Relation Results

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250270	Ser221	DHEKKAYsFCGTVEY	Chlorocebus aethiops	COS-7 Cell
pmid	sentence
10480933	Full-length RSK1, RSK2, and RSK3 Are Activated when Coexpressed with PDK1 in COS7 Cells. Ser221 phosphorylation is increased 2–3-fold during ERK-mediated activation of RSK1 in COS1 cells

Publications:

1

Organism:

Chlorocebus Aethiops

Pathways:

AMPK Signaling, FLT3-ITD signaling, MTOR Signaling

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252763	Ser221	DHEKKAYsFCGTVEY	Chlorocebus aethiops	COS-7 Cell
pmid	sentence
10480933	90-kDa ribosomal S6 kinase is phosphorylated and activated by 3-phosphoinositide-dependent protein kinase-1.

Publications:

1

Organism:

Chlorocebus Aethiops

Pathways:

FLT3-ITD signaling, PI3K/AKT Signaling

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-236633	Ser222	LIDSMANsFVGTRSY	Homo sapiens	HEK-293 Cell
pmid	sentence
15175348	In vitro kinase assay revealed that the direct targets of pdk1 in the mapk pathway were the upstream mapk kinases mek1 and mek2. The identified pdk1 phosphorylation sites in mek1 and mek2 are ser222 and ser226, respectively, and are known to be essential for full activation

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-125176	Ser226	LIDSMANsFVGTRSY	Homo sapiens
pmid	sentence
15175348	The identified pdk1 phosphorylation sites in mek1 and mek2 are ser222 and ser226, respectively, and are known to be essential for full activation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-161924	Ser227	DHEKKAYsFCGTVEY	Homo sapiens
pmid	sentence
19956600	We characterize two monoclonal antibodies raised against phosphorylated forms of the n- and c-terminal domain of rsk2 (p-s227 and p-t577, respectively). Using these two antibodies, we show that stress signals, such as uv light, induce phosphorylation and activation of the three rsks.

Identifier	Residue	Sequence	Organism
SIGNOR-70612	Ser227	DHEKKAYsFCGTVEY	Homo sapiens
pmid	sentence
10480933	We characterize two monoclonal antibodies raised against phosphorylated forms of the n- and c-terminal domain of rsk2 (p-s227 and p-t577, respectively). Using these two antibodies, we show that stress signals, such as uv light, induce phosphorylation and activation of the three rsks.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-250268	Ser241	SKQARANsFVGTAQY	Homo sapiens
pmid	sentence
11481331	In terms of the modulation of PDK1 activity by reversible phosphorylation, five pS sites have been identified on PDK1 in vivo, but only one of these sites, Ser-241 in the activation loop of PDK1, is essential for activity. It seems likely that PDK1 autophosphorylates itself on this residue.

Identifier	Residue	Sequence	Organism
SIGNOR-236789	Ser241	SKQARANsFVGTAQY	Homo sapiens
pmid	sentence
10455013	Pdk1 is itself phosphorylated in vivo and whether phosphorylation plays a role in regulating its activity/ phosphorylation of ser-241 is essential for the activity of 3-phosphoinositide-dependent protein kinase-1

Publications:

2

Organism:

Homo Sapiens

Pathways:

Adipogenesis, Acute Myeloid Leukemia, BCR-ABL in AML, FLT3 in AML, KIT in AML, miRNA in AML, AMPK Signaling, B-cell activation, EGFR Signaling, ErbB receptors in cancer, FAP: Insulin-mediated adipogenesis, FLT3-ITD signaling, Glioblastoma Multiforme, Hepatocellular Tumor, Insulin Signaling, Luminal Breast Cancer, mTOR in cancer, Malignant Melanoma, MTOR Signaling, IGF and Myogenesis, Non-small-cell lung cancer (NSCLC), Prostate Cancer, PI3K/AKT Signaling, Rhabdomyosarcoma, RTKs in cancer, Thyroid cancer, T cell activation, VEGF Signaling

Identifier	Residue	Sequence	Organism
SIGNOR-250077	Ser241	SKQARANsFVGTAQY	in vitro
pmid	sentence
12177059	PDK1 kinase activity is negatively regulated by binding to 14-3-3 through the PDK1 autophosphorylation site Ser-241. PDK1 binds to 14-3-3 in vivo and in vitro through the residues surrounding the autophosphorylation site Ser-241 and that the association is achieved only when Ser-241 has been phosphorylated

Publications:

1

Organism:

In Vitro

Pathways:

Adipogenesis, Acute Myeloid Leukemia, BCR-ABL in AML, FLT3 in AML, KIT in AML, miRNA in AML, AMPK Signaling, B-cell activation, EGFR Signaling, ErbB receptors in cancer, FAP: Insulin-mediated adipogenesis, FLT3-ITD signaling, Glioblastoma Multiforme, Hepatocellular Tumor, Insulin Signaling, Luminal Breast Cancer, mTOR in cancer, Malignant Melanoma, MTOR Signaling, IGF and Myogenesis, Non-small-cell lung cancer (NSCLC), Prostate Cancer, PI3K/AKT Signaling, Rhabdomyosarcoma, RTKs in cancer, Thyroid cancer, T cell activation, VEGF Signaling

Identifier	Residue	Sequence	Organism
SIGNOR-236777	Ser25	VVLCSCPsPSMVRTQ	Homo sapiens
pmid	sentence
10455013	3-phosphoinositide-dependent protein kinase-1 (pdk1) expressed in unstimulated 293 cells was phosphorylated at ser-25, ser-241, ser-393, ser-396 and ser-410 and the level of phosphorylation of each site was unaffected by stimulation with insulin-like growth factor-1. Mutation of ser-241 to ala abolished pdk1 activity, whereas mutation of the other phosphorylation sites individually to ala did not affect pdk1 activity

Identifier	Residue	Sequence	Organism
SIGNOR-235782	Ser393	MQVSSSSsSHSLSAS	Homo sapiens
pmid	sentence
10455013	3-phosphoinositide-dependent protein kinase-1 (pdk1) expressed in unstimulated 293 cells was phosphorylated at ser-25, ser-241, ser-393, ser-396 and ser-410 and the level of phosphorylation of each site was unaffected by stimulation with insulin-like growth factor-1. Mutation of ser-241 to ala abolished pdk1 activity, whereas mutation of the other phosphorylation sites individually to ala did not affect pdk1 activity

Identifier	Residue	Sequence	Organism
SIGNOR-236764	Ser396	SSSSSSHsLSASDTG	Homo sapiens
pmid	sentence
10455013	3-phosphoinositide-dependent protein kinase-1 (pdk1) expressed in unstimulated 293 cells was phosphorylated at ser-25, ser-241, ser-393, ser-396 and ser-410 and the level of phosphorylation of each site was unaffected by stimulation with insulin-like growth factor-1. Mutation of ser-241 to ala abolished pdk1 activity, whereas mutation of the other phosphorylation sites individually to ala did not affect pdk1 activity

