| + |
PBK |
phosphorylation
|
H3C1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-149716 |
Ser11 |
TKQTARKsTGGKAPR |
Homo sapiens |
|
| pmid |
sentence |
| 16982762 |
Pbk/topk could phosphorylate histone h3 at ser10 in vitro and in vivo, and mediated its growth-promoting effect through histone h3 modification. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PBK | up-regulates 
phosphorylation
|
PRDX1 |
0.263 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-166901 |
Ser32 |
QFKDISLsDYKGKYV |
Homo sapiens |
T-lymphocyte, Melanoma Cell, Skin Cancer Cell |
| pmid |
sentence |
| 20647304 |
We report that prx1 is newly discovered direct target of topk. Our results demonstrate that topk phosphorylation of prx1 at ser-32 inhibits uvb-induced apoptosis in rpmi7951 melanoma cells by increasing prx1 peroxidase activity and decreasing the intracellular accumulation of h2o2. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PBK | down-regulates activity 
phosphorylation
|
PTEN |
0.519 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271472 |
Ser380 |
EPDHYRYsDTTDSDP |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 24012691 |
PTEN is phosphorylated by TOPK and is required for mitotic entry. In addition, reduced PTEN phosphorylation levels upon TOPK knockdown correlated with decreased Akt activation (Fig. 4e) suggesting that TOPK mediated phosphorylation may lead to PTEN inactivation. By using various PTEN mutants in a kinase assay we concluded that TOPK phosphorylates PTEN at S380 residue in vitro (Fig. 4c). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PBK | down-regulates activity
phosphorylation
|
ULK1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277474 |
Ser469 |
IRRSGSTsPLGFARA |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 31378785 |
We found that TOPK could directly bind with and phosphorylate ULK1 at Ser469, Ser495, and Ser533. The phosphorylation of ULK1 at Ser469, Ser495, and Ser533 by TOPK decreased the activity and stability of ULK1. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277473 |
Ser495 |
GVLARKMsLGGGRPY |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 31378785 |
We found that TOPK could directly bind with and phosphorylate ULK1 at Ser469, Ser495, and Ser533. The phosphorylation of ULK1 at Ser469, Ser495, and Ser533 by TOPK decreased the activity and stability of ULK1. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277472 |
Ser533 |
AEMRGGRsPRPGSSA |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 31378785 |
We found that TOPK could directly bind with and phosphorylate ULK1 at Ser469, Ser495, and Ser533. The phosphorylation of ULK1 at Ser469, Ser495, and Ser533 by TOPK decreased the activity and stability of ULK1. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
PBK | up-regulates
phosphorylation
|
GPSM2 |
0.273 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-166461 |
Thr457 |
LKGKKYKtNSSTKVL |
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 20589935 |
We found that the 450th threonine (thr450) of lgn/gpsm2 was phosphorylated by the serine/threonine kinase pbk/topk during mitosis. Western blot analysis indicated the highest expression and the phosphorylated form of lgn/gpsm2 protein in g2/m phase. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CyclinB/CDK1 | up-regulates activity
phosphorylation
|
PBK |
0.568 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250720 |
Thr9 |
EGISNFKtPSKLSEK |
|
|
| pmid |
sentence |
| 15541388 |
During mitosis, TOPK-Thr-9 was phosphorylated by cdk1/cyclin B and TOPK significantly associates with mitotic spindles. When TOPK expression was suppressed, formation of spindle midzone was thinned and dimmed and cytokinesis was disturbed. |
|
| Publications: |
1 |
| + |
CDK1 |
phosphorylation
|
PBK |
0.568 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-130439 |
Thr9 |
EGISNFKtPSKLSEK |
Homo sapiens |
|
| pmid |
sentence |
| 15541388 |
Topk-thr-9 was phosphorylated by cdk1/cyclin b and topk significantly associates with mitotic spindles. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CyclinB/CDK1 |
phosphorylation
|
PBK |
0.568 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-216896 |
Thr9 |
EGISNFKtPSKLSEK |
Homo sapiens |
|
| pmid |
sentence |
| 15541388 |
Topk-thr-9 was phosphorylated by cdk1/cyclin b and topk significantly associates with mitotic spindles. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SRC | up-regulates quantity by stabilization
phosphorylation
|
PBK |
0.404 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277217 |
Tyr272 |
DFDDEAYyAALGTRP |
Homo sapiens |
SW-480 Cell |
| pmid |
sentence |
| 27016416 |
Phosphorylation of TOPK at Y74, Y272 by Src increases the stability of TOPK and promotes tumorigenesis of colon |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277218 |
Tyr74 |
NPICNDHyRSVYQKR |
Homo sapiens |
SW-480 Cell |
| pmid |
sentence |
| 27016416 |
Phosphorylation of TOPK at Y74, Y272 by Src increases the stability of TOPK and promotes tumorigenesis of colon |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
CHFR | down-regulates quantity by destabilization
polyubiquitination
|
PBK |
0.352 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271471 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 24012691 |
CHFR ubiquitinates and degrades TOPK. Our in vivo ubiquitination assays revealed that the polyubiquitination of TOPK occurs only in the presence of full length CHFR but not with the ΔRING or Δcysteine-rich domain deletion mutants (Fig. 2a). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
LNX1 | down-regulates quantity by destabilization
ubiquitination
|
PBK |
0.383 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272898 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 22889411 |
We used the Ligand of Numb protein X (LNX) family of E3s, a group of PDZ domain-containing RING-type E3 ubiquitin ligases, to demonstrate the feasibility of this strategy. Many potential substrates of LNX E3s were identified. Eight of the nine selected candidates were ubiquitinated in vitro, and two novel endogenous substrates, PDZ-binding kinase (PBK) and breakpoint cluster region protein (BCR), were confirmed in vivo. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PBK |
phosphorylation
|
Histone H3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265364 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16982762 |
Pbk/topk could phosphorylate histone h3 at ser10 in vitro and in vivo, and mediated its growth-promoting effect through histone h3 modification. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
PBK
- 
- 