| + |
PIM2 | down-regulates 
phosphorylation
|
BAD |
0.4 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-78015 |
Ser118 |
GRELRRMsDEFVDSF |
Homo sapiens |
|
| pmid |
sentence |
| 10837473 |
Similar to pim1, pim2 phosphorylates bad, which antagonizes the pro-apoptotic function of bax |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PIM2 | down-regulates activity
phosphorylation
|
BAD |
0.4 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250395 |
Ser118 |
GRELRRMsDEFVDSF |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 16403219 |
Pim kinases phosphorylate multiple sites on Bad and promote 14-3-3 binding and dissociation from Bcl-XL. pim kinases are constitutively active when expressed in HEK-293 cells and are able to phosphorylate the Bcl-2 family member Bad on three residues, Ser112, Ser136 and Ser155 in vitro and in cells. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249604 |
Ser75 |
EIRSRHSsYPAGTED |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 16403219 |
All three Pim kinase family members predominantly phosphorylate Bad on Ser112 and in addition are capable of phosphorylating Bad on multiple sites associated with the inhibition of the pro-apoptotic function of Bad in HEK-293 cells. This would be consistent with the proposed function of Pim kinases in promoting cell proliferation and preventing cell death. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250394 |
Ser99 |
PFRGRSRsAPPNLWA |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 16403219 |
Pim kinases phosphorylate multiple sites on Bad and promote 14-3-3 binding and dissociation from Bcl-XL. pim kinases are constitutively active when expressed in HEK-293 cells and are able to phosphorylate the Bcl-2 family member Bad on three residues, Ser112, Ser136 and Ser155 in vitro and in cells. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
PIM2 | up-regulates activity 
phosphorylation
|
PSMD2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273896 |
Ser361 |
ENNRFGGsGSQVDSA |
in vitro |
|
| pmid |
sentence |
| 31843888 |
Seven of these kinases (PIM1/2/3, MAP4K1/2, PKA, and NEK6) directly and robustly phosphorylated recombinant GST-Rpn1 at S361 in vitro (Fig. 3D and SI Appendix, Fig. S3 A and B). |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PIM2 | down-regulates activity
phosphorylation
|
PRKAA1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277471 |
Ser467 |
LQLYQVDsRTYLLDF |
Homo sapiens |
Endometrial Cancer Cell Line |
| pmid |
sentence |
| 31358902 |
Specifically, we found that PIM2 bound to AMPKα1, and directly phosphorylated it on Thr467. Phosphorylation of AMPKα1 by PIM2 led to decreasing AMPKα1 kinase activity, which in turn promoted aerobic glycolysis and tumor growth. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PIM2 | up-regulates quantity by stabilization
phosphorylation
|
PFKFB3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277554 |
Ser478 |
TKKPRINsFEEHVAS |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 33931981 |
We used biochemical methods to determine that PIM2 can directly bind and change the phosphorylation of PFKFB3 at Ser478 to enhance PFKFB3 protein stability through the ubiquitin-proteasome pathway. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PIM2 | up-regulates quantity by stabilization
phosphorylation
|
CDKN1A |
0.413 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-164646 |
Thr145 |
QGRKRRQtSMTDFYH |
Homo sapiens |
|
| pmid |
sentence |
| 20307683 |
Pim-2 phosphorylation of p21(cip1/waf1) enhances its stability and inhibits cell proliferation in hct116 cellsere we demonstrate that like pim-1, pim-2 also phosphorylates the cell cycle inhibitor p21(cip1/waf1) (p21) on thr145 in vitro and in vivo |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PIM2 | up-regulates quantity by stabilization
phosphorylation
|
PKM |
0.379 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260905 |
Thr454 |
RAPIIAVtRNPQTAR |
Homo sapiens |
|
| pmid |
sentence |
| 24142698 |
Importantly, we found that PIM2 could directly phosphorylate PKM2 on the Thr-454 residue, resulting in an increase of PKM2 protein levels. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267472 |
Thr454 |
RAPIIAVtRNPQTAR |
Homo sapiens |
|
| pmid |
sentence |
| 24142698 |
Here, we identified the protein-serine/threonine kinase PIM2, a known oncogene, as a novel binding partner of PKM2. The interaction between PIM2 and PKM2 was confirmed by multiple biochemical approaches in vitro and in cultured cells. Importantly, we found that PIM2 could directly phosphorylate PKM2 on the Thr-454 residue, resulting in an increase of PKM2 protein levels. Compared with wild type, PKM2 with the phosphorylation-defective mutation displayed a reduced effect on glycolysis |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
FLT3 | up-regulates quantity by expression 
transcriptional regulation
|
PIM2 |
0.344 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261541 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 15769897 |
The serine-threonine kinase Pim-2 is a functionally relevant downstream target of STAT5.24 Here, we observed only a weak induction of Pim-2 by Flt3-D835Y compared to the effects of Flt3-ITD. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
STAT5A | up-regulates quantity by expression
transcriptional regulation
|
PIM2 |
0.422 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261543 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 15769897 |
The serine-threonine kinase Pim-2 is a functionally relevant downstream target of STAT5. Here, we observed only a weak induction of Pim-2 by Flt3-D835Y compared to the effects of Flt3-ITD. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249622 |
|
|
|
|
| pmid |
sentence |
| 16146838 |
The results of 2 microarray experiments demonstrated that the aberrant activation of STAT proteins by Flt3-ITDs resulted in the up-regulation of several STAT5-responsive genes, such as Pim-1, Pim-2, and members of the SOCS (suppressor of cytokine signaling) protein family. These results are particularly interesting because recent data point to an important role of Pim kinases in the antiapoptosis of hematopoietic cells. |
|
| Publications: |
2 |
Organism: |
Mus Musculus, |
| + |
PIM2 | up-regulates quantity by stabilization
phosphorylation
|
PK |
0.379 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270287 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 24142698 |
Importantly, we found that PIM2 could directly phosphorylate PKM2 on the Thr-454 residue, resulting in an increase of PKM2 protein levels. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268151 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 24142698 |
Importantly, we found that PIM2 could directly phosphorylate PKM2 on the Thr-454 residue, resulting in an increase of PKM2 protein levels. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
SOX2/POU5F1 | up-regulates quantity by expression
transcriptional regulation
|
PIM2 |
0.27 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269241 |
|
|
|
|
| pmid |
sentence |
| 31583686 |
Both SOX2 and SOX17 are able to partner with OCT4 and, as a consequence, recognize and bind specific binding motifs.6, 7 In human and mouse ESCs, SOX2/OCT4 bind to canonical motifs (CTTTGTCATGCAAAT-like), which are composite SOX (CATTGTC-like) and OCT (ATGCAAAT-like) motifs|This way SOX17 and SOX2 regulate a common set of pluripotency and GC-related genes (PRDM14, DPPA4, TDGF1, NANOG, LIN28A, TRIM71, OTX2, PIM2) (Fig. 6). Additionally, in TCam-2 cells SOX17 binds to compressed motifs or SOX motifs (not bound by SOX2 in ECs), thereby regulating the PGC specifiers PRDM1 and TFAP2C, the GC-related genes NANOS3 and BMP7 and the cancer-related genes MYC and IGF1 (Fig. 6). In 2102EP cells, SOX2 further binds canonical elements or SOX motifs (not bound by SOX17 in TCam-2), regulating additional pluripotency genes (GDF3, LEFTY2, SALL4, SOX2 and POU5F1) (Fig. 6). |
|
| Publications: |
1 |
| + |
SGI-1776 | down-regulates
chemical inhibition
|
PIM2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-206862 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PIM2 | up-regulates activity
phosphorylation
|
NFATC1 |
0.265 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276772 |
|
|
in vitro |
|
| pmid |
sentence |
| 31730483 |
In addition to PIM1, also PIM2 and PIM3 were able to phosphorylate WT, but not MM NFATC1 in vitro (Fig. (Fig.22c). |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PIM2 | down-regulates activity
phosphorylation
|
PK |
0.379 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268148 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 24142698 |
Here, we identified the protein-serine/threonine kinase PIM2, a known oncogene, as a novel binding partner of PKM2. The interaction between PIM2 and PKM2 was confirmed by multiple biochemical approaches in vitro and in cultured cells. Importantly, we found that PIM2 could directly phosphorylate PKM2 on the Thr-454 residue, resulting in an increase of PKM2 protein levels. Compared with wild type, PKM2 with the phosphorylation-defective mutation displayed a reduced effect on glycolysis |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FOXN3 | down-regulates quantity by repression
transcriptional regulation
|
PIM2 |
0.301 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261607 |
|
|
Homo sapiens |
NCI-H1299 Cell |
| pmid |
sentence |
| 24403608 |
CHES1/FOXN3 regulates cell proliferation by repressing PIM2 and protein biosynthesis. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PIM2 | down-regulates 
|
Apoptosis |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256575 |
|
|
|
|
| pmid |
sentence |
| 16146838 |
The results of 2 microarray experiments demonstrated that the aberrant activation of STAT proteins by Flt3-ITDs resulted in the up-regulation of several STAT5-responsive genes, such as Pim-1, Pim-2, and members of the SOCS (suppressor of cytokine signaling) protein family. These results are particularly interesting because recent data point to an important role of Pim kinases in the antiapoptosis of hematopoietic cells. |
|
| Publications: |
1 |
| + |
SOX17/POU5F1 | up-regulates quantity by expression
transcriptional regulation
|
PIM2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269249 |
|
|
|
|
| pmid |
sentence |
| 31583686 |
Both SOX2 and SOX17 are able to partner with OCT4 and, as a consequence, recognize and bind specific binding motifs.6, 7 In human and mouse ESCs, SOX2/OCT4 bind to canonical motifs (CTTTGTCATGCAAAT-like), which are composite SOX (CATTGTC-like) and OCT (ATGCAAAT-like) motifs|This way SOX17 and SOX2 regulate a common set of pluripotency and GC-related genes (PRDM14, DPPA4, TDGF1, NANOG, LIN28A, TRIM71, OTX2, PIM2) (Fig. 6). Additionally, in TCam-2 cells SOX17 binds to compressed motifs or SOX motifs (not bound by SOX2 in ECs), thereby regulating the PGC specifiers PRDM1 and TFAP2C, the GC-related genes NANOS3 and BMP7 and the cancer-related genes MYC and IGF1 (Fig. 6). In 2102EP cells, SOX2 further binds canonical elements or SOX motifs (not bound by SOX17 in TCam-2), regulating additional pluripotency genes (GDF3, LEFTY2, SALL4, SOX2 and POU5F1) (Fig. 6). |
|
| Publications: |
1 |
3.0
PIM2
- 
- 