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Information on EC 1.14.11.53 - mRNA N6-methyladenine demethylase
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1.14.11.53 mRNA N6-methyladenine demethylaseIUBMB Comments
Contains iron(II). Catalyses oxidative demethylation of mRNA N6-methyladenine. The FTO enzyme from human can also demethylate N3-methylthymine from single stranded DNA and N3-methyluridine from single stranded RNA [1,2] with low activity .
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Word Map
- 1.14.11.53
-
demethylation
- demethylases
- mettl14
-
reader
-
writer
-
erasers
-
epitranscriptomic
-
ythdf1
-
m6a-related
-
hnrnpc
-
m6a-binding
-
igf2bp1
-
merip
-
m6a-dependent
-
methyltransferase-like
-
m6a-modified
The enzyme appears in viruses and cellular organisms
Reaction Schemes
N6-methyladenine in mRNA
+
+
=
adenine in mRNA
+
+
+
Synonyms
alkbh5, fat mass and obesity-associated protein, alkb homolog 5, m6a rna demethylase, alkbh5 demethylase, m6a mrna demethylase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ALKBH5
FTO
m6A RNA demethylase
ALKBH5
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
N6-methyladenine in mRNA + 2-oxoglutarate + O2 = adenine in mRNA + formaldehyde + succinate + CO2
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
mRNA-N6-methyladenosine,2-oxoglutarate:oxygen oxidoreductase (formaldehyde-forming)
Contains iron(II). Catalyses oxidative demethylation of mRNA N6-methyladenine. The FTO enzyme from human can also demethylate N3-methylthymine from single stranded DNA and N3-methyluridine from single stranded RNA [1,2] with low activity [3].
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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
5'-CUCGAUACG(m6A)UCCGGUCAAA-3' + 2-oxoglutarate + O2
5'-CUCGAUACGAUCCGGUCAAA-3' + formaldehyde + succinate + CO2
-
-
?
5'-UACACUCGAUCUGG(m6A)CUAAAGCUGCUC-3'-biotin + 2-oxoglutarate + O2
5'-UACACUCGAUCUGGCUAAAGCUGCUC-3'-biotin + formaldehyde + succinate + CO2
-
-
-
?
CCCC(m6A)CCCCCCCCC + 2-oxoglutarate + O2
? + formaldehyde + succinate + CO2
-
30% demethylation
-
?
GA(m6A)CA + 2-oxoglutarate + O2
GAACA + formaldehyde + succinate + CO2
-
39% demethylation
-
?
GCGG(m6A)CUCCAGAUG + 2-oxoglutarate + O2
GCGGACUCCAGAUG + formaldehyde + succinate + CO2
-
31% demethylation
-
?
GG(m6A)CU + 2-oxoglutarate + O2
GGACU + formaldehyde + succinate + CO2
-
37% demethylation
-
?
N3-methylcytosine in single-stranded DNA + 2-oxoglutarate + O2
cytosine in single-stranded DNA + formaldehyde + succinate + CO2
N3-methylthymine in single-stranded DNA + 2-oxoglutarate + O2
thymine in single-stranded DNA + formaldehyde + succinate + CO2
N3-methyluracil in single-stranded mRNA + 2-oxoglutarate + O2
uracil in single-stranded mRNA + formaldehyde + succinate + CO2
N6-methyladenine in mRNA + 2-oxoglutarate + O2
adenine in mRNA + formaldehyde + succinate + CO2
N6-methyladenine in NANOG mRNA + 2-oxoglutarate + O2
adenine in NANOG mRNA + formaldehyde + succinate + CO2
-
-
-
?
N6-methyladenine in single-stranded DNA + 2-oxoglutarate + O2
adenine in single-stranded DNA + formaldehyde + succinate + CO2
the ALKBH5 catalytic domain (residues 74–294) is active and can demethylate ssDNA and ssRNA with similar activity. m6A ssDNA may not be a physiologically relevant ALKBH5 substrate
-
?
N6-methyladenine in single-stranded DNA oligonucleotide + 2-oxoglutarate + O2
adenine in single-stranded DNA oligonucleotide + formaldehyde + succinate + CO2
-
-
?
N3-methylcytosine in single-stranded DNA + 2-oxoglutarate + O2
cytosine in single-stranded DNA + formaldehyde + succinate + CO2
strong preference toward N3-methylthymine over N3-methylcytosine in single-stranded DNA
-
?
N3-methylcytosine in single-stranded DNA + 2-oxoglutarate + O2
cytosine in single-stranded DNA + formaldehyde + succinate + CO2
strong preference toward N3-methylthymine over N3-methylcytosine in single-stranded DNA
-
?
N3-methylthymine in single-stranded DNA + 2-oxoglutarate + O2
thymine in single-stranded DNA + formaldehyde + succinate + CO2
strong preference toward N3-methylthymine over N3-methylcytosine in single-stranded DNA. Negligible activities against N3-methylthymine in double-stranded DNA
-
?
N3-methylthymine in single-stranded DNA + 2-oxoglutarate + O2
thymine in single-stranded DNA + formaldehyde + succinate + CO2
strong preference toward N3-methylthymine over N3-methylcytosine in single-stranded DNA. Negligible activities against N3-methylthymine in double-stranded DNA
-
?
N3-methyluracil in single-stranded mRNA + 2-oxoglutarate + O2
uracil in single-stranded mRNA + formaldehyde + succinate + CO2
2-fold preference for N3-methyluracil in single-stranded mRNA as the substrate over N3-methylthymine in single-stranded DNA. Slightly higher efficiency over that of N3-methylthymine in single-stranded DNA
-
?
N3-methyluracil in single-stranded mRNA + 2-oxoglutarate + O2
uracil in single-stranded mRNA + formaldehyde + succinate + CO2
2-fold preference for N3-methyluracil in single-stranded mRNA as the substrate over N3-methylthymine in single-stranded DNA. Slightly higher efficiency over that of N3-methylthymine in single-stranded DNA
-
?
N6-methyladenine in mRNA + 2-oxoglutarate + O2
adenine in mRNA + formaldehyde + succinate + CO2
-
-
?
N6-methyladenine in mRNA + 2-oxoglutarate + O2
adenine in mRNA + formaldehyde + succinate + CO2
-
-
-
?
N6-methyladenine in mRNA + 2-oxoglutarate + O2
adenine in mRNA + formaldehyde + succinate + CO2
-
-
?
N6-methyladenine in mRNA + 2-oxoglutarate + O2
adenine in mRNA + formaldehyde + succinate + CO2
-
-
?
N6-methyladenine in mRNA + 2-oxoglutarate + O2
adenine in mRNA + formaldehyde + succinate + CO2
-
-
-
?
N6-methyladenine in mRNA + 2-oxoglutarate + O2
adenine in mRNA + formaldehyde + succinate + CO2
m6A in nuclear RNA is the physiological substrate of the enzyme
-
?
N6-methyladenine in mRNA + 2-oxoglutarate + O2
adenine in mRNA + formaldehyde + succinate + CO2
-
m6A modification preferentially appears after G in the conserved motif RRm6ACH (R is A/G and H is A/C/U)
-
?
N6-methyladenine in mRNA + 2-oxoglutarate + O2
adenine in mRNA + formaldehyde + succinate + CO2
15-mer m6A-containing ssRNA or 15-mer m3U-containing ssRNA. Over 50-fold preference of the enzyme for m6A (at pH 7.0) over m3U (qat pH 6.0)
-
?
N6-methyladenine in mRNA + 2-oxoglutarate + O2
adenine in mRNA + formaldehyde + succinate + CO2
the ALKBH5 catalytic domain (residues 74–294) is active and can demethylate ssDNA and ssRNA with similar activity
-
?
N6-methyladenine in mRNA + 2-oxoglutarate + O2
adenine in mRNA + formaldehyde + succinate + CO2
-
-
?
additional information
?
-
very low activity toward repairing N1-methyladenine in 49 mer single-stranded DNA
-
?
additional information
?
-
negligible activity with m6A-containing dsDNA and dsRNA. Treatment with one molar equivalent of enzyme at 16°C overnight results in a demethylation yield of 40% for dsDNA and 24% for dsRNA, respectively
-
?
additional information
?
-
-
negligible activity with m6A-containing dsDNA and dsRNA. Treatment with one molar equivalent of enzyme at 16°C overnight results in a demethylation yield of 40% for dsDNA and 24% for dsRNA, respectively
-
?
additional information
?
-
-
the enzyme binds preferentially to pre-mRNAs in intronic regions, in the proximity of alternatively spliced exons and poly(A) sites
-
?
additional information
?
-
very low activity toward repairing N1-methyladenine in 49 mer single-stranded DNA
-
?