Identifier	Residue	Sequence	Organism
SIGNOR-236772	Ser410	GLPQRSGsNIEQYIH	Homo sapiens
pmid	sentence
10455013	3-phosphoinositide-dependent protein kinase-1 (pdk1) expressed in unstimulated 293 cells was phosphorylated at ser-25, ser-241, ser-393, ser-396 and ser-410 and the level of phosphorylation of each site was unaffected by stimulation with insulin-like growth factor-1. Mutation of ser-241 to ala abolished pdk1 activity, whereas mutation of the other phosphorylation sites individually to ala did not affect pdk1 activity

Publications:

4

Organism:

Homo Sapiens

Pathways:

Adipogenesis, Acute Myeloid Leukemia, BCR-ABL in AML, FLT3 in AML, KIT in AML, miRNA in AML, AMPK Signaling, B-cell activation, EGFR Signaling, ErbB receptors in cancer, FAP: Insulin-mediated adipogenesis, FLT3-ITD signaling, Glioblastoma Multiforme, Hepatocellular Tumor, Insulin Signaling, Luminal Breast Cancer, mTOR in cancer, Malignant Melanoma, MTOR Signaling, IGF and Myogenesis, Non-small-cell lung cancer (NSCLC), Prostate Cancer, PI3K/AKT Signaling, Rhabdomyosarcoma, RTKs in cancer, Thyroid cancer, T cell activation, VEGF Signaling

Identifier	Residue	Sequence	Organism
SIGNOR-250371	Ser370	TRQTPVDsPDDTALS	in vitro
pmid	sentence
11733037	Mutational analysis revealed that the phosphorylation of Thr241 and Thr401 in p70beta1 was indispensable for the kinase activity. In contrast, a p70beta1 mutant in which Ser383 was substituted with Gly (S383G) still retained nearly the half maximal activity. Sequential phosphorylation of wild-type and S383G mutant of p70beta1 with mTOR and 3-phosphoinositide-dependent protein kinase 1 (PDK1) in vitro synergistically activated their kinase activities.

Identifier	Residue	Sequence	Organism
SIGNOR-250273	Thr228	HEGAVTHtFCGTIEY	in vitro
pmid	sentence
11733037	Mutational analysis revealed that the phosphorylation of Thr241 and Thr401 in p70beta1 was indispensable for the kinase activity. In contrast, a p70beta1 mutant in which Ser383 was substituted with Gly (S383G) still retained nearly the half maximal activity. Sequential phosphorylation of wild-type and S383G mutant of p70beta1 with mTOR and 3-phosphoinositide-dependent protein kinase 1 (PDK1) in vitro synergistically activated their kinase activities.

Identifier	Residue	Sequence	Organism
SIGNOR-250272	Thr388	NQAFLGFtYVAPSVL	in vitro
pmid	sentence
11733037	Mutational analysis revealed that the phosphorylation of Thr241 and Thr401 in p70beta1 was indispensable for the kinase activity. In contrast, a p70beta1 mutant in which Ser383 was substituted with Gly (S383G) still retained nearly the half maximal activity. Sequential phosphorylation of wild-type and S383G mutant of p70beta1 with mTOR and 3-phosphoinositide-dependent protein kinase 1 (PDK1) in vitro synergistically activated their kinase activities.

Publications:

3

Organism:

In Vitro

Identifier	Residue	Sequence
SIGNOR-250376	Ser416	SSAFLGFsYAPEDDD
pmid	sentence
10548550	SGK2 and SGK3 are activated in vitro by PDK1, albeit more slowly than SGK1, and their activation is accompanied by the phosphorylation of Thr(193) and Thr(253) respectively. The PDK1-catalysed phosphorylation and activation of SGK2 and SGK3, like SGK1, is greatly potentiated by mutating Ser(356) and Ser(419) respectively to Asp, these residues being equivalent to the C-terminal phosphorylation site of PKB.

Identifier	Residue	Sequence
SIGNOR-250277	Thr193	EPEDTTStFCGTPEY
pmid	sentence
10548550	SGK2 and SGK3 are activated in vitro by PDK1, albeit more slowly than SGK1, and their activation is accompanied by the phosphorylation of Thr(193) and Thr(253) respectively. The PDK1-catalysed phosphorylation and activation of SGK2 and SGK3, like SGK1, is greatly potentiated by mutating Ser(356) and Ser(419) respectively to Asp, these residues being equivalent to the C-terminal phosphorylation site of PKB.

Publications:

2

Identifier	Residue	Sequence	Organism
SIGNOR-250274	Ser422	AEAFLGFsYAPPTDS	in vitro
pmid	sentence
10191262	The activation of SGK by PDK1 in vitro is unaffected by PtdIns(3,4,5)P3, abolished by the mutation of Ser422 to Ala, and greatly potentiated by mutation of Ser422 to Asp

Identifier	Residue	Sequence	Organism
SIGNOR-250275	Thr256	EHNSTTStFCGTPEY	in vitro
pmid	sentence
10191262	PDK1 activates SGK in vitro by phosphorylating Thr256.

Publications:

2

Organism:

In Vitro

Pathways:

Insulin Signaling

Identifier	Residue	Sequence	Organism
SIGNOR-67367	Ser473	RPHFPQFsYSASGTA	Homo sapiens
pmid	sentence
10226025	We have partially purified a kinase from brain extract that phosphorylates Ser473 of PKBalpha in a PtdIns(3,4,5)P3-dependent manner and that is immunoprecipitated with PDK1 antibodies.

Identifier	Residue	Sequence	Organism
SIGNOR-175675	Thr308	KDGATMKtFCGTPEY	Homo sapiens
pmid	sentence
21798082	Pip3 acts in turn as a docking site for two kinases, phosphoinositidedependent kinase 1 (pdk1) and akt, and the subsequent phosphorylation of akt at serine 308 by pdk1, leading to akt activation.

Identifier	Residue	Sequence	Organism
SIGNOR-91354	Thr308	KDGATMKtFCGTPEY	Homo sapiens
pmid	sentence
12167717	Together, these results suggest a mechanism in which 3' phosphoinositide lipid-dependent translocation of pkb to the plasma membrane promotes serine 473 phosphorylation, which is, in turn, necessary for pdk1-mediated phosphorylation of threonine 308 and, consequentially, full pkb activation.

