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

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 2.7.11.14 - rhodopsin kinase and Organism(s) Bos taurus and UniProt Accession P28327

for references in articles please use BRENDA:EC2.7.11.14
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
Requires G-protein for activation and therefore belongs to the family of G-protein-dependent receptor kinases (GRKs). Acts on the bleached or activated form of rhodopsin; also phosphorylates the beta-adrenergic receptor, but more slowly. Does not act on casein, histones or phosphvitin. Inhibited by Zn2+ and digitonin (cf. EC 2.7.11.15, beta-adrenergic-receptor kinase and EC 2.7.11.16, G-protein-coupled receptor kinase).
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Bos taurus
UNIPROT: P28327
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
hide
The taxonomic range for the selected organisms is: Bos taurus
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
hide
ATP
+
rhodopsin
=
ADP
+
phosphorhodopsin
+
=
+
Synonyms
rk, rhodopsin kinase, g protein-coupled receptor kinase, g-protein receptor kinase, g-protein coupled receptor kinase, g protein-coupled receptor kinase 1, gprk1, g-protein coupled receptor kinase 1, g-protein-coupled receptor kinase 1, g-protein receptor kinase-1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
G protein-coupled receptor kinase 1
-
G-protein coupled receptor kinase 1
-
GPCR kinase 1
-
rhodopsin kinase
-
G protein-coupled receptor kinase 1
-
-
-
-
GPCR kinase 1
-
-
-
-
kinase (phosphorylating), opsin
-
-
-
-
kinase (phosphorylating), rhodopsin
-
-
-
-
opsin kinase
-
-
-
-
rhodopsin kinase
-
-
RK
-
-
-
-
additional information
GRK1 is the founding member of the G protein-coupled receptor kinase, GRK kinase, family
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + rhodopsin = ADP + phosphorhodopsin
show the reaction diagram
mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:rhodopsin phosphotransferase
Requires G-protein for activation and therefore belongs to the family of G-protein-dependent receptor kinases (GRKs). Acts on the bleached or activated form of rhodopsin; also phosphorylates the beta-adrenergic receptor, but more slowly. Does not act on casein, histones or phosphvitin. Inhibited by Zn2+ and digitonin (cf. EC 2.7.11.15, beta-adrenergic-receptor kinase and EC 2.7.11.16, G-protein-coupled receptor kinase).
CAS REGISTRY NUMBER
COMMENTARY hide
54004-64-7
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + protein
ADP + phosphoprotein
show the reaction diagram
autophosphorylation
-
-
?
ATP + rhodopsin
ADP + phosphorhodopsin
show the reaction diagram
ATP + rhodopsin
ADP + phosphorylated rhodopsin
show the reaction diagram
light-dependent deactivation of rhodopsin involves receptor phosphorylation that is mediated by the highly specific protein kinases rhodopsin kinase
-
-
?
ATP + rhodopsin TM5
ADP + phosphorhodopsin TM5
show the reaction diagram
-
-
-
?
ATP + 11-cis-retinal-rhodopsin
ADP + 11-cis-retinal-phosphorhodopsin
show the reaction diagram
-
-
-
-
?
ATP + 13-cis-retinal-rhodopsin
ADP + 13-cis-retinal-phosphorhodopsin
show the reaction diagram
-
-
-
-
?
ATP + 338-SKTETSQVAPA-348
?
show the reaction diagram
ATP + 9-cis-retinal-rhodopsin
ADP + 9-cis-retinal-phosphorhodopsin
show the reaction diagram
-
-
-
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
show the reaction diagram
-
phosphorylates rhodopsin better than betaAR
-
-
?
ATP + DDEASTTVSKTETSQVARRR
?
show the reaction diagram
-
synthetic peptide C, very poor substrate
-
-
?
ATP + peptide
ADP + phosphopeptide
show the reaction diagram
ATP + rhodopsin
ADP + phosphorhodopsin
show the reaction diagram
ATP + rhodopsin
ADP + phosphorylated rhodopsin
show the reaction diagram
-
-
-
-
?
ATPgammaS + rhodopsin
?
show the reaction diagram
-
ATPgammaS is a good substrate, 2-3 mol phosphate/mol rhodopsin
-
-
?