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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
N6-methyladenine in mRNA + 2-oxoglutarate + O2
adenine in mRNA + formaldehyde + succinate + CO2
N6-methyladenine in NANOG mRNA + 2-oxoglutarate + O2
adenine in NANOG mRNA + formaldehyde + succinate + CO2
-
-
-
-
?
additional information
?
-
-
the enzyme binds preferentially to pre-mRNAs in intronic regions, in the proximity of alternatively spliced exons and poly(A) sites
-
-
?
N6-methyladenine in mRNA + 2-oxoglutarate + O2
adenine in mRNA + formaldehyde + succinate + CO2
-
-
-
?
N6-methyladenine in mRNA + 2-oxoglutarate + O2
adenine in mRNA + formaldehyde + succinate + CO2
-
-
-
-
?
N6-methyladenine in mRNA + 2-oxoglutarate + O2
adenine in mRNA + formaldehyde + succinate + CO2
-
-
-
?
N6-methyladenine in mRNA + 2-oxoglutarate + O2
adenine in mRNA + formaldehyde + succinate + CO2
-
-
-
?
N6-methyladenine in mRNA + 2-oxoglutarate + O2
adenine in mRNA + formaldehyde + succinate + CO2
-
-
-
-
?
N6-methyladenine in mRNA + 2-oxoglutarate + O2
adenine in mRNA + formaldehyde + succinate + CO2
m6A in nuclear RNA is the physiological substrate of the enzyme
-
-
?
N6-methyladenine in mRNA + 2-oxoglutarate + O2
adenine in mRNA + formaldehyde + succinate + CO2
-
m6A modification preferentially appears after G in the conserved motif RRm6ACH (R is A/G and H is A/C/U)
-
-
?
N6-methyladenine in mRNA + 2-oxoglutarate + O2
adenine in mRNA + formaldehyde + succinate + CO2
-
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
Mn2+
the enzyme requires binding of the cosubstrate 2-oxoglutarate and Fe2+ for catalysis. In the crystallization trial, Fe2+ is replaced with Mn2+ to obtain a catalytically inactive form of the enzyme
Fe2+
the enzyme requires binding of the cosubstrate 2-oxoglutarate and Fe2+ for catalysis
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
the presence of S-adenosyl-L-homocysteine, NaCl, MgCl2, dimethylsulfoxide, and Triton X-100 does not influence enzyme activity
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00166
N6-methyladenine in mRNA
-
pH and temperature not specified in the publication
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0029
N6-methyladenine in mRNA
-
pH and temperature not specified in the publication
-
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.75
N6-methyladenine in mRNA
-
pH and temperature not specified in the publication
-
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6
demethylation of N3-methylthymine in single-stranded DNA and N3-methyluracil in single-stranded RNA
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20
21
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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
localised in nuclear speckles, which are subnuclear structures that are enriched in pre-messenger RNA splicing factors
brenda
localised in nuclear speckles, which are subnuclear structures that are enriched in pre-messenger RNA splicing factors
brenda
localised in nuclear speckles, which are subnuclear structures that are enriched in pre-messenger RNA splicing factors
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
malfunction
Alkbh5-deficient male mice have increased m6A in mRNA and are characterized by impaired fertility resulting from apoptosis that affects meiotic metaphase stage spermatocytes
malfunction
Alkbh5-deficient male mice have increased m6A in mRNA and are characterized by impaired fertility resulting from apoptosis that affects meiotic metaphase stage spermatocytes
malfunction
-
enzyme knockdown in MDAMB-231 human breast cancer cells significantly reduces their capacity for tumor initiation as a result of reduced numbers of breast cancer stem cells
metabolism
N6-methylation of adenosine is the most ubiquitous and abundant modification of nucleoside in eukaryotic mRNA and long non-coding RNA. This modification plays an essential role in the regulation of mRNA translation and RNA metabolism
metabolism
-
the enzyme enhances NANOG mRNA stability by catalyzing m6A demethylation
physiological function
-
enzyme expression promotes m6A RNA demethylation in hypoxic breast cancer cells
physiological function
-
the enzyme FTO plays a role in human obesity and energy utilization. FTO is involved in various diseases including cardiovascular diseases,Alzheimer's disease, type II diabetes, breast cancer, and end-stage renal disease. The enzyme ALKHB5 is involoved in sperm development
physiological function
-
the enzyme triggers inclusion of alternatively spliced exons and regulates expression of last exons
Show AA Sequence and Transmembrane Helices (324 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
in complex with manganese(II) and 2-oxoglutarate, sitting drop vapor diffusion method, using 0.2 M sodium iodide, pH 7.0, 20% (w/v) polyethylene glycol 3350
