+ |
KAT6A | up-regulates
acetylation
|
TP53 |
0.656 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-201482 |
Lys120 |
FLHSGTAkSVTCTYS |
Homo sapiens |
Leukemia Cell |
pmid |
sentence |
23431171 |
We show here that moz is an acetyltransferase of p53 at k120 and k382 and colocalizes with p53 in promyelocytic leukemia (pml) nuclear bodies following cellular stress. The moz-pml-p53 interaction enhances moz-mediated acetylation of p53, and this ternary complex enhances p53-dependent p21 expression |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-201486 |
Lys382 |
QSTSRHKkLMFKTEG |
Homo sapiens |
Leukemia Cell |
pmid |
sentence |
23431171 |
We show here that moz is an acetyltransferase of p53 at k120 and k382 and colocalizes with p53 in promyelocytic leukemia (pml) nuclear bodies following cellular stress. The moz-pml-p53 interaction enhances moz-mediated acetylation of p53, and this ternary complex enhances p53-dependent p21 expression |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
KAT6A | form complex
binding
|
KAT6A/PML |
0.502 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-201478 |
|
|
Homo sapiens |
Leukemia Cell |
pmid |
sentence |
23431171 |
We show here that moz is an acetyltransferase of p53 at k120 and k382 and colocalizes with p53 in promyelocytic leukemia (pml) nuclear bodies following cellular stress. The moz-pml-p53 interaction enhances moz-mediated acetylation of p53, and this ternary complex enhances p53-dependent p21 expression |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
KAT6A | form complex
binding
|
KAT6A/KAT6B |
0.389 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-157304 |
|
|
Homo sapiens |
Leukemia Cell |
pmid |
sentence |
17694082 |
Like gcn5/pcaf and p300/cbp, moz and morf are transcriptional co-activators with intrinsic hat activity. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
KAT6A | up-regulates quantity by expression
transcriptional regulation
|
CCL3 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-251726 |
|
|
Homo sapiens |
JURKAT Cell |
pmid |
sentence |
12771199 |
We further demonstrate that the histone acetyltransferase, MOZ, can activate the MIP-1a promoter in T-cells and that this activation is largely dependent upon the proximal RUNX site. Moreover, we show that co-expression of MOZ and RUNX1 can activate the MIP-1a promoter. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
KAT6A | up-regulates
binding
|
RUNX2 |
0.313 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-117332 |
|
|
Homo sapiens |
T-lymphocyte, Leukemia Cell, Lymphoma Cell |
pmid |
sentence |
11965546 |
Moz and morf both interact with runx2 / while morf does not acetylate runx2, its sm domain potentiates runx2-dependent transcriptional activation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
KAT6A | up-regulates
binding
|
RUNX1 |
0.477 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-113056 |
|
|
Homo sapiens |
|
pmid |
sentence |
11742995 |
The activation domain of aml1 is required for its interaction with moz / moz activates aml1_mediated transcription |
|
Publications: |
1 |
Organism: |
Homo Sapiens |