| + |
Cullin 3-RBX1-Skp1 | down-regulates activity 
monoubiquitination
|
PLK1 |
0.422 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272110 |
Lys492 |
YMSEHLLkAGANITP |
in vitro |
|
| pmid |
sentence |
| 23455478 |
Here, we identify PLK1 as a target of the cullin 3 (CUL3)-based E3 ubiquitin ligase, containing the BTB adaptor KLHL22, which regulates chromosome alignment and PLK1 kinetochore localization but not PLK1 stability. In the absence of KLHL22, PLK1 accumulates on kinetochores, resulting in activation of the spindle assembly checkpoint (SAC). CUL3-KLHL22 ubiquitylates Lys 492, located within the PBD, leading to PLK1 dissociation from kinetochore phosphoreceptors. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PLK1 | down-regulates activity
phosphorylation
|
MAD2L1BP |
0.434 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265970 |
Ser102 |
KHFYRKPsPQAEEML |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 31118282 |
Purified Plk1 bound to p31comet and phosphorylated it, resulting in the suppression of its activity (with TRIP13) to disassemble checkpoint complexes. We conclude that Plk1 phosphorylates p31 on S102 and on five additional sites. The phosphorylation of the additional sites was possibly not detectable in HeLa cell extracts due to the opposing action of protein phosphatases. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PLK1 | down-regulates activity
phosphorylation
|
REST |
0.303 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-279380 |
Ser1030 |
MSEGSDDsGLHGARP |
Homo sapiens |
|
| pmid |
sentence |
| 25453754 |
Mass spectrometry revealed that PLK1 phosphorylates REST on serine-1030 ( xref and xref ).|Notably, PLK1 depletion significantly increased REST protein half-life (XREF_FIG, XREF_SUPPLEMENTARY), indicating PLK1 antagonizes REST abundance by restraining REST protein stability. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PLK1 | up-regulates activity 
phosphorylation
|
TTK |
0.376 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276220 |
Ser108 |
DKYGQNEsFARIQVR |
in vitro |
|
| pmid |
sentence |
| 26119734 |
Here, we demonstrate that Plk1 promotes checkpoint signaling at kinetochores through the phosphorylation of at least two Mps1 substrates, including KNL-1 and Mps1 itself. As a result, Plk1 activity enhances Mps1 catalytic activity as well as the recruitment of the SAC components Mad1:C-Mad2 and Bub3:BubR1 to kinetochores. Plk1 Targets Mps1 Autophosphorylation Sites In Vitro |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276216 |
Ser214 |
TVLTAQEsFSGSLGH |
in vitro |
|
| pmid |
sentence |
| 26119734 |
Here, we demonstrate that Plk1 promotes checkpoint signaling at kinetochores through the phosphorylation of at least two Mps1 substrates, including KNL-1 and Mps1 itself. As a result, Plk1 activity enhances Mps1 catalytic activity as well as the recruitment of the SAC components Mad1:C-Mad2 and Bub3:BubR1 to kinetochores. Plk1 Targets Mps1 Autophosphorylation Sites In Vitro |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276199 |
Ser291 |
CDVKTDDsVVPCFMK |
in vitro |
|
| pmid |
sentence |
| 26119734 |
Here, we demonstrate that Plk1 promotes checkpoint signaling at kinetochores through the phosphorylation of at least two Mps1 substrates, including KNL-1 and Mps1 itself. As a result, Plk1 activity enhances Mps1 catalytic activity as well as the recruitment of the SAC components Mad1:C-Mad2 and Bub3:BubR1 to kinetochores. Plk1 Targets Mps1 Autophosphorylation Sites In Vitro |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276212 |
Ser321 |
SKPSGNDsCELRNLK |
in vitro |
|
| pmid |
sentence |
| 26119734 |
Here, we demonstrate that Plk1 promotes checkpoint signaling at kinetochores through the phosphorylation of at least two Mps1 substrates, including KNL-1 and Mps1 itself. As a result, Plk1 activity enhances Mps1 catalytic activity as well as the recruitment of the SAC components Mad1:C-Mad2 and Bub3:BubR1 to kinetochores. Plk1 Targets Mps1 Autophosphorylation Sites In Vitro |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276197 |
Ser333 |
NLKSVQNsHFKEPLV |
in vitro |
|
| pmid |
sentence |
| 26119734 |
Here, we demonstrate that Plk1 promotes checkpoint signaling at kinetochores through the phosphorylation of at least two Mps1 substrates, including KNL-1 and Mps1 itself. As a result, Plk1 activity enhances Mps1 catalytic activity as well as the recruitment of the SAC components Mad1:C-Mad2 and Bub3:BubR1 to kinetochores. Plk1 Targets Mps1 Autophosphorylation Sites In Vitro |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276198 |
Ser345 |
PLVSDEKsSELIITD |
in vitro |
|
| pmid |
sentence |
| 26119734 |
Here, we demonstrate that Plk1 promotes checkpoint signaling at kinetochores through the phosphorylation of at least two Mps1 substrates, including KNL-1 and Mps1 itself. As a result, Plk1 activity enhances Mps1 catalytic activity as well as the recruitment of the SAC components Mad1:C-Mad2 and Bub3:BubR1 to kinetochores. Plk1 Targets Mps1 Autophosphorylation Sites In Vitro |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276200 |
Ser362 |
TLKNKTEsSLLAKLE |
in vitro |
|
| pmid |
sentence |
| 26119734 |
Here, we demonstrate that Plk1 promotes checkpoint signaling at kinetochores through the phosphorylation of at least two Mps1 substrates, including KNL-1 and Mps1 itself. As a result, Plk1 activity enhances Mps1 catalytic activity as well as the recruitment of the SAC components Mad1:C-Mad2 and Bub3:BubR1 to kinetochores. Plk1 Targets Mps1 Autophosphorylation Sites In Vitro |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276208 |
Ser363 |
LKNKTESsLLAKLEE |
in vitro |
|
| pmid |
sentence |
| 26119734 |
