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Information on EC 2.7.11.18 - myosin-light-chain kinase
for references in articles please use BRENDA:EC2.7.11.18
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EC Tree 2 Transferases
2.7 Transferring phosphorus-containing groups
2.7.11 Protein-serine/threonine kinases
2.7.11.18 myosin-light-chain kinase
IUBMB Comments
Requires Ca2+ and calmodulin for activity. The 20-kDa light chain from smooth muscle myosin is phosphorylated more rapidly than any other acceptor, but light chains from other myosins and myosin itself can act as acceptors, but more slowly.
The enzyme appears in viruses and cellular organisms
- 2.7.11.18
-
contractile
- actin
- junction
- artery
- rho
- pkc
- agonist
- gizzard
- cytoskeletal
- actomyosin
-
tension
- occludin
-
rock
-
calmodulin-binding
-
actin-activated
-
isometric
-
rho-associated
- mlc20
-
paracellular
-
ca2+-independent
-
actin-myosin
-
rho-kinase
- wortmannin
-
zonula
- mypt1
-
cam-binding
-
actin-binding
-
cam-dependent
- trifluoperazine
- caldesmon
-
myofilament
-
hyperpermeability
-
thrombin-induced
-
thiophosphorylation
- mg2+-atpase
- calyculin
-
pseudosubstrate
- blebbistatin
- idella
-
diphosphorylation
- calponin
-
cross-bridge
- meromyosin
- medicine
-
mgatpase
-
myosin-binding
-
monoxime
-
n-6-aminohexyl-5-chloro-1-naphthalenesulfonamide
-
calmodulin-activated
-
superprecipitation
- cak
showSynonyms
mlck, myosin light chain kinase, myosin light-chain kinase, mlc kinase, smooth muscle myosin light chain kinase, smmlck, nmmlck, myosin kinase, cmlck, skmlck, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Ca2+-dependent kinase myosin light chain kinase
calcium/calmodulin-dependent myosin light chain kinase
-
-
-
-
cardiac myosin light chain kinase
cardiac-MLCK
Citron kinase
cMLCK
DNA-dependent protein kinase catalytic subunit
-
EC 2.7.1.117
-
-
formerly
-
endothelial MLCK
endothelial myosin light chain kinase
im:7148400
kinase, myosin light-chain (phosphorylating)
-
-
-
-
MLC kinase
MLCK
MLCK-210
MYLK
Mylk3
mylk5
myosin kinase
-
-
-
-
myosin light chain kinase
myosin light chain kinase, smooth muscle
myosin light chain kinase, smooth muscle and non-muscle isozymes
myosin light chain protein kinase
-
-
-
-
myosin light-chain kinase
myosine light chain kinase
nmMLCK
non-muscle myosin light chain kinase
obscurin-associated kinase
obscurin-MLCK-like kinase
smMLCK
smooth muscle myosin light chain kinase
smooth-muscle-myosin-light-chain kinase
-
-
-
-
additional information
MLCK
-
-
MLCK
-
-
MLCK
-
-
myosin light chain kinase
-
myosin light chain kinase
-
-
myosin light chain kinase
-
-
myosin light chain kinase
-
-
myosin light chain kinase, smooth muscle and non-muscle isozymes
-
myosin light-chain kinase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + [myosin light chain] = ADP + [myosin light chain] phosphate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
ATP:[myosin light chain] O-phosphotransferase
Requires Ca2+ and calmodulin for activity. The 20-kDa light chain from smooth muscle myosin is phosphorylated more rapidly than any other acceptor, but light chains from other myosins and myosin itself can act as acceptors, but more slowly.
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CAS REGISTRY NUMBER
COMMENTARY
51845-53-5
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + 20kDa myosin light chain
ADP + 20kDa myosin light chain phosphate
-
Substrates: phosphorylation occurs at Ser-19 and Thr-18
Products: -
Products: -
?
ATP + BpaKKRAARATSNVFA
ADP + ?
-
Substrates: Bpa is the photoreactive amino acid p-benzoylphenylalanine
Products: -
Products: -
?
ATP + Dictyostelium myosin
ADP + Dictyostelium myosin phosphate
Substrates: -
Products: -
Products: -
?
ATP + kemptamide
ADP + kemptamide phosphate
Substrates: i.e. peptide KKRPQRATSNVFS-NH2, activated enzyme
Products: -
Products: -
?
ATP + Lys-Lys-Arg-Ala-Ala-Arg-Ala-Thr-Ser-Asn-Val-Phe-Ala
ADP + ?
-
Substrates: -
Products: -
Products: -
?
ATP + Lys-Lys-Arg-Pro-Gln-Arg-Ala-Thr-Ser-Asn-Val-Phe-Ser
ADP + ?
-
Substrates: -
Products: -
Products: -
?
ATP + myosin
ADP + myosin phosphate
Substrates: -
Products: -
Products: -
?
ATP + myosin II
ADP + myosin II phosphate
Substrates: from Dictyostelium discoideum, activated enzyme
Products: -
Products: -
?
ATP + myosin-II regulatory light chain
ADP + myosin-II regulatory light chain phosphate
-
Substrates: -
Products: -
Products: -
?
ATP + phosphorylated myosin II regulatory light chain
ADP + di-phosphorylated myosin II regulatory light chain
-
Substrates: -
Products: -
Products: -
?
ATP + protein
ADP + phosphoprotein
Substrates: intramolecular autophosphorylation activates the enzyme
Products: -
Products: -
?
ATP + telokin
ADP + ?
-
Substrates: telokin may modulate enzyme activity in vivo
Products: -
Products: -
?
ATP + TRPC5 channel
ADP + phosphorylated TRPC5 channel
Substrates: Ca2+/calmodulin-dependent myosin light chain kinase is essential for activation of plasma membrane TRPC5 channels, responsible for Ca2+ influx, from Drosophila melanogaster expressed in HEK-293 cells, phosphorylation sites are Ser698, Ser775, and Thr700, mutational analysis
Products: -
Products: -
?
ATP + unphosphorylated myosin II regulatory light chain
ADP + phosphorylated myosin II regulatory light chain
-
Substrates: -
Products: -
Products: -
?
ATP + [myosin II light chain]
ADP + [myosin II lihght chain] phosphate
Substrates: from Dictyostelium discoideum, activated enzyme
Products: -
Products: -
?
ATP + [myosin II regulatory light chain]
ADP + [myosin II regulatory light chain] phosphate
ATP + [non-muscle heavy meromyosin IIB]
ADP + [non-muscle heavy meromyosin IIB] phosphate
Substrates: -
Products: -
Products: -
?
ATP + [non-muscle regulatory light chain]
ADP + [non-muscle regulatory light chain] phosphate
Substrates: -
Products: -
Products: -
?
ATP + [rabbit white skeletal muscle myosin P-light chain]
ADP + [rabbit white skeletal muscle myosin P-light chain] phosphate
-
Substrates: -
Products: -
Products: -
?
ATP + [smooth muscle heavy meromyosin]
ADP + [smooth muscle heavy meromyosin] phosphate
Substrates: -
Products: -
Products: -
?
ATP + [smooth muscle regulatory light chain]
ADP + [smooth muscle regulatory light chain] phosphate
Substrates: -
Products: -
Products: -
?
ATP + [ventricular isoform of myosin regulatory light chain MLC2v]
ADP + [ventricular isoform of myosin regulatory light chain MLC2v] phosphate
-
Substrates: -
Products: -
Products: -
?
ATP + light chain myosin II
ADP + phosphorylated light chain myosin II
-
Substrates: causes endothelial contraction
Products: -
Products: -
?
ATP + light chain myosin II
ADP + phosphorylated light chain myosin II
-
Substrates: -
Products: -
Products: -
?
ATP + light chain myosin II
ADP + phosphorylated light chain myosin II
-
Substrates: cardiac-MLCK is essential for normal cardiac development and function in zebrafish embryos, deletion of the gene encoding cardiac-MLCK is lethal for embryos
Products: -
Products: -
?
ATP + light chain myosin II
ADP + phosphorylated light chain myosin II
-
Substrates: the cardiac-specific substrate cardiac-MLCKis phosphorylated by the cardiac-specific isozyme MLC2v
Products: -
Products: -
?
ATP + light chain myosin II
ADP + phosphorylated light chain myosin II
-
Substrates: the enzyme is important in regulation of shape, adhesion and migration of fibrosarcoma cells, overview
Products: -
Products: -
?
ATP + light chain myosin II
ADP + phosphorylated light chain myosin II
-
Substrates: -
Products: -
Products: -
?
ATP + light chain myosin II
ADP + phosphorylated light chain myosin II
-
Substrates: cytokine-induced epithelial barrier dysfunction can be mediated by increased MLCK expression and subsequent myosin II regulatory light chain phosphorylation, the enzyme is involved in the inflammatory bowel disease
Products: -
Products: -
?
ATP + light chain myosin II
ADP + phosphorylated light chain myosin II
-
Substrates: regulatory myosin chain, phosphorylation at Ser18 and Thr19 on the N-terminus
Products: -
Products: -
?
ATP + light chain myosin II
ADP + phosphorylated light chain myosin II
-
Substrates: the cardiac-specific substrate MLC2v is phosphorylated by the cardiac-specific isozyme cardiac-MLCK
Products: -
Products: -
?
ATP + light chain myosin II
ADP + phosphorylated light chain myosin II
-
Substrates: regulatory myosin light chain
Products: -
Products: -
?
ATP + light chain myosin II
ADP + phosphorylated light chain myosin II
-
Substrates: roles of MLCK and ROCK on myosin II activation, overview, a global, MLCK-dependent increase in myosin II cortical contractility accompanies the metaphase-anaphase transition in sea urchin eggs, overview
Products: -
Products: -
?
ATP + light chain myosin II
ADP + phosphorylated light chain myosin II
-
Substrates: phosphorylation at Ser19
Products: -
Products: -
?
ATP + light chain myosin II
ADP + phosphorylated light chain myosin II
-
Substrates: myosin II activation is essential for stress fiber and focal adhesion formation, and is implicated in integrin-mediated signaling events
Products: -
Products: -
?
ATP + light chain myosin II
ADP + phosphorylated light chain myosin II
-
Substrates: MLCK plays a key role in the control of MLC-phosphorylation status, and it modulates barrier function through its regulation of intracellular contractile machinery, overview, endothelial mechanism of MLC-dependent barrier injury in burns, overview
Products: -
Products: -
?
ATP + light chain myosin II
ADP + phosphorylated light chain myosin II
-
Substrates: -
Products: -
Products: -
?
ATP + light chain myosin II
ADP + phosphorylated light chain myosin II
-
Substrates: regulatory myosin chain, in thick filaments, isozyme L-MLCK plays a role in cytoskeleton organization
Products: -
Products: -
?
ATP + light chain myosin II
ADP + phosphorylated light chain myosin II
-
Substrates: MLC phosphorylation increases muscle contraction and plays a prominent role in skeletal muscle force potentiation of fast-twitch type IIb but not type I or IIa fibers, overview
Products: -
Products: -
?
ATP + light chain myosin II
ADP + phosphorylated light chain myosin II
-
Substrates: regulatory myosin chain, phosphorylation at Ser18 and Thr19 on the N-terminus
Products: -
Products: -
?
ATP + light chain myosin II
ADP + phosphorylated light chain myosin II
-
Substrates: regulatory myosin chain
Products: -
Products: -
?
ATP + light chain myosin II
ADP + phosphorylated light chain myosin II
-
Substrates: -
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: -
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: acceptor substrates are myosin light chains of smooth muscle myosin
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: no substrates are myosin heavy chain and phosvitin
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: acceptor substrates are myosin light chains of skeletal muscle
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: acceptor substrates are myosin light chains of cardiac muscle
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: no substrate is histone 2-A
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: no substrate is casein
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: phosphorylation sites: Thr-residues in smooth muscle and pancreas myosin light chain
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: phosphorylation sites: Ser-residues in smooth and skeletal muscle
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: acceptor substrates are myosin light chains of adrenal medullary myosin
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: no substrate is histone 2 b
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: highly specific for regulatory or P-light-chain
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: highly specific for 18 kDa light chain
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: no substrate is synapsin
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: 1 mol phosphate per mol light chain in skeletal muscle
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: no substrate is phosphorylase kinase
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: acceptor substrates are myosin light chains of smooth muscle
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: specific for 20 kDa light chain
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: phosphorylation sites: Ser-19 and Thr-18 in smooth muscle myosin light chain
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: no substrates are myelin basic protein, glycogen synthase, tubulin, microtubule-associated protein 2, kemptide and peptide pp60src
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: not 16 kDa light chain
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: no substrate is histone V-S
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: no substrate is phosphorylase b
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: no substrates are myosin heavy chain and phosvitin
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: acceptor substrates are myosin light chains of skeletal muscle
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: acceptor substrates are myosin light chains of non-muscle myosin
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: not specific for 22 kDa and 15 kDa light chain
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: no substrate is casein
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: no substrate is troponin
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: no substrate is phosphorylase kinase
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: acceptor substrates are myosin light chains of smooth muscle
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: no substrate is phosphorylase b
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: kinase from skeletal muscle with broader specificity than smooth muscle kinase
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: -
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: obligatory step in development of active tension in smooth muscle
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: involved in muscle contractility and motility of non-muscle cells
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: involved in regulation of actin-myosin contractile activity in adrenal medulla
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: event in initiation of smooth-muscle contraction
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: -
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: the enzyme has effects on the actin-myosin interaction in vitro, binding of full-length and fragmented enzyme, overview. The Asp-Phe-Arg-X-X-Leu motif plays a major role in the binding of MLCK to myofibrils. Regulation of actinmyosin interaction by MLCK through its non-kinase activity, overview
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
Substrates: 20 kDa regulatory light chain of smooth muscle
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: no substrates are myosin heavy chain and phosvitin
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: acceptor substrates are myosin light chains of skeletal muscle
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: acceptor substrates are myosin light chains of non-muscle myosin
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: not specific for 22 kDa and 15 kDa light chain
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: no substrate is casein
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: no substrate is troponin
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: no substrate is phosphorylase kinase
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: acceptor substrates are myosin light chains of smooth muscle
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: no substrate is phosphorylase b
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: kinase from skeletal muscle with broader specificity than smooth muscle kinase
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: involved in muscle contractility and motility of non-muscle cells
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: no substrates are myosin heavy chain and phosvitin
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: acceptor substrates are myosin light chains of skeletal muscle
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: acceptor substrates are myosin light chains of non-muscle myosin
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: not specific for 22 kDa and 15 kDa light chain
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: no substrate is casein
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: no substrate is troponin
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: no substrate is phosphorylase kinase
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: acceptor substrates are myosin light chains of smooth muscle
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: no substrate is phosphorylase b
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: kinase from skeletal muscle with broader specificity than smooth muscle kinase
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: involved in muscle contractility and motility of non-muscle cells
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
Substrates: no substrates are myosin heavy chain and phosvitin
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
Substrates: no substrate is histone 2-A
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
Substrates: no substrate is casein
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
Substrates: not 16 kDa light chain
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
Substrates: no substrate is phosphorylase b
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
Substrates: -
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
Substrates: no substrates are myosin heavy chain and phosvitin
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
Substrates: no substrate is histone 2-A
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
Substrates: no substrate is casein
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
Substrates: not 16 kDa light chain
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
Substrates: no substrate is phosphorylase b
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: -
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: acceptor substrates are myosin light chains of smooth muscle myosin
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: acceptor substrates are myosin light chains of skeletal muscle
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: acceptor substrates are myosin light chains of cardiac muscle
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: no substrate is histone 2-A
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: no substrate is casein
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: highly specific for regulatory or P-light-chain
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: 1 mol phosphate per mol light chain in skeletal muscle
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: acceptor substrates are myosin light chains of smooth muscle
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: specific for 20 kDa light chain
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: no substrate is histone V-S
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: no substrate is phosphorylase b
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: -
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: no substrates are myosin heavy chain and phosvitin
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: acceptor substrates are myosin light chains of skeletal muscle
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: acceptor substrates are myosin light chains of non-muscle myosin
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: not specific for 22 kDa and 15 kDa light chain
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: no substrate is casein
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: no substrate is troponin
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: no substrate is phosphorylase kinase
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: acceptor substrates are myosin light chains of smooth muscle
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: no substrate is phosphorylase b
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: kinase from skeletal muscle with broader specificity than smooth muscle kinase
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: -
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: involved in muscle contractility and motility of non-muscle cells
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: event in initiation of smooth-muscle contraction
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: inhibition of actin-myosin ineraction
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
Substrates: activated MLCK then phosphorylates the regulatory myosin light chains, triggering cross-bridge cycling and contraction, myosin light chain phosphorylation is increased under these conditions, suggesting that contraction would be potentiated by ablation of AMPK
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: -
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
Substrates: -
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: the enzyme has effects on the actin-myosin interaction in vitro, regulation of actin-myosin interaction by MLCK through its non-kinase activity, overview
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: 20 kDa regulatory light chain of smooth muscle
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: acceptor substrates are myosin light chains of smooth muscle myosin
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: no substrates are myosin heavy chain and phosvitin
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: no substrate is protamine
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: acceptor substrates are myosin light chains of skeletal muscle
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: acceptor substrates are myosin light chains of cardiac muscle
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: no substrate is histone 2-A
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: no substrate is casein
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: phosphorylation sites: Thr-residues in smooth muscle and pancreas myosin light chain
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: phosphorylation sites: Ser-residues in smooth and skeletal muscle
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: highly specific for regulatory or P-light-chain
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: acceptor substrates are myosin light chains of smooth muscle
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: specific for 20 kDa light chain
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: phosphorylation sites: Ser-19 and Thr-18 in smooth muscle myosin light chain
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: no substrate is histone V-S
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: no substrate is phosphorylase b
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: no substrates are myosin heavy chain and phosvitin
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: acceptor substrates are myosin light chains of skeletal muscle
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: acceptor substrates are myosin light chains of non-muscle myosin
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: not specific for 22 kDa and 15 kDa light chain
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: no substrate is casein
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: no substrate is troponin
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: no substrate is phosphorylase kinase
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: acceptor substrates are myosin light chains of smooth muscle
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: no substrate is phosphorylase b
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: kinase from skeletal muscle with broader specificity than smooth muscle kinase
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: -
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: involved in muscle contractility and motility of non-muscle cells
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
Substrates: MLCK plays a crucial role in the cell migration and tumor metastasis
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: -
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: the MLCK family plays an essential role in regulation of actin/myosin organization, sarcomere assembly and cytoskeletal dynamics
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
Substrates: -
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: phosphorylation at Ser19
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: -
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: no substrates are actin and tropomyosin
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: no substrate is histone 2-A
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: no substrate is casein
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: no substrate is histone 2 b
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: no substrate is histone H1
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: 1 mol phosphate per mol light chain in skeletal muscle
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: specific for 20 kDa light chain
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: -
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: -
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: acceptor substrates are myosin light chains of smooth muscle myosin
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: acceptor substrates are myosin light chains of skeletal muscle
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: acceptor substrates are myosin light chains of cardiac muscle
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: transfers the gamma-phosphate of ATP to a Ser-residue of myosin light chain
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: no substrate is histone 2-A
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: no substrate is casein
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: phosphorylation sites: Thr-residues in smooth muscle and pancreas myosin light chain
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: phosphorylation sites: Ser-residues in smooth and skeletal muscle
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: highly specific for regulatory or P-light-chain
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: no substrate is phosphorylase kinase
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: acceptor substrates are myosin light chains of smooth muscle
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: specific for 20 kDa light chain
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: phosphorylation sites: Ser-19 and Thr-18 in smooth muscle myosin light chain
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: not 16 kDa light chain
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: no substrate is histone V-S
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: no substrate is phosphorylase b
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: acceptor substrates are myosin light chains of smooth muscle myosin
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: no substrates are myosin heavy chain and phosvitin
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: acceptor substrates are myosin light chains of skeletal muscle
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: acceptor substrates are myosin light chains of non-muscle myosin
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: not specific for 22 kDa and 15 kDa light chain
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: no substrate is casein
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: no substrate is troponin
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: no substrate is phosphorylase kinase
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: acceptor substrates are myosin light chains of smooth muscle
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: specific for 20 kDa light chain
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: no substrate is phosphorylase b
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: kinase from skeletal muscle with broader specificity than smooth muscle kinase
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: -
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: involved in muscle contractility and motility of non-muscle cells
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: -
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: the MLCK family plays an essential role in regulation of actin/myosin organization, sarcomere assembly and cytoskeletal dynamics
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: -
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: -
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: -
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: acceptor substrates are myosin light chains of smooth muscle myosin
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: acceptor substrates are myosin light chains of skeletal muscle
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: acceptor substrates are myosin light chains of cardiac muscle
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: ITP, GTP, CTP or UTP cannot replace ATP
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: not specific for 22 kDa and 15 kDa light chain
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: no substrate is casein
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: no substrates are 15 kDa and 22 kDa light-chain or heavy-chain fractions of myosin from white skeletal muscle
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: phosphorylation sites: Thr-residues in smooth muscle and pancreas myosin light chain
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: phosphorylation sites: Ser-residues in smooth and skeletal muscle
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: no substrate is troponin
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: highly specific for regulatory or P-light-chain
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: highly specific for 18 kDa light chain
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: specific for 18.5 kDa Dictyostelium or 19 kDa skeletal muscle light chain
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: 1 mol phosphate per mol light chain in skeletal muscle
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
Substrates: acceptor substrates are myosin light chains of smooth muscle
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: acceptor substrates are myosin light chains of smooth muscle
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: no substrate is molluscan adductor myosin
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: specific for 20 kDa light chain
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: phosphorylation sites: Ser-19 and Thr-18 in smooth muscle myosin light chain
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: acceptor substrates are myosin light chains of Ml3-myosin rabbit muscle
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: no substrate is phosphorylase b
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: no substrate is histone III-S from thymus
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: -
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
Substrates: event in initiation of smooth-muscle contraction
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: no substrate is histone 2-A
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: no substrate is casein
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: no substrate is phosphorylase b
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: -
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
Substrates: MLCK plays a critically important role in regulation of contraction in both smooth muscle and non-muscle cells, MLCK is both necessary and sufficient to initiate smooth muscle contraction
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
Substrates: -
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: acceptor substrates are myosin light chains of skeletal muscle
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: acceptor substrates are myosin light chains of cardiac muscle
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: no substrate is histone 2-A
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: phosphorylation sites: Thr-residues in smooth muscle and pancreas myosin light chain
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: phosphorylation sites: Ser-residues in smooth and skeletal muscle
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: highly specific for regulatory or P-light-chain
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: highly specific for 18 kDa light chain
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: no substrate is synapsin
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: acceptor substrates are myosin light chains of smooth muscle
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: specific for 20 kDa light chain
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: phosphorylation sites: Ser-19 and Thr-18 in smooth muscle myosin light chain
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: no substrates are myosin heavy chain and phosvitin
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: acceptor substrates are myosin light chains of skeletal muscle
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: acceptor substrates are myosin light chains of non-muscle myosin
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: not specific for 22 kDa and 15 kDa light chain
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: no substrate is casein
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: no substrate is troponin
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: no substrate is phosphorylase kinase
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: acceptor substrates are myosin light chains of smooth muscle
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: no substrate is phosphorylase b
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: kinase from skeletal muscle with broader specificity than smooth muscle kinase
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: -
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: involved in myosin phosphorylation and enzyme secretion
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: involved in muscle contractility and motility of non-muscle cells
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: in airway smooth muscles, kinase/phosphatase-dependent phosphorylation and dephosphorylation of the myosin light chain is an important step in calcium signalling pathway from the variation of Ca2+ concentration in cytosol to the force development
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
Substrates: activated MLCK then phosphorylates the regulatory myosin light chains, triggering cross-bridge cycling and contraction, myosin light chain phosphorylation is increased under these conditions, suggesting that contraction would be potentiated by ablation of AMPK
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: -
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: the MLCK family plays an essential role in regulation of actin/myosin organization, sarcomere assembly and cytoskeletal dynamics
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: -
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
Substrates: -
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: -
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: myosin light chain is phosphorylated at Thr 18 and Ser 19 by myosin light chain kinase
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: no substrates are myosin heavy chain and phosvitin
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: no substrate is protamine
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: acceptor substrates are myosin light chains of skeletal muscle
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: acceptor substrates are myosin light chains of cardiac muscle
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: no substrate is casein
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: phosphorylation sites: Thr-residues in smooth muscle and pancreas myosin light chain
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: phosphorylation sites: Ser-residues in smooth and skeletal muscle
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: highly specific for regulatory or P-light-chain
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: highly specific for 18 kDa light chain
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: no substrate is phosphorylase kinase
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: specific for 20 kDa light chain
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: phosphorylation sites: Ser-19 and Thr-18 in smooth muscle myosin light chain
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: no substrate is phosphorylase b
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: -
Products: -
Products: -
?
ATP + myosin light chain
ADP + phosphorylated myosin light chain
Substrates: -
Products: -
Products: -
?
ATP + myosin light chain
ADP + phosphorylated myosin light chain
Substrates: -
Products: -
Products: -
?
ATP + myosin light chain
ADP + phosphorylated myosin light chain
Substrates: the enzyme phosphorylates the 18000 Da Dictyostelium myosin regulatory light chain
Products: -
Products: -
?
ATP + myosin light chain
ADP + phosphorylated myosin light chain
-
Substrates: -
Products: -
Products: -
?
ATP + myosin light chain
ADP + phosphorylated myosin light chain
Substrates: -
Products: -
Products: -
?
ATP + myosin light chain
ADP + phosphorylated myosin light chain
-
Substrates: -
Products: -
Products: -
?
ATP + myosin light chain
ADP + phosphorylated myosin light chain
Substrates: -
Products: -
Products: -
?
ATP + myosin light chain
ADP + phosphorylated myosin light chain
-
Substrates: -
Products: -
Products: -
?
ATP + myosin light chain
ADP + phosphorylated myosin light chain
Substrates: -
Products: -
Products: -
?
ATP + myosin light chain
ADP + phosphorylated myosin light chain
-
Substrates: -
Products: -
Products: -
?
ATP + myosin light chain
ADP + phosphorylated myosin light chain
Substrates: -
Products: -
Products: -
?
ATP + myosin light chain
ADP + phosphorylated myosin light chain
-
Substrates: -
Products: -
Products: -
?
ATP + myosin light chain
ADP + phosphorylated myosin light chain
Substrates: -
Products: -
Products: -
?
ATP + myosin light chain
ADP + phosphorylated myosin light chain
Substrates: phosphorylation of myosin light chains by myosin light chain kinase is a key event in agonist-mediated endothelial cell gap formation and vascular permeability
Products: -
Products: -
?
ATP + myosin light chain
ADP + phosphorylated myosin light chain
-
Substrates: -
Products: -
Products: -
?
ATP + myosin light chain
ADP + phosphorylated myosin light chain
-
Substrates: -
Products: -
Products: -
?
ATP + myosin light chain
ADP + phosphorylated myosin light chain
-
Substrates: activated MLCK then phosphorylates the regulatory myosin light chains, triggering cross-bridge cycling and contraction, in aortic rings from mice in which alpha1, the major catalytic subunit isoform in arterial smooth muscle, is deleted, KCl- or phenylephrine-induced contraction is increased, overview
Products: -
Products: -
?
ATP + myosin light chain
ADP + phosphorylated myosin light chain
-
Substrates: -
Products: -
Products: -
?
ATP + myosin light chain
ADP + phosphorylated myosin light chain
Substrates: -
Products: -
Products: -
?
ATP + myosin light chain
ADP + phosphorylated myosin light chain
-
Substrates: -
Products: -
Products: -
?
ATP + myosin light chain
ADP + phosphorylated myosin light chain
Substrates: -
Products: -
Products: -
?
ATP + myosin light chain
ADP + phosphorylated myosin light chain
Substrates: -
Products: -
Products: -
?
ATP + myosin light chain
ADP + phosphorylated myosin light chain
Substrates: -
Products: -
Products: -
?
ATP + myosin light chain 2
ADP + myosin light chain 2 phosphate
Substrates: MLCK is involved in sarcomere organization, cardiac MLCK promotes sarcomere organization and increases cardiomyocyte contractility, overview
Products: -
Products: -
?
ATP + myosin light chain 2
ADP + myosin light chain 2 phosphate
Substrates: -
Products: -
Products: -
?
ATP + myosin regulatory light chain
ADP + myosin regulatory light chain phosphate
-
Substrates: -
Products: -
Products: -
?
ATP + myosin regulatory light chain
ADP + myosin regulatory light chain phosphate
-
Substrates: -
Products: -
Products: -
?
ATP + myosin regulatory light chain
ADP + phosphorylated myosin regulatory light chain
Substrates: -
Products: -
Products: -
?
ATP + myosin regulatory light chain
ADP + phosphorylated myosin regulatory light chain
-
Substrates: -
Products: -
Products: -
?
ATP + [myosin II regulatory light chain]
ADP + [myosin II regulatory light chain] phosphate
-
Substrates: involved in many cellular cytoskeletal functions
Products: -
Products: -
?
ATP + [myosin II regulatory light chain]
ADP + [myosin II regulatory light chain] phosphate
-
Substrates: -
Products: -
Products: -
?
ATP + [myosin light chain 2a]
ADP + [myosin light chain 2a] phosphate
-
Substrates: MLC phosphorylation plays a regulatory role in inotropic response to alpha1-adrenergic stimulation in the heart, enzyme inhibition causes heart failure in ventricular trabeculae
Products: -
Products: -
?
ATP + [myosin light chain 2a]
ADP + [myosin light chain 2a] phosphate
-
Substrates: -
Products: -
Products: -
?
ATP + [myosin light chain]
ADP + [myosin light chain] phosphate
-
Substrates: the multifunctional regulatory enzyme stimulates smooth muscle myosin ATPase activity by binding to the myosin heads without phosphorylating the myosin light chain, kinetics, overview
Products: -
Products: -
?
ATP + [myosin light chain]
ADP + [myosin light chain] phosphate
-
Substrates: -
Products: -
Products: -
?
ATP + [myosin light chain]
ADP + [myosin light chain] phosphate
Substrates: -
Products: -
Products: -
?
ATP + [myosin light chain]
ADP + [myosin light chain] phosphate
Substrates: non-muscle myosin II
Products: -
Products: -
?
ATP + [myosin light chain]
ADP + [myosin light chain] phosphate
Substrates: non-muscle myosin II and preferred substrate smooth muscle myosin II
Products: -
Products: -
?
ATP + [myosin light chain]
ADP + [myosin light chain] phosphate
Substrates: smooth muscle myosin regulatory light chain phosphorylation at Ser19
Products: -
Products: -
?
ATP + [myosin light chain]
ADP + [myosin light chain] phosphate
Substrates: phosphorylation of myosin on Ser19 of the regulatory light chain. Non-muscle myosin II regulatory light chain and preferred substrate smooth muscle myosin II regulatory light chain
Products: -
Products: -
?
ATP + [myosin light chain]
ADP + [myosin light chain] phosphate
-
Substrates: -
Products: -
Products: -
?
ATP + [myosin light chain]
ADP + [myosin light chain] phosphate
-
Substrates: activation of the enzyme is a key regulatory step in the modulation of endothelial permeability, central to parthogenesis of inflammatory lung disease is disruption of the endothelial barrier function
Products: -
Products: -
?
ATP + [myosin light chain]
ADP + [myosin light chain] phosphate
-
Substrates: -
Products: -
Products: -
?
ATP + [myosin light chain]
ADP + [myosin light chain] phosphate
-
Substrates: the endothelial isozyme is a mutifunctional contractile effector involved in vascular barrier regulation, leukocyte diapedesis, apoptosis, and angiogenesis
Products: -
Products: -
?
ATP + [myosin light chain]
ADP + [myosin light chain] phosphate
-
Substrates: enzyme is regulating cytoskeletal rearrangement and cell motility
Products: -
Products: -
?
ATP + [myosin light chain]
ADP + [myosin light chain] phosphate
-
Substrates: -
Products: -
Products: -
?
ATP + [myosin light chain]
ADP + [myosin light chain] phosphate
-
Substrates: activated phosphorylated enzyme
Products: -
Products: -
?
ATP + [myosin light chain]
ADP + [myosin light chain] phosphate
Substrates: smooth muscle myosin II
Products: -
Products: -
?
ATP + [myosin light chain]
ADP + [myosin light chain] phosphate
-
Substrates: -
Products: -
Products: -
?
ATP + [myosin light chain]
ADP + [myosin light chain] phosphate
Substrates: -
Products: -
Products: -
?
ATP + [myosin light chain]
ADP + [myosin light chain] phosphate
-
Substrates: -
Products: -
Products: -
?
ATP + [myosin light chain]
ADP + [myosin light chain] phosphate
Substrates: -
Products: -
Products: -
?
ATP + [myosin light chain]
ADP + [myosin light chain] phosphate
Substrates: phosphorylation levels of MLC2v in the apex of the hearts. The MLC2v phosphorylation in strain C57BL/6N is significantly lower than that in C57BL/6J mice
Products: -
Products: -
?
ATP + [myosin light chain]
ADP + [myosin light chain] phosphate
Substrates: non-muscle myosin II and preferred substrate smooth muscle myosin II
Products: -
Products: -
?
ATP + [myosin light chain]
ADP + [myosin light chain] phosphate
Substrates: MLC2
Products: -
Products: -
?
ATP + [myosin light chain]
ADP + [myosin light chain] phosphate
Substrates: phosphorylation of Thr-18/Ser-19 on the regulatory light chain of myosin II
Products: -
Products: -
?
ATP + [myosin light chain]
ADP + [myosin light chain] phosphate
-
Substrates: -
Products: -
Products: -
?
ATP + [myosin light chain]
ADP + [myosin light chain] phosphate
Mus musculus C57BL/6N/C57BL/6J
Substrates: phosphorylation levels of MLC2v in the apex of the hearts. The MLC2v phosphorylation in strain C57BL/6N is significantly lower than that in C57BL/6J mice
Products: -
Products: -
?
ATP + [myosin light chain]
ADP + [myosin light chain] phosphate
Mus musculus C57BL/6N/C57BL/6J
Substrates: MLC2
Products: -
Products: -
?
ATP + [myosin light chain]
ADP + [myosin light chain] phosphate
Substrates: -
Products: -
Products: -
?
