+ |
SETDB2 | up-regulates activity
methylation
|
H3-4 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263895 |
Lys 10 |
RTKQTARkSTGGKAP |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
20404330 |
Here, we have characterized a previously undescribed member of the histone H3K9 methyltransferase family named CLLD8 (or SETDB2 or KMT1F). This protein contributes to the trimethylation of both interspersed repetitive elements and centromere-associated repeats and participates in the recruitment of heterochromatin protein 1 to centromeres. Methylation of histone H3 at lysine 9 (H3K9) has emerged as an important player in the formation of heterochromatin, chromatin condensation, and transcriptional repression. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
KDM3A | up-regulates activity
demethylation
|
H3-4 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276846 |
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 |
+ |
KDM4C | down-regulates activity
demethylation
|
H3-4 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263867 |
Lys10 |
RTKQTARkSTGGKAP |
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 |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263866 |
Lys37 |
APATGGVkKPHRYRP |
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: |
2 |
Organism: |
Homo Sapiens |
+ |
PHF2 | down-regulates activity
demethylation
|
H3-4 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-264520 |
Lys10 |
RTKQTARkSTGGKAP |
Homo sapiens |
|
pmid |
sentence |
21532585 |
PHF2, a jmjC demethylase, is enzymatically inactive by itself, but becomes an active H3K9Me2 demethylase through PKA-mediated phosphorylation. This modification leads to targeting of the PHF2–ARID5B complex to its target promoters, where it removes the repressive H3K9Me2 mark. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
KDM3B | down-regulates activity
demethylation
|
H3-4 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266635 |
Lys10 |
RTKQTARkSTGGKAP |
Chlorocebus aethiops |
|
pmid |
sentence |
16603237 |
We have purified a JmjC domain-containing protein, JHDM2A, which specifically demethylates mono- and dimethyl-H3K9. JHDM2A exhibits hormone-dependent recruitment to androgen-receptor target genes, resulting in H3K9 demethylation and transcriptional activation. Thus, our work identifies a histone demethylase and links its function to hormone-dependent transcriptional activation. |
|
Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
+ |
JMJD1C | down-regulates activity
demethylation
|
H3-4 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-265170 |
Lys10 |
RTKQTARkSTGGKAP |
Homo sapiens |
|
pmid |
sentence |
32034158 |
We now determine that JMJD1C is recruited by USF-1 to various lipogenic genes for H3K9 demethylation to enhance chromatin accessibility in the fed state. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
KAT2B | down-regulates activity
acetylation
|
H3-4 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-269613 |
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-269621 |
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 |
+ |
KAT2A | down-regulates activity
acetylation
|
H3-4 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-269596 |
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-269604 |
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 |
+ |
SAGA complex | down-regulates activity
acetylation
|
H3-4 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-269630 |
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-269638 |
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
|
H3-4 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-275870 |
Lys19 |
TGGKAPRkQLATKVA |
|
|
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-275876 |
Lys37 |
APATGGVkKPHRYRP |
|
|
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-275882 |
Lys38 |
PATGGVKkPHRYRPG |
|
|
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 |
+ |
SETD5 | up-regulates activity
methylation
|
H3-4 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-264621 |
Lys37 |
APATGGVkKPHRYRP |
in vitro |
|
pmid |
sentence |
31515109 |
SETD5 Exhibits Intrinsic Methyltransferase Activity on H3K36. This assay showed that SETD5 has specific histone methyltransferase activity toward K36 but not for other residues such as K4 and K27 (Figure 8B). we revealed that SETD5 is endowed with H3K36 methyltransferase, which is necessary for RNA elongation and processing and, ultimately, correct gene transcription. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
PHF2 | up-regulates activity
demethylation
|
H3-4 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-264517 |
Lys5 |
kQTARKST |
Homo sapiens |
|
pmid |
sentence |
21532585 |
PHF2, a jmjC demethylase, is enzymatically inactive by itself, but becomes an active H3K9Me2 demethylase through PKA-mediated phosphorylation. This modification leads to targeting of the PHF2–ARID5B complex to its target promoters, where it removes the repressive H3K9Me2 mark. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
KDM1A | up-regulates activity
demethylation
|
H3-4 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-264508 |
Lys5 |
kQTARKST |
Homo sapiens |
|
pmid |
sentence |
15620353 |
Here, we provide evidence that LSD1 (KIAA0601), a nuclear homolog of amine oxidases, functions as a histone demethylase and transcriptional corepressor. LSD1 specifically demethylates histone H3 lysine 4, which is linked to active transcription. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
KDM5A | up-regulates activity
demethylation
|
H3-4 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-264300 |
Lys5 |
kQTARKST |
Homo sapiens |
|
pmid |
sentence |
30246379 |
KDM5 subfamily is capable of removing tri‐ and di‐ methyl marks from lysine 4 on histone H3 (H3K4). Depending on the methylation site, its effect on transcription can be either activating or repressing. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
MLL1 complex | down-regulates activity
methylation
|
H3-4 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-268803 |
Lys5 |
kQTARKST |
Homo sapiens |
|
pmid |
sentence |
24680668 |
Dimethylation of h3k4 requires a sub-complex including wrad (wdr5, rbbp5, ash2l, and dpy-30), which binds to each set1 family member forming a minimal corecomplexthat is required for multiple lysine methylation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
KDM5B | up-regulates activity
demethylation
|
H3-4 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-264303 |
Lys5 |
kQTARKST |
Homo sapiens |
|
pmid |
sentence |
30246379 |
KDM5 subfamily is capable of removing tri‐ and di‐ methyl marks from lysine 4 on histone H3 (H3K4). Depending on the methylation site, its effect on transcription can be either activating or repressing. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
KDM5C | up-regulates activity
demethylation
|
H3-4 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-264306 |
Lys5 |
kQTARKST |
Homo sapiens |
|
pmid |
sentence |
30246379 |
KDM5 subfamily is capable of removing tri†and di†methyl marks from lysine 4 on histone H3 (H3K4). Depending on the methylation site, its effect on transcription can be either activating or repressing. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
Set1-Ash2 HMT complex | down-regulates activity
methylation
|
H3-4 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-264483 |
Lys5 |
kQTARKST |
Homo sapiens |
|
pmid |
sentence |
12670868 |
The Set1/Ash2 HMT methylates histone H3 at Lys 4 (K4), but not if the neighboring K9 residue is already methylated. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
MLL2 complex | down-regulates activity
methylation
|
H3-4 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-268800 |
Lys5 |
kQTARKST |
Homo sapiens |
|
pmid |
sentence |
24680668 |
Dimethylation of h3k4 requires a sub-complex including wrad (wdr5, rbbp5, ash2l, and dpy-30), which binds to each set1 family member forming a minimal corecomplexthat is required for multiple lysine methylation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
MLL3 complex | down-regulates activity
methylation
|
H3-4 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-268812 |
Lys5 |
kQTARKST |
Homo sapiens |
|
pmid |
sentence |
34156443 |
MLL3/KMT2C and MLL4/KMT2D are two paralogous histone modifiers that belong to the SET1/MLL (also named COMPASS) family of lysine methyltransferases and play critical roles in enhancer-regulated gene activation. MLL3 and MLL4 form identical multi-protein complexes for modifying mono-methylation of histone H3 lysine 4 (H3K4) at enhancers, which together with the p300/CBP-mediated H3K27 acetylation can generate an active enhancer landscape for long-range target gene activation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
KDM5D | up-regulates activity
demethylation
|
H3-4 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-264309 |
Lys5 |
kQTARKST |
Homo sapiens |
|
pmid |
sentence |
30246379 |
KDM5 subfamily is capable of removing tri‐ and di‐ methyl marks from lysine 4 on histone H3 (H3K4). Depending on the methylation site, its effect on transcription can be either activating or repressing. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
SETD1B | down-regulates activity
methylation
|
H3-4 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-265577 |
Lys5 |
kQTARKST |
Homo sapiens |
|
pmid |
sentence |
32546567 |
SETD1B encodes a lysine-specific methyltransferase that assists in transcriptional activation of genes by depositing H3K4 methyl marks. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
DOT1L |
methylation
|
H3-4 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-267142 |
Lys80 |
REIAQDFkTDLRFQS |
Homo sapiens |
|
pmid |
sentence |
12123582 |
HDOT1L Is a Nucleosomal H3-K79-Specific HMTase. We identified a human DOT1-like (DOT1L) protein and demonstrated that this protein possesses intrinsic H3-K79-specific histone methyltransferase (HMTase) activity in vitro and in vivo. Furthermore, we found that K79 methylation level is regulated throughout the cell cycle. By using two different methods, we demonstrate that the K79 methylation level decreases during S phase, reaches its lowest level in G2, increases during M phase, and maintains at a high level during G1 phase. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CKM complex | down-regulates activity
phosphorylation
|