Identifier	Residue	Sequence	Organism
SIGNOR-252611	Thr308	KDGATMKtFCGTPEY	Homo sapiens
pmid	sentence
12808134	Akt1 and akt2 are phosphorylated and activated by the protein kinase pdk1 at thr-308 or thr-309, respectively, in the activation t-loop, and further activation occurs through phosphorylation at ser-473 or ser-474, respectively. In this paper, we demonstrate that this is indeed the case, and report the purification and initial characterization of a 3 phosphoinositide-dependent protein kinase, pdk1, which activates pkb by phosphorylating it at thr308. Akt is directly phosphorylated and activated by pdk1. Akt/pkb activation requires the phosphorylation of thr308 in the activation loop by the phosphoinositide-dependent kinase 1 (pdk1).

Identifier	Residue	Sequence	Organism
SIGNOR-67363	Thr308	KDGATMKtFCGTPEY	Homo sapiens
pmid	sentence
10226025	Protein kinase b (pkb) is activated by phosphorylation of thr308 and of ser473. Thr308 is phosphorylated by the 3-phosphoinositide-dependent protein kinase-1 (pdk1) but the identity of the kinase that phosphorylates ser473 (provisionally termed pdk2) is unknown.

Publications:

5

Organism:

Homo Sapiens

Tissue:

Brain

Pathways:

Adipogenesis, FLT3-ITD signaling, Glioblastoma Multiforme, IGF and Myogenesis

Identifier	Residue	Sequence	Organism
SIGNOR-134481	Ser474	RTHFPQFsYSASIRE	Homo sapiens
pmid	sentence
15743829	Akt1 and akt2 are phosphorylated and activated by the protein kinase pdk1 at thr-308 or thr-309, respectively, in the activation t-loop, and further activation occurs through phosphorylation at ser-473 or ser-474, respectively. Pdk1 phosphorylates akt-2 at thr 309 in the catalytic domain, leading to enzymatic activation.

Identifier	Residue	Sequence	Organism
SIGNOR-134485	Thr309	SDGATMKtFCGTPEY	Homo sapiens
pmid	sentence
15743829	Akt1 and akt2 are phosphorylated and activated by the protein kinase pdk1 at thr-308 or thr-309, respectively, in the activation t-loop, and further activation occurs through phosphorylation at ser-473 or ser-474, respectively. Pdk1 phosphorylates akt-2 at thr 309 in the catalytic domain, leading to enzymatic activation.

Identifier	Residue	Sequence	Organism
SIGNOR-236785	Thr309	SDGATMKtFCGTPEY	Homo sapiens
pmid	sentence
9512493	The activation of pkbbeta and pkbgamma by pdk1 was accompanied by the phosphorylation of the residues equivalent to thr308 in pkbalpha, namely thr309 (pkbbeta) and thr305 (pkbgamma)

Publications:

3

Organism:

Homo Sapiens

Tissue:

Muscle, Skeletal Muscle, Myotube

Identifier	Residue	Sequence
SIGNOR-250278	Ser486	DDAFVGFsYAPPSED
pmid	sentence
10548550	SGK2 and SGK3 are activated in vitro by PDK1, albeit more slowly than SGK1, and their activation is accompanied by the phosphorylation of Thr(193) and Thr(253) respectively. The PDK1-catalysed phosphorylation and activation of SGK2 and SGK3, like SGK1, is greatly potentiated by mutating Ser(356) and Ser(419) respectively to Asp, these residues being equivalent to the C-terminal phosphorylation site of PKB.

Identifier	Residue	Sequence
SIGNOR-250279	Thr320	AISDTTTtFCGTPEY
pmid	sentence
10548550	SGK2 and SGK3 are activated in vitro by PDK1, albeit more slowly than SGK1, and their activation is accompanied by the phosphorylation of Thr(193) and Thr(253) respectively. The PDK1-catalysed phosphorylation and activation of SGK2 and SGK3, like SGK1, is greatly potentiated by mutating Ser(356) and Ser(419) respectively to Asp, these residues being equivalent to the C-terminal phosphorylation site of PKB.

Publications:

2

Identifier	Residue	Sequence	Organism
SIGNOR-273844	Ser549	VWRQRYQsHPDAAVQ	Homo sapiens
pmid	sentence
35318320	Here we report that ribosomal protein S6 kinase beta 1 (S6K1), a member of AGC kinases and downstream target of mechanistic target of rapamycin complex 1 (mTORC1), directly phosphorylates PDK1 at its pleckstrin homology (PH) domain, and impairs PDK1 interaction with and activation of AKT.

Publications:

1

Organism:

Homo Sapiens

Pathways:

FLT3-ITD signaling, Insulin Signaling, MTOR Signaling

Identifier	Residue	Sequence	Organism
SIGNOR-249174	Ser68	RSLSRSIsQSSTDSY	Chlorocebus aethiops
pmid	sentence
17635105	Residue 68 resides in a consensus phosphorylation site for PKD (Figure 1A) [22,23]. Interestingly, phosphorylation of Ser68 could allow for subsequent phosphorylation of Ser71, Ser74, Ser77 and Ser80 by CK1, for which the consensus phosphorylation site is pS/T-X-X-S/T\| We found that phosphorylation of Ser71 and Ser74 were sufficient to enable inhibition of IP3 binding to the IP3R

Publications:

1

Organism:

Chlorocebus Aethiops

Identifier	Residue	Sequence	Organism
SIGNOR-260786	Thr168	SHRELSQtFCGSTAY	in vitro
pmid	sentence
16336268	We elucidated the mechanism of regulation of TSSK3 activity showing that autophosphorylation and PDK1 phosphorylation in the ‘activation loop’ are necessary for activation.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-126076	Thr228	HEGAVTHtFCGTIEY	Homo sapiens
pmid	sentence
15209375	A regulatory link between p70s6k and pkb was demonstrated, as pdk1 was found to selectively phosphorylate p70s6k at thr229. More importantly, pdk1 activated p70s6k in vitro and in vivo, whereas the catalytically inactive pdk1 blocked insulin-induced activation of p70s6k. one of the most studied signalling events controlled by ptdins(3,4,5)p3, comprises the activation of a group of agc family protein kinases, including isoforms of protein kinase b (pkb)/akt, p70 ribosomal s6 kinase (s6k), serum- and glucocorticoid-induced protein kinase (sgk) and protein kinase c (pkc), which play crucial roles in regulating physiological processes relevant to metabolism, growth, proliferation and survival. Here, we review recent biochemical, genetic and structural studies on the 3-phosphoinositide-dependent protein kinase-1 (pdk1), which phosphorylates and activates the agc kinase members regulated by pi 3-kinase. We also discuss whether inhibitors of pdk1 might have chemotherapeutic potential in the treatment of cancers in which the pdk1-regulated agc kinases are constitutively activated.

Identifier	Residue	Sequence	Organism
SIGNOR-55371	Thr228	HEGAVTHtFCGTIEY	Homo sapiens
pmid	sentence
9445476	A regulatory link between p70s6k and pkb was demonstrated, as pdk1 was found to selectively phosphorylate p70s6k at thr229. More importantly, pdk1 activated p70s6k in vitro and in vivo, whereas the catalytically inactive pdk1 blocked insulin-induced activation of p70s6k. one of the most studied signalling events controlled by ptdins(3,4,5)p3, comprises the activation of a group of agc family protein kinases, including isoforms of protein kinase b (pkb)/akt, p70 ribosomal s6 kinase (s6k), serum- and glucocorticoid-induced protein kinase (sgk) and protein kinase c (pkc), which play crucial roles in regulating physiological processes relevant to metabolism, growth, proliferation and survival. Here, we review recent biochemical, genetic and structural studies on the 3-phosphoinositide-dependent protein kinase-1 (pdk1), which phosphorylates and activates the agc kinase members regulated by pi 3-kinase. We also discuss whether inhibitors of pdk1 might have chemotherapeutic potential in the treatment of cancers in which the pdk1-regulated agc kinases are constitutively activated.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277402	Thr243	IGGGMAFtFLKVLNN	Homo sapiens	U-87MG Cell
pmid	sentence
30029001	PDPK1 Phosphorylates PGK1 T243. Macrophages increase PGK1 pT243 to reduce the 3-PG affinity of PGK1, which alters the equilibrium of the PGK1-catalyzed reaction toward glycolysis, promoting tumor cell proliferation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-55306	Thr252	HDGTVTHtFCGTIEY	Homo sapiens
pmid	sentence
9445476	A regulatory link between p70s6k and pkb was demonstrated, as pdk1 was found to selectively phosphorylate p70s6k at thr229. More importantly, pdk1 activated p70s6k in vitro and in vivo, whereas the catalytically inactive pdk1 blocked insulin-induced activation of p70s6k. one of the most studied signalling events controlled by ptdins(3,4,5)p3, comprises the activation of a group of agc family protein kinases, including isoforms of protein kinase b (pkb)/akt, p70 ribosomal s6 kinase (s6k), serum- and glucocorticoid-induced protein kinase (sgk) and protein kinase c (pkc), which play crucial roles in regulating physiological processes relevant to metabolism, growth, proliferation and survival. Here, we review recent biochemical, genetic and structural studies on the 3-phosphoinositide-dependent protein kinase-1 (pdk1), which phosphorylates and activates the agc kinase members regulated by pi 3-kinase. We also discuss whether inhibitors of pdk1 might have chemotherapeutic potential in the treatment of cancers in which the pdk1-regulated agc kinases are constitutively activated.

Identifier	Residue	Sequence	Organism
SIGNOR-188907	Thr252	HDGTVTHtFCGTIEY	Homo sapiens
pmid	sentence
19864428	A regulatory link between p70s6k and pkb was demonstrated, as pdk1 was found to selectively phosphorylate p70s6k at thr229. More importantly, pdk1 activated p70s6k in vitro and in vivo, whereas the catalytically inactive pdk1 blocked insulin-induced activation of p70s6k. One of the most studied events controlled by ptdins(3,4,5)p3, comprises the activation of a of agc family protein kinases, including isoforms of protein kinase b (pkb)/akt, p70 ribosomal s6 kinase (s6k), serum- and glucocorticoid-induced protein kinase (sgk) and protein kinase c (pkc), which play crucial roles in regulating physiological processes relevant to metabolism, growth, proliferation and survival. Here, we review recent biochemical, genetic and structural studies on the 3-phosphoinositide-dependent protein kinase-1 (pdk1), which phosphorylates and activates the agc kinase members regulated by pi 3-kinase. We also discuss whether inhibitors of pdk1 might have chemotherapeutic potential in the treatment of cancers in which the pdk1-regulated agc kinases are constitutively activated. Phosphorylation and activation of p70s6k by pdk1.

Identifier	Residue	Sequence	Organism
SIGNOR-55310	Thr412	NQVFLGFtYVAPSVL	Homo sapiens
pmid	sentence
9445476	A regulatory link between p70s6k and pkb was demonstrated, as pdk1 was found to selectively phosphorylate p70s6k at thr229. More importantly, pdk1 activated p70s6k in vitro and in vivo, whereas the catalytically inactive pdk1 blocked insulin-induced activation of p70s6k. one of the most studied signalling events controlled by ptdins(3,4,5)p3, comprises the activation of a group of agc family protein kinases, including isoforms of protein kinase b (pkb)/akt, p70 ribosomal s6 kinase (s6k), serum- and glucocorticoid-induced protein kinase (sgk) and protein kinase c (pkc), which play crucial roles in regulating physiological processes relevant to metabolism, growth, proliferation and survival. Here, we review recent biochemical, genetic and structural studies on the 3-phosphoinositide-dependent protein kinase-1 (pdk1), which phosphorylates and activates the agc kinase members regulated by pi 3-kinase. We also discuss whether inhibitors of pdk1 might have chemotherapeutic potential in the treatment of cancers in which the pdk1-regulated agc kinases are constitutively activated.

Identifier	Residue	Sequence	Organism
SIGNOR-188911	Thr412	NQVFLGFtYVAPSVL	Homo sapiens
pmid	sentence
9445476	A regulatory link between p70s6k and pkb was demonstrated, as pdk1 was found to selectively phosphorylate p70s6k at thr229. More importantly, pdk1 activated p70s6k in vitro and in vivo, whereas the catalytically inactive pdk1 blocked insulin-induced activation of p70s6k.

Publications:

4

Organism:

Homo Sapiens

Pathways:

FLT3-ITD signaling, Insulin Signaling, MTOR Signaling

Identifier	Residue	Sequence	Organism
SIGNOR-243338	Thr252	HDGTVTHtFCGTIEY	in vitro
pmid	sentence
9445476	The results presented here are consistent with PDK1 as the in vivo kinase responsible for mediating Thr252 phosphorylation in the catalytic domain of p70s6k.

Publications:

1

Organism:

In Vitro

Pathways:

FLT3-ITD signaling, Insulin Signaling, MTOR Signaling

Identifier	Residue	Sequence	Organism
SIGNOR-236800	Thr256	EHNSTTStFCGTPEY	Chlorocebus aethiops
pmid	sentence
12387817	Thus, it was suggested that NHERF2 mediates the activation and phosphorylation of SGK1 by PDK1 through its first PDZ domain and PIF motif, as a novel SGK1 activation mechanism.

