+ |
PRKACA |
phosphorylation
|
STK24 |
0.218 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-74284 |
Thr18 |
ALNKRRAtLPHPGGS |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
10644707 |
Further experiments demonstrated that mst3b, but not mst3, was effectively phosphorylated by activation of cyclic amp-dependent protein kinase (pka) in both in vivo and in vitro assays. The mutation of thr-18 into ala in mst3b (t18a), a putative pka phosphorylation site that is absent in mst3, abolished its phosphorylation by pka. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Tissue: |
Brain, Kidney |
+ |
STK24 | up-regulates
phosphorylation
|
STK24 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-150131 |
Thr190 |
DTQIKRNtFVGTPFW |
Homo sapiens |
|
pmid |
sentence |
17046825 |
Inhibition of cell migration by autophosphorylated mammalian sterile 20-like kinase 3 (mst3) involves paxillin and protein-tyrosine phosphatase-pest. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Tissue: |
Kidney |
+ |
STK24 | up-regulates
phosphorylation
|
STK38L |
0.451 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-142510 |
Thr442 |
DWVFLNYtYKRFEGL |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
16314523 |
Ndr1/ndr2 protein kinase is activated by phosphorylation on the activation loop phosphorylation site ser281/ser282 and the hydrophobic motif phosphorylation site thr444/thr442. Autophosphorylation of ndr is responsible for phosphorylation on ser281/ser282, whereas thr444/thr442 is targeted by an upstream kinase. Here we show that mst3, a mammalian ste20-like protein kinase, is able to phosphorylate ndr protein kinase at thr444/thr442. In vitro, mst3 selectively phosphorylated thr442 of ndr2, resulting in a 10-fold stimulation of ndr activity. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
STK24 | up-regulates
phosphorylation
|
STK38 |
0.39 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-142467 |
Thr444 |
DWVFINYtYKRFEGL |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
16314523 |
Ndr1/ndr2 protein kinase is activated by phosphorylation on the activation loop phosphorylation site ser281/ser282 and the hydrophobic motif phosphorylation site thr444/thr442. Autophosphorylation of ndr is responsible for phosphorylation on ser281/ser282, whereas thr444/thr442 is targeted by an upstream kinase. Here we show that mst3, a mammalian ste20-like protein kinase, is able to phosphorylate ndr protein kinase at thr444/thr442. In vitro, mst3 selectively phosphorylated thr442 of ndr2, resulting in a 10-fold stimulation of ndr activity. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
STK24 | up-regulates activity
phosphorylation
|
RAB8A |
0.278 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-260265 |
Thr72 |
AGQERFRtITTAYYR |
in vitro |
|
pmid |
sentence |
32227113 |
In a screen for Rab8A kinases we identify TAK1 and MST3 kinases that can efficiently phosphorylate the Switch II residue Threonine72 (Thr72) in a similar manner as LRRK2 in vitro. |Overall our data suggests that the phosphorylation of Rab8A at Ser111 may influence Switch II-binding by regulators, thus disrupting interactions with its cognate GEF and moderately impairs its interaction with GAPs.|The antagonistic interplay between Ser111 phosphorylation and Thr72 phosphorylation is genetically concordant with how respective mutations in PINK1 and LRRK2 cause Parkinson’s disease |
|
Publications: |
1 |
Organism: |
In Vitro |