ALKBH566–292 is crystallized in sitting drops at 20°C by the vapour diffusion method in the presence of Mn2+ and (1-chloro-4-hydroxyisoquinoline-3-carbonyl)glycine. Crystallization drops contain 0.2 ml of a protein solution containing a final concentration of 10 mg/ml hexahistidine-tagged ALKBH566–292, 0.5 mM MnCl2 and 2 mM IOX3 mixed with 0.1 ml of well solution containing 125 mM potassium nitrate and 15% (w/v) polyethylene glycol 3350. Crystals (size 100 x 50 x 50 mM) appeared after 3 months. Crystals are harvested using nylon loops and cryoprotected using well solution diluted with 25% (v/v) glycerol and flashcooled in liquid nitrogen. Crystal structure of human ALKBH5 (residues 66-292) to 2.0 A resolution. ALKBH566–292 has a double-stranded beta-helix core fold. The active site metal is octahedrally coordinated by an HXD...H motif (comprising residues His204, Asp206 and His266) and three water molecules. ALKBH5 shares a nucleotide recognition lid and conserved active site residues with other ferrous iron-dependent nucleic acid oxygenase
crystallizations are performed at 24 and 4°C using both the hanging drop and sitting drop vapor diffusion methods. Five high resolution crystal structures of the catalytic core of Alkbh5 in complex with different ligands. These findings provide a structural basis for understanding the substrate recognition specificity of Alkbh5 and offer a foundation for selective drug design against AlkB members
hanging drop vapor diffusion method at 18 °C. The ALKBH5–2-oxoglutarate-Mn2+ is crystallized in a buffer containing 0.2 M ammonium dihydrogen phosphate, 20% PEG 3350. The ALKBH5 is crystallized with citrate in a buffer containing ammonium citrate, 20% PEG 3350. Before flashfreezing crystals in liquid nitrogen, crystals are soaked in a cryoprotectant consisting mother liquor plus 12% glycerol
hanging drop vapor diffusion method, using 0.2 M ammonium citrate dibasic pH 5.1, 20% (w/v) PEG 3350
-
hanging-drop vapour-diffusion method, crystal structure of FTO in complex with the mononucleotide 3-methylthymine
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
269A/Q271A
double mutation shows no impact on the repair efficiency of Alkbh5
F232D/Q233D/F234E
the mutant enzyme displays a severe loss of activity, demonstrating only 13.5% of wild-type activity
H231A/D233A
K231A/K235A
double mutation shows no impact on the repair capacity of Alkbh5
K231E/K235E
double mutation shows no impact on the repair capacity of Alkbh5
R316Q
mutation abolishes 80% of the wild-type activity towards m6A demethylation in vitro
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the purified recombinant mRNA N6-methyladenine demethylase appears to be more stable than the purified recombinant murine mRNA N6-methyladenine demethylase in vitro
the purified recombinant mRNA N6-methyladenine demethylase appears to be more stable than the purified recombinant murine mRNA N6-methyladenine demethylase in vitro
the purified recombinant mRNA N6-methyladenine demethylase appears to be more stable than the purified recombinant murine mRNA N6-methyladenine demethylase in vitro
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
DE52 column chromatography, Ni-NTA column chromatography, and Superdex 200 gel filtration
-
Ni affinity column chromatography, HiTrap Q column chromatography, and Superdex 75 gel filtration
-
Ni-NTA column chromatography, MonoS column chromatography, and Superdex 200 gel filtration
Ni-NTA His-Bind resin column chromatography, Source 15S column chromatography, and Superdex 200 gel filtration
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
a plasmid with the vector backbone pNIC28-Bsa4 encoding a hexahistidine-tagged ALKBH566–292 construct is transformed into Escherichia coli BL21 (DE3) cells
expression in Escherichia coli BL21 Star (DE3)
mutants of human Alkbh5 are amplified by PCR and subcloned into a modified pET-28a (Novagen) vector encoding a tobacco etch virus protease recognition site. The final clones are verified by DNA sequencing. All of the recombinant plasmids are transformed into Escherichia coli strain BL21(DE3)
the human ALKBH5 catalytic AlkB domain (residues 74–294) is subcloned into pET28a-MHL vector and expressed. The cloned vector is transformed into Escherichia coli BL21-V2R-pRARE2. Recombinant protein is produced at 16°C as an N-terminal His-tagged protein
Wild-type and various mutant enzymes cloned into pET-15b are expressed in Escherichia coli strain BL21
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
ALKBH5 mRNA levels are significantly increased under hypoxic conditions by greater than 1.6fold in SUM-159 and MDA-MB-435 cells and greater than 2fold in MDA-MB-231 and MCF-7 cells
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Jia, G.; Yang, C.G.; Yang, S.; Jian, X.; Yi, C.; Zhou, Z.; He, C.