Identifier	Residue	Sequence	Organism
SIGNOR-236637	Thr256	EHNSTTStFCGTPEY	Homo sapiens
pmid	sentence
15209375	Here, we review recent biochemical, genetic and structural studies on the 3-phosphoinositide-dependent protein kinase-1 (pdk1), which phosphorylates and activates the agc kinase members regulated by pi 3-kinase. We also discuss whether inhibitors of pdk1 might have chemotherapeutic potential in the treatment of cancers in which the pdk1-regulated agc kinases are constitutively activated.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-236796	Thr256	EHNSTTStFCGTPEY	Homo sapiens	HEK-293 Cell
pmid	sentence
10191262	This is followed by the ptdins(3,4,5)p3-independent phosphorylation at thr256 that activates sgk, and is catalysed by pdk1

Publications:

3

Organism:

Chlorocebus Aethiops, Homo Sapiens

Pathways:

Insulin Signaling

Identifier	Residue	Sequence	Organism
SIGNOR-55937	Thr305	TDAATMKtFCGTPEY	Homo sapiens
pmid	sentence
9512493	The activation of pkbbeta and pkbgamma by pdk1 was accompanied by the phosphorylation of the residues equivalent to thr308 in pkbalpha, namely thr309 (pkbbeta) and thr305 (pkbgamma)

Publications:

1

Organism:

Homo Sapiens

Tissue:

Muscle, Skeletal Muscle, Myotube

Identifier	Residue	Sequence
SIGNOR-249629	Thr308	KDGATMKtFCGTPEY
pmid	sentence
19951971	PIP3 recruits PDK1 and AKT to the plasma membrane, where PDK1 phosphorylates AKT on Thr308 in the activation loop of the kinase domain.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252612	Thr308	KDGATMKtFCGTPEY	Homo sapiens	HeLa Cell
pmid	sentence
15718470	Akt/PKB activation requires the phosphorylation of Thr308 in the activation loop by the phosphoinositide-dependent kinase 1 (PDK1) and Ser473 within the carboxyl-terminal hydrophobic motif by an unknown kinase.

Publications:

2

Organism:

, Homo Sapiens

Pathways:

Adipogenesis, FLT3-ITD signaling, Glioblastoma Multiforme, IGF and Myogenesis

Identifier	Residue	Sequence	Organism
SIGNOR-134477	Thr308	KDGATMKtFCGTPEY	Mus musculus
pmid	sentence
12808134	Akt1 and akt2 are phosphorylated and activated by the protein kinase pdk1 at thr-308 or thr-309, respectively, in the activation t-loop, and further activation occurs through phosphorylation at ser-473 or ser-474, respectively. In this paper, we demonstrate that this is indeed the case, and report the purification and initial characterization of a 3 phosphoinositide-dependent protein kinase, pdk1, which activates pkb by phosphorylating it at thr308. Akt is directly phosphorylated and activated by pdk1. Akt/pkb activation requires the phosphorylation of thr308 in the activation loop by the phosphoinositide-dependent kinase 1 (pdk1).

Identifier	Residue	Sequence	Organism
SIGNOR-244421	Thr308	KDGATMKtFCGTPEY	Rattus norvegicus
pmid	sentence
10226025	Protein kinase B (PKB) is activated by phosphorylation of Thr308 and of Ser473. Thr308 is phosphorylated by the 3-phosphoinositide-dependent protein kinase-1 (PDK1) but the identity of the kinase that phosphorylates Ser473 (provisionally termed PDK2) is unknown.

Identifier	Residue	Sequence	Organism
SIGNOR-243203	Thr308	KDGATMKtFCGTPEY	Homo sapiens
pmid	sentence
15718470	Akt/PKB activation requires the phosphorylation of Thr308 in the activation loop by the phosphoinositide-dependent kinase 1 (PDK1) and Ser473 within the carboxyl-terminal hydrophobic motif by an unknown kinase.

Identifier	Residue	Sequence	Organism
SIGNOR-244480	Thr308	KDGATMKtFCGTPEY	Homo sapiens
pmid	sentence
9512493	The activation of PKBbeta and PKBamma by PDK11 was accompanied by the phosphorylation of the residues equivalent to Thr308 in PKBalpha, namely Thr309 (PKBbeta) and Thr305 (PKBgamma)

Identifier	Residue	Organism
SIGNOR-244469		Homo sapiens
pmid	sentence
15743829	3-phosphoinositide-dependent kinase 1 (PDK1) phosphorylates the activation loop of a number of protein serine/threonine kinases of the AGC kinase superfamily, including protein kinase B (PKB; also called Akt),

Publications:

5

Organism:

Mus Musculus, Rattus Norvegicus, Homo Sapiens

Tissue:

Brain, Muscle, Skeletal Muscle, Myotube

Pathways:

Acute Myeloid Leukemia, BCR-ABL in AML, FLT3 in AML, KIT in AML, miRNA in AML, AMPK Signaling, B-cell activation, EGFR Signaling, ErbB receptors in cancer, FAP: Insulin-mediated adipogenesis, FLT3-ITD signaling, Glioblastoma Multiforme, Hepatocellular Tumor, Insulin Signaling, Luminal Breast Cancer, mTOR in cancer, Malignant Melanoma, MTOR Signaling, Non-small-cell lung cancer (NSCLC), Prostate Cancer, PI3K/AKT Signaling, Rhabdomyosarcoma, RTKs in cancer, Thyroid cancer, T cell activation, VEGF Signaling

Identifier	Residue	Sequence	Organism
SIGNOR-147213	Thr320	AISDTTTtFCGTPEY	Homo sapiens
pmid	sentence
16790420	Full-length sgk3 contains a complete phox homology (px) domain that targets the protein to endosomes. Both a functional px domain and pi3k activation are necessary for phosphorylation of sgk3 at two regulatory sites (thr-320 and ser-486) and subsequent induction of kinase activity. Pdk1 phosphorylates endosome-associated sgk3 at thr-320

Identifier	Residue	Organism
SIGNOR-126236		Homo sapiens
pmid	sentence
15209375	One of the most studied events controlled by ptdins(3,4,5)p3, comprises the activation of a of agc family protein kinases, including isoforms of protein kinase b (pkb)/akt, p70 ribosomal s6 kinase (s6k), serum- and glucocorticoid-induced protein kinase (sgk) and protein kinase c (pkc), which play crucial roles in regulating physiological processes relevant to metabolism, growth, proliferation and survival. Here, we review recent biochemical, genetic and structural studies on the 3-phosphoinositide-dependent protein kinase-1 (pdk1), which phosphorylates and activates the agc kinase members regulated by pi 3-kinase. We also discuss whether inhibitors of pdk1 might have chemotherapeutic potential in the treatment of cancers in which the pdk1-regulated agc kinases are constitutively activated.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276414	Thr354	WENLHQQtPPKLTAY	Homo sapiens	HEK-293 Cell
pmid	sentence
22544756	The results showed that MPK38 interacted with and inhibited PDK1 activity via Thr(354) phosphorylation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-85501	Thr410	GPGDTTStFCGTPNY	Homo sapiens
pmid	sentence
11141077	Our findings suggest that insulin, via pip(3), provokes increases in pkc-zeta enzyme activity through (a) pdk-1-dependent t410 loop phosphorylation, (b) t560 autophosphorylationcytoskeletal reorganization;tnni1(induces);desmin(induces);tpm1(induces);myo1c(induces);tnnt1(induces);

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250267	Thr423	PEQSKRStMVGTPYW	Chlorocebus aethiops	COS-7 Cell
pmid	sentence
10995762	P21-activated kinase (PAK1) is phosphorylated and activated by 3-phosphoinositide-dependent kinase-1 (PDK1). We identify threonine 423, a conserved threonine in the activation loop of kinase subdomain VIII, as the PDK1 phosphorylation site on PAK1.

