Relation Results

Identifier	Residue	Sequence	Organism
SIGNOR-156946	Ser11	TKQTARKsTGGKAPR	Homo sapiens
pmid	sentence
17643117	Pim1-dependent phosphorylation of histone h3 at serine 10 is required for myc-dependent transcriptional activation and oncogenic transformation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-250390	Ser118	GRELRRMsDEFVDSF	Homo sapiens
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
SIGNOR-249607	Ser75	EIRSRHSsYPAGTED	Homo sapiens
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-250392	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

Pathways:

Acute Myeloid Leukemia, FLT3-ITD in AML, FLT3-ITD signaling

Identifier	Residue	Sequence	Organism
SIGNOR-262961	Ser146	GRKRRQTsMTDFYHS	Homo sapiens
pmid	sentence
31575057	Pim-1, PKC, and Akt1 kinases phosphorylate Thr-145 and Ser-146 sites on p21 protein. Phosphorylation at Thr-145 promotes cytoplasmic translocation and stability of p21. Ser-146 phosphorylation mediated by Akt1 enhances p21 stabilization and promotes cell survival.

Identifier	Residue	Sequence	Organism
SIGNOR-164642	Thr145	QGRKRRQtSMTDFYH	Homo sapiens
pmid	sentence
20307683	Pim-2 phosphorylation of p21(cip1/waf1) enhances its stability and inhibits cell proliferation in hct116 cellshere 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:

2

Organism:

Homo Sapiens

Pathways:

Acute Myeloid Leukemia, FLT3-ITD in AML, FLT3-ITD signaling

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276779	Ser151	VLPSSKRsPSTATLS	Homo sapiens	PC-3 Cell
pmid	sentence
31730483	Phosphorylation of NFATC1 at PIM1 target sites is essential for its ability to promote prostate cancer cell migration and invasion. Here we have identified ten PIM1 target sites in NFATC1 and found that prevention of their phosphorylation significantly decreases the transcriptional activity as well as the pro-migratory and pro-invasive effects of NFATC1 in prostate cancer cells.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276774	Ser153	PSSKRSPsTATLSLP	Homo sapiens	PC-3 Cell
pmid	sentence
31730483	Phosphorylation of NFATC1 at PIM1 target sites is essential for its ability to promote prostate cancer cell migration and invasion. Here we have identified ten PIM1 target sites in NFATC1 and found that prevention of their phosphorylation significantly decreases the transcriptional activity as well as the pro-migratory and pro-invasive effects of NFATC1 in prostate cancer cells.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276770	Ser245	PSTSPRAsVTEESWL	Homo sapiens	PC-3 Cell
pmid	sentence
31730483	Phosphorylation of NFATC1 at PIM1 target sites is essential for its ability to promote prostate cancer cell migration and invasion. Here we have identified ten PIM1 target sites in NFATC1 and found that prevention of their phosphorylation significantly decreases the transcriptional activity as well as the pro-migratory and pro-invasive effects of NFATC1 in prostate cancer cells.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276768	Ser256	ESWLGARsSRPASPC	Homo sapiens	PC-3 Cell
pmid	sentence
31730483	Phosphorylation of NFATC1 at PIM1 target sites is essential for its ability to promote prostate cancer cell migration and invasion. Here we have identified ten PIM1 target sites in NFATC1 and found that prevention of their phosphorylation significantly decreases the transcriptional activity as well as the pro-migratory and pro-invasive effects of NFATC1 in prostate cancer cells.

Identifier	Residue	Sequence	Organism
SIGNOR-276767	Ser257	SWLGARSsRPASPCN	in vitro
pmid	sentence
31730483	Phosphorylation of NFATC1 at PIM1 target sites is essential for its ability to promote prostate cancer cell migration and invasion. Here we have identified ten PIM1 target sites in NFATC1 and found that prevention of their phosphorylation significantly decreases the transcriptional activity as well as the pro-migratory and pro-invasive effects of NFATC1 in prostate cancer cells.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276769	Ser269	PCNKRKYsLNGRQPP	Homo sapiens	PC-3 Cell
pmid	sentence
31730483	Phosphorylation of NFATC1 at PIM1 target sites is essential for its ability to promote prostate cancer cell migration and invasion. Here we have identified ten PIM1 target sites in NFATC1 and found that prevention of their phosphorylation significantly decreases the transcriptional activity as well as the pro-migratory and pro-invasive effects of NFATC1 in prostate cancer cells.

