+ |
MAP3K7 | up-regulates activity
phosphorylation
|
RAB1A |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277270 |
Thr75 |
AGQERFRtITSSYYR |
in vitro |
|
pmid |
sentence |
27482120 |
TAK1 preferentially phosphorylates the inactive (GDP-bound) state of Rab1. Phosphorylation of Rab1 disrupts interaction with GDP dissociation inhibitor 1 (GDI1), but not guanine exchange factor (GEF) or GTPase-activating protein (GAP) enzymes, and is exclusive to membrane-localized Rab1, suggesting phosphorylation may stimulate Rab1 membrane association. Furthermore, we found phosphorylation of Rab1 at T75 to be essential for Rab1 function. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
RAB1A | up-regulates activity
binding
|
mTORC1 |
0.321 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261286 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
27479033 |
Hemagglutinin (HA)-Rab1A is associated with mTOR and Raptor, not Rictor (Figure S2A), and is bound more with Myc-Raptor than Myc-mTOR (Figures S2B and S2C).|Rab1A Is an mTORC1 Activator and a Colorectal Oncogene |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
RAB1A | up-regulates activity
relocalization
|
GOLGA2 |
0.707 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261285 |
|
|
Rattus norvegicus |
|
pmid |
sentence |
11285137 |
Here, we demonstrate that the cis ‐Golgi tethering protein GM130, complexed with GRASP65 and other proteins, forms a novel Rab1 effector complex that interacts with activated Rab1‐GTP in a p115‐independent manner and is required for coat protein II vesicle targeting/fusion with the cis ‐Golgi |
|
Publications: |
1 |
Organism: |
Rattus Norvegicus |
+ |
RAB1A | up-regulates activity
relocalization
|
ULK1 |
0.548 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261299 |
|
|
Homo sapiens |
|
pmid |
sentence |
27334615 |
C9orf72 acts as an effector of Rab1a that recruits active Rab1a to theULK1 complex to promote translocation of the ULK1 complex to thephagophore during autophagy initiation |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
RAB1A | up-regulates activity
binding
|
USO1 |
0.79 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261287 |
|
|
in vitro |
|
pmid |
sentence |
10903204 |
Here, the tethering factor p115 was shown to be a Rab1 effector that binds directly to activated Rab1. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
C9orf72 | up-regulates activity
binding
|
RAB1A |
0.488 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261297 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
27334615 |
C9orf72 acts as an effector of Rab1a that recruits active Rab1a to theULK1 complex to promote translocation of the ULK1 complex to thephagophore during autophagy initiation |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
RAB1A | up-regulates activity
binding
|
C9orf72 |
0.488 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261282 |
|
|
Homo sapiens |
|
pmid |
sentence |
27334615 |
Thus, our data identify C9orf72 as a novel Rab1a effector in the regulation of autophagy and indicate that C9orf72 haploinsufficiency and associated reductions in autophagy might be the underlying cause of C9ALS/FTD-associated p62 pathology. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
RAB1A | up-regulates activity
binding
|
ULK1/Atg13/Fip200 |
0.382 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261283 |
|
|
Homo sapiens |
HeLa Cell |
pmid |
sentence |
27334615 |
Thus, these data show ULK1–Rab1a interaction in intact cells and reveal that this interaction is C9orf72 dependent. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CDK1 | down-regulates activity
phosphorylation
|
RAB1A |
0.506 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261284 |
|
|
Homo sapiens |
HeLa Cell |
pmid |
sentence |
1902553 |
We now present biochemical evidence for a mitosis-specific p34cdc2 phosphorylation of RablAp and Rab4p.We also show that the distribution of RablAp and Rab4p between cytosolic and membrane-bound forms is different in interphase and mitotic cells. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |