| + |
MSL acetyltransferase | down-regulates activity 
monoubiquitination
|
Histone H2B |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271978 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 21726816 |
MSL1/2 ubiquitylates histone H2B on K 34. Importantly, only mono-ubiquitylation of H2B by MSL1/2 was detected in cells (data not shown), suggesting that MSL1/2, like RNF20/RNF40, was mainly a mono-ubiquitylase under physiological conditions.the MOF-MSL complex functions to promote both H4 K16ac and H2B K34ub. H2B K34ub, in turn, promotes H2B K120ub, H3 K4me3 and K79me2 to facilitate transcription elongation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SLBP | up-regulates quantity by expression 
translation regulation
|
Histone H2B |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265375 |
|
|
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 |
| + |
BAF250b E3 ligase | down-regulates activity
ubiquitination
|
Histone H2B |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271441 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 20086098 |
In the present work, we show that BAF250 associates with elongin C (Elo C), cullin 2 (Cul2), and Roc1 to form an E3 ubiquitin ligase. BAF250 forms an E3 ubiquitin ligase with Elo B/C, Cul2, and Roc1 that targets histone H2B. H2B-Ub has been shown to be required for transcriptional activation in vitro |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Histone H2B | up-regulates
binding
|
RNF168 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265372 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19203578 |
Rnf168 is recruited to sites of dna damage by binding to ubiquitylated histone h2a. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ARID1B | down-regulates activity
ubiquitination
|
Histone H2B |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271442 |
|
|
in vitro |
|
| pmid |
sentence |
| 20086098 |
The immunopurified BAF250b E3 ubiquitin ligase was found to target histone H2B at lysine 120 for monoubiquitination in vitro. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
Histone H2B | form complex 
binding
|
Nucleosome |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265310 |
|
|
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 |
3.0
Histone H2B