+ |
AKT | down-regulates
phosphorylation
|
PHF20 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-196112 |
Ser291 |
ELRRRKIsKGCEVPL |
Homo sapiens |
|
pmid |
sentence |
22334668 |
Akt phosphorylates phf20 at ser(291) in vitro and in vivo, which results in its translocation from the nucleus to the cytoplasm and attenuation of phf20 function. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
AKT1 | down-regulates
phosphorylation
|
PHF20 |
0.533 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-252529 |
Ser291 |
ELRRRKIsKGCEVPL |
Homo sapiens |
|
pmid |
sentence |
22334668 |
Akt phosphorylates phf20 at ser(291) in vitro and in vivo, which results in its translocation from the nucleus to the cytoplasm and attenuation of phf20 function. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PHF20 | form complex
binding
|
NSL histone acetyltransferase |
0.67 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-267159 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
20018852 |
Here we report an analysis of the subunit composition and substrate specificity of the NSL complex. Proteomic analyses of complexes purified through multiple candidate subunits reveal that NSL is composed of nine subunits. Two of its subunits, WD repeat domain 5 (WDR5) and host cell factor 1 (HCF1), are shared with members of the MLL/SET family of histone H3 lysine 4 (H3K4) methyltransferase complexes, and a third subunit, MCRS1, is shared with the human INO80 chromatin-remodeling complex. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |