram
-
muscle
-
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
show the reaction diagram
-
muscle
-
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
show the reaction diagram
-
muscle
-
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
show the reaction diagram
-
muscle
-
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
show the reaction diagram
-
muscle
-
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
show the reaction diagram
-
chicken gizzard 20 kDa myosin light-chain phosphate
-
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
show the reaction diagram
Rattus norvegicus Sprague-Dawley
-
-
-
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
show the reaction diagram
Meleagris gallopavo MLCP
-
myosin regulatory light chain RLC from chicken gizzard, specificity of MLCP toward various phosphorylation sites of RCL, N-terminal region of RLC plays an important role in substrate recognition, dephosphorylation of the myosin regulatory light chain of myosin, which is phosphorylated at various sites at its N-terminal region
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
show the reaction diagram
Canis lupus familiaris Madin Darby
-
muscle
-
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
show the reaction diagram
Gallus gallus PP-1
-
the 130 kDa subunit and the 20 kDa subunit enhance activity of the catalytic subunit towards heavy meromyosin or the isolated P-light-chain from smooth muscle
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
show the reaction diagram
Mus musculus BALB/c
-
-
-
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
show the reaction diagram
Gallus gallus MLCP
-
-
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
show the reaction diagram
Sus scrofa SMPP-1M
-
20 kDa myosin light chain, 110 kDa/21 kDa complex accelerates dephosphorylation induced by the catalytic subunit PP1C by 1.6fold, the N-terminal sequence 1-309 of the 110 kDa subunit is sufficient to enhance the PP1C activity in muscle
-
?
myosin regulatory light-chain phosphate + H2O
myosin regulatory light-chain + phosphate
show the reaction diagram
-
nonmuscle
-
-
?
myosin regulatory light-chain phosphate + H2O
myosin regulatory light-chain + phosphate
show the reaction diagram
Canis lupus familiaris, Canis lupus familiaris Madin Darby
-
nonmuscle
-
-
?
phosphorylated glycogen synthase + H2O
glycogen synthase + phosphate
show the reaction diagram
Gallus gallus, Gallus gallus PP-1
-
the 130 kDa subunit and the 20 kDa subunit suppress activity of the catalytic subunit towards phosphorylase A and glycogen synthase
-
-
?
phosphorylated heavy meromyosin + H2O
heavy meromyosin + phosphate
show the reaction diagram
-
from turkey gizzard
-
-
?
phosphorylated heavy meromyosin + H2O
heavy meromyosin + phosphate
show the reaction diagram
-
the 130 kDa subunit and the 20 kDa subunit enhance activity of the catalytic subunit towards heavy meromyosin or the isolated P-light-chain from smooth muscle
-
-
?
phosphorylated heavy meromyosin + H2O
heavy meromyosin + phosphate
show the reaction diagram
-
a chymotryptic fragment of myosin, only SMP-III and SMP-IV are active, SMP-I and SMP-II not
-
-
?
phosphorylated heavy meromyosin + H2O
heavy meromyosin + phosphate
show the reaction diagram
Gallus gallus PP-1
-
the 130 kDa subunit and the 20 kDa subunit enhance activity of the catalytic subunit towards heavy meromyosin or the isolated P-light-chain from smooth muscle
-
-
?
phosphorylated myosin + H2O
myosin + phosphate
show the reaction diagram
-
-
-
?
phosphorylated myosin + H2O
myosin + phosphate
show the reaction diagram
-
-
-
?
phosphorylated myosin + H2O
myosin + phosphate
show the reaction diagram
-
-
-
?
phosphorylated myosin + H2O
myosin + phosphate
show the reaction diagram
-
-
-
?
phosphorylated myosin + H2O
myosin + phosphate
show the reaction diagram
-
-
-
?
phosphorylated myosin + H2O
myosin + phosphate
show the reaction diagram
-
-
-
?
phosphorylated myosin + H2O
myosin + phosphate
show the reaction diagram
-
from turkey gizzard
-
?
phosphorylated myosin + H2O
myosin + phosphate
show the reaction diagram
-
from turkey gizzard
-
?
phosphorylated myosin + H2O
myosin + phosphate
show the reaction diagram
-
catalytic subunit is active, holoenzyme not
-
?
phosphorylated myosin + H2O
myosin + phosphate
show the reaction diagram
-
myosin heavy chain plays a role in the smooth muscle MLCP-myosin regulatory light chain interaction, specificity toward myosin phosphorylated at various sites of the myosin regulatory light chain RLC, role of the N-terminal region of RLC in the dephosphorylation of myosin
-
?
phosphorylated myosin + H2O
myosin + phosphate
show the reaction diagram
-
isoenzyme PP-1G dephosphorylates myosin, myosin P-light-chain and phosphorylase A at comparable rates, isoenzyme PP-1M is more active towards native myosin than PP-1G
-
?
phosphorylated myosin + H2O
myosin + phosphate
show the reaction diagram
-
isoenzyme PP-1M is more active towards native myosin than isolated myosin P-light-chains or phosphorylase A
-
?
phosphorylated myosin + H2O
myosin + phosphate
show the reaction diagram
-
from bovine stomach, P-myosin assembly is essential for SMMP activity
-
?
phosphorylated myosin + H2O
myosin + phosphate
show the reaction diagram
-
isoenzyme PP-2A: low activity with native myosin
-
?
phosphorylated myosin + H2O
myosin + phosphate
show the reaction diagram
-
only SMP-III and SMP-IV are active, SMP-I and SMP-II not
-
?
phosphorylated myosin + H2O
myosin + phosphate
show the reaction diagram
-
dephosphorylates myosin in vivo, dephosphorylation of the myosin regulatory light chain, which is phosphorylated at various sites at its N-terminal region
-
?
phosphorylated myosin + H2O
myosin + phosphate
show the reaction diagram
Meleagris gallopavo MLCP
-
from turkey gizzard, myosin heavy chain plays a role in the smooth muscle MLCP-myosin regulatory light chain interaction, specificity toward myosin phosphorylated at various sites of the myosin regulatory light chain RLC, role of the N-terminal region of RLC in the dephosphorylation of myosin, dephosphorylates myosin in vivo, dephosphorylation of the myosin regulatory light chain, which is phosphorylated at various sites at its N-terminal region
-
?
phosphorylated myosin + H2O
myosin + phosphate
show the reaction diagram
Sus scrofa SMPP-1M
-
-
-
?
phosphorylated myosin-light chain kinase + H2O
myosin light-chain kinase + phosphate
show the reaction diagram
-
holoenzyme and isolated catalytic subunit are active, phosphorylated at 2 sites, in absence of bound calmodulin rapid dephosphorylation at both sites, in presence of bound calmodulin dephosphorylation of only one site
-
?
phosphorylated myosin-light chain kinase + H2O
myosin light-chain kinase + phosphate
show the reaction diagram
-
autophosphorylated myosin light chain kinase is a good substrate for the kinase- and myosin-associated protein phosphatase KAMPPase
-
-
?
phosphorylated myosin-light chain kinase + H2O
myosin light-chain kinase + phosphate
show the reaction diagram
-
SMP-I modulates the activity of myosin-light chain kinase
-
?
phosphorylated phoshorylase A + H2O
phosphorylase A + phosphate
show the reaction diagram
-
-
-
?
