| + |
CREBBP | down-regulates activity
acetylation
|
FBL |
0.269 |
| 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 |
0.271 |
| 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 |
| + |
FBL | form complex
binding
|
U3 snoRNP |
0.98 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280836 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29414516 |
The small subunit processome is the first precursor of the small eukaryotic ribosomal subunit. Eukaryotic ribosome biogenesis is initiated by the seven-subunit UtpA complex (Utp4, Utp5, Utp8, Utp9, Utp10, Utp15 & Utp17). UtpA binding and the presence of additional parts of the 5′ ETS appear to be required for the subsequent recruitment of the six-subunit UtpB complex (Utp1/Pwp2, Utp6, Utp12, Utp13, Utp18 & Utp21) and the U3 snoRNP (U3 snoRNA, Nop1/fibrillarin, Snu13, Nop56 & Nop58) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
USP36 | up-regulates quantity by stabilization
deubiquitination
|
FBL |
0.361 |
| 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 |