+ |
PIAS1 | down-regulates
sumoylation
|
FHL1 |
0.259 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-154801 |
Lys144 |
GTGSFFPkGEDFYCV |
Homo sapiens |
|
pmid |
sentence |
17509614 |
Pias1 (the protein inhibitor of activated stat1) interacts with kyot2 directly and attenuates kyot2-mediated transcriptional repression. We demonstrate that kyot2 is modified by sumoylation at two lysine residues, k144 and k171. Sumoylation of the transfected kyot2 is enhanced by pias1 |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-154805 |
Lys300 |
PRGPGLVkAPVWWPM |
Homo sapiens |
|
pmid |
sentence |
17509614 |
Pias1 (the protein inhibitor of activated stat1) interacts with kyot2 directly and attenuates kyot2-mediated transcriptional repression. We demonstrate that kyot2 is modified by sumoylation at two lysine residues, k144 and k171. Sumoylation of the transfected kyot2 is enhanced by pias1 |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
RING1 | up-regulates
binding
|
FHL1 |
0.364 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-123150 |
|
|
Homo sapiens |
|
pmid |
sentence |
14999091 |
The polycombprotein ring1 interacts with the lim domains of kyot2 in yeast and mammalian cells. The interaction between kyot2 and ring1 was detected both in vitro and in vivo |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
FHL1 | down-regulates
binding
|
RBPJ |
0.669 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-54277 |
|
|
Homo sapiens |
|
pmid |
sentence |
9418910 |
It was demonstrated by emsa that kyot2 can form a complex with dna-bound rbp-j, but the dna-binding affinity of the kyot2rbp-j complex is greatly weakened and it exists mostly dissociated from dna |
|
Publications: |
1 |
Organism: |
Homo Sapiens |