Publications:

1

Organism:

Chlorocebus Aethiops

Pathways:

EGFR Signaling, T cell activation

Identifier	Residue	Sequence	Organism
SIGNOR-150857	Thr500	WDGVTTKtFCGTPDY	Homo sapiens
pmid	sentence
17115692	The catalytic or kinase domain requires phosphorylation at three sites for full activation (24, 25): ? Phosphorylation of threonine 500 (thr-500) in the activation loop by the upstream kinase pdk-1 is a prerequisite for the maturation of the enzyme (26), which subsequently leads to autophosphorylation at threonine 641 (thr-641) in the turn motif and serine 660 (ser-660) in the hydrophobic motif

Identifier	Residue	Organism
SIGNOR-126069		Homo sapiens
pmid	sentence
15209375	One of the most studied events controlled by ptdins(3,4,5)p3, comprises the activation of a of agc family protein kinases, including isoforms of protein kinase b (pkb)/akt, p70 ribosomal s6 kinase (s6k), serum and glucocorticoid-induced protein kinase (sgk) and protein kinase c (pkc), which play crucial roles in regulating physiological processes relevant to metabolism, growth, proliferation and survival. Here, we review recent biochemical, genetic and structural studies on the 3-phosphoinositide-dependent protein kinase-1 (pdk1), which phosphorylates and activates the agc kinase members regulated by pi 3-kinase. We also discuss whether inhibitors of pdk1 might have chemotherapeutic potential in the treatment of cancers in which the pdk1-regulated agc kinases are constitutively activated.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250269	Thr507	FGESRAStFCGTPDY	Homo sapiens	HEK-293 Cell
pmid	sentence
9748166	PDK1 phosphorylated the activation loop sites of PKCzeta and PKCdelta in vitro and in a phosphoinositide 3-kinase (PI 3-kinase)-dependent manner in vivo in human embryonic kidney (293) cells. PKCδ was also phosphorylated in the activation loop site (T505)

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-117320	Thr566	LNGVTTTtFCGTPDY	Homo sapiens
pmid	sentence
11964154	In the present study, we analysed the contribution of the phosphoinositide-dependent kinase 1 (pdk-1) and pkcepsilon kinase activity in controlling the phosphorylation of thr(566) and ser(729). pdk-1 phosphorylation of the activation loop triggers autophosphorylation of the hydrophobic motif

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-76640	Thr774	GYGDRTStFCGTPEF	Homo sapiens
pmid	sentence
10753910	It is shown that activation in vitro and in vivo involves the activation loop phosphorylation of prk1/2 by 3-phosphoinositide-dependent protein kinase-1 (pdk1) /pdk1 phosphorylates the prks at their conserved activation loop threonines (thr-774 and thr-816 for prk1 and prk2, respectively)

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-250266	Thr779	LYKEATStFTNITYR	in vitro
pmid	sentence
10896934	PDK1 specifically phosphorylates Thr-753 in 3. Our data argue that phosphorylation of Thr-753, which is conserved in many subunits, reduces the ability of PTB-containing proteins to bind the NXX(pY) motif in 3.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-76710	Thr816	GYGDRTStFCGTPEF	Homo sapiens
pmid	sentence
10753910	It is shown that activation in vitro and in vivo involves the activation loop phosphorylation of prk1/2 by 3-phosphoinositide-dependent protein kinase-1 (pdk1) /pdk1 phosphorylates the prks at their conserved activation loop threonines (thr-774 and thr-816 for prk1 and prk2, respectively)

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-236548	Tyr373	SEDDEDCyGNYDNLL	in vitro
pmid	sentence
20044479	IGF-1R Directly Interacts with and Phosphorylates PDK1 in Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-166710	Tyr373	SEDDEDCyGNYDNLL	Homo sapiens
pmid	sentence
20643654	Previous studies indicate that optimal activation of PDK1 requires phosphorylation of Tyr373/376 (11, 12, 14, 17), and growth factor receptor activation leads to PDK1 recruitment to the plasma membrane, followed by sequential phosphorylation of Tyr9 and then Tyr373/376

Identifier	Residue	Sequence	Organism
SIGNOR-166714	Tyr376	DEDCYGNyDNLLSQF	Homo sapiens
pmid	sentence
20643654	Previous studies indicate that optimal activation of PDK1 requires phosphorylation of Tyr373/376, and growth factor receptor activation leads to PDK1 recruitment to the plasma membrane, followed by sequential phosphorylation of Tyr9 and then Tyr373/376

Identifier	Residue	Sequence	Organism
SIGNOR-236544	Tyr376	DEDCYGNyDNLLSQF	Homo sapiens
pmid	sentence
20044479	We have described that upon ligand binding, igf-1r directly interacts with and phosphorylates pdk1 at tyr373/376

Publications:

4

Organism:

In Vitro, Homo Sapiens

Pathways:

Hepatocellular Tumor, IGF and Myogenesis, Non-small-cell lung cancer (NSCLC), Rhabdomyosarcoma

Identifier	Residue	Sequence	Organism
SIGNOR-166718	Tyr373	SEDDEDCyGNYDNLL	Homo sapiens
pmid	sentence
20643654	Src-dependent pdk1 tyr373/376 tyrosine phosphorylation. / optimal activation of pdk1 requires phosphorylation of tyr373/376

Identifier	Residue	Sequence	Organism
SIGNOR-166722	Tyr376	DEDCYGNyDNLLSQF	Homo sapiens
pmid	sentence
20643654	Src-dependent pdk1 tyr373/376 tyrosine phosphorylation. / optimal activation of pdk1 requires phosphorylation of tyr373/376

Publications:

2

Organism:

Homo Sapiens

Pathways:

EGFR Signaling, Rhabdomyosarcoma

Identifier	Residue	Sequence	Organism
SIGNOR-235863	Tyr9	ARTTSQLyDAVPIQS	Cricetulus griseus
pmid	sentence
12738763	Ret/ptc (rearranged in transformation/papillary thyroid carcinomas) tyrosine kinase phosphorylates and activates phosphoinositide-dependent kinase 1 (pdk1) ret/ptc phosphorylates a specific tyrosine (y9) residue located in the n-terminal region of pdk1.

