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ATP + myosin heavy chain kinase
ADP + myosin heavy chain kinase phosphate
ATP + AAYKTKKKK
?
-
-
-
?
ATP + AKRVSMMR
ADP + AKRVS(-phosphate)MMR
peptide derived from myosin I heavy chain kinase amino acid residues 4-11, exchange at position 4: Ser to Ala
phophorylation site is Ser8
?
ATP + caldesmon
ADP + caldesmon phosphate
catalytic domain
-
-
?
ATP + casein
ADP + casein phosphate
ATP + GRSARVSTYA
ADP + GRSARVS(-phosphate)TYA
peptide derived from Dictyostelium myosin ID
-
?
ATP + histone 2A
ADP + histone 2A phosphate
-
low activity
-
-
?
ATP + MH1 peptide
ADP + MH1 peeptide phosphate
-
-
-
?
ATP + myelin basic protein
?
-
-
-
?
ATP + myelin basic protein
ADP + myelin basic protein phosphate
catalytic domain
-
-
?
ATP + myosin heavy chain kinase
ADP + myosin heavy chain kinase phosphate
ATP + myosin heavy-chain
ADP + myosin heavy chain phosphate
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
ATP + myosin II heavy chain
ADP + myosin II heavy chain phosphate
ATP + myosin regulatory light chain
ADP + myosin regulatory light chain phosphate
catalytic domain
-
-
?
ATP + peptide LMM58 of heavy chain
?
-
4 mol phosphate per mol, Thr-residues are phosphorylated
-
-
?
ATP + phosvitin
ADP + phosvitin phosphate
-
low activity
-
-
?
ATP + RKKFGESEKTKTKEFL-amide
?
ATP + synthetic peptides
?
ATP + [myosin heavy-chain]
ADP + [myosin heavy-chain] phosphate
ATP + [myosin II heavy-chain]
ADP + [myosin II heavy-chain] phosphate
-
-
-
?
ATP + [myosin-heavy-chain]
ADP + [myosin-heavy-chain]phosphate
ATP + [protein LMM58 heavy chain]
ADP + [protein LMM58 heavy chain] phosphate
-
-
-
-
?
additional information
?
-
ATP + myosin heavy chain kinase
ADP + myosin heavy chain kinase phosphate
intramolecular autophosphorylation
-
?
ATP + myosin heavy chain kinase
ADP + myosin heavy chain kinase phosphate
enzyme incorporates 20 mol phosphate per mol of kinase
-
?
ATP + myosin heavy chain kinase
ADP + myosin heavy chain kinase phosphate
the enzyme contains a cluster of 23 serine and threonine residues at the carboxyterminal end that might be the autophosphorylation domain
-
?
ATP + myosin heavy chain kinase
ADP + myosin heavy chain kinase phosphate
increased activity during chemotaxis
-
?
ATP + casein
ADP + casein phosphate
-
no activity
-
-
?
ATP + casein
ADP + casein phosphate
catalytic domain, low activity
-
-
?
ATP + myosin heavy chain kinase
ADP + myosin heavy chain kinase phosphate
-
intramolecular autophosphorylation
-
?
ATP + myosin heavy chain kinase
ADP + myosin heavy chain kinase phosphate
-
intramolecular autophosphorylation
-
?
ATP + myosin heavy chain kinase
ADP + myosin heavy chain kinase phosphate
-
intramolecular autophosphorylation
-
?
ATP + myosin heavy chain kinase
ADP + myosin heavy chain kinase phosphate
-
intramolecular autophosphorylation
-
?
ATP + myosin heavy chain kinase
ADP + myosin heavy chain kinase phosphate
intramolecular autophosphorylation
-
?
ATP + myosin heavy chain kinase
ADP + myosin heavy chain kinase phosphate
enzyme incorporates 1 mol of phosphate per mol of enzyme
-
-
?
ATP + myosin heavy chain kinase
ADP + myosin heavy chain kinase phosphate
-
4 phosphorylation sites on each heavy chain
-
?
ATP + myosin heavy chain kinase
ADP + myosin heavy chain kinase phosphate
-
enzyme incorporates 2-3 mol phosphate per mol of 130 kDa subunit
-
?
ATP + myosin heavy chain kinase
ADP + myosin heavy chain kinase phosphate
-
leads to activation of the phosphorylation activity towards myosin I
-
?
ATP + myosin heavy chain kinase
ADP + myosin heavy chain kinase phosphate
-
leads to activation of the phosphorylation activity towards myosin I
-
?
ATP + myosin heavy chain kinase
ADP + myosin heavy chain kinase phosphate
-
leads to activation of the phosphorylation activity towards myosin I
-
?
ATP + myosin heavy chain kinase
ADP + myosin heavy chain kinase phosphate
-
leads to activation of the phosphorylation activity towards myosin I
-
?
ATP + myosin heavy-chain
ADP + myosin heavy chain phosphate
-
-
-
?
ATP + myosin heavy-chain
ADP + myosin heavy chain phosphate
role of RasGEF Q in regulating myosin II function through MHCK A, overview
-
-
?
ATP + myosin heavy-chain
ADP + myosin heavy chain phosphate
phosphorylation of myosin takes place at three threonine residues in the tail region by myosin II heavy chain kinases
-
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
-
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
myosin light chains are no substrates
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
myosin light chains are no substrates
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
4 mol phosphate per mol of myosin
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
phosphorylation of residues Thr1833 and Thr2029
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
phosphorylation of residues Thr1833 and Thr2029
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
phosphorylates threonine residues
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
phosphorylates threonine residues
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
phosphorylates threonine residues
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
phosphorylates threonine residues
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
1.9 mol phosphate per mol myosin
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
10 mol phosphate per mol of kinase subunit
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
20 mol phosphate per mol of kinase subunit, kinetics
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
major site of phosphorylation is Ser8
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
bovine muscle myosin is no substrate
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
no substrates are human platelet myosin, ovalbumin and smooth muscle myosin from turkey
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
6-8 mol phosphate per mol of enzyme
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
substrate: myosin ID
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
substrate: myosin ID
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
reaction in regulatory contractile activity in Dictyostelium discoideum
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
involved in regulation of myosin II filament assembly
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
involved in regulation of myosin II filament assembly
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
increased activity during chemotaxis
-
?
ATP + myosin II heavy chain
ADP + myosin II heavy chain phosphate
-
-
-
?
ATP + myosin II heavy chain
ADP + myosin II heavy chain phosphate
-
-
?
ATP + myosin II heavy chain
ADP + myosin II heavy chain phosphate
-
-
-
?
ATP + myosin II heavy chain
ADP + myosin II heavy chain phosphate
-
-
?
ATP + myosin II heavy chain
ADP + myosin II heavy chain phosphate
-
specific isozyme A for the heavy chain of myosin II
-
?
ATP + myosin II heavy chain
ADP + myosin II heavy chain phosphate
-
specific isozyme A for the heavy chain of myosin II
-
?
ATP + myosin II heavy chain
ADP + myosin II heavy chain phosphate
isozyme MHCK B
-
?
ATP + myosin II heavy chain
ADP + myosin II heavy chain phosphate
-
drives filament disassembly in vitro
-
?
ATP + myosin II heavy chain
ADP + myosin II heavy chain phosphate
drives filament disassembly in vitro
-
?
ATP + myosin II heavy chain
ADP + myosin II heavy chain phosphate
catalytic domain
-
?
ATP + myosin II heavy chain
ADP + myosin II heavy chain phosphate
-
phosphorylates primarly threonine residues
-
?
ATP + myosin II heavy chain
ADP + myosin II heavy chain phosphate
phosphorylates primarly threonine residues
-
?
ATP + myosin II heavy chain
ADP + myosin II heavy chain phosphate
involved in regulation of myosin II filament assembly
-
?