GTP + rhodopsin
GDP + phosphorhodopsin
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + rhodopsin
ADP + phosphorhodopsin
show the reaction diagram
ATP + rhodopsin
ADP + phosphorylated rhodopsin
show the reaction diagram
light-dependent deactivation of rhodopsin involves receptor phosphorylation that is mediated by the highly specific protein kinases rhodopsin kinase
-
-
?
ATP + rhodopsin TM5
ADP + phosphorhodopsin TM5
show the reaction diagram
-
-
-
?
ATP + rhodopsin
ADP + phosphorhodopsin
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
Ca2+ controls the binding of recoverin to the enzyme
additional information
-
Ca2+-independent phosphorylation of rhodopsin
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-(6-Amino-9H-purin-9-yl)-1-deoxy-N-ethyl-beta-D-furanuronamide
-
good inhibitor
2',3'-dideoxyadenosine
-
-
2-chloroadenosine
-
-
3'-deoxyadenosine
-
-
5'-(N-ethylcarbamoyl)adenosine
-
-
5'-AMP
5'-deoxyadenosine
-
-
5'-[p-(fluorosulfonyl)benzoyl]adenosine
-
pseudo-first-order kinetics, MgATP and ATP protect almost completely, rhodopsin only slightly, Mg2+ not at all
5,6-Dichloro-1-(beta-ribofuranosyl)-benzimidazole
-
-
8,2'-Anhydro-8-mercapto-9-(beta-D-arabinofuranosyl)adenine
-
weak
8,3'-Anhydro-8-oxy-9-(beta-D-xylofuranosyl)adenine
-
good inhibitor
8,5'-Anhydro-8-oxy-9-(beta-D-ribofuranosyl)adenine
-
-
8-Bromoadenosine
-
good inhibitor
adenine
-
-
adenosine
adenosine 5'-monosulfate
-
-
ADPbetaS
-
-
AMPS
-
-
ATP-analogues
-
weak or no inhibition, overview
ATPalphaS
-
S-isomer
Ca2+
-
at concentrations equal to Mg2+, forms an unproductive Ca-ATP complex, Mg2+ partially reverses
Calmodulin
cAMP
-
weak
chelator
-
-
-
D-myo-Inositol 1-phosphate
-
weak, above 0.1 mM, stimulates below
dibutyryl-cAMP
-
weak, not in the dark
Digitonin
diphosphate
-
-
EDTA
-
-
emulphogene
Formycin monophosphate
-
-
heparin
-
modest inhibition
inositol triphosphate
-
weak
isoquinoline derivative
-
-
-
K+
-
weak, only at high concentrations
nucleoside analogue
-
overview
papaverine
-
weak, not in the dark
Peptides from cytosolic surface of rhodopsin
-
-
-
Phosphodiesterase inhibitor SQ 20009
-
light-dependent
polyanion
-
-
-
purine nucleotide
-
overview
-
pyrrolopyrimidine derivative
-
preferentially in anti-configuration, strong
-
recoverin
-
Sangivamycin
-
strong, in vivo and in vitro
Synthetic peptide
-
corresponding to sequences within opsin loops 3-4 and 5-6 and the C-terminus, bleached rhodopsin as substrate
-
theophylline
-
light-dependent
Toyocamycin
-
strong
Triphosphate
-
-
tubercidin 5'-phosphate
-
good inhibitor
Zn2+
-
1 mM, 90% inhibition
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
D-myo-Inositol 1-phosphate
-
about 20% activation, between 0.0003 mM and 0.1 mM, slightly inhibitory at higher concentrations
mastoparan
polycation
-
activates approximately 2fold
-
rhodopsin
spermidine
-
slight stimulation
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0015 - 0.0067
rhodopsin
0.0016 - 0.166
ATP
0.027
ATPgammaS
-
pH 7.5, 30°C
7.1
DDEASTTVSKTETSQVARRR
-
pH 7.5, 30°C, peptide C
0.4 - 1
GTP
0.00062 - 30
rhodopsin
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
ATP: 2.2 mol of phosphate bound/min, GTP: 0.12 mol of phosphate bound/min
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.016
1-(6-Amino-9H-purin-9-yl)-1-deoxy-N-ethyl-beta-D-furanuronamide
-
pH 7.5, 30°C
0.065
2',3'-dideoxyadenosine
-
pH 7.5, 25°C
0.016
3'-deoxyadenosine
-
pH 7.5, 25°C
0.005
5'-AMP
0.01
5'-deoxyadenosine
-
pH 7.5, 25°C
0.9
5'-[p-(fluorosulfonyl)benzoyl]adenosine
-
pH 7.5, 25°C
0.004
5,6-Dichloro-1-(beta-ribofuranosyl)-benzimidazole
-
pH 7.5, 30°C
0.52
8,2'-Anhydro-8-mercapto-9-(beta-D-arabinofuranosyl)adenine
-
pH 7.5, 30°C
0.01
8,3'-Anhydro-8-oxy-9-(beta-D-xylofuranosyl)adenine
-
pH 7.5, 30°C
0.027
8,5'-Anhydro-8-oxy-9-(beta-D-ribofuranosyl)adenine
-
pH 7.5, 30°C
0.02
8-Bromoadenosine
-
pH 7.5, 30°C
0.0087
adenine
-
pH 7.5, 30°C
0.004
adenosine
0.08
adenosine 5'-monosulfate
-
pH 7.5, 25°C
0.012
ADP
0.022
ADPbetaS
-
pH 7.5, 30°C
0.022
AMPS
-
pH 7.5, 30°C
0.035
ATPalphaS
-
pH 7.5, 30°C, S-isomer
0.024
diphosphate
-
pH 7.5, 30°C
0.036
Formycin monophosphate
-
pH 7.5, 30°C
0.3
heparin
-
pH 7.5, 30°C
0.00018
Sangivamycin
-
pH 7.5, 30°C
0.014
Triphosphate
-
pH 7.5, 30°C
0.0036
tubercidin 5'-phosphate
-
pH 7.5, 30°C
additional information
additional information
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.01
-
pH 7.4
0.013
-
-
0.017
-
pH 7.4, 37°C
0.026 - 0.033
0.028
-
pH 7.4, 37°C
0.04
-
pH 7.4, 30°C, recombinant RK expressed in COS-1 cells, purified in absence or presence of ATP
0.062
-
pH 7.5, 23°C
0.097
-
pH 7.5, 30°C
0.1 - 0.7
-
-
0.18 - 0.55
-
32°C
0.5 - 0.85
0.555
pH 7.5
0.96
-
pH 7.5, 25°C
1.2
-
recombinant RK expressed in SF9 cells
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 8
-
-
6.5
-
recombinant RK expressed in Sf21 cells
6.67
-
RK from rod outer segments
7.2
-
assay at
8.5
-
assay at, synthetic peptide substrates
additional information
-
activity/pH-profile with synthetic peptide 327-347 as substrate
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.3 - 8.7
-
pH 6.3: about 75% of maximal activity, pH 8.7: about half-maximal activity
6.67
-
RK from rod outer segments: 60% of activity is lost with one pH unit change, recombinant RK expressed in COS-1 cells shows broader activity profile
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
assay at
30
assay at
23
-
assay at
32
-
assay at
36
-
about, native RK and recombinant RK expressed in Sf21 cells
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
rod membranes
Manually annotated by BRENDA team
-
cytosolic protein
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
GRK1_BOVIN
561
0
62934
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
62900
x * 62900, calculated from the amino acid sequence
50000
-
1 * 50000, SDS-PAGE
53000
-
gel filtration
62000
64000
65000
66000
67000
-
gel filtration
68000
-
sucrose density gradient centrifugation
70000
-
1 * 70000, SDS-PAGE
additional information
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 62900, calculated from the amino acid sequence
dimer
wild-type, crystal structure
monomer
mutant L166K, crystal structure
monomer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
enzyme is autophosphorylated
lipoprotein
-
the enzyme is myristoylated in a Ca2+-dependent manner
phosphoprotein
side-chain modification
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme, X-ray diffraction structure determination and analysis, molecular replacement
the structure of GRK1-L166K is determined in complex with Mg2+-ATP to 2.5 A resolution. GRK1-L166K crystallizes in a novel space group as a monomer and exhibits little overall conformational difference from wild-type GRK1
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D164A
site-directed mutagenesis, a dimer interface mutant showing only slightly altered kinetics compared to the wild-type enzyme
D164A/L166K
site-directed mutagenesis, a dimer interface mutant showing reduced activity compared to the wild-type enzyme
D164A/W531A
site-directed mutagenesis, inactive mutant
L116K
L166K mutation disrupts dimer interface. The structure of GRK1-L166K is determined in complex with Mg2+-ATP to 2.5 A resolution. GRK1-L166K crystallizes in a novel space group as a monomer and exhibits little overall conformational difference from wild-type GRK1
L166K
site-directed mutagenesis, a dimer interface mutant showing reduced activity compared to the wild-type enzyme
L166K/W531A
site-directed mutagenesis, inactive mutant
S5A
site-directed mutagenesis, an N-terminal mutant showing reduced activity compared to the wild-type enzyme
S5D
site-directed mutagenesis, inactive mutant
T8A
site-directed mutagenesis, an N-terminal mutant showing reduced activity compared to the wild-type enzyme
T8D
site-directed mutagenesis, inactive mutant
T8E
site-directed mutagenesis, an N-terminal mutant showing reduced activity compared to the wild-type enzyme
