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Literature summary for 2.3.2.B11 extracted from

  • Ziegenhagen, R.; Jennissen, H.P.
    Plant and fungus calmodulins are polyubiquitinated at a single site in a Ca2+-dependent manner (1990), FEBS Lett., 273, 253-256.
    View publication on PubMed

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ required Oryctolagus cuniculus

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus
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-
-

Source Tissue

Source Tissue Comment Organism Textmining
reticulocyte
-
Oryctolagus cuniculus
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
[RING-E3-ubiquitin-carrier protein]-S-ubiquitinyl-L-cysteine + [calmodulin]-L-lysine calmodulin from vertebrates, plants (spinach) and Neurospora crassa Oryctolagus cuniculus [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 with the vertebrate calmodulins, only one lysine residue is linked to ubiquitin and the incorporation of additional ubiquitin molecules leads to a polyubiquitin chain Oryctolagus cuniculus [RING-E3-ubiquitin-carrier protein]-L-cysteine + [calmodulin]-N6-ubiquitinyl-L-lysine
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?