Identifier	Residue	Sequence	Organism
SIGNOR-276776	Ser335	GDGVPVKsRKTTLEQ	in vitro
pmid	sentence
31730483	Phosphorylation of NFATC1 at PIM1 target sites is essential for its ability to promote prostate cancer cell migration and invasion. Here we have identified ten PIM1 target sites in NFATC1 and found that prevention of their phosphorylation significantly decreases the transcriptional activity as well as the pro-migratory and pro-invasive effects of NFATC1 in prostate cancer cells.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276777	Thr154	SSKRSPStATLSLPS	Homo sapiens	PC-3 Cell
pmid	sentence
31730483	Phosphorylation of NFATC1 at PIM1 target sites is essential for its ability to promote prostate cancer cell migration and invasion. Here we have identified ten PIM1 target sites in NFATC1 and found that prevention of their phosphorylation significantly decreases the transcriptional activity as well as the pro-migratory and pro-invasive effects of NFATC1 in prostate cancer cells.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276775	Thr338	VPVKSRKtTLEQPPS	Homo sapiens	PC-3 Cell
pmid	sentence
31730483	Phosphorylation of NFATC1 at PIM1 target sites is essential for its ability to promote prostate cancer cell migration and invasion. Here we have identified ten PIM1 target sites in NFATC1 and found that prevention of their phosphorylation significantly decreases the transcriptional activity as well as the pro-migratory and pro-invasive effects of NFATC1 in prostate cancer cells.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276771	Thr339	PVKSRKTtLEQPPSV	Homo sapiens	PC-3 Cell
pmid	sentence
31730483	Phosphorylation of NFATC1 at PIM1 target sites is essential for its ability to promote prostate cancer cell migration and invasion. Here we have identified ten PIM1 target sites in NFATC1 and found that prevention of their phosphorylation significantly decreases the transcriptional activity as well as the pro-migratory and pro-invasive effects of NFATC1 in prostate cancer cells.

Publications:

10

Organism:

Homo Sapiens, In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-178615	Ser166	SSRRRAIsETEENSD	Homo sapiens
pmid	sentence
18467333	Additionally, the pim kinases phosphorylate mdm2 in vitro and in cultured cells at ser166 and ser186, two previously identified targets of other signaling pathways, including akt.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Acute Myeloid Leukemia, FLT3-ITD signaling

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-178619	Ser186	RQRKRHKsDSISLSF	Homo sapiens	Lymphoma Cell
pmid	sentence
18467333	Additionally, the pim kinases phosphorylate mdm2 in vitro and in cultured cells at ser166 and ser186, two previously identified targets of other signaling pathways, including akt.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Acute Myeloid Leukemia, FLT3-ITD signaling

Identifier	Residue	Sequence	Organism
SIGNOR-263029	Ser212	KKRKHKSsKSNEGSD	in vitro
pmid	sentence
10931201	PAP-1 was phosphorylated in vitro by Pim-1, but not a kinase-negative Pim-1 mutant. The two serine residues of PAP-1 at amino acids 204 and 206 near the C-terminus were phosphorylated by Pim-1. PAP-1 is thus thought to be a target protein for Pim-1 kinase.

Identifier	Residue	Sequence	Organism
SIGNOR-263030	Ser214	RKHKSSKsNEGSDSE	in vitro
pmid	sentence
10931201	PAP-1 was phosphorylated in vitro by Pim-1, but not a kinase-negative Pim-1 mutant. The two serine residues of PAP-1 at amino acids 204 and 206 near the C-terminus were phosphorylated by Pim-1. PAP-1 is thus thought to be a target protein for Pim-1 kinase.

