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3 S-adenosyl-L-methionine + a [histone H3]-L-lysine79
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine79
S-adenosyl-L-methionine + a [histone H3]-L-lysine79
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine79
S-adenosyl-L-methionine + a [histone H3]-N6,N6-dimethyl-L-lysine79
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine79
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine79
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine79
S-adenosyl-L-methionine + histone 3(K79)
?
-
-
-
-
?
S-adenosyl-L-methionine + histone H3(K76)
?
S-adenosyl-L-methionine + histone H3(K79)
?
-
-
-
-
?
S-adenosyl-L-methionine + histone L-lysine
S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine
-
-
-
-
?
S-adenosyl-L-methionine + [histone H3]-L-lysine79
S-adenosyl-L-homocysteine + [histone H3]-N6-methyl-L-lysine79
-
-
-
-
?
S-adenosyl-L-methionine + [histone H3]-N6-methyl-L-lysine79
S-adenosyl-L-homocysteine + [histone H3]-N6,N6-dimethyl-L-lysine79
-
-
-
-
?
additional information
?
-
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine79
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine79
overall reaction
-
-
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine79
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine79
-
overall reaction
-
-
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine79
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine79
overall reaction
-
-
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine79
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine79
-
overall reaction
-
-
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine79
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine79
overall reaction
-
-
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine79
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine79
-
overall reaction
-
-
?
S-adenosyl-L-methionine + a [histone H3]-L-lysine79
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine79
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-L-lysine79
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine79
-
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-L-lysine79
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine79
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-L-lysine79
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine79
-
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-L-lysine79
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine79
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-L-lysine79
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine79
-
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6,N6-dimethyl-L-lysine79
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine79
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6,N6-dimethyl-L-lysine79
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine79
-
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6,N6-dimethyl-L-lysine79
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine79
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6,N6-dimethyl-L-lysine79
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine79
-
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6,N6-dimethyl-L-lysine79
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine79
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6,N6-dimethyl-L-lysine79
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine79
-
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine79
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine79
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine79
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine79
-
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine79
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine79
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine79
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine79
-
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine79
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine79
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine79
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine79
-
-
-
-
?
S-adenosyl-L-methionine + histone H3(K76)
?
-
-
-
-
?
S-adenosyl-L-methionine + histone H3(K76)
?
-
-
-
-
?
additional information
?
-
-
mDot1a directly or indirectly associates with and hypermethylated histone H3 K79 at specific portions of the ENaCalpha 5'-flanking region, inducing a local alteration of the chromatin structure that facilitates ENaCalpha mRNA expression
-
-
?
additional information
?
-
-
AF10 bound to the enzyme simultaneously senses unmodified histone H3 lysine 27 via its PHD finger-Zn knuckle-PHD finger domain and enables the enzyme to methylate histone H3 at lysine 79. Knockout embryos, lacking Af10, have reduced [histone H3]-N6-methyl-L-lysine79 in developing nasal processes and reduced expression of AP2alpha, a gene required for cranial neural crest cell development
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine79
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine79
S-adenosyl-L-methionine + a [histone H3]-L-lysine79
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine79
S-adenosyl-L-methionine + a [histone H3]-N6,N6-dimethyl-L-lysine79
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine79
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine79
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine79
S-adenosyl-L-methionine + histone L-lysine
S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine
-
-
-
-
?
S-adenosyl-L-methionine + [histone H3]-L-lysine79
S-adenosyl-L-homocysteine + [histone H3]-N6-methyl-L-lysine79
-
-
-
-
?
S-adenosyl-L-methionine + [histone H3]-N6-methyl-L-lysine79
S-adenosyl-L-homocysteine + [histone H3]-N6,N6-dimethyl-L-lysine79
-
-
-
-
?
additional information
?
-
-
AF10 bound to the enzyme simultaneously senses unmodified histone H3 lysine 27 via its PHD finger-Zn knuckle-PHD finger domain and enables the enzyme to methylate histone H3 at lysine 79. Knockout embryos, lacking Af10, have reduced [histone H3]-N6-methyl-L-lysine79 in developing nasal processes and reduced expression of AP2alpha, a gene required for cranial neural crest cell development
-
-
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine79
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine79
overall reaction
-
-
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine79
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine79
-
overall reaction
-
-
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine79
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine79
overall reaction
-
-
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine79
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine79
-
overall reaction
-
-
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine79
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine79
overall reaction
-
-
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine79
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine79
-
overall reaction
-
-
?
