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S-adenosyl-L-methionine + calmodulin L-lysine
S-adenosyl-L-homocysteine + calmodulin N6-methyl-L-lysine
S-adenosyl-L-methionine + calmodulin L-lysine-115
S-adenosyl-L-homocysteine + calmodulin N6-methyl-L-lysine-115
S-adenosyl-L-methionine + mushroom demethylcalmodulin
?
-
Substrates: -
Products: -
?
S-adenosyl-L-methionine + Octopus calmodulin L-lysine
S-adenosyl-L-homocysteine + Octopus calmodulin N6-methyl-L-lysine
-
Substrates: -
Products: -
r
S-adenosyl-L-methionine + VU-1 calmodulin L-lysine
S-adenosyl-L-homocysteine + VU-1 calmodulin N6-methyl-L-lysine
-
Substrates: -
Products: -
r
additional information
?
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S-adenosyl-L-methionine + calmodulin L-lysine

S-adenosyl-L-homocysteine + calmodulin N6-methyl-L-lysine
-
Substrates: the enzyme transfers three methyl groups to a highly conserved lysyl residue at position 115 in calmodulin
Products: -
?
S-adenosyl-L-methionine + calmodulin L-lysine
S-adenosyl-L-homocysteine + calmodulin N6-methyl-L-lysine
-
Substrates: calmodulin is methylated at Lys315
Products: -
?
S-adenosyl-L-methionine + calmodulin L-lysine
S-adenosyl-L-homocysteine + calmodulin N6-methyl-L-lysine
-
Substrates: -
Products: -
?
S-adenosyl-L-methionine + calmodulin L-lysine
S-adenosyl-L-homocysteine + calmodulin N6-methyl-L-lysine
Substrates: -
Products: -
?
S-adenosyl-L-methionine + calmodulin L-lysine
S-adenosyl-L-homocysteine + calmodulin N6-methyl-L-lysine
Substrates: -
Products: -
?
S-adenosyl-L-methionine + calmodulin L-lysine
S-adenosyl-L-homocysteine + calmodulin N6-methyl-L-lysine
-
Substrates: -
Products: -
?
S-adenosyl-L-methionine + calmodulin L-lysine
S-adenosyl-L-homocysteine + calmodulin N6-methyl-L-lysine
Substrates: -
Products: -
?
S-adenosyl-L-methionine + calmodulin L-lysine
S-adenosyl-L-homocysteine + calmodulin N6-methyl-L-lysine
-
Substrates: Pisum sativum calmodulin
Products: -
?
S-adenosyl-L-methionine + calmodulin L-lysine
S-adenosyl-L-homocysteine + calmodulin N6-methyl-L-lysine
-
Substrates: posttranslational modification of calmodulin
Products: -
?
S-adenosyl-L-methionine + calmodulin L-lysine
S-adenosyl-L-homocysteine + calmodulin N6-methyl-L-lysine
-
Substrates: -
Products: trimethyllysine calmodulin, major product, + dimethyllysine + monomethyllysine
?
S-adenosyl-L-methionine + calmodulin L-lysine
S-adenosyl-L-homocysteine + calmodulin N6-methyl-L-lysine
-
Substrates: highly specific
Products: -
?
S-adenosyl-L-methionine + calmodulin L-lysine
S-adenosyl-L-homocysteine + calmodulin N6-methyl-L-lysine
-
Substrates: highly specific
Products: 3 mol of methyl per mol of calmodulin are incorporated into lysine 115 of des(methyl) calmodulin from Dictyostelium discoideum resulting in formation of 1 mol of trimethyllysine at the site normally methylated
?
S-adenosyl-L-methionine + calmodulin L-lysine
S-adenosyl-L-homocysteine + calmodulin N6-methyl-L-lysine
-
Substrates: highly specific
Products: trimethyllysine calmodulin, major product, + dimethyllysine + monomethyllysine
?
S-adenosyl-L-methionine + calmodulin L-lysine
S-adenosyl-L-homocysteine + calmodulin N6-methyl-L-lysine
-
Substrates: Dictyostelium discoideum calmodulin
Products: 3 mol of methyl per mol of calmodulin are incorporated into lysine 115 of des(methyl) calmodulin from Dictyostelium discoideum resulting in formation of 1 mol of trimethyllysine at the site normally methylated
?
