1.14.11.67: [histone H3]-trimethyl-L-lysine4 demethylase
This is an abbreviated version!
For detailed information about [histone H3]-trimethyl-L-lysine4 demethylase, go to the full flat file.
Word Map on EC 1.14.11.67
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1.14.11.67
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chromatin
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demethylases
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trimethylation
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polycomb
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x-linked
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pluripotency
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ccrcc
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methyltransferases
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intellectual
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self-renewal
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corepressors
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h3k4me2
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chip-seq
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x-inactivation
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histone-modifying
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corest
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prc1
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chromatin-modifying
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lys4
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nanog
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k-specific
- 1.14.11.67
- chromatin
- demethylases
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trimethylation
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polycomb
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x-linked
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pluripotency
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ccrcc
- methyltransferases
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intellectual
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self-renewal
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corepressors
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h3k4me2
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chip-seq
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x-inactivation
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histone-modifying
- corest
- prc1
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chromatin-modifying
- lys4
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nanog
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k-specific
Reaction
Synonyms
amine oxidase (flavin-containing) domain 1, AOF1, At2g34880, CG33182, CG33185, CG3654, dJARID2, dJARID2/CG3654, dJMJD2(1), dJMJD2(1)/CG15835, dJMJD2(2), dJMJD2(2)/CG33182, Fbxl10, GH09982, H3K4 demethylase, H3K4 demethylase lysine-specific demethylase 5A, H3K4 histone demethylase, H3K4me3 demethylase, H3K4me3 histone demethylase, H3K4me3-specific demethylase, H3K4me3/2 histone demethylase, H3K9 trimethyl demethylase, histone 3 lysine 4 demethylase, histone demethylase, histone H3 lysine 4 demethylase, histone H3 lysine-4 demethylase, histone H3-K4 demethylase, histone H3K4 demethylase, histone H3K4-specific demethylase, histone lysine demethylase, histone-H3K4-specific demethylase, Jarid1, Jarid1a, JARID1B, JARID1C, Jarid2, JaridB, Jhd2, Jhdm1b/Kdm2b, JMJ15, JMJ703, JmjC domain histone demethylase, JmjC domain-containing histone demethylation protein 3A, JmjC domain-containing histone demethylation protein 3b, JmjC+N, JmjC+N histone demethylase, JMJD2A, JMJD2A-tudor, JMJD2B, jumonji AT rich interactive domain 1B, jumonji AT-rich interactive domain 1B, Jumonji demethylase, KDM1, KDM1B, KDM2, KDM5, KDM5A, KDM5B, KDM5b/JARID1b, KDM5C, KDM5D, Lid, little imaginal discs, LSD1, lysine demethylase, lysine demethylase 5b, lysine demethylase 7, lysine-specific demethylase, lysine-specific demethylase 1, lysine-specific demethylase 5A, lysine-specific demethylase 5B, lysine-specific demethylase JMJ703, Lysine-specific demethylase SE14, More, Ndy1, Os03g0151300, PHD finger protein 8, PHF8, PKDM7B, PLU-1, PLU1, RB-binding protein 2, RBP2, RBR-2, retinoblastoma binding protein 2, SE14, SMCX, trimethylated lysine 4 of histone H3 demethylase
ECTree
1.14.11.67 [histone H3]-trimethyl-L-lysine4 demethylaseAdvanced search results
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results (Engineering
Engineering on EC 1.14.11.67 - [histone H3]-trimethyl-L-lysine4 demethylase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
A388P
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the mutant shows 14.4% of wild type activity with [histone H3]-N6,N6-dimethyl-L-lysine4 and 45.1% of wild type activity with [histone H3]-N6,N6,N6-trimethyl-L-lysine4
D328A
site-directed mutagenesis, a loss-of-function mutations in the PHD1 finger domain
D939R
the mutation increases the Kd of JMJD2A for H4K20me3 by about 200fold but does not markedly change the affinity for H3K4me3
D945R
the mutation increases the Kd of JMJD2A for H3K4me3 by about 200fold, but does not affect the interaction with H4K20me3
F642L
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the mutant shows 40.1% of wild type activity with [histone H3]-N6,N6-dimethyl-L-lysine4 and 71.6% of wild type activity with [histone H3]-N6,N6,N6-trimethyl-L-lysine4
H18G
the mutation increases the Kd for H3K4me3 by fivefold compared to the wild-type enzyme
H499A
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the mutant shows significantly reduced activity compared to the wild type enzyme
H514A
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the mutant shows no activity with [histone H3]-N6,N6-dimethyl-L-lysine4 and 2.0% of wild type activity with [histone H3]-N6,N6,N6-trimethyl-L-lysine4
L326W
site-directed mutagenesis, a loss-of-function mutations in the PHD1 finger domain
L731F
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the mutant shows 37.2% of wild type activity with [histone H3]-N6,N6-dimethyl-L-lysine4 and 48.1% of wild type activity with [histone H3]-N6,N6,N6-trimethyl-L-lysine4
N940R
the mutation does not perturb JMJD2A binding to H4K20me3 but decreases its affinity for H3K4me3 by about 46fold
T968A
the mutation does not appreciably alter the interaction of JMJD2A with either H3K4me3 or H4K20me3
T968R
the mutation does not appreciably alter the interaction of JMJD2A with either H3K4me3 or H4K20me3
W1502A
site-directed mutagenesis, a loss-of-function mutations in the PHD3 finger domain
Y751C
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the mutant shows 51.4% of wild type activity with [histone H3]-N6,N6-dimethyl-L-lysine4 and 56.6% of wild type activity with [histone H3]-N6,N6,N6-trimethyl-L-lysine4
Y942A
the mutation has no marked effect on the Kd of JMJD2A for H3K4me3 or H4K20me3
Y942R
the mutation has no marked effect on the Kd of JMJD2A for H3K4me3 or H4K20me3
E396A
site directed mutagenesis of a Fe2+ binding active site residue, inactive mutant, the mutation impairs the H3K4 demethylase activity of JMJ703 in tobacco cells
G376A
site directed mutagenesis, inactive mutant, the mutation impairs the H3K4 demethylase activity of JMJ703 in tobacco cells, the mutation impairs the H3K4 demethylase activity of JMJ703 in tobacco cells
H394A
site directed mutagenesis of a Fe2+ binding active site residue, inactive mutant
H482A
site directed mutagenesis of a Fe2+ binding active site residue, inactive mutant
K412A
site directed mutagenesis, the mutation abolishes the demethylation activity of H3K4 in all three methylation states
N496A
site directed mutagenesis, the mutant retains a residual activity to demethylate H3K4me2/3, the mutation impairs the H3K4 demethylase activity of JMJ703 in tobacco cells
Y321A
site directed mutagenesis decreases H3K4me1 demethylase activity but does not affect H3K4me2 and H3K4me3 demethylase activity
Y383A
site directed mutagenesis, the mutant retains a residual activity to demethylate H3K4me2, the mutation impairs the H3K4 demethylase activity of JMJ703 in tobacco cells
additional information
additional information
construction of JMJ15 T-DNA insertion mutants, phenotypes, overview
additional information
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construction of JMJ15 T-DNA insertion mutants, phenotypes, overview
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additional information
generation of a rbr-2(tm3141) mutant, expression of wild-type rbr-2 gene completely rescues the PVQ defects
additional information
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generation of a rbr-2(tm3141) mutant, expression of wild-type rbr-2 gene completely rescues the PVQ defects
additional information
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transgenic flies expressing inverted repeats of the CG11033 coding region under the influence of the UAS promoter are crossed with act5CGal4 flies. The presence of Gal4 leads to transcription of inverted repeats under the influence of UAS promoter bearing Gal4 binding sites. Flies bearing only the inverted repeats are used as a control. The expression of dsRNA arising out of transcription of inverted repeats brings about downregulation of CG11033. The mutants exhibit multiple nucleoli, which are smaller in size. Quantitative real time PCR analysis shows reduction of dKDM2 transcript level relative to tubulin mRNA level in RNAi knockdown larvae. Analysis of histone modifications in the dKDM2 RNAi knockdown mutants, overview
additional information
GH09982 (CG3654) corresponds to a truncated form missing part of the N-terminal region but carrying the complete C-terminal part containing the JmjN, JmjC and ARID domains (amino acid positions 1521 to 2351). Overexpression of CG3654 shows no significant effect on the levels of H3K4me3, H3K9me3, H3K27me3, H3K36me3 and H4K20me3
additional information
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GH09982 (CG3654) corresponds to a truncated form missing part of the N-terminal region but carrying the complete C-terminal part containing the JmjN, JmjC and ARID domains (amino acid positions 1521 to 2351). Overexpression of CG3654 shows no significant effect on the levels of H3K4me3, H3K9me3, H3K27me3, H3K36me3 and H4K20me3
additional information
internal deletion of the ARID and PHD1 domains has a negligible effect on in vitro enzymatic kinetics of the KDM5 family of enzymes
additional information
internal deletion of the ARID and PHD1 domains has a negligible effect on in vitro enzymatic kinetics of the KDM5 family of enzymes
additional information
internal deletion of the ARID and PHD1 domains has a negligible effect on in vitro enzymatic kinetics of the KDM5 family of enzymes
additional information
internal deletion of the ARID and PHD1 domains has a negligible effect on in vitro enzymatic kinetics of the KDM5 family of enzymes. Generation of a KDM5B(1-755)DELTAAP mutant by deleting ARID and PHD1 (AP) domains by connecting residues 100 and 363. The DELTAAP constructs represent the domain arrangement of the conventional Jumonji domain followed by a C-terminal helical zinc binding domain. Deletion of DELTAAP has no effect on kinetics of KDM5C
additional information
internal deletion of the ARID and PHD1 domains has a negligible effect on in vitro enzymatic kinetics of the KDM5 family of enzymes. Generation of a KDM5B(1-755)DELTAAP mutant by deleting ARID and PHD1 (AP) domains by connecting residues 100 and 363. The DELTAAP constructs represent the domain arrangement of the conventional Jumonji domain followed by a C-terminal helical zinc binding domain. Deletion of DELTAAP has no effect on kinetics of KDM5C
additional information
internal deletion of the ARID and PHD1 domains has a negligible effect on in vitro enzymatic kinetics of the KDM5 family of enzymes. Generation of a KDM5B(1-755)DELTAAP mutant by deleting ARID and PHD1 (AP) domains by connecting residues 100 and 363. The DELTAAP constructs represent the domain arrangement of the conventional Jumonji domain followed by a C-terminal helical zinc binding domain. Deletion of DELTAAP has no effect on kinetics of KDM5C
additional information
internal deletion of the ARID and PHD1 domains has a negligible effect on in vitro enzymatic kinetics of the KDM5 family of enzymes. Generation of a KDM5C(1-789)DELTAAP mutant by deleting ARID and PHD1 (AP) domains by connecting residues 100 and 363. The DELTAAP constructs represent the domain arrangement of the conventional Jumonji domain followed by a C-terminal helical zinc binding domain
additional information
internal deletion of the ARID and PHD1 domains has a negligible effect on in vitro enzymatic kinetics of the KDM5 family of enzymes. Generation of a KDM5C(1-789)DELTAAP mutant by deleting ARID and PHD1 (AP) domains by connecting residues 100 and 363. The DELTAAP constructs represent the domain arrangement of the conventional Jumonji domain followed by a C-terminal helical zinc binding domain
additional information
internal deletion of the ARID and PHD1 domains has a negligible effect on in vitro enzymatic kinetics of the KDM5 family of enzymes. Generation of a KDM5C(1-789)DELTAAP mutant by deleting ARID and PHD1 (AP) domains by connecting residues 100 and 363. The DELTAAP constructs represent the domain arrangement of the conventional Jumonji domain followed by a C-terminal helical zinc binding domain
additional information
siRNA-mediated knockdown of KDM5A, and CHD4 or SIN3B in HeLa cells, and analysis of the changes in gene expression by microarray analysis. At least 435 genes (corresponding to 468 probes) are dysregulated in the KDM5A-knockdown cells. 66 and 63% of the KDM5A-regulated genes are also dysregulated in CHD4-and SIN3B-knockdown cells, respectively, and 47% of the KDM5A-regulated genes are affected by either CHD4 or SIN3B knockdown. Among the 435 KDM5A-regulated genes, 40% are upregulated, although more than half are downregulated. A similar proportion of genes is downregulated in response to SIN3B knockdown
additional information
the enzyme is knocked out by expression of specific siRNA for LSD1 in chondrocytes
additional information
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the enzyme is knocked out by expression of specific siRNA for LSD1 in chondrocytes
additional information
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transient overexpression of KDM5b in embryonic stem cells decreases the expression of at least three different modulators of cell fate decisions, Egr1, p27KIP1, and BMI1, by demethylation of their promoters. Constitutively increased KDM5b expression results in an increased mitotic rate and a decreased global 3meH3K4 but no change in cell identity
additional information
RBP2 enzyme knockout by transfection of siRNA, that targets Rbp2, into Piasy+/+ MEFs
additional information
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RBP2 enzyme knockout by transfection of siRNA, that targets Rbp2, into Piasy+/+ MEFs
additional information
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Ndy1 knockdown by siRNA in fibroblasts. Significant reduction in K36-dimethylated histone H3 associated with the promoters of Nqo1 and Prdx4 genes in cells engineered to overexpress Ndy1 but not its CXXC deletion mutant. Trimethylation of histone H3 at K4 is also reduced in the promoter regions of both genes, though in a spatially restricted manner that spared the region near the transcription start site. But the effect of Ndy1 on histone H3K4 trimethylation is weak
additional information
T-DNA insertion and RNAi mutation sof gene JMJ703, phenotypes, overview
additional information
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T-DNA insertion and RNAi mutation sof gene JMJ703, phenotypes, overview
additional information
generation of Se14-deficient mutant line HS112, an early flowering time mutant, Diurnal expression of flowering time genes in the wild-type and HS112, overview
additional information
overexpression of JMJ703-YFP-HA reduces the levels of H3K4me3/2/1 in vivo. T-DNA insertion disruption of JMJ703 transcription, four of the validated target genes show the decreased CpG methylation at their 5' regions with the increased H3K4me3 in the mutant compared with wild-type. Loss-of-function mutant jmj703 derepresses thousands of genes, especially those involved in chromatin assembly. Mutant jmj703 displays pleiotropic defects that could be due to ectopic expression or upregulation of direct targets of JMJ703
additional information
generation of an enzyme mutant jhd2DELTA, jhd2DELTA profoundly enhances rDNA silencing. Overexpression of wild-type Jhd2 significantly reduces H3K4me3 levels, whereas overexpression of jhd2-H427A has little effect on H3K4me3
additional information
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generation of an enzyme mutant jhd2DELTA, jhd2DELTA profoundly enhances rDNA silencing. Overexpression of wild-type Jhd2 significantly reduces H3K4me3 levels, whereas overexpression of jhd2-H427A has little effect on H3K4me3
additional information
generation of enzyme mutant Jhd2DELTA MSY724 cells
additional information
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generation of enzyme mutant Jhd2DELTA MSY724 cells
