+ |
RPS6KB1 | up-regulates activity
phosphorylation
|
TARBP2 |
0.329 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-274065 |
Ser283 |
ILSLRSCsLGSLGAL |
in vitro |
|
pmid |
sentence |
27407113 |
We demonstrate that S6 kinases can phosphorylate the extended C-terminal domain of TRBP and interact with TRBP in situ in primary cells. TRBP serines 283/286 are essential for S6K-mediated TRBP phosphorylation, optimal expression of TRBP, and the S6K-TRBP interaction in human primary cells. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-274068 |
Ser286 |
LRSCSLGsLGALGPA |
in vitro |
|
pmid |
sentence |
27407113 |
We demonstrate that S6 kinases can phosphorylate the extended C-terminal domain of TRBP and interact with TRBP in situ in primary cells. TRBP serines 283/286 are essential for S6K-mediated TRBP phosphorylation, optimal expression of TRBP, and the S6K-TRBP interaction in human primary cells. |
|
Publications: |
2 |
Organism: |
In Vitro |
+ |
AKT1 | up-regulates activity
phosphorylation
|
TARBP2 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-274064 |
Ser283 |
ILSLRSCsLGSLGAL |
in vitro |
|
pmid |
sentence |
27407113 |
We demonstrate that S6 kinases can phosphorylate the extended C-terminal domain of TRBP and interact with TRBP in situ in primary cells. TRBP serines 283/286 are essential for S6K-mediated TRBP phosphorylation, optimal expression of TRBP, and the S6K-TRBP interaction in human primary cells. In vitro kinase assays demonstrated that TRBP-D3 can be phosphorylated by S6K1, S6K2, but also AKT1 (Figure (Figure1C),1C), |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-274067 |
Ser286 |
LRSCSLGsLGALGPA |
in vitro |
|
pmid |
sentence |
27407113 |
We demonstrate that S6 kinases can phosphorylate the extended C-terminal domain of TRBP and interact with TRBP in situ in primary cells. TRBP serines 283/286 are essential for S6K-mediated TRBP phosphorylation, optimal expression of TRBP, and the S6K-TRBP interaction in human primary cells. |
|
Publications: |
2 |
Organism: |
In Vitro |
+ |
RPS6KB2 | up-regulates activity
phosphorylation
|
TARBP2 |
0.34 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-274066 |
Ser283 |
ILSLRSCsLGSLGAL |
in vitro |
|
pmid |
sentence |
27407113 |
We demonstrate that S6 kinases can phosphorylate the extended C-terminal domain of TRBP and interact with TRBP in situ in primary cells. TRBP serines 283/286 are essential for S6K-mediated TRBP phosphorylation, optimal expression of TRBP, and the S6K-TRBP interaction in human primary cells. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-274069 |
Ser286 |
LRSCSLGsLGALGPA |
in vitro |
|
pmid |
sentence |
27407113 |
We demonstrate that S6 kinases can phosphorylate the extended C-terminal domain of TRBP and interact with TRBP in situ in primary cells. TRBP serines 283/286 are essential for S6K-mediated TRBP phosphorylation, optimal expression of TRBP, and the S6K-TRBP interaction in human primary cells. |
|
Publications: |
2 |
Organism: |
In Vitro |
+ |
TARBP2 | form complex
binding
|
RISC(DICER1/AGO2/TARBP2) |
0.901 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-140229 |
|
|
Homo sapiens |
|
pmid |
sentence |
16142218 |
Dicer and trbp interact in vivo and in vitro /our data indicate that trbp is primarily required for the assembly and/or functioning of si_ or mi_riscs in mammalian cells, but it may also facilitate the cleavage of pre_mirnas by dicer. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
TARBP2 | up-regulates
binding
|
DICER1 |
0.938 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-140226 |
|
|
Homo sapiens |
|
pmid |
sentence |
16142218 |
Dicer and trbp interact in vivo and in vitro /our data indicate that trbp is primarily required for the assembly and/or functioning of si? Or mi?RISCs In mammalian cells, but it may also facilitate the cleavage of pre?miRNAs By dicer. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |