+ |
PAK3 | down-regulates
phosphorylation
|
TNNI3 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-134593 |
Ser150 |
TLRRVRIsADAMMQA |
Homo sapiens |
|
pmid |
sentence |
15769444 |
In vitro addition of pak3 to skinned rat cardiac fibres increased myofilament ca2+ sensitivity with no change in maximal ca2+-activated force [67]. These effects were associated with pak3-induced phosphorylation of myofilament proteins, including ctni which was phosphorylated at a novel site, ser149, located in the region forming a ca2+-sensitive interaction with the n-terminal regulatory domain of tnc. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Tissue: |
Muscle |
+ |
PAK3 |
phosphorylation
|
TNNI3 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-92990 |
Ser150 |
TLRRVRIsADAMMQA |
Homo sapiens |
|
pmid |
sentence |
12242269 |
Importantly, cardiac troponin i was found to be phosphorylated at serine 149 of human cardiac troponin i, representing a novel phosphorylation site. These findings suggest a novel mechanism of modulating the calcium sensitivity of cardiac muscle contraction. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Tissue: |
Muscle |
+ |
PAK3 | up-regulates activity
phosphorylation
|
PAK3 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250245 |
Ser154 |
VNNQKYMsFTSGDKS |
in vitro |
|
pmid |
sentence |
11278486 |
Both in vivo and in vitro analyses demonstrate that, although most phosphorylation events in the PAK N-terminal regulatory domain play no direct role in activation, a phosphorylation of alphaPAK serine 144 or betaPAK serine 139, which lie in the kinase inhibitory domain, significantly contribute to activation. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
PAK3 | up-regulates
phosphorylation
|
RAF1 |
0.535 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-62043 |
Ser338 |
RPRGQRDsSYYWEIE |
Homo sapiens |
|
pmid |
sentence |
9823899 |
The protein kinase pak3 positively regulates raf-1 activity through phosphorylation of serine 338. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PAK3 | up-regulates activity
phosphorylation
|
SYN1 |
0.339 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250246 |
Ser605 |
AGPTRQAsQAGPVPR |
Rattus norvegicus |
PC-12 Cell |
pmid |
sentence |
12237306 |
Synapsin I is phosphorylated at Ser603 by p21-activated kinases. the Ser603 residue must be one of the pivotal sites for the release |
|
Publications: |
1 |
Organism: |
Rattus Norvegicus |
+ |
PAK3 | down-regulates
phosphorylation
|
CALD1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-167976 |
Ser714 |
EGVRNIKsMWEKGNV |
Homo sapiens |
|
pmid |
sentence |
20858431 |
We investigated the effects of phosphorylation by p(21)-activated kinase 3 (pak) and calmodulin on the 22 kda c-terminal fragment of caldesmon (cad22). We substituted the major pak sites, ser-672 and ser-702, with either alanine or aspartic acid to mimic nonphosphorylated and constitutively phosphorylated states of caldesmon, respectively. Phosphorylation at these sites weakened ca(2+)-calmodulin binding further and reduced the inhibitory activity of cad22 in the absence of ca(2+)-calmodulin. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-167980 |
Ser744 |
GLKVGVSsRINEWLT |
Homo sapiens |
|
pmid |
sentence |
20858431 |
We investigated the effects of phosphorylation by p(21)-activated kinase 3 (pak) and calmodulin on the 22 kda c-terminal fragment of caldesmon (cad22). We substituted the major pak sites, ser-672 and ser-702, with either alanine or aspartic acid to mimic nonphosphorylated and constitutively phosphorylated states of caldesmon, respectively. Phosphorylation at these sites weakened ca(2+)-calmodulin binding further and reduced the inhibitory activity of cad22 in the absence of ca(2+)-calmodulin. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
Tissue: |
Muscle, Smooth Muscle |
+ |
PAK3 | down-regulates activity
phosphorylation
|
SORT1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273719 |
Ser793 |
RFLVHRYsVLQQHAE |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
31767632 |
PAKs specifically phosphorylate Ser15 of the sortilin-cd and alter its trafficking. It can be concluded that PAK1-3 may indeed instigate the phosphorylation of sortilin and that they target a single serine residue (Ser15) located in the kinase domain-binding site of the sortilin-cd. Full-length sortilins with the serine at position 793 (residue 15 in the cytoplasmic domain) (for the sequence, see Fig. 2). Phosphorylation (Ser15) downregulates the sortilin–AP-1 interaction. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PAK3 | up-regulates activity
phosphorylation
|
MYO6 |
0.341 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250244 |
Thr405 |
TAGGTKGtVIKVPLK |
in vitro |
|
pmid |
sentence |
11517222 |
P21-activated kinase 3 phosphorylated myosin VI, and the site was identified as Thr(406). The phosphorylation of myosin VI significantly facilitated the actin-translocating activity of myosin VI. |
|
Publications: |
1 |
Organism: |
In Vitro |