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Information on EC 2.3.2.B11 - ubiquitin transferase RING E3 (calmodulin-selective)
for references in articles please use BRENDA:EC2.3.2.B11
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Please check here for current data: EC unknown
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preliminary BRENDA-supplied EC number
EC Tree 2 Transferases
2.3 Acyltransferases
2.3.2 Aminoacyltransferases
2.3.2.B11 ubiquitin transferase RING E3 (calmodulin-selective)
The enzyme appears in viruses and cellular organisms
- 2.3.2.B11
- ligases
-
polyubiquitination
- finger
-
ubiquitin-proteasome
- mdm2
- parkin
- adaptor
-
ubiquitin-like
-
ubiquitin-dependent
-
sumoylation
- sumo
-
monoubiquitination
- skp2
-
ubiquitin-mediated
-
proteasome-dependent
-
itch
-
cullin-ring
-
k63-linked
-
deubiquitinase
- nedd4-2
-
ring-type
-
neddylation
-
sumo-targeted
-
angelman
-
kaufman
-
scfskp2
-
pten-induced
-
autoubiquitination
- bard1
- smurf2
-
hsc70-interacting
Reaction Schemes
show+
=
+
S-ubiquitinyl-[RING-E3-ubiquitin-carrier protein]-L-cysteine
+
[calmodulin]-L-lysine22
=
[RING-E3-ubiquitin-carrier protein]-L-cysteine
+
N6-ubiquitinyl-[calmodulin]-L-lysine22
Synonyms
ubiquitin e3 ligase, ube3b, asr1p, ucam-synthetase, ubiquityl-calmodulin synthetase, e3-cam, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
E3-CaM
-
-
-
-
synthetase, ubiquitin-calmodulin
-
-
-
-
ubiquityl-calmodulin synthase
-
-
-
-
ubiquityl-calmodulin synthetase
-
-
-
-
uCaM-synthetase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
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
S-ubiquitinyl-[RING-E3-ubiquitin-carrier protein]-L-cysteine + [calmodulin]-L-lysine22 = [RING-E3-ubiquitin-carrier protein]-L-cysteine + N6-ubiquitinyl-[calmodulin]-L-lysine22
The enzyme specifically ubiquitylates calmodulin in a Ca2+-dependent manner. The direct interaction requires a functional RING domain, occurs in vivo and depends on physiological concentrations of Ca2+.
-
-
-
S-ubiquitinyl-[RING-E3-ubiquitin-carrier protein]-L-cysteine + [calmodulin]-L-lysine22 = [RING-E3-ubiquitin-carrier protein]-L-cysteine + N6-ubiquitinyl-[calmodulin]-L-lysine22
calmodilin is a small calcium binding protein that is able to transduce an influx of calcium ions to effector proteins. Purified Asr1p E3 ligase, the E1 enzyme and the E2 enzyme UbcH5a are sufficient for in vitro ubiquitylation of calmodulin, requiring a function Asr1p Ring domain. Asr1p specifically ubiquitylates calmodulin
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
peptide synthase reaction
-
-
-
-
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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.
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CAS REGISTRY NUMBER
COMMENTARY
119632-60-9
-
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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
[RING-E3-ubiquitin-carrier protein]-S-ubiquitinyl-L-cysteine + [calmodulin]-L-lysine
[RING-E3-ubiquitin-carrier protein]-L-cysteine + [calmodulin]-N6-ubiquitinyl-L-lysine
n ATP + calmodulin + n ubiquitin
?
-
Substrates: specific function of the enzyme in the Ca2+-dependent breakdown of calmodulin in vertebrate (eukaryotic) cells
Products: -
Products: -
?
n ATP + calmodulin + n ubiquitin
?
-
Substrates: Ca2+-dependent ubiquitination only of free calmodulin may provide an efficient scavenging mechanism (with subsequent breakdown) for all free calmodulin in excess of that amount which can be found by the calmodulin-binding proteins in the cell
Products: -
Products: -
?
n ATP + calmodulin + n ubiquitin
?
-
Substrates: the activity is regulated by the binding of the second messenger Ca2+ to the substrate calmodulin, which increases the activity ca. 10fold
Products: -
Products: -
?
n ATP + calmodulin + n ubiquitin
?
