| + |
KAT2A | down-regulates activity 
acetylation
|
H3-5 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269600 |
Lys10 |
RTKQTARkSTGGKAP |
Homo sapiens |
|
| pmid |
sentence |
| 34811519 |
The HAT module within the SAGA and ADA complexes acetylates histone H3, mainly on residues K9 and K14. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269608 |
Lys15 |
ARKSTGGkAPRKQLA |
Homo sapiens |
|
| pmid |
sentence |
| 34811519 |
The HAT module within the SAGA and ADA complexes acetylates histone H3, mainly on residues K9 and K14. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
KAT2B | down-regulates activity
acetylation
|
H3-5 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269617 |
Lys10 |
RTKQTARkSTGGKAP |
Homo sapiens |
|
| pmid |
sentence |
| 34811519 |
The HAT module within the SAGA and ADA complexes acetylates histone H3, mainly on residues K9 and K14. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269625 |
Lys15 |
ARKSTGGkAPRKQLA |
Homo sapiens |
|
| pmid |
sentence |
| 34811519 |
The HAT module within the SAGA and ADA complexes acetylates histone H3, mainly on residues K9 and K14. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
KDM3A | up-regulates activity 
demethylation
|
H3-5 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276847 |
Lys10 |
RTKQTARkSTGGKAP |
Homo sapiens |
|
| pmid |
sentence |
| 16603237 |
Using a biochemical assay coupled with chromatography, we have purified a JmjC domain-containing protein, JHDM2A, which specifically demethylates mono- and dimethyl-H3K9. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SAGA complex | down-regulates activity
acetylation
|
H3-5 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269634 |
Lys10 |
RTKQTARkSTGGKAP |
Homo sapiens |
|
| pmid |
sentence |
| 34811519 |
The HAT module within the SAGA and ADA complexes acetylates histone H3, mainly on residues K9 and K14. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269642 |
Lys15 |
ARKSTGGkAPRKQLA |
Homo sapiens |
|
| pmid |
sentence |
| 34811519 |
The HAT module within the SAGA and ADA complexes acetylates histone H3, mainly on residues K9 and K14. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
SIRT7 | up-regulates activity
deacetylation
|
H3-5 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275873 |
Lys19 |
TGGKAPRkQLATKAA |
|
|
| pmid |
sentence |
| 22722849 |
SIRT7 links H3K18 deacetylation to maintenance of oncogenic transformation.|Genome-wide binding studies reveal that SIRT7 binds to promoters of a specific set of gene targets, where it deacetylates H3K18Ac and promotes transcriptional repression. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275879 |
Lys37 |
TPSTCGVkPHRYRPG |
|
|
| pmid |
sentence |
| 30653310 |
Besides confirming the previously reported histone H3K18 deacylation activity, our results revealed that SIRT7 has an astonishingly high activity to catalyze deacylation of H3K36 and is also catalytically active to deacylate H3K37. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275885 |
Lys38 |
K-->P |
|
|
| pmid |
sentence |
| 30653310 |
Besides confirming the previously reported histone H3K18 deacylation activity, our results revealed that SIRT7 has an astonishingly high activity to catalyze deacylation of H3K36 and is also catalytically active to deacylate H3K37. |
|
| Publications: |
3 |
| + |
Sin3B_complex | down-regulates activity
binding
|
H3-5 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266972 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 21041484 |
We report here the identification of a mammalian complex containing the corepressor Sin3B, the histone deacetylase HDAC1, Mrg15, and the PHD finger-containing Pf1 and show that this complex plays important roles in regulation of transcription. Sin3B, Pf1, Mrg15, and HDAC1 associate within a stable complex that binds H3K4me3/H3K36me3-enriched nucleosomes. We identify mammalian Pf1, a PHD finger protein, as a homologue of Rco1, and show that all four components, Sin3B, HDAC1, Mrg15, and Pf1, can form a stable complex, which is recruited downstream of the transcriptional start site through complex interactions with histones. these results indicate that the Pf1/Sin3B-containing complex is recruited at discrete sites within actively transcribed loci, likely through its interaction with H3K4me3/H3K36me3-enriched chromatin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SLBP | up-regulates quantity by expression
translation regulation
|
H3-5 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265420 |
|
|
Homo sapiens |
U2-OS Cell |
| pmid |
sentence |
| 19155325 |
Synthesis of mature histone mRNA requires only a single processing reaction: an endonucleolytic cleavage between a conserved stem-loop and a purine-rich downstream element to form the 3' end. The stem-loop binding protein (SLBP) is required for processing, and following processing, histone mRNA is transported to the cytoplasm, where SLBP participates in translation of the histone mRNA|We used radiolabeled probes generated by PCR targeting the open reading frame (ORF) to detect histones H2A, H2B, H3, H4, and H1 and used 7SK snRNA as a loading control (Fig. 2A). The abundance of histone H2A, H2B, H3, and H4 mRNAs is reduced to 37% to 70% of control levels in the SLBP knockdown cells when compared to the C2 control. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BAZ2B | down-regulates activity
binding
|
H3-5 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266621 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 31999386 |
The BAZ2B bromodomain has been shown to bind to acetylated H3K14 (H3K14ac), whose presence at promoter regions is generally associated with gene activation. This suggests a potential role for BAZ2B in transcriptional activation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
H3-5
- 
- 