+ |
ARHGAP8 | up-regulates activity
binding
|
LAMTOR3 |
0.255 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-275551 |
|
|
|
|
pmid |
sentence |
28092672 |
Furthermore, we identify that BPGAP1 (a BCH domain-containing, Cdc42GAP-like Rho GTPase-activating protein) promotes MEK partner 1 (MP1)-induced ERK activation on late endosome through scaffolding MP1/MEK1 complex. This regulatory function requires phosphorylation of BPGAP1 by JNK at its C terminal tail (Ser424) to unlock its autoinhibitory conformation. |
|
Publications: |
1 |
+ |
LAMTOR3 | form complex
binding
|
LAMTOR |
0.929 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-164775 |
|
|
Homo sapiens |
|
pmid |
sentence |
20381137 |
Mammals express four rag proteinsRaga, ragb, ragc, and ragdthat form heterodimers consisting of raga or ragb with ragc or ragd. Raga and ragb, like ragc and ragd, are highly similar to each other and are functionally redundant |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
LAMTOR3 | up-regulates
binding
|
MAP2K1 |
0.599 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-130924 |
|
|
Homo sapiens |
|
pmid |
sentence |
15547943 |
We analyzed the ability of mp1 to bind to mek1, erk1, and to itself, and the regulation of these interactions. Gel filtration of cell lysates revealed two major mp1 peaks: a broad high molecular weight peak and a 28 kda complex. An mp1 mutant that lost mek1 binding no longer enhanced rasv12-stimulated erk1 activity, and functioned as a dominant negative, consistent with the concept that mp1 function depends on facilitating these oligomerizations. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
LAMTOR3 | up-regulates
binding
|
MEK1/2 |
0.6 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-244874 |
|
|
Homo sapiens |
|
pmid |
sentence |
15547943 |
We analyzed the ability of mp1 to bind to mek1, erk1, and to itself, and the regulation of these interactions. Gel filtration of cell lysates revealed two major mp1 peaks: a broad high molecular weight peak and a 28 kda complex. An mp1 mutant that lost mek1 binding no longer enhanced rasv12-stimulated erk1 activity, and functioned as a dominant negative, consistent with the concept that mp1 function depends on facilitating these oligomerizations. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
LAMTOR3 | up-regulates
binding
|
MAPK3 |
0.589 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-59877 |
|
|
Homo sapiens |
|
pmid |
sentence |
9733512 |
A protein called mp1 (mek partner 1) was identified that bound specifically to mek1 and erk1 and facilitated their activation. When overexpressed in cultured cells, mp1 enhanced activation of erk1 and activation of a reporter driven by the transcription factor elk-1. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |