+ |
KAT5 | down-regulates
acetylation
|
NOTCH1 |
0.424 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-156911 |
Lys2029 |
NAVDDLGkSALHWAA |
Homo sapiens |
|
pmid |
sentence |
17636029 |
This result implies that the residues k2019, k2039, k2044, and k2068 of notch1-ic are the major targets of the acetyltransferase activity of tip60. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-156915 |
Lys2049 |
DAAVVLLkNGANKDM |
Homo sapiens |
|
pmid |
sentence |
17636029 |
This result implies that the residues k2019, k2039, k2044, and k2068 of notch1-ic are the major targets of the acetyltransferase activity of tip60. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-156919 |
Lys2054 |
LLKNGANkDMQNNRE |
Homo sapiens |
|
pmid |
sentence |
17636029 |
This result implies that the residues k2019, k2039, k2044, and k2068 of notch1-ic are the major targets of the acetyltransferase activity of tip60. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-156923 |
Lys2078 |
EGSYETAkVLLDHFA |
Homo sapiens |
|
pmid |
sentence |
17636029 |
This result implies that the residues k2019, k2039, k2044, and k2068 of notch1-ic are the major targets of the acetyltransferase activity of tip60. |
|
Publications: |
4 |
Organism: |
Homo Sapiens |
Pathways: | Acute Myeloid Leukemia |
+ |
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 |
+ |
KAT5 | up-regulates activity
acetylation
|
CHKA |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-267648 |
Lys247 |
MPFNKEPkWLFGTME |
Homo sapiens |
|
pmid |
sentence |
34929314 |
Glucose deprivation induces the binding of choline kinase α2 (CHKα2) to lipid droplets, followed by a continuous PTMs to promote lipolysis of lipid droplets, which are in turn mediated by AMPK-dependent CHKα2 Serine 279 phosphorylation and KAT5-dependent CHKα2 Lysine 247 acetylation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
KAT5 | up-regulates activity
acetylation
|
ATM |
0.792 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-275891 |
Lys3016 |
VLMRLQEkLKGVEEG |
|
|
pmid |
sentence |
30944854 |
Here, we report that sirtuin 7 (SIRT7)-mediated deacetylation is essential for dephosphorylation and deactivation of ATM. We show that SIRT7, a class III histone deacetylase, interacts with and deacetylates ATM in vitro and in vivo. |Upon DNA damage, ATM is activated via a series of highly organized machineries, including acetylation by the histone acetyltransferase TIP60 at lysine 3016 |
|
Publications: |
1 |
+ |
KAT5 | down-regulates
acetylation
|
SRSF2 |
0.478 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-170594 |
Lys52 |
IPRDRYTkESRGFAF |
Homo sapiens |
|
pmid |
sentence |
21157427 |
In this study, we provide the first evidence that the acetyltransferase tip60 acetylates srsf2 on its lysine 52 residue inside the rna recognition motif, and promotes its proteasomal degradation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | Acute Myeloid Leukemia, IDH-TET in AML |
+ |
CyclinB/CDK1 | up-regulates activity
phosphorylation
|
KAT5 |
0.428 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250641 |
Ser86 |
TKNGLPGsRPGSPER |
Homo sapiens |
HeLa Cell |
pmid |
sentence |
12468530 |
Baculovirus-based expression and purification of Tip60 combined with mass spectrometry allowed the identification of serines 86 and 90 as two major sites of phosphorylation in vivo. The phosphorylation of Tip60 was found to modulate its histone acetyltransferase activity. One of the identified phosphorylated serines, Ser-90, was within a consensus cyclin B/Cdc2 site. Ser-90 was specifically phosphorylatedin vitro by the cyclin B/Cdc2 complex. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250642 |
Ser90 |
LPGSRPGsPEREVPA |
Homo sapiens |
HeLa Cell |
pmid |
sentence |
12468530 |
Baculovirus-based expression and purification of Tip60 combined with mass spectrometry allowed the identification of serines 86 and 90 as two major sites of phosphorylation in vivo. The phosphorylation of Tip60 was found to modulate its histone acetyltransferase activity. One of the identified phosphorylated serines, Ser-90, was within a consensus cyclin B/Cdc2 site. Ser-90 was specifically phosphorylatedin vitro by the cyclin B/Cdc2 complex. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
GSK3B | up-regulates
phosphorylation
|
KAT5 |
0.375 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-174049 |
Ser86 |
TKNGLPGsRPGSPER |
Homo sapiens |
|
pmid |
sentence |
21658600 |
We demonstrate that gsk-3 phosphorylates serine 86 of the p53-acetyltransferase tip60. A tip60(s86a) mutant was less active to induce p53 k120 acetylation, histone 4 acetylation, and expression of puma |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | Acute Myeloid Leukemia |
+ |
CDK1 | up-regulates
phosphorylation
|
KAT5 |
0.49 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-139649 |
Ser86 |
TKNGLPGsRPGSPER |
Homo sapiens |
|
pmid |
sentence |
16103124 |
Moreover, app stabilized tip60 through cdk-dependent phosphorylation |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-139653 |
Ser90 |
LPGSRPGsPEREVPA |
Homo sapiens |
|
pmid |
sentence |
16103124 |
Moreover, app stabilized tip60 through cdk-dependent phosphorylation |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
Pathways: | Acute Myeloid Leukemia, IDH-TET in AML |
+ |
ABL1 | down-regulates activity
phosphorylation
|
KAT5 |
0.633 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276598 |
Tyr294 |
HPPGNEIyRKGTISF |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
24044023 |
We present evidence that Tip60 is modified on tyrosine 327 by Abl kinase. We show that this causes functional changes in HAT activity and the subcellular localization of TIP60, which forms a complex with Abl kinase. The Tip60 mutation Y327F abolished tyrosine phosphorylation, reduced the inhibition of Tip60 HAT activity, and caused G0-G1 arrest and association with FE65. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
KAT5 | up-regulates activity
binding
|
MYOD1 |
0.372 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-237675 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
21936881 |
Tip60 regulates myoblast differentiation by enhancing the transcriptional activity of MyoD via their physical interactions. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
MDM2 | down-regulates quantity by destabilization
polyubiquitination
|
KAT5 |
0.639 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272613 |
|
|
Homo sapiens |
U2-OS Cell |
pmid |
sentence |
11927554 |
Furthermore, we provide evidence that Mdm2, the ubiquitin ligase of the p53 tumour suppressor, interacts physically with Tip60 and induces its ubiquitylation and proteasome-dependent degradation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | Acute Myeloid Leukemia, IDH-TET in AML |
+ |
KAT5 | form complex
binding
|
NuA4 complex |
0.776 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-269297 |
|
|
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 |