+ |
TLE5 | down-regulates activity
binding
|
SIX3 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-234586 |
|
|
in vitro |
|
pmid |
sentence |
12441302 |
Biochemical and mutational analysis shows that the Six domain of both SIX3 and SIX6 strongly interact with the QD domain of TLE1 and AES. AES abrogates SIX3- and SIX6-induced phenotypes |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
TLE5 | down-regulates activity
binding
|
SIX6 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-234589 |
|
|
in vitro |
|
pmid |
sentence |
12441302 |
Biochemical and mutational analysis shows that the Six domain of both SIX3 and SIX6 strongly interact with the QD domain of TLE1 and AES. AES abrogates SIX3- and SIX6-induced phenotypes |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
PHF12 | up-regulates activity
binding
|
TLE5 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266990 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
11390640 |
We have cloned and characterized a new member of the PHD zinc finger family called Pf1 that interacts with two global transcription corepressors: mSin3A and TLE. Pf1 interacts with TLE. The Groucho/TLE proteins are members of an abundant corepressor family, and we hypothesized that Pf1 might interact with TLE family members. Together, these data suggest that in the absence of interactions with mSin3A, Gal4-Pf1 (102–273 L212P/A216P)-dependent repression can be attributed to interaction with endogenous TLE. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
TLE5 | down-regulates activity
binding
|
ZNF503 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261192 |
|
|
Chlorocebus aethiops |
|
pmid |
sentence |
19056829 |
these results show that Grg5 can specifically interact with the C-terminus of Nolz1. these data suggest that Nolz1 functions as a repressor molecule, and that Grg5 interactions with Nolz1 serve to modulate Nolz1 repressor function. Mechanistically, Grg5 is known to modulate Grg co-repressor activity, raising the possibility that classical Grg proteins mediate Nolz1-dependent transcriptional repression. GalNolz1ΔC22 showed increased repressor activity compared with GalNolz1, consistent with the ability of Grg5 to modulate Nolz1 repressor function. |
|
Publications: |
1 |
Organism: |
Chlorocebus Aethiops |