W531A
site-directed mutagenesis, inactive mutant
A11R
-
site-directed mutagenesis, the mutation of the residues leads to alterd binding of recoverin to the N-terminal fragment compared to the wild-type enzyme, kinetics constant, overview
C588S
-
unprenylated mutant
D2A
-
site-directed mutagenesis, the mutation of the residues leads to alterd binding of recoverin to the N-terminal fragment compared to the wild-type enzyme, kinetics constant, overview
DELTA1-102
-
deletion fragment containing the first 102 amino acids interacts with calmodulin
DELTA1-25
-
recoverin interacts with the rhodopsin fragment containing the first 25 amino acids of the enzyme. Calmodulin does not interact with this fragment
DELTA102-183
-
deletion fragment containing only amino acids 102-183 shows a very high interaction with calmodulin
DELTA20-535
-
deletion of 19 N-terminal amino acids results in increased flexibility in the active site and interdomain contacts of this enzyme: peptides that directly interact with ATP are not as highly stabilized by adding Mg2+-ATP, and dynamics are greater in the interface between the large lobe of the kinase domain and the regulator of the G protein signaling homology domain compared to wild-type
E7A
-
site-directed mutagenesis, the mutation of the residues leads to alterd binding of recoverin to the N-terminal fragment compared to the wild-type enzyme, kinetics constant, overview
F15A
-
site-directed mutagenesis, the mutation of the residues leads to alterd binding of recoverin to the N-terminal fragment compared to the wild-type enzyme, kinetics constant, overview
F3A
-
site-directed mutagenesis, the mutation of the residues leads to alterd binding of recoverin to the N-terminal fragment compared to the wild-type enzyme, kinetics constant, overview
G4A
-
site-directed mutagenesis, the mutation of the residues leads to alterd binding of recoverin to the N-terminal fragment compared to the wild-type enzyme, kinetics constant, overview
K491A
-
mutant is unable to phosphorylate acidic peptides, residue participates in substrate binding
L6A
-
site-directed mutagenesis, the mutation of the residues leads to alterd binding of recoverin to the N-terminal fragment compared to the wild-type enzyme, kinetics constant, overview
N12A
-
site-directed mutagenesis, the mutation of the residues leads to alterd binding of recoverin to the N-terminal fragment compared to the wild-type enzyme, kinetics constant, overview
S13A
-
site-directed mutagenesis, the mutation of the residues leads to alterd binding of recoverin to the N-terminal fragment compared to the wild-type enzyme, kinetics constant, overview
S488A
S488D
S489A
-
autophosphorylation site mutant with increased activity for the phosphorylation of rhodopsin in the dark
S5A
-
site-directed mutagenesis, the mutation of the residues leads to alterd binding of recoverin to the N-terminal fragment compared to the wild-type enzyme, kinetics constant, overview
T489A
T489D
T8A
-
site-directed mutagenesis, the mutation of the residues leads to alterd binding of recoverin to the N-terminal fragment compared to the wild-type enzyme, kinetics constant, overview
V10A
-
site-directed mutagenesis, the mutation of the residues leads to alterd binding of recoverin to the N-terminal fragment compared to the wild-type enzyme, kinetics constant, overview
V9A
-
site-directed mutagenesis, the mutation of the residues leads to alterd binding of recoverin to the N-terminal fragment compared to the wild-type enzyme, kinetics constant, overview
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
dilution inactivates
-
freezing at liquid N2 temperatures or -20°C, in water or inositol leads to 80% loss of activity, in sucrose to 20% loss of activity
-
glycerol does not protect against inactivation during purification
-
instability of enzyme, protease inhibitors stabilize during purification
-
monovalent cations, e.g. K+ or NH4+, and 15% glycerol stabilize to some extent
-
stable in 6 mM dodecyl maltoside for at least 15 min
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ethanol
-
marked sensitivity to organic solvents, e.g. 5% ethanol reduces the activity by 45% within 2-3 min
urea
-
5 M, almost complete denaturation of enzyme
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 20% adonitol, several months, stable
-
-20°C, kinase solution, solid sucrose, initially loses 30% of activity, stable to further storage
-
-70°C, several months, stable
-
0°C, 20 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane, 2 mM MgCl2, 0.1 mM EDTA, 1 mM dithiothreitol, pH 7.4, 280 mM NaCl, 0.004% Tween 80, 1 mM benzamidine, 0.1 mM phenylmethanesulfonylfluoride, 5 days, 10% loss of activity
-
3°C, 0.1 M KCl, 1 week, 50% loss of activity
-
4°C, crude extract, t1/2: 30 days, highly purified enzyme, t1/2: 3-5 h
-
4°C, highly unstable, partially purified preparation, within 4-5 days, 90% loss of activity, mixture of protease inhibitors stabilizes for several weeks
-
on ice, RK mutants, 2 days, stable
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
glutathione-Sepharose column chromatography
recombinant His-tagged wild-type and mutant enzymes from High Five insect cells by nickel affinity chromatography and ion exchange chromatography
using Ni-NTA chromatography
1055fold, to near homogeneity
-
87-110fold
-
native and recombinant RK purified from baculovirus-infected Sf21 cells: 63fold
-
native and recombinant RK, expressed in SF9 cells, recovering affinity chromatography
-
native RK, recombinant RK and mutants expressed in COS-7 cells
-
partially by isolation of the rod outer segment membrane, partial solubilization by Triton X-100 in presence of Ca2+
-
recombinant GST-tagged enzyme peptide fragments by glutathione affinity chromatography and gel filtration, recombinant His6-tagged truncation mutant 32–562 from Escherichia coli by nickel affinity chromatography and gel filtration, recombinant enzyme N-terminal fragment from Spodoptera frugiperda Sf9 cells by recoverin affinity chromatography and gel filtration to homogeneity
-
recombinant His-tagged enzyme fragment RK25 from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
recombinant RK expressed in SF9 cells
-
recombinant RK purified from baculovirus-infected Sf21 cells
-
recombinant RK with N-terminal hexahistidine tag, expressed in Pichia pastoris GS115, COS-1 cells: 210-222fold, and HEK-293 cell line
-
using Ni-NTA chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
a peptide containing the first 25 amino acids of GRK1 (MDFGSLETVVANSAFIAARGSFDAS) plus GST-tag is expressed in Escherichia coli BL21 cells
cDNA encoding enzyme is cloned and expressed in COS-7 cells, sequence of the 561 amino acids protein
expressed in Escherichia coli as a His-tagged fusion protein
expression of His6-tagged wild-type and mutant enzymes in High Five insect cells using the baculovirus transfection system
cDNA encoding RK is characterized and sequenced, 561 amino acids protein
-
expressed as a GST-fusion protein
-
expressed in Escherichia coli as a His-tagged fusion protein
-
expression of functional residues 1-25 of the enzyme as His-tagged peptide RK25 in Escherichia coli strain BL21(DE3)
-
expression of GST-tagged enzyme peptide fragments, expression of residues 1–562 of rhodopsin kinase in Spodoptera frugiperda Sf9 cells, expression of the truncation mutant comprising residues 32–562 in Escherichia coli as C-terminally His6-tagged protein
-
expression of RK and mutants in COS-7 cells
-
RK gene expression in baculovirus-infected Sf21 cells
-
RK gene is cloned and expressed in Pichia pastoris GS115, COS-1 cells and HEK-293 stable cell line, best in COS-1 cells with correct posttranslational modifications
-
RK is cloned and expressed in SF9 cells
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lorenz, W.; Inglese, J.; Palczewski, K.; Onorato, J.J.; Caron, M.G.; Lefkowitz, R.J.