Publications:

1

Organism:

Cricetulus Griseus

Pathways:

Thyroid cancer

Identifier	Residue	Sequence	Organism
SIGNOR-109533	Tyr9	ARTTSQLyDAVPIQS	Homo sapiens
pmid	sentence
11481331	Using site-directed mutants, we show that, although phosphorylation on tyr-373/376 is important for pdk1 activity, phosphorylation on tyr-9 has no effect on the activity of the kinase. Both of these residues can be phosphorylated by v-src tyrosine kinase in vitro, and co-expression of v-src leads to tyrosine phosphorylation and activation of pdk1.

Publications:

1

Organism:

Homo Sapiens

Pathways:

EGFR Signaling, Rhabdomyosarcoma

Identifier	Residue	Organism
SIGNOR-243511		Homo sapiens
pmid	sentence
21075311	Here, we show that PPP2R2B, encoding the B55² regulatory subunit of the PP2A complex, is epigenetically inactivated by DNA hypermethylation in colorectal cancer. B55²-associated PP2A interacts with PDK1 and modulates its activity toward Myc phosphorylation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-126072		Homo sapiens
pmid	sentence
15209375	One of the most studiedevents controlled by ptdins(3,4,5)p3, comprises the activation of aof agc family protein kinases, including isoforms of protein kinase b (pkb)/akt, p70 ribosomal s6 kinase (s6k), serum- and glucocorticoid-induced protein kinase (sgk) and protein kinase c (pkc), which play crucial roles in regulating physiological processes relevant to metabolism, growth, proliferation and survival. Here, we review recent biochemical, genetic and structural studies on the 3-phosphoinositide-dependent protein kinase-1 (pdk1), which phosphorylates and activates the agc kinase members regulated by pi 3-kinase. We also discuss whether inhibitors of pdk1 might have chemotherapeutic potential in the treatment of cancers in which the pdk1-regulated agc kinases are constitutively activated.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-252186		Rattus norvegicus
pmid	sentence
15212950	We characterize the network of 43 genes induced by GDNF overproduction of neuronal progenitor cells (ST14A), which mainly regulate migration and differentiation of neuronal progenitor cells.Laminin, Mpl3, Alcam, Bin1, Id1, Id2, Id3, neuregulin1, the ephrinB2-receptor, neuritin, focal adhesion kinase (FAK), Tc10, Pdpk1, clusterin, GTP-cyclooxygenase1, and follistatin are genes up-regulated by GDNF overexpression.

Publications:

1

Organism:

Rattus Norvegicus

Identifier	Residue	Organism
SIGNOR-190804		Homo sapiens
pmid	sentence
Other

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-197715		Homo sapiens
pmid	sentence
Other

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-134869		Homo sapiens	T-lymphocyte
pmid	sentence
15802604	We demonstrate that 3-phosphoinositide-dependent kinase 1 (pdk1) has an essential role in this pathway by regulating the activation of pkc and through signal-dependent recruiting of both pkc and card11 to lipid rafts.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-175253		Homo sapiens
pmid	sentence
21798082	Pip3 acts in turn as a docking site for two kinases, phosphoinositide-dependent kinase 1 (PDK1) and AKT, and the subsequent phosphorylation of AKT at serine 308 by PDK1, leading to AKT activation.

Identifier	Residue	Organism
SIGNOR-243274		in vitro
pmid	sentence
9094314	We tested the kinase in the presence of several inositol phospholipids and found that only low micromolar concentrations of the D enantiomers of either phosphatidylinositol 3,4,5-triphosphate (PtdIns(3,4,5)P3) or PtdIns(3,4)P2 were effective in potently activating the kinase, which has been named PtdIns(3,4,5)P3-dependent protein kinase-1 (PDK1)

Identifier	Residue	Organism
SIGNOR-249628		Homo sapiens
pmid	sentence
19951971	PIP3 recruits PDK1 and AKT to the plasma membrane, where PDK1 phosphorylates AKT on Thr308 in the activation loop of the kinase domain.

Identifier	Residue	Organism
SIGNOR-58313		Chlorocebus aethiops
pmid	sentence
9637919	In response to PDGF, binding of ptdlns (3,4,5)p3 and/or ptdlns(3,4)p2 to the PH domain of PDK-1 causes its translocation to the plasma membrane where it co-localises with PKB, significantly contributing to the scale of PKB activation.

Publications:

4

Organism:

Homo Sapiens, In Vitro, Chlorocebus Aethiops

Pathways:

Adipogenesis, Acute Myeloid Leukemia, BCR-ABL in AML, FLT3 in AML, KIT in AML, miRNA in AML, AMPK Signaling, B-cell activation, EGFR Signaling, ErbB receptors in cancer, FAP: Insulin-mediated adipogenesis, FLT3-ITD signaling, Glioblastoma Multiforme, Hepatocellular Tumor, Insulin Signaling, mTOR in cancer, Malignant Melanoma, MTOR Signaling, Non-small-cell lung cancer (NSCLC), Prostate Cancer, PI3K/AKT Signaling, RTKs in cancer, Thyroid cancer, T cell activation, VEGF Signaling

Identifier	Residue	Organism
SIGNOR-60567		Homo sapiens
pmid	sentence
9768361	Recent reports have also shown that the phosphoinositide-dependent protein kinase-1 (pdk-1), which binds with high affinity to the pi 3-kinase lipid product phosphatidylinositol-3,4,5-trisphosphate (ptdins-3,4,5-p), phosphorylates and potently activates two other pi 3-kinase targets, the protein kinases akt/pkb and p70s6k.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-134866		Homo sapiens	T-lymphocyte
pmid	sentence
15802604	We demonstrate that 3-phosphoinositide-dependent kinase 1 (pdk1) has an essential role in this pathway by regulating the activation of pkc and through signal-dependent recruiting of both pkc and card11 to lipid rafts.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-243519		Homo sapiens	HEK-293 Cell, Colorectal Adenocarcinoma Cell Line
pmid	sentence
23887393	Here, we report that PDK1 directly induces phosphorylation of Polo-like kinase 1 (PLK1), which in turn induces MYC phosphorylation and protein accumulation. We show that PDK1-PLK1-MYC signaling is critical for cancer cell growth and survival, and small-molecule inhibition of PDK1/PLK1 provides an effective approach for therapeutic targeting of MYC dependency

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-244396		Homo sapiens
pmid	sentence
21798082	Positive feedback involves mtorc2, which phosphorylates akt at serine 473, a phosphorylation required for maximum activation of akt in addition to phosphorylation at threonine 308 by pdk1.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Acute Myeloid Leukemia, BCR-ABL in AML, FLT3 in AML, KIT in AML, miRNA in AML, AMPK Signaling, B-cell activation, EGFR Signaling, ErbB receptors in cancer, FAP: Insulin-mediated adipogenesis, FLT3-ITD signaling, Glioblastoma Multiforme, Hepatocellular Tumor, Insulin Signaling, Luminal Breast Cancer, mTOR in cancer, Malignant Melanoma, MTOR Signaling, Non-small-cell lung cancer (NSCLC), Prostate Cancer, PI3K/AKT Signaling, Rhabdomyosarcoma, RTKs in cancer, Thyroid cancer, T cell activation, VEGF Signaling