Oxidative demethylation of 3-methylthymine and 3-methyluracil in single-stranded DNA and RNA by mouse and human FTO
FEBS Lett.
582
3313-3319
2008
Mus musculus (Q8BGW1), Homo sapiens (Q9C0B1)
brenda
Aik, W.; Scotti, J.S.; Choi, H.; Gong, L.; Demetriades, M.; Schofield, C.J.; McDonough, M.A.
Structure of human RNA N6-methyladenine demethylase ALKBH5 provides insights into its mechanisms of nucleic acid recognition and demethylation
Nucleic Acids Res.
42
4741-4754
2014
Homo sapiens (Q6P6C2), Homo sapiens
brenda
Zhou, B.; Han, Z.
Crystallization and preliminary X-ray diffraction of the RNA demethylase ALKBH5
Acta Crystallogr. Sect. F
69
1231-1234
2013
Homo sapiens
brenda
Zhu, C.; Yi, C.
Switching demethylation activities between AlkB family RNA/DNA demethylases through exchange of active-site residues
Angew. Chem. Int. Ed. Engl.
53
3659-3662
2014
Homo sapiens
brenda
Liu, K.; Ding, Y.; Ye, W.; Liu, Y.; Yang, J.; Liu, J.; Qi, C.
Structural and functional characterization of the proteins responsible for N6-methyladenosine modification and recognition
Curr. Protein Pept. Sci.
17
306-318
2016
Homo sapiens
brenda
Chen, W.; Zhang, L.; Zheng, G.; Fu, Y.; Ji, Q.; Liu, F.; Chen, H.; He, C.
Crystal structure of the RNA demethylase ALKBH5 from zebrafish
FEBS Lett.
588
892-898
2014
Danio rerio (Q08BA6), Danio rerio
brenda
Landfors, M.; Nakken, S.; Fusser, M.; Dahl, J.A.; Klungland, A.; Fedorcsak, P.
Sequencing of FTO and ALKBH5 in men undergoing infertility work-up identifies an infertility-associated variant and two missense mutations
Fertil. Steril.
105
1170-1179
2016
Homo sapiens
brenda
Feng, C.; Liu, Y.; Wang, G.; Deng, Z.; Zhang, Q.; Wu, W.; Tong, Y.; Cheng, C.; Chen, Z.
Crystal structures of the human RNA demethylase Alkbh5 reveal basis for substrate recognition
J. Biol. Chem.
289
11571-11583
2014
Homo sapiens (Q6P6C2), Homo sapiens
brenda
Xu, C.; Liu, K.; Tempel, W.; Demetriades, M.; Aik, W.; Schofield, C.J.; Min, J.
Structures of human ALKBH5 demethylase reveal a unique binding mode for specific single-stranded N6-methyladenosine RNA demethylation
J. Biol. Chem.
289
17299-17311
2014
Homo sapiens (Q6P6C2), Homo sapiens
brenda
Li, F.; Kennedy, S.; Hajian, T.; Gibson, E.; Seitova, A.; Xu, C.; Arrowsmith, C.H.; Vedadi, M.
A Radioactivity-based assay for screening human m6A-RNA methyltransferase, METTL3-METTL14 complex, and demethylase ALKBH5
J. Biomol. Screen.
21
290-297
2016
Homo sapiens
brenda
Shen, F.; Huang, W.; Huang, J.T.; Xiong, J.; Yang, Y.; Wu, K.; Jia, G.F.; Chen, J.; Feng, Y.Q.; Yuan, B.F.; Liu, S.M.
Decreased N6-methyladenosine in peripheral blood RNA from diabetic patients is associated with FTO expression rather than ALKBH5
J. Clin. Endocrinol. Metab.
100
E148-E154
2015
Homo sapiens
brenda
Zheng, G.
