Information on EC 2.3.2.B11 - ubiquitin transferase RING E3 (calmodulin-selective)

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.3.2.B11
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
ubiquitin transferase RING E3 (calmodulin-selective)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-ubiquitinyl-[RING-E3-ubiquitin-carrier protein]-L-cysteine + [calmodulin]-L-lysine22 = [RING-E3-ubiquitin-carrier protein]-L-cysteine + N6-ubiquitinyl-[calmodulin]-L-lysine22
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
peptide synthase reaction
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-
-
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SYSTEMATIC NAME
IUBMB Comments
[RING-E3-ubiquitin-carrier protein]-S-ubiquitinyl-L-cysteine:calmodulin ubiquitin transferase (isopeptide bond-forming)
Specific for Ca2+-calmodulin from vertebrates. At least three ubiquitin molecules can be coupled to lysine residues in calmodulin.
CAS REGISTRY NUMBER
COMMENTARY hide
119632-60-9
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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involved in calcium signalling. The interaction with calmodulin occurs in vivo and depends on physiological concentrations of Ca2+
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
n ATP + calmodulin + n ubiquitin
?
show the reaction diagram
[RING-E3-ubiquitin-carrier protein]-S-ubiquitinyl-L-cysteine + [calmodulin]-L-lysine
[RING-E3-ubiquitin-carrier protein]-L-cysteine + [calmodulin]-N6-ubiquitinyl-L-lysine
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
n ATP + calmodulin + n ubiquitin
?
show the reaction diagram
[RING-E3-ubiquitin-carrier protein]-S-ubiquitinyl-L-cysteine + [calmodulin]-L-lysine
[RING-E3-ubiquitin-carrier protein]-L-cysteine + [calmodulin]-N6-ubiquitinyl-L-lysine
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Trifluoperazine
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0.03 mM
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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calmodulin is not ubiquitinated by the enzyme unless E1 and UBC4 are present; traces of activity are also observed when RAD6 replaces UBC4; weak, but distinct activity is observed when UBC4 is replaced by UBC1
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0009 - 0.0081
Calmodulin
additional information
additional information
-
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0001218
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uCaM synthetase
0.0396
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uCaM Syn-F1
additional information
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-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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a nonessential RIND/PHD finger protein that constitutively shuttles between cytoplasm and nucelus
Manually annotated by BRENDA team
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a nonessential RIND/PHD finger protein that constitutively shuttles between cytoplasm and nucelus
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
213000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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2 * 111600, SDS-PAGE; 2 * 111975, calculation from nucleotide sequence; 2 * 112140, electrospray ion mass spectrometry
additional information
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
during purification on ubiquitin-Sepharose the Ca2+-dependent activity is lost and an essentially Ca2+-independent enzyme is obtained which is purified 90fold
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purification of the holoenzyme system uCaM synthetase. Fractionation yields two essentially inactive components: uCaM Syn-F1 and uCaM Syn-F2
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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removal of the 41 C-terminal amino acids (fourth Ca2+-binding loop) separated by several nanometers from Lys21 drastically decreases the affinity and reactivity of the synthetase for calmodulin