ATP + [myosin light chain]
ADP + [myosin light chain] phosphate
-
Substrates: -
Products: -
Products: -
?
ATP + [myosin light chain]
ADP + [myosin light chain] phosphate
-
Substrates: the non-muscle myosin light chain kinase is involved in regulation of hepatic functions in response to intra- and extracellular signals
Products: -
Products: -
?
ATP + [myosin light chain]
ADP + [myosin light chain] phosphate
-
Substrates: -
Products: -
Products: -
?
ATP + [myosin light chain]
ADP + [myosin light chain] phosphate
Substrates: smooth muscle myosin
Products: -
Products: -
?
ATP + [myosin light chain]
ADP + [myosin light chain] phosphate
Substrates: myyosin II
Products: -
Products: -
?
ATP + [myosin light chain]
ADP + [myosin light chain] phosphate
Substrates: myosin II
Products: -
Products: -
?
ATP + [myosin light chain]
ADP + [myosin light chain] phosphate
Substrates: smooth muscle myosin
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme possesses ATPase activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: skeletal, gizzard smooth and cardiac enzymes perform intramolecular autophosphorylation in the absence of acceptor substrate
Products: -
Products: -
?
additional information
?
-
-
Substrates: infection of brain endothelial cells with Haemophilus somnus causes alterations in brain endothelial cell and blood-brain barrier integrity and causes inflammation involving the enzyme, which acts in rapid cytoskeletal rearrangement, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: actin-myosin interaction of smooth muscle could be activated by the non-kinase activity of MLCK, a mechanism that is quite independent of MLC20 phosphorylation, role of non-kinase activity of myosin light-chain kinase in regulating smooth muscle contraction, overview
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme also exerts non-kinase activity on myosin motor and myosin ATPase activities
Products: -
Products: -
?
additional information
?
-
-
Substrates: skeletal, gizzard smooth and cardiac enzymes perform intramolecular autophosphorylation in the absence of acceptor substrate
Products: -
Products: -
?
additional information
?
-
-
Substrates: skeletal, gizzard smooth and cardiac enzymes perform intramolecular autophosphorylation in the absence of acceptor substrate
Products: -
Products: -
?
additional information
?
-
Substrates: skeletal, gizzard smooth and cardiac enzymes perform intramolecular autophosphorylation in the absence of acceptor substrate
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme does not require interaction with RhoA to localize to the cleavage site
Products: -
Products: -
-
additional information
?
-
-
Substrates: skeletal, gizzard smooth and cardiac enzymes perform intramolecular autophosphorylation in the absence of acceptor substrate
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is a potential cytoskeleton integrator through its unique N-terminal domain, the enzyme binds tubulin and actin, and is involved in microtubule/microfilament association
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is a key regulator of various forms of cell motility involving actin and myosin II
Products: -
Products: -
?
additional information
?
-
Substrates: MLCK is a substrate of AMP-activated protein kinase, AMPK
Products: -
Products: -
?
additional information
?
-
-
Substrates: MLCK is a substrate of AMP-activated protein kinase, AMPK
Products: -
Products: -
?
additional information
?
-
-
Substrates: actin-myosin interaction of smooth muscle could be activated by the non-kinase activity of MLCK, a mechanism that is quite independent of MLC20 phosphorylation, role of non-kinase activity of myosin light-chain kinase in regulating smooth muscle contraction, overview. MLCK phosphorylated at Ser828 stimulates the ATPase activity of unphosphorylated myosin more effectively than the control MLCK
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme also exerts non-kinase activity on myosin motor and myosin ATPase activities
Products: -
Products: -
?
additional information
?
-
Substrates: non-muscle myosin and smooth muscle myosin are the only known substrates of MLCK in vivo
Products: -
Products: -
?
additional information
?
-
Substrates: static substrate binding structure of streptavidin-tagged enzyme, overview
Products: -
Products: -
?
additional information
?
-
Substrates: MLCK has a 2fold higher kcat for both smooth muscle myosin II substrates compared with non-muscle myosin IIB substrates, whereas Km values are very similar. Myosin light chain kinase has a 1.6fold and 1.5fold higher specificity (kcat/Km) for smooth versus non-muscle-free regulatory light chain and heavy meromyosin, respectively, suggesting that differences in specificity are dictated by regulatory light chain sequences. Three residues, Glu70, Gly71, and Ser74, are found to be surface exposed in the N-terminal half of the regulatory light chain, consistent with their importance in substrate recognition. Substrate recognition and specificity, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: skeletal, gizzard smooth and cardiac enzymes perform intramolecular autophosphorylation in the absence of acceptor substrate
Products: -
Products: -
?
additional information
?
-
Substrates: the differentiation-dependent enzyme splice variant MLCK1 regulates epithelial tight junction permeability, the endothelial isozyme is responsible for Na+-glucose cotransport-induced tight junction regulation
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme activity is cell cycle regulated with a decrease in activity during mitosis due to phosphorylation, inhibition of enzyme phosphorylation during mitosis leads to microtubule defects, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme interacts with macrophage migration inhibition factor MIF in endothelium which may be important for the regulation of both non-muscle cytoskeletal dynamics as well as pathobiological vascular events involving the enzyme
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme mediates eosinophil chemotaxis in a mitogen-activated protein kinase-dependent manner
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme plays an important role in TNFalpha-dependent induction of NFkappaB activity, mechanism
Products: -
Products: -
?
additional information
?
-
-
Substrates: inhibition of MLCK results in spherical cells and marked impairment of adhesion and migration of fibrosarcoma cells, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: ventricular/cardiac muscle isozyme cardiac-MLCK, which is involved in the development of human cardiomyopathy, is an important structural protein that affects physiologic cardiac sarcomere formation and heart development, the cardiac MLCK regulates sarcomere assembly in the vertebrate heart, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: increased MLCK activity accompanies increases in MLC expression, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: Human T cell leukemia virus 1-infected lymphocytes can cause a breakdown of the blood-brain barrier inducing an increase in paracellular endothelial permeability and transcellular migration, this disruption is associated with tight junction disorganization between endothelial cells and altered tight junction proteinexpression involving the enzyme MLCK, enzyme inhibition prevents the changes in endothelial cells, overview
Products: -
Products: -
?
additional information
?
-
Substrates: MLCK in the plasma membrane distribution of TRPC5 channels, overview
Products: -
Products: -
?
additional information
?
-
Substrates: MLCK in the plasma membrane distribution of TRPC5 channels, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: MLCK in the plasma membrane distribution of TRPC5 channels, overview
Products: -
Products: -
?
additional information
?
-
Substrates: myosin light-chain kinase contributes to the proliferation and migration of breast cancer cells through cross-talk with activated ERK1/2, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: cytochalasin-induced increases in paracellular permeability are also mediated by MLC in Caco-2 monolayers
Products: -
Products: -
?
additional information
?
-
-
Substrates: PKA regulates beta2-integrin avidity activation via a MLCK-dependent pathway, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is involved in inflammation response, including apoptosis, vascular permeability, and leukocyte diapedesis. Single nucleotide polymorphisms are involved in the risk of sepsis-related acute lung injury and asthma
Products: -
Products: -
?
additional information
?
-
Substrates: MLCK and truncated 1-75 MLCK interaction analysis with actin, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: KIF14 is required for the localization of the enzyme
Products: -
Products: -
-
additional information
?
-
-
Substrates: no intramolecular autophosphorylation in the absence of acceptor substrate
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate specificity and binding structure, the enzyme depends on basic residues for substrate recognition, autoregulation by a pseudosubstrate mechanism, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is involved, probably via microfilament assembly, in sperm chromatin-induced cortical reorganization during oocyte maturation to a polarized egg
Products: -
Products: -
?
additional information
?
-
-
Substrates: the myosin light chain kinase plays a role in the regulation of epithelial cell survival, and in the generation of pro-survival signals in both untransformed and transformed epithelial cells, apoptosis following inhibition of myosin II activation by MLCK is probably meditated through the death receptor pathway, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: inhibition of the enzyme retards the growth of mammary cancer cells
Products: -
Products: -
?
additional information
?
-
-
Substrates: regulation of the MLCK promoters and gene expression involving myocardin, model, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: MLCK is a substrate of AMP-activated protein kinase, AMPK
Products: -
Products: -
?
additional information
?
-
-
Substrates: myosin light chain kinase is central to smooth muscle contraction and required for gastrointestinal motility in mice, overview
Products: -
Products: -
?
additional information
?
-
Substrates: the cardiac-specific isozyme probably performs also autophosphorylation
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme binds to thin filaments with high affinity, myofilament binding by Ig-like modules is blocked by disassembling of the filaments, overview
Products: -
Products: -
?
additional information
?
-
Substrates: postnatal decreases in vascular reactivity involve decreases in the thick filament component of myofilament calcium sensitivity, which is measured as the relationship between cytosolic calcium concentration and myosin light chain phosphorylation, relations between myosin light chain phosphorylation and contractile force, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: skeletal, gizzard smooth and cardiac enzymes perform intramolecular autophosphorylation in the absence of acceptor substrate
Products: -
Products: -
?
additional information
?
-
-
Substrates: MLCK is probably involved in development of diabetic nephropathy, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is not a regulator of synaptic vesicle trafficking during repetitive exocytosis in cultured hippocampal neurons, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme negatively regulates synaptic plasticity and fear learning in the lateral nucleus of the amygdala, the enzyme is involved in memory aquisitoion, rather than in posttraining consolidation of memory, the enzyme may help to prevent aquisition of irrelevant fears, thus enzyme deficiency or defects can lead to pathological fear learning, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: inhibition of the enzyme retards the growth of prostate cancer cells
Products: -
Products: -
?
additional information
?
-
Substrates: MLCK is a substrate of AMP-activated protein kinase, AMPK
Products: -
Products: -
?
additional information
?
-
-
Substrates: no intramolecular autophosphorylation in the absence of acceptor substrate
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + myosin light chain 2
ADP + myosin light chain 2 phosphate
Substrates: MLCK is involved in sarcomere organization, cardiac MLCK promotes sarcomere organization and increases cardiomyocyte contractility, overview
Products: -
Products: -
?
ATP + [myosin II regulatory light chain]
ADP + [myosin II regulatory light chain] phosphate
-
Substrates: involved in many cellular cytoskeletal functions
Products: -
Products: -
?
ATP + [myosin light chain 2a]
ADP + [myosin light chain 2a] phosphate
-
Substrates: MLC phosphorylation plays a regulatory role in inotropic response to alpha1-adrenergic stimulation in the heart, enzyme inhibition causes heart failure in ventricular trabeculae
Products: -
Products: -
?
ATP + [ventricular isoform of myosin regulatory light chain MLC2v]
ADP + [ventricular isoform of myosin regulatory light chain MLC2v] phosphate
-
Substrates: -
Products: -
Products: -
?
ATP + light chain myosin II
ADP + phosphorylated light chain myosin II
-
Substrates: causes endothelial contraction
Products: -
Products: -
?
ATP + light chain myosin II
ADP + phosphorylated light chain myosin II
-
Substrates: cardiac-MLCK is essential for normal cardiac development and function in zebrafish embryos, deletion of the gene encoding cardiac-MLCK is lethal for embryos
Products: -
Products: -
?
ATP + light chain myosin II
ADP + phosphorylated light chain myosin II
-
Substrates: the enzyme is important in regulation of shape, adhesion and migration of fibrosarcoma cells, overview
Products: -
Products: -
?
ATP + light chain myosin II
ADP + phosphorylated light chain myosin II
-
Substrates: -
Products: -
Products: -
?
ATP + light chain myosin II
ADP + phosphorylated light chain myosin II
-
Substrates: cytokine-induced epithelial barrier dysfunction can be mediated by increased MLCK expression and subsequent myosin II regulatory light chain phosphorylation, the enzyme is involved in the inflammatory bowel disease
Products: -
Products: -
?
ATP + light chain myosin II
ADP + phosphorylated light chain myosin II
-
Substrates: roles of MLCK and ROCK on myosin II activation, overview, a global, MLCK-dependent increase in myosin II cortical contractility accompanies the metaphase-anaphase transition in sea urchin eggs, overview
Products: -
Products: -
?
ATP + light chain myosin II
ADP + phosphorylated light chain myosin II
-
Substrates: myosin II activation is essential for stress fiber and focal adhesion formation, and is implicated in integrin-mediated signaling events
Products: -
Products: -
?
ATP + light chain myosin II
ADP + phosphorylated light chain myosin II
-
Substrates: MLCK plays a key role in the control of MLC-phosphorylation status, and it modulates barrier function through its regulation of intracellular contractile machinery, overview, endothelial mechanism of MLC-dependent barrier injury in burns, overview
Products: -
Products: -
?
ATP + light chain myosin II
ADP + phosphorylated light chain myosin II
-
Substrates: regulatory myosin chain, in thick filaments, isozyme L-MLCK plays a role in cytoskeleton organization
Products: -
Products: -
?
ATP + light chain myosin II
ADP + phosphorylated light chain myosin II
-
Substrates: MLC phosphorylation increases muscle contraction and plays a prominent role in skeletal muscle force potentiation of fast-twitch type IIb but not type I or IIa fibers, overview
Products: -
Products: -
?
ATP + light chain myosin II
ADP + phosphorylated light chain myosin II
-
Substrates: -
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: -
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: obligatory step in development of active tension in smooth muscle
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: involved in muscle contractility and motility of non-muscle cells
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: involved in regulation of actin-myosin contractile activity in adrenal medulla
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: event in initiation of smooth-muscle contraction
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: -
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: involved in muscle contractility and motility of non-muscle cells
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: involved in muscle contractility and motility of non-muscle cells
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
Substrates: -
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: -
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: involved in muscle contractility and motility of non-muscle cells
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: event in initiation of smooth-muscle contraction
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: inhibition of actin-myosin ineraction
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
Substrates: activated MLCK then phosphorylates the regulatory myosin light chains, triggering cross-bridge cycling and contraction, myosin light chain phosphorylation is increased under these conditions, suggesting that contraction would be potentiated by ablation of AMPK
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: -
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: -
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: involved in muscle contractility and motility of non-muscle cells
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
Substrates: MLCK plays a crucial role in the cell migration and tumor metastasis
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: -
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: the MLCK family plays an essential role in regulation of actin/myosin organization, sarcomere assembly and cytoskeletal dynamics
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: -
Products: -
Products: -
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: -
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ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: involved in muscle contractility and motility of non-muscle cells
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ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: -
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?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: the MLCK family plays an essential role in regulation of actin/myosin organization, sarcomere assembly and cytoskeletal dynamics
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ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: -
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ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: -
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ATP + myosin light chain
ADP + myosin light chain phosphate
Substrates: event in initiation of smooth-muscle contraction
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ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: -
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ATP + myosin light chain
ADP + myosin light chain phosphate
Substrates: MLCK plays a critically important role in regulation of contraction in both smooth muscle and non-muscle cells, MLCK is both necessary and sufficient to initiate smooth muscle contraction
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ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: -
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ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: involved in myosin phosphorylation and enzyme secretion
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?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: involved in muscle contractility and motility of non-muscle cells
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ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: in airway smooth muscles, kinase/phosphatase-dependent phosphorylation and dephosphorylation of the myosin light chain is an important step in calcium signalling pathway from the variation of Ca2+ concentration in cytosol to the force development
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ATP + myosin light chain
ADP + myosin light chain phosphate
Substrates: activated MLCK then phosphorylates the regulatory myosin light chains, triggering cross-bridge cycling and contraction, myosin light chain phosphorylation is increased under these conditions, suggesting that contraction would be potentiated by ablation of AMPK
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ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: -
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ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: the MLCK family plays an essential role in regulation of actin/myosin organization, sarcomere assembly and cytoskeletal dynamics
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ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: -
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ATP + myosin light chain
ADP + myosin light chain phosphate
-
Substrates: -
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ATP + myosin light chain
ADP + phosphorylated myosin light chain
Substrates: -
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ATP + myosin light chain
ADP + phosphorylated myosin light chain
Substrates: -
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ATP + myosin light chain
ADP + phosphorylated myosin light chain
Substrates: the enzyme phosphorylates the 18000 Da Dictyostelium myosin regulatory light chain
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ATP + myosin light chain
ADP + phosphorylated myosin light chain
-
Substrates: -
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ATP + myosin light chain
ADP + phosphorylated myosin light chain
Substrates: -
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ATP + myosin light chain
ADP + phosphorylated myosin light chain
-
Substrates: -
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ATP + myosin light chain
ADP + phosphorylated myosin light chain
Substrates: -
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ATP + myosin light chain
ADP + phosphorylated myosin light chain
-
Substrates: -
Products: -
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?
