Gene Ontology annotation through association of InterPro records with GO terms
Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Gene Ontology annotation based on curation of immunofluorescence data
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
huASH1 protein, a putative transcription factor encoded by a human homologue of the Drosophila ash1 gene, localizes to both nuclei and cell-cell tight junctions.
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Human ASH1L immunostaining supports intranuclear speckles and an additional tight-junction pool; the latter does not establish an adhesion-signaling function.
"the protein is distributed in intranuclear
speckles, and unexpectedly also in intercellular junctions."
Crystal structure of the human histone methyltransferase ASH1L catalytic domain and its implications for the regulatory mechanism.
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The human catalytic domain has a post-SET autoinhibitory loop and H3K36 specificity. The separately accessed Figure 3 caption assigns additional trimethylation to hyperactive Q2265A, which must be distinguished from ordinary ASH1L.
"human ASH1L specifically
methylates histone H3 Lys-36."
Screen identifies bromodomain protein ZMYND8 in chromatin recognition of transcription-associated DNA damage that promotes homologous recombination.
Kinetic characterization of human histone H3 lysine 36 methyltransferases, ASH1L and SETD2.
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Human ASH1L methylates recombinant nucleosomal H3K36 to mono- and dimethylated products; K36A loses activity, H3K4 is not a substrate, and only SETD2 trimethylates under the tested conditions.
"both enzymes mono- and dimethylate
H3K36 and are inactive with H3K4 as substrate"
WHSC1 (KMT3G), NSD1 (KMT3B), SMYD2 (KMT3C) methylate lysine-37 of histone H3 (H3K36)
WHSC1 (KMT3G), NSD1 (KMT3B), SMYD2 (KMT3C), ASH1L methylate methyl-lysine-37 of histone H3 (H3K36)
Mammalian ASH1L is a histone methyltransferase that occupies the transcribed region of active genes.
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Historical human/mammalian ASH1L experiments report H3K4 catalytic activity as well as active-gene chromatin occupancy. The catalytic substrate assignment conflicts with later human K36-specific assays.
"the SET
domain of ASH1L methylates H3K4 in vitro"
Prdm3 and Prdm16 are H3K9me1 methyltransferases required for mammalian heterochromatin integrity.
Histone methyltransferase Ash1l suppresses interleukin-6 production and inflammatory autoimmune diseases by inducing the ubiquitin-editing enzyme A20.
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Mouse macrophage experiments report Ash1l-dependent H3K4 methylation and A20/Tnfaip3 regulation. Their constructs and readouts remain to be reconciled with human K36-specific assays.
"Ash1l enhanced A20 expression
through induction of H3K4 modification at the Tnfaip3 promoter"
Structure-function relationship of ASH1L and histone H3K36 and H3K4 methylation.
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Human ASH1L PHD reads H3K4me2/3, neighboring BD/BAH regions bind DNA, and recombinant catalytic constructs produce H3K36 mono-/dimethylation. Mouse ES differentiation and reanalyzed human MV4-11 occupancy are separate experimental systems.
"ASH1LPHD recognizes H3K4me2/3,
whereas the neighboring ASH1LBD and ASH1LBAH have DNA binding activities."