phosphorylated phoshorylase A + H2O
phosphorylase A + phosphate
show the reaction diagram
-
PP-2A: 30fold more effective in dephosphorylating myosin P-light-chains than native myosin, 10fold more active towards myosin P-light-chains than phosphorylase A
-
?
phosphorylated phoshorylase A + H2O
phosphorylase A + phosphate
show the reaction diagram
-
isoenzyme PP-1M is more active towards native myosin than isolated myosin P-light-chains or phosphorylase A
-
?
phosphorylated phoshorylase A + H2O
phosphorylase A + phosphate
show the reaction diagram
-
isoenzyme PP-1G dephosphorylates myosin, myosin P-light-chains and phosphorylase A at comparable rates
-
?
phosphorylated phoshorylase A + H2O
phosphorylase A + phosphate
show the reaction diagram
-
38 kDa catalytic subunit PP1c
-
?
phosphorylated phoshorylase B + H2O
phosphorylase B + phosphate
show the reaction diagram
-
myosin-associated PP-1M
-
?
phosphorylated phosphorylase kinase + H2O
phosphorylase kinase + phosphate
show the reaction diagram
Gallus gallus, Gallus gallus PP-1
-
the 130 kDa subunit and the 20 kDa subunit suppress activity of the catalytic subunit towards phosphorylase A and glycogen synthase
-
-
?
radixin + H2O
?
show the reaction diagram
-
-, an ERM protein
-
-
?
regulatory myosin light-chain phosphate + H2O
regulatory myosin light-chain + phosphate
show the reaction diagram
Rattus norvegicus, Rattus norvegicus Sprague-Dawley
-
-
-
-
?
[myosin light-chain] phosphate + H2O
[myosin light-chain] + phosphate
show the reaction diagram
-
-
-
-
?
[myosin light-chain] phosphate + H2O
[myosin light-chain] + phosphate
show the reaction diagram
-
-
-
-
?
[myosin light-chain] phosphate + H2O
[myosin light-chain] + phosphate
show the reaction diagram
-
-
-
-
?
[myosin light-chain] phosphate + H2O
[myosin light-chain] + phosphate
show the reaction diagram
-
substrate is regulatory light chain (LC20) of myosin II, MLCP-mediated dephosphorylation of LC20 at Ser19
-
-
?
[myosin light-chain] phosphate + H2O
[myosin light-chain] + phosphate
show the reaction diagram
-
substrate is phosphorylated Physarum myosin II
-
-
?
[myosin regulatory light chain] phosphate + H2O
[myosin regulatory light chain] + phosphate
show the reaction diagram
-
from chicken gizzard
-
-
?
histone deacetylase 7 phosphate + H2O
histone deacetylase 7 + phosphate
show the reaction diagram
Mus musculus, Mus musculus BALB/c
-
HDAC7, dephosphorylation induces reimport into the nucleus
-
-
?
additional information
?
-
-
-
-
-
-
additional information
?
-
-
-
-
-
-
additional information
?
-
-
studies with fragments of the 110 kDa subunit on their ability to regulate relaxation and 20 kDa myosin light-chain dephosphorylation of rabbit permeabilized portal vein induced by the catalytic subunit PP1C
-
-
-
additional information
?
-
-
regulation of the MLCP activity
-
-
-
additional information
?
-
-
regulation mechanism of MLCP activity
-
-
-
additional information
?
-
O60237
role of the heart-specific small regulatory subunit hHS-M21 of MLCP
-
-
-
additional information
?
-
-
KAMPPase: kinase- and myosin-associated protein phosphatase, functional multienzyme complex composed of a myofibrillar form of smooth muscle myosin light chain phosphatase and myosin light chain kinase with or without calmodulin, regulation of the phosphatase activity
-
-
-
additional information
?
-
-
enzyme binds to vesicles of acidic phospholipids, i.e. phosphatidylserine, phosphatidylinositol and phosphatidic acid, but not to neutral phospholipids, phosphatidylserine binding decreases by increasing ionic strength and Mg2+ concentration, phospholipid binding is associated with the C-terminal part of the 130/133 kDa myosin-binding subunit and the 20 kDa regulatory subunit
-
-
-
additional information
?
-
-
130 kDa subunit MLCPa: elongated structure with 3 globular domains connected by flexible strands
-
-
-
additional information
?
-
-
interactions among the 38 kDa catalytic subunit PP1c, the 130 kDa and the 20 kDa non-catalytic subunits M130 and M20 or fragments of them, M130 has 2 binding sites for PP1c: one site in the N-terminal 38 residues and a weaker site in the ankyrin repeats region, activation of phosphatase and binding of PP1c and substrate are properties of the N-terminal one-third of M130
-
-
-
additional information
?
-
-
involved in force regulation in smooth muscle, the relative expression of splice-in/splice-out myosin-targeting subunit isoforms determines the magnitude of agonist-induced force enhancement/Ca2+ sensitization
-
-
-
additional information
?
-
-
two forms of SMP-I, the intact form and the catalytic subunit, may act in an opposite manner to regulate smooth muscle contraction in vivo
-
-
-
additional information
?
-
-
pulmonary hypertension down-regulates pulmonary vascular MLCP expression, the maintenance of a high pulmonary vascular resistance may be secondary to abnormalities in tissue content and/or activity of MLCP
-
-
-
additional information
?
-
-
involved in smooth muscle relaxation
-
-
-
additional information
?
-
-
thrombin activates the Rho/Rho kinase pathway to inactivate myosin light chain phosphatase as part of a signaling network that controls myosin light chain phosphorylation and contraction in endothelial cells
-
-
-
additional information
?
-
-
involved in the regulation of smooth muscle contraction, regulation of the MLCP activity
-
-
-
additional information
?
-
-
together with myosin light chain kinase key regulatory enzyme of smooth muscle
-
-
-
additional information
?
-
-
plays a key role in platelet function
-
-
-
additional information
?
-
Gallus gallus MLCP
-
130 kDa subunit MLCPa: elongated structure with 3 globular domains connected by flexible strands
-
-
-
additional information
?
-
Sus scrofa SMPP-1M
-
studies with fragments of the 110 kDa subunit on their ability to regulate relaxation and 20 kDa myosin light-chain dephosphorylation of rabbit permeabilized portal vein induced by the catalytic subunit PP1C
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
show the reaction diagram
-
important role in regulating myofibroblast contraction, Rho/Rho kinase-mediated inhibition of MLCPPase is necessary for lysophosphatidic acid-promoted myofibroblast contraction, in contrast to smooth muscle cells, in which MLCPPase activity only regulates the sensitivity of the contractile response to Ca2+
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
show the reaction diagram
-
role in the variable coupling between force and myosin light chain phosphorylation
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
show the reaction diagram
-
reaction is a prerequisite for the actin activation of the myosin Mg2+-ATPase
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
show the reaction diagram
-
key smooth muscle regulatory protein, MLCP is required for muscle relaxation
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
show the reaction diagram
-
dephosphorylation of the myosin regulatory light chain of myosin, which is phosphorylated at various sites at its N-terminal region
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
show the reaction diagram
-
plays a critical regulatory role in the Ca2+ sensitivity of myosin phosphorylation and smooth muscle contraction
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
show the reaction diagram
Meleagris gallopavo MLCP
-
dephosphorylation of the myosin regulatory light chain of myosin, which is phosphorylated at various sites at its N-terminal region
-
?
phosphorylated myosin + H2O
myosin + phosphate
show the reaction diagram
Meleagris gallopavo, Meleagris gallopavo MLCP
-
dephosphorylates myosin in vivo, dephosphorylation of the myosin regulatory light chain, which is phosphorylated at various sites at its N-terminal region
-
?
phosphorylated myosin-light chain kinase + H2O
myosin light-chain kinase + phosphate
show the reaction diagram
-
SMP-I modulates the activity of myosin-light chain kinase
-
?
radixin + H2O
?
show the reaction diagram
-
an ERM protein
-
-
?