Publications:

2

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-252966	Ser253	APRRRAVsMDNSNKY	Homo sapiens
pmid	sentence
18593906	Pim-mediated phosphorylation and inactivation of forkhead transcription factors, foxo1a and foxo3a, was involved in the transcriptional repression of the p27(kip1) gene.

Identifier	Residue	Sequence	Organism
SIGNOR-252967	Thr32	QSRPRSCtWPLQRPE	Homo sapiens
pmid	sentence
18593906	Pim1s expression induced the phosphorylation of foxo3a (fig. 5a and b) and inactivated its transcriptional activity (fig. 5c). A previous report showed that phosphorylation at t32, s253, and s315 residues in foxo3a induced 14-3-3 binding, nuclear export, and proteasomemediated degradation (42).

Publications:

2

Organism:

Homo Sapiens

Pathways:

Acute Myeloid Leukemia, FLT3 in AML, FLT3-ITD in AML, FLT3-ITD signaling

Identifier	Residue	Sequence	Organism
SIGNOR-179304	Ser253	APRRRAVsMDNSNKY	Homo sapiens
pmid	sentence
18593906	Pim-mediated phosphorylation and inactivation of forkhead transcription factors, foxo1a and foxo3a, was involved in the transcriptional repression of the p27(kip1) gene.

Publications:

1

Organism:

Homo Sapiens

Pathways:

FLT3 in AML

Identifier	Residue	Sequence	Organism
SIGNOR-189125	Ser276	SMQLRRPsDRELSEP	Homo sapiens
pmid	sentence
19911008	In this study we show that phosphorylation of rela/p65 at ser276 prevents its degradation by ubiquitin-mediated proteolysis. importantly, we identify pim-1 as a further kinase responsible for the phosphorylation of rela/p65 at ser276.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Acute Myeloid Leukemia, FLT3-ITD in AML

Identifier	Residue	Sequence	Organism
SIGNOR-277349	Ser311	S-->R	Homo sapiens
pmid	sentence
28394343	Here we report that UHRF1 is a novel substrate of PIM1 kinase, which could be phosphorylated at Ser311 and therefore promoted to degradation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-273895	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

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277346	Ser372	SAVYVLSsMARQRRA	Homo sapiens	HEK-293T Cell
pmid	sentence
28348080	Pim-1 binds to and phosphorylates the transcription factor high mobility group box transcription factor 1 (HBP1), activating it.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277347	Ser380	MARQRRAsLSCGGPG	Homo sapiens	HEK-293T Cell
pmid	sentence
28348080	Pim-1 binds to and phosphorylates the transcription factor high mobility group box transcription factor 1 (HBP1), activating it.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277310	Ser435	GKAILPPsQPWATEL	Homo sapiens	HEK-293T Cell
pmid	sentence
34211090	PIM1 kinase directly phosphorylates HIF-1α at threonine 455, a previously uncharacterized site within its oxygen-dependent degradation domain. This phosphorylation event disrupts the ability of prolyl hydroxylases to bind and hydroxylate HIF-1α, interrupting its canonical degradation pathway and promoting constitutive transcription of HIF-1 target genes. Moreover, phosphorylation of the analogous site in HIF-2α (S435) stabilizes the protein through the same mechanism, indicating post-translational modification within the oxygen-dependent degradation domain as a mechanism of regulating the HIF-α subunits.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277574	Ser64	SSWRVVSsIEQKTEG	Homo sapiens	LNCaP Cell
pmid	sentence
34697370	PIM1 phosphorylates the AR and 14-3-3 ζ and coordinates their interaction. PIM1 phosphorylation of the AR and 14-3-3 ζ enhances their interaction and shifts their occupancy on chromatin, resulting in 14-3-3 ζ co-regulation of AR, likely by recruiting other AR co-regulators such as hnRNPK and TRIM28.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-259818	Ser64	SNLGHPEsPPRKRLK	Homo sapiens	HeLa Cell
pmid	sentence
20663873	We found that expression of Pim-1 increases the level of Skp2 through direct binding and phosphorylation of multiple sites on this protein. Along with known Skp2 phosphorylation sites including Ser(64) and Ser(72), we have identified Thr(417) as a unique Pim-1 phosphorylation target. Phosphorylation of Thr(417) controls the stability of Skp2 and its ability to degrade p27.