ATP + myosin light chain
ADP + phosphorylated myosin light chain
Substrates: -
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ATP + myosin light chain
ADP + phosphorylated myosin light chain
-
Substrates: -
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ATP + myosin light chain
ADP + phosphorylated myosin light chain
Substrates: -
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ATP + myosin light chain
ADP + phosphorylated myosin light chain
-
Substrates: -
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ATP + myosin light chain
ADP + phosphorylated myosin light chain
Substrates: -
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ATP + myosin light chain
ADP + phosphorylated myosin light chain
Substrates: phosphorylation of myosin light chains by myosin light chain kinase is a key event in agonist-mediated endothelial cell gap formation and vascular permeability
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ATP + myosin light chain
ADP + phosphorylated myosin light chain
-
Substrates: -
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ATP + myosin light chain
ADP + phosphorylated myosin light chain
-
Substrates: -
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ATP + myosin light chain
ADP + phosphorylated myosin light chain
-
Substrates: activated MLCK then phosphorylates the regulatory myosin light chains, triggering cross-bridge cycling and contraction, in aortic rings from mice in which alpha1, the major catalytic subunit isoform in arterial smooth muscle, is deleted, KCl- or phenylephrine-induced contraction is increased, overview
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ATP + myosin light chain
ADP + phosphorylated myosin light chain
Substrates: -
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?
ATP + myosin light chain
ADP + phosphorylated myosin light chain
-
Substrates: -
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ATP + myosin light chain
ADP + phosphorylated myosin light chain
Substrates: -
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ATP + myosin light chain
ADP + phosphorylated myosin light chain
Substrates: -
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ATP + myosin light chain
ADP + phosphorylated myosin light chain
Substrates: -
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ATP + myosin regulatory light chain
ADP + phosphorylated myosin regulatory light chain
Substrates: -
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?
ATP + myosin regulatory light chain
ADP + phosphorylated myosin regulatory light chain
-
Substrates: -
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ATP + [myosin light chain]
ADP + [myosin light chain] phosphate
-
Substrates: the multifunctional regulatory enzyme stimulates smooth muscle myosin ATPase activity by binding to the myosin heads without phosphorylating the myosin light chain, kinetics, overview
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ATP + [myosin light chain]
ADP + [myosin light chain] phosphate
Substrates: -
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?
ATP + [myosin light chain]
ADP + [myosin light chain] phosphate
Substrates: non-muscle myosin II
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ATP + [myosin light chain]
ADP + [myosin light chain] phosphate
Substrates: non-muscle myosin II and preferred substrate smooth muscle myosin II
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ATP + [myosin light chain]
ADP + [myosin light chain] phosphate
-
Substrates: -
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ATP + [myosin light chain]
ADP + [myosin light chain] phosphate
-
Substrates: activation of the enzyme is a key regulatory step in the modulation of endothelial permeability, central to parthogenesis of inflammatory lung disease is disruption of the endothelial barrier function
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ATP + [myosin light chain]
ADP + [myosin light chain] phosphate
-
Substrates: -
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ATP + [myosin light chain]
ADP + [myosin light chain] phosphate
-
Substrates: the endothelial isozyme is a mutifunctional contractile effector involved in vascular barrier regulation, leukocyte diapedesis, apoptosis, and angiogenesis
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ATP + [myosin light chain]
ADP + [myosin light chain] phosphate
-
Substrates: enzyme is regulating cytoskeletal rearrangement and cell motility
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ATP + [myosin light chain]
ADP + [myosin light chain] phosphate
-
Substrates: -
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ATP + [myosin light chain]
ADP + [myosin light chain] phosphate
Substrates: smooth muscle myosin II
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ATP + [myosin light chain]
ADP + [myosin light chain] phosphate
-
Substrates: -
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ATP + [myosin light chain]
ADP + [myosin light chain] phosphate
Substrates: -
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ATP + [myosin light chain]
ADP + [myosin light chain] phosphate
-
Substrates: -
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ATP + [myosin light chain]
ADP + [myosin light chain] phosphate
Substrates: -
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ATP + [myosin light chain]
ADP + [myosin light chain] phosphate
Substrates: phosphorylation levels of MLC2v in the apex of the hearts. The MLC2v phosphorylation in strain C57BL/6N is significantly lower than that in C57BL/6J mice
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ATP + [myosin light chain]
ADP + [myosin light chain] phosphate
Substrates: non-muscle myosin II and preferred substrate smooth muscle myosin II
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ATP + [myosin light chain]
ADP + [myosin light chain] phosphate
-
Substrates: -
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ATP + [myosin light chain]
ADP + [myosin light chain] phosphate
Mus musculus C57BL/6N/C57BL/6J
Substrates: phosphorylation levels of MLC2v in the apex of the hearts. The MLC2v phosphorylation in strain C57BL/6N is significantly lower than that in C57BL/6J mice
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ATP + [myosin light chain]
ADP + [myosin light chain] phosphate
Substrates: -
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?
ATP + [myosin light chain]
ADP + [myosin light chain] phosphate
-
Substrates: -
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ATP + [myosin light chain]
ADP + [myosin light chain] phosphate
-
Substrates: the non-muscle myosin light chain kinase is involved in regulation of hepatic functions in response to intra- and extracellular signals
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ATP + [myosin light chain]
ADP + [myosin light chain] phosphate
Substrates: smooth muscle myosin
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?
ATP + [myosin light chain]
ADP + [myosin light chain] phosphate
Substrates: myyosin II
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ATP + [myosin light chain]
ADP + [myosin light chain] phosphate
Substrates: smooth muscle myosin
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additional information
?
-
-
Substrates: infection of brain endothelial cells with Haemophilus somnus causes alterations in brain endothelial cell and blood-brain barrier integrity and causes inflammation involving the enzyme, which acts in rapid cytoskeletal rearrangement, overview
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?
additional information
?
-
-
Substrates: actin-myosin interaction of smooth muscle could be activated by the non-kinase activity of MLCK, a mechanism that is quite independent of MLC20 phosphorylation, role of non-kinase activity of myosin light-chain kinase in regulating smooth muscle contraction, overview
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additional information
?
-
-
Substrates: the enzyme is a potential cytoskeleton integrator through its unique N-terminal domain, the enzyme binds tubulin and actin, and is involved in microtubule/microfilament association
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additional information
?
-
-
Substrates: the enzyme is a key regulator of various forms of cell motility involving actin and myosin II
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additional information
?
-
Substrates: MLCK is a substrate of AMP-activated protein kinase, AMPK
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?
additional information
?
-
-
Substrates: MLCK is a substrate of AMP-activated protein kinase, AMPK
Products: -
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?
additional information
?
-
-
Substrates: actin-myosin interaction of smooth muscle could be activated by the non-kinase activity of MLCK, a mechanism that is quite independent of MLC20 phosphorylation, role of non-kinase activity of myosin light-chain kinase in regulating smooth muscle contraction, overview. MLCK phosphorylated at Ser828 stimulates the ATPase activity of unphosphorylated myosin more effectively than the control MLCK
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?
additional information
?
-
Substrates: non-muscle myosin and smooth muscle myosin are the only known substrates of MLCK in vivo
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additional information
?
-
Substrates: the differentiation-dependent enzyme splice variant MLCK1 regulates epithelial tight junction permeability, the endothelial isozyme is responsible for Na+-glucose cotransport-induced tight junction regulation
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additional information
?
-
-
Substrates: the enzyme activity is cell cycle regulated with a decrease in activity during mitosis due to phosphorylation, inhibition of enzyme phosphorylation during mitosis leads to microtubule defects, overview
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additional information
?
-
-
Substrates: the enzyme interacts with macrophage migration inhibition factor MIF in endothelium which may be important for the regulation of both non-muscle cytoskeletal dynamics as well as pathobiological vascular events involving the enzyme
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?
additional information
?
-
-
Substrates: the enzyme mediates eosinophil chemotaxis in a mitogen-activated protein kinase-dependent manner
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additional information
?
-
-
Substrates: the enzyme plays an important role in TNFalpha-dependent induction of NFkappaB activity, mechanism
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additional information
?
-
-
Substrates: inhibition of MLCK results in spherical cells and marked impairment of adhesion and migration of fibrosarcoma cells, overview
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additional information
?
-
-
Substrates: ventricular/cardiac muscle isozyme cardiac-MLCK, which is involved in the development of human cardiomyopathy, is an important structural protein that affects physiologic cardiac sarcomere formation and heart development, the cardiac MLCK regulates sarcomere assembly in the vertebrate heart, overview
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additional information
?
-
-
Substrates: increased MLCK activity accompanies increases in MLC expression, overview
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additional information
?
-
-
Substrates: Human T cell leukemia virus 1-infected lymphocytes can cause a breakdown of the blood-brain barrier inducing an increase in paracellular endothelial permeability and transcellular migration, this disruption is associated with tight junction disorganization between endothelial cells and altered tight junction proteinexpression involving the enzyme MLCK, enzyme inhibition prevents the changes in endothelial cells, overview
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?
additional information
?
-
Substrates: myosin light-chain kinase contributes to the proliferation and migration of breast cancer cells through cross-talk with activated ERK1/2, overview
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additional information
?
-
-
Substrates: cytochalasin-induced increases in paracellular permeability are also mediated by MLC in Caco-2 monolayers
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additional information
?
-
-
Substrates: PKA regulates beta2-integrin avidity activation via a MLCK-dependent pathway, overview
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additional information
?
-
-
Substrates: the enzyme is involved in inflammation response, including apoptosis, vascular permeability, and leukocyte diapedesis. Single nucleotide polymorphisms are involved in the risk of sepsis-related acute lung injury and asthma
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additional information
?
-
-
Substrates: the enzyme is involved, probably via microfilament assembly, in sperm chromatin-induced cortical reorganization during oocyte maturation to a polarized egg
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additional information
?
-
-
Substrates: the myosin light chain kinase plays a role in the regulation of epithelial cell survival, and in the generation of pro-survival signals in both untransformed and transformed epithelial cells, apoptosis following inhibition of myosin II activation by MLCK is probably meditated through the death receptor pathway, overview
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additional information
?
-
-
Substrates: inhibition of the enzyme retards the growth of mammary cancer cells
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additional information
?
-
-
Substrates: regulation of the MLCK promoters and gene expression involving myocardin, model, overview
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additional information
?
-
-
Substrates: MLCK is a substrate of AMP-activated protein kinase, AMPK
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additional information
?
-
-
Substrates: myosin light chain kinase is central to smooth muscle contraction and required for gastrointestinal motility in mice, overview
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additional information
?
-
-
Substrates: the enzyme binds to thin filaments with high affinity, myofilament binding by Ig-like modules is blocked by disassembling of the filaments, overview
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additional information
?
-
Substrates: postnatal decreases in vascular reactivity involve decreases in the thick filament component of myofilament calcium sensitivity, which is measured as the relationship between cytosolic calcium concentration and myosin light chain phosphorylation, relations between myosin light chain phosphorylation and contractile force, overview
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additional information
?
-
-
Substrates: MLCK is probably involved in development of diabetic nephropathy, overview
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additional information
?
-
-
Substrates: the enzyme is not a regulator of synaptic vesicle trafficking during repetitive exocytosis in cultured hippocampal neurons, overview
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additional information
?
-
-
Substrates: the enzyme negatively regulates synaptic plasticity and fear learning in the lateral nucleus of the amygdala, the enzyme is involved in memory aquisitoion, rather than in posttraining consolidation of memory, the enzyme may help to prevent aquisition of irrelevant fears, thus enzyme deficiency or defects can lead to pathological fear learning, overview
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additional information
?
-
-
Substrates: inhibition of the enzyme retards the growth of prostate cancer cells
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additional information
?
-
Substrates: MLCK is a substrate of AMP-activated protein kinase, AMPK
Products: -
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Calmodulin
-
trypsin or chymotrypsin digested smooth muscle enzyme is independent of Ca2+/calmodulin
Calmodulin
-
trypsin or chymotrypsin digested smooth muscle enzyme is independent of Ca2+/calmodulin
Calmodulin
-
trypsin or chymotrypsin digested smooth muscle enzyme is independent of Ca2+/calmodulin
Calmodulin
-
trypsin or chymotrypsin digested smooth muscle enzyme is independent of Ca2+/calmodulin
Calmodulin
-
trypsin or chymotrypsin digested smooth muscle enzyme is independent of Ca2+/calmodulin
Calmodulin
-
trypsin or chymotrypsin digested smooth muscle enzyme is independent of Ca2+/calmodulin
Calmodulin
-
trypsin or chymotrypsin digested smooth muscle enzyme is independent of Ca2+/calmodulin
Calmodulin
-
trypsin or chymotrypsin digested smooth muscle enzyme is independent of Ca2+/calmodulin
Calmodulin
-
trypsin or chymotrypsin digested smooth muscle enzyme is independent of Ca2+/calmodulin
Calmodulin
-
only active as ternary complex of calmodulin, Ca2+ and kinase: activation is initiated by binding of Ca2+ to calmodulin
Calmodulin
-
calmodulin in presence of Ca2+ abolishes the inhibition of actin-myosin interaction
Calmodulin
-
optimal ratio of enzyme to calmodulin for telokin phosphorylation is 1:4
Calmodulin
-
lower affinity for Ca2+/caldesmon after phosphorylation by cAMP-dependent protein kinase, Ka: 0.0000006 mM
Calmodulin
-
requirement
Calmodulin
-
requirement
Calmodulin
-
requirement
Calmodulin
-
binding site I at residue 1002-1022, binding site II at residues 26-42, complex formation with Ca2+
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Mg2+
Ca2+
-
dependent on, antagonizes the binding to actin, Ca/CaM binds at the Ala796-Ser815 sequence to regulate the kinase activity MLCK
Ca2+
-
-
Ca2+
-
Ca2+ in presence of calmodulin abolishes the inhibition of actin-myosin interaction
Ca2+
-
-
Ca2+
-
the enzyme is dependent on Ca2+ and calmodulin, the intracellular Ca2+ concentration has regulatory effect, overview
Mg2+
-
requirement, varies with ATP-concentration, MgATP2- is the active substrate
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
11-(3-chloro-6-iminopyridazin-1(6H)-yl)-N-(6-phenylpyridazin-3-yl)undecanamide
-
highly specific inhibitor, competitive to ATP binding
AKKLSKDRMAAYMARRK
-
synthetic peptide, analog of inhibitory region of myosin light chain kinase
AKKLSKDRMKKYMA
-
synthetic peptide, analog of inhibitory region of myosin light chain kinase
AKKLSKDRMKKYMAAAA
-
synthetic peptide, analog of inhibitory region of myosin light chain kinase
AKKLSKDRMKKYMARR
-
synthetic peptide, analog of inhibitory region of myosin light chain kinase
AKKLSKDRMKKYMARRK
-
synthetic peptide, analog of inhibitory region of myosin light chain kinase
AKKLSKDRMKKYMARRKWQKTG
-
synthetic peptide, analog of inhibitory region of myosin light chain kinase
alkylamine
-
long and straight chain, most effective with chain length C-13 to C-18
Carbachol
-
increases Ca2+ concentration, MLCK activation and regulatory light chain phosphorylation
human arrest defective-1
-
human arrest defective-1 is a bona fide regulator of MLCK, human arrest defective-1 associates with an IgG motif of MLCK and acetylates the Lys-608 residue in this motif and by so doing deactivates MLCK
-
KDRMKKYMARR
-
synthetic peptide, analog of inhibitory region of myosin light chain kinase
KT5926
-
i.e. (8R,9S,11S)-(-)-9-hydroxy-9-methoxycarbonyl-8-methyl-14-n-propoxy-2,3,9,10-tetrahydro-8,11-epoxy,1H,8H,11H-2,7beta,11alpha-triazadeibenzo[a,g]cycloocta[cde]triden-1-one, specific inhibitor
LSKDRMKKYMARRKWQK
-
synthetic peptide, analog of inhibitory region of myosin light chain kinase
MLCK inhibitor peptide 18
-
a membrane permeant nonapeptide inhibitor of MLCK. Treatment with the MLCK inhibitor peptide 18 attenuates the increased epithelial monolayer permeability and occludin endocytosis caused by anoxia/reoxygenation injury