Here, we demonstrate that Plk1 promotes checkpoint signaling at kinetochores through the phosphorylation of at least two Mps1 substrates, including KNL-1 and Mps1 itself. As a result, Plk1 activity enhances Mps1 catalytic activity as well as the recruitment of the SAC components Mad1:C-Mad2 and Bub3:BubR1 to kinetochores. Plk1 Targets Mps1 Autophosphorylation Sites In Vitro |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276206 |
Ser37 |
EDLTDELsLNKISAD |
in vitro |
|
| pmid |
sentence |
| 26119734 |
Here, we demonstrate that Plk1 promotes checkpoint signaling at kinetochores through the phosphorylation of at least two Mps1 substrates, including KNL-1 and Mps1 itself. As a result, Plk1 activity enhances Mps1 catalytic activity as well as the recruitment of the SAC components Mad1:C-Mad2 and Bub3:BubR1 to kinetochores. Plk1 Targets Mps1 Autophosphorylation Sites In Vitro |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276202 |
Thr12 |
DLSGRELtIDSIMNK |
in vitro |
|
| pmid |
sentence |
| 26119734 |
Here, we demonstrate that Plk1 promotes checkpoint signaling at kinetochores through the phosphorylation of at least two Mps1 substrates, including KNL-1 and Mps1 itself. As a result, Plk1 activity enhances Mps1 catalytic activity as well as the recruitment of the SAC components Mad1:C-Mad2 and Bub3:BubR1 to kinetochores. Plk1 Targets Mps1 Autophosphorylation Sites In Vitro |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276219 |
Thr210 |
LSASTVLtAQESFSG |
in vitro |
|
| pmid |
sentence |
| 26119734 |
Here, we demonstrate that Plk1 promotes checkpoint signaling at kinetochores through the phosphorylation of at least two Mps1 substrates, including KNL-1 and Mps1 itself. As a result, Plk1 activity enhances Mps1 catalytic activity as well as the recruitment of the SAC components Mad1:C-Mad2 and Bub3:BubR1 to kinetochores. Plk1 Targets Mps1 Autophosphorylation Sites In Vitro |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276204 |
Thr33 |
KFKNEDLtDELSLNK |
in vitro |
|
| pmid |
sentence |
| 26119734 |
Here, we demonstrate that Plk1 promotes checkpoint signaling at kinetochores through the phosphorylation of at least two Mps1 substrates, including KNL-1 and Mps1 itself. As a result, Plk1 activity enhances Mps1 catalytic activity as well as the recruitment of the SAC components Mad1:C-Mad2 and Bub3:BubR1 to kinetochores. Plk1 Targets Mps1 Autophosphorylation Sites In Vitro |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276210 |
Thr371 |
LLAKLEEtKEYQEPE |
in vitro |
|
| pmid |
sentence |
| 26119734 |
Here, we demonstrate that Plk1 promotes checkpoint signaling at kinetochores through the phosphorylation of at least two Mps1 substrates, including KNL-1 and Mps1 itself. As a result, Plk1 activity enhances Mps1 catalytic activity as well as the recruitment of the SAC components Mad1:C-Mad2 and Bub3:BubR1 to kinetochores. Plk1 Targets Mps1 Autophosphorylation Sites In Vitro |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276222 |
Thr458 |
CKTPSSNtLDDYMSC |
in vitro |
|
| pmid |
sentence |
| 26119734 |
Here, we demonstrate that Plk1 promotes checkpoint signaling at kinetochores through the phosphorylation of at least two Mps1 substrates, including KNL-1 and Mps1 itself. As a result, Plk1 activity enhances Mps1 catalytic activity as well as the recruitment of the SAC components Mad1:C-Mad2 and Bub3:BubR1 to kinetochores. Plk1 Targets Mps1 Autophosphorylation Sites In Vitro |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276218 |
Thr46 |
NKISADTtDNSGTVN |
in vitro |
|
| pmid |
sentence |
| 26119734 |
Here, we demonstrate that Plk1 promotes checkpoint signaling at kinetochores through the phosphorylation of at least two Mps1 substrates, including KNL-1 and Mps1 itself. As a result, Plk1 activity enhances Mps1 catalytic activity as well as the recruitment of the SAC components Mad1:C-Mad2 and Bub3:BubR1 to kinetochores. Plk1 Targets Mps1 Autophosphorylation Sites In Vitro |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276214 |
Thr564 |
LEEADNQtLDSYRNE |
in vitro |
|
| pmid |
sentence |
| 26119734 |
Here, we demonstrate that Plk1 promotes checkpoint signaling at kinetochores through the phosphorylation of at least two Mps1 substrates, including KNL-1 and Mps1 itself. As a result, Plk1 activity enhances Mps1 catalytic activity as well as the recruitment of the SAC components Mad1:C-Mad2 and Bub3:BubR1 to kinetochores. Plk1 Targets Mps1 Autophosphorylation Sites In Vitro |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276221 |
Thr594 |
RLYDYEItDQYIYMV |
in vitro |
|
| pmid |
sentence |
| 26119734 |
Here, we demonstrate that Plk1 promotes checkpoint signaling at kinetochores through the phosphorylation of at least two Mps1 substrates, including KNL-1 and Mps1 itself. As a result, Plk1 activity enhances Mps1 catalytic activity as well as the recruitment of the SAC components Mad1:C-Mad2 and Bub3:BubR1 to kinetochores. Plk1 Targets Mps1 Autophosphorylation Sites In Vitro |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-278246 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 26119734 |
As a result, Plk1 activity enhances Mps1 catalytic activity as well as the recruitment of the spindle assembly checkpoint components Mad1:C-Mad2 and Bub3:BubR1 to kinetochores.|When assayed in vitro, Plk1 readily phosphorylated kinase-dead Mps1, confirming earlier data (Dou et al., 2011). |
|
| Publications: |
18 |
Organism: |
In Vitro, Homo Sapiens |
| + |
PLK1 | down-regulates
phosphorylation
|
PINX1 |
0.358 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-166317 |
Ser110 |
SDKKEKKsFSLEEKS |
Homo sapiens |
|
| pmid |
sentence |
| 20573420 |