S-adenosyl-L-methionine + a [histone H3]-L-lysine79
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine79
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-L-lysine79
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine79
-
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-L-lysine79
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine79
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-L-lysine79
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine79
-
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-L-lysine79
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine79
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-L-lysine79
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine79
-
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6,N6-dimethyl-L-lysine79
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine79
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6,N6-dimethyl-L-lysine79
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine79
-
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6,N6-dimethyl-L-lysine79
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine79
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6,N6-dimethyl-L-lysine79
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine79
-
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6,N6-dimethyl-L-lysine79
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine79
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6,N6-dimethyl-L-lysine79
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine79
-
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine79
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine79
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine79
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine79
-
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine79
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine79
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine79
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine79
-
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine79
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine79
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine79
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine79
-
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
malfunction
-
failure to recruit Rad9 or Dot1 to histone H3 leads to an increase in Mec1 activation
malfunction
-
transcriptionally silent telomeric variant surface glycoproteins become partially derepressed when DOT1B is deleted, whereas nontelomeric loci are unaffected
malfunction
enzyme deletion impedes leukemia cell proliferation as well as switches exon skipping to the inclusion isoform in MLL-rearranged acute myeloid leukemia cell lines
malfunction
enzyme inhibition leads to increased sensitivity to chemotherapeutic agents and PARP inhibition
malfunction
-
enzyme knockdown enhances cell fusion and resorption activity in RAW264.7 osteoclastogenesis model. Enzyme inhibition enhances bone loss in ovariectomized mice
malfunction
enzyme knockdown reduces histone H3 lysine 79 methylation and N-Myc protein binding at the ODC1 and E2F2 gene promoters and reduces neuroblastoma cell proliferation
malfunction
-
enzyme knockdown severely retards the growth of the tadpoles and leads to tadpole lethality prior to metamorphosis
malfunction
-
transcriptionally silent telomeric variant surface glycoproteins become partially derepressed when DOT1B is deleted, whereas nontelomeric loci are unaffected
-
physiological function
-
Dot1 and Rad9 inhibit single-stranded DNA accumulation at DSBs and uncapped telomeres, Dot1 contributes to checkpoint activation in response to low levels of telomere uncapping but is not essential with high levels of uncapping, Rad9 contributes to DNA damage metabolism because Rad9 inhibits the accumulation of single stranded DNA at uncapped telomeres
physiological function
-
Dot1 is required for efficient sister chromatid recombination, Dot1 promotes DNA double-strand break-induced loading of cohesin onto chromatin
physiological function
-
DOT1B is required to maintain strict variant surface glycoproteins silencing and to ensure rapid transcriptional variant surface glycoproteins switching
physiological function
-
the gene grappa encoding a histone methyltransferase is required for normal lifespan and stress resistance, its overexpression increases stress resistance in Drosophila, without obvious induction of representative anti-oxidant genes
physiological function
-
Dot1 and histone H3(K79) methylation are required for global genomic repair in both nucleosomal core regions and internucleosomal linker DNA but the enzyme is entirely dispensable for transcription coupled repair
physiological function
enzyme-mediated histone H3 lysine 79 methylation likely functions in transcription via the recruitment of reader proteins which act directly or indirectly to affect RNA polymerase II activity. Aberrant transcriptional activation via histone H3 lysine 79 methylation by the enzyme is implicated in the development of leukemias
physiological function
enzyme-mediated methylation of [histone H3]-L-lysine79 is involved in the regulation of telomeric silencing, cell-cycle regulation, transcription elongation, DNA repair, cardiac function, embryonic development, erythropoiesis, and leukemia. Enzyme-mediated methylation of histone H3 lysine79 on the HOXA9 promoter contributes to increased expression of Hoxa9 in acute myeloid leukemia
physiological function
-
enzyme-mediated [histone H3]-N6,N6-dimethyl-L-lysine79 modification critically regulates gene expression during cardiomyocyte differentiation. DOTL1 is a key enzyme for cardiomyocyte differentiation and maturation
physiological function
-
the enzyme inhibits osteoclastogenesis and protects against osteoporosis
physiological function
the enzyme is necessary for C/EBPbeta to promote gene expression in ovarian cancer cells. The promotional effect of C/EBPbeta on cisplatin resistance of tumor cells is mediated by the enzyme
physiological function
the enzyme is required for mixed lineage leukemia-AF9 (MLL-AF9) leukemogenesis. The degree of enzyme recruitment to MLL-AF9 defines the level of hematopoietic transformation
physiological function
the enzyme is required for MYCN-amplified neuroblastoma cell proliferation
physiological function
the enzyme is the major regulator in mediating skipping exon in MLL-rearranged acute myeloid leukemia progression
physiological function
-
the enzyme plays an important role for tadpole growth and development prior to metamorphosis into a frog
physiological function
the enzyme plays an important role in an early DNA damage response and repair of DNA double-strand breaks via the homologous recombination pathway
physiological function
-
DOT1B is required to maintain strict variant surface glycoproteins silencing and to ensure rapid transcriptional variant surface glycoproteins switching
-
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Shanower, G.A.; Muller, M.; Blanton, J.L.; Honti, V.; Gyurkovics, H.; Schedl, P.
