| + |
DZIP3 | up-regulates activity 
monoubiquitination
|
H2AX |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271752 |
Lys119 |
IQAVLLPkKTSATVG |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 18206970 |
2A-HUB catalyzes monoubiquitination of H2A at lysine 119, functioning as a combinatoric component of the repression machinery required for specific gene regulation programs. Thus, 2A-HUB mediates a selective repression of a specific set of chemokine genes in macrophages, critically modulating migratory responses to TLR activation. H2A monoubiquitination acts to prevent FACT recruitment at the transcriptional promoter region, blocking RNA polymerase II release at the early stage of elongation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RNF168 |
ubiquitination
|
H2AX |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262063 |
Lys14 |
TGGKARAkAKSRSSR |
Homo sapiens |
|
| pmid |
sentence |
| 22980979 |
We find that K63 ubiquitin chains are conjugated to RNF168-dependent H2A/H2AX monoubiquitination at K13-15 and not on K118-119. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PPM1D | down-regulates 
dephosphorylation
|
H2AX |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-163693 |
Ser140 |
GKKATQAsQEY |
Homo sapiens |
|
| pmid |
sentence |
| 20118229 |
Wild-type p53-induced phosphatase 1 dephosphorylates histone variant gamma-h2ax and suppresses dna double strand break repair. Here, we demonstrate that the wild-type p53-induced phosphatase 1 (wip1) also dephosphorylates gamma-h2ax at serine 139 in vitro and in vivo. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MAPK9 | up-regulates
phosphorylation
|
H2AX |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-160210 |
Ser140 |
GKKATQAsQEY |
Homo sapiens |
|
| pmid |
sentence |
| 18158901 |
H2ax interacts with numerous proteins required for dna damage signaling and repair when phosphorylated on ser-140. Phosphorylation of ser-140 (h2ax139ph) in response to ionizing radiation is mediated by both atm and prkdc. Our data showed that h2ax is phosphorylated by uva-activated jnk. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ATM | up-regulates
phosphorylation
|
H2AX |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-160206 |
Ser140 |
GKKATQAsQEY |
Homo sapiens |
|
| pmid |
sentence |
| 18158901 |
H2ax interacts with numerous proteins required for dna damage signaling and repair when phosphorylated on ser-140. Phosphorylation of ser-140 (h2ax139ph) in response to ionizing radiation is mediated by both atm and prkdc. Our data showed that h2ax is phosphorylated by uva-activated jnk. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-174442 |
Ser140 |
GKKATQAsQEY |
Homo sapiens |
|
| pmid |
sentence |
| 21690091 |
Upon dna damage, h2ax is phosphorylated by ataxia telangiectasia mutated (atm) and atm-related kinases at serine 139, known as ?_?_?_-H2ax, which serves as a docking site to recruit the mediator of dna damage checkpoint protein 1 (mdc1) to sites of dna damage, named dna damage foci |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | FLT3-ITD signaling |
| + |
MAPK8 | up-regulates
phosphorylation
|
H2AX |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-184146 |
Ser140 |
GKKATQAsQEY |
Homo sapiens |
|
| pmid |
sentence |
| 19234442 |
The stress-response kinase jnk1, activated by dna damage and initiating a pro-apoptotic program, has been recently shown to translocate into the nucleus upon activation where it phosphorylates substrates including h2ax s139, an event critical for dna degradation mediated by caspase-activated dnase (cad) in apoptotic cells |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Kidney |
| + |
BAZ1B | up-regulates
phosphorylation
|
H2AX |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-182831 |
Tyr143 |
ATQASQEy |
Homo sapiens |
|
| pmid |
sentence |
| 19092802 |
We show that wstf phosphorylates tyr 142 of h2a.x, and that wstf activity has an important role in regulating several events that are critical for the dna damage response |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
EYA1 | down-regulates
dephosphorylation
|
H2AX |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-168879 |
Tyr143 |
ATQASQEy |
Homo sapiens |
|
| pmid |
sentence |
| 20965415 |
Tyr142 is dephosphorylated by the tyr phosphatases eya1 and eya3. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
EYA3 | down-regulates
dephosphorylation
|
H2AX |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-168927 |
Tyr143 |
ATQASQEy |
Homo sapiens |
|
| pmid |
sentence |
| 20965415 |
Tyr142 is dephosphorylated by the tyr phosphatases eya1 and eya3. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKDC | up-regulates
phosphorylation
|
H2AX |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-192443 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23620287 |
Dna-dependentprotein_ kinase_ (dna-pk) that phosphorylate h2ax at dsbs |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NatA | down-regulates activity
acetylation
|
H2AX |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267227 |
|
|
Homo sapiens |
HCT-116 Cell |
| pmid |
sentence |
| 21351257 |
The human protein N(α)-terminal acetyltransferase A complex (hNatA), composed of the catalytic hNaa10p (hArd1) and auxiliary hNaa15p (hNat1/NATH/Tubedown) subunits, was reported to be important for cell survival and growth of various types of cancer. lack of acetylation by hNatA activated H2A.X and Chk2 in both HCT116 cell lines independent of TP53 status (Fig. 6). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BRCA1-BARD1 complex | up-regulates activity
ubiquitination
|
H2AX |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263235 |
|
|
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 |
| + |
RNF8 | up-regulates
ubiquitination
|
H2AX |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-159309 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18001824 |
Rnf8 can ubiquitylate histone h2a and h2ax, |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SLBP | up-regulates quantity by expression
translation regulation
|
H2AX |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265405 |
|
|
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 |
| + |
KDM4C | down-regulates quantity by repression 
transcriptional regulation
|
H2AX |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263872 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29207681 |
Knockdown of JMJD2C gene led to the up-regulation of basal γ-H2AX expression. and γ-H2AX together with its phosphorylated C-terminal (Sre residues 139–140, γ-H2AX) are crucial for DNA repair |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
H2AX | up-regulates
binding
|
NBN |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-133020 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15635255 |
Nbs1 physically interacts with ?-H2ax to form nuclear foci at dna damage sites. The inhibition of this interaction by introduction of anti-?-H2ax antibody into cells abolishes nbs1 foci formation in response to dna damage. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
UBE2N | up-regulates
ubiquitination
|
H2AX |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-159880 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18077395 |
In an h2ax- and mdc1-dependent manner , rnf8/ubc13 complexes go to sites of dna damage through their fha domain and initiate the synthesis of k63 polyubiquitin chains on chromatin that recruit the brca1 a complex through the uim domains of rap80. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
H2AX | up-regulates
binding
|
MDC1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-143377 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16377563 |
Here, we demonstrate that mammalian mdc1/nfbd1 directly binds to phospho-h2ax (gammah2ax) by specifically interacting with the phosphoepitope at the gammah2ax carboxyl terminus. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
H2AX
- 
- 