Dahl, J.A.; Niu, Y.; Fedorcsak, P.; Huang, C.M.; Li, C.J.; Vagbo, C.B.; Shi, Y.; Wang, W.L.; Song, S.H.; Lu, Z.; Bosmans, R.P.; Dai, Q.; Hao, Y.J.; Yang, X.; Zhao, W.M.; Tong, W.M.; Wang, X.J.; Bogdan, F.; Furu, K.; Fu, Y.; Jia, G.; Zhao, X.; Liu, J.; Krokan, H.E.; Klungland, A.; Yang, Y.G.; He, C.: ALKBH5 is a mammalian RNA demethylase that impacts RNA metabolism and mouse fertility
Mol. Cell
49
18-29
2013
Mus musculus (Q3TSG4), Mus musculus, Homo sapiens (Q6P6C2)
brenda
Jia, G.; Fu, Y.; Zhao, X.; Dai, Q.; Zheng, G.; Yang, Y.; Yi, C.; Lindahl, T.; Pan, T.; Yang, Y.G.; He, C.
N6-methyladenosine in nuclear RNA is a major substrate of the obesity-associated FTO
Nat. Chem. Biol.
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885-887
2011
Homo sapiens (Q9C0B1), Homo sapiens
brenda
Han, Z.; Niu, T.; Chang, J.; Lei, X.; Zhao, M.; Wang, Q.; Cheng, W.; Wang, J.; Feng, Y.; Chai, J.
Crystal structure of the FTO protein reveals basis for its substrate specificity
Nature
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1205-1209
2010
Homo sapiens (Q9C0B1)
brenda
Huang, Y.; Yan, J.; Li, Q.; Li, J.; Gong, S.; Zhou, H.; Gan, J.; Jiang, H.; Jia, G.F.; Luo, C.; Yang, C.G.
Meclofenamic acid selectively inhibits FTO demethylation of m6A over ALKBH5
Nucleic Acids Res.
43
373-384
2015
Homo sapiens (Q6P6C2), Homo sapiens
brenda
Zhang, C.; Samanta, D.; Lu, H.; Bullen, J.W.; Zhang, H.; Chen, I.; He, X.; Semenza, G.L.
Hypoxia induces the breast cancer stem cell phenotype by HIF-dependent and ALKBH5-mediated m6A-demethylation of NANOG mRNA
Proc. Natl. Acad. Sci. USA
113
E2047-E2056
2016
Homo sapiens
brenda
Zou, S.; Toh, J.D.; Wong, K.H.; Gao, Y.G.; Hong, W.; Woon, E.C.
N6-methyladenosine: a conformational marker that regulates the substrate specificity of human demethylases FTO and ALKBH5
Sci. Rep.
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2016
Homo sapiens
brenda
Chandola, U.; Das, R.; Panda, B.
Role of the N6-methyladenosine RNA mark in gene regulation and its implications on development and disease
Brief. Funct. Genomics
14
169-179
2015
Homo sapiens
brenda
Liu, K.; Ding, Y.; Ye, W.; Liu, Y.; Yang, J.; Liu, J.; Qi, C.
Structural and functional characterization of the proteins responsible for N6-methyladenosine modification and recognition
Curr. Protein Pept. Sci.
17
306-318
2015
Homo sapiens
brenda
Ye, F.; Zhang, L.; Jin, L.; Zheng, M.; Jiang, H.; Luo, C.
Repair of methyl lesions in RNA by oxidative demethylation
MedChemComm
5
1797-1803
2014
Homo sapiens
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brenda
Bartosovic, M.; Molares, H.C.; Gregorova, P.; Hrossova, D.; Kudla, G.; Vanacova, S.
N6-methyladenosine demethylase FTO targets pre-mRNAs and regulates alternative splicing and 3-end processing
Nucleic Acids Res.
45
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2017
Homo sapiens
brenda
Berulava, T.; Rahmann, S.; Rademacher, K.; Klein-Hitpass, L.; Horsthemke, B.
N6-adenosine methylation in miRNAs
PLoS ONE
10
e0118438
2015
Homo sapiens
brenda
Yang, Y.; Huang, W.; Huang, J.T.; Shen, F.; Xiong, J.; Yuan, E.F.; Qin, S.S.; Zhang, M.; Feng, Y.Q.; Yuan, B.F.; Liu, S.M.
Increased N6-methyladenosine in human sperm RNA as a risk factor for asthenozoospermia
Sci. Rep.
6
24345
2016
Homo sapiens
brenda
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