2.3.2.B11: ubiquitin transferase RING E3 (calmodulin-selective)
This is an abbreviated version!
For detailed information about ubiquitin transferase RING E3 (calmodulin-selective), go to the full flat file.
Word Map on EC 2.3.2.B11
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2.3.2.B11
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ligases
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polyubiquitination
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finger
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ubiquitin-proteasome
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mdm2
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parkin
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adaptor
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ubiquitin-like
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ubiquitin-dependent
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sumoylation
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sumo
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monoubiquitination
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skp2
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ubiquitin-mediated
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proteasome-dependent
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itch
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cullin-ring
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k63-linked
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deubiquitinase
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nedd4-2
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ring-type
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neddylation
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sumo-targeted
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angelman
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kaufman
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scfskp2
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pten-induced
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autoubiquitination
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bard1
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smurf2
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hsc70-interacting
- 2.3.2.B11
- ligases
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polyubiquitination
- finger
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ubiquitin-proteasome
- mdm2
- parkin
- adaptor
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ubiquitin-like
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ubiquitin-dependent
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sumoylation
- sumo
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monoubiquitination
- skp2
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ubiquitin-mediated
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proteasome-dependent
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itch
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cullin-ring
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k63-linked
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deubiquitinase
- nedd4-2
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ring-type
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neddylation
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sumo-targeted
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angelman
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kaufman
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scfskp2
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pten-induced
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autoubiquitination
- bard1
- smurf2
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hsc70-interacting
Reaction
Synonyms
Asr1p, E3-CaM, More, synthetase, ubiquitin-calmodulin, UBE3B, ubiquitin E3 ligase, ubiquityl-calmodulin synthase, ubiquityl-calmodulin synthetase, uCaM-synthetase
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Substrates Products
Substrates Products on EC 2.3.2.B11 - ubiquitin transferase RING E3 (calmodulin-selective)
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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
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specific function of the enzyme in the Ca2+-dependent breakdown of calmodulin in vertebrate (eukaryotic) cells
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n ATP + calmodulin + n ubiquitin
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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
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n ATP + calmodulin + n ubiquitin
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the activity is regulated by the binding of the second messenger Ca2+ to the substrate calmodulin, which increases the activity ca. 10fold
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n ATP + calmodulin + n ubiquitin
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it is very probably that the ubiquitination of calmodulin belongs to the normal regulatory repertoire of the eukaryotic cell
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n ATP + calmodulin + n ubiquitin
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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
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[RING-E3-ubiquitin-carrier protein]-L-cysteine + [calmodulin]-N6-ubiquitinyl-L-lysine
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[RING-E3-ubiquitin-carrier protein]-S-ubiquitinyl-L-cysteine + [calmodulin]-L-lysine
[RING-E3-ubiquitin-carrier protein]-L-cysteine + [calmodulin]-N6-ubiquitinyl-L-lysine
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calmodulin from bovine testis, Xenopus laevis or Paramecium tetraurelia. Paramecium calmodulin which is dimethylated at Lys13 is an efficient susbstrate
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[RING-E3-ubiquitin-carrier protein]-S-ubiquitinyl-L-cysteine + [calmodulin]-L-lysine
[RING-E3-ubiquitin-carrier protein]-L-cysteine + [calmodulin]-N6-ubiquitinyl-L-lysine
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several (possibly interdependent) forms of uCaM-synthetase exist which display different substrate specificities for calmodulin
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[RING-E3-ubiquitin-carrier protein]-S-ubiquitinyl-L-cysteine + [calmodulin]-L-lysine
[RING-E3-ubiquitin-carrier protein]-L-cysteine + [calmodulin]-N6-ubiquitinyl-L-lysine
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specific for Ca2+-calmodulin from vertebrates, at least 3 ubiquitin molecules can be coupled to lysine residues in calmodulin
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[RING-E3-ubiquitin-carrier protein]-S-ubiquitinyl-L-cysteine + [calmodulin]-L-lysine
[RING-E3-ubiquitin-carrier protein]-L-cysteine + [calmodulin]-N6-ubiquitinyl-L-lysine
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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
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[RING-E3-ubiquitin-carrier protein]-S-ubiquitinyl-L-cysteine + [calmodulin]-L-lysine
[RING-E3-ubiquitin-carrier protein]-L-cysteine + [calmodulin]-N6-ubiquitinyl-L-lysine
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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
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[RING-E3-ubiquitin-carrier protein]-S-ubiquitinyl-L-cysteine + [calmodulin]-L-lysine
[RING-E3-ubiquitin-carrier protein]-L-cysteine + [calmodulin]-N6-ubiquitinyl-L-lysine
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calmodulin from vertebrates, plants (spinach) and Neurospora crassa
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[RING-E3-ubiquitin-carrier protein]-S-ubiquitinyl-L-cysteine + [calmodulin]-L-lysine
[RING-E3-ubiquitin-carrier protein]-L-cysteine + [calmodulin]-N6-ubiquitinyl-L-lysine
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Saccharomyces cerevisiae enzyme conjugates ubiquitin to yeast and bovine calmodulin
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[RING-E3-ubiquitin-carrier protein]-S-ubiquitinyl-L-cysteine + [calmodulin]-L-lysine
[RING-E3-ubiquitin-carrier protein]-L-cysteine + [calmodulin]-N6-ubiquitinyl-L-lysine
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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
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[RING-E3-ubiquitin-carrier protein]-S-ubiquitinyl-L-cysteine + [calmodulin]-L-lysine
[RING-E3-ubiquitin-carrier protein]-L-cysteine + [calmodulin]-N6-ubiquitinyl-L-lysine
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with the vertebrate calmodulins, only one lysine residue is linked to ubiquitin and the incorporation of additional ubiquitin molecules leads to a polyubiquitin chain
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[RING-E3-ubiquitin-carrier protein]-S-ubiquitinyl-L-cysteine + [calmodulin]-L-lysine
[RING-E3-ubiquitin-carrier protein]-L-cysteine + [calmodulin]-N6-ubiquitinyl-L-lysine
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2-3 ubiquitin molecules can be incorporated per yeast calmodulin
2-3 ubiquitin molecules can be incorporated per yeast calmodulin
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[RING-E3-ubiquitin-carrier protein]-S-ubiquitinyl-L-cysteine + [calmodulin]-L-lysine
[RING-E3-ubiquitin-carrier protein]-L-cysteine + [calmodulin]-N6-ubiquitinyl-L-lysine
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specific for calmodulin
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UBE3B shows HECT E3 ubiquitin ligase activity and exhibits time-dependent auto-ubiquitylation activity
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additional information
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UBE3B shows HECT E3 ubiquitin ligase activity and exhibits time-dependent auto-ubiquitylation activity
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additional information
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no activity with beta-lactoglobulin, beta-casein, kappa-casein, alpha-casein and oxidized ribonuclease
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additional information
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in vivo calmodulin is ubiquitylated at lysine 22
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additional information
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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
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