-
MS-347a
-
from Aspergillus sp. KY52178, structurally related to sydowinin B, irreversible, inhibition of calmodulin-dependent and independent activity, IC50: 0.0092 mM
Peptide 18
-
i.e. H-RKKYKYRRK-NH2, specifically inhibits the enzyme and prevents sperm chromatin-induced cortical reorganization in eggs in vivo
-
SKDRMKKYMARRKWQKTGHAVRAI
-
autoregulatory pseudosubstrate sequence of smooth muscle enzyme, residues 787-810
SQRLLKKYLMKRRWKKNFIAVSAA
-
autoregulatory pseudosubstrate sequence of the skeletal muscle enzyme, residues 570-593
1-(5-Iodonaphthalene-1-sulfonyl)-1H-hexahydro-1,4-diazepine hydrochloride
inhibitor targeting the ATPase domain of the enzyme; inhibitor targeting the ATPase domain of the enzyme
1-(5-Iodonaphthalene-1-sulfonyl)-1H-hexahydro-1,4-diazepine hydrochloride
-
-
cAMP-dependent protein kinase
-
phosphorylates light chain myosin kinase leading to decreased affinity from calmodulin
-
cAMP-dependent protein kinase
-
phosphorylates light chain myosin kinase leading to decreased affinity from calmodulin
-
cAMP-dependent protein kinase
-
phosphorylates light chain myosin kinase leading to decreased affinity from calmodulin
-
kaempferol
-
i.e. 3,5,7-trihydroxy-2-(4-hydroxyphenyl)-1-benzopyran-4-one, IC50: 0.00045 mM
KCl
-
increases Ca2+ concentration, MLCK activation and regulatory light chain phosphorylation
ML-7
-
i.e. 1-(5-iodonaphthalene-1-sulfonyl)-1H-hexahydro-1,4-diazepine HCl, specific inhibitor
ML-7
ie. 1-(5-iodonaphthalene-1-sulfonyl)-1H-hexahydro-1,4-diazapine hydrochloride, a specific inhibitor of MLCK, ML-7 is able to depress the cell proliferation and migration in vivo using two parallel breast cancer cell lines. ML-7 not only blocks MLCK but also downregulates activated ERK1/2 with downstream effectors of beta-catenin-survivin-cyclin D1-c-Myc, overview
ML-7
-
specifically inhibits the enzyme and prevents sperm chromatin-induced cortical reorganization in eggs in vivo
ML-7
-
specific inhibitor of MLCK, has a chemopreventive effect in an in vitro mouse mammary organ culture model, in vivo the inhibitor retards the growth of mammary tumours, acts as an adjuvant to etoposide stimulating its ability to prevent growth of established tomours, overview
ML-7
-
inhibition of MLCK induces apoptosis in adherent cells and disrupts cell-cell adhesion
ML-7
-
calmodulin/enzyme-specific inhibitor, inhibits cell attachment to extracellular substrate in vivo, attenuates the activation of GTP-binding protein Rac and cell migration
ML-7
-
specific inhibitor of MLCK, in vivo the inhibitor retards the growth of prostate tumours, acts as an adjuvant to etoposide stimulating its ability to prevent growth of established tomours, overview
ML-7
-
specificity, overview, ML-7 changes action potential amplitude and voltage-gated Ca2+ channel current nonspecifically, but does not affect calcimycin-induced release and vesicle readily releasable pool RRP recovery after depletion
ML-7
-
a specific inhibitor, in vivo the inhibitor enhances the short-term and long-term memory, when applied before fear conditioning, but not immediately afterwards, the inhibitor has no effet on memory retrieval and behaviour when the training stimuli are presented in a non-associative manner
ML-7
chemical inhibition of myosin light chain kinase (MLCK) slows down endocytosis
ML-9
impairs the plasma membrane localization of TRPC5 channels; impairs the plasma membrane localization of TRPC5 channels
ML-9
-
i.e. 1-(5-chloronaphthalene-1-sulfonyl)-1H-hexahydro-1,4-diazepine, inhibits MLCK and paracellular permeability increases in several intestinal epithelial models
ML-9
-
inhibition of MLCK induces apoptosis in adherent cells and disrupts cell-cell adhesion
ML-9
-
i.e. 1-(5-chloronaphthalene-1-sulfonyl)-1H-hexahydro-1,4-diazepine, inhibits MLCK and paracellular permeability increases in several intestinal epithelial models
ML-9
-
i.e. 1-(5-chloronaphthalene-1-sulfonyl)-1H-hexahydro-1,4-diazepine, inhibits MLCK and paracellular permeability increases in several intestinal epithelial models
RKKYKYRRK-NH2
specific enzyme inhibitor targeting the kinase domain; specific enzyme inhibitor targeting the kinase domain
W-7
-
calmodulin/enzyme-specific inhibitor, attenuates cell migration in vivo
Wortmannin
-
i.e. MS-54, IC50: 0.0019 mM, irreversible, highly selective, kinetics, high concentrations of ATP protect
additional information
-
non-kinase, inhibitory activity of N-terminal, actin-binding domain of MLCK
-
additional information
the enzyme is regulated by an autoinhibitory domain
-
additional information
residues 283-288 function as an autoinhibitory domain, autoinhibition is fully relieved by Thr166 phosphorylation
-
additional information
-
synthesis of peptides behaving as pseudosubstrates, determination of inhibitory potential
-
additional information
autoregulatory domain extends from Asn780 to Arg808. The peptide Leu774 to Ser787 does not inhibit smMLCK, peptides of similar or shorter length from the pseudosubstrate region, Ser787 to Val807, are potent inhibitors
-
additional information
-
autoregulatory domain extends from Asn780 to Arg808. The peptide Leu774 to Ser787 does not inhibit smMLCK, peptides of similar or shorter length from the pseudosubstrate region, Ser787 to Val807, are potent inhibitors
-
additional information
-
no inhibition by epicatechin, pseudobabtisin, 4-dimethylaminobenzaldehyde
-
additional information
-
oxytoxin and phorbol ester do not affect the enzyme activity. Non-kinase, inhibitory activity of N-terminal, actin-binding domain of MLCK
-
additional information
phosphorylation at serine residues 140/149 by cAMP-dependent protein kinase (PKA) and Aurora B leads to a decrease in N27-157 binding to actin
-
additional information
MLCK is inhibited as the ionic strength increases
-
additional information
the inhibitor of ERK1/2, PD98059, downregulates the levels of MLCK and phosphorylated myosin light chain
-
additional information
-
PAK phosphorylation of MLCK by p21-activated kinase, a kinase activated by the Rho family of GTPases, can inhibit MLCK activity
-
additional information
-
protein kinase A inhibits MLCK and myosin loght chain dephosphorylation, the latter via effects on the Rho kinase/MLC phosphatase pathway, reversible by KT5720, an inhibitor of PKA. Inhibition of MLC phosphorylation leads to beta2-integrin activation and adhesion, overview
-
additional information
-
inhibitor effects on enzyme activity in intestinal tissues, overview
-
additional information
-
the enzyme is inhibited by its regulatory subunit masking the active site, autoregulation by a pseudosubstrate mechanism, protein substrate-pseudosubstrate interactions, overview
-
additional information
-
structural requirements of autoinhibition of myosin light chain kinase
-
additional information
-
no inhibition by diacylglycerol, phosphatidylserine
-
additional information
-
PAK phosphorylation of MLCK by p21-activated kinase, a kinase activated by the Rho family of GTPases, can inhibit MLCK activity
-
additional information
-
inhibitor effects on enzyme activity in intestinal tissues, overview
-
additional information
-
no inhibition by 3',5'-cAMP; no inhibition by AMP
-
additional information
-
PAK phosphorylation of MLCK by p21-activated kinase, a kinase activated by the Rho family of GTPases, can inhibit MLCK activity
-
additional information
-
inhibitor effects on enzyme activity in intestinal tissues, overview
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
calyculin A
calyculin A increased papillary muscle MLC2v phosphorylation to a similar extent in both strains but increased the phenylephrine-induced inotropic response only in C57BL/6N
F-actin
-
binding via the DFRXXL motifs in the N-terminal region of isozymes S-MLCK and L-MLCK, the latter also uses the six Ig-like modules in its N-terminal extension for binding, the first two of which are minimally required for microfilament binding, overview
-
methylcellulose
enhances the rate of MLCK-induced phosphorylation of smooth muscle myosin and MLCK-induced mechanical activation of smooth muscle myosin to move actin filaments
-
thrombin
-
stimulates endothelial isozyme activity in endothelium, and increases EC MLCK interaction with macrophage migration inhibition factor MIF
-
TNFalpha
-
stimulates endothelial isozyme activity in endothelium, and increases EC MLCK interaction with macrophage migration inhibition factor MIF
-
Calmodulin
-
dependent on, antagonizes the binding to actin, residues 26-41 of MLCK act as a CaM-binding region that regulates the binding of MLCK to actin, Ca/CaM is also binds at the Ala796-Ser815 sequence to regulate the kinase activity MLCK
tumor necrosis factor-alpha
-
i.e TNF-alpha, activates enzyme activity in endothelial cells
-
additional information
-
no activation by Ca2+ plus beta-lactoglobulin, cytochrome c, troponin C or parvalbumin
-
additional information
-
tumor necrosis factor-alpha induces enzyme activity in vivo
-
additional information
140fold activation through phosphorylation at Thr166
-
additional information
-
oxytoxin and phorbol ester do not affect the enzyme activity
-
additional information
kinetics of myosin light chain kinase activation of smooth muscle myosin in an in vitro model system, overview. Actin has no activating effect on the enzyme activity
-
additional information
enzyme MLCK210 possesses actin binding regions both in the central part of the molecule and in its N-terminal tail domain
-
additional information
-
the endothelial isozyme EC MLCK contains a unique N-terminal sequence which is a target for upregulation by signaling cascade components such as p60src
-
additional information
-
oxidized low density lipoprotein induces the enzyme expression and activation in umbilical vein endothelial cells, which is inhibited by melatonin and PD98059
-
additional information
-
activation of the RhoA pathway can inhibit myosin phosphatase activity, thereby enhancing the effects of the kinase-mediated phosphorylation of myosin light chain
-
additional information
-
pp60src- or c-Abl-mediated phosphorylation of nmMLCK at Y464 and Y471 increases MLC kinase activity
-
additional information
-
the enzyme is activated by phosphorylation through mitogen activated protein kinase MAPK
-
additional information
-
myocardin, a cardiac SAP, SAF-A/B, acinus, PIAS, domain-containing protein, is important in regulation of enzyme expression, overview, induction of enzyme expression by the thyrotroph embryonic factor binding to the the CArG box of the promoter, TEF
-
additional information
-
activation of the RhoA pathway can inhibit myosin phosphatase activity, thereby enhancing the effects of the kinase-mediated phosphorylation of myosin light chain
-
additional information
-
treatment with pentoxifylline attenuates activation of MLCK likely through its ability to decrease local tumor necrosis factor-alpha synthesis and nucleat factor kappaB activation after burn
-
additional information
-
electric stimulation of intact skeletal muscles activate the enzyme activity, overview
-
additional information
-
activation of the RhoA pathway can inhibit myosin phosphatase activity, thereby enhancing the effects of the kinase-mediated phosphorylation of myosin light chain
-
additional information
-
epilactose induces myosin light chain phosphorylation via MLCK
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0075
BpaKKRAARATSNVFA
-
25°C, pH 7, Bpa is the photoreactive amino acid p-benzoylphenylalanine
0.1 - 0.2
[rabbit white skeletal muscle myosin P-light chain]
-
27°C, pH 7.6
-
0.005
[ventricular isoform of myosin regulatory light chain MLC2v]
-
at 25°C, pH not specified in the publication
-
additional information
additional information
-
in the presence of wortmannin
-
additional information
additional information
-
kinetic constants for enzymes from various sources with different myosin light chains as substrates
-
additional information
additional information
-
kinetic constants for enzymes from various sources with different myosin light chains as substrates
-
additional information
additional information
-
kinetic constants for enzymes from various sources with different myosin light chains as substrates
-
additional information
additional information
-
kinetic constants for enzymes from various sources with different myosin light chains as substrates
-
additional information
additional information
-
kinetic constants for enzymes from various sources with different myosin light chains as substrates
-
additional information
additional information
-
kinetic constants for enzymes from various sources with different myosin light chains as substrates
-
additional information
additional information
-
kinetic constants for enzymes from various sources with different myosin light chains as substrates
-
additional information
additional information
-
Michaelis-Menten kinetics, kinetic scheme of the mathematical model considers interactions among Ca2+, calmodulin and MLCK, and the well-known 4-state actomyosin latch bridge model, whereby a link between them is accomplished by the conservation relation of all species of MLCK, detailed overview
-
additional information
additional information
kinetics of myosin light chain kinase activation of smooth muscle myosin in an in vitro model system, kinetic modelling, overview. The dissociation of MLCK from phosphorylated smooth muscle myosin is rate-limiting and that the rate of the phosphorylation step is faster than this dissociation rate. Association to smooth muscle myosin is much faster than to smooth muscle myosin. The probability of MLCK interacting with unphosphorylated versus smooth muscle myosin is 55-460 times greater
-
additional information
additional information
steady-state kinetic parameters of MLCK toward 4 different substrates: the 2-headed heavy meromyosin (HMM) soluble subfragments of both smooth muscle myosin II and non-muscle myosin IIB, each containing their respective smooth or non-muscle regulatory light chains, and the 2 types of free regulatory light chains. MLCK has an about 2fold higher kcat for both smooth muscle myosin II substrates compared with non-muscle myosin IIB substrates, whereas Km values are very similar
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
steady-state kinetics: comparison of smooth muscle myosin II and non-muscle myosin IIB as substrates, overview. MLCK has an about 2fold higher kcat for both smooth muscle myosin II substrates compared with non-muscle myosin IIB substrates, whereas Km values are very similar
-
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
myosin light chain kinase has a 1.6fold and 1.5fold higher kcat/Km for smooth versus non-muscle-free regulatory light chain and heavy meromyosin, respectively
-
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.008
dihydrosphingosine
Gallus gallus
-
erythro- and threo-dihydrosphingosine, IC50: 0.008 mM
0.0092
MS-347a
Gallus gallus
-
from Aspergillus sp. KY52178, structurally related to sydowinin B, irreversible, inhibition of calmodulin-dependent and independent activity, IC50: 0.0092 mM
0.0019
Wortmannin
Gallus gallus
-
i.e. MS-54, IC50: 0.0019 mM, irreversible, highly selective, kinetics, high concentrations of ATP protect
0.00045
kaempferol
Bos taurus
-
i.e. 3,5,7-trihydroxy-2-(4-hydroxyphenyl)-1-benzopyran-4-one, IC50: 0.00045 mM
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1.8
7.9
additional information
additional information
-
quantification of enzyme activity using a Ca2+/calmodulin-dependent fluorescent biosensor MLCK in vitro or in vivo, overview
additional information
quantitative determination of phosphorylated myosin light chain
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.7 - 8.2
-
about half-maximal activity at pH 5.7 and 8.2, with a small shoulder of 77% of maximal activity at 7-7.5
6.8 - 8.8
-
about half-maximal activity at pH 6.8 and about 75% of maximal activity at pH 8.8
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22
25
30
37
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5
-
isoelectric focusing, pH 3-10, 4% polyacrylamide gel or flat bed isoelectric focusing with Sephadex G-200
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
brenda
-
640619, 640620, 640621, 640622, 640623, 640624, 640625, 640632, 640635, 640646, 660857, 673994, 684910
-
-
brenda
cardiac/ventricular isozyme cardiac-MLCK encoded by gene MLCK3, and smooth muscle isozyme encoded by gene MLCK2
-
-
brenda
-
491268, 640620, 640624, 640629, 640633, 640634, 640635, 640639, 640640, 640643, 640644, 640645, 640647, 640648, 640649, 640650, 640651, 640652, 640653, 640655, 640662, 661664, 672981, 684910
-
-
brenda
-
640618, 640626, 640631, 640632, 640645, 640646, 640663, 661436, 661665, 661729, 661920, 662502, 662503, 663446, 671753, 672981, 675212, 675729
-
-
brenda
-
-
-
brenda
2 isozymes encoded by a single gene and translated from 2 different splicing variants
-
-
brenda
cardiac/ventricular isozyme cardiac-MLCK encoded by gene MLCK3, and smooth muscle isozyme encoded by gene MLCK2
-
-
brenda
splicing variant 1, i.e. isozyme MLCK1; 2 endothelial isozymes MLCK1 and MLCK2
SwissProt
brenda
splicing variant 2, i.e. isozyme MLCK2; 2 endothelial isozymes MLCK1 and MLCK2
SwissProt
brenda
2 isozymes encoded by a single gene and translated from 2 different splicing variants
-
-
brenda
gene mylk1, encoding two isozymes: the endothelial, long or nonmuscle 220-kDa MLCK and a short, smooth muscle 130-kDa MLCK
-
-
brenda
-
-
-
brenda
domain characterization of the skeletal muscle enzyme
SwissProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
fetal and adult, quantification of the enzyme and its product
brenda
-
myofibroblast-like stellate cell line, previously called Ito cells, lipocytes, or fat-storing cells
brenda
-
LNCaP cells express both long (non-muscle) and short (smooth muscle) isoforms of MLCK
brenda
-
smMLCK expresses in almost every tissue, including plaeta
brenda
-
the long isoform of MLCK, MLCK-210, is the predominant isoform expressed in vascular endothelial cells
brenda
additional information
maximal stimulation-induced in situ myosin light chain kinase activity is upregulated in fetal compared to adult ovine carotid arteries
brenda
-
cMLCK is exclusively expressed in cardic muscle, smMLCK expresses in almost every tissue, including cardiac muscles
brenda
-
from embryos, in myofibril precursors and sarcomeric Z-lines, co-localization with myosin IIB
brenda
-
from patients who had not been treated with chemotherapy or radiotherapy, freshlys collected at the time of surgical resection for malignant or non-inflammatory disease
brenda
-
-
640620, 640624, 640635, 640639, 640640, 640645, 640648, 640649, 640650, 640651, 640652, 640653, 640655
brenda
-
rat pancreatic and turkey gizzard enzyme are immunologically related
brenda
-
-
brenda
-
pregnant sheep myometrium, turkey and chicken gizzard enzyme are immunologically related
brenda
-
specific cardiac/ventricular isozyme cardiac-MLCK encoded by gene MLCK3, expression analysis in healthy hearts and hearts from patients with heart failure
brenda
-
left ventricle tissue, MLCK occurs in a cross-striated pattern overlapping with the distribution of alpha-actin
brenda
-
ileal epithelial MLCK expression is mildly upregulated in inactive inflammatory bowel disease, and highly upregulated in active IBD
brenda
-
epithelium, expression of MLVK is upregulated by inflammatory bowel disease
brenda
from 2 d or 4 d postfertilization (dpf) embryos, im:7148400 is the only MLCK isozyme in keratocytes
brenda
-
from 2 d or 4 d postfertilization (dpf) embryos, im:7148400 is the only MLCK isozyme in keratocytes
-
brenda
-
expression analysis of MLCK in healthy and streptozotocin-induced diabetic rats, expression in glomerulus, renal tubule and glomerular arteriolar, glomerulus expression is increased in diabetic rats, overview
brenda
-
expression of obscurin-MLCK-like kinase is restricted to muscles in the myonucleus
brenda
-