The receptor kinase family: primary structure of rhodopsin kinase reveals similarities to the beta-adrenergic receptor kinase
Proc. Natl. Acad. Sci. USA
88
8715-8719
1991
Bos taurus, Bos taurus (P28327)
Manually annotated by BRENDA team
Palczewski, K.; Buczylko, J.; Van Hooser, P.; Carr, S.A.; Huddleston, M.J.; Crabb, J.W.
Identification of the autophosphorylation sites in rhodopsin kinase
J. Biol. Chem.
267
18991-18998
1992
Bos taurus, Bos taurus (P28327)
Manually annotated by BRENDA team
Weller, M.; Virmaux, N.; Mandel, P.
Light-stimulated phosphorylation of rhodopsin in the retina: the presence of a protein kinase that is specific for photobleached rhodopsin
Proc. Natl. Acad. Sci. USA
72
381-385
1975
Bos taurus
Manually annotated by BRENDA team
Shichi, H.; Somers, R.L.
Light-dependent phosphorylation of rhodopsin. Purification and properties of rhodopsin kinase
J. Biol. Chem.
253
7040-7046
1978
Bos taurus, Lithobates pipiens
Manually annotated by BRENDA team
Shichi, H.; Somers, R.L.; Yamamoto, K.
Rhodopsin kinase
Methods Enzymol.
99
362-366
1983
Bos taurus
Manually annotated by BRENDA team
Benovic, J.L.; Mayor, F.; Somers, R.L.; Caron, M.G.; Lefkowitz, R.J.
Light-dependent phosphorylation of rhodopsin by beta-adrenergic receptor kinase
Nature
321
869-872
1986
Bos taurus
Manually annotated by BRENDA team
Palczewski, K.; McDowell, J.H.; Hargrave, P.A.
Purification and characterization of rhodopsin kinase
J. Biol. Chem.
263
14067-14073
1988
Bos taurus
Manually annotated by BRENDA team
Palczewski, K.; Buzylko, J.; Kaplan, M.W.; Polans, A.S.; Crabb, J.W.
Mechanism of rhodopsin kinase activation
J. Biol. Chem.
266
12949-12955
1991
Bos taurus
Manually annotated by BRENDA team
Adamus, G.; Arendt, A.; Hargrave, P.A.; Heyduk, T.; Palczewski, K.
The kinetics of multiphosphorylation of rhodopsin
Arch. Biochem. Biophys.
304
443-447
1993
Bos taurus
Manually annotated by BRENDA team
Sitaramayya, A.
Rhodopsin kinase prepared from bovine rod disk membranes quenches light activation of cGMP phosphodiesterase in a reconstituted system
Biochemistry
25
5460-5468
1986
Bos taurus
Manually annotated by BRENDA team
Palczewski, K.; McDowell, J.H.; Hargrave, P.A.
Rhodopsin kinase: substrate specificity and factors that influence activity
Biochemistry
27
2306-2313
1988
Bos taurus
Manually annotated by BRENDA team
Lee, R.H.; Brown, B.M.; Lolley, R.N.
Autophosphorylation of rhodopsin kinase from retinal rod outer segments
Biochemistry
21
3303-3307
1982
Bos taurus
Manually annotated by BRENDA team
Palczewski, K.; Kahn, N.; Hargrave, P.A.
Nucleoside inhibitors of rhodopsin kinase
Biochemistry
29
6276-6282
1990
Bos taurus
Manually annotated by BRENDA team
Kelleher, D.J.; Johnson, G.L.
