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Information on EC 2.1.1.85 - protein-histidine N-methyltransferase
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2.1.1.85 protein-histidine N-methyltransferaseIUBMB Comments
Highly specific for histidine residues, for example, in actin.
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Synonyms
actin His73 nmethyltransferase, actin histidine methyltransferase, actin histidine-N3 methyltransferase, actin-specific histidine methyltransferase, actin-specific histidine N-methyltransferase, actin-specific methyltransferase, methyltransferase, protein (histidine), protein (actin) histidine MTase, protein methylase IV, S-adenosyl methionine:protein-histidine N-methyltransferase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
actin His73 nmethyltransferase
actin histidine methyltransferase
actin-specific histidine methyltransferase
-
-
-
-
methyltransferase, protein (histidine)
-
-
-
-
protein methylase IV
-
-
-
-
S-adenosyl methionine:protein-histidine N-methyltransferase
-
-
-
-
SET domain protein 3
setd3
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + protein L-histidine = S-adenosyl-L-homocysteine + protein Ntau-methyl-L-histidine
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
methyl group transfer
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-
-
-
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:protein-L-histidine N-tele-methyltransferase
Highly specific for histidine residues, for example, in actin.
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CAS REGISTRY NUMBER
COMMENTARY
108022-17-9
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + actin L-histidine73
S-adenosyl-L-homocysteine + actin Ntau-methyl-L-histidine73
S-adenosyl-L-methionine + beta-actin L-histidine73
S-adenosyl-L-homocysteine + beta-actin Ntau-methyl-L-histidine73
-
-
-
?
S-adenosyl-L-methionine + human beta-actin (residues 66-80)
S-adenosyl-L-homocysteine + human beta-actin (residues 66-80) Ntau-methyl-L-histidine
sequence TLKYPIEHGIVTNWD
-
-
?
S-adenosyl-L-methionine + human beta-actin L-histidine73
S-adenosyl-L-homocysteine + protein Ntau-methyl-L-histidine73
-
-
-
-
?
S-adenosyl-L-methionine + protein L-histidine
S-adenosyl-L-homocysteine + protein Ntau-methyl-L-histidine
S-adenosyl-L-methionine + protein L-histidine73
S-adenosyl-L-homocysteine + protein Ntau-methyl-L-histidine73
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-
-
-
?
S-adenosyl-L-methionine + synthetic peptide corresponding to residue 66-80 of actin
?
-
-
-
?
S-adenosyl-L-methionine + synthetic peptide corresponding to residue 66-88 of beta-actin
?
-
-
-
?
S-adenosyl-L-methionine + synthetic peptide corresponding to residue 69-77 of actin
S-adenosyl-L-homocysteine + peptide Ntau-methyl-L-histidine
S-adenosyl-L-methionine + actin L-histidine73
S-adenosyl-L-homocysteine + actin Ntau-methyl-L-histidine73
in a pre-reactive complex the enzyme binds the N3-protonated form of actin His73, and in a post-reactive product complex, the enzyme generates the methylated histidine in an N1-protonated and N3-methylated form
-
-
?
S-adenosyl-L-methionine + actin L-histidine73
S-adenosyl-L-homocysteine + actin Ntau-methyl-L-histidine73
-
-
-
?
S-adenosyl-L-methionine + actin L-histidine73
S-adenosyl-L-homocysteine + actin Ntau-methyl-L-histidine73
-
-
-
-
?
S-adenosyl-L-methionine + protein L-histidine
S-adenosyl-L-homocysteine + protein Ntau-methyl-L-histidine
-
-
-
-
?
S-adenosyl-L-methionine + protein L-histidine
S-adenosyl-L-homocysteine + protein Ntau-methyl-L-histidine
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chicken beta-actin expressed in E. coli as a fusion protein with 80 amino acids of an influenza protein, NS1
-
?
S-adenosyl-L-methionine + protein L-histidine
S-adenosyl-L-homocysteine + protein Ntau-methyl-L-histidine
-
naturally occuring actins are poor substrates, due to preexistent methylation at His 73
-
?
S-adenosyl-L-methionine + protein L-histidine
S-adenosyl-L-homocysteine + protein Ntau-methyl-L-histidine
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negligible activity with: bovine serum albumin, fibrinogen, casein, histone type IIA, gelatin, human gamma-globulin
-
?
S-adenosyl-L-methionine + protein L-histidine
S-adenosyl-L-homocysteine + protein Ntau-methyl-L-histidine
-
some activity with gluten
-
?
S-adenosyl-L-methionine + protein L-histidine
S-adenosyl-L-homocysteine + protein Ntau-methyl-L-histidine
-
specifically methylates histidine residues of actin
-
?
S-adenosyl-L-methionine + protein L-histidine
S-adenosyl-L-homocysteine + protein Ntau-methyl-L-histidine
-
specifically methylates histidine residues of actin
-
?
S-adenosyl-L-methionine + protein L-histidine
S-adenosyl-L-homocysteine + protein Ntau-methyl-L-histidine
-
-
-
-
?
S-adenosyl-L-methionine + synthetic peptide corresponding to residue 69-77 of actin
S-adenosyl-L-homocysteine + peptide Ntau-methyl-L-histidine
-
-
-
-
?
S-adenosyl-L-methionine + synthetic peptide corresponding to residue 69-77 of actin
S-adenosyl-L-homocysteine + peptide Ntau-methyl-L-histidine
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Tyr-Pro-Ile-Glu-His-Gly-Ile-Ile-Thr
-
-
?
additional information
?
-
the enzyme does not methylate histones and shows no activity on actin I71A/W79E double mutations
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-
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additional information
?
-
-
the enzyme does not methylate histones and shows no activity on actin I71A/W79E double mutations
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additional information
?
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the enzyme has weak lysine methylation activity on an actin peptide in which the target His73 is substituted by a L-lysine
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additional information
?
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no activity with histone H3 L-lysine4 (1-23), histone H3 L-lysine36 (25-47), and beta-actin (66-88) H73A mutant
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-
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additional information
?
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no activity with human beta-actin mutant H73A, ATP-bound actin or ADP-bound actin
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-
-
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + actin L-histidine73
S-adenosyl-L-homocysteine + actin Ntau-methyl-L-histidine73
S-adenosyl-L-methionine + beta-actin L-histidine73
S-adenosyl-L-homocysteine + beta-actin Ntau-methyl-L-histidine73
-
-
-
?
S-adenosyl-L-methionine + protein L-histidine
S-adenosyl-L-homocysteine + protein Ntau-methyl-L-histidine
-
-
-
-
?
S-adenosyl-L-methionine + protein L-histidine73
S-adenosyl-L-homocysteine + protein Ntau-methyl-L-histidine73
-
-
-
-
?
S-adenosyl-L-methionine + synthetic peptide corresponding to residue 69-77 of actin
S-adenosyl-L-homocysteine + peptide Ntau-methyl-L-histidine
-
-
-
-
?
S-adenosyl-L-methionine + actin L-histidine73
S-adenosyl-L-homocysteine + actin Ntau-methyl-L-histidine73
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-
-
?
S-adenosyl-L-methionine + actin L-histidine73
S-adenosyl-L-homocysteine + actin Ntau-methyl-L-histidine73
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-
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
reducing agents e.g. mercaptoethanol, required for activity, 4fold stimulation
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Carcinogenesis
SETD3 acts as a prognostic marker in breast cancer patients and modulates the viability and invasion of breast cancer cells.
Carcinoma
SETD3 acts as a prognostic marker in breast cancer patients and modulates the viability and invasion of breast cancer cells.
Neoplasms
[NSD3 suppresses LPS-triggered TNF-? production via promoting the dimethylation of histone H3K36 in macrophages].
Uterine Cervical Neoplasms
SETD3 reduces KLC4 expression to improve the sensitization of cervical cancer cell to radiotherapy.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000047
beta-actin L-histidine73
mutant enzyme N278A, at pH 7.2 and 37°C
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0.001115
beta-actin L-histidine73
mutant enzyme R316A, at pH 7.2 and 37°C
-
0.000305
beta-actin L-histidine73
mutant enzyme N256D, at pH 7.2 and 37°C
-
0.001087
beta-actin L-histidine73
mutant enzyme R215A, at pH 7.2 and 37°C
-
0.000449
beta-actin L-histidine73
mutant enzyme N256A, at pH 7.2 and 37°C
-
0.000502
beta-actin L-histidine73
wild type enzyme, at pH 7.2 and 37°C
-
0.000565
beta-actin L-histidine73
mutant enzyme R75A, at pH 7.2 and 37°C
-
0.000581
beta-actin L-histidine73
mutant enzyme Y313F, at pH 7.2 and 37°C
-
0.000784
beta-actin L-histidine73
mutant enzyme N256Q, at pH 7.2 and 37°C
-
0.000103
S-adenosyl-L-methionine
mutant enzyme N256Q, at pH 7.2 and 37°C
0.006543
S-adenosyl-L-methionine
mutant enzyme Y313F, at pH 7.2 and 37°C
0.000686
S-adenosyl-L-methionine
mutant enzyme N256A, at pH 7.2 and 37°C
0.000165
S-adenosyl-L-methionine
mutant enzyme R215A, at pH 7.2 and 37°C
0.000165
S-adenosyl-L-methionine
mutant enzyme N256D, at pH 7.2 and 37°C
0.000149
S-adenosyl-L-methionine
mutant enzyme R316A, at pH 7.2 and 37°C
0.006
synthetic peptide corresponding to residue 66-80 of actin
mutant enzyme N255A, at pH 10.5 and 37°C
-
0.0092
synthetic peptide corresponding to residue 66-80 of actin
mutant enzyme N255V, at pH 10.5 and 37°C
-
0.43
synthetic peptide corresponding to residue 66-80 of actin
wild type enzyme, at pH 10.5 and 37°C
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000017
beta-actin L-histidine73
mutant enzyme N278A, at pH 7.2 and 37°C
-
0.011
beta-actin L-histidine73
mutant enzyme N256Q, at pH 7.2 and 37°C
-
0.0035
beta-actin L-histidine73
mutant enzyme R215A, at pH 7.2 and 37°C
-
0.0029
beta-actin L-histidine73
mutant enzyme R316A, at pH 7.2 and 37°C
-
0.00097
beta-actin L-histidine73
mutant enzyme N256D, at pH 7.2 and 37°C
-
0.00052
beta-actin L-histidine73
mutant enzyme N256A, at pH 7.2 and 37°C
-
0.00037
beta-actin L-histidine73
mutant enzyme Y313F, at pH 7.2 and 37°C
-
0.000033
beta-actin L-histidine73
mutant enzyme R75A, at pH 7.2 and 37°C
-
0.000017
S-adenosyl-L-methionine
mutant enzyme N278A, at pH 7.2 and 37°C
0.0012
synthetic peptide corresponding to residue 66-80 of actin
mutant enzyme N255A, at pH 10.5 and 37°C
-
0.00036
synthetic peptide corresponding to residue 66-80 of actin
mutant enzyme N255V, at pH 10.5 and 37°C
-
0.00017
synthetic peptide corresponding to residue 66-80 of actin
wild type enzyme, at pH 10.5 and 37°C
-
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00036
synthetic peptide corresponding to residue 66-80 of actin
wild type enzyme, at pH 10.5 and 37°C
-
0.203
synthetic peptide corresponding to residue 66-80 of actin
mutant enzyme N255A, at pH 10.5 and 37°C
-
0.039
synthetic peptide corresponding to residue 66-80 of actin
mutant enzyme N255V, at pH 10.5 and 37°C
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
different fractions after ammonium sulfate precipitation
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
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
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
the enzyme plays important roles in hypoxic pulmonary hypertension, muscle differentiation, and carcinogenesis
malfunction
enzyme depletion impairs signal-induced contraction in primary uterine smooth muscle cells
malfunction
-
enzyme-deficient female mice have severely decreased litter sizes owing to primary maternal dystocia that is refractory to ecbolic induction agents
Show AA Sequence and Transmembrane Helices (1056 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme in complex with an actin peptide (residues 66-80) that contains His73 in the presence of S-adenosyl-L-homocysteine, hanging drop vapor diffusion method, using either 0.2 M ammonium acetate, 0.1 M sodium citrate tribasic dihydrate pH 5.6 and 30% (w/v) polyethylene glycol 4000, or 0.2 M ammonium sulfate or 0.2 M sodium chloride, 0.1 M Bis-Tris pH 5.5, 25% (w/v) polyethylene glycol 3350 and 0.1 M Bis-Tris pH 5.5, 25% (w/v) polyethylene glycol 3350
S-adenosyl-L-homocysteine-bound enzyme in complex with either an unmodified beta-actin peptide or its His-methylated variant, sitting drop vapor diffusion method, using 0.1 M sodium cacodylate trihydrate (pH 6.5), 0.2 M magnesium acetate tetrahydrate, and 20% (w/v) polyethylene glycol 8000
sitting drop vapor diffusion method, using 0.2 M ammonium acetate, 0.1 M sodium citrate tribasic dihydrate pH 5.6 and 30% (w/v) polyethylene glycol 4000
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
N255A
the mutant has increased lysine methylation activity and decreased histidine methylation activity compared to the wild type enzyme
N255V
the mutant has increased lysine methylation activity and decreased histidine methylation activity compared to the wild type enzyme
N256A
the mutant shows severely reduced activity compared to the wild type enzyme
N256D
the mutant shows severely reduced activity compared to the wild type enzyme
N256Q
the mutant shows about 50% activity compared to the wild type enzyme
N278A
the mutant shows severely reduced activity compared to the wild type enzyme
R215A
the mutant shows severely reduced activity compared to the wild type enzyme
R316A
the mutant shows severely reduced activity compared to the wild type enzyme
R75A
the mutant shows severely reduced activity compared to the wild type enzyme
Y313F
the mutant shows severely reduced activity compared to the wild type enzyme
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
2°C, 4 days, 75% loss of activity, no stabilization by mercaptoethanol or glycerol
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
DEAE-Sepharose column chromatography, Q-Sepharose column chromatography, phenyl Sepharose column chromatography, HiScreen Blue Sepharose column chromatography, Reactive Red 120 agarose column chromatography, and Superdex S200 gel filtration
-
glutathione Sepharose column chromatography and Ni-NTA agarose column chromatography
glutathione Sepharose column chromatography, HiTrap Q column chromatography, and Superdex S200 gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Raghavan, M.; Lindberg, U.; Schutt, C.
The use of alternative substrates in the characterization of actin-methylating and carnosine-methylating enzymes
Eur. J. Biochem.
210
311-318
1992
Oryctolagus cuniculus
brenda
Vijayasarathy, C.; Rao, B.S.N.
Partial purification and characterisation of S-adenosylmethionine:protein-histidine N-methyltransferase from rabbit skeletal muscle
Biochim. Biophys. Acta
923
156-165
1987
Oryctolagus cuniculus
brenda
Kwiatkowski, S.; Seliga, A.K.; Vertommen, D.; Terreri, M.; Ishikawa, T.; Grabowska, I.; Tiebe, M.; Teleman, A.A.; Jagielski, A.K.; Veiga-da-Cunha, M.; Drozak, J.
SETD3 protein is the actin-specific histidine N-methyltransferase
eLife
7
e37921
2018
Rattus norvegicus
brenda
Guo, Q.; Liao, S.; Kwiatkowski, S.; Tomaka, W.; Yu, H.; Wu, G.; Tu, X.; Min, J.; Drozak, J.; Xu, C.
Structural insights into SETD3-mediated histidine methylation on beta-actin
eLife
8
e43676
2019
Homo sapiens (Q86TU7)
brenda
Dai, S.; Horton, J.R.; Woodcock, C.B.; Wilkinson, A.W.; Zhang, X.; Gozani, O.; Cheng, X.
Structural basis for the target specificity of actin histidine methyltransferase SETD3
Nat. Commun.
10
3541
2019
Homo sapiens (Q86TU7)
brenda
Wilkinson, A.W.; Diep, J.; Dai, S.; Liu, S.; Ooi, Y.S.; Song, D.; Li, T.M.; Horton, J.R.; Zhang, X.; Liu, C.; Trivedi, D.V.; Ruppel, K.M.; Vilches-Moure, J.G.; Casey, K.M.; Mak, J.; Cowan, T.; Elias, J.E.; Nagamine, C.M.; Spudich, J.A.; Cheng, X.; Carette, J.E.; Gozani, O.
SETD3 is an actin histidine methyltransferase that prevents primary dystocia
Nature
565
372-376
2019
Homo sapiens (Q86TU7), Homo sapiens, Mus musculus
brenda
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