expression of obscurin-MLCK-like kinase is restricted to muscles in the myonucleus
brenda
telokin, the carboxyl terminus of the smooth muscle myosin light chain kinase which is expressed as an independent protein, is expressed in some smooth muscle tissues but not in aortic smooth muscle or in any non-muscle tissues
brenda
-
expression of obscurin-MLCK-like kinase is restricted to muscles in the myonucleus
brenda
-
adult, MLCK occurs in a cross-striated pattern overlapping with the distribution of alpha-actin
brenda
-
pregnant sheep myometrium, turkey and chicken gizzard enzyme are immunologically related
brenda
-
rat pancreatic and turkey gizzard enzyme are immunologically related
brenda
-
skeletal muscle expresses a specific MLCK called skeletal-muscle-type myosin light chain kinase, smooth muscle myosin light chain kinase expresses in almost every tissue including skeletal muscles
brenda
-
smMLCK expresses in almost every tissue, incnluding small intestine
brenda
-
specific smooth muscle isozyme smMLCK encoded by gene MLCK2
brenda
-
-
brenda
-
specific smooth muscle isozyme smMLCK encoded by gene MLCK2
brenda
the abundance of active MLCK, which is tightly associated with the contractile apparatus, is low relative to that of smooth muscle myosin
brenda
-
smMLCK expresses in almost every tissue, including smooth muscles
brenda
long (220 kDa) and short (130 kDa) MLCK isozymes
brenda
additional information
-
myosin light chain kinases in smooth muscle and non-muscle tissues are the same protein
brenda
additional information
-
myosin light chain kinases in smooth muscle and non-muscle tissues are the same protein
brenda
additional information
myosin light chain kinase is a ubiquitous Ca2+/calmodulin (CaM)-activated kinase found in smooth, cardiac, and skeletal muscle as well as in mammalian non-muscle cells
brenda
additional information
the human MLCK gene yields multiple nonmuscle MLCK isoforms by alternative splicing of its transcribed mRNA precursor with differential distribution of these isoforms in various human tissues and cells
brenda
additional information
-
the human MLCK gene yields multiple nonmuscle MLCK isoforms by alternative splicing of its transcribed mRNA precursor with differential distribution of these isoforms in various human tissues and cells
brenda
additional information
expression profile of isozymes MLCK1 and MLCK2
brenda
additional information
-
tissue dependent MLCK expression analysis of 26 inflammatory bowel disease patients
brenda
additional information
-
developmental pattern of obscurin and obscurin-associated kinase expression, overview
brenda
additional information
-
two isozymes: the endothelial, long or nonmuscle 220-kDa MLCK and a short, smooth muscle 130-kDa MLCK, mechanism of regulation of tissue-specific mylk gene expression, overview
brenda
additional information
-
developmental pattern of obscurin and obscurin-associated kinase expression, overview
brenda
additional information
-
myosin light chain kinases in smooth muscle and non-muscle tissues are the same protein
brenda
additional information
myosin light chain kinases in smooth muscle and non-muscle tissues are the same protein
brenda
additional information
-
myosin light chain kinases in smooth muscle and non-muscle tissues are the same protein
brenda
additional information
-
developmental pattern of obscurin and obscurin-associated kinase expression, overview
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
MLCK and the N-terminal 75 residues of MLCK move on actin bundles and stress fibers of smooth muscle cell cytoskeletons by a random one-dimensional diffusion mechanism, modelling, overview. MLCK motion is permitted only if actomyosin and MLCKmyosin interactions are weak
brenda
additional information
-
the enzyme is dispersed to the cytoplasm in prometaphase and associated with midzone spindles by a Rho-independent signal. Rho is then activated, binds to the enzyme and translocates it to cell cortex, where the complex is then concentrated in the cleavage furrow by the action of actin cytoskeleton beneath the equator of dividing cells
brenda
additional information
-
subcellular localization study of MLCK in embryonic cardiomyocytes, overview
-
brenda
additional information
isozyme MLCK1 is predominantly located in the perijunctional actomyosin ring in villus enterocytes
-
brenda
additional information
-
peripherally in hepatocytes, rarely in cytoplasm
-
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
additional information
-
structure-function analysis of the non-muscle myosin light chain kinase (nmMLCK) isoform by NMR spectroscopy and molecular modeling, overview. The two major nmMLCK splice variants, nmMLCK1 (about 211 kDa) and nmMLCK2 (about 203 kDa), differ by 69 amino acids within exon 11 (partially deleted in nmMLCK2), a stretch that contains the highly phosphorylated Y464 and Y471, suggesting that nmMLCK splice variants are differentially regulated by Tyr phosphorylation. Potential involvement of S147P and P21H SNP sites in nmMLCK1 in phosphorylation-dependent binding of 14-3-3 proteins
malfunction
-
MLCK-deficient mice lack bronchial constrictions in normal and asthmatic airways, while the asthmatic inflammation response is not affected
malfunction
-
MLCK enzyme inhibitors reduce paracellular barrier dysfunction in ischemic porcine ileum. Pharmacological inhibitions of MLCK significantly reduce paracellular permeability and occludin internalization in in vitro anoxia/reoxygenation injury and ex vivo porcine ischemic injury experimental models
malfunction
MLCK depletion modifies voltage-operated Ca2+ channels. KCl- and AVP-induced Ca2+ signals and voltage-activated Ca2+ current are decreased in MLCK-depleted A7r5 cells. MLCK enzyme inhibition leads to a significant inhibition of cytosolic Ca2+ increase (64%) and contraction induced by 50 mM KCl (92%). Phenotype, detailed overview. Voltage-dependent Ca2+ channel gene expression is decreased by MLCK downregulation
malfunction
induced endocytosis is slowed by acute inhibition of MLCK and by downregulation of MLCK via RNA interference while the total amount of vesicle exocytosis and somatic Ca2+channel current does not change with MLCK down-regulation. Downregulation of MLCK prevents depolarization-induced phosphorylation of myosin light chain, an effect shared by blockers of Ca2+ channels and calmodulin. Downregulation of MLCK does not decrease the amount of exocytosis
malfunction
in meiosis I, MLCK inhibition and other myosin perturbations impair spindle migration and first polar body emission. Inhibition of the MEK1/2-MAPK pathway with U0126 leads to reduced levels of phosphorylated myosin-regulatory light chain (pMRLC) and causes a reduction in cortical tension, effects that are mimicked by treatment with the myosin light chain kinase (MLCK) inhibitor ML-7. MAPK or MLCK inhibition induces loss of normal cortical spindle localization or parthenogenetic egg activation. This parthenogenesis is dependent on cytosolic and extracellular calcium and can be rescued by hyperloading eggs with zinc, suggesting that these effects of inhibition of MLCK or the MAPK pathway are linked with dysregulation of ion homeostasis, overview
malfunction
-
non-muscle myosin light chain kinase (nmMLCK) mutations P21H, S147P, and V261A (all located to loops that connect the immunoglobulin-like domains of nmMLCK) alter the enzyme conformation and the N-terminal amino acid sequence of the non-muscle isoform of MLCK and are highly associated with susceptibility to acute lung injury and asthma, especially in individuals of African descent
malfunction
in cultured cardiomyocytes, the knockdown of cMLCK impaired epinephrine-induced activation of sarcomere reassemble and overexpression of cMLCK promoted sarcomere organization. The lack of MLC2 phosphorylation in heart induces reduction in cardiac performance in genetically modified cMLCK knockout mice. Reduced levels of MLC2 phosphorylation induces cardiac dysfunction
malfunction
mutation S140D/S149D attenuates the phosphorylation at Ser140 and Ser149 by PKA and Aurora B kinases
malfunction
in knockout mice, the lack of MLCK-mediated phosphorylation of myosin in tracheal, bronchial, and gastrointestinal smooth muscle cannot be rescued by other kinases
malfunction
MLCK activates myosin Mg-ATPase activity by phosphorylating Thr-18/Ser-19 on the RLC of myosin II, thereby initiating cross-bridge movements of both smooth muscle and non-muscle. MLCK deletion causes enhanced cell protrusion along with a reduction of membrane tension and is rescued by kinase-dead MLCK or five-DFRXXL motif. The deletion of MLCK results in fast cell migration, enhanced protrusion formation, but no alteration of myosin light chain phosphorylation. The mutant cells show reduced membrane tether force and fewer membrane F-actin filaments, as well as a higher average migrating velocity and protrusion compared to wild-type
malfunction
decreasing MLCK activity in 4-dpf cells results in longer edge lifetimes and wider edges. Enzyme inhibition causes no change in the lateral propagation rate, but an increase in edge lifetime, which suggests that MLCK activity regulates edge size by controlling edge lifetime
malfunction
-
mice harboring a deletion of the nmMLCK gene exhibit protection from radiation-induced lung injury, as assessed by attenuated vascular leakage and leukocyte infiltration
malfunction
-
overexpression of enzyme mutants results in the production of multinucleate cells. A kinase-active mutant causes abnormal contraction during cytokinesis
malfunction
-
MLCK depletion modifies voltage-operated Ca2+ channels. KCl- and AVP-induced Ca2+ signals and voltage-activated Ca2+ current are decreased in MLCK-depleted A7r5 cells. MLCK enzyme inhibition leads to a significant inhibition of cytosolic Ca2+ increase (64%) and contraction induced by 50 mM KCl (92%). Phenotype, detailed overview. Voltage-dependent Ca2+ channel gene expression is decreased by MLCK downregulation
-
malfunction
-
in meiosis I, MLCK inhibition and other myosin perturbations impair spindle migration and first polar body emission. Inhibition of the MEK1/2-MAPK pathway with U0126 leads to reduced levels of phosphorylated myosin-regulatory light chain (pMRLC) and causes a reduction in cortical tension, effects that are mimicked by treatment with the myosin light chain kinase (MLCK) inhibitor ML-7. MAPK or MLCK inhibition induces loss of normal cortical spindle localization or parthenogenetic egg activation. This parthenogenesis is dependent on cytosolic and extracellular calcium and can be rescued by hyperloading eggs with zinc, suggesting that these effects of inhibition of MLCK or the MAPK pathway are linked with dysregulation of ion homeostasis, overview
-
malfunction
Mus musculus C57BL/6N/C57BL/6J
-
in cultured cardiomyocytes, the knockdown of cMLCK impaired epinephrine-induced activation of sarcomere reassemble and overexpression of cMLCK promoted sarcomere organization. The lack of MLC2 phosphorylation in heart induces reduction in cardiac performance in genetically modified cMLCK knockout mice. Reduced levels of MLC2 phosphorylation induces cardiac dysfunction
-
malfunction
-
decreasing MLCK activity in 4-dpf cells results in longer edge lifetimes and wider edges. Enzyme inhibition causes no change in the lateral propagation rate, but an increase in edge lifetime, which suggests that MLCK activity regulates edge size by controlling edge lifetime
-
malfunction
-
MLCK enzyme inhibitors reduce paracellular barrier dysfunction in ischemic porcine ileum. Pharmacological inhibitions of MLCK significantly reduce paracellular permeability and occludin internalization in in vitro anoxia/reoxygenation injury and ex vivo porcine ischemic injury experimental models
-
metabolism
MAPK3/1 (ERK1/2, EC 2.7.11.24) and myosin light chain kinase in mammalian eggs affect myosin-II function and regulate the metaphase II state in a calcium- and zinc-dependent manner. Vertebrate eggs are arrested at metaphase of meiosis II, a state classically known as cytostatic factor arrest. Maintenance of this arrest until the time of fertilization and then fertilizationinduced exit from metaphase II are crucial for reproductive success, overview
metabolism
-
MAPK3/1 (ERK1/2, EC 2.7.11.24) and myosin light chain kinase in mammalian eggs affect myosin-II function and regulate the metaphase II state in a calcium- and zinc-dependent manner. Vertebrate eggs are arrested at metaphase of meiosis II, a state classically known as cytostatic factor arrest. Maintenance of this arrest until the time of fertilization and then fertilizationinduced exit from metaphase II are crucial for reproductive success, overview
-
physiological function
-
phosphorylation of myosin light chains by myosin light chain kinase activates endothelial contractile elements and results in a rearrangement of the cytoskeleton
physiological function
-
MLCK phosphorylates myosin regulatory light chain and controls muscle contraction of skeletal muscle, smooth muscle, and cardiac muscle
physiological function
-
myosin light chain kinase acts as a central participant in the contractile signaling module of tonic smooth muscle
physiological function
-
myosin light chain kinase mediates transcellular intravasation of breast cancer cells through the underlying endothelial cells
physiological function
-
myosin light chain kinase (MLCK) has been shown to alter barrier function via regulation of interepithelial tight junctions. Intestinal anoxia/reoxygenation injury disrupts tight junctions barrier function via MLCK activation and myosin light chain phosphorylation, MLC phosphorylation was significantly increased by anoxia/reoxygenation injury. MLCK-induced occludin endocytosis mediates intestinal epithelial barrier dysfunction during anoxia/reoxygenation injury. The perijunctional actomyosin ring contracts in response to myosin light chain (MLC) phosphorylation, primarily by myosin light chain kinase (MLCK) activation. This in turn leads to tight junction opening
physiological function
myosin light chain kinase is required for smooth muscle contraction and regulation of tone in most of the hollow organs of the body. MLCK and the N-terminal 75 residues of MLCK move on actin bundles and stress fibers of smooth muscle cell cytoskeletons by a random one-dimensional diffusion mechanism in a Ca2+/calmodulin- and ATP-dependent manner, modelling, overview. MLCK motion is permitted only if acto-myosin and MLCK-myosin interactions are weak. One-dimensional diffusion of MLCK along actin ensures that diffusion is not rate limiting for phosphorylation, allows MLCK to locate to areas in which myosin is not yet phosphorylated, and allows MLCK to avoid getting stuck on myosins that have already been phosphorylated. Diffusion of MLCK along actin filaments may be an important mechanism for enhancing the rate of smooth muscle myosin phosphorylation in smooth muscle. In the absence of added ATP or Ca2+/calmodulin, the myosin in the stress fibers is dephosphorylated and in a rigor state (no ATP) in which actin and myosin bind strongly
physiological function
stimulation of vascular smooth muscle cells increases cytosolic Ca2+ concentration as a result of Ca2+ entry from the extracellular space through plasma membrane Ca2+ channels and/or Ca2+ release from intracellular stores via the sarcoplasmic reticulum Ca2+ channels. The increase in Ca2+/calmodulin complex activates myosin light chain kinase (MLCK) triggering contraction, which regulates vasoactivity and blood flow
physiological function
myosin light chain kinase (MLCK) facilitates endocytosis of synaptic vesicles at hippocampal boutons through activity-dependent phosphorylation of myosin downstream of Ca2+/calmodulin. MLCK is an important activity-dependent regulator of vesicle recycling in hippocampal neurons, which are critical for learning and memory. MLCK positively regulates vesicle endocytosis at hippocampal boutons. MLCK regulates endocytosis by functioning between Ca2+/calmodulin and myosin
physiological function
MLCK phosphorylates myosin regulatory light chain (MRLC, also known as MYL9), which enables myosin-II organization into bipolar thick filaments
physiological function
-
the MYLK gene encodes the multifunctional enzyme, myosin light chain kinase (MLCK), involved in isoform-specific non-muscle and smooth muscle contraction and regulation of vascular permeability during inflammation. Reversible Ser/Thr and Tyr nmMLCK phosphorylation contributes to differential regulation of enzymatic activity and cellular spatial targeting of the kinase. Inhibition of Tyr phosphatase activities results in significant accumulation of pTyr-containing nmMLCK, increased MLC kinase activity, endothelial cell contraction and barrier dysfunction. nmMLCK regulation by reversible Tyr phosphorylation, overview. The N-terminal SH2 and SH3 domain-binding motifs (including an SH2-binding motif containing phosphorylated Y464) regulate nmMLCK interactions with other cytoskeletal regulatory proteins
physiological function
in cardiac muscle the dominant regulatory mechanism is centered on the thin-filament protein, troponin, where binding of Ca2+ to troponin C induces contraction. MLC2 phosphorylation plays modulatory roles. The spatial gradient of MLC2 phosphorylation from base to apex and from endocardium to epicardium plays a physiological role in producing cardiac torsion and maintaining normal cardiac contraction. MLC2 phosphorylation may influence actin-myosin interactions independent to the actin-bound regulatory proteins. Cardiac myosin light chain kinase (cMLCK) plays an obligatory role in maintaining the phosphorylation levels of regulatory myosin light chain (MLC2), which is thought to be crucial for regulation of cardiac function. The papillary muscle twitch tension induced by electrical field stimulation is smaller in C57BL/6N than C57BL/6J. Phenylephrine has no effect on MLC2v phosphorylation in either strains but increased the twitch tension more potently in C57BL/6J than in C57BL/6N. Calyculin A increased papillary muscle MLC2v phosphorylation to a similar extent in both strains but increased the phenylephrine-induced inotropic response only in C57BL/6N. cMLCK is an indispensable kinase for MLC2 phosphorylation in myocardium
physiological function
MLCK-induced phosphorylation of smooth muscle myosin and MLCK-induced mechanical activation of smooth muscle myosin to move actin filaments, likely by increasing the time the MLCK remains close to the surface-attached myosin
physiological function
high molecular weight myosin light chain kinase is a multifunctional protein involved in myosin II activation and integration of cytoskeletal components in cells, phosphorylation regulates interaction of 210-kDa myosin light chain kinase N-terminal domain with actin cytoskeleton. Phosphorylation at serine residues 140/149 by cAMP-dependent protein kinase (PKA) and Aurora B leads to a decrease in N27-157 binding to actin. Enzyme-cytoskeleton interactions: in non-muscle cells, MLCK210 functions as a cytoskeleton integrator and motility organizer. MLCK210 resides on microfilament bundles via its central high affinity actin binding site, whereas both the N- and C-terminal tails of the molecule are engaged in reversible interaction with other cytoskeletal and motile components of the cell. While MLCK210 resides on actin filaments, its KRPdomain binds to soluble monomeric non-muscle myosin II and facilitates the presentation of myosin II to the catalytic core of the kinase. Phosphorylation of myosin II allows selfassembly of myosin filaments, thereby supporting localized actomyosin motility, modelling
physiological function
phosphorylation of myosin on S19 of the regulatory light chain (also called LC20) activates myosin ATPase activity in the presence of actin, which is necessary and sufficient for muscle contraction. All smooth muscles express two forms of myosin II, SMM (most abundant in adult tissues; includes 4 alternatively spliced variants derived from a single SMM heavy chain gene: 1A, 1B, 2A, and 2B) and NMM (IIA, IIB, and IIC minor). The smooth muscle enzyme prefers the smooth muscle myosin II regulatory light chain to the non-muscle myosin II. Non-muscle myosin IIB may participate in a physiologically relevant pathway for force maintenance in smooth muscle
physiological function
MLCK regulates cell migration not by myosin regulatory light chain phosphorylation but possibly through a membrane tension-based mechanism, which is a distinct regulatory mechanism of protrusion during cell migration. MLCK is not required for myosin phosphorylation in a migrating cell, but negatively controls migration by maintaining membrane tension. A critical role of MLCK in cell migration involves regulating the cell membrane tension and protrusion necessary for migration, thereby stabilizing the membrane skeleton through F-actin-binding activity. MLCK regulates the membrane F-actin skeleton. MLCK regulates cell spreading through 5DFRXXL in a kinase-independent manner
physiological function
keratocytes from 2 d postfertilization (dpf) embryos resemble canonical fanshaped keratocytes, but keratocytes from 4 dpf embryos often form multiple protrusions despite unchanged membrane tension. 4-dpf Cells have multiple protrusions because the protrusions are intrinsically small. The multiple-protrusion phenotype is primarily due to increased myosin light chain kinase (MLCK) expression. MLCK activity influences cell polarity by increasing myosin accumulation in lamellipodia, which locally decreases protrusion lifetime, limiting lamellipodial size and allowing for multiple protrusions to coexist within the context of membrane tension limiting protrusion globally, while Rho kinase regulates myosin accumulation at the cell rear and does not determine protrusion size. MLCK-specific mechanism for controlling cell polarity via regulation of myosin activity in protrusions, overview. Enzyme inhibition causes no change in the lateral propagation rate, but an increase in edge lifetime, which suggests that MLCK activity regulates edge size by controlling edge lifetime
physiological function
-
the enzyme is essential for the increase in intestinal permeability induced by tumor necrosis factor-alpha
physiological function
-
the nonmuscle myosin light chain kinase plays a key role in vascular barrier regulation in radiation-induced lung injury
physiological function
-
lamellipodia contractility regulated by the enzyme is responsible for the intriguing turning behavior of T cells climbing sharp-edged ramp-like structures. The enzyme activity is responsible for the reduction of velocity and turning of T cells encountering ramp-like structures
physiological function
the enzyme maintains correct RhoA localization at the cleavage site, which is necessary for proper RhoA activity and contractile ring dynamics
physiological function
-
the enzyme is required for KIF14 localization to the midbody and cytokinesis
physiological function
-
the enzyme regulates cytokinesis at a step after Rho in the contractile process
physiological function
-
stimulation of vascular smooth muscle cells increases cytosolic Ca2+ concentration as a result of Ca2+ entry from the extracellular space through plasma membrane Ca2+ channels and/or Ca2+ release from intracellular stores via the sarcoplasmic reticulum Ca2+ channels. The increase in Ca2+/calmodulin complex activates myosin light chain kinase (MLCK) triggering contraction, which regulates vasoactivity and blood flow
-
physiological function
-
MLCK phosphorylates myosin regulatory light chain (MRLC, also known as MYL9), which enables myosin-II organization into bipolar thick filaments
-
physiological function
Mus musculus C57BL/6N/C57BL/6J
-
in cardiac muscle the dominant regulatory mechanism is centered on the thin-filament protein, troponin, where binding of Ca2+ to troponin C induces contraction. MLC2 phosphorylation plays modulatory roles. The spatial gradient of MLC2 phosphorylation from base to apex and from endocardium to epicardium plays a physiological role in producing cardiac torsion and maintaining normal cardiac contraction. MLC2 phosphorylation may influence actin-myosin interactions independent to the actin-bound regulatory proteins. Cardiac myosin light chain kinase (cMLCK) plays an obligatory role in maintaining the phosphorylation levels of regulatory myosin light chain (MLC2), which is thought to be crucial for regulation of cardiac function. The papillary muscle twitch tension induced by electrical field stimulation is smaller in C57BL/6N than C57BL/6J. Phenylephrine has no effect on MLC2v phosphorylation in either strains but increased the twitch tension more potently in C57BL/6J than in C57BL/6N. Calyculin A increased papillary muscle MLC2v phosphorylation to a similar extent in both strains but increased the phenylephrine-induced inotropic response only in C57BL/6N. cMLCK is an indispensable kinase for MLC2 phosphorylation in myocardium
-
physiological function
-
keratocytes from 2 d postfertilization (dpf) embryos resemble canonical fanshaped keratocytes, but keratocytes from 4 dpf embryos often form multiple protrusions despite unchanged membrane tension. 4-dpf Cells have multiple protrusions because the protrusions are intrinsically small. The multiple-protrusion phenotype is primarily due to increased myosin light chain kinase (MLCK) expression. MLCK activity influences cell polarity by increasing myosin accumulation in lamellipodia, which locally decreases protrusion lifetime, limiting lamellipodial size and allowing for multiple protrusions to coexist within the context of membrane tension limiting protrusion globally, while Rho kinase regulates myosin accumulation at the cell rear and does not determine protrusion size. MLCK-specific mechanism for controlling cell polarity via regulation of myosin activity in protrusions, overview. Enzyme inhibition causes no change in the lateral propagation rate, but an increase in edge lifetime, which suggests that MLCK activity regulates edge size by controlling edge lifetime
-
physiological function
-
myosin light chain kinase (MLCK) has been shown to alter barrier function via regulation of interepithelial tight junctions. Intestinal anoxia/reoxygenation injury disrupts tight junctions barrier function via MLCK activation and myosin light chain phosphorylation, MLC phosphorylation was significantly increased by anoxia/reoxygenation injury. MLCK-induced occludin endocytosis mediates intestinal epithelial barrier dysfunction during anoxia/reoxygenation injury. The perijunctional actomyosin ring contracts in response to myosin light chain (MLC) phosphorylation, primarily by myosin light chain kinase (MLCK) activation. This in turn leads to tight junction opening
-
Show AA Sequence and Transmembrane Helices (1849 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
130000
150000
152000
155000
190000
210000
214000
34000
94000
additional information
190000
-
x * 190000, recombinant Ca2+/calmodulin-dependent fluorescent biosensor MLCK, SDS-PAGE
190000
-
x * 190000, recombinant enzyme mutant MLCK1745, SDS-PAGE, x * 210000, wild-type enzyme and mutant MLCKATPdel, SDS-PAGE
210000
-
x * 190000, recombinant enzyme mutant MLCK1745, SDS-PAGE, x * 210000, wild-type enzyme and mutant MLCKATPdel, SDS-PAGE
additional information
amino acid sequence of an active fragment of rabbit skeletal muscle myosin light chain kinase
additional information
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amino acid sequence of an active fragment of rabbit skeletal muscle myosin light chain kinase
additional information
amino acid sequence of rabbit skeletal muscle myosin light chain kinase
additional information
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amino acid sequence of rabbit skeletal muscle myosin light chain kinase
additional information
-
different molecular weights may be due to high sensitivity to proteolysis during purification
additional information
-
different molecular weights may be due to high sensitivity to proteolysis during purification
additional information
-
different molecular weights may be due to high sensitivity to proteolysis during purification
additional information
-
different molecular weights may be due to high sensitivity to proteolysis during purification
additional information
-
different molecular weights may be due to high sensitivity to proteolysis during purification
additional information
-
different molecular weights may be due to high sensitivity to proteolysis during purification
additional information
-
different molecular weights may be due to high sensitivity to proteolysis during purification
additional information
-
relative masses of various animal skeletal muscle enzymes
additional information
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relative masses of various animal skeletal muscle enzymes
additional information
-
relative masses of various animal skeletal muscle enzymes
additional information
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relative masses of various animal skeletal muscle enzymes
additional information
-
relative masses of various animal skeletal muscle enzymes
additional information
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relative masses of various animal skeletal muscle enzymes
additional information
-
relative masses of various animal skeletal muscle enzymes
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
additional information
?
-
x * 190000, recombinant Ca2+/calmodulin-dependent fluorescent biosensor MLCK, SDS-PAGE
?
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x * 190000, recombinant enzyme mutant MLCK1745, SDS-PAGE, x * 210000, wild-type enzyme and mutant MLCKATPdel, SDS-PAGE
additional information
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skeletal muscle enzyme structure: overall asymmetric shape, globular head and tail region
additional information
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different molecular weights may be due to high sensitivity to proteolysis during purification
additional information
-
MLCK domain structure, a fusion protein consisting of the N-terminal actin-binding domain, the central catalytic domain, and the C-terminal myosin-binding domain
additional information
-
different molecular weights may be due to high sensitivity to proteolysis during purification
additional information
-
different molecular weights may be due to high sensitivity to proteolysis during purification
additional information
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multienzyme complex with smooth muscle myosin light chain phosphatase
additional information
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skeletal muscle myosin light chain kinases from different species share more identity than skeletal muscle and smooth muscle myosin light chain kinases from the same species
additional information
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skeletal muscle enzyme structure: overall asymmetric shape, globular head and tail region
additional information
-
different molecular weights may be due to high sensitivity to proteolysis during purification
additional information
-
MLCK-210 contains an additional actin-binding domain at the N-terminus
additional information
-
MLCK domain structure, a fusion protein consisting of the Nterminal actin-binding domain, the central catalytic domain, and the C-terminal myosin-binding domain
additional information
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the high molecular weight endothelial enzyme is stably associated to a complex containing p60src and 80000 cortactin
additional information
-
different molecular weights may be due to high sensitivity to proteolysis during purification
additional information
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the endothelial isozyme possesses a catalytic domain including the actin-binding domain and the calmodulin binding domain, like the smooth muscle isozyme, but also a protein-protein interaction domain including SH2 and SH3 domains
additional information
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the endothelial isozyme EC MLCK contains a unique N-terminal sequence which is a target for upregulation by signaling cascade components such as p60src, EC MLCK splice variants doamin structure
additional information
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structure-function analysis of the non-muscle myosin light chain kinase (nmMLCK) isoform by NMR spectroscopy and molecular modeling, overview
additional information
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skeletal muscle enzyme structure: overall asymmetric shape, globular head and tail region
additional information
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different molecular weights may be due to high sensitivity to proteolysis during purification
additional information
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the endothelial isozyme possesses a catalytic domain including the actin-binding domain and the calmodulin binding domain, like the smooth muscle isozyme, but also a protein-protein interaction domain including SH2 and SH3 domains
additional information
the MLCK locus encodes three transcripts from alternative promoters and produces two MLCK isoforms (short MLCK and long MLCK) and a C-terminal Ig module (telokin). Long MLCK (L-MLCK) is identical to short MLCK (S-MLCK) apart from a unique N-terminal extension containing two extra DFRXXL motifs and six Ig modules
additional information
the carboxyl terminus of the smooth muscle myosin light chain kinase is expressed as an independent protein, telokin
additional information
-
gel electrophoresis in various buffers gives different molecular weights
additional information
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skeletal muscle enzyme structure: overall asymmetric shape, globular head and tail region
additional information
-
different molecular weights may be due to high sensitivity to proteolysis during purification
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
phosphoprotein
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protein kinase A phosphorylates MLCK in its regulatory domain at Ser1021 and Ser1034. The kinase activity of MLCK phosphorylated at Ser1021 is reduced, whereas that of MLCK phosphorylated at Ser1034 is not reduced
phosphoprotein
the enzyme is 140fold activated through phosphorylation at Thr166 by a recombinant constitutively active Ca2+/calmodulin-dependent protein kinase kinase, the enzyme performs autophosphorylation at Thr289, subsequent to Thr166 phosphorylation by the protein kinase kinase, and at several serine residues, leading to release of the autoinhibitory domain from the catalytic core, identification of phosphorylation sites
phosphoprotein
-
protein kinase A phosphorylates MLCK in its regulatory domain at Ser815 and Ser828. The kinase activity of MLCK phosphorylated at Ser815 is reduced, whereas that of MLCK phosphorylated at Ser828 is not reduced
phosphoprotein
in vitro, the N-terminal actinbinding domain of MLCK210 is located within residues 27-157 and is phosphorylated by cAMP-dependent protein kinase (PKA) and Aurora B at serine residues 140/149 leading to a decrease in N27-157 binding to actin, leading role of the S149D mutation in attenuation of N27-157 binding to the cytoskeletal structures. In vitro phosphorylation and determination of phosphorylation sites, overview
phosphoprotein
-
diffential phosphorylation by Aurora B on serine residues, e.g. in the enzyme's IgG domain, during interphase and mitosis has regulatory function, phosphorylation sites for Aurora B on the enzyme, overview
phosphoprotein
-
eotaxin induces enzyme phosphorylation by serine/threonine protein kinases e.g. by MAP kinases ERK1/2 and p38 at Thr43, phosphorylation is required for activation of the enzyme
phosphoprotein
-
PAK phosphorylation of MLCK by p21- activated kinase, a kinase activated by the Rho family of GTPases, can inhibit MLCK activity
phosphoprotein
-
reversible Ser/Thr and Tyr nmMLCK phosphorylation contributes to differential regulation of enzymatic activity and cellular spatial targeting of the kinase. cAMP-dependent protein kinase A (PKA)-mediated phosphorylation of nmMLCK exerts paradoxical effects on kinase activity depending on whether the Ser/Thr phosphorylation sites resides within the unique nmMLCK N-terminus, the putative Src homology (SH) 3-binding sequences, or the calcium/calmodulin binding region. Tyr phosphorylation of nmMLCK by pp60src or c-Abl occurs during barrier disruption, during recovery, as well as following exposure to barrier enhancing stimuli. pp60src- or c-Abl-mediated phosphorylation of nmMLCK at Y464 and Y471 increases MLC kinase activity. The two major nmMLCK splice variants, nmMLCK1 (about 211 kDa) and nmMLCK2 (about 203 kDa), differ by 69 amino acids within exon 11 (partially deleted in nmMLCK2), a stretch that contains the highly phosphorylated Y464 and Y471, suggesting that nmMLCK splice variants are differentially regulated by Tyr phosphorylation
phosphoprotein
-
the enzyme is phosphorylated and activated by mitogen activated protein kinase MAPK
phosphoprotein
the cardiac-specific isozyme probably performs also autophosphorylation
phosphoprotein
-
PAK phosphorylation of MLCK by p21- activated kinase, a kinase activated by the Rho family of GTPases, can inhibit MLCK activity
phosphoprotein
-
diffential phosphorylation by Aurora B on serine residues during interphase and mitosis has regulatory function, phosphorylation sites for Aurora B on the enzyme, overview
phosphoprotein
-
PAK phosphorylation of MLCK by p21- activated kinase, a kinase activated by the Rho family of GTPases, can inhibit MLCK activity
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
isolution structure of a calmodulin-target peptide complex by multidimensional NMR
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
S140D/S149D
site-directed mutagenesis of MLCK, the mutation attenuates the phosphorylation at Ser140 and Ser149 by PKA and Aurora B kinases, overview
A27F/A29R/A31R/A32F
-
mutant enzyme with defective ATP binding site, mutant leads to nearly unaltered MLC phosphorylation activity and altered morphology in transfected CV1 cells
H21P
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naturally occuring single nucleotide polymorphism increasing the risk for acute lung injury within 5 das of traumatic insult
P147S
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naturally occuring single nucleotide polymorphism increasing the risk for acute lung injury within 5 das of traumatic insult
P21H
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site-directed mutagenesis, alters the N-terminal amino acid sequence of the non-muscle isoform of MLCK (nmMLCK) and is highly associated with susceptibility to acute lung injury and asthma, especially in individuals of African descent, the mutation causes minimal conformational changes compared to the wild-type enzyme
S147P
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site-directed mutagenesis, alters the N-terminal amino acid sequence of the non-muscle isoform of MLCK (nmMLCK) and is highly associated with susceptibility to acute lung injury and asthma, especially in individuals of African descent, the mutation causes minimal conformational changes compared to the wild-type enzyme
V261A
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site-directed mutagenesis, alters the N-terminal amino acid sequence of the non-muscle isoform of MLCK (nmMLCK) and is highly associated with susceptibility to acute lung injury and asthma, especially in individuals of African descent, the mutation causes minimal conformational changes compared to the wild-type enzyme
T146A
A986P
-
significantly increase in Ca2+ required for half-maximal activity, slightly decreased KM for regulatory light chain