Here, we show that polo-like kinase 1 (plk1) is a novel interacting protein of pinx1. Plk1 interacts with and phosphorylates pinx1 in vivo and in vitro. Moreover, plk1-mediated phosphorylation of pinx1 at five phosphorylation sites is essential for its plk1-induced degradation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-166321 |
Ser117 |
SFSLEEKsKISKNRV |
Homo sapiens |
|
| pmid |
sentence |
| 20573420 |
Here, we show that polo-like kinase 1 (plk1) is a novel interacting protein of pinx1. Plk1 interacts with and phosphorylates pinx1 in vivo and in vitro. Moreover, plk1-mediated phosphorylation of pinx1 at five phosphorylation sites is essential for its plk1-induced degradation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-166325 |
Ser226 |
ATGKDVEsYLQPKAK |
Homo sapiens |
|
| pmid |
sentence |
| 20573420 |
Here, we show that polo-like kinase 1 (plk1) is a novel interacting protein of pinx1. Plk1 interacts with and phosphorylates pinx1 in vivo and in vitro. Moreover, plk1-mediated phosphorylation of pinx1 at five phosphorylation sites is essential for its plk1-induced degradation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-166329 |
Thr141 |
DLSSRSKtDLDCIFG |
Homo sapiens |
|
| pmid |
sentence |
| 20573420 |
Here, we show that polo-like kinase 1 (plk1) is a novel interacting protein of pinx1. Plk1 interacts with and phosphorylates pinx1 in vivo and in vitro. Moreover, plk1-mediated phosphorylation of pinx1 at five phosphorylation sites is essential for its plk1-induced degradation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-166333 |
Thr317 |
EDATLEEtLVKKKKK |
Homo sapiens |
|
| pmid |
sentence |
| 20573420 |
Here, we show that polo-like kinase 1 (plk1) is a novel interacting protein of pinx1. Plk1 interacts with and phosphorylates pinx1 in vivo and in vitro. Moreover, plk1-mediated phosphorylation of pinx1 at five phosphorylation sites is essential for its plk1-induced degradation. |
|
| Publications: |
5 |
Organism: |
Homo Sapiens |
| + |
PLK1 | down-regulates activity
dephosphorylation
|
STAG2 |
0.749 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275534 |
Ser1137 |
KRLRPEDsFMSVYPM |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 15737063 |
Two phosphorylation sites in Scc1 (Thr144 and Thr312) match the consensus proposed by Nakajima et al. [24]. These two sites, in addition to one in Scc1 (Ser454) and three in SA2 (Thr1109, Ser1137, and Ser1224) conform with the consensus proposed by Barr et al. [25]. These findings are consistent with the possibility that at least some of the sites in Scc1 and SA2 are directly phosphorylated by Plk1.|Phosphorylation of SA2 Is Essential for the Dissociation of Cohesin from Chromosomes during Prophase and Prometaphase |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275532 |
Ser1224 |
PASIMDEsVLGVSMF |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 15737063 |
Two phosphorylation sites in Scc1 (Thr144 and Thr312) match the consensus proposed by Nakajima et al. [24]. These two sites, in addition to one in Scc1 (Ser454) and three in SA2 (Thr1109, Ser1137, and Ser1224) conform with the consensus proposed by Barr et al. [25]. These findings are consistent with the possibility that at least some of the sites in Scc1 and SA2 are directly phosphorylated by Plk1.|Phosphorylation of SA2 Is Essential for the Dissociation of Cohesin from Chromosomes during Prophase and Prometaphase |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275533 |
Thr1109 |
MWLSREQtLHTPVMM |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 15737063 |
Two phosphorylation sites in Scc1 (Thr144 and Thr312) match the consensus proposed by Nakajima et al. [24]. These two sites, in addition to one in Scc1 (Ser454) and three in SA2 (Thr1109, Ser1137, and Ser1224) conform with the consensus proposed by Barr et al. [25]. These findings are consistent with the possibility that at least some of the sites in Scc1 and SA2 are directly phosphorylated by Plk1.|Phosphorylation of SA2 Is Essential for the Dissociation of Cohesin from Chromosomes during Prophase and Prometaphase |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
PLK1 | down-regulates activity
phosphorylation
|
SNCB |
0.312 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-176079 |
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 |
| + |
PLK1 | down-regulates
phosphorylation
|
WEE1 |
0.656 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-139473 |
Ser123 |
EEGFGSSsPVKSPAA |
Homo sapiens |
|
| pmid |
sentence |
| 16085715 |
Phosphorylation of serines 53 and 123 (s53 and s123) of wee1a by polo-like kinase 1 (plk1) and cdk, respectively, are required for binding to beta-trcp. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-128643 |
Ser53 |
GHSTGEDsAFQEPDS |
Homo sapiens |
|
| pmid |
sentence |
| 15350223 |
Phosphorylation of serines 53 and 123 (s53 and s123) of wee1a by polo-like kinase 1 (plk1) and cdk, respectively, are required for binding to beta-trcp. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-139477 |
Ser53 |
GHSTGEDsAFQEPDS |
Homo sapiens |
|
| pmid |
sentence |
| 16085715 |
Phosphorylation of serines 53 and 123 (s53 and s123) of wee1a by polo-like kinase 1 (plk1) and cdk, respectively, are required for binding to beta-trcp. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-123832 |
Ser53 |
GHSTGEDsAFQEPDS |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 15070733 |
Phosphorylation of serines 53 and 123 (s53 and s123) of wee1a by polo-like kinase 1 (plk1) and cdk, respectively, are required for binding to beta-trcp. |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| + |
PLK1 | up-regulates activity
phosphorylation
|
CLASP2 |
0.64 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-278321 |
Ser1234 |
QGYDNSEsSVRKACV |
Homo sapiens |
|
| pmid |
sentence |
| 23045552 |
Cdk1 and Plk1 mediate a CLASP2 phospho-switch that stabilizes kinetochore-microtubule attachments.|Finally, we demonstrate that CLASP2 phosphorylation on S1234 and S1255 by Cdk1 and Plk1, respectively, increases with conditions that allow the establishment and stabilization of KT\u2013MT attachments ( xref ). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PLK1 | up-regulates activity
phosphorylation
|
CCNB1 |
0.927 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-105707 |
Ser126 |
PILVDTAsPSPMETS |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 11242082 |
Phosphorylation of cyclin b1 is central to its nuclear translocationduring cell-cycle progression in hela cells, a change in the kinase activity of endogenous plk1 toward s147 and/or s133 correlates with a kinase activity in the cell extractsa mutant cyclin b1 in which s133 and s147 are replaced by alanines remains in the cytoplasm, whereas wild-type cyclin b1 accumulates in the nucleus during prophase.Together, these results suggest that phosphorylation of s133 and s147 is necessary for the nuclear translocation of cyclin b1 during prophase, and that phosphorylation of s126 and s128 may stimulate the nuclear translocation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-105711 |
Ser128 |
LVDTASPsPMETSGC |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 11242082 |
Phosphorylation of cyclin b1 is central to its nuclear translocationduring cell-cycle progression in hela cells, a change in the kinase activity of endogenous plk1 toward s147 and/or s133 correlates with a kinase activity in the cell extractsa mutant cyclin b1 in which s133 and s147 are replaced by alanines remains in the cytoplasm, whereas wild-type cyclin b1 accumulates in the nucleus during prophase.Together, these results suggest that phosphorylation of s133 and s147 is necessary for the nuclear translocation of cyclin b1 during prophase, and that phosphorylation of s126 and s128 may stimulate the nuclear translocation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-105715 |
Ser133 |
SPSPMETsGCAPAEE |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 11242082 |
Phosphorylation of cyclin b1 is central to its nuclear translocationduring cell-cycle progression in hela cells, a change in the kinase activity of endogenous plk1 toward s147 and/or s133 correlates with a kinase activity in the cell extractsa mutant cyclin b1 in which s133 and s147 are replaced by alanines remains in the cytoplasm, whereas wild-type cyclin b1 accumulates in the nucleus during prophase.Together, these results suggest that phosphorylation of s133 and s147 is necessary for the nuclear translocation of cyclin b1 during prophase, and that phosphorylation of s126 and s128 may stimulate the nuclear translocation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-105719 |
Ser147 |
EDLCQAFsDVILAVN |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 11242082 |
Phosphorylation of cyclin b1 is central to its nuclear translocationduring cell-cycle progression in hela cells, a change in the kinase activity of endogenous plk1 toward s147 and/or s133 correlates with a kinase activity in the cell extractsa mutant cyclin b1 in which s133 and s147 are replaced by alanines remains in the cytoplasm, whereas wild-type cyclin b1 accumulates in the nucleus during prophase.Together, these results suggest that phosphorylation of s133 and s147 is necessary for the nuclear translocation of cyclin b1 during prophase, and that phosphorylation of s126 and s128 may stimulate the nuclear translocation. |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| + |
PLK1 | down-regulates activity
phosphorylation
|
SNCA |
0.344 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-189045 |
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 |
| + |
PLK1 | up-regulates
phosphorylation
|
TOP2A |
0.471 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-160233 |
Ser1337 |
LDSDEDFsDFDEKTD |
Homo sapiens |
|
| pmid |
sentence |
| 18171681 |
Plk1 phosphorylates ser(1337) and ser(1524) of topoiialpha plk1-associated phosphorylation is essential for the functions of topoiialpha in mitosis |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-160237 |
Ser1525 |
PIKYLEEsDEDDLF |
Homo sapiens |
|
| pmid |
sentence |
| 18171681 |
Plk1 phosphorylates ser(1337) and ser(1524) of topoiialpha plk1-associated phosphorylation is essential for the functions of topoiialpha in mitosis |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-182844 |
Ser1525 |
PIKYLEEsDEDDLF |
Homo sapiens |
|
| pmid |
sentence |
| 19098900 |
Here we report that when phosphorylated, ser 1524 of topo iialpha acts as a binding site for the brct domain of mdc1 (mediator of dna damage checkpoint protein-1), thereby recruiting mdc1 to chromatin |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
PLK1 | up-regulates
phosphorylation
|
RAN |
0.263 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-149073 |
Ser135 |
DRKVKAKsIVFHRKK |
Homo sapiens |
|
| pmid |
sentence |
| 16930555 |
Plk1 is capable of phosphorylating co-immunoprecipitated ran in vitro on serine-135 and ran is phosphorylated in vivo at the same site during mitosis when plk1 is normally activated. Deregulation of ran phosphorylation disrupts normal spindle structure and segregation of chromosomes. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PLK1 | up-regulates activity
phosphorylation
|
RSF1 |
0.349 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273590 |
Ser1359 |
ENVGKVGsPLDYSLV |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 26259146 |
Moreover, CDK1 phosphorylates RSF1 at Ser1375, and this phosphorylation is necessary for PLK1 recruitment. Subsequently, PLK1 phosphorylates RSF1 at Ser1359, stabilizing PLK1 deposition. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CHEK1 | up-regulates activity
phosphorylation
|
PLK1 |
0.312 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-279502 |
Ser137 |
LELCRRRsLLELHKR |
Homo sapiens |
|
| pmid |
sentence |
| 34197606 |
These results suggest that both PLK1 S137 and T210 sites can be phosphorylated in vitro by CHK1, but that S137 is the major site.|We reason that PARG and CHK1 inhibitors should also cause synthetic lethality : PARG inhibition sustains PLK1 inhibition at the PAR forest , while CHK1 inhibition blocks PLK1 reactivation and RAD51 phosphorylation at S14 and T309 . |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-279501 |
Thr210 |
YDGERKKtLCGTPNY |
Homo sapiens |
|
| pmid |
sentence |
| 34197606 |
These results suggest that both PLK1 S137 and T210 sites can be phosphorylated in vitro by CHK1, but that S137 is the major site.|We reason that PARG and CHK1 inhibitors should also cause synthetic lethality : PARG inhibition sustains PLK1 inhibition at the PAR forest , while CHK1 inhibition blocks PLK1 reactivation and RAD51 phosphorylation at S14 and T309 . |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PPP4C | down-regulates activity
dephosphorylation
|
PLK1 |
0.407 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277076 |
Ser137 |
LELCRRRsLLELHKR |
Homo sapiens |
|
| pmid |
sentence |
| 35546066 |
PPP4C dephosphorylated PLK1 at the S137 site, negatively regulating its activity in the DSB response in early embryonic cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PLK1 | down-regulates activity
phosphorylation
|
SUN1 |
0.446 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263098 |
Ser138 |
RPPVLDEsWIREQTT |
Homo sapiens |
|
| pmid |
sentence |
| 25482198 |
Here, we show that SUN1, located in the INM, undergoes mitosis-specific phosphorylation on at least 3 sites within its nucleoplasmic N-terminus. We further identify Cdk1 as the kinase responsible for serine 48 and 333 phosphorylation, while serine 138 is phosphorylated by Plk1. Together, these data support a model whereby mitotic phosphorylation of SUN1 disrupts interactions with nucleoplasmic binding partners, promoting disassembly of the nuclear lamina and, potentially, its chromatin interactions. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PLK1 | down-regulates quantity by destabilization
phosphorylation
|
CENPQ |
0.605 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265228 |
Ser138 |
MEDLTNVsSLLNMER |
Homo sapiens |
|
| pmid |
sentence |
| 25670858 |
Notably, although Plk1 did not alter the level of PBIP1 and CENP-Q ubiquitination, Plk1-dependent phosphorylation and delocalization of these proteins from kinetochores appeared to indirectly lead to their degradation in the cytosol. From these analyses, we identified nine CENP-Q residues (Thr-123, Thr-135, Ser-138, Ser-139, Ser-248, Ser-249, Ser-253, Ser-255, and Thr-256) that were phosphorylated in both in vitro and in vivo samples (Fig. 4B), suggesting that Plk1 phosphorylates these sites. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265233 |
Ser139 |
EDLTNVSsLLNMERA |
Homo sapiens |
|
| pmid |
sentence |
| 25670858 |
Notably, although Plk1 did not alter the level of PBIP1 and CENP-Q ubiquitination, Plk1-dependent phosphorylation and delocalization of these proteins from kinetochores appeared to indirectly lead to their degradation in the cytosol. From these analyses, we identified nine CENP-Q residues (Thr-123, Thr-135, Ser-138, Ser-139, Ser-248, Ser-249, Ser-253, Ser-255, and Thr-256) that were phosphorylated in both in vitro and in vivo samples (Fig. 4B), suggesting that Plk1 phosphorylates these sites. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265227 |
Ser248 |
DLDILHNsSQMKSMS |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 25670858 |
Notably, although Plk1 did not alter the level of PBIP1 and CENP-Q ubiquitination, Plk1-dependent phosphorylation and delocalization of these proteins from kinetochores appeared to indirectly lead to their degradation in the cytosol. From these analyses, we identified nine CENP-Q residues (Thr-123, Thr-135, Ser-138, Ser-139, Ser-248, Ser-249, Ser-253, Ser-255, and Thr-256) that were phosphorylated in both in vitro and in vivo samples (Fig. 4B), suggesting that Plk1 phosphorylates these sites. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265230 |
Ser249 |
LDILHNSsQMKSMST |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 25670858 |
Notably, although Plk1 did not alter the level of PBIP1 and CENP-Q ubiquitination, Plk1-dependent phosphorylation and delocalization of these proteins from kinetochores appeared to indirectly lead to their degradation in the cytosol. From these analyses, we identified nine CENP-Q residues (Thr-123, Thr-135, Ser-138, Ser-139, Ser-248, Ser-249, Ser-253, Ser-255, and Thr-256) that were phosphorylated in both in vitro and in vivo samples (Fig. 4B), suggesting that Plk1 phosphorylates these sites. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265232 |
Ser253 |
HNSSQMKsMSTFIEE |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 25670858 |
Notably, although Plk1 did not alter the level of PBIP1 and CENP-Q ubiquitination, Plk1-dependent phosphorylation and delocalization of these proteins from kinetochores appeared to indirectly lead to their degradation in the cytosol. From these analyses, we identified nine CENP-Q residues (Thr-123, Thr-135, Ser-138, Ser-139, Ser-248, Ser-249, Ser-253, Ser-255, and Thr-256) that were phosphorylated in both in vitro and in vivo samples (Fig. 4B), suggesting that Plk1 phosphorylates these sites. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265226 |