Identifier	Residue	Organism
SIGNOR-126177		Homo sapiens
pmid	sentence
15209375	One of the most studiedevents controlled by ptdins(3,4,5)p3, comprises the activation of aof agc family protein kinases, including isoforms of protein kinase b (pkb)/akt, p70 ribosomal s6 kinase (s6k), serum- and glucocorticoid-induced protein kinase (sgk) and protein kinase c (pkc), which play crucial roles in regulating physiological processes relevant to metabolism, growth, proliferation and survival. Here, we review recent biochemical, genetic and structural studies on the 3-phosphoinositide-dependent protein kinase-1 (pdk1), which phosphorylates and activates the agc kinase members regulated by pi 3-kinase. We also discuss whether inhibitors of pdk1 might have chemotherapeutic potential in the treatment of cancers in which the pdk1-regulated agc kinases are constitutively activated.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-244934		Homo sapiens	HEK-293 Cell
pmid	sentence
15175348	In vitro kinase assay revealed that the direct targets of pdk1 in the mapk pathway were the upstream mapk kinases mek1 and mek2. The identified pdk1 phosphorylation sites in mek1 and mek2 are ser222 and ser226, respectively, and are known to be essential for full activation

Publications:

1

Organism:

Homo Sapiens

Pathways:

Adipogenesis, Acute Myeloid Leukemia, BCR-ABL in AML, FLT3 in AML, KIT in AML, B-cell activation, EGFR Signaling, ErbB receptors in cancer, FLT3-ITD signaling, Glioblastoma Multiforme, Hepatocellular Tumor, Insulin Signaling, Luminal Breast Cancer, Malignant Melanoma, Non-small-cell lung cancer (NSCLC), PI3K/AKT Signaling, Rhabdomyosarcoma, RTKs in cancer, Thyroid cancer, T cell activation, VEGF Signaling

Identifier	Residue	Organism
SIGNOR-244938		Homo sapiens
pmid	sentence
15175348	The identified pdk1 phosphorylation sites in mek1 and mek2 are ser222 and ser226, respectively, and are known to be essential for full activation.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Adipogenesis, Acute Myeloid Leukemia, BCR-ABL in AML, FLT3 in AML, KIT in AML, B-cell activation, EGFR Signaling, ErbB receptors in cancer, FLT3-ITD signaling, Glioblastoma Multiforme, Hepatocellular Tumor, Insulin Signaling, Luminal Breast Cancer, Malignant Melanoma, Non-small-cell lung cancer (NSCLC), PI3K/AKT Signaling, Rhabdomyosarcoma, RTKs in cancer, Thyroid cancer, T cell activation, VEGF Signaling

Identifier	Residue	Organism	Cell Line
SIGNOR-174612		Homo sapiens	Leukemia Cell
pmid	sentence
21715304	Consistent with the results described in figures 3c and and4a,4a, treatment of 32d/bcr-abl cells with the bcr-abl inhibitor imatinib, the pi3k inhibitor ly294002 or the akt/pdpk1 inhibitor pht-427 substantially reduced atf5 promoter-directed luciferase activity

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-268577		Homo sapiens	HEK-293 Cell
pmid	sentence
35104164	We found that Ser261 in OXTR was phosphorylated by protein kinase D1 (PKD1).\|In HEK293A cells, the PKD1-mediated phosphorylation of OXTR promoted its binding to Gq protein and, in turn, OXTR-mediated phosphorylation of PKD1, indicating a positive feedback loop.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-126066		Homo sapiens
pmid	sentence
15209375	One of the most studied events controlled by ptdins(3,4,5)p3, comprises the activation of a of agc family protein kinases, including isoforms of protein kinase b (pkb)/akt, p70 ribosomal s6 kinase (s6k), serum and glucocorticoid-induced protein kinase (sgk) and protein kinase c (pkc), which play crucial roles in regulating physiological processes relevant to metabolism, growth, proliferation and survival. Here, we review recent biochemical, genetic and structural studies on the 3-phosphoinositide-dependent protein kinase-1 (pdk1), which phosphorylates and activates the agc kinase members regulated by pi 3-kinase. We also discuss whether inhibitors of pdk1 might have chemotherapeutic potential in the treatment of cancers in which the pdk1-regulated agc kinases are constitutively activated.

Publications:

1

Organism:

Homo Sapiens

Pathways:

B-cell activation, T cell activation, VEGF Signaling

Identifier	Residue	Organism
SIGNOR-243515		Homo sapiens
pmid	sentence
21075311	Here, we show that PPP2R2B, encoding the B55² regulatory subunit of the PP2A complex, is epigenetically inactivated by DNA hypermethylation in colorectal cancer. B55²-associated PP2A interacts with PDK1 and modulates its activity toward Myc phosphorylation.

Publications:

1

Organism:

Homo Sapiens

Name	PDPK1 View Modifications
Full Name	3-phosphoinositide-dependent protein kinase 1
Synonyms	hPDK1 \| PDK1, PDK1
Primary ID	O15530
Links	- -
Type	protein
Relations	93
Pathways	Adipogenesis, Acute Myeloid Leukemia, BCR-ABL in AML, FLT3 in AML, KIT in AML, miRNA in AML, AMPK Signaling, B-cell activation, EGFR Signaling, ErbB receptors in cancer, FAP: In vitro induction of adipogenesis, FAP: Insulin-mediated adipogenesis, FAP: INSR, FLT3-ITD signaling, Glioblastoma Multiforme, Hepatocellular Tumor, Insulin Signaling, Luminal Breast Cancer, mTOR in cancer, Mitochondrial dynamics in T cell exhaustion, Malignant Melanoma, MTOR Signaling, Myostatin, Non-small-cell lung cancer (NSCLC), Prostate Cancer, PI3K/AKT Signaling, Pericyte: In vitro induction of adipogenesis, Rhabdomyosarcoma, RTKs in cancer, Satellite: miRNA network, Thyroid cancer, T cell activation, VEGF Signaling
Inhibitors	N-[3-[[5-bromo-4-[2-(1H-imidazol-5-yl)ethylamino]-2-pyrimidinyl]amino]phenyl]-1-pyrrolidinecarboxamide; OSU-03012; PHT-427
Function	Serine/threonine kinase which acts as a master kinase, phosphorylating and activating a subgroup of the AGC family of protein kinases. Its targets include

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