ATP + myosin II heavy chain
ADP + myosin II heavy chain phosphate
involved in regulation of myosin II filament assembly
-
?
ATP + myosin II heavy chain
ADP + myosin II heavy chain phosphate
-
key role in regulating myosin localization
-
?
ATP + myosin II heavy chain
ADP + myosin II heavy chain phosphate
key role in regulating myosin localization
-
?
ATP + myosin II heavy chain
ADP + myosin II heavy chain phosphate
the enzymes anterior localization is dynamically regulated during chemotaxis, phagocytosis, and other polarized cell motility events via direct binding to F-actin
-
?
ATP + RKKFGESEKTKTKEFL
?
-
-
-
?
ATP + RKKFGESEKTKTKEFL
?
isozyme MHCK B
-
-
?
ATP + RKKFGESEKTKTKEFL
?
synthetic peptide MH1
-
-
?
ATP + RKKFGESEKTKTKEFL-amide
?
low activity
-
-
?
ATP + RKKFGESEKTKTKEFL-amide
?
catalytic domain
-
-
?
ATP + RKKFGESEKTKTKEFL-amide
?
-
isozyme myosin II heavy chain kinase A
-
-
?
ATP + RKKFGESEKTKTKEFL-amide
?
-
synthetic peptide MH-3
-
-
?
ATP + RKKFGESEKTKTKEFL-amide
?
synthetic peptide MH-3
-
-
?
ATP + synthetic peptides
?
-
-
-
-
?
ATP + synthetic peptides
?
-
peptide MH-3, corresponding to myosin II heavy chain from residues 2020 to 2035 except that Ser-2026 and Thr-2031 have been replaced by alanine
-
-
?
ATP + YAYDTRYRR
?
consensus sequence
-
-
?
ATP + YAYDTRYRR
?
catalytic domain of the enzyme
-
-
?
ATP + [myosin heavy-chain]
ADP + [myosin heavy-chain] phosphate
-
-
-
-
?
ATP + [myosin heavy-chain]
ADP + [myosin heavy-chain] phosphate
-
-
-
?
ATP + [myosin heavy-chain]
ADP + [myosin heavy-chain] phosphate
-
-
-
-
?
ATP + [myosin heavy-chain]
ADP + [myosin heavy-chain] phosphate
-
-
-
?
ATP + [myosin heavy-chain]
ADP + [myosin heavy-chain] phosphate
-
-
-
?
ATP + [myosin heavy-chain]
ADP + [myosin heavy-chain] phosphate
phosphorylation of sites within the MHC alpha-helical, coiled-coil tail by MHCK A
-
-
?
ATP + [myosin-heavy-chain]
ADP + [myosin-heavy-chain]phosphate
-
-
-
?
ATP + [myosin-heavy-chain]
ADP + [myosin-heavy-chain]phosphate
-
-
-
-
?
additional information
?
-
enzyme possesses binding domains for the Ras-related GTP-binding proteins Cdc42 and Rac
-
-
?
additional information
?
-
the Mg2+-ATPase activity of the substrate myosin II is inhibited in vitro by its phosphorylation
-
-
?
additional information
?
-
-
the Mg2+-ATPase activity of the substrate myosin II is inhibited in vitro by its phosphorylation
-
-
?
additional information
?
-
O76739
localization of autophosphorylation sites
-
-
?
additional information
?
-
localization of autophosphorylation sites
-
-
?
additional information
?
-
localization of autophosphorylation sites
-
-
?
additional information
?
-
biochemical mechanism for the spatial regulation of myosin II filament disassembly acts via MHCK A activation by actin
-
-
?
additional information
?
-
-
biochemical mechanism for the spatial regulation of myosin II filament disassembly acts via MHCK A activation by actin
-
-
?
additional information
?
-
C-terminal phosphorylation of myosin heavy chain is required for regulation of myosin II filament assembly, regulation mechanism
-
-
?
additional information
?
-
-
C-terminal phosphorylation of myosin heavy chain is required for regulation of myosin II filament assembly, the 3 isozymes MHCK A, MHCK B, and MHCK C show differential localization patterns in living cells
-
-
?
additional information
?
-
MHCK A performs autophosphorylation
-
-
?
additional information
?
-
-
MHCK A performs autophosphorylation
-
-
?
additional information
?
-
MHCK A contains active RasB, and is the predominant exchange factor for RasB. RasGEF Q can bind to F-actin and has the potential to form complexes with MHCK A, overview
-
-
?
additional information
?
-
-
MHCK A contains active RasB, and is the predominant exchange factor for RasB. RasGEF Q can bind to F-actin and has the potential to form complexes with MHCK A, overview
-
-
?
additional information
?
-
substrate specificity of the MHCK A catalytic domain: a lysine or arginine in the P+1 position on the C-terminal side of the phosphoacceptor threonine, P site, is critical for peptide substrate recognition by MHCK A. Phosphorylation by MHCK A is enhanced 2 to 4fold by basic residues in the P+2, P+3 and P+4 positions, with a strong preference for threonine as the phosphoacceptor amino acid, overview
-
-
?
additional information
?
-
substrate specificity of the MHCK A catalytic domain: a lysine or arginine in the P+1 position on the C-terminal side of the phosphoacceptor threonine, P site, is critical for peptide substrate recognition by MHCK A. Phosphorylation by MHCK A is enhanced 2 to 4fold by basic residues in the P+2, P+3 and P+4 positions, with a strong preference for threonine as the phosphoacceptor amino acid, overview
-
-
?
additional information
?
-
-
substrate specificity of the MHCK A catalytic domain: a lysine or arginine in the P+1 position on the C-terminal side of the phosphoacceptor threonine, P site, is critical for peptide substrate recognition by MHCK A. Phosphorylation by MHCK A is enhanced 2 to 4fold by basic residues in the P+2, P+3 and P+4 positions, with a strong preference for threonine as the phosphoacceptor amino acid, overview
-
-
?
additional information
?
-
substrate specificity of the MHCK B catalytic domain: a lysine or arginine in the P+1 position on the C-terminal side of the phosphoacceptor threonine, P site, is critical for peptide substrate recognition by MHCK B. Phosphorylation by MHCK B is further enhanced 8fold by a basic residue in the P+2 position, strong preference for threonine as the phosphoacceptor amino acid, overview
-
-
?
additional information
?
-
substrate specificity of the MHCK B catalytic domain: a lysine or arginine in the P+1 position on the C-terminal side of the phosphoacceptor threonine, P site, is critical for peptide substrate recognition by MHCK B. Phosphorylation by MHCK B is further enhanced 8fold by a basic residue in the P+2 position, strong preference for threonine as the phosphoacceptor amino acid, overview
-
-
?
additional information
?
-
-
substrate specificity of the MHCK B catalytic domain: a lysine or arginine in the P+1 position on the C-terminal side of the phosphoacceptor threonine, P site, is critical for peptide substrate recognition by MHCK B. Phosphorylation by MHCK B is further enhanced 8fold by a basic residue in the P+2 position, strong preference for threonine as the phosphoacceptor amino acid, overview
-
-
?
additional information
?
-
the enzyme also exhibits ATPase and unspecific Ser/Thr protein kinase activities
-
-
?
additional information
?
-
-
the enzyme also exhibits ATPase and unspecific Ser/Thr protein kinase activities
-
-
?
additional information
?
-
the enzyme performs autophosphorylation at Thr825
-
-
?
additional information
?
-
-
the enzyme performs autophosphorylation at Thr825
-
-
?
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ATP + myosin heavy chain kinase
ADP + myosin heavy chain kinase phosphate
ATP + myosin heavy-chain
ADP + myosin heavy chain phosphate
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
ATP + myosin II heavy chain
ADP + myosin II heavy chain phosphate
ATP + [myosin heavy-chain]
ADP + [myosin heavy-chain] phosphate
ATP + [myosin II heavy-chain]
ADP + [myosin II heavy-chain] phosphate
-
-
-
?
ATP + [myosin-heavy-chain]
ADP + [myosin-heavy-chain]phosphate
additional information
?
-
ATP + myosin heavy chain kinase
ADP + myosin heavy chain kinase phosphate
intramolecular autophosphorylation
-
?
ATP + myosin heavy chain kinase
ADP + myosin heavy chain kinase phosphate
increased activity during chemotaxis
-
?
ATP + myosin heavy-chain
ADP + myosin heavy chain phosphate
-
-
-
?
ATP + myosin heavy-chain
ADP + myosin heavy chain phosphate
role of RasGEF Q in regulating myosin II function through MHCK A, overview
-
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
-
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
reaction in regulatory contractile activity in Dictyostelium discoideum
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
involved in regulation of myosin II filament assembly
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
involved in regulation of myosin II filament assembly
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
increased activity during chemotaxis
-
?
ATP + myosin II heavy chain
ADP + myosin II heavy chain phosphate
-
-
-
?
ATP + myosin II heavy chain
ADP + myosin II heavy chain phosphate
-
-
-
?
ATP + myosin II heavy chain
ADP + myosin II heavy chain phosphate
-
-
?
ATP + myosin II heavy chain
ADP + myosin II heavy chain phosphate
involved in regulation of myosin II filament assembly
-
?
ATP + myosin II heavy chain
ADP + myosin II heavy chain phosphate
involved in regulation of myosin II filament assembly
-
?
ATP + myosin II heavy chain
ADP + myosin II heavy chain phosphate
-
key role in regulating myosin localization
-
?
ATP + myosin II heavy chain
ADP + myosin II heavy chain phosphate
key role in regulating myosin localization
-
?
ATP + myosin II heavy chain
ADP + myosin II heavy chain phosphate
the enzymes anterior localization is dynamically regulated during chemotaxis, phagocytosis, and other polarized cell motility events via direct binding to F-actin
-
?
ATP + [myosin heavy-chain]
ADP + [myosin heavy-chain] phosphate
-
-
-
?
ATP + [myosin heavy-chain]
ADP + [myosin heavy-chain] phosphate
-
-
-
-
?
ATP + [myosin heavy-chain]
ADP + [myosin heavy-chain] phosphate
-
-
-
?
ATP + [myosin heavy-chain]
ADP + [myosin heavy-chain] phosphate
-
-
-
?
ATP + [myosin-heavy-chain]
ADP + [myosin-heavy-chain]phosphate
-
-
-
?
ATP + [myosin-heavy-chain]
ADP + [myosin-heavy-chain]phosphate
-
-
-
-
?
additional information
?
-
biochemical mechanism for the spatial regulation of myosin II filament disassembly acts via MHCK A activation by actin
-
-
?
additional information
?
-
-
biochemical mechanism for the spatial regulation of myosin II filament disassembly acts via MHCK A activation by actin
-
-
?
additional information
?
-
C-terminal phosphorylation of myosin heavy chain is required for regulation of myosin II filament assembly, regulation mechanism
-
-
?
additional information
?
-
-
C-terminal phosphorylation of myosin heavy chain is required for regulation of myosin II filament assembly, the 3 isozymes MHCK A, MHCK B, and MHCK C show differential localization patterns in living cells
-
-
?
additional information
?
-
MHCK A contains active RasB, and is the predominant exchange factor for RasB. RasGEF Q can bind to F-actin and has the potential to form complexes with MHCK A, overview
-
-
?
additional information
?
-
-
MHCK A contains active RasB, and is the predominant exchange factor for RasB. RasGEF Q can bind to F-actin and has the potential to form complexes with MHCK A, overview
-
-
?
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C800A
catalytic domain mutation, no remaining activity when expressed as full length enzyme or as catalytic domain only in a deficient Dictyostelium discoideum cell line
D766A
site-directed mutagenesis of the central active site residue, inactive mutant
D766E
site-directed mutagenesis of the central active site residue, inactive mutant
E713A
the mutant shows about 10% activity compared to the wild type enzyme
E713D
the mutant shows about 3% activity compared to the wild type enzyme
K645A
site-directed mutagenesis of an alpha-kinase domain residue, the mutant shows 98.5% reduced activity compared to the wild-type enzyme
K645R
the mutant shows about 3% activity compared to the wild type enzyme
K722N
the mutant shows about 20% activity compared to the wild type enzyme
L716S
the mutant shows about 1% activity compared to the wild type enzyme
Q758A
the mutant shows about 3% activity compared to the wild type enzyme
Q768A
the mutant shows about 70% activity compared to the wild type enzyme
Q822R/Q823R/T825S
site-directed mutagenesis
R592A
site-directed mutagenesis of an alpha-kinase domain residue, the mutant shows 92% reduced activity compared to the wild-type enzyme
R592L
the mutant shows about 30% activity compared to the wild type enzyme
T825A
site-directed mutagenesis
T825E
site-directed mutagenesis
T825S
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
D663A
inactive
D663A
the mutant shows about 3% activity compared to the wild type enzyme
D766S
inactive
D766S
site-directed mutagenesis of the central active site residue, inactive mutant
additional information
-
construction of single, double, and triple MHCK knockout cell lines concerning the 3 isozymes MHCK A, MHCK B, and MHCK C, the mutant cells defects in cytokinesis and myosin II overassembly increasing with the number of mutations, overview
additional information
the truncation mutant DELTAcoil-MHCK A comprising residues 1-498 is not affected in its autophosphorylation rate by F-actin
additional information
the truncation mutant DELTAcoil-MHCK A comprising residues 1-498 is not affected in its autophosphorylation rate by F-actin
additional information
-
the truncation mutant DELTAcoil-MHCK A comprising residues 1-498 is not affected in its autophosphorylation rate by F-actin
additional information
overexpression of the RasGEF Q GEF domain activates RasB, causes enhanced recruitment of MHCK A to the cortex, and leads to cytokinesis defects in suspension phenocopying cells expressing constitutively active RasB, and myosin-null mutants, phenotype, overview. Cells overexpressing the GEF domain show at least 2fold higher levels of MHCK A associated with the cytoskeletal fractions
additional information
-
overexpression of the RasGEF Q GEF domain activates RasB, causes enhanced recruitment of MHCK A to the cortex, and leads to cytokinesis defects in suspension phenocopying cells expressing constitutively active RasB, and myosin-null mutants, phenotype, overview. Cells overexpressing the GEF domain show at least 2fold higher levels of MHCK A associated with the cytoskeletal fractions
additional information
version with deleted WD repeat domain: unable to phosphorylate myosin heavy chain to a significant level, phosphorylates MH-1 peptide
additional information
-
version with deleted WD repeat domain: unable to phosphorylate myosin heavy chain to a significant level, phosphorylates MH-1 peptide
additional information
generation of a DELTA809 truncation mutant, phosphothreonine and the QQG(p)TMVMPD peptide restore the phosphorylation and also the ATPase activity of the mutant alpha-kinade domain, but mutations R734A and D762A abolish the ability of phosphothreonine to activate mutant alpha-kinase domain DELTA809
additional information
-
generation of a DELTA809 truncation mutant, phosphothreonine and the QQG(p)TMVMPD peptide restore the phosphorylation and also the ATPase activity of the mutant alpha-kinade domain, but mutations R734A and D762A abolish the ability of phosphothreonine to activate mutant alpha-kinase domain DELTA809
additional information
generation of the MHCKB truncation lacking only the WD-repeat domain and of a mutant lacking the N-rich region. Cells overexpressing the MHCK mutant lacking only the WD-repeat domain exhibit cytokinesis defects and decreased myosin II assembly
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