[myosin light-chain] phosphate + H2O
[myosin light-chain] + phosphate
show the reaction diagram
-
-
-
-
?
[myosin light-chain] phosphate + H2O
[myosin light-chain] + phosphate
show the reaction diagram
-
-
-
-
?
[myosin light-chain] phosphate + H2O
[myosin light-chain] + phosphate
show the reaction diagram
-
substrate is regulatory light chain (LC20) of myosin II, MLCP-mediated dephosphorylation of LC20 at Ser19
-
-
?
additional information
?
-
-
involved in force regulation in smooth muscle, the relative expression of splice-in/splice-out myosin-targeting subunit isoforms determines the magnitude of agonist-induced force enhancement/Ca2+ sensitization
-
-
-
additional information
?
-
-
two forms of SMP-I, the intact form and the catalytic subunit, may act in an opposite manner to regulate smooth muscle contraction in vivo
-
-
-
additional information
?
-
-
pulmonary hypertension down-regulates pulmonary vascular MLCP expression, the maintenance of a high pulmonary vascular resistance may be secondary to abnormalities in tissue content and/or activity of MLCP
-
-
-
additional information
?
-
-
involved in smooth muscle relaxation
-
-
-
additional information
?
-
-
thrombin activates the Rho/Rho kinase pathway to inactivate myosin light chain phosphatase as part of a signaling network that controls myosin light chain phosphorylation and contraction in endothelial cells
-
-
-
additional information
?
-
-
involved in the regulation of smooth muscle contraction, regulation of the MLCP activity
-
-
-
additional information
?
-
-
together with myosin light chain kinase key regulatory enzyme of smooth muscle
-
-
-
additional information
?
-
-
plays a key role in platelet function
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Mg2+
-
required by enzyme SMP-II
Mg2+
-
activates at 0.0085 mM
Mn2+
-
highly activating at 0.0016 mM
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(S)-2-methyl-1-[(4-methyl-5-isoquinolinyl)sulfonyl]-hexahydro-1H-1,4-diazepine
-
H-1152, 0.0003 mM produces a strong inhibition of basal MYPT1-pT853 by nearly 75%, KCl produces an approximate 1.75-2fold increase in MYPT1-pT853 in the presence and absence of H-1152
14-3-3beta protein
-
70% inhibition in the presence of 0.5 mM 14-3-3beta, dissociates MLCP from myosin II
-
acidic phospholipid
-
interaction of enzyme with acidic phospholipids inhibits activity toward phosphorylated myosin
-
ADP
-
SMP-I, catalytic subunit is more sensitive than holoenzyme
AMP
-
SMP-I, catalytic subunit is more sensitive than holoenzyme
arachidonic acid
-
inhibits SMPP-1M, dissociates the catalytic subunit from the native holoenzyme, inhibits the regulatory action of the 110 kDa/21 kDa subunit complex on the catalytic subunit PP1C activity, the C-terminal half of the 110 kDa subunit is required for inhibition
ATP
-
SMP-I, catalytic subunit is more sensitive than holoenzyme
ATP
-
enzyme SMP-IV is less sensitive than the other enzymes
Ca2+
-
partial inhibition of SMP-I, only with myosin light chain as substrate
Ca2+
-
inhibits at 0.01 mM
calyculin
-
type 1 and type 2A phosphatase inhibitor, inhibits MLCPPase
CPI-17
-
specific inhibitor predominantly expressed in smooth muscles and neurons, phosphorylation of CPI-17 at Thr38 is necessary and sufficient to convert the protein into a potent inhibitor of myosin phosphatase
-
CPI-17
-
17-kDa protein kinase C-dependent MLCP inhibitor
-
dephosphorylated myosin light chain
-
SMP-I, product inhibition
diphosphate
-
SMP-I, catalytic subunit is more sensitive than holoenzyme, most potent inhibitor among the phosphate analogs
diphosphate
-
enzyme SMP-IV is less sensitive than the other enzymes
flavone
-
inhibits U46619-induced regulatory myosin light-chain phosphorylation
fragment 654-880 of human myosin phosphatase targeting subunit GST-fusion
-
-
-
fragment 697-880 of human myosin phosphatase targeting subunit GST-fusion
-
-
-
glycerol
-
inhibits SMMP activity, dissociates P-myosin primarily into an extended conformation
KCl
-
at high concentrations
Mg2+
-
partial inhibition of SMP-I, only with myosin light chain as substrate
Mg2+
-
above 5 mM
MgATP2-
-
inhibits SMMP activity towards P-myosin, disassembles P-myosin mostly into a folded conformation
NaF
-
at high concentrations
NaF
-
enzyme SMP-IV is less sensitive than the other enzymes
okadaic acid
-
0.005 mM, more than 90% inhibition
okadaic acid
-
potent inhibitor of PP-1 and PP-2A
okadaic acid
-
at 1 nM almost complete inhibition of PP-2A; PP-1: 0.001 mM, 88% inhibition
okadaic acid
-
at 1 nM almost complete inhibition of PP-2A
okadaic acid
-
more potent inhibitor of type 2A phosphatase than of type 1 phosphatase
phosphate
-
SMP-I, holoenzyme and catalytic subunit, product inhibition
phosphatidic acid
-
most effective inhibitor among acidic phospholipids, followed by phosphatidylserine and phosphatidylinositol, phosphorylated myosin as substrate
phosphatidylinositol
-
phosphatidic acid is the most effective inhibitor among acidic phospholipids, followed by phosphatidylserine and phosphatidylinositol, phosphorylated myosin as substrate
phosphatidylserine
-
phosphatidic acid is the most effective inhibitor among acidic phospholipids, followed by phosphatidylserine and phosphatidylinositol, phosphorylated myosin as substrate
phospho-CPI-17
-
MLCP inhibitor protein, phosphorylation at Thr-38 of CPI-17 results in inhibition of MLCP activity
-
phospho-CPI-17
-
-
-
phospho-CPI-17
-
MLCP inhibitor protein, phosphorylation at Thr-38 of CPI-17 results in inhibition of MLCP activity; Rho kinase and protein kinase C phosphorylate CPI-17 at Thr-38, CPI-17 phosphorylation plays a role in MLCP regulation
-
Rho/Rho kinase
-
activated by thrombin to inactivate PP-1M
-
Rho/Rho kinase
-
Rho/Rho kinase-mediated inhibition of MLCPPase
-
smoothelin-like 1 protein
-
originally called CHASM (calponin homology-associated smooth muscle), 55% inhibition at 0.0025 mM, 75% inhibition at up to 0.02 mM
-
tautomycetin
-
type 1 phosphatase inhibitor
tautomycin
-
PP-1M inhibitor
Thrombin
-
activates Rho/Rho kinase to inactivate PP-1M
-
microcystin
-
-
-
additional information
-
increases in the ionic strength inhibit SMMP activity
-
additional information
-
phosphorylation at Thr-695 of the MLCP regulatory subunit MYPT1 inhibits MLCP activity
-
additional information
-
pulmonary hypertension down-regulates pulmonary vascular MLCP expression
-
additional information
-
phosphorylation of the myosin-binding subunit of MLCP at Thr-641 inhibits MLCP activity
-
additional information
-
inhibitory effect of several truncation mutants of the 130 kDa subunit M130 on the activity of the catalytic subunit PP1c, IC50 values
-
additional information
-
relaxation of submaximally contracted mouse arteries with urocortin results in a decrease in phosphorylation of myosin light chain S19 by 60% and of enzyme regulatory subunit T696 and T850 by 28 and 52%, resp. Effect of urocortin is blocked by Rp-8-CPT-cAMPS and mimicked by Sp-5,6-DCl-cBIMPS
-
additional information
-
elevation of cAMP and maximal cAMP-dependent protein kinase activation cause a 50% reduction in myosin II regulatory light chain phosphorylation and a 35% drop in isometric tension
-
additional information
-
