| + |
MSL acetyltransferase | down-regulates activity 
monoubiquitination
|
H2BC11 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271980 |
Lys35 |
KKRKRSRkESYSIYV |
Homo sapiens |
|
| 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 |
| + |
H2BC11 | form complex 
binding
|
Nucleosome_H3.3 variant |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263875 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15776021 |
Variant histone H3.3 is incorporated into nucleosomes by a mechanism that does not require DNA replication and has also been implicated as a potential mediator of epigenetic memory of active transcriptional states. In this study, we have used chromatin immunoprecipitation analysis to show that H3.3 is found mainly at the promoters of transcriptionally active genes. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SLBP | up-regulates quantity by expression 
translation regulation
|
H2BC11 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265381 |
|
|
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 |
| + |
H2BC11 | form complex
binding
|
Nucleosome_H3.1t variant |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263727 |
|
|
in vitro |
|
| pmid |
sentence |
| 20498094 |
A histone H3 variant, H3T, is highly expressed in the testis, suggesting that it may play an important role in the chromatin reorganization required for meiosis and/or spermatogenesis. In the present study, we found that the nucleosome containing human H3T is significantly unstable both in vitro and in vivo, as compared to the conventional nucleosome containing H3.1. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
H2BC11 | form complex
binding
|
Nucleosome_H2A.Z.1 variant |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263716 |
|
|
in vitro |
|
| pmid |
sentence |
| 24311584 |
In the nucleosome, two of each of the histones H2A, H2B, H3 and H4 form the histone octamer and about 145–147 base pairs of DNA are wrapped around it . The histone H2A.Z variant is widely conserved among eukaryotes. Two isoforms, H2A.Z.1 and H2A.Z.2, have been identified in vertebrates and may have distinct functions in cell growth and gene expression. However, no structural differences between H2A.Z.1 and H2A.Z.2 have been reported. In the present study, the crystal structures of nucleosomes containing human H2A.Z.1 and H2A.Z.2 were determined. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
H2BC11 | form complex
binding
|
Nucleosome_H3.1 variant |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263720 |
|
|
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 |
| + |
H2BC11 | form complex
binding
|
CENP-A nucleosome |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263699 |
|
|
in vitro |
|
| pmid |
sentence |
| 23324462 |
In vitro assembly of both yeast and human CENP-A nucleosomes yields standard octameric structures containing two copies each of CENP-A, H2A, H2B and H4 histones. Human CENP-A also produces rigidified homotypic CENP-A/H4 tetramers in vitro. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
H2BC11 | form complex
binding
|
Nucleosome_H2A.Z.2 variant |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263710 |
|
|
in vitro |
|
| pmid |
sentence |
| 24311584 |
In the nucleosome, two of each of the histones H2A, H2B, H3 and H4 form the histone octamer and about 145–147 base pairs of DNA are wrapped around it . The histone H2A.Z variant is widely conserved among eukaryotes. Two isoforms, H2A.Z.1 and H2A.Z.2, have been identified in vertebrates and may have distinct functions in cell growth and gene expression. However, no structural differences between H2A.Z.1 and H2A.Z.2 have been reported. In the present study, the crystal structures of nucleosomes containing human H2A.Z.1 and H2A.Z.2 were determined. |
|
| Publications: |
1 |
Organism: |
In Vitro |
3.0
H2BC11
- 
- 