-
Substrates: it is very probably that the ubiquitination of calmodulin belongs to the normal regulatory repertoire of the eukaryotic cell
Products: -
Products: -
?
n ATP + calmodulin + n ubiquitin
?
-
Substrates: monoubiquitylation strongly decreases the biological activity of calmodulin towards phosphorylase kinase by reducing its affinity approximately threefold and the maximal degree of activation approximately twofold
Products: -
Products: -
?
[RING-E3-ubiquitin-carrier protein]-S-ubiquitinyl-L-cysteine + [calmodulin]-L-lysine
[RING-E3-ubiquitin-carrier protein]-L-cysteine + [calmodulin]-N6-ubiquitinyl-L-lysine
-
Substrates: up to 3 molecules of ubiquitin can be incorporated into one molecule of calmodulin. If methylated ubiquitin is employed only one conjugate corresponding to the mono-ubiquitination product of calmodulin is formed. Only a single Lys residue in calmodulin is conjugated to ubiquitin. All other higher molecular weight ubiquitin-calmodulin conjugates must therefore be composed of one calmodulin to which an oligo- or polyubiquitin chain is linked
Products: up to 3 molecules of ubiquitin can be incorporated into one molecule of calmodulin. If methylated ubiquitin is employed only one conjugate corresponding to the mono-ubiquitination product of calmodulin is formed. Only a single Lys residue in calmodulin is conjugated to ubiquitin. All other higher molecular weight ubiquitin-calmodulin conjugates must therefore be composed of one calmodulin to which an oligo- or polyubiquitin chain is linked
Products: up to 3 molecules of ubiquitin can be incorporated into one molecule of calmodulin. If methylated ubiquitin is employed only one conjugate corresponding to the mono-ubiquitination product of calmodulin is formed. Only a single Lys residue in calmodulin is conjugated to ubiquitin. All other higher molecular weight ubiquitin-calmodulin conjugates must therefore be composed of one calmodulin to which an oligo- or polyubiquitin chain is linked
?
[RING-E3-ubiquitin-carrier protein]-S-ubiquitinyl-L-cysteine + [calmodulin]-L-lysine
[RING-E3-ubiquitin-carrier protein]-L-cysteine + [calmodulin]-N6-ubiquitinyl-L-lysine
-
Substrates: -
Products: -
Products: -
?
[RING-E3-ubiquitin-carrier protein]-S-ubiquitinyl-L-cysteine + [calmodulin]-L-lysine
[RING-E3-ubiquitin-carrier protein]-L-cysteine + [calmodulin]-N6-ubiquitinyl-L-lysine
-
Substrates: calmodulin from bovine testis, Xenopus laevis or Paramecium tetraurelia. Paramecium calmodulin which is dimethylated at Lys13 is an efficient susbstrate
Products: -
Products: -
?
[RING-E3-ubiquitin-carrier protein]-S-ubiquitinyl-L-cysteine + [calmodulin]-L-lysine
[RING-E3-ubiquitin-carrier protein]-L-cysteine + [calmodulin]-N6-ubiquitinyl-L-lysine
-
Substrates: several (possibly interdependent) forms of uCaM-synthetase exist which display different substrate specificities for calmodulin
Products: -
Products: -
?
[RING-E3-ubiquitin-carrier protein]-S-ubiquitinyl-L-cysteine + [calmodulin]-L-lysine
[RING-E3-ubiquitin-carrier protein]-L-cysteine + [calmodulin]-N6-ubiquitinyl-L-lysine
-
Substrates: specific for Ca2+-calmodulin from vertebrates, at least 3 ubiquitin molecules can be coupled to lysine residues in calmodulin
Products: -
Products: -
?
[RING-E3-ubiquitin-carrier protein]-S-ubiquitinyl-L-cysteine + [calmodulin]-L-lysine
[RING-E3-ubiquitin-carrier protein]-L-cysteine + [calmodulin]-N6-ubiquitinyl-L-lysine
-
Substrates: the ubiquitylation site has the octapeptide structure -L-F-D-K21-D-G-D-G- with Lys21 being the ubiquitylated residue in vertebrate and other calmodulins. 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. The nearly identical site -V-F-D-K94-D-G-N-G- in the third Ca2+-binding loop of vertebrate calmodulin is apparently not ubiquitylated by the synthetase
Products: -
Products: -
?