Characterization of the grappa gene, the Drosophila histone H3 lysine 79 methyltransferase
Genetics
169
173-184
2005
Drosophila melanogaster
brenda
Zhang, W.; Xia, X.; Jalal, D.I.; Kuncewicz, T.; Xu, W.; Lesage, G.D.; Kone, B.C.
Aldosterone-sensitive repression of ENaCalpha transcription by a histone H3 lysine-79 methyltransferase
Am. J. Physiol. Cell Physiol.
290
C936-C946
2006
Homo sapiens, Mus musculus
brenda
Lazzaro, F.; Sapountzi, V.; Granata, M.; Pellicioli, A.; Vaze, M.; Haber, J.E.; Plevani, P.; Lydall, D.; Muzi-Falconi, M.
Histone methyltransferase Dot1 and Rad9 inhibit single-stranded DNA accumulation at DSBs and uncapped telomeres
EMBO J.
27
1502-1512
2008
Saccharomyces cerevisiae
brenda
Conde, F.; Refolio, E.; Cordon-Preciado, V.; Cortes-Ledesma, F.; Aragon, L.; Aguilera, A.; San-Segundo, P.A.
The Dot1 histone methyltransferase and the Rad9 checkpoint adaptor contribute to cohesin-dependent double-strand break repair by sister chromatid recombination in Saccharomyces cerevisiae
Genetics
182
437-446
2009
Saccharomyces cerevisiae
brenda
List, O.; Togawa, T.; Tsuda, M.; Matsuo, T.; Elard, L.; Aigaki, T.
Overexpression of grappa encoding a histone methyltransferase enhances stress resistance in Drosophila
Hereditas
146
19-28
2009
Drosophila melanogaster
brenda
Figueiredo, L.M.; Janzen, C.J.; Cross, G.A.
A histone methyltransferase modulates antigenic variation in African trypanosomes
PLoS Biol.
6
e161
2008
Trypanosoma brucei, Trypanosoma brucei Lister 427
brenda
Tatum, D.; Li, S.
Evidence that the histone methyltransferase Dot1 mediates global genomic repair by methylating histone H3 on lysine 79
J. Biol. Chem.
286
17530-17535
2011
Saccharomyces cerevisiae
brenda
Wood, K.; Tellier, M.; Murphy, S.
DOT1L and H3K79 methylation in transcription and genomic stability
Biomolecules
8
E11
2018
Homo sapiens (Q8TEK3)
brenda
Wong, M.; Tee, A.E.L.; Milazzo, G.; Bell, J.L.; Poulos, R.C.; Atmadibrata, B.; Sun, Y.; Jing, D.; Ho, N.; Ling, D.; Liu, P.Y.; Zhang, X.D.; Huettelmaier, S.; Wong, J.W.H.; Wang, J.; Polly, P.; Perini, G.; Scarlett, C.J.; Liu, T.
The histone methyltransferase DOT1L promotes neuroblastoma by regulating gene transcription
Cancer Res.
77
2522-2533
2017
Homo sapiens (Q8TEK3)
brenda
Cattaneo, P.; Kunderfranco, P.; Greco, C.; Guffanti, A.; Stirparo, G.G.; Rusconi, F.; Rizzi, R.; Di Pasquale, E.; Locatelli, S.L.; Latronico, M.V.; Bearzi, C.; Papait, R.; Condorelli, G.
DOT1L-mediated H3K79me2 modification critically regulates gene expression during cardiomyocyte differentiation
Cell Death Differ.