S-adenosyl-L-methionine + calmodulin L-lysine
S-adenosyl-L-homocysteine + calmodulin N6-methyl-L-lysine
-
Substrates: octopus calmodulin
Products: enzyme methylates a specific lysine residue of octopus calmodulin
?
S-adenosyl-L-methionine + calmodulin L-lysine
S-adenosyl-L-homocysteine + calmodulin N6-methyl-L-lysine
-
Substrates: octopus calmodulin
Products: formation of epsilon-N-mono-, epsilon-N-di- and epsilon-N-trimethyllysine, the labelled N-methyllysine lies in the 107-126 peptide
?
S-adenosyl-L-methionine + calmodulin L-lysine
S-adenosyl-L-homocysteine + calmodulin N6-methyl-L-lysine
-
Substrates: mushroom demthylcalmodulin
Products: trimethyllysine calmodulin, major product, + dimethyllysine + monomethyllysine
?
S-adenosyl-L-methionine + calmodulin L-lysine
S-adenosyl-L-homocysteine + calmodulin N6-methyl-L-lysine
-
Substrates: posttranslational modification of calmodulin
Products: -
?
S-adenosyl-L-methionine + calmodulin L-lysine-115

S-adenosyl-L-homocysteine + calmodulin N6-methyl-L-lysine-115
-
Substrates: -
Products: -
?
S-adenosyl-L-methionine + calmodulin L-lysine-115
S-adenosyl-L-homocysteine + calmodulin N6-methyl-L-lysine-115
-
Substrates: -
Products: -
?
additional information

?
-
-
Substrates: structural requirements of calmodulin
Products: -
?
additional information
?
-
-
Substrates: troponin C has low activity at very high troponin concentration
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
S-adenosyl-L-methionine + calmodulin L-lysine
S-adenosyl-L-homocysteine + calmodulin N6-methyl-L-lysine
S-adenosyl-L-methionine + calmodulin L-lysine

S-adenosyl-L-homocysteine + calmodulin N6-methyl-L-lysine
-
Substrates: the enzyme transfers three methyl groups to a highly conserved lysyl residue at position 115 in calmodulin
Products: -
?
S-adenosyl-L-methionine + calmodulin L-lysine
S-adenosyl-L-homocysteine + calmodulin N6-methyl-L-lysine
-
Substrates: calmodulin is methylated at Lys315
Products: -
?
S-adenosyl-L-methionine + calmodulin L-lysine
S-adenosyl-L-homocysteine + calmodulin N6-methyl-L-lysine
Substrates: -
Products: -
?
S-adenosyl-L-methionine + calmodulin L-lysine
S-adenosyl-L-homocysteine + calmodulin N6-methyl-L-lysine
Substrates: -
Products: -
?
S-adenosyl-L-methionine + calmodulin L-lysine
S-adenosyl-L-homocysteine + calmodulin N6-methyl-L-lysine
-
Substrates: -
Products: -
?
S-adenosyl-L-methionine + calmodulin L-lysine
S-adenosyl-L-homocysteine + calmodulin N6-methyl-L-lysine
-
Substrates: posttranslational modification of calmodulin
Products: -
?
S-adenosyl-L-methionine + calmodulin L-lysine
S-adenosyl-L-homocysteine + calmodulin N6-methyl-L-lysine
-
Substrates: posttranslational modification of calmodulin
Products: -
?
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Sitaramayya, A.; Wright, L.S.; Siegel, F.L.
Enzymatic methylation of calmodulin in rat brain cytosol
J. Biol. Chem.
255
8894-8900
1980
Rattus norvegicus
brenda
Murtaugh, T.J.; Rowe, P.M.; Vincent, P.L.; Wright, L.S.; Siegel, F.L.
Posttranslational modification of calmodulin
Methods Enzymol.
102
158-170
1983
Rattus norvegicus
brenda
Rowe, P.M.; Wright, L.S.; Siegel, F.L.
Calmodulin N-methyltransferase. Partial purification and characterization
J. Biol. Chem.
261
7060-7069
1986
Rattus norvegicus
brenda
Oh, S.H.; Roberts, D.M.
Analysis of the state of posttranslational calmodulin methylation in developing pea plants
Plant Physiol.
