+ |
RRAGA | form complex
binding
|
RAGAD |
0.767 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-228167 |
|
|
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 |
+ |
RNF152 | down-regulates activity
polyubiquitination
|
RRAGA |
0.73 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272222 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
25936802 |
Here, we identified the lysosome-anchored E3 ubiquitin ligase RNF152 as an essential negative regulator of the mTORC1 pathway by targeting RagA for K63-linked ubiquitination. RNF152 interacts with and ubiquitinates RagA in an amino-acid-sensitive manner. The mutation of RagA ubiquitination sites abolishes this effect of RNF152 and enhances the RagA-mediated activation of mTORC1. Ubiquitination by RNF152 generates an anchor on RagA to recruit its inhibitor GATOR1, a GAP complex for Rag GTPases. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
GATOR1 | down-regulates activity
gtpase-activating protein
|
RRAGA |
0.874 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-253562 |
|
|
in vitro |
|
pmid |
sentence |
23723238 |
GATOR1 has GTPase-activating protein (GAP) activity for RagA and RagB, and its components are mutated in human cancer. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
RRAGA | form complex
binding
|
RAGAC |
0.77 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-228164 |
|
|
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 |