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n ATP + calmodulin + n ubiquitin
?
[RING-E3-ubiquitin-carrier protein]-S-ubiquitinyl-L-cysteine + [calmodulin]-L-lysine
[RING-E3-ubiquitin-carrier protein]-L-cysteine + [calmodulin]-N6-ubiquitinyl-L-lysine
additional information
?
-
n ATP + calmodulin + n ubiquitin
?
-
specific function of the enzyme in the Ca2+-dependent breakdown of calmodulin in vertebrate (eukaryotic) cells
-
-
?
n ATP + calmodulin + n ubiquitin
?
-
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
-
-
?
n ATP + calmodulin + n ubiquitin
?
-
the activity is regulated by the binding of the second messenger Ca2+ to the substrate calmodulin, which increases the activity ca. 10fold
-
-
?
n ATP + calmodulin + n ubiquitin
?
-
it is very probably that the ubiquitination of calmodulin belongs to the normal regulatory repertoire of the eukaryotic cell
-
-
?
n ATP + calmodulin + n ubiquitin
?
-
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
-
-
?
[RING-E3-ubiquitin-carrier protein]-S-ubiquitinyl-L-cysteine + [calmodulin]-L-lysine
[RING-E3-ubiquitin-carrier protein]-L-cysteine + [calmodulin]-N6-ubiquitinyl-L-lysine
-
-
-
-
?
[RING-E3-ubiquitin-carrier protein]-S-ubiquitinyl-L-cysteine + [calmodulin]-L-lysine
[RING-E3-ubiquitin-carrier protein]-L-cysteine + [calmodulin]-N6-ubiquitinyl-L-lysine
-
calmodulin from bovine testis, Xenopus laevis or Paramecium tetraurelia. Paramecium calmodulin which is dimethylated at Lys13 is an efficient susbstrate
-
-
?
[RING-E3-ubiquitin-carrier protein]-S-ubiquitinyl-L-cysteine + [calmodulin]-L-lysine
[RING-E3-ubiquitin-carrier protein]-L-cysteine + [calmodulin]-N6-ubiquitinyl-L-lysine
-
several (possibly interdependent) forms of uCaM-synthetase exist which display different substrate specificities for 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
-
specific for Ca2+-calmodulin from vertebrates, at least 3 ubiquitin molecules can be coupled to lysine residues in 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
-
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
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
-
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
-
-
?
[RING-E3-ubiquitin-carrier protein]-S-ubiquitinyl-L-cysteine + [calmodulin]-L-lysine
[RING-E3-ubiquitin-carrier protein]-L-cysteine + [calmodulin]-N6-ubiquitinyl-L-lysine
-
calmodulin from vertebrates, plants (spinach) and Neurospora crassa
-
-
?
[RING-E3-ubiquitin-carrier protein]-S-ubiquitinyl-L-cysteine + [calmodulin]-L-lysine
[RING-E3-ubiquitin-carrier protein]-L-cysteine + [calmodulin]-N6-ubiquitinyl-L-lysine
-
Saccharomyces cerevisiae enzyme conjugates ubiquitin to yeast and bovine 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
-
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
-
-
?
[RING-E3-ubiquitin-carrier protein]-S-ubiquitinyl-L-cysteine + [calmodulin]-L-lysine
[RING-E3-ubiquitin-carrier protein]-L-cysteine + [calmodulin]-N6-ubiquitinyl-L-lysine
-
with the vertebrate calmodulins, only one lysine residue is linked to ubiquitin and the incorporation of additional ubiquitin molecules leads to a polyubiquitin chain
-
-
?
[RING-E3-ubiquitin-carrier protein]-S-ubiquitinyl-L-cysteine + [calmodulin]-L-lysine
[RING-E3-ubiquitin-carrier protein]-L-cysteine + [calmodulin]-N6-ubiquitinyl-L-lysine
-
2-3 ubiquitin molecules can be incorporated per yeast calmodulin
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
-
specific for calmodulin
-
-
?
additional information
?
-
UBE3B shows HECT E3 ubiquitin ligase activity and exhibits time-dependent auto-ubiquitylation activity
-
-
-
additional information
?
-
-
UBE3B shows HECT E3 ubiquitin ligase activity and exhibits time-dependent auto-ubiquitylation activity
-
-
-
additional information
?
-
-
no activity with beta-lactoglobulin, beta-casein, kappa-casein, alpha-casein and oxidized ribonuclease
-
-
?
additional information
?
-
-
in vivo calmodulin is ubiquitylated at lysine 22
-
-
?
additional information
?
-
-
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
n ATP + calmodulin + n ubiquitin
?
[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
?
-
specific function of the enzyme in the Ca2+-dependent breakdown of calmodulin in vertebrate (eukaryotic) cells
-
-
?
n ATP + calmodulin + n ubiquitin
?
-
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
-
-
?
n ATP + calmodulin + n ubiquitin
?
-
the activity is regulated by the binding of the second messenger Ca2+ to the substrate calmodulin, which increases the activity ca. 10fold
-
-
?
n ATP + calmodulin + n ubiquitin
?
-
it is very probably that the ubiquitination of calmodulin belongs to the normal regulatory repertoire of the eukaryotic cell
-
-
?
n ATP + calmodulin + n ubiquitin
?
-
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
-
-
?
[RING-E3-ubiquitin-carrier protein]-S-ubiquitinyl-L-cysteine + [calmodulin]-L-lysine
[RING-E3-ubiquitin-carrier protein]-L-cysteine + [calmodulin]-N6-ubiquitinyl-L-lysine
-
specific for Ca2+-calmodulin from vertebrates, at least 3 ubiquitin molecules can be coupled to lysine residues in 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
-
Saccharomyces cerevisiae enzyme conjugates ubiquitin to yeast and bovine calmodulin
-
-
?
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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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
Saccharomyces cerevisiae, Oryctolagus cuniculus
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