Identifier	Residue	Sequence	Organism
SIGNOR-259819	Ser72	PPRKRLKsKGSDKDF	Homo sapiens
pmid	sentence
20663873	We found that expression of Pim-1 increases the level of Skp2 through direct binding and phosphorylation of multiple sites on this protein. Along with known Skp2 phosphorylation sites including Ser(64) and Ser(72), we have identified Thr(417) as a unique Pim-1 phosphorylation target. Phosphorylation of Thr(417) controls the stability of Skp2 and its ability to degrade p27.

Identifier	Residue	Sequence	Organism
SIGNOR-259817	Thr417	WGIKCRLtLQKPSCL	Homo sapiens
pmid	sentence
20663873	We found that expression of Pim-1 increases the level of Skp2 through direct binding and phosphorylation of multiple sites on this protein. Along with known Skp2 phosphorylation sites including Ser(64) and Ser(72), we have identified Thr(417) as a unique Pim-1 phosphorylation target. Phosphorylation of Thr(417) controls the stability of Skp2 and its ability to degrade p27.

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-256153	Ser65	HSHSPRHsLRHSPGS	Homo sapiens
pmid	sentence
30017192	In this study, we found that PKCα stabilized and activated PIM-1L by phosphorylation at Ser65. The PIM-1L phosphorylation suppressed sotrastaurin-induced apoptosis. These findings suggest that PKCα promotes cell survival and proliferation by upregulating PIM-1L in acute myeloid leukemia.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-272511	Ser683	QAQDRKLsTKEALDE	Homo sapiens	HEK-293 Cell
pmid	sentence
24333728	Protein phosphatase complex PP5/PPP2R3C dephosphorylates P-glycoprotein/ABCB1 and down-regulates the expression and function\|P-gp is known to be phosphorylated at Ser667, Ser671, and Ser683 by PKA; at Ser661, Ser667, and Ser671 by PKC; and at Ser683 by Pim-1\|simultaneous expression of PP5 and PPP2R3C reduced the phosphorylation detected by the antibodies that specifically recognize serine/threonine phosphorylated by PKA or serine phosphorylated by PKC. These results suggest that the PP5/PPP2R3C complex dephosphorylates PKA- and PKC-phosphorylated serine residues on P-gp

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-187905	Ser83	ATRGRGSsVGGGSRR	Homo sapiens	NCI-H1299 Cell
pmid	sentence
19749799	Pim1 phosphorylates and negatively regulates ask1-mediated apoptosispim1 phosphorylation of ask1 on ser83 inhibited ask1-mediated c-jun n-terminal kinase phosphorylation

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-128260	Ser96	KTQLNPTsLQKLFRE	Homo sapiens
pmid	sentence
15319445	Here we show that the protein kinase cdc25 c-associated kinase 1 (c-tak1) is a binding partner and a substrate of pim-1.

Identifier	Residue	Sequence	Organism
SIGNOR-128264	Thr90	AIKIIDKtQLNPTSL	Homo sapiens
pmid	sentence
15319445	Here we show that the protein kinase cdc25 c-associated kinase 1 (c-tak1) is a binding partner and a substrate of pim-1.

Identifier	Residue	Sequence	Organism
SIGNOR-128268	Thr95	DKTQLNPtSLQKLFR	Homo sapiens
pmid	sentence
15319445	Here we show that the protein kinase cdc25 c-associated kinase 1 (c-tak1) is a binding partner and a substrate of pim-1.