M968P
-
10% Ca2+/calmodulin independent activity of total activity, decreased KM for regulatory light chain
additional information
T146A
a naturally occuring point mutation in strain C57BL/6N, the mutation locates in exon1 of gene Mylk3
T146A
Mus musculus C57BL/6N/C57BL/6J
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a naturally occuring point mutation in strain C57BL/6N, the mutation locates in exon1 of gene Mylk3
-
additional information
an antisense morpholino oligonucleotide is designed to induce mis-splicing of exon 9 of im:7148400 and early termination of the transcript before its kinase domain
additional information
-
an antisense morpholino oligonucleotide is designed to induce mis-splicing of exon 9 of im:7148400 and early termination of the transcript before its kinase domain
additional information
-
an antisense morpholino oligonucleotide is designed to induce mis-splicing of exon 9 of im:7148400 and early termination of the transcript before its kinase domain
-
additional information
-
deletion of DRFXXL motifs leads to a worse binding to actin filaments especially in the presence of Mg2+
additional information
-
downregulation of MLCK in cultured smooth muscle cells reveals that MLC20 phosphorylation is not obligatory for the smooth muscle to contract, overview
additional information
the kinase activity of biotinylated-MLCK is comparable to MLCK without biotinylation using the regulatory light chain as the substrate. Biotinylated-MLCK and biotinylated-MLCK with attached streptavidin tag are able to fully phosphorylate smooth muscle myosin regulatory light chain
additional information
silencing of MLCK1 via specific siRNA increases transepithelial resistance in Caco-2 cells
additional information
-
construction of an enzyme mutant MLCK1745 which lacks the C-terminal amino acids including the autoinhibitory domain, and the myosin- and the calmodulin-binding sites, the MLCK1745 mutation leads to increased growth rates of transfected CV1 fibroblasts and an increase in basal level MLC phosphorylation compared to untransfected cells, stress fiber formation is unaffected by the mutation
additional information
-
construction of an enzyme mutant MLCK1745 which lacks the C-terminal amino acids including the autoinhibitory domain, and the myosin- and the calmodulin-binding sites, the MLCK1745 mutant increases the TNFalpha response to upregulate NFkappaB activity in transfected endothelial cells, MLCKATPdel mutant enzyme with defective ATP binding site inhibits TNFalpha-induced NFkappaB-activation activity in transfected endothelial cells
additional information
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knockdown of cardiac-MLCK by specific siRNAs decreases cardiac-MLCK phosphorylation and impairs epinephrine-induced activation of sarcomere reassembly, knockdown of zcardiac-MLCK expression using morpholino antisense oligonucleotides results in dilated cardiac ventricles and immature sarcomere structures
additional information
expression of a dominant-negative mutant of MLCK inhibits the TRPC5 channel activity, revealing an essential role of MLCK in maintaining TRPC5 channel activity
additional information
expression of a dominant-negative mutant of MLCK inhibits the TRPC5 channel activity, revealing an essential role of MLCK in maintaining TRPC5 channel activity
additional information
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expression of a dominant-negative mutant of MLCK inhibits the TRPC5 channel activity, revealing an essential role of MLCK in maintaining TRPC5 channel activity
additional information
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vascular endothelial overexpression of the human nonmuscle isozyme of myosin light chain kinase-2 renders the transgenic mice susceptible to lipopolysaccharide-induced or mechanical-induced inflammatory lung injury, the homozygous mice show reduced fecundity and litter survival until weaning, as well as initially delayed growth compared to wild-type mice, phenotype and modeling, overview
additional information
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single nucleotide polymorphisms are involved in the risk of sepsis-related acute lung injury and asthma, haplotype analysis, overview
additional information
generation of a fragment comprising the N-terminal 75 residues of MLCK
additional information
-
construction of eMLCK or smMLCK knockout mutant mice by genetic or chemical methods, overview
additional information
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long isozyme MLCK-210-deficient mice display a significantly improved survival with a greatly attenuated microvascular hyperpermeability response to albumin and fluid
additional information
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generation of tamoxifen-inducible and smooth muscle-specific MLCK knockout mutant mice with loss of function and impaired smooth muscle contraction, severe gut dysmotility, phenotype, overview
additional information
generation of enzyme MLCK deletion in intestinal smooth muscle cells, phenotype, overview
additional information
serial carboxy-terminal deletions of the regulatory and catalytic domains are constructed and expressed in COS cells. The truncated kinases have no detectable myosin light chain kinase activity
additional information
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serial carboxy-terminal deletions of the regulatory and catalytic domains are constructed and expressed in COS cells. The truncated kinases have no detectable myosin light chain kinase activity
additional information
-
construction of truncation mutants of long and short MLCKs
additional information
-
construction of transgenic mice that express an skeletal muscle-MLCK, i.e. skMLCK, CaM biosensor in skeletal muscle to determine whether skMLCK or calmodulin is limiting to twitch force potentiation. Three transgenic mouse lines exhibited up to 22-fold increases in skMLCK protein expression in fast-twitch extensor digitorum longus muscle containing type IIa and IIb fibers, with comparable expressions in slow-twitch soleus muscle containing type I and IIa fibers, overview
additional information
MLCK is downregulated by transfection with a small interfering RNA targeting MLCK (MLCK-siRNA) in rat small resistance mesenteric artery and in the rat embryonic aortic cell line A7r5. Expression of long (220 kDa) and short (130 kDa) MLCK is inhibited in MLCK-siRNA-transfected cells. Noradrenaline-induced contraction and Ca2+ signal are significantly depressed in MLCK-siRNA compared to scramble-siRNA-transfected small resistance mesenteric artery. Contraction and Ca2+ signal induced by high KCl and voltage-activated Ca2+ current are also significantly decreased in MLCK-siRNAtransfected resistance mesenteric artery
additional information
knockdown of endogenous MLCK by two shRNA sequences: shMLCK1 is 5-GCTAGATTTGACTGCAAGATT-3' and shMLCK 2 is 5'-ACTGTCCTCTATGGCAATGAT-3'
additional information
-
MLCK is downregulated by transfection with a small interfering RNA targeting MLCK (MLCK-siRNA) in rat small resistance mesenteric artery and in the rat embryonic aortic cell line A7r5. Expression of long (220 kDa) and short (130 kDa) MLCK is inhibited in MLCK-siRNA-transfected cells. Noradrenaline-induced contraction and Ca2+ signal are significantly depressed in MLCK-siRNA compared to scramble-siRNA-transfected small resistance mesenteric artery. Contraction and Ca2+ signal induced by high KCl and voltage-activated Ca2+ current are also significantly decreased in MLCK-siRNAtransfected resistance mesenteric artery
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
protease inhibitors stabilize during purification
protease inhibitors with broad specificity and glycerol stabilize during initial purification, unstable to further purification
-
repeated freeze-thawing decreases activity
unstable upon lyophilization
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
affinity chromatography on calmodulin-Sepharose
calmodulin-Sepharose column chromatography, DEAE 650M Toyopearl column chromatography, and Superose 6 gel filtration
partial
purified to homogeneity from a number of vertebrate muscles and partially purified from non-muscle tissues
recombinant GST-tagged C-terminal enzyme fragment by glutathione affinity chromatography
-
recombinant His-tagged wild-type and mutant isozymes from Escherichia coli strain Bl21(DE3) by nickel affinity chromatograpyh
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recombinant wild-type and mutant enzymes from transfected bovine endothelial cells
-
recombinant wild-type and mutant isozymes nmMLCK1 from Escherichia coli strain BL21(DE3) by chromatography on a chitin column and dialysis
-
purified to homogeneity from a number of vertebrate muscles and partially purified from non-muscle tissues
-
purified to homogeneity from a number of vertebrate muscles and partially purified from non-muscle tissues
-
purified to homogeneity from a number of vertebrate muscles and partially purified from non-muscle tissues
-
purified to homogeneity from a number of vertebrate muscles and partially purified from non-muscle tissues
-
purified to homogeneity from a number of vertebrate muscles and partially purified from non-muscle tissues
-
purified to homogeneity from a number of vertebrate muscles and partially purified from non-muscle tissues
-
purified to homogeneity from a number of vertebrate muscles and partially purified from non-muscle tissues
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, expression analysis in cardiac smooth muscle, overview, expression of HA-tagged MLCK
DNA and amino acid sequence determination and analysis, expressionin HEK-293 cells, co-expression with TRPC5 from Drosophila melanogaster
DNA sequence determination and analysis of splicing variant 1 of long endothelial enzyme, large scale expression of endothelial isozyme MLCK1 in Spodoptera frugiperda Sf9 cells via Baculovirus transfection system
DNA sequence determination and analysis of splicing variant 2 of long endothelial enzyme, large scale expression of endothelial isozyme MLCK2 in Spodoptera frugiperda Sf9 cells via Baculovirus transfection system
DNA sequence determination and analysis, overexpression in Escherichia coli strain XL-1 Blue
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domain organization of chicken gizzard myosin light chain kinase deduced from a cloned cDNA
expressed in Escherichia coli BL21(DE3) cells
expression in A7r5 rat thoracic aorta smooth muscle cells as GFP-fusion protein
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expression of a C-terminal enzyme fragment comprising residues 860-1176 as GST-fusion protein in Escherichia coli strain Bl21(DE3), the GST-tag slightly reduces the activity of the recombinant enzyme fragment compared to the untagged fragment
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expression of calmodulin-independent mutant MLCK1745 and of MLVKATPdel mutant in African green monkey kidney CV1 fibroblasts as V5-epitope- and His-tagged proteins
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expression of calmodulin-independent mutant MLCK1745, lacking the C-terminal part including the autoinhibitory domain, and the myosin- and the calmodulin-binding sites, and of MLVKATPdel mutant with a defective ATP-binding site in bovine pulmonary artery endothelial cells BPAEC as V5-epitope-tagged proteins
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expression of epitope-tagged endothelial isozyme in endothelial cells, expression of GST-fusion isozyme EC MLCK in bacteria, expression of endothelial iszyme EC MLCK and macrophage migration inhibition factor MIF in the yeast two-hybrid system, overview
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expression of His6-tagged MLCK-210 nad His-tagged N452-MLCK in Escherichia coli, expression of GFP-tagged MLCK-210 and GFP-tagged N452-MLCK in CV-1 African green monkey kidney cells
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expression of the long isozyme L-MLCK in murine NIH3T3 cells, expression of GFP-tagged wild-type and mutant isozymes in COS-7 cells and as His-tagged proteins in Escherichia coli strain BL21(DE3)
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expression of wild-type and dominant-negative MLCK in untransformed and Ras-transformed MCF-10A cells
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expression of wild-type full-length MLCK and of several enzyme fragments in Escherichia coli with the use of a cold-shock promoter
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gene Mlck, expression analysis, transgenic expression in mice bladder smooth muscle via adenoviral transfection
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gene Myl12b, analysis of MLCK, L-type (CaV1.2), P/Q-type (CaV2.1), and T-type (CaV3.1) voltage-dependent Ca2+ channels and RPL32 mRNA expression by real-time quantitative-PCR
gene MYLK, DNA and amino acid sequence determination and analysis of wild-type and single nucleotide mutants, genotyping
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gene MYLK, recombinant expression of wild-type and truncated enzyme, the latter comprising the N-terminal 75 residues of MLCK
gene Mylk, the MLCK locus encodes three transcripts from alternative promoters and produces two MLCK isoforms (short MLCK and long MLCK) and a C-terminal Ig module (telokin). Long MLCK (L-MLCK) is identical to short MLCK (S-MLCK) apart from a unique N-terminal extension containing two extra DFRXXL motifs and six Ig modules
gene mylk1, located on chromosome 16, contains at least 31 exons, DNA and amino acid sequence determination and analysis, genetic structure and regulation, the serum response factor myocardin plays a central role in regulating mylk1 gene expression, a highly conserved CArG element within 130-kDa MLCK intron 1 is important for promoter activity binding activation factors like myocardin, homebox proteins, GATA family members, and the thyrotroph embryonic factor, regulation model, overview
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gene Mylk3, two isoforms X1 and isoform X2, DNA and amino acid sequence determination and analysis, sequence comparions
genes MYLK2 and MYLK3, DNA and amino acid sequence determination and analysis, expression analysis in heart
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genes MYLK2 and MYLK3, DNA and amino acid sequence determination and analysis, expression analysis in heart, sequence comparisons
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isolation of cDNA
obscurin-associated kinase, DNA and amino acid sequence determination, sequence and expression analysis and comparison, both the mouse and human obscurinassociated kinase-like transcripts also share a conserved putative translation initiation site, overview. Expression in Escherichia coli strain BL21(DE3)
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recombinant expression of FLAG-tagged N27-157 wild-type or phospho-mutant S140A/S149A constructs in HeLa cells
sequence and expression analysis and comparison, both the mouse and human obscurinassociated kinase-like transcripts also share a conserved putative translation initiation site, overview
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stable expression of a constructed Ca2+/calmodulin-dependent fluorescent biosensor MLCK in HEK-293 cells
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telokin, the carboxyl terminus of the smooth muscle myosin light chain kinase which is expressed as an independent protein
the full-length enzyme as well as a truncated form lacking the putative auto-inhibitory domain are expressed in bacterial cells
transient expression as GFP fusion protein in A7r5, HeLa, NIH3T3 or COS-7 cells
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two major nmMLCK splice variants, nmMLCK1 (about 211 kDa) and nmMLCK2 (about 203 kDa), differ by 69 amino acids within exon 11 (partially deleted in nmMLCK2), a stretch that contains the highly phosphorylated Y464 and Y471. Recombinant expression of wild-type and mutant isozymes nmMLCK1 in Escherichia coli strain BL21(DE3), recombinant expression of Flag-tagged nmMLCK1, recombinant expression of two variants of the 1-494aa segments, wild type (P21-S147-V261)-1-494-biotin and a single SNP (P147)-1-494-biotin
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
0.1 nM androgen R1881 causes a progressive decrease in MLCK mRNA levels which decreases by 70% and 90%, respectively, at 24 and 48 h
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10 ng/ml tumour necrosis factor-alpha causes a significant increase of myosin light chain kinase gene activity, tumour necrosis factor-alpha causes an increase in nuclear factor-kappaB to the nuclear factor-kappaB1 binding motif which presumably leads to the activation of MLCK promoter
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breast cancer cells transiently activate endothelial MLCK at tumor invasion sites
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expression of myosin light chain kinase protein is rapidly increased by angiotensin II
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Lactobacillus rhamnosus alleviates intestinal barrier dysfunction in part by increasing expression of myosin light-chain kinase in vivo
MLCK expression is significantly up-regulated after controlled cortical impact with a maximum 12 h post-injury
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severe burn injury increases intestinal MLCK protein levels 3.6fold after 2h in animals resuscitated with normal saline
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the expression level of the splice variant MLCK1 is significantly increased in actively inflamed tissues of the Crohn's disease and ulcerative colitis patient samples. The splice variant MLCK1 is overexpressed in colonic biopsy specimens of inflammatory bowel disease patients. Treatment with low-dose cytokines tumor necrosis factor-like 1A
the expression levels of splice variant MLCK2 is significantly increased in actively inflamed tissues of the Crohn's disease and ulcerative colitis patient samples. The splice variant MLCK2 is overexpressed in colonic biopsy specimens of inflammatory bowel disease patients. Treatment with low-dose cytokines tumour necrosis factor-like 1A and interferon gamma upregulates isoform MLCK2 transcript
the expression of MLCK is increased in endobronchial biopsies from humans with mild asthma
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thoracic irradiation significantly augments protein expression and enzymatic activity of the nonmuscle isoform of myosin light chain kinase
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tumor necrosis factor-alpha induces an increase in enzyme mRNA expression in intestinal epithelial cells
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Lactobacillus rhamnosus alleviates intestinal barrier dysfunction in part by increasing expression of myosin light-chain kinase in vivo
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Lactobacillus rhamnosus alleviates intestinal barrier dysfunction in part by increasing expression of myosin light-chain kinase in vivo
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
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therapeutic inhibition via specific chemical inhibitors of endothelial isozyme, i.e. 11-(3-chloro-6-immino-6H-pyridazin-1-yl)-undecanoic acid (6-phenyl-pyridazin-3-yl)-amide, represents an important new target for the treatment of inflammatory lung disease with less side effects than other therapies
medicine
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long isozyme MLCK-210 is a potential therapeutic target in the treatment of burn edema
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Release 2026.1 (March 2026)
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