Characterization of rhodopsin kinase purified from bovine rod outer segments
J. Biol. Chem.
265
2632-2639
1990
Bos taurus
Manually annotated by BRENDA team
Onorato, J.J.; Palczewski, K.; Regan, J.W.; Caron, M.G.; Lefkowitz, R.J.; Benovic, J.L.
Role of acidic amino acids in peptide substrates of the beta-adrenergic receptor kinase and rhodopsin kinase
Biochemistry
30
5118-5125
1991
Bos taurus
Manually annotated by BRENDA team
Chen, C.K.; Hurley, J.B.
Purification of rhodopsin kinase by recoverin affinity chromatography
Methods Enzymol.
315
404-410
2000
Bos taurus
Manually annotated by BRENDA team
Dean, K.R.; Akhtar, M.
Novel mechanism for the activation of rhodopsin kinase: Implications for other G protein-coupled receptor kinases (GRK's)
Biochemistry
35
6164-6172
1996
Bos taurus
Manually annotated by BRENDA team
Senin, I.I.; Koch, K.W.; Akhtar, M.; Philippov, P.P.
Ca2+-dependent control of rhodopsin phosphorylation: Recoverin and rhodopsin kinase
Adv. Exp. Med. Biol.
514
69-99
2002
Bos taurus, Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Sokal, I.; Pulvermller, A.; Buczylko, J.; Hofmann, K.P.; Palczewski, K.
Rhodopsin and its kinase
Methods Enzymol.
343
578-600
2001
Bos taurus, Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Cai, K.; Klein-Seetharaman, J.; Hwa, J.; Hubbell, W.L.; Khorana, H.G.
Structure and function in rhodopsin: Effects of disulfide cross-links in the cytoplasmic face of rhodopsin on transducin activation and phosphorylation by rhodopsin kinase
Biochemistry
38
12893-12898
1999
Bos taurus
Manually annotated by BRENDA team
Zhao, X.; Yokoyama, K.; Whitten, M.E.; Huang, J.; Gelb, M.H.; Palczewski, K.
A novel form of rhodopsin kinase from chicken retina and pineal gland
FEBS Lett.
454
115-121
1999
Bos taurus, Gallus gallus (O73685), Gallus gallus
Manually annotated by BRENDA team
Bruel, C.; Cha, K.; Reeves, P.J.; Getmanova, E.; Khorana, H.G.
Rhodopsin kinase: Expression in mammalian cells and a two-step purification
Proc. Natl. Acad. Sci. USA
97
3004-3009
2000
Bos taurus
Manually annotated by BRENDA team
Cha, K.; Bruel, C.; Inglese, J.; Khorana, H.G.
Rhodopsin kinase: Expression in baculovirus-infected insect cells, and characterization of post-translational modifications
Proc. Natl. Acad. Sci. USA
94
10577-10582
1997
Bos taurus
Manually annotated by BRENDA team
Chen, C.K.; Inglese, J.; Lefkowitz, R.J.; Hurley, J.B.
Ca2+-dependent interaction of recoverin with rhodopsin kinase
J. Biol. Chem.
270
18060-18066
1995
Bos taurus
Manually annotated by BRENDA team
Palczewski, K.; Ohguro, H.; Premont, R.T.; Inglese, J.
Rhodopsin kinase autophosphorylation. Characterization of site-specific mutations
J. Biol. Chem.
270
15294-15298
1995
Bos taurus
Manually annotated by BRENDA team
Satpaev, D.K.; Chen, C.K.; Scotti, A.; Simon, M.I.; Hurley, J.B.; Slepak, V.Z.
Autophosphorylation and ADP regulate the Ca2+-dependent interaction of recoverin with rhodopsin kinase
Biochemistry
37
10256-10262
1998
Bos taurus
Manually annotated by BRENDA team
Shi, W.; Sports, C.D.; Raman, D.; Shirakawa, S.; Osawa, S.; Weiss, E.R.
Rhodopsin arginine-135 mutants are phosphorylated by rhodopsin kinase and bind arrestin in the absence of 11-cis-retinal
Biochemistry
37
4869-4874
1998
Bos taurus
Manually annotated by BRENDA team
Maeda, T.; Imanishi, Y.; Palczewski, K.