Ser255 |
SSQMKSMsTFIEEAY |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 25670858 |
Notably, although Plk1 did not alter the level of PBIP1 and CENP-Q ubiquitination, Plk1-dependent phosphorylation and delocalization of these proteins from kinetochores appeared to indirectly lead to their degradation in the cytosol. From these analyses, we identified nine CENP-Q residues (Thr-123, Thr-135, Ser-138, Ser-139, Ser-248, Ser-249, Ser-253, Ser-255, and Thr-256) that were phosphorylated in both in vitro and in vivo samples (Fig. 4B), suggesting that Plk1 phosphorylates these sites. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265231 |
Thr123 |
RLLQQCEtLKVPPKK |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 25670858 |
Notably, although Plk1 did not alter the level of PBIP1 and CENP-Q ubiquitination, Plk1-dependent phosphorylation and delocalization of these proteins from kinetochores appeared to indirectly lead to their degradation in the cytosol. From these analyses, we identified nine CENP-Q residues (Thr-123, Thr-135, Ser-138, Ser-139, Ser-248, Ser-249, Ser-253, Ser-255, and Thr-256) that were phosphorylated in both in vitro and in vivo samples (Fig. 4B), suggesting that Plk1 phosphorylates these sites. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265234 |
Thr135 |
PKKMEDLtNVSSLLN |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 25670858 |
Notably, although Plk1 did not alter the level of PBIP1 and CENP-Q ubiquitination, Plk1-dependent phosphorylation and delocalization of these proteins from kinetochores appeared to indirectly lead to their degradation in the cytosol. From these analyses, we identified nine CENP-Q residues (Thr-123, Thr-135, Ser-138, Ser-139, Ser-248, Ser-249, Ser-253, Ser-255, and Thr-256) that were phosphorylated in both in vitro and in vivo samples (Fig. 4B), suggesting that Plk1 phosphorylates these sites. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265229 |
Thr256 |
SQMKSMStFIEEAYK |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 25670858 |
Notably, although Plk1 did not alter the level of PBIP1 and CENP-Q ubiquitination, Plk1-dependent phosphorylation and delocalization of these proteins from kinetochores appeared to indirectly lead to their degradation in the cytosol. From these analyses, we identified nine CENP-Q residues (Thr-123, Thr-135, Ser-138, Ser-139, Ser-248, Ser-249, Ser-253, Ser-255, and Thr-256) that were phosphorylated in both in vitro and in vivo samples (Fig. 4B), suggesting that Plk1 phosphorylates these sites. |
|
| Publications: |
9 |
Organism: |
Homo Sapiens |
| + |
PLK1 | down-regulates activity
phosphorylation
|
ESPL1 |
0.784 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276082 |
Ser1399 |
KVNFSDDsDLEDPVS |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 17974570 |
Although mutation of serine 1126 and threonine 1346 to alanine had no effect (lanes 2 and 5), additional mutation of threonine 1363 and serine 1399 rendered separase almost completely resistant to phosphorylation (lane 3). Serine 1399 seems to be the one residue within this large separase fragment that is most efficiently phosphorylated by polo-like kinase, because a corresponding point mutation was sufficient to reduce the labeling by 80% compared with wild type (lane 6). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276083 |
Thr1363 |
AGPHVPFtVFEEVCP |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 17974570 |
Although mutation of serine 1126 and threonine 1346 to alanine had no effect (lanes 2 and 5), additional mutation of threonine 1363 and serine 1399 rendered separase almost completely resistant to phosphorylation (lane 3). Serine 1399 seems to be the one residue within this large separase fragment that is most efficiently phosphorylated by polo-like kinase, because a corresponding point mutation was sufficient to reduce the labeling by 80% compared with wild type (lane 6). |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PLK1 | up-regulates activity
phosphorylation
|
RAD51 |
0.5 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-278187 |
Ser14 |
LEANADTsVEEESFG |
Homo sapiens |
|
| pmid |
sentence |
| 26811421 |
Mechanistically, TOPBP1 physically binds PLK1 and promotes PLK1 kinase-mediated phosphorylation of RAD51 at serine 14, a modification required for RAD51 recruitment to chromatin.|Mechanistically, TOPBP1 physically binds PLK1 and promotes PLK1 kinase\u2013mediated phosphorylation of RAD51 at serine 14, a modification required for RAD51 recruitment to chromatin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PLK1 | down-regulates quantity by destabilization
phosphorylation
|
CDH1 |
0.295 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274054 |
Ser146 |
LLTFPNSsPGLRRQK |
|
|
| pmid |
sentence |
| 23972993 |
Priming phosphorylation of Cdh1 by the Cdk2/cyclin A kinase complex allows Plk1 to bind to Cdh1 and phosphorylate Cdh1 at Ser138 and Ser146. Phosphorylation of Cdh1 at Ser138 and Ser146 then triggers its interaction with, and subsequent ubiquitination by, SCFbeta-TRCP |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274053 |
|
|
|
|
| pmid |
sentence |
| 23972993 |
Priming phosphorylation of Cdh1 by the Cdk2/cyclin A kinase complex allows Plk1 to bind to Cdh1 and phosphorylate Cdh1 at Ser138 and Ser146. Phosphorylation of Cdh1 at Ser138 and Ser146 then triggers its interaction with, and subsequent ubiquitination by, SCFbeta-TRCP |
|
| Publications: |
2 |
| + |
PLK1 | down-regulates activity
phosphorylation
|
STK3 |