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-179296	Thr157	GIRKRPAtDDSSTQN	Homo sapiens
pmid	sentence
18593906	We show, herein, that all the pim family members (pim1, pim2, and pim3) bind to and directly phosphorylate the cyclin-dependent kinase inhibitor p27(kip1) at threonine-157 and threonine-198 residues in cells and in vitro.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Acute Myeloid Leukemia

Identifier	Residue	Sequence	Organism
SIGNOR-179300	Thr198	PGLRRRQt	Homo sapiens
pmid	sentence
18593906	We show, herein, that all the pim family members (pim1, pim2, and pim3) bind to and directly phosphorylate the cyclin-dependent kinase inhibitor p27(kip1) at threonine-157 and threonine-198 residues in cells and in vitro.\|Pim kinases promote cell cycle progression and tumorigenesis by down-regulating p27(Kip1) expression at both transcriptional and posttranslational levels.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Acute Myeloid Leukemia

Identifier	Residue	Sequence	Organism
SIGNOR-179308	Thr32	QSRPRSCtWPLQRPE	Homo sapiens
pmid	sentence
18593906	Pim1s expression induced the phosphorylation of foxo3a (fig. 5a and b) and inactivated its transcriptional activity (fig. 5c). A previous report showed that phosphorylation at t32, s253, and s315 residues in foxo3a induced 14-3-3 binding, nuclear export, and proteasomemediated degradation (42).

Publications:

1

Organism:

Homo Sapiens

Pathways:

FLT3 in AML

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-264420	Thr362	GEKKKKItVFKEISY	Homo sapiens	Prostate Gland Cancer Cell
pmid	sentence
18056989	Pim-1 kinase phosphorylates BCRP/ABCG2 and thereby promotes its multimerization and drug-resistant activity in human prostate cancer cells\|This is further corroborated by our finding that the plasma membrane localization and drug-resistant activity of BCRP were compromised by T362A mutation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277311	Thr455	LAMSPLPtAETPKPL	Homo sapiens	HEK-293T Cell
pmid	sentence
34211090	PIM1 kinase directly phosphorylates HIF-1α at threonine 455, a previously uncharacterized site within its oxygen-dependent degradation domain. This phosphorylation event disrupts the ability of prolyl hydroxylases to bind and hydroxylate HIF-1α, interrupting its canonical degradation pathway and promoting constitutive transcription of HIF-1 target genes.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-259927	Tyr591	SSDNEYFyVDFREYE	Homo sapiens	MOLM-14 Cell
pmid	sentence
24040307	Pim-1 Kinase Phosphorylates and Stabilizes 130 kDa FLT3 and Promotes Aberrant STAT5 Signaling in Acute Myeloid Leukemia with FLT3 Internal Tandem Duplication[...]Pim-1 inhibition also decreased phosphorylation of FLT3 at tyrosine 591 and of STAT5, and expression of Pim-1 itself, consistent with inhibition of the FLT3-ITD-STAT5 signaling pathway.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Acute Myeloid Leukemia, FLT3 in AML, FLT3-ITD in AML, FLT3-ITD signaling

Identifier	Residue	Organism
SIGNOR-261517		Mus musculus
pmid	sentence
15498859	Pim-1 is a proto-oncogene and is known to be up-regulated by signal transducer and activator of transcription 5 (STAT5), which itself is a downstream target of FLT3 signaling. constitutively activated FLT3 signaling up-regulates Pim-1 expression in leukemia cells.

Identifier	Residue	Organism
SIGNOR-249606		Homo sapiens
pmid	sentence
15498859	Pim-1 is know to be up regulated by signal transducer and activator of transcription 5 (stat5)

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249621
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:

3

Organism:

Mus Musculus, Homo Sapiens,

Pathways:

Acute Myeloid Leukemia, FLT3 in AML, FLT3-ITD in AML, FLT3-ITD signaling

Identifier	Residue	Organism	Cell Line
SIGNOR-141411		Homo sapiens	HEK-293 Cell
pmid	sentence
16266891	The pim-1/rps19 interaction was demonstrated both in vitro and in living cells and led to phosphorylation of rps19 in an in vitro kinase assay.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-256657
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

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249623
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

Pathways:

Acute Myeloid Leukemia, FLT3 in AML, FLT3-ITD in AML, FLT3-ITD signaling

Identifier	Residue	Organism
SIGNOR-265366		Homo sapiens
pmid	sentence
17643117	Pim1-dependent phosphorylation of histone h3 at serine 10 is required for myc-dependent transcriptional activation and oncogenic transformation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-254065		Homo sapiens
pmid	sentence
22140532	ERG deregulation induces PIM1 over-expression and aneuploidy in prostate epithelial cells. The up-regulation of PIM1 induced by tERG over-expression significantly modified Cyclin B1 levels and increased the percentage of aneuploid cells in the RWPE-1 cell line after taxane-based treatment. Here we provide the first evidence for an ERG-mediated PIM1 up-regulation in prostate cells in vitro and in vivo, suggesting a direct effect of ERG transcriptional activity in the alteration of genetic stability.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-277575		Homo sapiens	LNCaP Cell
pmid	sentence
34697370	PIM1 phosphorylates the AR and 14-3-3 ζ and coordinates their interaction. PIM1 phosphorylation of the AR and 14-3-3 ζ enhances their interaction and shifts their occupancy on chromatin, resulting in 14-3-3 ζ co-regulation of AR, likely by recruiting other AR co-regulators such as hnRNPK and TRIM28.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-259820		Homo sapiens	HeLa Cell
pmid	sentence
20663873	Pim-1 phosphorylates Cdh1 and impairs binding of this protein to another APC/C complex member, CDC27. These modifications inhibit Skp2 from degradation.Pim-1 Impairs Cdh1 and CDC27 Interaction and Phosphorylates Cdh1.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-206859		Homo sapiens
pmid	sentence
Other

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-261557		Homo sapiens
pmid	sentence
25280219	FLT3-ITD kinase may regulate c-MYC through STAT5-induced enhancement of PIM kinases (Choudhary et al., 2009), which can modulate c-MYC stability and activity via phosphorylation (van der Lugt et al., 1995s). This is supported by the observation that FLT3-ITD CD34+ cells showed higher PIM activity compared to cells expressing FLT3-WT, indicated by increased expression of the PIM targets including p-BAD (Ser112), p-4EBP1 (Thr37/46), and p-c-MYC (Ser62) (Figure 6C); and by the observation that siRNA-mediated inhibition of PIM1, but not PIM2, expression resulted in significantly decreased p-c-MYC (Ser62), c-MYC, and SIRT1 expression in MV4-11 cells

Publications:

1

Organism:

Homo Sapiens

Pathways:

Acute Myeloid Leukemia, FLT3 in AML, FLT3-ITD in AML, FLT3-ITD signaling

Identifier	Residue	Organism	Cell Line
SIGNOR-261632		Homo sapiens	U-937 Cell
pmid	sentence
17327400	Thus Pim1 appears to be a direct transcriptional target of HOXA9 and a mediator of its antiapoptotic and proproliferative effects in early cells.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Acute Myeloid Leukemia

Identifier	Residue	Organism
SIGNOR-261519		Mus musculus
pmid	sentence
15498859	Pim-1 is a proto-oncogene and is known to be up-regulated by signal transducer and activator of transcription 5 (STAT5), which itself is a downstream target of FLT3 signaling. constitutively activated FLT3 signaling up-regulates Pim-1 expression in leukemia cells.

Publications:

1

Organism:

Mus Musculus

Pathways:

Acute Myeloid Leukemia, FLT3 in AML, FLT3-ITD in AML, FLT3-ITD signaling

Name	PIM1 View Modifications
Full Name	Serine/threonine-protein kinase pim-1
Synonyms	PIM1_HUMAN
Primary ID	P11309
Links	- -
Type	protein
Relations	59
Pathways	Acute Myeloid Leukemia, FLT3 in AML, FLT3-ITD in AML, FLT3-ITD signaling
Inhibitors	SGI-1776
Function	Proto-oncogene with serine/threonine kinase activity involved in cell survival and cell proliferation and thus providing a selective advantage in tumorigenesis. Exerts its oncogenic activity through

The SIGnaling Network
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