93
880-887
1990
Ovis aries
brenda
Morino, H.; Kawamoto, T.; Miyake, M.; Kakimoto, Y.
Purification and properties of calmodulin-lysine N-methyltransferase from rat brain cytosol
J. Neurochem.
48
1201-1208
1987
Rattus norvegicus
brenda
Han, C.H.; Roberts, D.M.
Altered methylation substrate kinetics and calcium binding of a calmodulin with a Val136->Thr substitution
Eur. J. Biochem.
244
904-912
1997
Escherichia coli
brenda
Pech, L.L.; Nelson, D.L.
Purification and characterization of calmodulin (lysine 115) N-methyltransferase from Paramecium tetraurelia
Biochim. Biophys. Acta
1199
183-194
1994
Paramecium tetraurelia
brenda
Wright, L.S.; Bertics, P.J.; Siegel, F.L.
Calmodulin N-methyltransferase. Kinetics, mechanism, and inhibitors
J. Biol. Chem.
271
12737-12743
1996
Escherichia coli, Rattus norvegicus
brenda
Cobb, J.A.; Roberts, D.M.
Structural requirements for N-trimethylation of lysine 115 of calmodulin
J. Biol. Chem.
275
18969-18975
2000
Escherichia coli
brenda
Magnani, R.; Dirk, L.M.; Trievel, R.C.; Houtz, R.L.
Calmodulin methyltransferase is an evolutionarily conserved enzyme that trimethylates Lys-115 in calmodulin
Nat. Commun.
1
43
2010
Homo sapiens, Rattus norvegicus
brenda
Banerjee, J.; Magnani, R.; Nair, M.; Dirk, L.M.; DeBolt, S.; Maiti, I.B.; Houtz, R.L.
Calmodulin-mediated signal transduction pathways in Arabidopsis are fine-tuned by methylation
Plant Cell
25
4493-4511
2013
Arabidopsis thaliana
brenda
Haziza, S.; Magnani, R.; Lan, D.; Keinan, O.; Saada, A.; Hershkovitz, E.; Yanay, N.; Cohen, Y.; Nevo, Y.; Houtz, R.L.; Sheffield, V.C.; Golan, H.; Parvari, R.
Calmodulin methyltransferase is required for growth, muscle strength, somatosensory development and brain function
PLoS Genet.
11
e1005388
2015
Mus musculus (Q3U2J5), Mus musculus
brenda
Magen, S.; Magnani, R.; Haziza, S.; Hershkovitz, E.; Houtz, R.; Cambi, F.; Parvari, R.
Human calmodulin methyltransferase: expression, activity on calmodulin, and Hsp90 dependence
PLoS ONE
7
e52425
2012
Homo sapiens (Q7Z624), Homo sapiens, Mus musculus (Q3U2J5), Mus musculus
brenda
Magnani, R.; Chaffin, B.; Dick, E.; Bricken, M.L.; Houtz, R.L.; Bradley, L.H.
Utilization of a calmodulin lysine methyltransferase co-expression system for the generation of a combinatorial library of post-translationally modified proteins
Protein Expr. Purif.
86
83-88
2012
Homo sapiens (Q7Z624)
brenda
Serre, N.B.C.; Sarthou, M.; Gigarel, O.; Figuet, S.; Corso, M.; Choulet, J.; Rofidal, V.; Alban, C.; Santoni, V.; Bourguignon, J.; Verbruggen, N.; Ravanel, S.
Protein lysine methylation contributes to modulating the response of sensitive and tolerant Arabidopsis species to cadmium stress
Plant Cell Environ.
43
760-774
2020
Arabidopsis thaliana
brenda
Cho, H.J.; Lee, D.J.; Yi, Y.S.
Anti-inflammatory activity of calmodulin-lysine N-methyltransferase through suppressing the caspase-11 non-canonical inflammasome
Immunobiology
228
152758
2023
Mus musculus (Q3U2J5)
brenda
Nandi, D.; Gain, H.; Paul, S.; Mitra, A.; Banerjee, J.
Bioinformatics analyses of rice calmodulin-lysine N-methyltransferases gene (OsCaM KMT) and characterization of its promoter from Oryza sativa L. sub sp. indica through transgenic approach
South Afr. J. Bot.
150
873-885
2022
Oryza sativa Japonica Group (Q10P78)
-
brenda