0.324 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277904 |
Ser15 |
KSKLKKLsEDSLTKQ |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 37739411 |
We conclude that TRIM69A promotes multi-site phosphorylation of MST2.We demonstrate that TRIM69 stimulates formation of an MST2-PLK1 complex and promotes phosphorylation of MST2 at S15, a known PLK1 site. PLK1-mediated MST2 phosphorylation at S15 is necessary for subsequent phosphorylation of NEK2A to dissociate c-NAP1 from daughter centrioles (7). Thus, we provide a new molecular mechanism by which TRIM69 promotes MST2- and PLK1-mediated centrosome disjunction. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PLK1 | up-regulates
phosphorylation
|
RACGAP1 |
0.623 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-185746 |
Ser157 |
GSILSDIsFDKTDES |
Homo sapiens |
|
| pmid |
sentence |
| 19468302 |
Tandem mass spectrometry analysis of a purified hscyk-4 fragment (hscyk-4n) phosphorylated by plk1 in vitro identified four major sites (s157, s170, s214, and s260 plk1 phosphorylation of hscyk-4 localizes ect2 at the midzone and stimulates rhoa-dependent contractile ring assembly at the equatorial cortex. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-185750 |
Ser170 |
ESLDWDSsLVKTFKL |
Homo sapiens |
|
| pmid |
sentence |
| 19468302 |
Tandem mass spectrometry analysis of a purified hscyk-4 fragment (hscyk-4n) phosphorylated by plk1 in vitro identified four major sites (s157, s170, s214, and s260 plk1 phosphorylation of hscyk-4 localizes ect2 at the midzone and stimulates rhoa-dependent contractile ring assembly at the equatorial cortex. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-185754 |
Ser214 |
AVDQGNEsIVAKTTV |
Homo sapiens |
|
| pmid |
sentence |
| 19468302 |
Tandem mass spectrometry analysis of a purified hscyk-4 fragment (hscyk-4n) phosphorylated by plk1 in vitro identified four major sites (s157, s170, s214, and s260 plk1 phosphorylation of hscyk-4 localizes ect2 at the midzone and stimulates rhoa-dependent contractile ring assembly at the equatorial cortex. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-185758 |
Thr260 |
QPWNSDStLNSRQLE |
Homo sapiens |
|
| pmid |
sentence |
| 19468302 |
Tandem mass spectrometry analysis of a purified hscyk-4 fragment (hscyk-4n) phosphorylated by plk1 in vitro identified four major sites (s157, s170, s214, and s260 plk1 phosphorylation of hscyk-4 localizes ect2 at the midzone and stimulates rhoa-dependent contractile ring assembly at the equatorial cortex. |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| + |
PLK1 | down-regulates activity
phosphorylation
|
TP53BP1 |
0.581 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264413 |
Ser1618 |
LTKAADIsLDNLVEG |
in vitro |
|
| pmid |
sentence |
| 24703952 |
Here we show that 53BP1 is phosphorylated during mitosis on two residues, T1609 and S1618, located in its well-conserved ubiquitination-dependent recruitment (UDR) motif.|Dephosphorylation enables the recruitment of 53BP1 to double-strand DNA breaks |Addition of the inhibitors for PLK1 and the p38 MAPK leads to a complete loss of pT1609/pS1618 signal within 3 hr in mitotic cells |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PLK1 | down-regulates quantity by destabilization
phosphorylation
|
CDC20 |
0.978 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276493 |
Ser170 |
KTCRYIPsLPDRILD |
in vitro |
|
| pmid |
sentence |
| 23643811 |
Plk1 directly bound to Cdc20 and phosphorylates it on serine-170 located in CRY-box. Whereas wild-type Cdc20 was degraded according to progress cell cycle beyond mitosis, the phosphorylation-defective mutant, which serine-170 was changed into alanine, was not destroyed in early G1 phase. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PLK1 | up-regulates quantity
phosphorylation
|
YBX1 |
0.252 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-279254 |
Ser174 |
SGEKNEGsESAPEGQ |
Homo sapiens |
|
| pmid |
sentence |
| 36805592 |
Here we identify that PLK1 inhibition can induce apoptosis and DNA damage of GSCs, we have also delineat the possible underlying molecular mechanisms: PLK1 interacts with YBX1 and directly phosphorylates serine 174 and serine 176 of YBX1.|Inhibition of PLK1 reduces the phosphorylation level of YBX1, and decreased phosphorylation of YBX1 prevents its nuclear translocation, thereby inducing apoptosis and DNA damage of GSCs. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-279255 |
Ser176 |
EKNEGSEsAPEGQAQ |
Homo sapiens |
|
| pmid |
sentence |
| 36805592 |
Here we identify that PLK1 inhibition can induce apoptosis and DNA damage of GSCs, we have also delineat the possible underlying molecular mechanisms: PLK1 interacts with YBX1 and directly phosphorylates serine 174 and serine 176 of YBX1.|Inhibition of PLK1 reduces the phosphorylation level of YBX1, and decreased phosphorylation of YBX1 prevents its nuclear translocation, thereby inducing apoptosis and DNA damage of GSCs. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PLK1 | down-regulates quantity by destabilization
dephosphorylation
|
RAD21 |
0.75 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275535 |
Ser175 |
REIMREGsAFEDDDM |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 15737063 |
We suspected that the observed enhancement of Scc1's cleavability in the presence of Plk1 might be due to phosphorylation at two sites that are directly adjacent to the cleavage sites, Ser175 and Ser454, which we had found to be phosphorylated in mitosis in vivo (Table 1). We therefore mutated these two residues to alanine, thereby creating mutant Scc1-S175A/S454A (see Figure 1C), and tested the cleavability of this mutant in the absence or presence of Plk1 in vitro. |Scc1 phosphorylation is dispensable for cohesin dissociation from chromosomes in early mitosis but enhances the cleavability of Scc1 by separase. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275536 |
Ser454 |
EPSRLQEsVMEASRT |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 15737063 |
We suspected that the observed enhancement of Scc1's cleavability in the presence of Plk1 might be due to phosphorylation at two sites that are directly adjacent to the cleavage sites, Ser175 and Ser454, which we had found to be phosphorylated in mitosis in vivo (Table 1). We therefore mutated these two residues to alanine, thereby creating mutant Scc1-S175A/S454A (see Figure 1C), and tested the cleavability of this mutant in the absence or presence of Plk1 in vitro. |Scc1 phosphorylation is dispensable for cohesin dissociation from chromosomes in early mitosis but enhances the cleavability of Scc1 by separase. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PLK1 | up-regulates
phosphorylation
|
OPTN |
0.561 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-196367 |
Ser177 |
SSGSSEDsFVEIRMA |
Homo sapiens |
|
| pmid |
sentence |
| 22365832 |
Here we show that at mitotic entry, plk1 phosphorylates optineurin (optn) at serine 177 and that this dissociates optn from the golgi-localized gtpase rab8, inducing its translocation into the nucleus. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PLK1 | up-regulates
phosphorylation
|
DCTN1 |
0.512 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-167281 |
Ser179 |
SASAGELsSSEPSTP |
Homo sapiens |
|
| pmid |
sentence |
| 20679239 |
Plk1-mediated phosphorylation of p150(glued) at ser-179 positively regulates its accumulation at the nuclear envelope during prophase. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PLK1 | down-regulates quantity by destabilization
phosphorylation
|
NOTCH1 |
0.394 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277491 |
Ser1791 |
REPLGEDsVGLKPLK |
Homo sapiens |
HaCaT Cell |
| pmid |
sentence |
| 31597699 |
As shown in Fig. S4D, the C-terminal NOTCH1 fragment was readily phosphorylated by PLK1. Additionally, when the two putative phosphorylation sites, Ser-1791 and Ser-2349, were replaced by Ala, WT NOTCH1-IC but not the mutant was efficiently phosphorylated (Fig. S4E). We found that mutation of Ser-1791/2349 promotes NOTCH1-IC stabilization (Fig. S4F). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277490 |
Ser2439 |
SFLSGEPsQADVQPL |
Homo sapiens |
HaCaT Cell |
| pmid |
sentence |
| 31597699 |
As shown in Fig. S4D, the C-terminal NOTCH1 fragment was readily phosphorylated by PLK1. Additionally, when the two putative phosphorylation sites, Ser-1791 and Ser-2349, were replaced by Ala, WT NOTCH1-IC but not the mutant was efficiently phosphorylated (Fig. S4E). We found that mutation of Ser-1791/2349 promotes NOTCH1-IC stabilization (Fig. S4F). |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PLK1 | up-regulates activity
phosphorylation
|
LRRK1 |
0.337 |
| 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 |
| + |
PLK1 | down-regulates activity
phosphorylation
|
BRCA2 |
0.528 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-102486 |
Ser193 |
AEVDPDMsWSSSLAT |
Homo sapiens |
U2-OS Cell |
| pmid |
sentence |
| 12815053 |
M phase-specific phosphorylation of brca2 by polo-like kinase 1 correlates with the dissociation of the brca2-p/caf complex.Plk1 interacts with brca2 in vivo, and mutation of ser193, ser205/206, and thr203/207 to ala in br-n1 abolished plk1 phosphorylation, suggesting that brca2 is the substrate of plk1 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-102490 |
Ser205 |
LATPPTLsSTVLIVR |
Homo sapiens |
U2-OS Cell |
| pmid |
sentence |
| 12815053 |
M phase-specific phosphorylation of brca2 by polo-like kinase 1 correlates with the dissociation of the brca2-p/caf complex.Plk1 interacts with brca2 in vivo, and mutation of ser193, ser205/206, and thr203/207 to ala in br-n1 abolished plk1 phosphorylation, suggesting that brca2 is the substrate of plk1 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-102494 |
Ser206 |
ATPPTLSsTVLIVRN |
Homo sapiens |
|
| pmid |
sentence |
| 12815053 |
M phase-specific phosphorylation of brca2 by polo-like kinase 1 correlates with the dissociation of the brca2-p/caf complex.Plk1 interacts with brca2 in vivo, and mutation of ser193, ser205/206, and thr203/207 to ala in br-n1 abolished plk1 phosphorylation, suggesting that brca2 is the substrate of plk1 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-102498 |
Thr203 |
SSLATPPtLSSTVLI |
Homo sapiens |
|
| pmid |
sentence |
| 12815053 |
M phase-specific phosphorylation of brca2 by polo-like kinase 1 correlates with the dissociation of the brca2-p/caf complex.Plk1 interacts with brca2 in vivo, and mutation of ser193, ser205/206, and thr203/207 to ala in br-n1 abolished plk1 phosphorylation, suggesting that brca2 is the substrate of plk1 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-102502 |
Thr207 |
TPPTLSStVLIVRNE |
Homo sapiens |
U2-OS Cell |
| pmid |
sentence |
| 12815053 |
M phase-specific phosphorylation of brca2 by polo-like kinase 1 correlates with the dissociation of the brca2-p/caf complex.Plk1 interacts with brca2 in vivo, and mutation of ser193, ser205/206, and thr203/207 to ala in br-n1 abolished plk1 phosphorylation, suggesting that brca2 is the substrate of plk1 |
|
| Publications: |
5 |
Organism: |
Homo Sapiens |
| + |
PLK1 |
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Stack trace:
#0 /home/prisca/signor/relation_result.php(2084): implode()
#1 {main}
thrown in /home/prisca/signor/relation_result.php on line 2084
4.0
PLK1
- 
- 