| + |
RPS6KA5 | down-regulates 
phosphorylation
|
Histone H2A |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265314 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15010469 |
We found that msk1 phosphorylated histone h2a on serine 1, and mutation of serine 1 to alanine blocked the inhibition of transcription by msk1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SLBP | up-regulates quantity by expression 
translation regulation
|
Histone H2A |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265374 |
|
|
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 |
| + |
NuA4 complex | down-regulates activity
acetylation
|
Histone H2A |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269287 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 14966270 |
NuA4 (for nucleosome acetyltransferase of H4) is a 12-subunit HAT complex responsible for acetylation of histone H4 and H2A N-terminal tails. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RNF168 | up-regulates quantity
ubiquitination
|
Histone H2A |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266784 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 31225475 |
L3MBTL2 links RNF8 and RNF168 in the DNA double strand break response. The protein kinase ATM phosphorylates L3MBTL2, which recruits it to the DNA lesion by promoting the interaction between MDC1 and L3MBTL2. L3MBTL2 is subsequently ubiquitinated by RNF8, which acts as a docking site for RNF168, thereby recruiting the ubiquitin ligase to the damage site. RNF168, in turn, ubiquitinates H2A-type histones to amplify the DNA damage response and recruit downstream DNA repair proteins for proper DSB signaling. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Histone H2A | form complex 
binding
|
Nucleosome |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265309 |
|
|
in vitro |
|
| pmid |
sentence |
| 21812398 |
The elemental repeating unit of chromatin is the nucleosome core particle (NCP), which consists of 146 base pairs of DNA wrapped in 1.65 left-handed superhelical turns around the histone octamer. The histone octamer comprises two each of the core histones, H2A, H2B, H3 and H4, which form two H2A/H2B dimers and an H3/H4 tetramer, respectively, in the NCP. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
Histone H2A | form complex
binding
|
Nucleosome_H3.1 variant |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267756 |
|
|
in vitro |
|
| pmid |
sentence |
| 21812398 |
The elemental repeating unit of chromatin is the nucleosome core particle (NCP), which consists of 146 base pairs of DNA wrapped in 1.65 left-handed superhelical turns around the histone octamer. The histone octamer comprises two each of the core histones, H2A, H2B, H3 and H4, which form two H2A/H2B dimers and an H3/H4 tetramer, respectively, in the NCP. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
USP16 | down-regulates activity
deubiquitination
|
Histone H2A |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277348 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17914355 |
Here we report the identification and functional characterization of the major deubiquitinase for histone H2A, Ubp-M (also called USP16). Ubp-M prefers nucleosomal substrates in vitro, and specifically deubiquitinates histone H2A but not H2B in vitro and in vivo. This study identifies the major deubiquitinase for histone H2A and demonstrates that H2A deubiquitination is critically involved in cell cycle progression and gene expression. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
KDM4C | down-regulates activity
demethylation
|
Histone H2A |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265315 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29207681 |
As one member of the Jumonji-C histone demethylase family, JMJD2C has the ability to demethylate tri- or di-methylated histone 3 and 2 in either K9 (lysine residue 9) or K36 (lysine residue 36) sites by an oxidative reaction, thereby affecting heterochromatin formation, genomic imprinting, X-chromosome inactivation, and transcriptional regulation of genes.JMJD2C has been proved to be a demethylase for H3K9 methylation, in the manner of catalyzing the demethylation of H3K9me3/me2 (the known repressive markers of gene regulation), a histone mark found in heterochromatin associated with euchromatic transcriptional silencing and heterochromatin formation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RING1 | down-regulates activity
ubiquitination
|
Histone H2A |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271417 |
|
|
Mus musculus |
MEF Cell |
| pmid |
sentence |
| 16359901 |
Polycomb group (PcG) proteins exist in at least two biochemically distinct protein complexes, the EED-EZH2 complex and the PRC1 complex, that respectively possess H3-K27 methyltransferase and H2A-K119 ubiquitin E3 ligase activities. How the enzymatic activities are regulated and what their role is in Hox gene silencing are not clear. Here, we demonstrate that Bmi-1 and Ring1A, two components of the PRC1 complex, play important roles in H2A ubiquitylation and Hox gene silencing. We show that both proteins positively regulate H2A ubiquitylation. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
RNF8 | up-regulates
ubiquitination
|
Histone H2A |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265313 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20551964 |
Rnf8 and ubc13 ubiquitylate h2a and h2ax, but other substrates probably exist. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Polycomb repressive complex 1 | down-regulates activity
ubiquitination
|
Histone H2A |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266815 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 25519132 |
Mechanism of transcriptional activation. PRC1 can monoubiquitinate H2AK119 through its RING1B component. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BRCC3 | down-regulates
deubiquitination
|
Histone H2A |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265312 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20656690 |
Brcc36 regulates the abundance of lys(63)-linked ubiquitin chains at chromatin and that one of its substrates is diubiquitinated histone h2a |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
Histone H2A