forskolin, the phosphoinositide 3-kinase inhibitor 2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one, LY 294002, and the Rho kinase inhibitor (R)-(+)-trans-N-(4-pyridyl)-4-(1-aminoethyl)-cyclohexanecarboxamide, Y27632, inhibit KCl-induced contraction in organ culture
-
additional information
-
MLCP holoenzyme is inhibited by binding of 14-3-3beta protein to MYPT1, 14-3-3beta protein diminishes the binding between MYPT1 and myosin II, and abolishes MYPT1 localization at stress fibers
-
additional information
-
MLCP inhibition may occur through RhoA/Rhokinase and/or protein kinase C with phosphorylation of myosin phosphatase targeting subunit-1 and protein kinase C-potentiated phosphatase inhibitor (CPI-17), respectively
-
additional information
-
phosphorylation on Thr695 and Thr850 (inhibitory sites) result in inhibition
-
additional information
-
phosphorylation of myosin phosphatase targeting subunit on Thr696 and Thr853 (inhibitory sites) results in inhibition
-
additional information
-
two major ROK phosphorylation sites, Thr697 and Thr855, on MYPT1 elicit MLCP inhibition. Phosphorylation of both sites inhibits MLCP activity. MYPT1-T855 phosphorylation may also interfere with the binding of MYPT1 to myosin
-
additional information
-
inhibition of MLC phosphatase by either the catalytic subunit of MLC phosphatase, CS1beta, or myosin PPase targeting subunit 1, MYPT1, siRNA-based depletion results in significant attenuation of purine nucleotide (ATP and adenosine)-induced EC barrier enhancement
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
p116Rip
-
RhoA-binding protein, activates enzyme activity of the holoenzyme due to binding to MYPT 1 targeting subunit. Activation is specific to myosin as substrate
-
sodium nitroprusside
-
nitrovasodilator, increases MLCP activity in intact carotid media, mechanism
type I cGMP-dependent protein kinase
-
-
-
U46619
-
thromboxane A2 analogue at 10-7 mol/L, increases phosphorylation of MYPT1 and regulatory myosin light-chain
KCl
-
in organ culture
additional information
-
telokin facilitates the dissociation of the phosphatase or its catalytic subunit from myosin light chain kinase oligomers increasing the MLCPase activity of the multienzyme complex, but no effect on the activity of the purified MLCPase holoenzyme or its catalytic subunit
-
additional information
-
P-myosin assembly is essential for SMMP activity
-
additional information
-
C-terminal leucine-zipper of MYPT 1 subunit is required for cGMP-mediated activation of enzyme
-
additional information
-
rhoA kinase 1 and rhoA kinase 2 isoforms both regulate MLCP phosphorylation
-
additional information
-
the activity of the catalytic subunit of MLCP, CSbeta, towards myosin depends on its associated regulatory subunit, namely myosin PPase targeting subunit 1, MYPT1
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0059
-
heavy meromyosin
-
pH 7, 30C, enzyme SMP-IV
-
0.0015
-
myosin light-chain
-
pH 7, 30C, enzyme SMP-IV
0.01
-
myosin light-chain
-
pH 7, 30C, SMP-I holoenzyme
0.05
-
myosin light-chain
-
pH 7, 30C, catalytic subunit of SMP-I
0.00103
-
myosin light-chain phosphate
-
smooth muscle, type 1 protein phosphatase delta and MYPT1
0.00136
-
myosin light-chain phosphate
-
smooth muscle, type 1 protein phosphatase delta and MYPT2
0.00394
-
myosin light-chain phosphate
-
smooth muscle, type 1 protein phosphatase delta only
0.00502
-
myosin light-chain phosphate
-
cardiac muscle, type 1 protein phosphatase delta and MYPT1
0.00551
-
myosin light-chain phosphate
-
cardiac muscle, type 1 protein phosphatase delta and MYPT2
0.01117
-
myosin light-chain phosphate
-
cardiac muscle, type 1 protein phosphatase delta only
0.00045
-
Phosphorylated myosin
-
at a ionic strength of 0.15 M
-
0.0024
-
Phosphorylated myosin
-
at a ionic strength of 0.15 M, in the presence of 0.1 mM MgATP
-
0.01
-
[myosin light-chain] phosphate
-
pH 7.6, temperature not specified in the publication
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0115
-
dephosphorylated myosin light chain
-
pH 7, 30C, SMP-I
1.5
-
phosphate
-
pH 7, 30C, SMP-I
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0000011
-
phosphorylated fragment 654-880 of human myosin phosphatase targeting subunit GST-fusion
-
-
-
0.00006
-
phosphorylated fragment 697-880 of human myosin phosphatase targeting subunit GST-fusion
-
-
-
0.0014
-
unphosphorylated fragment 654-880 of human myosin phosphatase targeting subunit GST-fusion
-
-
-
0.0061
-
unphosphorylated fragment 697-880 of human myosin phosphatase targeting subunit GST-fusion
-
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.00085
-
-
in virgin rats
0.00102
-
-
in pregnant rats with hypertension
0.00121
-
-
in pregnant rats
0.028
-
-
purified enzyme, pH 7.6, temperature not specified in the publication
1.6
-
-
pH 7, 30C, myosin light-chain, enzyme SMP-IV
1.84
-
-
pH 7, 30C, heavy meromyosin, enzyme SMP-IV
4
7.7
-
pH 7, 30C, myosin light-chain, enzyme SMP-I
additional information
-
-
-
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7
-
-
dephosphorylation of intact myosin or isolated myosin light-chain by the catalytic subunit
7
-
-
assay at
7
-
-
assay at
7.4
-
-
assay at
7.4
-
-
assay at
7.5
-
-
dephosphorylation of myosin light-chain by the holoenzyme
7.5
-
-
assay at
7.5
-
-
assay at
7.6
-
-
assay at
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
-
assay at
25
-
-
assay at, dephosphorylation of myosin light chain kinase in presence or absence of calmodulin bound to the kinase
25
-
-
assay at
30
-
-
assay at
30
-
-
assay at
30
-
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
fragments of the 110 kDa subunit
Manually annotated by BRENDA team
-
fetal, same MLCP activities in normal and pulmonary hypertensive fetal sheep
Manually annotated by BRENDA team
-
embryonic and adult, smooth muscle, throughout development, exclusive expression of the splice-in myosin-targeting subunit isoform
Manually annotated by BRENDA team
-
and large capacitance vessels, predominantly expression of 3-exon-out/leucine-zipper positive MYPT 1 isoform
Manually annotated by BRENDA team
-
expression of leucine-zipper positive isoform of MYPT 1 predominantes in healthy animal
Manually annotated by BRENDA team
Q9TV77
endothelial cells, subunit MYPT1
Manually annotated by BRENDA team
Rattus norvegicus Sprague-Dawley
-
thorax
-
Manually annotated by BRENDA team
-
first-order mesenteric resistance artery, high expression of enzyme with predominance of 3-exon-excluded, leucine-zipper negative MYPT 1 isoform; pulmonary artery, predominantly expression of 3-exon-out/leucine-zipper positive MYPT 1 isoform
Manually annotated by BRENDA team
-
intrapulmonary arterial tissue, enzyme protein increases with age and is highest in adult rat. In contrast, enzyme specific activity is significantly higher in fetal compared with adult tissue
Manually annotated by BRENDA team
-
iliac artery, expression of leucine-zipper positive isoform of MYPT 1 predominates in healthy animal
Manually annotated by BRENDA team
-
monolayers of pulmonary artery endothelial cells
Manually annotated by BRENDA team
-
coronary artery smooth muscle
Manually annotated by BRENDA team
Sus scrofa SMPP-1M
-
SMPP-1M
-
Manually annotated by BRENDA team
-
expression of MYPT1 and MYPT2, the 2 isoforms of the large subunit
