+ |
CREBBP | down-regulates activity
acetylation
|
FBL |
0.274 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-275898 |
Lys102 |
GVFICRGkEDALVTK |
|
|
pmid |
sentence |
30540930 |
Here, we show that FBL is acetylated at several lysine residues by the acetyltransferase CBP and deacetylated by SIRT7.|hyperacetylation impairs the interaction of FBL with histone H2A and chromatin, thereby compromising H2AQ104 methylation (H2AQ104me) and rDNA transcription. SIRT7-dependent deacetylation of FBL ensures H2AQ104me and high levels of rRNA synthesis during interphase. |Global acetylome studies have shown that FBL is acetylated at four conserved lysine residues (K102, K121, K205, and K206) |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-275899 |
Lys121 |
GESVYGEkRVSISEG |
|
|
pmid |
sentence |
30540930 |
Here, we show that FBL is acetylated at several lysine residues by the acetyltransferase CBP and deacetylated by SIRT7.|hyperacetylation impairs the interaction of FBL with histone H2A and chromatin, thereby compromising H2AQ104 methylation (H2AQ104me) and rDNA transcription. SIRT7-dependent deacetylation of FBL ensures H2AQ104me and high levels of rRNA synthesis during interphase. |Global acetylome studies have shown that FBL is acetylated at four conserved lysine residues (K102, K121, K205, and K206) |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-275896 |
Lys205 |
RDLINLAkKRTNIIP |
|
|
pmid |
sentence |
30540930 |
Here, we show that FBL is acetylated at several lysine residues by the acetyltransferase CBP and deacetylated by SIRT7.|hyperacetylation impairs the interaction of FBL with histone H2A and chromatin, thereby compromising H2AQ104 methylation (H2AQ104me) and rDNA transcription. SIRT7-dependent deacetylation of FBL ensures H2AQ104me and high levels of rRNA synthesis during interphase. |Global acetylome studies have shown that FBL is acetylated at four conserved lysine residues (K102, K121, K205, and K206) |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-275897 |
Lys206 |
DLINLAKkRTNIIPV |
|
|
pmid |
sentence |
30540930 |
Here, we show that FBL is acetylated at several lysine residues by the acetyltransferase CBP and deacetylated by SIRT7.|hyperacetylation impairs the interaction of FBL with histone H2A and chromatin, thereby compromising H2AQ104 methylation (H2AQ104me) and rDNA transcription. SIRT7-dependent deacetylation of FBL ensures H2AQ104me and high levels of rRNA synthesis during interphase. |Global acetylome studies have shown that FBL is acetylated at four conserved lysine residues (K102, K121, K205, and K206) |
|
Publications: |
4 |
+ |
SIRT7 | up-regulates activity
deacetylation
|
FBL |
0.274 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-275894 |
Lys102 |
GVFICRGkEDALVTK |
|
|
pmid |
sentence |
30540930 |
Here, we show that FBL is acetylated at several lysine residues by the acetyltransferase CBP and deacetylated by SIRT7.|hyperacetylation impairs the interaction of FBL with histone H2A and chromatin, thereby compromising H2AQ104 methylation (H2AQ104me) and rDNA transcription. SIRT7-dependent deacetylation of FBL ensures H2AQ104me and high levels of rRNA synthesis during interphase. |Global acetylome studies have shown that FBL is acetylated at four conserved lysine residues (K102, K121, K205, and K206) |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-275895 |
Lys121 |
GESVYGEkRVSISEG |
|
|
pmid |
sentence |
30540930 |
Here, we show that FBL is acetylated at several lysine residues by the acetyltransferase CBP and deacetylated by SIRT7.|hyperacetylation impairs the interaction of FBL with histone H2A and chromatin, thereby compromising H2AQ104 methylation (H2AQ104me) and rDNA transcription. SIRT7-dependent deacetylation of FBL ensures H2AQ104me and high levels of rRNA synthesis during interphase. |Global acetylome studies have shown that FBL is acetylated at four conserved lysine residues (K102, K121, K205, and K206) |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-275892 |
Lys205 |
RDLINLAkKRTNIIP |
|
|
pmid |
sentence |
30540930 |
Here, we show that FBL is acetylated at several lysine residues by the acetyltransferase CBP and deacetylated by SIRT7.|hyperacetylation impairs the interaction of FBL with histone H2A and chromatin, thereby compromising H2AQ104 methylation (H2AQ104me) and rDNA transcription. SIRT7-dependent deacetylation of FBL ensures H2AQ104me and high levels of rRNA synthesis during interphase. |Global acetylome studies have shown that FBL is acetylated at four conserved lysine residues (K102, K121, K205, and K206) |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-275893 |
Lys206 |
DLINLAKkRTNIIPV |
|
|
pmid |
sentence |
30540930 |
Here, we show that FBL is acetylated at several lysine residues by the acetyltransferase CBP and deacetylated by SIRT7.|hyperacetylation impairs the interaction of FBL with histone H2A and chromatin, thereby compromising H2AQ104 methylation (H2AQ104me) and rDNA transcription. SIRT7-dependent deacetylation of FBL ensures H2AQ104me and high levels of rRNA synthesis during interphase. |Global acetylome studies have shown that FBL is acetylated at four conserved lysine residues (K102, K121, K205, and K206) |
|
Publications: |
4 |
+ |
USP36 | up-regulates quantity by stabilization
deubiquitination
|
FBL |
0.369 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272291 |
|
|
Homo sapiens |
HeLa Cell |
pmid |
sentence |
19208757 |
USP36 deubiquitylated the nucleolar proteins nucleophosmin/B23 and fibrillarin, and stabilized them by counteracting ubiquitylation-mediated proteasomal degradation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |