+ |
PLK3 | down-regulates activity
phosphorylation
|
SNCB |
0.389 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-189057 |
Ser118 |
LMEPEGEsYEDPPQE |
Homo sapiens |
|
pmid |
sentence |
19889641 |
Polo-like kinase (plk) family (plk1, plk2, and plk3) phosphorylate alpha-syn and beta-syn specifically at ser-129 and ser-118, respectively. Polo-like kinase 2 (plk2) phosphorylates alpha-synuclein at serine 129 in central nervous system. The membrane association of pd-linked mutant alpha -synuclein, but not wild-type -synuclein, was increased by serine 129 phosphorylation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PLK3 | down-regulates activity
phosphorylation
|
SNCA |
0.324 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-189053 |
Ser129 |
NEAYEMPsEEGYQDY |
Homo sapiens |
|
pmid |
sentence |
19889641 |
Polo-like kinase (plk) family (plk1, plk2, and plk3) phosphorylate alpha-syn and beta-syn specifically at ser-129 and ser-118, respectively. Polo-like kinase 2 (plk2) phosphorylates alpha-synuclein at serine 129 in central nervous system. The membrane association of pd-linked mutant alpha -synuclein, but not wild-type -synuclein, was increased by serine 129 phosphorylation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PLK3 | up-regulates
phosphorylation
|
CDC25C |
0.721 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-122090 |
Ser191 |
EDQAEEIsDELMEFS |
Homo sapiens |
|
pmid |
sentence |
14968113 |
Cdc25c phosphorylation on serine 191 by plk3 promotes its nuclear translocation |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-122094 |
Ser198 |
SDELMEFsLKDQEAK |
Homo sapiens |
|
pmid |
sentence |
14968113 |
Cdc25c phosphorylation on serine 191 by plk3 promotes its nuclear translocation |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
PLK3 | up-regulates activity
phosphorylation
|
TP53 |
0.695 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-109239 |
Ser20 |
PLSQETFsDLWKLLP |
Homo sapiens |
Fibroblast |
pmid |
sentence |
11447225 |
Upon exposure of cells to hydrogen peroxide (h(2)o(2)) phosphorylation of p53 was rapidly induced in human fibroblast gm00637, and this phosphorylation occurred on serine 9, serine 15, serine 20, but not on serine 392. In addition, h(2)o(2)-induced phosphorylation of p53 was followed by induction of p21, suggesting functional activation of p53. Ectopic expression of a plk3 dominant negative mutant, plk3(k52r), in gm00637 cells suppressed h(2)o(2)-induced serine 20 phosphorylation. Taken together, our studies strongly suggest that the oxidative stress-induced activation of p53 is at least in part mediated by plk3. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PLK3 |
phosphorylation
|
CDC25C |
0.721 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-249030 |
Ser216 |
SGLYRSPsMPENLNR |
in vitro |
|
pmid |
sentence |
10557092 |
The physical association and phosphorylation of Cdc25C protein phosphatase by Prk. | Further studies reveal that His6-Prk phosphorylates Cdc25C on serine216, a residue also phosphorylated by Chk1 and Chk2. Together, these observations strongly suggest that Prk's role in mitosis is at least partly mediated through direct regulation of Cdc25C. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
PLK3 | up-regulates
phosphorylation
|
VRK1 |
0.487 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-182858 |
Ser342 |
DDGKLDLsVVENGGL |
Homo sapiens |
|
pmid |
sentence |
19103756 |
Vrk1 does not phosphorylate plk3, but plk3 phosphorylates the c-terminal region of vrk1 in ser342. Vrk1 with substitutions in s342 is catalytically active but blocks golgi fragmentation, indicating that its specific phosphorylation is necessary for this process. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PLK3 | down-regulates activity
phosphorylation
|
PTEN |
0.342 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-168469 |
Ser370 |
TSVTPDVsDNEPDHY |
Homo sapiens |
|
pmid |
sentence |
20940307 |
Plk3 phosphorylates pten on thr-366 and ser-370. Plk3-mediated phosphorylation facilitates pten stabilization, thereby negatively regulating the pi3k/pdk1/akt1 signaling axis |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-168473 |
Thr366 |
ASSSTSVtPDVSDNE |
Homo sapiens |
|
pmid |
sentence |
20940307 |
Plk3 phosphorylates pten on thr-366 and ser-370. Plk3-mediated phosphorylation facilitates pten stabilization, thereby negatively regulating the pi3k/pdk1/akt1 signaling axis |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
PLK3 | up-regulates
phosphorylation
|
BCL2L1 |
0.399 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-172230 |
Ser49 |
ESEMETPsAINGNPS |
Homo sapiens |
|
pmid |
sentence |
21336504 |
Polo kinase 3 (plk3) was implicated in bcl-xl(ser49) phosphorylation. These data indicate that, during g2 checkpoint, phospho-bcl-xl(ser49) is another downstream target of plk3, acting to stabilize g2 arrest. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PLK3 | down-regulates
phosphorylation
|
HIF1A |
0.355 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-178739 |
Ser576 |
DDDFQLRsFDQLSPL |
Homo sapiens |
HeLa Cell |
pmid |
sentence |
18519666 |
Polo-like kinase 3 functions as a tumor suppressor and is a negative regulator of hypoxia-inducible factor-1 alpha under hypoxic conditionsplk3 can potentially inhibit hif-1_ by physical interaction and direct phosphorylation |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-178743 |
Ser657 |
ETTSATSsPYRDTQS |
Homo sapiens |
HeLa Cell |
pmid |
sentence |
18519666 |
Polo-like kinase 3 functions as a tumor suppressor and is a negative regulator of hypoxia-inducible factor-1 alpha under hypoxic conditionsplk3 can potentially inhibit hif-1_ by physical interaction and direct phosphorylation |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
PLK3 | up-regulates activity
phosphorylation
|
CHEK2 |
0.644 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276052 |
Ser62 |
SSSGTLSsLETVSTQ |
in vitro |
|
pmid |
sentence |
16481012 |
Plk3 phosphorylates Chk2 at two residues, serine 62 (S62) and serine 73 (S73) in vitro, and this phosphorylation facilitates subsequent phosphorylation of Chk2 on T68 by ATM in response to DNA damage. When the Chk2 mutant construct GFP-Chk2 S73A (serine 73 mutated to alanine) is transfected into cells, it no longer associates with a large complex in vivo, and manifests a significant reduction in kinase activity. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276051 |
Ser73 |
VSTQELYsIPEDQEP |
in vitro |
|
pmid |
sentence |
16481012 |
Plk3 phosphorylates Chk2 at two residues, serine 62 (S62) and serine 73 (S73) in vitro, and this phosphorylation facilitates subsequent phosphorylation of Chk2 on T68 by ATM in response to DNA damage. When the Chk2 mutant construct GFP-Chk2 S73A (serine 73 mutated to alanine) is transfected into cells, it no longer associates with a large complex in vivo, and manifests a significant reduction in kinase activity. |
|
Publications: |
2 |
Organism: |
In Vitro |
+ |
PLK3 | up-regulates
phosphorylation
|
JUN |
0.379 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-179551 |
Ser63 |
KNSDLLTsPDVGLLK |
Homo sapiens |
|
pmid |
sentence |
18650425 |
Stress-induced c-jun activation mediated by polo-like kinase 3 in corneal epithelial cells. Hypoxia/reoxygenation activated plk3 in hce cells to directly phosphorylate c-jun proteins at phosphorylation sites ser-63 and ser-73, and to increase dna binding activity of c-jun. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-157721 |
Ser63 |
KNSDLLTsPDVGLLK |
Homo sapiens |
|
pmid |
sentence |
17804415 |
Stress-induced c-jun activation mediated by polo-like kinase 3 in corneal epithelial cells. Hypoxia/reoxygenation activated plk3 in hce cells to directly phosphorylate c-jun proteins at phosphorylation sites ser-63 and ser-73, and to increase dna binding activity of c-jun. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-157725 |