Manually annotated by BRENDA team
-
isoenzyme PP-1M accounts for 90% of the myosin phosphatase activity, isoenzyme PP-1G is essentially absent
Manually annotated by BRENDA team
O60237
the small regulatory subunit hHS-M21 is expressed only in cardiac muscle, not in smooth muscle
Manually annotated by BRENDA team
-
smooth muscle
Manually annotated by BRENDA team
Q9TV77
from aorta thoracica, subunit MYPT1
Manually annotated by BRENDA team
-
from umbilical vein, myosin-bound PP-1M
Manually annotated by BRENDA team
-
monlayers of pulmonary artery endothelial cells
Manually annotated by BRENDA team
-
imaginal disc epithelium of Drosophila
Manually annotated by BRENDA team
-
normal and pulmonary hypertensive fetal sheep, pulmonary artery, aorta and vena cava
Manually annotated by BRENDA team
-
embryonic, large myosin phosphatase target subunit MYPT
Manually annotated by BRENDA team
Gallus gallus MLCP, Gallus gallus PP-1M
-
-
-
Manually annotated by BRENDA team
-
myofibrillar form of MLCPase
Manually annotated by BRENDA team
-
embryonic and adult, early during development, expression of the splice-in myosin-targeting subunit isoform, then shift from the splice-in to the splice-out isoform, exclusive expression of the splice-out isoform in adult chicken
Manually annotated by BRENDA team
Gallus gallus PP-1, Meleagris gallopavo MLCP
-
-
-
Manually annotated by BRENDA team
-
expression of MYPT1 and MYPT2, the 2 isoforms of the large subunit
Manually annotated by BRENDA team
-
portal vein, expression of MYPT 1 subunit increases 2fold between postnatal days 6 and 12 with similar increase in enzyme activity. MYPT 1 switches from leucine-zipper positive to leucine-zipper negative isoforms, concordant with a switch from sensitive to resisitant to cGMP-mediated vascular relaxation
Manually annotated by BRENDA team
-
coronary artery smooth muscle
Manually annotated by BRENDA team
-
72.5 kDa N-terminal fragment of the 110 kDa subunit
Manually annotated by BRENDA team
-
epithelial cells II
Manually annotated by BRENDA team
Canis lupus familiaris Madin Darby
-
epithelial cells II
-
Manually annotated by BRENDA team
-
coronary artery smooth muscle
Manually annotated by BRENDA team
-
fast and slow muscle fibres
Manually annotated by BRENDA team
-
granuloma pouch model of granulation tissue, organ culture
Manually annotated by BRENDA team
Rattus norvegicus Sprague-Dawley
-
granuloma pouch model of granulation tissue, organ culture
-
Manually annotated by BRENDA team
-
primary culture of neuronal cells
Manually annotated by BRENDA team
-
from venous blood, myosin phosphatase in platelets is composed of the catalytic subunit of PP-1 plus a subunit similar to the 130 kDa regulatory myosin-binding subunit of the smooth muscle phosphatase, major phosphatase is PP-1, also PP-2A
Manually annotated by BRENDA team
-
phasic smooth muscle
Manually annotated by BRENDA team
-
fetal, MLCP activity in pulmonary hypertensive fetal sheep is significantly lower than in normal fetal sheep
Manually annotated by BRENDA team
-
rat embryonic fibroblast cells, mitotic, 133 kDa myosin-binding subunit
Manually annotated by BRENDA team
-
phasic portal vein and vas deferens smooth muscles
Manually annotated by BRENDA team
-
from femoral arteries
Manually annotated by BRENDA team
-
artery of
Manually annotated by BRENDA team
Mus musculus BALB/c
-
T cell
-
Manually annotated by BRENDA team
-
phasic smooth muscle
Manually annotated by BRENDA team
-
mesenteric vein, high expression of enzyme with predominance of 3-exon-excluded, leucine-zipper negative MYPT 1 isoform
Manually annotated by BRENDA team
-
fetal, same MLCP activities in normal and pulmonary hypertensive fetal sheep
Manually annotated by BRENDA team
-
lung pulmonary artery, enzyme specific activity is related to Rho-kinase activation during lung morphogenesis
Manually annotated by BRENDA team
additional information
O60237
expression profiles of the heart-specific small subunit hHS-M21 and of the large myosin-binding subunit of MLCP
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Q9TV77
subunit MYPT1, in confluent endothelial cells, at the cell membrane and cell-cell contacts
-
Manually annotated by BRENDA team
-
depending on fixation method for immunohistochemistry, localization of myosin phosphatase target subunit found in nucleus, nucleolus, or cytoplasm
Manually annotated by BRENDA team
-
platelet, only PP-1, not PP-2A
Manually annotated by BRENDA team
-
dominant activity is PP-2A
Manually annotated by BRENDA team
-
133 kDa myosin-binding subunit
Manually annotated by BRENDA team
-
myofibrillar form of smooth muscle myosin light chain phosphatase forms a multienzyme complex with myosin light chain kinase
Manually annotated by BRENDA team
-
PP-1M activity is associated with the myofibrillar fraction
Manually annotated by BRENDA team
Gallus gallus PP-1
-
-
-
Manually annotated by BRENDA team
-
depending on fixation method for immunohistochemistry, localization of myosin phosphatase target subunit found in nucleus, nucleolus, or cytoplasm
Manually annotated by BRENDA team
-
depending on fixation method for immunohistochemistry, localization of myosin phosphatase target subunit found in nucleus, nucleolus, or cytoplasm
Manually annotated by BRENDA team
-
full-length enzyme and deletion mutants that contain the N-terminal nuclear localization signal
Manually annotated by BRENDA team
-
133 kDa myosin-binding subunit
Manually annotated by BRENDA team
Q9TV77
subunit MYPT1, in growing endothelial cells
-
Manually annotated by BRENDA team
-
large subunit MYPT, embryo fibroblasts
-
Manually annotated by BRENDA team
-
enzyme may interact with membranes, phosphorylation by protein kinase A may modify interaction, distribution of the 130/133 kDa myosin-binding subunit at the membrane
Manually annotated by BRENDA team
additional information
Q9TV77
subcellular localization of the subunit MYPT1 in growing and confluent endothelial cells
-
Manually annotated by BRENDA team
additional information
-
localization of PP-1 and PP-2A and their subunits in platelets
-
Manually annotated by BRENDA team
additional information
-
subcellular localization of the large subunit MYPT in embryo fibroblasts
-
Manually annotated by BRENDA team
additional information
-
-
-
Manually annotated by BRENDA team
additional information
-
close to the Z-line, the A-Band and mitochondrion
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
18500
-
-
small subunit of MP, mass spectrometry
50000
-
-
gel filtration
65000
-
-
catalytic subunit of KAMPPase, gel filtration
110000
-
-
isoenzyme PP-1M, gel filtration
130000
-
-
Western blot analysis
130000
-
-
myosin binding subunit, SDS-PAGE
150000
-
-
kinase- and myosin-associated protein phosphatase KAMPPase, gel filtration
165000
-
-
sedimentation equilibrium centrifugation
230000
-
-
gel filtration
230000
-
-
glycerol gradient centrifugation, gel filtration, sedimentation data
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 37000 + x * 67000, 37 kDa catalytic subunit, 67 kDa targeting subunit binds to the catalytic subunit, to myosin light chain kinase and Ca2+-independently to calmodulin, ratio of subunits 1:2, MLCPase of the multienzyme complex with myosin light chain kinase is named KAMPPase, SDS-PAGE
?
-
x * 60000 + x * 55000 + x * 38000, 38 kDa catalytic subunit, ratio 1:1:1, enzyme SMP-I, SDS-PAGE
?
-
x * 58000 + x * 40000, enzyme SMP-IV; x * 60000 + x * 55000 + x * 38000, 38 kDa catalytic subunit, ratio 1:1:1, enzyme SMP-I, SDS-PAGE
?
-
x * 130000 + x * 38000 + x * 20000, 130 kDa regulatory myosin-binding subunit, 38 kDa catalytic subunit, 20 kDa regulatory subunit, SDS-PAGE
?
-
x * 130000 + x * 38000 + x * 20000, 38 kDa catalytic subunit PP1c, 130 kDa and 20 kDa non-catalytic subunits M130 and M20, investigation of the interactions among PP1c, M20 and various mutants of M130 using the yeast two-hybrid system
?
Gallus gallus MLCP
-
x * 130000 + x * 38000 + x * 20000, 130 kDa regulatory myosin-binding subunit, 38 kDa catalytic subunit, 20 kDa regulatory subunit, SDS-PAGE
-
heterotrimer
-
1 * 130000 + 1 * 38000 + 1 * 20000, 38 kDa catalytic subunit is the type 1delta isoform, 130 kDa regulatory subunit binds myosin and the catalytic subunit, amino acid sequences
heterotrimer
-
x * 130000 + x * 37000 + x * 20000, 37 kDa catalytic subunit, ratio 1:1:1, SDS-PAGE
heterotrimer
-
1 * 110000 + 1 * 37000 + 1 * 21000, enzyme SMPP-1M, 37 kDa catalytic subunit PP1C, 110 kDa regulatory subunit M110
heterotrimer
-
-
heterotrimer
-
gizzard MP, 3 subunits: the two isoforms of the large subunit M130/M133 differ by a central insert at residues 512-552, the catalytic subunit PP1c delta isoform, two isoforms of the small subunit M20/M21 differing in the C-terminal sequence and in the presence or absence of leucin zipper motifs; interactions between the 3 subunits of MP
heterotrimer
-
interactions between the 3 subunits of MP
heterotrimer
Gallus gallus PP-1M
-
-
-
heterotrimer
Gallus gallus PP-1
-
x * 130000 + x * 37000 + x * 20000, 37 kDa catalytic subunit, ratio 1:1:1, SDS-PAGE
-
heterotrimer
Sus scrofa SMPP-1M
-
1 * 110000 + 1 * 37000 + 1 * 21000, enzyme SMPP-1M, 37 kDa catalytic subunit PP1C, 110 kDa regulatory subunit M110
-
trimer
-
1 * 20000 + 1 * 38000 + 1 * 110000
trimer
-
smooth muscle MLCP is a trimeric holoenzyme complex composed of 38 kDa PP1c-delat phosphatase, 110-130 kDa regulatory, myosin-targeting subunit, MYPT1, and a small, 20 kDa M20 subunit, presence of an acid residue cluster and LZ the presence of leucine zipper motifs in the LZ+ MYPT1 splice variant
trimer
-
myosin light chain phosphatase consists of a catalytic subunit, a large subunit, MYPT1 or MYPT2, and a small subunit
monomer
-
1 * 43000, enzyme SMP-II
additional information
-
the myosin-targeting subunit MYPT has 2 isoforms produced by alternative splicing that differ by a central insert: 133 kDa splice-in and 130 kDa splice-out isoform, expression of the MYPT isoforms is both developmentally regulated and tissue-specific
additional information
-
structure and molecular properties of the 18.5 kDa isoform of the small subunit of MP with 21 kDa on SDS-PAGE and 18.4 kDa predicted from the amino acid sequence, 2 isoforms: 18.5 and 21 kDa, the small and the 107 kDa targeting subunit form a complex as 1:1 heterodimer
additional information
O60237
the heart-specific small regulatory subunit hHS-M21 of MLCP increases the Ca2+ sensitivity in muscle and binds to the large myosin-binding subunit, it plays a regulatory role in cardiac muscle contraction by its binding to the large subunit MBS, MBS encoded by the MYPT1 gene, not by MYPT2, is the main target subunit of hHS-M21
additional information
-
enzyme interacts with synaptophysin
additional information
-
enzyme binds to retinoblastoma protein
additional information
-
myosin phosphatase is a heterotrimer composed of the catalytic subunit belonging to protein phosphatase 1 PP1, the myosin phosphatase targeting subunit MYPT1, and M21
additional information
-
enzyme has 3 subunits, the catalytic subunit type 1 protein phosphatase delta, the regulatory subunit MYPT1 and a small subunit M20
additional information
-
enzyme has 3 subunits, the catalytic subunit type 1 protein phosphatase delta, the regulatory subunit MYPT1 in smooth muscle and MYPT 2 an isoform of MYPT1 in striated muscle
additional information
-
MLCP is a heterotrimer composed of the catalytic subunit belonging to protein phosphatase 1c PPC1, the myosin-binding subunit MBS, and M20
additional information
-
myosin phosphatase is a heterotrimer composed of the catalytic subunit belonging to protein phosphatase 1 PP1, the myosin phosphatase targeting subunit MYPT1, and M21
additional information
-
The leucine-zipper motif at the N terminus of PKG forms a homodimeric coiled coil, the one at the C terminus of MYPT1 is monomeric and non-helical. The leucine-zipper motif of PKG binds to that of MYPT1 to form a heterodimer. When the leucine-zipper motif of MYPT1 is absent, the PKG leucine-zipper motif binds to the coiled coil region and upstream segments of MYPT1 via formation of a heterotetramer
additional information
-
MLCP is a heterotrimer composed of the catalytic subunit belonging to protein phosphatase 1c PPC1, the myosin phosphatase targeting subunit MYPT1, and M21
additional information
-
MLCP is a heterotrimer composed of the catalytic subunit belonging to protein phosphatase 1c PPC1, the myosin phosphatase targeting subunit MYPT1, and M21
additional information
-
myosin phosphatase is a complex that consists of a catalytic subunit protein phosphatase 1c, PP1cbeta, a large subunit myosin phosphatase targeting subunit, MYPT, and a small subunit. Stability of PP1cbeta and MYPT1 is interdependent, knocking down one of the subunits decreases the expression level of the other. MYPT1 binding is restricted to PP1cbeta, the central region of PP1cbeta confers the isoform-specific binding, while the variable, C-terminal domain of PP1cbeta is the region key for isoform-specific interaction with MYPT1. Sequence comparison of PP1 isoforms, overview
additional information
Gallus gallus PP-1M
-
structure and molecular properties of the 18.5 kDa isoform of the small subunit of MP with 21 kDa on SDS-PAGE and 18.4 kDa predicted from the amino acid sequence, 2 isoforms: 18.5 and 21 kDa, the small and the 107 kDa targeting subunit form a complex as 1:1 heterodimer
-
additional information
Mus musculus BALB/c
-
myosin phosphatase is a heterotrimer composed of the catalytic subunit belonging to protein phosphatase 1 PP1, the myosin phosphatase targeting subunit MYPT1, and M21
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
phosphoprotein
-
