| + |
HAT1 | down-regulates activity 
acetylation
|
H4C1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264790 |
Lys13 |
KGGKGLGkGGAKRHR |
in vitro |
|
| pmid |
sentence |
| 28143904 |
Histone acetyltransferase 1 is the founding member of the histone acetyltransferase superfamily and catalyzes lysine acetylation of newly synthesized histone H4|Lys12 for direct attack of the acetyl group of the cofactor.| It is postulated that histone acetylation, through charge neutralization of the cationic histone tails, weakens nucleosomal electrostatic interactions with anionic DNA, thus destabilizing internucleosomal contacts and nucleosomal structure and facilitating access to the promoter region for RNA polymerase and transcription factors. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264791 |
Lys6 |
kGGKGLGK |
in vitro |
|
| pmid |
sentence |
| 11585814 |
During nucleosome assembly in vivo, newly synthesized histone H4 is specifically diacetylated on lysines 5 and 12 within the H4 NH(2)-terminal tail domain. The highly conserved "K5/K12" deposition pattern of acetylation is thought to be generated by the Hat1 histone acetyltransferase, which in vivo is found in the HAT-B complex. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
MSL acetyltransferase | down-regulates activity
acetylation
|
H4C1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263944 |
Lys17 |
GLGKGGAkRHRKVLR |
Homo sapiens |
|
| pmid |
sentence |
| 16227571 |
We describe a stable, multisubunit human histone acetyltransferase complex (hMSL) that contains homologs of the Drosophila dosage compensation proteins MOF, MSL1, MSL2, and MSL3. This complex shows strong specificity for histone H4 lysine 16 in chromatin in vitro, and RNA interference-mediated knockdown experiments reveal that it is responsible for the majority of H4 acetylation at lysine 16 in the cell. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NSL histone acetyltransferase | down-regulates activity
acetylation
|
H4C1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267166 |
Lys17 |
GLGKGGAkRHRKVLR |
Homo sapiens |
|
| pmid |
sentence |
| 20018852 |
Here we report an analysis of the subunit composition and substrate specificity of the NSL complex. Proteomic analyses of complexes purified through multiple candidate subunits reveal that NSL is composed of nine subunits. by comparing the substrate specificities of the MSL and NSL complexes, we obtain evidence that MOF HAT activity is differentially regulated by assembly into the MSL complex, where it acetylates nucleosomal histone H4 on lysine 16, and the NSL complex, where it also acetylates nucleosomal histone H4 on lysines 5 and 8. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267167 |
Lys6 |
kGGKGLGK |
Homo sapiens |
|
| pmid |
sentence |
| 20018852 |
Here we report an analysis of the subunit composition and substrate specificity of the NSL complex. Proteomic analyses of complexes purified through multiple candidate subunits reveal that NSL is composed of nine subunits. by comparing the substrate specificities of the MSL and NSL complexes, we obtain evidence that MOF HAT activity is differentially regulated by assembly into the MSL complex, where it acetylates nucleosomal histone H4 on lysine 16, and the NSL complex, where it also acetylates nucleosomal histone H4 on lysines 5 and 8. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267168 |
Lys9 |
SGRGKGGkGLGKGGA |
Homo sapiens |
|
| pmid |
sentence |
| 20018852 |
Here we report an analysis of the subunit composition and substrate specificity of the NSL complex. Proteomic analyses of complexes purified through multiple candidate subunits reveal that NSL is composed of nine subunits. by comparing the substrate specificities of the MSL and NSL complexes, we obtain evidence that MOF HAT activity is differentially regulated by assembly into the MSL complex, where it acetylates nucleosomal histone H4 on lysine 16, and the NSL complex, where it also acetylates nucleosomal histone H4 on lysines 5 and 8. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
KMT5B | down-regulates activity
methylation
|
H4C1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266651 |
Lys21 |
GGAKRHRkVLRDNIQ |
in vitro |
|
| pmid |
sentence |
| 24396869 |
SUV420H1 and SUV420H2 are two highly homologous enzymes that methylate lysine 20 of histone H4 (H4K20), a mark that has been implicated in transcriptional regulation. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
KAT5 | down-regulates activity
acetylation
|
H4C1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262061 |
Lys21 |
GGAKRHRkVLRDNIQ |
Homo sapiens |
|
| pmid |
sentence |
| 12776177 |
Thus, the TIP60 HAT complex is recruited to MYC-target genes and, probably with other other HATs, contributes to histone acetylation in response to mitogenic signals. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
KMT5C | down-regulates activity
methylation
|
H4C1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266650 |
Lys21 |
GGAKRHRkVLRDNIQ |
in vitro |
|
| pmid |
sentence |
| 24396869 |
SUV420H1 and SUV420H2 are two highly homologous enzymes that methylate lysine 20 of histone H4 (H4K20), a mark that has been implicated in transcriptional regulation. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
UFL1 | up-regulates activity 
ubiquitination
|
H4C1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265072 |
Lys32 |
DNIQGITkPAIRRLA |
Homo sapiens |
HEK-293 Cell, U2-OS Cell |
| pmid |
sentence |
| 30886146 |
Here we report that UFM1 specific ligase 1 (UFL1), an ufmylation E3 ligase, is important for ATM activation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
DTX3L | down-regulates activity
monoubiquitination
|
H4C1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271897 |
Lys92 |
MDVVYALkRQGRTLY |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 19818714 |
Herein, we demonstrate that BBAP selectively monoubiquitylates histone H4 lysine 91 and protects cells exposed to DNA-damaging agents. Disruption of BBAP-mediated monoubiquitylation of histone H4K91 is associated with the loss of chromatin-associated H4K20 methylase, mono- and dimethyl H4K20, and a delay in the kinetics of 53BP1 foci formation at sites of DNA damage. In response to DNA damage, BBAP expression increases and the E3 ligase selectively monoubiquitylates H4K91. Disruption of BBAP-mediated monoubiquitylation of H4K91 is associated with loss of chromatin-associated PR-Set7/Set8 and mono- and dimethyl H4K20, delayed kinetics of 53BP1 foci formation and increased sensitivity to DNA damage. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
H4C1 | form complex 
binding
|
Nucleosome |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265311 |
|
|
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 |
| + |
H4C1 | up-regulates activity
relocalization
|
BRD4 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262065 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 27991587 |
BRD4 interacts with acetylated nucleosomes via both its BD1 and BD2 domains. Our results indicate that BRD4-BD1 binds to nucleosomes through the acetylated histone H4 tail and does not additionally interact with DNA. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
H4C1 | form complex
binding
|
Nucleosome_H3.1t variant |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263726 |
|
|
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 |
| + |
MAML1 | down-regulates activity
acetylation
|
H4C1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-153041 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17300219 |
We speculated that maml1, in addition to recruiting p300, might directly interact with histones to facilitate histone acetylation. We had observed acetylation of the histones h3 and h4. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
H4C1 | form complex
binding
|
Nucleosome_H2A.Z.2 variant |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263712 |
|
|
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 |
| + |
H4C1 | form complex
binding
|
CENP-A nucleosome |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263701 |
|
|
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 |
| + |
H4C1 | up-regulates activity
relocalization
|
BRDT |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262066 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 27991587 |
BRDT interacts with acetylated nucleosomes via its BD1 domain. Binding may be initiated through non-specific interactions with DNA, which allow BRDT to localize to chromatin. Specificity is generated through recognition of tandem acetylated lysine residues (K5ac/K8ac) on the histone H4 tail, |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Integrator complex | down-regulates quantity by repression 
transcriptional regulation
|
H4C1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261481 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 25675981 |
Integrator-dependent function at promoter proximal sites that is unrelated to NELF-regulated pausing. Given its termination function at both the U2 snRNA and Histone H4 genes, we favor a model in which Integrator also has a termination function at promoter proximal sites. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
H4C1 | form complex
binding
|
Nucleosome_H2A.Z.1 variant |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263718 |
|
|
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 |
| + |
SLBP | up-regulates quantity by expression
translation regulation
|
H4C1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265376 |
|
|
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 |
| + |
H4C1 | form complex
binding
|
Nucleosome_H3.1 variant |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263722 |
|
|
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 |
| + |
H4C1 | form complex
binding
|
Nucleosome_H3.3 variant |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263877 |
|
|
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 |
| + |
NuA4 complex | down-regulates activity
acetylation
|
H4C1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269286 |
|
|
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 |
| + |
H4C1 | up-regulates activity
relocalization
|
BRD2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262062 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12776177 |
Thus, the TIP60 HAT complex is recruited to MYC-target genes and, probably with other other HATs, contributes to histone acetylation in response to mitogenic signals. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BRCA1-BARD1 complex | up-regulates activity
ubiquitination
|
H4C1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263234 |
|
|
in vitro |
|
| pmid |
sentence |
| 12485996 |
Strikingly, as well as H2AX, the nucleosome core histones H2A, H2B, H3 and H4 were all ubiquitylated efficiently by BRCA1/BARD1, while the linker histone H1 was not (Figure 3).| Generally, histone proteins are required for compaction of nuclear DNA into chromatin, and their modification is thought to loosen this compaction. Therefore, one might envisage that ubiquitylation of γH2AX by BRCA1/BARD1 at DNA breaks modulates local chromatin packaging to facilitate the action of DNA repair enzymes. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
TP53BP1 |
binding
|
H4C1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-151654 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17190600 |
Here we demonstrate that this link occurs through direct binding of 53bp1 and crb2 to histone h4. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
H4C1
- 
- 