Ser73 |
VGLLKLAsPELERLI |
Homo sapiens |
|
pmid |
sentence |
17804415 |
Stress-induced c-jun activation mediated by polo-like kinase 3 in corneal epithelial cells. Hypoxia/reoxygenation activated plk3 in hce cells to directly phosphorylate c-jun proteins at phosphorylation sites ser-63 and ser-73, and to increase dna binding activity of c-jun. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-179555 |
Ser73 |
VGLLKLAsPELERLI |
Homo sapiens |
|
pmid |
sentence |
18650425 |
Stress-induced c-jun activation mediated by polo-like kinase 3 in corneal epithelial cells. Hypoxia/reoxygenation activated plk3 in hce cells to directly phosphorylate c-jun proteins at phosphorylation sites ser-63 and ser-73, and to increase dna binding activity of c-jun. |
|
Publications: |
4 |
Organism: |
Homo Sapiens |
+ |
PLK3 | up-regulates
phosphorylation
|
TOP2A |
0.272 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-159596 |
Thr1343 |
FSDFDEKtDDEDFVP |
Homo sapiens |
|
pmid |
sentence |
18062778 |
The direct phosphorylation of thr(1342) of topoisomerase iialpha by plk3 was demonstrated with an in vitro kinase assay, and overexpression of plk3 induced the phosphorylation of thr(1342) in cellular topoisomerase iialpha. it is possible that plk3 regulates the activity of topoisomerase iia by phosphorylation in a cell-cycle dependent manner. Another possibility is that plk3 regulates the activity of topoisomerase iia when the checkpoint is activated. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PLK3 | up-regulates activity
phosphorylation
|
CASP8 |
0.346 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272995 |
Thr273 |
DAGALTTtFEELHFE |
|
|
pmid |
sentence |
27325299 |
Furthermore, we identify caspase-8 as a new substrate for Plk3. Phosphorylation occurs on T273 and results in stimulation of caspase-8 proapoptotic function. |
|
Publications: |
1 |
+ |
PLK3 | up-regulates
phosphorylation
|
ATF2 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-170004 |
Thr69 |
SVIVADQtPTPTRFL |
Homo sapiens |
|
pmid |
sentence |
21098032 |
Kinase activity of plk3 was significantly activated by hyperosmotic stimulation. Further downstream, active plk3 phosphorylated atf-2 at the thr-71 site in vivo and in vitro. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-163270 |
Thr69 |
SVIVADQtPTPTRFL |
Homo sapiens |
|
pmid |
sentence |
20068231 |
Phosphorylation of thr-69 by mapk14 and mapk11, and at thr-71 by mapk1/erk2, mapk3/erk1, mapk11, mapk12 and mapk14 in response to external stimulus like insulin causes increased transcriptional activity. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-170008 |
Thr71 |
IVADQTPtPTRFLKN |
Homo sapiens |
|
pmid |
sentence |
21098032 |
Kinase activity of plk3 was significantly activated by hyperosmotic stimulation. Further downstream, active plk3 phosphorylated atf-2 at the thr-71 site in vivo and in vitro. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-163274 |
Thr71 |
IVADQTPtPTRFLKN |
Homo sapiens |
|
pmid |
sentence |
20068231 |
Phosphorylation of thr-69 by mapk14 and mapk11, and at thr-71 by mapk1/erk2, mapk3/erk1, mapk11, mapk12 and mapk14 in response to external stimulus like insulin causes increased transcriptional activity. |
|
Publications: |
4 |
Organism: |
Homo Sapiens |
+ |
PLK3 | down-regulates
phosphorylation
|
CDC25A |
0.393 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-160228 |
Thr80 |
RMGSSEStDSGFCLD |
Homo sapiens |
|
pmid |
sentence |
18167338 |
Here, we demonstrate that glycogen synthase kinase-3beta (gsk-3beta) phosphorylates cdc25a to promote its proteolysis in early cell-cycle phases. Phosphorylation by gsk-3beta requires priming of cdc25a, and this can be catalyzed by polo-like kinase 3 (plk-3) |
|
Publications: |
1 |
Organism: |
Homo Sapiens |