130/133 kDa myosin-binding subunits M130/M133 and 20 kDa regulatory subunit M20 are phosphorylated by protein kinase A to 3 and 1 mol phosphate/mol of subunit, phosphorylation of holoenzyme decreases phospholipid binding, M130/133: C-terminal phosphorylation site involved in regulation of phospholipid binding, no phosphorylation of the catalytic subunit PP-1cdelta, protein kinase C also phosphorylates M130/M133 and M20, but no effect on binding of phospholipids
phosphoprotein
-
inhibition of enzyme activity by phosphorylation of its myosin-targeting subunit, only in adult gizzard, not in adult aortic smooth muscle, phosphorylation is not required for Ca2+ sensitization of force
phosphoprotein
-
Thr-654 and Thr-695 are the major phosphorylation sites of the large subunit MYPT isoforms M130 and M133
phosphoprotein
-
large subunit MYPT1: phosphorylation site Thr-695, potential site for phosphorylation by protein kinase A is Thr-853
phosphoprotein
-
myosin light chain phosphatase is regulated by phosphorylation of the catalytic subunit
phosphoprotein
-
regulatory subunit of enzmye is phopshorylated at T696, contraction of intact mouse arteries induced with noradrenaline is associated with a 2fold increase in phosphorylation, which is reversed in arteries relaxed with urocortin
phosphoprotein
-
phosphorylation at Thr-695 of the MLCP regulatory subunit MYPT1 inhibits MLCP activity, Thr-695 phosphorylation is independent of stimulation of G-proteins, Rho-kinase or protein kinase C, MYPT1 can also be phosphorylated at Thr-850, which is a non-inhibitory Rho-kinase site, Thr-850 phosphorylation is activated by G-proteins
phosphoprotein
-
phosphorylation of the myosin-binding subunit of MLCP at the inhibitory site Thr-641 inhibits MLCP activity, but may not play a significant role in a mechanism for MLCP regulation, Rho kinase phosphorylates Thr-799, but not Thr-641
phosphoprotein
-
-
phosphoprotein
-
myosin-binding subunit of MLCP is phosphorylated at Thr-641 and Thr-799 by Rho kinase to 2 mol phosphate/mol of MBS
phosphoprotein
-
phosphorylation of MYPT1 is a major mechanism of MLCP regulation. Two major ROK phosphorylation sites, Thr697 and Thr855, on MYPT1 elicit MLCP inhibition. Phosphorylation of both sites inhibits MLCP activity. MYPT1-T855 phosphorylation may also interfere with the binding of MYPT1 to myosin
phosphoprotein
-
Ca2+-desensitizing hypoxic relaxation requires dephosphorylation of myosin phosphatase regulatory subunit
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
determination of three-dimensional structure of the 57-residue peptide corresponding to residue 658-714 of myosin phosphatase targeting subunit 1 using multi-dimensional NMR techniques
O14974
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, several months, stable
-
-20C, enzyme SMP-I, 20 mM KCl, 20 mM Tris-HCl, pH 7.4, 50% glycerol, 0.5 mM EGTA, 0.5 mM EDTA, 1 mM dithiothreitol, at least 1 year, stable
-
-20C, enzyme SMP-IV, 20 mM KCl, 20 mM Tris-HCl, pH 7.4, 50% glycerol, 0.1 mM EGTA, 0.1 mM EDTA, 1 mM dithiothreitol, 0.1 mM phenylmethylsulfonyl fluoride, several months, stable
-
-70C, enzyme SMP-I, 1 M KCl, 20 mM Tris-HCl, pH 7.4, 0.5 mM EGTA, 0.5 mM EDTA, 1 mM dithiothreitol, at least 1 year, stable
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
native holoenzyme; recombinant 133 kDa myosin-binding subunit and 20 kDa regulatory subunit, expressed in Escherichia coli
-
native holoenzyme; recombinant 18 kDa small subunit, expressed in Escherichia coli
-
recombinant 130 kDa regulatory myosin-binding subunit, expressed in SF9 cells
-
GSH affinity chromatography
-
immobilized metal ion affinity chromatography (Ni2+)
O14974
Ni2+-NTA-agarose column chromatography
-
of the recombinant peptides by chitin beads
-
recombinant heart-specific small regulatory subunit isoforms hHS-M21 A and B of MLCP
O60237
of the native and recombinant proteins by immunoprecipitation
-
KAMPPase, copurification of MLCPase and myosin light chain kinase activities, forming a multienzyme complex
-
SMP-I, holoenzyme and 38 kDa catalytic subunit
-
SMP-IV, 2000-6133fold
-
by immunoprecipitation from primary thymocytes using anti-PP1a, anti-PP1b, anti-MYPT1 antibodies in combination with protein A-Sepharose slurry, myosin phosphatase subunits PP1b and MYPT1 coimmunoprecipitate with HDAC7
-
native enzyme 340fold by ion exchange and hydrophobic interaction chromatography
-
Flag MYPT1 using anti-Flag affinity chromatography, His tagged proteins by Ni-NTA chromatography
-
recombinant myosin-binding subunit of MLCP, expressed in SF9 cells
-
SMPP-1M, subunits M110, M21 and PP1C catalytic subunit
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
the lethal mutation FP41 is a missense mutation changing one of the six highly conserved residues in the catalytic domain, D222N in flw-PA and D91N in flw-PB, it is mapped by meiotic recombination with visible recessive markers to the region between cut (7B4) and vermilion (9F11) and between P-elements PBac(WH)CG34408f03664 (9B7) and PBac(WH)Neb-cGPf02352 (9C4), sequence determination of the wild-type and mutant gene from genomic DNA from single FP41/Y larvae and controls
-
cDNAs encoding the 133 kDa myosin-binding subunit and the 20 kDa regulatory subunit are cloned and expressed in Escherichia coli BL21(DE3)
-
cDNAs encoding the 2 isoforms of the 130 kDa myosin binding subunit are cloned and sequenced
-
cloning of the cDNAs encoding the 130 kDa regulatory myosin-binding subunit MLCPa, the 38 kDa catalytic subunit MLCPc and the 20 kDa regulatory subunit MLCPsr, the full-length 130 kDa subunit is expressed in SF9 insect cells using the baculovirus expression system and sequenced
-
the 18.5 kDa isoform of the small subunit of MP is cloned and expressed in Escherichia coli KS1000(DE3)
-
cDNAs encoding the heart-specific small regulatory subunit isoforms hHS-M21 A and B of MLCP are cloned, sequenced and expressed in Escherichia coli, the small subunit is the product of the same gene as the large subunit: MYPT2, genomic structure of the gene for hHS-M21, the genes MYPT1 and MYPT2 encoding the large myosin-binding subunit MBS are cloned and expressed in Escherichia coli, genomic organisation of the MYPT2 gene, located on chromosome 1q32
O60237
co-expression of each of two myc-tagged myosin PPase targeting subunit 1 (MYPT1) isozymes with HA-tagged MLC phosphatase catalytic subunit CS1beta in COS-7 cells, and co-expression with ERM proteins ezrin, radixin, and moesin in COS-7 cells
-
expressed in Escherichia coli XL-10 Gold cells
-
expressed in Mus musculus
-
expression of FLAG-tagged full-length catalytic subunit MYPT1 in COS-7 cells, co-expression with Rho-associated kinase
-
expression of wild-type and mutant enzymes in CHO cells using a retroviral vector
-
His-tagged 57-residue peptide corresponding to residue 658-714 of myosin phosphatase targeting subunit 1 expressed in Escherichia coli
O14974
in Escherichia coli, expression of various C-terminal MYPT1 peptides bearing various combinations of a predicted coiled coil region, extensions preceding this coiled coil region, and the leucine-zipper motif
-
several isoforms of the large targeting subunit MYPT are encoded by 2 genes: MYPT1 and MYPT2, located on chromosomes 12 and 1, structure of MYPT1, MYPT2 is cloned from brain
-
targeting subunit of myosin phosphatase
-
various parts of myosin phosphatase targeting subunit GST-fusions expressed in Escherichia coli
-
overexpression of MYPT1 and MYPT2 in primary cultures of cardiac myocytes and in COS7 cells using baculoviral and adenoviral expression systems
-
expression in DO11/10 T cells, downregulation of myosin phosphatase genes by using siRNA for PP1 isoforms and MYPT1
-
a 72.5 kDa N-terminal fragment of the 110 kDa subunit is cloned
-
myosin-binding subunit of MLCP is cloned and expressed in SF9 cells
-
of MYPT1 in yeast AH109 strain for yeast two hybrid screening, MLCP holoenzyme in Sf9 cells by coinfection of rat His MYPT1, Flag MYPT1, rat PP1delta, and rat M21 expressing viruses, transfection of COS7 or NIH3T3 cells
-
an 89.6 kDa N-terminal fragment of MYPT1, an isoform of the 130 kDa regulatory targeting subunit of myosin phosphatase, is cloned and sequenced, MYPT is expressed by 2 genes, the two gene classes are termed MYPT1 and MYPT2
Q9TV77
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
stability of subunits PP1cbeta and MYPT1 is interdependent, knocking down one of the subunits decreases the expression level of the other
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
A233S
-
site-directed mutagenesis of subunit PP1cgamma
A281G
-
site-directed mutagenesis of subunit PP1cgamma
F38A
-
site-directed mutagenesis of subunit MYPT1, the mutant subunit is unable to bind to subunit PP1cbeta
G280A
-
site-directed mutagenesis of subunit PP1cbeta, the mutation does not affect interaction with MYPT1
N124A
-
catalytic subunit mutant, catalytically inactive
N236H/R237K
-
site-directed mutagenesis of subunit PP1cbeta, the mutation does not affect interaction with MYPT1
Q198T
-
site-directed mutagenesis of subunit PP1cgamma, mutant subunit is unable to bind to subunit MYPT1
S232A
-
site-directed mutagenesis of subunit PP1cbeta, the mutation does not affect interaction with MYPT1
T197Q
-
site-directed mutagenesis of subunit PP1cbeta, the mutant subunit is unable to bind to subunit MYPT1
additional information
-
mutants of the 133 kDa myosin-binding subunit
additional information
-
various truncation mutants of the 130 kDa subunit M130
additional information
-
overexpression of full-length enzyme in NIH3T3 cells in presence of serum causes a marked decrease in number of attached cells, block in the cell cycle prior to M phase and signs of increased apoptosis
H237N/K238R
-
site-directed mutagenesis of subunit PP1cgamma, the mutant subunit shows over 90% reduced ability to bind to subunit MYPT1
additional information
-
knock down of either or both isoforms of enzyme subunit MYPT 1 results in inhibition of myosin regulatory light chain dephosphorylation, of cell migration and adhesion, and in an increase of F-actin relative to G-actin in HeLa-cells
additional information
-
overexpression of full-length enzyme in NIH3T3 cells in presence of serum causes a marked decrease in number of attached cells, block in the cell cycle prior to M phase and signs of increased apoptosis
T696D
-
part of myosin phosphatase targeting subunit, inhibitory site
additional information
-
deletion of the C-terminal residues of MYPT1 at codon 39, 172, 297 and 517 by site directed mutagenesis
additional information
-
construction of synthetic segments of MYPT1 (1-19) and (24-41) and MYPT1(1-19) and (24-41) peptides
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
medicine
-
DMBS maintains epithelial integrity, loss of DMBS causes cell shape changes, loss of localization of the apical markers cadherin and increased accumulations of phospho-myosin regulatory light chain and F-actin, DMBS regulates the reorganization of cytoskeleton through down-regulation of myosin II, DMBS fits many of the criteria for a potential neoplastic type tumor suppressor gene
medicine
-
congestive heart failure is associated with a decrease in the COOH-terminus leucine zipper and the myosin targeting subunit of MLPC expression
medicine
-
in response to portal hypertension, abundance of MYPT 1 subunit is significantly reduced and switches to the leucine-zipper positive isoform
medicine
-
upon induction of congestive heart failure, left ventricular function is reduced to about 30% with concomitant decrease in sensitivity to 8-Br-+cGMP and expression of leucine-zipper positive isoform of MYPT 1 subunit
medicine
-
MYPT1 is downregulated and switches to the splice variant isoform that codes for the COOH-terminal leucine zipper motif in the hypertension of pregnancy model. These changes in MP expression are prevented by treatment with the antihypertensive medicine hydralazine. Early and effective treatment of hypertension during pregnancy may be able to reverse some of the adverse effects on uterine perfusion and fetal development in this disease
medicine
-
myosin light chain phosphatase pathway is critical in regulating in vivo myofibroblast differentiation during wound healing and fibrocontractive diseases
medicine
Rattus norvegicus Sprague-Dawley
-
myosin light chain phosphatase pathway is critical in regulating in vivo myofibroblast differentiation during wound healing and fibrocontractive diseases
-
additional information
-
dephosphorylation of myosin regulatory light-chain is essential for rapid recruitment or assembly of myosin II filaments, myosin phosphatase localizes to stress fibers depending on the activity of myosin II ATPase
additional information
Canis lupus familiaris Madin Darby
-
dephosphorylation of myosin regulatory light-chain is essential for rapid recruitment or assembly of myosin II filaments, myosin phosphatase localizes to stress fibers depending on the activity of myosin II ATPase
-
medicine
-
Ca2+-desensitizing hypoxic relaxation requires dephosphorylation of myosin phosphatase regulatory subunit
additional information
-
phosphorylation of endogenous inhibitor proteins provides a mechanism for reciprocal coordination of kinase and phosphatase activities