23
555-564
2016
Mus musculus
brenda
Gao, Y.; Ge, W.
The histone methyltransferase DOT1L inhibits osteoclastogenesis and protects against osteoporosis
Cell Death Dis.
9
33
2018
Mus musculus
brenda
Kuntimaddi, A.; Achille, N.J.; Thorpe, J.; Lokken, A.A.; Singh, R.; Hemenway, C.S.; Adli, M.; Zeleznik-Le, N.J.; Bushweller, J.H.
Degree of recruitment of DOT1L to MLL-AF9 defines level of H3K79 di- and tri-methylation on target genes and transformation potential
Cell Rep.
11
808-820
2015
Homo sapiens (Q8TEK3), Homo sapiens
brenda
Kari, V.; Raul, S.K.; Henck, J.M.; Kitz, J.; Kramer, F.; Kosinsky, R.L.; Uebelmesser, N.; Mansour, W.Y.; Eggert, J.; Spitzner, M.; Najafova, Z.; Bastians, H.; Grade, M.; Gaedcke, J.; Wegwitz, F.; Johnsen, S.A.
The histone methyltransferase DOT1L is required for proper DNA damage response, DNA repair, and modulates chemotherapy responsiveness
Clin. Epigenetics
11
4-4
2019
Homo sapiens (Q8TEK3)
brenda
Evanno, E.; Godet, J.; Piccirilli, N.; Guilhot, J.; Milin, S.; Gombert, J.; Fouchaq, B.; Roche, J.
Tri-methylation of H3K79 is decreased in TGF-beta1-induced epithelial-to-mesenchymal transition in lung cancer
Clin. Epigenetics
9
80
2017
Homo sapiens (Q8TEK3)
brenda
Wen, L.; Fu, L.; Guo, X.; Chen, Y.; Shi, Y.B.
Histone methyltransferase Dot1L plays a role in postembryonic development in Xenopus tropicalis
FASEB J.
29
385-393
2015
Xenopus tropicalis
brenda
Jang, S.; Kang, C.; Yang, H.S.; Jung, T.; Hebert, H.; Chung, K.Y.; Kim, S.J.; Hohng, S.; Song, J.J.
Structural basis of recognition and destabilization of the histone H2B ubiquitinated nucleosome by the DOT1L histone H3 Lys79 methyltransferase
Genes Dev.
33
620-625
2019
Homo sapiens (Q8TEK3)
brenda
Li, T.; Liu, Q.; Garza, N.; Kornblau, S.; Jin, V.
Integrative analysis reveals functional and regulatory roles of H3K79me2 in mediating alternative splicing
Genome Med.
10
30
2018
Homo sapiens (Q8TEK3)
brenda
Valencia-Sanchez, M.I.; De Ioannes, P.; Wang, M.; Vasilyev, N.; Chen, R.; Nudler, E.; Armache, J.P.; Armache, K.J.
Structural basis of Dot1L stimulation by histone H2B lysine 120 ubiquitination
Mol. Cell
74
1010-1019
2019
Homo sapiens (Q8TEK3)
brenda
Farooq, Z.; Banday, S.; Pandita, T.; Altaf, M.
The many faces of histone H3K79 methylation
Mutat. Res. Rev. Mutat. Res.
768
46-52
2016
Saccharomyces cerevisiae (Q04089), Homo sapiens (Q8TEK3)
brenda
Liu, D.; Zhang, X.X.; Li, M.C.; Cao, C.H.; Wan, D.Y.; Xi, B.X.; Tan, J.H.; Wang, J.; Yang, Z.Y.; Feng, X.X.; Ye, F.; Chen, G.; Wu, P.; Xi, L.; Wang, H.; Zhou, J.F.; Feng, Z.H.; Ma, D.; Gao, Q.L.
C/EBPbeta enhances platinum resistance of ovarian cancer cells by reprogramming H3K79 methylation
Nat. Commun.
9
1739
2018
Homo sapiens (Q8TEK3)
brenda
Ogoh, H.; Yamagata, K.; Nakao, T.; Sandell, L.; Yamamoto, A.; Yamashita, A.; Tanga, N.; Suzuki, M.; Abe, T.; Kitabayashi, I.; Watanabe, T.; Sakai, D.
Mllt10 knockout mouse model reveals critical role of Af10-dependent H3K79 methylation in midfacial development
Sci. Rep.
7
11922
2017
Mus musculus
brenda