H3-4 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273174 |
Ser11 |
TKQTARKsTGGKAPR |
|
|
pmid |
sentence |
18418385 |
However, within T/G-Mediator, cdk8 phosphorylates serine-10 on histone H3, which in turn stimulates H3K14 acetylation by GCN5L within the complex. Tandem phosphoacetylation of H3 correlates with transcriptional activation, and ChIP assays demonstrate co-occupancy of T/G-Mediator components at several activated genes in vivo. |
|
Publications: |
1 |
+ |
RPS6KA5 |
phosphorylation
|
H3-4 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-249213 |
Ser11 |
TKQTARKsTGGKAPR |
Mus musculus |
|
pmid |
sentence |
12773393 |
The results presented here show that MSK2 and, to a lesser extent, MSK1 are the major protein kinases required for the phosphorylation of histone H3 at both Ser10 and Ser28 |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-249214 |
Ser29 |
ATKVARKsAPATGGV |
Mus musculus |
|
pmid |
sentence |
12773393 |
The results presented here show that MSK2 and, to a lesser extent, MSK1 are the major protein kinases required for the phosphorylation of histone H3 at both Ser10 and Ser28 |
|
Publications: |
2 |
Organism: |
Mus Musculus |
+ |
CDK8 | down-regulates activity
phosphorylation
|
H3-4 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273175 |
Ser11 |
TKQTARKsTGGKAPR |
|
|
pmid |
sentence |
18418385 |
However, within T/G-Mediator, cdk8 phosphorylates serine-10 on histone H3, which in turn stimulates H3K14 acetylation by GCN5L within the complex. Tandem phosphoacetylation of H3 correlates with transcriptional activation, and ChIP assays demonstrate co-occupancy of T/G-Mediator components at several activated genes in vivo. |
|
Publications: |
1 |
+ |
RPS6KA4 |
phosphorylation
|
H3-4 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-249211 |
Ser11 |
TKQTARKsTGGKAPR |
Mus musculus |
|
pmid |
sentence |
12773393 |
The results presented here show that MSK2 and, to a lesser extent, MSK1 are the major protein kinases required for the phosphorylation of histone H3 at both Ser10 and Ser28 |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-249212 |
Ser29 |
ATKVARKsAPATGGV |
Mus musculus |
|
pmid |
sentence |
12773393 |
The results presented here show that MSK2 and, to a lesser extent, MSK1 are the major protein kinases required for the phosphorylation of histone H3 at both Ser10 and Ser28 |
|
Publications: |
2 |
Organism: |
Mus Musculus |
+ |
BAZ2B | down-regulates activity
binding
|
H3-4 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266620 |
|
|
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 |
+ |
CBX3 | up-regulates activity
binding
|
H3-4 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-264495 |
|
|
Homo sapiens |
|
pmid |
sentence |
19111658 |
A core characteristic of heterochromatin is its association with heterochromatin protein 1 (HP1) proteins, a highly conserved family of chromosomal proteins that bind to di- and trimethylated H3K9 via a conserved N-terminal domain called the chromodomain (CD) HP1 proteins are a highly conserved family of eukaryotic proteins that bind to methylated histone H3 lysine 9 (H3K9) and are required for heterochromatic gene silencing. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
Sin3B_complex | down-regulates activity
binding
|
H3-4 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266971 |
|
|
Homo sapiens |
|
pmid |
sentence |
21041483 |
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 |
+ |
CBX5 | up-regulates activity
binding
|
H3-4 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-264489 |
|
|
Homo sapiens |
|
pmid |
sentence |
19111658 |
A core characteristic of heterochromatin is its association with heterochromatin protein 1 (HP1) proteins, a highly conserved family of chromosomal proteins that bind to di- and trimethylated H3K9 via a conserved N-terminal domain called the chromodomain (CD) HP1 proteins are a highly conserved family of eukaryotic proteins that bind to methylated histone H3 lysine 9 (H3K9) and are required for heterochromatic gene silencing. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
SLBP | up-regulates quantity by expression
translation regulation
|
H3-4 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-265417 |
|
|
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 |
+ |
CBX1 | up-regulates activity
binding
|
H3-4 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-264492 |
|
|
Homo sapiens |
|
pmid |
sentence |
19111658 |
A core characteristic of heterochromatin is its association with heterochromatin protein 1 (HP1) proteins, a highly conserved family of chromosomal proteins that bind to di- and trimethylated H3K9 via a conserved N-terminal domain called the chromodomain (CD) HP1 proteins are a highly conserved family of eukaryotic proteins that bind to methylated histone H3 lysine 9 (H3K9) and are required for heterochromatic gene silencing. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
H3-4 | form complex
binding
|
Nucleosome_H3.1t variant |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263725 |
|
|
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. |
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Publications: |
1 |
Organism: |
In Vitro |