| + |
PRKCA | up-regulates activity 
phosphorylation
|
LRRK1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276866 |
Ser1064 |
NRKVTIYsFTGNQRN |
in vitro |
|
| pmid |
sentence |
| 36040231 |
PKCα unexpectedly does not activate LRRK1 by phosphorylating the kinase domain, but instead phosphorylates a cluster of conserved residues (Ser1064, Ser1074 and Thr1075) located within a region of the CORB domain of the GTPase domain. we postulate that phosphorylation of Ser1064, Ser1074 and Thr1075 activates LRRK1 by promoting interaction and stabilization of the αC-helix on the kinase domain. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276867 |
Ser1074 |
GNQRNRCsTFRVKRN |
in vitro |
|
| pmid |
sentence |
| 36040231 |
PKCα unexpectedly does not activate LRRK1 by phosphorylating the kinase domain, but instead phosphorylates a cluster of conserved residues (Ser1064, Ser1074 and Thr1075) located within a region of the CORB domain of the GTPase domain. we postulate that phosphorylation of Ser1064, Ser1074 and Thr1075 activates LRRK1 by promoting interaction and stabilization of the αC-helix on the kinase domain. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276865 |
Thr1075 |
NQRNRCStFRVKRNQ |
in vitro |
|
| pmid |
sentence |
| 36040231 |
PKCα unexpectedly does not activate LRRK1 by phosphorylating the kinase domain, but instead phosphorylates a cluster of conserved residues (Ser1064, Ser1074 and Thr1075) located within a region of the CORB domain of the GTPase domain. we postulate that phosphorylation of Ser1064, Ser1074 and Thr1075 activates LRRK1 by promoting interaction and stabilization of the αC-helix on the kinase domain. |
|
| Publications: |
3 |
Organism: |
In Vitro |
| + |
LRRK1 | up-regulates activity
phosphorylation
|
CDK5RAP2 |
0.509 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275468 |
Ser140 |
SLAEAGGsEIQRVKE |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 26192437 |
Interestingly, LRRK1 in turn phosphorylates CDK5RAP2(Cep215), a human homologue of Drosophila Centrosomin (Cnn), in its gamma-tubulin-binding motif, thus promoting the interaction of CDK5RAP2 with gamma-tubulin. LRRK1 phosphorylation of CDK5RAP2 Ser 140 is necessary for CDK5RAP2-dependent microtubule nucleation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PLK1 | up-regulates activity
phosphorylation
|
LRRK1 |
0.346 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275467 |
Ser1817 |
GDSIADVsIMYSEEL |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 26192437 |
Here we show that LRRK1 is a PLK1 substrate that is phosphorylated on Ser 1790. PLK1 phosphorylation is required for CDK1-mediated activation of LRRK1 at the centrosomes |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
LRRK1 | up-regulates activity
phosphorylation
|
RAB7A |
0.389 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-278212 |
Ser72 |
AGQERFQsLGVAFYR |
Homo sapiens |
|
| pmid |
sentence |
| 33459343 |
Overall, these data suggest that LRRK1 is able to phosphorylate endogenous Rab7A at Ser72. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
LRRK1 | up-regulates activity
phosphorylation
|
CLIP1 |
0.402 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275469 |
Thr1430 |
EMFGHWAtNCNDDET |
|
|
| pmid |
sentence |
| 25413345 |
LRRK1 phosphorylates CLIP-170 at Thr1384, located in its C-terminal zinc knuckle motif, and this promotes the association of CLIP-170 with dynein-dynactin complexes. |
|
| Publications: |
1 |
| + |
EGFR | down-regulates activity 
phosphorylation
|
LRRK1 |
0.344 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262856 |
Tyr971 |
TQQTEEQyFQFLAKF |
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 22337768 |
In this study, we demonstrate that EGFR regulates the kinase activity of LRRK1 via tyrosine phosphorylation and that this is required for proper endosomal trafficking of EGFR. Phosphorylation of LRRK1 at Tyr-944 results in reduced LRRK1 kinase activity. |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
3.0
LRRK1
- 
- 