Rhodopsin phosphorylation: 30 years later
Prog. Retin. Eye Res.
22
417-434
2003
Bos taurus, Homo sapiens, Homo sapiens (Q15835), Oryzias latipes, Mus musculus, Rattus norvegicus, Gallus gallus (O73685), Enteroctopus dofleini (O97020), Doryteuthis pealeii (Q9N2R0)
Manually annotated by BRENDA team
Komolov, K.E.; Zinchenko, D.V.; Churumova, V.A.; Vaganova, S.A.; Weiergraeber, O.H.; Senin, I.I.; Philippov, P.P.; Koch, K.W.
One of the Ca2+ binding sites of recoverin exclusively controls interaction with rhodopsin kinase
Biol. Chem.
386
285-289
2005
Bos taurus
Manually annotated by BRENDA team
Senin, I.I.; Hoeppner-Heitmann, D.; Polkovnikova, O.O.; Churumova, V.A.; Tikhomirova, N.K.; Philippov, P.P.; Koch, K.W.
Recoverin and rhodopsin kinase activity in detergent-resistant membrane rafts from rod outer segments
J. Biol. Chem.
279
48647-48653
2004
Bos taurus
Manually annotated by BRENDA team
Higgins, M.K.; Oprian, D.D.; Schertler, G.F.
Recoverin binds exclusively to an amphipathic peptide at the N terminus of rhodopsin kinase, inhibiting rhodopsin phosphorylation without affecting catalytic activity of the kinase
J. Biol. Chem.
281
19426-19432
2006
Bos taurus
Manually annotated by BRENDA team
Ames, J.B.; Levay, K.; Wingard, J.N.; Lusin, J.D.; Slepak, V.Z.
Structural basis for calcium-induced inhibition of rhodopsin kinase by recoverin
J. Biol. Chem.
281
37237-37245
2006
Bos taurus
Manually annotated by BRENDA team
Singh, P.; Wang, B.; Maeda, T.; Palczewski, K.; Tesmer, J.J.
Structures of rhodopsin kinase in different ligand states reveal key elements involved in G protein-coupled receptor kinase activation
J. Biol. Chem.
283
14053-14062
2008
Bos taurus (P28327)
Manually annotated by BRENDA team
Tesmer, J.J.; Nance, M.R.; Singh, P.; Lee, H.
Structure of a monomeric variant of rhodopsin kinase at 2.5 A resolution
Acta Crystallogr. Sect. F
68
622-625
2012
Bos taurus (P28327)
Manually annotated by BRENDA team
Orban, T.; Huang, C.C.; Homan, K.T.; Jastrzebska, B.; Tesmer, J.J.; Palczewski, K.
Substrate-induced changes in the dynamics of rhodopsin kinase (G protein-coupled receptor kinase 1)
Biochemistry
51
3404-3411
2012
Bos taurus
Manually annotated by BRENDA team
Grigoriev, I.; Senin, I.; Tikhomirova, N.; Komolov, K.; Permyakov, S.; Zerni, E.; Koch, K.; Philippov, P.
Synergetic effect of recoverin and calmodulin on regulation of rhodopsin kinase
Front. Mol. Neurosci.
5
28
2012
Bos taurus
Manually annotated by BRENDA team
Jones Brunette, A.M.; Sinha, A.; David, L.; Farrens, D.L.
Evidence that the rhodopsin kinase (GRK1) N-terminus and the transducin Galpha C-terminus interact with the same hydrophobic patch on rhodopsin TM5
Biochemistry
55
3123-3135
2016
Bos taurus (P28327)
Manually annotated by BRENDA team
Araujo, N.A.; Sanz-Rodriguez, C.E.; Bubis, J.
Binding of rhodopsin and rhodopsin analogues to transducin, rhodopsin kinase and arrestin-1
World J. Biol. Chem.
5
254-268
2014
Bos taurus
Manually annotated by BRENDA team
Abbas, S.; Marino, V.; Dell Orco, D.; Koch, K.W.
Molecular recognition of rhodopsin kinase GRK1 and recoverin is tuned by switching intra- and intermolecular electrostatic interactions
Biochemistry
58
4374-4385
2019
Bos taurus (P28327)
Manually annotated by BRENDA team