[RING-E3-ubiquitin-carrier protein]-S-ubiquitinyl-L-cysteine + [calmodulin]-L-lysine
[RING-E3-ubiquitin-carrier protein]-L-cysteine + [calmodulin]-N6-ubiquitinyl-L-lysine
-
Substrates: calmodulin from vertebrates, plants (spinach) and Neurospora crassa
Products: -
Products: -
?
[RING-E3-ubiquitin-carrier protein]-S-ubiquitinyl-L-cysteine + [calmodulin]-L-lysine
[RING-E3-ubiquitin-carrier protein]-L-cysteine + [calmodulin]-N6-ubiquitinyl-L-lysine
-
Substrates: Saccharomyces cerevisiae enzyme conjugates ubiquitin to yeast and bovine calmodulin
Products: -
Products: -
?
[RING-E3-ubiquitin-carrier protein]-S-ubiquitinyl-L-cysteine + [calmodulin]-L-lysine
[RING-E3-ubiquitin-carrier protein]-L-cysteine + [calmodulin]-N6-ubiquitinyl-L-lysine
-
Substrates: mammalian calmodulin containing trimethyllysine 115, only the free form of calmodulin can be ubiquitinated. Neither calmodulin bound to phosphorylase kinase as an integral subunit (delta-subunit) not that bound as a peripheral subunit (delta-subunit) is ubiquitinated
Products: -
Products: -
?
[RING-E3-ubiquitin-carrier protein]-S-ubiquitinyl-L-cysteine + [calmodulin]-L-lysine
[RING-E3-ubiquitin-carrier protein]-L-cysteine + [calmodulin]-N6-ubiquitinyl-L-lysine
-
Substrates: with the vertebrate calmodulins, only one lysine residue is linked to ubiquitin and the incorporation of additional ubiquitin molecules leads to a polyubiquitin chain
Products: -
Products: -
?
[RING-E3-ubiquitin-carrier protein]-S-ubiquitinyl-L-cysteine + [calmodulin]-L-lysine
[RING-E3-ubiquitin-carrier protein]-L-cysteine + [calmodulin]-N6-ubiquitinyl-L-lysine
-
Substrates: 2-3 ubiquitin molecules can be incorporated per yeast calmodulin
Products: 2-3 ubiquitin molecules can be incorporated per yeast calmodulin
Products: 2-3 ubiquitin molecules can be incorporated per yeast calmodulin
?
[RING-E3-ubiquitin-carrier protein]-S-ubiquitinyl-L-cysteine + [calmodulin]-L-lysine
[RING-E3-ubiquitin-carrier protein]-L-cysteine + [calmodulin]-N6-ubiquitinyl-L-lysine
-
Substrates: specific for calmodulin
Products: -
Products: -
?
additional information
?
-
Substrates: UBE3B shows HECT E3 ubiquitin ligase activity and exhibits time-dependent auto-ubiquitylation activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: UBE3B shows HECT E3 ubiquitin ligase activity and exhibits time-dependent auto-ubiquitylation activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with beta-lactoglobulin, beta-casein, kappa-casein, alpha-casein and oxidized ribonuclease
Products: -
Products: -
?
additional information
?
-
-
Substrates: purified Asr1p E3 ligase, the E1 enzyme and the E2 enzyme UbcH5a are sufficient for in vitro ubiquitylation of calmodulin, requiring a function Asr1p Ring domain
Products: -
Products: -
?
additional information
?
-
-
Substrates: in vivo calmodulin is ubiquitylated at lysine 22
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
[RING-E3-ubiquitin-carrier protein]-S-ubiquitinyl-L-cysteine + [calmodulin]-L-lysine
[RING-E3-ubiquitin-carrier protein]-L-cysteine + [calmodulin]-N6-ubiquitinyl-L-lysine
n ATP + calmodulin + n ubiquitin
?
-
Substrates: specific function of the enzyme in the Ca2+-dependent breakdown of calmodulin in vertebrate (eukaryotic) cells
Products: -
Products: -
?
n ATP + calmodulin + n ubiquitin
?
-
Substrates: Ca2+-dependent ubiquitination only of free calmodulin may provide an efficient scavenging mechanism (with subsequent breakdown) for all free calmodulin in excess of that amount which can be found by the calmodulin-binding proteins in the cell
Products: -
Products: -
?
n ATP + calmodulin + n ubiquitin
?
-
Substrates: the activity is regulated by the binding of the second messenger Ca2+ to the substrate calmodulin, which increases the activity ca. 10fold
Products: -
Products: -
?
n ATP + calmodulin + n ubiquitin
?
-
Substrates: it is very probably that the ubiquitination of calmodulin belongs to the normal regulatory repertoire of the eukaryotic cell
Products: -
Products: -
?
n ATP + calmodulin + n ubiquitin
?
-
Substrates: monoubiquitylation strongly decreases the biological activity of calmodulin towards phosphorylase kinase by reducing its affinity approximately threefold and the maximal degree of activation approximately twofold
Products: -
Products: -
?
[RING-E3-ubiquitin-carrier protein]-S-ubiquitinyl-L-cysteine + [calmodulin]-L-lysine
[RING-E3-ubiquitin-carrier protein]-L-cysteine + [calmodulin]-N6-ubiquitinyl-L-lysine
-
Substrates: specific for Ca2+-calmodulin from vertebrates, at least 3 ubiquitin molecules can be coupled to lysine residues in calmodulin
Products: -
Products: -
?
[RING-E3-ubiquitin-carrier protein]-S-ubiquitinyl-L-cysteine + [calmodulin]-L-lysine
[RING-E3-ubiquitin-carrier protein]-L-cysteine + [calmodulin]-N6-ubiquitinyl-L-lysine
-
Substrates: Saccharomyces cerevisiae enzyme conjugates ubiquitin to yeast and bovine calmodulin
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Ca2+
-
the activity is regulated by the binding of the second messenger Ca2+ to the substrate calmodulin, which increases the activity ca. 10fold
Ca2+
-
required
Ca2+
-
during purification on ubiquitin-Sepharose the Ca2+-dependent activity is lost and an essentially Ca2+-independent enzyme is obtained which is purified 90fold
Ca2+
-
Asr1p is involved in calcium signalling. The interaction with calmodulin occurs in vivo and depends on physiological concentrations of Ca2+. A plataeu is reached at 100-500 nM CaCl2
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Calmodulin
UBE3B interacts with calmodulin via its N-terminal isoleucine-glutamine motif. Deletion of the motif (amino acids 29-58) results in loss of calmodulin binding and a significant increase in the in vitro ubiquitylation activity of UBE3B. Changes in calcium levels in vitro disrupt the calmodulin-UBE3B interaction
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ca2+
when the concentration of calcium is increased, calmodulin is released from UBE3B, resulting in an increase in ubiquitylation activity
additional information
-
traces of activity are also observed when RAD6 replaces UBC4
-
additional information
-
weak, but distinct activity is observed when UBC4 is replaced by UBC1
-
additional information
-
calmodulin is not ubiquitinated by the enzyme unless E1 and UBC4 are present
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
brenda
several possibly interdependent forms of uCaM-synthetase exist which display different specificities for calmodulin
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
a nonessential RIND/PHD finger protein that constitutively shuttles between cytoplasm and nucelus
brenda
-
a nonessential RIND/PHD finger protein that constitutively shuttles between cytoplasm and nucelus
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
physiological function
physiological function
-
involved in calcium signalling. The interaction with calmodulin occurs in vivo and depends on physiological concentrations of Ca2+
physiological function
mutating the catalytic cysteine or deleting the entire HECT domain (amino acids 758-1068) results in loss of UBE3B's ubiquitylation activity. Knockdown of UBE3B in human cells induces changes in mitochondrial morphology and physiology, a decrease in mitochondrial volume, and a severe suppression of cellular proliferation
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
additional information
additional information
-
two components of the ligase can be identified: uCaM Syn-F1 and uCaM Syn-F2, the first of which binds to ubiquitin and the second which binds to calmodulin
additional information
-
two putitive calmodulin motifs wihin Asr1p are identified that are sufficient and necessary for interaction with calmodulin
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
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
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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
-
purification of the holoenzyme system uCaM synthetase. Fractionation yields two essentially inactive components: uCaM Syn-F1 and uCaM Syn-F2
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Jennissen, H.P.; Laub, M.
Ubiquitin-calmodulin conjugating activity from cardiac muscle
Biol. Chem. Hoppe-Seyler
369
1325-1330
1988
Oryctolagus cuniculus
brenda
Ziegenhagen, R.; Jennissen, H.P.
Multiple ubiquitination of vertebrate calmodulin by reticulocyte lysate and inhibition of calmodulin conjugation by phosphorylase kinase
Biol. Chem. Hoppe-Seyler
369
1317-1324
1988
Oryctolagus cuniculus
brenda
Majetschak, M.; Laub, M.; Jennissen, H.P.
Q ubiquityl-calmodulin synthetase that effectively recognizes the Ca2+-free form of calmodulin
FEBS Lett.
315
347-352
1993
Oryctolagus cuniculus
brenda
Laub, M.; Jennissen, H.P.
Ubiquitination of endogenous calmodulin in rabbit tissue extracts
FEBS Lett.
294
229-233
1991
Oryctolagus cuniculus
brenda
Jennissen, H.P.; Botzet, G.; Majetschak, M.; Laub, M.; Ziegenhagen, R.; Demiroglou, A.
Ca2+-dependent ubiquitination of calmodulin in yeast
FEBS Lett.
296
51-56
1992
Oryctolagus cuniculus, Saccharomyces cerevisiae
brenda
Ziegenhagen, R.; Goldberg, M.; Rakutt, W.D.; Jennissen, H.P.
Multiple ubiquitination of calmodulin results in one polyubiquitin chain linked to calmodulin
FEBS Lett.
271
71-75
1990
Oryctolagus cuniculus
brenda
Ziegenhagen, R.; Jennissen, H.P.
Plant and fungus calmodulins are polyubiquitinated at a single site in a Ca2+-dependent manner
FEBS Lett.
273
253-256
1990
Oryctolagus cuniculus
brenda
Laub, M.; Steppuhn, J.A.; Bluggel, M.; Immler, D.; Meyer, H.E.; Jennissen, H.P.
Modulation of calmodulin function by ubiquitin-calmodulin ligase and identification of the responsible ubiquitylation site in vertebrate calmodulin
Eur. J. Biochem.
255
422-431
1998
Oryctolagus cuniculus
brenda
Majetschak, M.; Laub, M.; Meyer, H.E.; Jennissen, H.P.
The ubiquityl-calmodulin synthetase system from rabbit reticulocytes: isolation of the ubiquitin-binding first component, a ubiquitin-activating enzyme
Eur. J. Biochem.
255
482-491
1998
Oryctolagus cuniculus
brenda
Parag, H.A.; Dimitrovsky, D.; Raboy, B.; Kulka, R.G.
Selective ubiquitination of calmodulin by UBC4 and a putative ubiquitin protein ligase (E3) from Saccharomyces cerevisiae
FEBS Lett.
325
242-246
1993
Saccharomyces cerevisiae
brenda
Laub, M.; Jennissen, H.P.
Synthesis and decay of calmodulin-ubiquitin conjugates in cell-free extracts of various rabbit tissues
Biochim. Biophys. Acta
1357
173-191
1997
Oryctolagus cuniculus
brenda
Fries, T.; Frank, R.; Bailer, S.M.
The Saccharomyces cerevisiae ubiquitin E3 ligase Asr1p targets calmodulin for ubiquitylation
Biochem. Biophys. Res. Commun.
411
197-201
2011
Saccharomyces cerevisiae
brenda
Braganza, A.; Li, J.; Zeng, X.; Yates, N.; Dey, N.; Andrews, J.; Clark, J.; Zamani, L.; Wang, X.; St Croix, C.; OSullivan, R.; Garcia-Exposito, L.; Brodsky, J.; Sobol, R.
UBE3B is a calmodulin-regulated, mitochondrion-associated E3 ubiquitin ligase
J. Biol. Chem.
292
2470-2484
2017
Homo sapiens (Q7Z3V4), Homo sapiens
brenda
EXTERNAL LINKS (specific for EC-Number 2.3.2.B11)
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